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other provinces and regions in Vietnam and other country.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Address\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Headquarters of Can Tho Journal of Medicine and Pharmacy, located Scientific Research and International Cooperation Office: 179 Nguyen Van Cu Street, An Khanh Ward, Ninh Kieu District, Can Tho City, Vietnam.\u003C\u002Fspan>\u003C\u002Fp>","\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Ngày 16\u002F7\u002F2015, Tạp chí Y Dược học Cần Thơ được cấp chỉ số quốc tế: ISSN 2354-1210.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Từ tháng 4\u002F2016, Tạp chí đã được Hội đồng Giáo sư ngành Y đưa vào danh sách các tạp chí khoa học Y học được tính điểm công trình 0-0,5 điểm cho một bài báo đăng.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Năm 2020 Tạp chí Y Dược học Cần Thơ đã được phê duyệt vào danh mục của các Hội đồng Giáo sư ngành Dược học được tính điểm công trình 0-0,5 điểm cho một bài báo đăng.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ ra 12 số\u002Fnăm, 180-200 trang\u002Fsố.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Từ tháng 12\u002F2022 Tạp chí Y Dược học Cần Thơ là thành viên của hệ thống Crossref và từ tháng 01\u002F2023 tạp chí thực hiện bình duyệt online kín 2 chiều nhằm tăng tính minh bạch, tin cậy của các công trình nghiên cứu khoa học và đảm bảo tốt nhất chất lượng khoa học của bài viết.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tôn chỉ, mục đích và phạm vi của tạp chí\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tôn chỉ và mục đích hoạt động của tạp chí: xuất bản nhằm mục đích phổ biến kết quả từ các đề tài nghiên cứu khoa học; giao lưu trao đổi khoa học, chia sẻ kinh nghiệm, học tập, đồng thời cập nhật thông tin khoa học mới trong các lĩnh vực y, sinh, dược học trong và ngoài nước.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Phạm vi của tạp chí: Tạp chí xuất bản được chia thành 3 chuyên mục: (i) Bài báo nghiên cứu khoa học là kết quả công trình nghiên cứu khoa học có giá trị đã được triển khai nghiên cứu, (ii) Bài tổng quan y, sinh, dược học: phục vụ mục tiêu đào tạo liên tục trong lĩnh vực y, sinh, dược học; nhằm hệ thống hóa những kiến thức kinh điển và hiện đại; (iii) Thông tin cập nhật kiến thức mới về y, sinh, dược học trong nước và trên thế giới.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Chính sách truy cập mở\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ áp dụng chính sách truy cập mở đối với các bài báo đã xuất bản đến với độc giả, nhằm mở rộng cơ hội tiếp cận các kết quả nghiên cứu chất lượng cao và tăng cường trao đổi kiến thức. Tạp chí đăng tải trực tuyến (miễn phí) toàn văn các bài báo được công bố trên website của Tạp chí (https:\u002F\u002Ftapchi.ctump.edu.vn).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Đạo đức xuất bản\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ cam kết tuân thủ đạo đức xuất bản phù hợp với các hướng dẫn và tiêu chuẩn của the Committee on Publication Ethics (COPE), tuân thủ các nguyên tắc của COPE’s Core Practices, Best Practices Guidelines for Journal Editors và Guidelines on Good Publication Practices.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Bản thảo bài báo chỉ được chấp nhận khi được tác giả chịu trách nhiệm chính cam kết các nội dung sau: Các nội dung của bản thảo chưa được đăng tải toàn bộ hoặc một phần ở các tạp chí khác; Tất cả các tác giả đều có đóng góp một cách đáng kể vào quá trình nghiên cứu hoặc chuẩn bị bản thảo và cùng chịu trách nhiệm về các nội dung của bản thảo; Tuân thủ các biện pháp đảm bảo đạo đức nghiên cứu (ví dụ thỏa thuận đồng ý tham gia nghiên cứu).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Cam kết bảo mật\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí cam kết thực hiện và tuân thủ các quy định của luật và các văn bản hướng dẫn liên quan đến bảo mật thông tin cá nhân trên không gian mạng. Các thông tin mà người dùng (tác giả, độc giả, biên tập viên, người phản biện) nhập vào các biểu mẫu trên Hệ thống Quản lý xuất bản trực tuyến của tạp chí chỉ được sử dụng vào các mục đích đã được tuyên bố rõ ràng và sẽ không được cung cấp cho bất kỳ bên thứ ba nào khác, hay dùng vào bất kỳ mục đích nào khác.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Phí gửi bài\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Lệ phí gửi đăng bài: 1.000.000đ\u002Fbài báo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Lệ phí gửi đăng nhanh: 1.500.000đ\u002Fbài báo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Đối với tác giả là cán bộ viên chức thuộc Trường Đại học Y Dược Cần Thơ thì được hỗ trợ 50% lệ phí gửi đăng bài.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Đối với sinh viên thực hiện đề tài nghiên cứu khoa học cấp trường được hỗ trợ 100% lệ phí đăng bài ( Tác giả gửi đính kèm “ Quyết định về việc giao tổ chức thực hiện đề tài nghiên cứu khoa học cấp Trường của sinh viên”).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Hình thức nộp lệ phí:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Tiền mặt:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Nộp trực tiếp tại Phòng Tài chính - Kế toán, Trường Đại học Y Dược Cần Thơ, số 179 Nguyễn Văn Cừ, P. An Khánh, Q. Ninh Kiều, thành phố Cần Thơ.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Chuyển khoản:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tên Tài khoản: Trường ĐHYD Cần Thơ, Số TK: 0111000115668, tại ngân hàng Vietcombank chi nhánh Cần Thơ.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Thời gian: Áp dụng từ ngày 01\u002F02\u002F2023.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">* Phí gửi bài không được hoàn trả khi bài viết bị từ chối hoặc tác giả xin rút bài viết.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Quy trình phản biện bài báo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ thực hiện quy trình phản biện kín hai chiều nghiêm ngặt. Danh tính của những người phản biện không được tiết lộ cho các tác giả và ngược lại. Quy trình thẩm định bài báo đăng gồm các bước sau:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tiếp nhận bản thảo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tác giả liên hệ gửi bản thảo đến Tạp chí qua hệ thống trực tuyến tại website: https:\u002F\u002Ftapchi.ctump.edu.vn. Hướng dẫn về cách đăng ký, gửi bài và chuẩn bị bản thảo được cung cấp trên website của Tạp chí.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Sàng lọc sơ bộ\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Sau khi Tòa soạn nhận được bài báo của tác giả, Ban Thư ký sẽ tiến hành kiểm tra sơ bộ bài báo (các yêu cầu về nội dung và hình thức). Những bài báo không đúng quy cách hoặc có nội dung không phù hợp hoặc vi phạm bản quyền sẽ bị từ chối (Ban Thư ký thông báo phản hồi đến tác giả trong vòng 1 tuần). Những bài báo đủ điều kiện, được Ban Thư ký tòa soạn chuyển đến Ban Biên tập có cùng chuyên môn với nội dung bài báo để đề xuất người phản biện. Thời gian kể từ khi Ban Biên tập nhận bài báo đến khi đề xuất người phản biện bài báo chậm nhất là 5 ngày.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Vòng phản biện\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Ban Thư ký gửi bài và yêu cầu phản biện đến 02 phản biện độc lập.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Các phản biện gởi nhận xét cho Ban Thư ký. Thời gian từ khi gửi bài cho phản biện đến khi nhận ý kiến của phản biện tối đa là 20 ngày.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Xử ký kết quả phản biện\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Nếu ý kiến đồng ý cho đăng và không cần chỉnh sửa, Ban Thư ký tiếp tục đăng bài theo qui trình.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Nếu ý kiến đồng ý đăng và cần chỉnh sửa, Ban Thư ký sẽ thông tin đến tác giả chỉnh sửa theo yêu cầu của người phản biện. Thời gian chỉnh sửa và gửi lại kéo dài không quá 2 tuần, từ khi tác giả bài báo nhận được thông tin (Quá trình này có thể lặp lại tối đa 2 lần\u002F1 bài báo). Khi có sự thống nhất, đồng ý của người phản biện; bài báo được tiếp tục đăng theo qui trình.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">3. Những bài báo có chất lượng không đạt yêu cầu, cả 2 phản biện không đồng ý cho đăng sẽ bị Tòa soạn từ chối đăng.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Xuất bản\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Ban Thư ký tổng hợp các bản thảo đã được tác giả hoàn thiện sau thẩm định trình Ban Biên tập xem xét, Tổng Biên tập phê duyệt, quyết định bài đăng theo các tiêu chí: sự phù hợp nội dung với tôn chỉ và mục đích, thể loại bài viết (ưu tiên các bài có bài có nghiên cứu chuyên sâu, hàm lượng khoa học cao), đóng góp mới bài báo, bài báo được ưu tiên đăng trong số gần nhất của Tạp chí theo thứ tự: tính thời sự, chất lượng bài báo và thời gian gửi bài.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Ban Biên tập và Ban Thư ký biên tập bản thảo, chế bản, đọc rà soát lỗi. Thời gian hoàn thành từ 10-15 ngày.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">3. Ban Thư ký có trách nhiệm thông báo cho tác giả bài báo (bằng e-mail) về tình hình phê duyệt bài báo, thời gian, số kỳ, tập xuất bản bài báo theo qui định.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">4. 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Med. Chem., 51, 4359, 10.1021\u002Fjm800219f","https:\u002F\u002Fdoi.org\u002F10.1021\u002Fjm800219f",{"mag":917,"openalex":918,"pm":919,"doi":920},"2033043158","W2033043158","18570365","10.1021\u002Fjm800219f",{"id":26,"text":922,"url":26,"identifiers":923},"Whitford, 1994, Report for Working Group I: strategies for improving the assessment of fluoride accumulation in body fluids and tissues, Adv. Dent. Res., 8, 113, 10.1177\u002F08959374940080010401",{"doi":924},"10.1177\u002F08959374940080010401",{"id":26,"text":926,"url":927,"identifiers":928},"Gutknecht, 1981, A hydrofluoric and nitric acid transport through lipid bilayer membranes, Biochim. Biophys. 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Acta, 1104, 160, 10.1016\u002F0005-2736(92)90145-C","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002F000527369290145C",{"doi":944},"10.1016\u002F0005-2736(92)90145-c",{"id":946,"text":947,"url":948,"identifiers":949},"ab5f343b-1c23-470c-b4d7-0c1bb2f0a0c5","Gofa, 1996, NaF potentiates a K(+)-selective ion channel in G292 osteoblastic cells, J. Membr. Biol., 149, 211, 10.1007\u002Fs002329900021","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs002329900021",{"doi":950},"10.1007\u002Fs002329900021",{"id":952,"text":953,"url":954,"identifiers":955},"16a42aa9-10c4-48de-8a70-ba06e53cdc0f","Whitford, 1997, Effects of fluoride on structure and function of canine gastric mucosa, Dig. Dis. Sci., 42, 2146, 10.1023\u002FA:1018895207333","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1023\u002FA:1018895207333",{"doi":956},"10.1023\u002FA:1018895207333",{"id":884,"text":958,"url":886,"identifiers":959},"Sireli, 2004, The effect of acute fluoride poisoning on nitric oxide and methemoglobin formation in the Guinea pig, Turk. J. Vet. Anim. Sci., 28, 591",{"doi":888},{"id":26,"text":961,"url":962,"identifiers":963},"Bigay, 1987, Fluoride complexes of aluminium or beryllium act on G-proteins as reversibly bound analogues of the gamma phosphate of GTP, EMBO J., 6, 2907, 10.1002\u002Fj.1460-2075.1987.tb02594.x","https:\u002F\u002Fdoi.org\u002F10.1002\u002Fj.1460-2075.1987.tb02594.x",{"mag":964,"pmc":965,"openalex":966,"pm":967,"doi":968},"1498793897","553725","W1498793897","2826123","10.1002\u002Fj.1460-2075.1987.tb02594.x",{"id":26,"text":970,"url":971,"identifiers":972},"Combeau, 1988, Probing the mechanism of ATP hydrolysis on F-actin using vanadate and the structural analogs of phosphate, BeF3- and AlF4, J. Biol. Chem., 263, 17429, 10.1016\u002FS0021-9258(19)77854-5","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002Fs0021-9258(19)77854-5",{"doi":973},"10.1016\u002Fs0021-9258(19)77854-5",{"id":975,"text":976,"url":977,"identifiers":978},"10569793-7adc-42de-b3d1-88d319d6a69a","Brigitte, 1993, Aluminum fluoride interactions with troponin C, Biophys. J., 65, 2511, 10.1016\u002FS0006-3495(93)81305-5","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0006349593813055",{"doi":979},"10.1016\u002Fs0006-3495(93)81305-5",{"id":26,"text":981,"url":982,"identifiers":983},"Neri, 1997, Fluoride binding in hemoproteins: the importance of the distal cavity structure, Biochemistry, 36, 8947, 10.1021\u002Fbi970248+","https:\u002F\u002Fdoi.org\u002F10.1021\u002Fbi970248+",{"mag":984,"openalex":985,"pm":986,"doi":987},"2013253110","W2013253110","9609724","10.1021\u002Fbi970248+",{"id":884,"text":989,"url":886,"identifiers":990},"Adamek, 2005, In vitro and in vivo effects of fluoride ions on enzyme activity, Ann. Acad. Med. Stetin, 51, 69",{"doi":888},{"id":992,"text":993,"url":994,"identifiers":995},"39c59919-932d-43b3-bf4f-8f08cc56f2de","Mendoza-Schulz, 2009, The effects of fluoride on cell migration, cell proliferation, and cell metabolism in GH4C1 pituitary tumour cells, Toxicol. Lett., 190, 179, 10.1016\u002Fj.toxlet.2009.07.014","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0378427409012260",{"doi":996},"10.1016\u002Fj.toxlet.2009.07.014",{"id":26,"text":998,"url":999,"identifiers":1000},"Karube, 2009, NaF activates MAPKs and induces apoptosis in odontoblast-like cells, J. Dent. 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Bialost., 49, 180",{"doi":888},{"id":26,"text":1034,"url":1035,"identifiers":1036},"Lee, 2008, Involvement of both mitochondrial- and death receptor-dependent apoptotic pathways regulated by Bcl-2 family in sodium fluoride-induced apoptosis of the human gingival fibroblasts, Toxicology, 243, 340, 10.1016\u002Fj.tox.2007.10.026","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.tox.2007.10.026",{"mag":1037,"openalex":1038,"pm":1039,"doi":1040},"2073913408","W2073913408","18069112","10.1016\u002Fj.tox.2007.10.026",{"id":1042,"text":1043,"url":1044,"identifiers":1045},"efd409d7-6dbf-4a2d-a3c3-db01ee1ce3fc","Liu, 2003, Fluoride causing abnormally elevated serum nitric oxide levels in chicks, Environ. Toxicol. Pharmacol., 13, 199, 10.1016\u002FS1382-6689(03)00002-4","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1382668903000024",{"doi":1046},"10.1016\u002FS1382-6689(03)00002-4",{"id":26,"text":1048,"url":1049,"identifiers":1050},"Hassan, 2009, Mitigating effects of antioxidant properties of black berry juice on sodium fluoride induced hepatotoxicity and oxidative stress in rats, Food Chem. Toxicol., 47, 2332, 10.1016\u002Fj.fct.2009.06.023","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.fct.2009.06.023",{"mag":1051,"openalex":1052,"pm":1053,"doi":1054},"2023664390","W2023664390","19540898","10.1016\u002Fj.fct.2009.06.023",{"id":26,"text":1056,"url":1057,"identifiers":1058},"García-Montalvo, 2009, Fluoride exposure impairs glucose tolerance via decreased insulin expression and oxidative stress, Toxicology, 263, 75, 10.1016\u002Fj.tox.2009.06.008","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.tox.2009.06.008",{"mag":1059,"openalex":1060,"pm":1061,"doi":1062},"2155411288","W2155411288","19540901","10.1016\u002Fj.tox.2009.06.008",{"id":26,"text":1064,"url":1065,"identifiers":1066},"Izquierdo-Vega, 2008, Decreased in vitro fertility in male rats exposed to fluoride-induced oxidative stress damage and mitochondrial transmembrane potential loss, Toxicol. Appl. Pharmacol., 230, 352, 10.1016\u002Fj.taap.2008.03.008","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.taap.2008.03.008",{"mag":1067,"openalex":1068,"pm":1069,"doi":1070},"2159481986","W2159481986","18455746","10.1016\u002Fj.taap.2008.03.008",{"id":1072,"text":1073,"url":1074,"identifiers":1075},"4900cec6-cd4a-4587-a080-b196b461abf9","Nobes, 1995, Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia, Cell, 81, 53, 10.1016\u002F0092-8674(95)90370-4","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002F0092867495903704",{"doi":1076},"10.1016\u002F0092-8674(95)90370-4",{"id":1078,"text":1079,"url":1080,"identifiers":1081},"09434570-324f-433a-80af-740279efac67","Zhang, 2007, Effects of fluoride on the expression of NCAM, oxidative stress, and apoptosis in primary cultured hippocampal neurons, Toxicology, 236, 208, 10.1016\u002Fj.tox.2007.04.007","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0300483X07002156",{"doi":1082},"10.1016\u002Fj.tox.2007.04.007",{"id":1084,"text":1085,"url":1086,"identifiers":1087},"6915951a-cfcb-4115-ae5d-07b3e6a62efe","Ghosh, 2008, Cytoprotective effect of arjunolic acid in response to sodium fluoride mediated oxidative stress and cell death via necrotic pathway, Toxicol. In Vitro, 22, 1918, 10.1016\u002Fj.tiv.2008.09.010","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0887233308002385",{"doi":1088},"10.1016\u002Fj.tiv.2008.09.010",{"id":26,"text":1090,"url":1091,"identifiers":1092},"Mittal, 2006, Effects of individual and combined exposure to sodium arsenite and sodium fluoride on tissue oxidative stress, arsenic and fluoride levels in male mice, Chem. Biol. Interact., 162, 128, 10.1016\u002Fj.cbi.2006.05.018","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.cbi.2006.05.018",{"mag":1093,"openalex":1094,"pm":1095,"doi":1096},"2046101078","W2046101078","16828073","10.1016\u002Fj.cbi.2006.05.018",{"id":884,"text":1098,"url":886,"identifiers":1099},"Shivarajashankara, 2001, Oxidative stress in children with endemic skeletal fluorosis, Fluoride, 34, 108",{"doi":888},{"id":26,"text":1101,"url":1102,"identifiers":1103},"Ridley, 2009, Fluoride-induced cyclooxygenase-2 expression and prostaglandin E2 production in A549 human pulmonary epithelial cells, Toxicol. Lett., 188, 180, 10.1016\u002Fj.toxlet.2009.04.007","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.toxlet.2009.04.007",{"mag":1104,"openalex":1105,"pm":1106,"doi":1107},"2085428549","W2085428549","19376214","10.1016\u002Fj.toxlet.2009.04.007",{"id":26,"text":1109,"url":1110,"identifiers":1111},"Paul, 1997, Stress-activated protein kinases: activation, regulation and function, Cell Signal., 9, 403, 10.1016\u002FS0898-6568(97)00042-9","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fs0898-6568(97)00042-9",{"mag":1112,"openalex":1113,"pm":1114,"doi":1115},"2091821996","W2091821996","9376221","10.1016\u002Fs0898-6568(97)00042-9",{"id":26,"text":1117,"url":1118,"identifiers":1119},"Gremer, 2008, Fluoride complexes of oncogenic Ras mutants to study the Ras-RasGap interaction, Biol. Chem., 389, 1163, 10.1515\u002FBC.2008.132","https:\u002F\u002Fdoi.org\u002F10.1515\u002Fbc.2008.132",{"mag":1120,"openalex":1121,"pm":1122,"doi":1123},"2003378159","W2003378159","18713003","10.1515\u002Fbc.2008.132",{"id":26,"text":1125,"url":1126,"identifiers":1127},"Refsnes, 2003, Fluoride-induced apoptosis in human epithelial lung cells (A549 cells): role of different G protein-linked signal systems, Hum. Exp. Toxicol., 22, 111, 10.1191\u002F0960327103ht322oa","https:\u002F\u002Fdoi.org\u002F10.1191\u002F0960327103ht322oa",{"mag":1128,"openalex":1129,"pm":1130,"doi":1131},"2052743322","W2052743322","12723891","10.1191\u002F0960327103ht322oa",{"id":26,"text":1133,"url":1134,"identifiers":1135},"Zhan, 2006, Effects of fluoride on hepatic antioxidant system and transcription of Cu\u002FZn SOD gene in young pigs, J. Trace Elem. Med. Biol., 20, 83, 10.1016\u002Fj.jtemb.2005.11.003","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jtemb.2005.11.003",{"mag":1136,"openalex":1137,"pm":1138,"doi":1139},"1971805715","W1971805715","16785047","10.1016\u002Fj.jtemb.2005.11.003",{"id":884,"text":1141,"url":886,"identifiers":1142},"Morgan, 2002, Application of cDNA microarray technology to in vitro toxicology and the selection of genes for a real-time RT-PCR-based screen for oxidative stress in Hep-G2 Cells, Toxicol. Pathol., 30, 435",{"doi":888},{"id":26,"text":1144,"url":1145,"identifiers":1146},"Chen, 2009, Selenium increases expression of HSP70 and antioxidant enzymes to lessen oxidative damage in Fincoal-type fluorosis, J. Toxicol. Sci., 34, 399, 10.2131\u002Fjts.34.399","https:\u002F\u002Fdoi.org\u002F10.2131\u002Fjts.34.399",{"mag":1147,"openalex":1148,"pm":1149,"doi":1150},"2016150224","W2016150224","19652462","10.2131\u002Fjts.34.399",{"id":1152,"text":1153,"url":1154,"identifiers":1155},"c57bf689-4e11-49a5-94a2-e9bb1cbb5c67","Sun, 2010, Effects of sodium fluoride on hyperactivation and Ca(2+) signaling pathway in sperm from mice: an in vivo study, Arch. Toxicol., 84, 353, 10.1007\u002Fs00204-009-0508-x","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs00204-009-0508-x",{"doi":1156},"10.1007\u002Fs00204-009-0508-x",{"id":1158,"text":1159,"url":1160,"identifiers":1161},"d5a38f41-2fb5-4c86-a908-5490713a4bd3","Mohammadi, 2009, Up-regulation of CatSper genes family by selenium, Reprod. Biol. Endocrinol., 7, 126, 10.1186\u002F1477-7827-7-126","https:\u002F\u002Frbej.biomedcentral.com\u002Farticles\u002F10.1186\u002F1477-7827-7-126",{"doi":1162},"10.1186\u002F1477-7827-7-126",{"id":26,"text":1164,"url":1165,"identifiers":1166},"Matsui, 2007, Some characteristics of fluoride-induced cell death in rat thymocytes: cytotoxicity of sodium fluoride, Toxicol. In Vitro, 21, 1113, 10.1016\u002Fj.tiv.2007.04.006","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.tiv.2007.04.006",{"mag":1167,"openalex":1168,"pm":1169,"doi":1170},"2089350985","W2089350985","17544615","10.1016\u002Fj.tiv.2007.04.006",{"id":26,"text":1172,"url":1173,"identifiers":1174},"Franco, 2009, Apoptosis and glutathione: beyond an antioxidant, Cell Death Differ., 16, 1303, 10.1038\u002Fcdd.2009.107","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fcdd.2009.107",{"mag":1175,"openalex":1176,"pm":1177,"doi":1178},"2078394930","W2078394930","19662025","10.1038\u002Fcdd.2009.107",{"id":26,"text":1180,"url":1181,"identifiers":1182},"Flora, 2009, Co-exposure to arsenic and fluoride on oxidative stress, glutathione linked enzymes, biogenic amines and DNA damage in mouse brain, J. Neurol. Sci., 285, 198, 10.1016\u002Fj.jns.2009.07.001","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jns.2009.07.001",{"mag":1183,"openalex":1184,"pm":1185,"doi":1186},"2008041243","W2008041243","19635623","10.1016\u002Fj.jns.2009.07.001",{"id":1188,"text":1189,"url":1190,"identifiers":1191},"4ca257cf-3f51-4b39-af15-a76fc7e70436","Chlubek, 2003, Activity of pancreatic antioxidative enzymes and malondialdehyde concentrations in rats with hyperglycemia caused by fluoride intoxication, J. Trace Elem. Med. Biol., 17, 57, 10.1016\u002FS0946-672X(03)80047-0","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0946672X03800470",{"doi":1192},"10.1016\u002Fs0946-672x(03)80047-0",{"id":26,"text":1194,"url":1195,"identifiers":1196},"Kubota, 2005, Fluoride induces endoplasmic reticulum stress in ameloblasts responsible for dental enamel formation, J. Biol. Chem., 280, 23194, 10.1074\u002Fjbc.M503288200","https:\u002F\u002Fdoi.org\u002F10.1074\u002Fjbc.m503288200",{"mag":1197,"openalex":1198,"pm":1199,"doi":1200},"1985247208","W1985247208","15849362","10.1074\u002Fjbc.m503288200",{"id":1202,"text":1203,"url":1204,"identifiers":1205},"bb61ed14-7612-4ce0-a7ed-11aaacbb0037","Borke, 1999, Chronic fluoride ingestion decreases 45Ca uptake by rat kidney membranes, J. Nutr., 129, 1209, 10.1093\u002Fjn\u002F129.6.1209","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0022316623020771",{"doi":1206},"10.1093\u002Fjn\u002F129.6.1209",{"id":884,"text":1208,"url":886,"identifiers":1209},"Dominguez, 1991, Fluoride mobilizes intracellular calcium and promotes Ca2+ influx in rat proximal tubules, Am. J. Physiol., 261, F318",{"doi":888},{"id":1211,"text":1212,"url":1213,"identifiers":1214},"e19ffb5d-4379-4223-9a74-f6888e9be014","Hirano, 1997, Fluoride mediates apoptosis in osteosarcoma UMR 106 and its cytotoxicity depends on the pH, Arch. Toxicol., 72, 52, 10.1007\u002Fs002040050468","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs002040050468",{"doi":1215},"10.1007\u002Fs002040050468",{"id":1217,"text":1218,"url":1219,"identifiers":1220},"04a6f45b-c7d6-4fd4-85c1-106f84f0f5df","Xu, 2007, Effects of fluoride on the intracellular free Ca2+ and Ca2+-ATPase of kidney, Biol. Trace Elem. Res., 116, 279, 10.1007\u002FBF02698012","http:\u002F\u002Flink.springer.com\u002F10.1007\u002FBF02698012",{"doi":1221},"10.1007\u002FBF02698012",{"id":26,"text":1223,"url":1224,"identifiers":1225},"Murao, 2000, Sodium fluoride increases intracellular calcium in rat renal epithelial cell line NRK-52E, Biol. Pharm. Bull., 23, 581, 10.1248\u002Fbpb.23.581","https:\u002F\u002Fdoi.org\u002F10.1248\u002Fbpb.23.581",{"mag":1226,"openalex":1227,"pm":1228,"doi":1229},"1963488368","W1963488368","10823668","10.1248\u002Fbpb.23.581",{"id":26,"text":1231,"url":26,"identifiers":1232},"B. Xu, Z. Xu, T. Xia, P. He, P. Gao, W. He, M. Zhang, L. Guo, Q. Niu, A. Wang, Effects of the Fas\u002FFas-L pathway on fluoride-induced apoptosis in SH-SY5Y cells, Environ. Toxicol., in press, doi:10.1002\u002Ftox.20543.",{"doi":1233},"10.1002\u002Ftox.20543",{"id":26,"text":1235,"url":1236,"identifiers":1237},"Park, 2001, Tumor necrosis factor-related apoptosis inducing ligand (TRAIL)-induced apoptosis is dependent on activation of cysteine and serine proteases, Cytokine, 15, 166, 10.1006\u002Fcyto.2001.0893","https:\u002F\u002Fdoi.org\u002F10.1006\u002Fcyto.2001.0893",{"mag":1238,"openalex":1239,"pm":1240,"doi":1241},"2092654689","W2092654689","11554786","10.1006\u002Fcyto.2001.0893",{"id":26,"text":1243,"url":1244,"identifiers":1245},"Salgado-Bustamante, 2010, Pattern of expression of apoptosis and inflammatory genes in humans exposed to arsenic and\u002For fluoride, Sci. Total Environ., 408, 760, 10.1016\u002Fj.scitotenv.2009.11.016","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.scitotenv.2009.11.016",{"mag":1246,"openalex":1247,"pm":1248,"doi":1249},"2157840325","W2157840325","19962721","10.1016\u002Fj.scitotenv.2009.11.016",{"id":26,"text":1251,"url":26,"identifiers":1252},"Mellman, 2000, The road taken: past and future foundations of membrane traffic, Cell, 100, 99, 10.1016\u002FS0092-8674(00)81687-6",{"doi":1253},"10.1016\u002FS0092-8674(00)81687-6",{"id":26,"text":1255,"url":26,"identifiers":1256},"Yan, 2007, Micromolar fluoride alters ameloblast lineage cells in vitro, J. Dent. Res., 86, 336, 10.1177\u002F154405910708600407",{"doi":1257},"10.1177\u002F154405910708600407",{"id":26,"text":1259,"url":26,"identifiers":1260},"Aoba, 2002, Dental fluorosis: chemistry and biology, Crit. Rev. Oral Biol. Med., 13, 155, 10.1177\u002F154411130201300206",{"doi":1261},"10.1177\u002F154411130201300206",{"id":1263,"text":1264,"url":1265,"identifiers":1266},"44091e65-888a-4c96-930f-cc2cae8a08e1","Matsuo, 1996, Influence of fluoride on secretory pathway of the secretory ameloblast in rat incisor tooth germs exposed to sodium fluoride, Arch. Toxicol., 70, 420, 10.1007\u002Fs002040050294","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs002040050294",{"doi":1267},"10.1007\u002Fs002040050294",{"id":1269,"text":1270,"url":1271,"identifiers":1272},"a6fc4cb2-a379-4e3a-be86-055b66a13b21","Skobe, 1976, The secretory stage of amelogenesis in rat mandibular incisor teeth observed by scanning electron microscopy, Calcif. Tissue Res., 21, 83, 10.1007\u002FBF02547385","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02547385",{"doi":1273},"10.1007\u002FBF02547385",{"id":26,"text":1275,"url":1276,"identifiers":1277},"Sharma, 2008, Fluoride induces endoplasmic reticulum stress and inhibits protein synthesis and secretion, Environ. Health Perspect., 116, 1142, 10.1289\u002Fehp.11375","https:\u002F\u002Fdoi.org\u002F10.1289\u002Fehp.11375",{"mag":1278,"pmc":1279,"openalex":1280,"pm":1281,"doi":1282},"2058412892","2535613","W2058412892","18795154","10.1289\u002Fehp.11375",{"id":26,"text":1284,"url":1285,"identifiers":1286},"Lin, 1976, Effects of iodoacetate and fluoride on islate respiration and insulin biosynthesis, Horm. Metab. Res., 8, 353, 10.1055\u002Fs-0028-1093632","http:\u002F\u002Fdx.doi.org\u002F10.1055\u002Fs-0028-1093632",{"doi":1287},"10.1055\u002Fs-0028-1093632",{"id":884,"text":1289,"url":886,"identifiers":1290},"Komatsu, 1995, Sodium fluoride stimulates exocytosis at a late site of calcium interaction in stimulus-secretion coupling: studies with the RINm5F beta cell line, Mol. Pharmacol., 47, 496",{"doi":888},{"id":1292,"text":1293,"url":1294,"identifiers":1295},"20628fa0-4666-467c-ae56-e7adbb735d25","Borasio, 2004, Low concentrations of sodium fluoride inhibit neurotransmitter release from the guinea-pig superior cervical ganglion, Neurosci. Lett., 364, 86, 10.1016\u002Fj.neulet.2004.03.089","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0304394004004707",{"doi":1296},"10.1016\u002Fj.neulet.2004.03.089",{"id":26,"text":1298,"url":1299,"identifiers":1300},"Gardiner, 1990, Modulation of gamma-aminobutyric acid release in cerebral cortex by fluoride, phorbol ester, and phosphodiesterase inhibitors: differential sensitivity of acetylcholine release to fluoride and K+ channel blockers, J. Neurochem., 54, 1130, 10.1111\u002Fj.1471-4159.1990.tb01939.x","http:\u002F\u002Fdx.doi.org\u002F10.1111\u002Fj.1471-4159.1990.tb01939.x",{"doi":1301},"10.1111\u002Fj.1471-4159.1990.tb01939.x",{"id":26,"text":1303,"url":1304,"identifiers":1305},"Enomoto, 1995, Modification of frequency augmentation-potentiation by GTP gamma S in the frog neuromuscular junction, Cell Biochem. Funct., 13, 105, 10.1002\u002Fcbf.290130207","http:\u002F\u002Fdx.doi.org\u002F10.1002\u002Fcbf.290130207",{"doi":1306},"10.1002\u002Fcbf.290130207",{"id":26,"text":1308,"url":26,"identifiers":1309},"Blackmer, 2001, G protein betagamma subunit-mediated presynaptic inhibition: regulation of exocytotic fusion downstream of Ca2+ entry, Science, 292, 293, 10.1126\u002Fscience.1058803",{"doi":1310},"10.1126\u002Fscience.1058803",{"id":1312,"text":1313,"url":1314,"identifiers":1315},"c9cef585-bd80-4af0-8758-7b62a75ccee4","Decorti, 1999, Endocytosis of gentamicin in a proximal tubular renal cell line, Life Sci., 65, 1115, 10.1016\u002FS0024-3205(99)00345-8","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0024320599003458",{"doi":1316},"10.1016\u002Fs0024-3205(99)00345-8",{"id":26,"text":1318,"url":1319,"identifiers":1320},"Barbier, 2005, Effect of heavy metals on, and handling by, the kidney, Nephron Physiol., 99, 105, 10.1159\u002F000083981","https:\u002F\u002Fdoi.org\u002F10.1159\u002F000083981",{"mag":1321,"openalex":1322,"pm":1323,"doi":1324},"2106228333","W2106228333","15722646","10.1159\u002F000083981",{"id":26,"text":1326,"url":1327,"identifiers":1328},"Dimke, 2009, Hereditary tubular transport disorders: implications for renal handling of Ca2+ and Mg2+, Clin. Sci., 118, 1, 10.1042\u002FCS20090086","https:\u002F\u002Fdoi.org\u002F10.1042\u002Fcs20090086",{"mag":1329,"openalex":1330,"pm":1331,"doi":1332},"2097159368","W2097159368","19780717","10.1042\u002Fcs20090086",{"id":884,"text":1334,"url":886,"identifiers":1335},"Peters, 1948, Beneficial effects of calcium chloride in fluoride poisoning, Fed. Proc., 7, 92",{"doi":888},{"id":884,"text":1337,"url":886,"identifiers":1338},"Ba, 2010, Serum calciotropic hormone levels, and dental fluorosis in children exposed to different concentrations of fluoride and iodine in drinking water, Chin. Med. J., 123, 675",{"doi":888},{"id":1340,"text":1341,"url":1342,"identifiers":1343},"2b08d870-7604-4f50-a114-97522590ad72","Clapham, 1995, Calcium signalling, Cell, 80, 259, 10.1016\u002F0092-8674(95)90408-5","https:\u002F\u002Flinkinghub.elsevier.com\u002Fretrieve\u002Fpii\u002F0092867495904085",{"doi":1344},"10.1016\u002F0092-8674(95)90408-5",{"id":1346,"text":1347,"url":1348,"identifiers":1349},"b0353bcb-8974-4c81-b5b6-61f1f75bdc1d","Berridge, 2000, The versatility and universality of calcium signalling, Nat. Rev. Mol. Cell Biol., 1, 11, 10.1038\u002F35036035","https:\u002F\u002Fwww.nature.com\u002Farticles\u002F35036035",{"doi":1350},"10.1038\u002F35036035",{"id":26,"text":1352,"url":1353,"identifiers":1354},"Knot, 2005, Twenty years of calcium imaging: cell physiology to dye for, Mol. Interv., 5, 112, 10.1124\u002Fmi.5.2.8","https:\u002F\u002Fdoi.org\u002F10.1124\u002Fmi.5.2.8",{"mag":1355,"pmc":1356,"openalex":1357,"pm":1358,"doi":1359},"2139250080","4861218","W2139250080","15821159","10.1124\u002Fmi.5.2.8",{"id":1361,"text":1362,"url":1363,"identifiers":1364},"7c6ec06e-1851-496b-9a41-55206111f2ad","Das, 1993, Effect of long-term administration of sodium fluoride on plasma calcium level in relation to intestinal absorption and urinary excretion in rabbits, Environ. Res., 62, 14, 10.1006\u002Fenrs.1993.1084","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0013935183710844",{"doi":1365},"10.1006\u002Fenrs.1993.1084",{"id":26,"text":1367,"url":1368,"identifiers":1369},"Kawase, 1988, The calcium mobilizing action of low concentrations of sodium fluoride in single fibroblasts, Life Sci., 43, 1253, 10.1016\u002F0024-3205(88)90557-7","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002F0024-3205(88)90557-7",{"doi":1370},"10.1016\u002F0024-3205(88)90557-7",{"id":26,"text":1372,"url":26,"identifiers":1373},"Zerwekh, 1990, Fluoride rapidly and transiently raises intracellular calcium in human osteoblasts, J. Bone Miner. Res., 5, S131, 10.1002\u002Fjbmr.5650051320",{"doi":1374},"10.1002\u002Fjbmr.5650051320",{"id":26,"text":1376,"url":26,"identifiers":1377},"Hughes, 1987, The stimulation by sodium fluoride of plasma-membrane Ca2+ inflow in isolated hepatocytes. Evidence that a GTP-binding regulatory protein is involved in the hormonal stimulation of Ca2+ inflow, Biochem. J., 241, 41, 10.1042\u002Fbj2450041",{"doi":1378},"10.1042\u002Fbj2450041",{"id":26,"text":1380,"url":1381,"identifiers":1382},"Narayanan, 1991, Inhibitory and stimulatory effects of fluoride on the calcium pump of cardiac sarcoplasmic reticulum, Biochim. Biophys. Acta, 1070, 83, 10.1016\u002F0005-2736(91)90149-3","https:\u002F\u002Fdoi.org\u002F10.1016\u002F0005-2736(91)90149-3",{"mag":1383,"openalex":1384,"pm":1385,"doi":1386},"1997734459","W1997734459","1836355","10.1016\u002F0005-2736(91)90149-3",{"id":26,"text":1388,"url":1389,"identifiers":1390},"Davies, 2009, Organellar calcium signalling mechanisms in Drosophila epithelial function, J. Exp. Biol., 212, 387, 10.1242\u002Fjeb.024513","https:\u002F\u002Fdoi.org\u002F10.1242\u002Fjeb.024513",{"mag":1391,"openalex":1392,"pm":1393,"doi":1394},"2116645795","W2116645795","19151214","10.1242\u002Fjeb.024513",{"id":26,"text":1396,"url":1397,"identifiers":1398},"Caverzasio, 1996, Characteristics and regulation of Pi transport in osteogenic cells for bone metabolism, Kidney Int., 49, 975, 10.1038\u002Fki.1996.138","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fki.1996.138",{"mag":1399,"openalex":1400,"pm":1401,"doi":1402},"2023531176","W2023531176","8691747","10.1038\u002Fki.1996.138",{"id":1404,"text":1405,"url":1406,"identifiers":1407},"efaffb11-ba1b-45a4-b5e4-8e3e669c3739","Peerce, 1995, Effect of substrates and pH on the intestinal Na+\u002Fphosphate cotransporter: evidence for an intervesicular divalent phosphate allosteric regulatory site, Biochim Biophys. Acta, 1239, 1, 10.1016\u002F0005-2736(95)00115-J","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002F000527369500115J",{"doi":1408},"10.1016\u002F0005-2736(95)00115-j",{"id":26,"text":1410,"url":26,"identifiers":1411},"Trivedi, 1993, Reversible impairment of glucose tolerance in patients with endemic fluorosis. Fluoride Collaborative Study Group, Diabetologia, 368, 826, 10.1007\u002FBF00400357",{"doi":1412},"10.1007\u002FBF00400357",{"id":26,"text":1414,"url":1415,"identifiers":1416},"Rigalli, 1992, Bone mass increase and glucose tolerance in rats chronically treated with sodium fluoride, Bone Miner., 16, 101, 10.1016\u002F0169-6009(92)90880-M","https:\u002F\u002Fdoi.org\u002F10.1016\u002F0169-6009(92)90880-m",{"mag":1417,"openalex":1418,"pm":1419,"doi":1420},"2041981701","W2041981701","1576485","10.1016\u002F0169-6009(92)90880-m",{"id":884,"text":1422,"url":886,"identifiers":1423},"Menoyo, 2005, Effect of fluoride on the secretion of insulin in the rat, Arzneimittelforschung, 55, 455",{"doi":888},{"id":26,"text":1425,"url":1426,"identifiers":1427},"Yuasa, 2009, The Rab GTPase-activating protein AS160 as a common regulator of insulin- and Galphaq-mediated intracellular GLUT4 vesicle distribution, Endocr. J., 56, 345, 10.1507\u002Fendocrj.K08E-216","http:\u002F\u002Fdx.doi.org\u002F10.1507\u002Fendocrj.k08e-216",{"doi":1428},"10.1507\u002Fendocrj.k08e-216",{"id":26,"text":1430,"url":1431,"identifiers":1432},"Suketa, 2002, Fundamental and applied studies on transport and metabolism of electrolytes and glucose—aim to contact with molecular biology, Yakugaku Zasshi., 122, 507, 10.1248\u002Fyakushi.122.507","https:\u002F\u002Fdoi.org\u002F10.1248\u002Fyakushi.122.507",{"mag":1433,"openalex":1434,"pm":1435,"doi":1436},"2949966509","W2949966509","12187767","10.1248\u002Fyakushi.122.507",{"id":26,"text":1438,"url":1439,"identifiers":1440},"Murphy, 1992, Inhibition of the Na,K-ATPase by fluoride. Parallels with its inhibition of the sarcoplasmic reticulum CaATPase, J. Biol. Chem., 267, 16700, 10.1016\u002FS0021-9258(18)41883-2","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fs0021-9258(18)41883-2",{"mag":1441,"openalex":1442,"pm":1443,"doi":1444},"1596604986","W1596604986","1324918","10.1016\u002Fs0021-9258(18)41883-2",{"id":26,"text":1446,"url":26,"identifiers":1447},"Suketa, 1995, Effect of fluoride on the activities of the Na+\u002Fglucose cotransporter and Na+\u002FK(+)-ATPase in brush border and basolateral membranes of rat kidney (in vitro and in vivo), Biol. Pharm. Bull., 18, 273, 10.1248\u002Fbpb.18.273",{"doi":1448},"10.1248\u002Fbpb.18.273",{"id":26,"text":1450,"url":1451,"identifiers":1452},"Cittanova, 2002, Fluoride ion toxicity in rabbit kidney thick ascending limb cells, Eur. J. Anaesthesiol., 19, 341, 10.1097\u002F00003643-200205000-00005","https:\u002F\u002Fdoi.org\u002F10.1017\u002Fs0265021502000558",{"mag":1453,"openalex":1454,"pm":1455,"doi":1456},"2143024740","W2143024740","12095014","10.1017\u002Fs0265021502000558",{"id":26,"text":1458,"url":1459,"identifiers":1460},"Ekambaram, 2002, Modulation of fluoride toxicity in rats by calcium carbonate and by withdrawal of fluoride exposure, Pharmacol. Toxicol., 90, 53, 10.1034\u002Fj.1600-0773.2002.900201.x","https:\u002F\u002Fdoi.org\u002F10.1034\u002Fj.1600-0773.2002.900201.x",{"mag":1461,"openalex":1462,"pm":1463,"doi":1464},"2064736337","W2064736337","12071426","10.1034\u002Fj.1600-0773.2002.900201.x",{"id":884,"text":1466,"url":886,"identifiers":1467},"Kravtsova, 2004, Inactivation of Na+, K+-ATPase from cattle brain by sodium fluoride, Ukr. Biokhim. Zh., 76, 39",{"doi":888},{"id":1469,"text":1470,"url":1471,"identifiers":1472},"e2d5cc4e-2125-4a54-9e43-94ce519982d3","Anderson, 1984, Effects of cortisol and fluoride on ion-transporting ATPase activities in cultured osteoblastlike cells, In Vitro, 20, 847, 10.1007\u002FBF02619630","http:\u002F\u002Flink.springer.com\u002F10.1007\u002FBF02619630",{"doi":1473},"10.1007\u002FBF02619630",{"id":26,"text":1475,"url":1476,"identifiers":1477},"L’hoste, 2009, CFTR mediates cadmium-induced apoptosis through modulation of ROS level in mouse proximal tubule cells, Free Radic. Biol. Med., 46, 1017, 10.1016\u002Fj.freeradbiomed.2008.12.009","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002Fj.freeradbiomed.2008.12.009",{"doi":1478},"10.1016\u002Fj.freeradbiomed.2008.12.009",{"id":884,"text":1480,"url":886,"identifiers":1481},"Berger, 1998, Fluoride stimulates cystic fibrosis transmembrane conductance regulator Cl− channel activity, Am. J. Physiol., 274, L305",{"doi":888},{"id":26,"text":1483,"url":1484,"identifiers":1485},"Shanthakumari, 2004, Effect of fluoride intoxication on lipid peroxidation and antioxidant status in experimental rats, Toxicology, 204, 219, 10.1016\u002Fj.tox.2004.06.058","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002Fj.tox.2004.06.058",{"doi":1486},"10.1016\u002Fj.tox.2004.06.058",{"id":26,"text":1488,"url":1489,"identifiers":1490},"Chouhan, 2010, Fluoride-induced changes in haem biosynthesis pathway, neurological variables and tissue histopathology of rats, J. Appl. Toxicol., 30, 63, 10.1002\u002Fjat.1474","https:\u002F\u002Fdoi.org\u002F10.1002\u002Fjat.1474",{"mag":1491,"openalex":1492,"pm":1493,"doi":1494},"2010351226","W2010351226","19743388","10.1002\u002Fjat.1474",{"id":26,"text":1496,"url":1497,"identifiers":1498},"Arakawa, 2009, Low concentration fluoride stimulates cell motility of epithelial cells in vitro, Biomed. Res., 30, 271, 10.2220\u002Fbiomedres.30.271","https:\u002F\u002Fdoi.org\u002F10.2220\u002Fbiomedres.30.271",{"mag":1499,"openalex":1500,"pm":1501,"doi":1502},"2000962313","W2000962313","19887723","10.2220\u002Fbiomedres.30.271",{"id":26,"text":1504,"url":26,"identifiers":1505},"Jing, 2006, Effects of overdosed fluoride on rat's incisor expression of matrix metalloproteinase-20 and tissue inhibitors of metalloproteinase-2, Hua Xi Kou Qiang Yi Xue Za Zhi, 24, 199",{},{"id":26,"text":1507,"url":26,"identifiers":1508},"Li, 2006, Effect of industrial fluoride pollution on col2a1 gene expression in rib cartilage of Inner Mongolia cashmere goats, Fluoride, 39, 285",{},{"id":884,"text":1510,"url":886,"identifiers":1511},"Jia, 2006, Combined effect of fluoride and arsenate on gene expression of osteoclast differentiation factor and osteoprotegerin, Biomed. Environ. Sci., 19, 375",{"doi":888},{"id":1513,"text":1514,"url":1515,"identifiers":1516},"d90b3f70-62cf-4c79-bbee-bf6f8d673d06","Wurtz, 2008, Fluoride at non-toxic dose affects odontoblast gene expression in vitro, Toxicology, 249, 26, 10.1016\u002Fj.tox.2008.04.013","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0300483X08001650",{"doi":1517},"10.1016\u002Fj.tox.2008.04.013",{"id":26,"text":1519,"url":1520,"identifiers":1521},"Wang, 2005, Effects on protein and mRNA expression levels of p53 induced by fluoride in human embryonic hepatocytes, Toxicol. Lett., 158, 158, 10.1016\u002Fj.toxlet.2005.03.010","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.toxlet.2005.03.010",{"mag":1522,"openalex":1523,"pm":1524,"doi":1525},"2052099540","W2052099540","15950406","10.1016\u002Fj.toxlet.2005.03.010",{"id":26,"text":1527,"url":1528,"identifiers":1529},"Vousden, 2002, Live or let die: the cell's response to p53, Nat. Rev. Cancer, 2, 594, 10.1038\u002Fnrc864","http:\u002F\u002Fdx.doi.org\u002F10.1038\u002Fnrc864",{"doi":1530},"10.1038\u002Fnrc864",{"id":26,"text":1532,"url":26,"identifiers":1533},"Lund, 2002, Human exposure to hydrogen fluoride induces acute neutrophilic, eicosanoid, and antioxidant changes in nasal lavage fluid, Inhal. Toxicol., 14, 119, 10.1080\u002F089583701753403944",{"doi":1534},"10.1080\u002F089583701753403944",{"id":26,"text":1536,"url":1537,"identifiers":1538},"Aydin, 2003, Histopathological and biochemical changes in lung tissues of rats following administration of fluoride over several generations, J. Appl. Toxicol., 23, 437, 10.1002\u002Fjat.935","https:\u002F\u002Fdoi.org\u002F10.1002\u002Fjat.935",{"mag":1539,"openalex":1540,"pm":1541,"doi":1542},"1495124424","W1495124424","14635268","10.1002\u002Fjat.935",{"id":26,"text":1544,"url":1545,"identifiers":1546},"Mukaida, 2003, Pathophysiological roles of interleukin-8\u002FCXCL8 in pulmonary diseases, Am. J. Physiol. Lung Cell. Mol. Physiol., 284, L566, 10.1152\u002Fajplung.00233.2002","https:\u002F\u002Fdoi.org\u002F10.1152\u002Fajplung.00233.2002",{"mag":1547,"openalex":1548,"pm":1549,"doi":1550},"2136822492","W2136822492","12618418","10.1152\u002Fajplung.00233.2002",{"id":26,"text":1552,"url":1553,"identifiers":1554},"Schwarze, 2000, Role of signal transduction pathways in lung inflammatory responses, Toxicol. Lett., 112–113, 165, 10.1016\u002FS0378-4274(99)00280-5","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fs0378-4274(99)00280-5",{"mag":1555,"openalex":1556,"pm":1557,"doi":1558},"2121672205","W2121672205","10720727","10.1016\u002Fs0378-4274(99)00280-5",{"id":26,"text":1560,"url":1561,"identifiers":1562},"Wölfl, 1996, In vitro activation of the NADPH oxidase by fluoride. Possible involvement of a factor activating GTP hydrolysis on Rac (Rac-GAP), Eur. J. Biochem., 239, 369, 10.1111\u002Fj.1432-1033.1996.0369u.x","https:\u002F\u002Fhal.science\u002Fhal-00820790",{"openalex":1563,"doi":1564},"W4390647974","10.1111\u002Fj.1432-1033.1996.0369u.x",{"id":26,"text":1566,"url":1567,"identifiers":1568},"Miranda, 2007, Endothelium-dependent and -independent hepatic artery vasodilatation is not impaired in a canine model of liver ischemia-reperfusion injury, Braz. J. Med. Biol. Res., 40, 857, 10.1590\u002FS0100-879X2007000600016","https:\u002F\u002Fdoi.org\u002F10.1590\u002Fs0100-879x2007000600016",{"mag":1569,"openalex":1570,"pm":1571,"doi":1572},"2035768041","W2035768041","17581686","10.1590\u002Fs0100-879x2007000600016",{"id":26,"text":1574,"url":1575,"identifiers":1576},"Wang, 2001, Mechanisms of sodium fluoride-induced endothelial cell barrier dysfunction: role of MLC phosphorylation, Am. J. Physiol. Lung Cell Mol. Physiol., 281, L1472, 10.1152\u002Fajplung.2001.281.6.L1472","https:\u002F\u002Fdoi.org\u002F10.1152\u002Fajplung.2001.281.6.l1472",{"mag":1577,"openalex":1578,"pm":1579,"doi":1580},"1905874194","W1905874194","11704544","10.1152\u002Fajplung.2001.281.6.l1472",{"id":26,"text":1582,"url":1583,"identifiers":1584},"Rønneberg, 1995, Mortality and cancer morbidity in workers from an aluminium smelter with prebaked carbon anodes—part III: mortality from circulatory and respiratory diseases, Occup. Environ. Med., 52, 255, 10.1136\u002Foem.52.4.255","https:\u002F\u002Fdoi.org\u002F10.1136\u002Foem.52.4.255",{"mag":1585,"pmc":1586,"openalex":1587,"pm":1588,"doi":1589},"2122195617","1128204","W2122195617","7795741","10.1136\u002Foem.52.4.255",{"id":1591,"text":1592,"url":1593,"identifiers":1594},"695a1c2f-94e9-493c-ac9e-cb0fda8c934d","Varol, 2010, Aortic elasticity is impaired in patients with endemic fluorosis, Biol. Trace Elem. Res., 133, 121, 10.1007\u002Fs12011-009-8578-4","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs12011-009-8578-4",{"doi":1595},"10.1007\u002Fs12011-009-8578-4",{"id":1597,"text":1598,"url":1599,"identifiers":1600},"9ebf3bcc-0d8d-421b-9569-7196f313bea5","Zigmond, 1996, Signal transduction and actin filament organization, Curr. Opin. Cell Biol., 8, 66, 10.1016\u002FS0955-0674(96)80050-0","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0955067496800500",{"doi":1601},"10.1016\u002Fs0955-0674(96)80050-0",{"id":26,"text":1603,"url":1604,"identifiers":1605},"Hall, 2005, Rho, GTPases and the control of cell behavior, Biochem. Soc. Trans., 33, 891, 10.1042\u002FBST0330891","http:\u002F\u002Fdx.doi.org\u002F10.1042\u002Fbst20050891",{"doi":1606},"10.1042\u002Fbst20050891",{"id":26,"text":1608,"url":1609,"identifiers":1610},"Ridley, 1992, Distinct patterns of actin organization regulated by the small GTP-binding proteins Rac and Rho, Cold Spring Harb. Symp. Quant. Biol., 57, 661, 10.1101\u002FSQB.1992.057.01.072","https:\u002F\u002Fdoi.org\u002F10.1101\u002Fsqb.1992.057.01.072",{"mag":1611,"openalex":1612,"pm":1613,"doi":1614},"1984455350","W1984455350","1339704","10.1101\u002Fsqb.1992.057.01.072",{"id":26,"text":1616,"url":1617,"identifiers":1618},"Takai, 2001, Small GTP-binding proteins, Physiol. Rev., 81, 153, 10.1152\u002Fphysrev.2001.81.1.153","https:\u002F\u002Fdoi.org\u002F10.1152\u002Fphysrev.2001.81.1.153",{"mag":1619,"openalex":1620,"pm":1621,"doi":1622},"2111778006","W2111778006","11152757","10.1152\u002Fphysrev.2001.81.1.153",{"id":26,"text":1624,"url":1625,"identifiers":1626},"Oka, 1994, Inhibition of GTP hydrolysis by Sar1p causes accumulation of vesicles that are a functional intermediate of the ER-to-Golgi transport in yeast, J. Cell. Biol., 124, 425, 10.1083\u002Fjcb.124.4.425","https:\u002F\u002Fdoi.org\u002F10.1083\u002Fjcb.124.4.425",{"mag":1627,"pmc":1628,"openalex":1629,"pm":1630,"doi":1631},"2094503700","2119918","W2094503700","8106544","10.1083\u002Fjcb.124.4.425",{"id":26,"text":1633,"url":1634,"identifiers":1635},"Radhakrishna, 1996, Aluminum fluoride stimulates surface protrusions in cells overexpressing the ARF6 GTPase, J. Cell. Biol., 134, 935, 10.1083\u002Fjcb.134.4.935","https:\u002F\u002Fdoi.org\u002F10.1083\u002Fjcb.134.4.935",{"mag":1636,"pmc":1637,"openalex":1638,"pm":1639,"doi":1640},"2119438819","2120964","W2119438819","8769418","10.1083\u002Fjcb.134.4.935",{"id":26,"text":1642,"url":1643,"identifiers":1644},"Chabre, 1990, Aluminofluoride and beryllofluoride complexes: a new phosphate analogs in enzymology, Trends Biochem. Sci., 15, 6, 10.1016\u002F0968-0004(90)90117-T","https:\u002F\u002Fdoi.org\u002F10.1016\u002F0968-0004(90)90117-t",{"mag":1645,"openalex":1646,"pm":1647,"doi":1648},"2074129396","W2074129396","2180149","10.1016\u002F0968-0004(90)90117-t",{"id":26,"text":1650,"url":1651,"identifiers":1652},"Norman, 1994, Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins, J. Cell. Biol., 126, 1005, 10.1083\u002Fjcb.126.4.1005","https:\u002F\u002Fdoi.org\u002F10.1083\u002Fjcb.126.4.1005",{"mag":1653,"pmc":1654,"openalex":1655,"pm":1656,"doi":1657},"2169132737","2120121","W2169132737","8051203","10.1083\u002Fjcb.126.4.1005",{"id":26,"text":1659,"url":1660,"identifiers":1661},"Horgan, 1984, Developmental expression of G proteins in a migratory population of embryonic neurons, Development, 120, 729, 10.1242\u002Fdev.120.4.729","http:\u002F\u002Fdx.doi.org\u002F10.1242\u002Fdev.120.4.729",{"doi":1662},"10.1242\u002Fdev.120.4.729",{"id":26,"text":1664,"url":1665,"identifiers":1666},"M. Inoue, A.P. Rodriguez, N. Nagai, H. Nagatsuka, R.Z. Legeros, H. Tsujigiwa, M. Inoue, E. Kishimoto, S. Takagi, Effect of fluoride-substituted apatite on in vivo bone formation, J. Biomater. Appl., in press, doi:10.1177\u002F0885328209357109.","https:\u002F\u002Fdoi.org\u002F10.1177\u002F0885328209357109",{"mag":1667,"openalex":1668,"pm":1669,"doi":1670},"2027270442","W2027270442","20219846","10.1177\u002F0885328209357109",{"id":26,"text":1672,"url":1673,"identifiers":1674},"Crichlow, 2009, Structural and kinetic analyses of macrophage migration inhibitory factor active site interactions, Biochemistry, 48, 132, 10.1021\u002Fbi8014423","https:\u002F\u002Fdoi.org\u002F10.1021\u002Fbi8014423",{"openalex":1675,"pm":1676,"doi":1677},"W4298281524","19090677","10.1021\u002Fbi8014423",{"id":26,"text":1679,"url":1680,"identifiers":1681},"Tatin, 2010, Sodium fluoride induces podosome formation in endothelial cells, Biol. Cell., 102, 489, 10.1042\u002FBC20100030","https:\u002F\u002Fdoi.org\u002F10.1042\u002Fbc20100030",{"mag":1682,"openalex":1683,"pm":1684,"doi":1685},"2122842079","W2122842079","20504277","10.1042\u002Fbc20100030",{"id":26,"text":1687,"url":1688,"identifiers":1689},"Thrane, 2001, Fluoride-induced apoptosis in epithelial lung cells involves activation of MAP kinases p38 and possibly JNK, Toxicol. Sci., 61, 83, 10.1093\u002Ftoxsci\u002F61.1.83","https:\u002F\u002Fdoi.org\u002F10.1093\u002Ftoxsci\u002F61.1.83",{"mag":1690,"openalex":1691,"pm":1692,"doi":1693},"2115575149","W2115575149","11294978","10.1093\u002Ftoxsci\u002F61.1.83",{"id":884,"text":1695,"url":886,"identifiers":1696},"Thaweboon, 2003, Effect of fluoride on human dental pulp cells in vitro, Southeast Asian J. Trop. Med. Public Health, 34, 915",{"doi":888},{"id":26,"text":1698,"url":1699,"identifiers":1700},"Khokher, 1990, Fluoride stimulates [3H]thymidine incorporation and alkaline phosphatase production by human osteoblasts, Metabolism, 39, 1118, 10.1016\u002F0026-0495(90)90081-M","http:\u002F\u002Fdx.doi.org\u002F10.1016\u002F0026-0495(90)90081-m",{"doi":1701},"10.1016\u002F0026-0495(90)90081-m",{"id":26,"text":1703,"url":1704,"identifiers":1705},"Inoue, 2005, In vivo effect of fluoride-substituted apatite on rat bone, Dent. Mater. J., 24, 398, 10.4012\u002Fdmj.24.398","https:\u002F\u002Fdoi.org\u002F10.4012\u002Fdmj.24.398",{"mag":1706,"openalex":1707,"pm":1708,"doi":1709},"2022440034","W2022440034","16279730","10.4012\u002Fdmj.24.398",{"id":884,"text":1711,"url":886,"identifiers":1712},"Yamaguchi, 2007, Fluoride and bone metabolism, Clin. Calcium, 17, 217",{"doi":888},{"id":884,"text":1714,"url":886,"identifiers":1715},"Zhang, 2003, Effects of fluoride on cell cycle and apoptosis in cultured osteoblasts of rats, Wei Sheng Yan Jiu, 32, 432",{"doi":888},{"id":884,"text":1717,"url":886,"identifiers":1718},"Yu, 2002, Effects of selenium and zinc on rat renal apoptosis and change of cell cycle induced by fluoride, Zhonghua Yu Fang Yi Xue Za Zhi, 36, 219",{"doi":888},{"id":26,"text":1720,"url":1721,"identifiers":1722},"Lu, 2010, Proteomics analysis of liver samples from puffer fish Takifugu rubripes exposed to excessive fluoride: an insight into molecular response to fluorosis, J. Biochem. Mol. Toxicol., 24, 21, 10.1002\u002Fjbt.20308","https:\u002F\u002Fdoi.org\u002F10.1002\u002Fjbt.20308",{"mag":1723,"openalex":1724,"pm":1725,"doi":1726},"2012761315","W2012761315","20146379","10.1002\u002Fjbt.20308",{"id":26,"text":1728,"url":1729,"identifiers":1730},"Zeiger, 1993, Genetic toxicity of fluoride, Environ. Mol. Mutagen., 21, 309, 10.1002\u002Fem.2850210402","https:\u002F\u002Fdoi.org\u002F10.1002\u002Fem.2850210402",{"mag":1731,"openalex":1732,"pm":1733,"doi":1734},"2100818953","W2100818953","8491210","10.1002\u002Fem.2850210402",{"id":1736,"text":1737,"url":1738,"identifiers":1739},"12b5db03-e127-486e-8c90-3f092b7d7c00","Tiwari, 2010, Curcumin supplementation protects from genotoxic effects of arsenic and fluoride, Food Chem. Toxicol., 48, 1234, 10.1016\u002Fj.fct.2010.02.015","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS027869151000116X",{"doi":1740},"10.1016\u002Fj.fct.2010.02.015",{"id":26,"text":1742,"url":1743,"identifiers":1744},"Mahoney, 1991, Bone cancer incidence rates in New York State: time trends and fluoridated drinking water, Am. J. Public Health, 81, 475, 10.2105\u002FAJPH.81.4.475","https:\u002F\u002Fdoi.org\u002F10.2105\u002Fajph.81.4.475",{"mag":1745,"pmc":1746,"openalex":1747,"pm":1748,"doi":1749},"2091335786","1405037","W2091335786","2003628","10.2105\u002Fajph.81.4.475",{"id":884,"text":1751,"url":886,"identifiers":1752},"Ramesh, 2001, Low levels of p53 mutations in Indian patients with osteosarcoma and the correlation with fluoride levels in bone, J. Environ. Pathol. Toxicol. Oncol., 20, 237",{"doi":888},{"id":26,"text":1754,"url":1755,"identifiers":1756},"Eyre, 2009, Epidemiology of bone tumours in children and young adults, Pediatr. Blood Cancer, 53, 941, 10.1002\u002Fpbc.22194","http:\u002F\u002Fdx.doi.org\u002F10.1002\u002Fpbc.22194",{"doi":1757},"10.1002\u002Fpbc.22194",{"id":26,"text":1759,"url":1760,"identifiers":1761},"Schlichting, 1999, pH influences fluoride coordination number of the AlFx phosphoryl transfer transition state analog, Nat. Struct. Biol., 6, 721, 10.1038\u002F11485","https:\u002F\u002Fdoi.org\u002F10.1038\u002F11485",{"mag":1762,"openalex":1763,"pm":1764,"doi":1765},"2151920771","W2151920771","10426946","10.1038\u002F11485",{"id":884,"text":1767,"url":886,"identifiers":1768},"Strunecká, 2002, Fluoride plus aluminum: useful tools in laboratory investigations, but messengers of false information, Physiol. Res., 51, 557",{"doi":888},{"id":26,"text":1770,"url":26,"identifiers":1771},"Li, 2003, The biochemistry and physiology of metallic fluoride: action, mechanism, and implications, Crit. Rev. Oral Biol. Med., 14, 100, 10.1177\u002F154411130301400204",{"doi":1772},"10.1177\u002F154411130301400204",{"id":26,"text":1774,"url":1775,"identifiers":1776},"McLachlan, 1996, Risk for neuropathologically confirmed Alzheimer's disease and residual aluminum in municipal drinking water employing weighted residential histories, Neurology, 46, 401, 10.1212\u002FWNL.46.2.401","http:\u002F\u002Fdx.doi.org\u002F10.1212\u002Fwnl.46.2.401",{"doi":1777},"10.1212\u002Fwnl.46.2.401",{"id":26,"text":1779,"url":1780,"identifiers":1781},"Kawahara, 2005, Effects of aluminum on the nervous system and its possible link with neurodegenerative diseases, J. Alzheimers Dis., 8, 171, 10.3233\u002FJAD-2005-8210","https:\u002F\u002Fdoi.org\u002F10.3233\u002Fjad-2005-8210",{"mag":1782,"openalex":1783,"pm":1784,"doi":1785},"101981630","W101981630","16308486","10.3233\u002Fjad-2005-8210",{"id":884,"text":1787,"url":886,"identifiers":1788},"Still, 1994, Aluminum neurotoxicity and Alzheimer's disease, J. S. C. Med. Assoc., 90, 560",{"doi":888},{"id":26,"text":1790,"url":26,"identifiers":1791},"Kraus, 1992, Aluminum, fluoride and the prevention of Alzheimer's disease, Can. J. Public Health, 83, 97",{},{"id":26,"text":1793,"url":1794,"identifiers":1795},"Shcherbatykh, 2007, The role of metals in the etiology of Alzheimer's disease, J. Alzheimers Dis., 11, 191, 10.3233\u002FJAD-2007-11207","http:\u002F\u002Fdx.doi.org\u002F10.3233\u002Fjad-2007-11207",{"doi":1796},"10.3233\u002Fjad-2007-11207",{"id":26,"text":1798,"url":1799,"identifiers":1800},"Mittal, 2007, Vitamin E supplementation protects oxidative stress during arsenic and fluoride antagonism in male mice, Drug Chem. Toxicol., 3, 263, 10.1080\u002F01480540701380075","https:\u002F\u002Fdoi.org\u002F10.1080\u002F01480540701380075",{"mag":1801,"openalex":1802,"pm":1803,"doi":1804},"2117778626","W2117778626","17613011","10.1080\u002F01480540701380075",{"id":1806,"text":1807,"url":1808,"identifiers":1809},"7c356a64-08fd-4712-8afe-f634f5446476","Del Razo, 1993, Fluoride levels in well-water from a chronic arsenicism area of Northern Mexico, Environ. Pollut., 80, 91, 10.1016\u002F0269-7491(93)90015-G","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002F026974919390015G",{"doi":1810},"10.1016\u002F0269-7491(93)90015-g",{"id":1812,"text":1813,"url":1814,"identifiers":1815},"109a78c6-3a28-445f-b53f-4d09e0770137","Zheng, 2002, The absorption and excretion of fluoride and arsenic in humans, Toxicol. Lett., 133, 77, 10.1016\u002FS0378-4274(02)00082-6","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0378427402000826",{"doi":1816},"10.1016\u002FS0378-4274(02)00082-6",{"id":26,"text":1818,"url":1819,"identifiers":1820},"Rocha-Amador, 2007, Decreased intelligence in children and exposure to fluoride and arsenic in drinking water, Cad. Saude Publica, 23, S579, 10.1590\u002FS0102-311X2007001600018","https:\u002F\u002Fdoi.org\u002F10.1590\u002Fs0102-311x2007001600018",{"mag":1821,"openalex":1822,"pm":1823,"doi":1824},"2119249685","W2119249685","18038039","10.1590\u002Fs0102-311x2007001600018",{"id":884,"text":1826,"url":886,"identifiers":1827},"Masters, 2000, Association of silicofluoride treated water with elevated blood lead, Neurotoxicology, 21, 1091",{"doi":888},{"id":26,"text":1829,"url":1830,"identifiers":1831},"Macek, 2006, Blood lead concentrations in children and method of water fluoridation in the United States, 1988–1994, Environ. Health Perspect., 114, 130, 10.1289\u002Fehp.8319","https:\u002F\u002Fdoi.org\u002F10.1289\u002Fehp.8319",{"mag":1832,"pmc":1833,"openalex":1834,"pm":1835,"doi":1836},"2063219996","1332668","W2063219996","16393670","10.1289\u002Fehp.8319",{"id":1838,"text":1839,"url":1840,"identifiers":1841},"d35de41f-a96f-4990-8179-3ac9761b5c7a","Maas, 2007, Effects of fluoridation and disinfection agent combinations on lead leaching from leaded-brass parts, Neurotoxicology, 28, 1023, 10.1016\u002Fj.neuro.2007.06.006","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0161813X07001404",{"doi":1842},"10.1016\u002Fj.neuro.2007.06.006",{"id":1844,"text":1845,"url":1846,"identifiers":1847},"cd838637-d854-40af-b5f3-23f31cd41fe2","Sawan, 2010, Fluoride increases lead concentrations in whole blood and in calcified tissues from lead-exposed rats, Toxicology, 271, 21, 10.1016\u002Fj.tox.2010.02.002","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0300483X10000351",{"doi":1848},"10.1016\u002Fj.tox.2010.02.002",{"id":1850,"text":1851,"url":1852,"identifiers":1853},"17d41808-74b7-4347-bffb-0177d6d12117","Gao, 2008, Oxidative stress might be a mechanism connected with the decreased alpha 7 nicotinic receptor influenced by high-concentration of fluoride in SH-SY5Y neuroblastoma cells, Toxicol, In Vitro, 22, 837, 10.1016\u002Fj.tiv.2007.12.017","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0887233308000027",{"doi":1854},"10.1016\u002Fj.tiv.2007.12.017",{"id":26,"text":1856,"url":26,"identifiers":1857},"Z.H. Wang, X.L. Li, Z.Q. Yang, M. Xu, Fluorine-induced apoptosis and lipid peroxidation in human hair follicles, In Vitro Biol. Trace Elem. Res., in press, doi:10.1007\u002Fs12011-009r-r8592-6.",{"doi":1858},"10.1007\u002Fs12011-009r-r8592-6",{"id":26,"text":1860,"url":26,"identifiers":1861},"Ghosh, 2002, Testicular toxicity in sodium fluoride treated rats; association with oxidative stress, Reprod. Toxicol., 16, 383, 10.1016\u002FS0890-6238(02)00038-2",{"doi":1862},"10.1016\u002FS0890-6238(02)00038-2",{"id":26,"text":1864,"url":26,"identifiers":1865},"Guo, 2003, Oxidative stress from fluoride-induced hepatotoxicity in rats, Fluoride, 36, 25",{},{"id":26,"text":1867,"url":26,"identifiers":1868},"Zhan, 2005, Effects of fluorosis on lipid peroxidation and antioxidant systems in young pigs, Fluoride, 38, 157",{},{"id":26,"text":1870,"url":26,"identifiers":1871},"Guney, 2007, Protective effects of vitamins C and E against endometrial damage and oxidative stress in fluoride intoxication, Clin. Exp. Pharmacol. Physiol., 34, 467, 10.1111\u002Fj.1440-1681.2007.04596.x",{"doi":1872},"10.1111\u002Fj.1440-1681.2007.04596.x",{"id":1874,"text":1875,"url":1876,"identifiers":1877},"3f8089d3-9fce-452b-842c-9884cd98d0e8","Chouhan, 2008, Effects of fluoride on the tissue oxidative stress and apoptosis in rats: biochemical assays supported by IR spectroscopy data, Toxicology, 254, 61, 10.1016\u002Fj.tox.2008.09.008","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0300483X08004344",{"doi":1878},"10.1016\u002Fj.tox.2008.09.008",{"id":1880,"text":1881,"url":1882,"identifiers":1883},"d501e882-15d2-4b5c-b98e-a4735dd9b9b1","Jhala, 2008, Mitigating effects of some antidotes on fluoride and arsenic induced free radical toxicity in mice ovary, Food Chem. Toxicol., 46, 1138, 10.1016\u002Fj.fct.2007.11.009","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0278691507005339",{"doi":1884},"10.1016\u002Fj.fct.2007.11.009",{"id":1886,"text":1887,"url":1888,"identifiers":1889},"57b26e31-c736-4638-acbc-59f2d3e47738","Kanbur, 2009, Effects of sodium fluoride exposure on some biochemical parameters in mice: evaluation of the ameliorative effect of royal jelly applications on these parameters, Food Chem. Toxicol., 47, 1184, 10.1016\u002Fj.fct.2009.02.008","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS027869150900074X",{"doi":1890},"10.1016\u002Fj.fct.2009.02.008",{"id":26,"text":1892,"url":1893,"identifiers":1894},"Bharti, 2009, Fluoride-induced oxidative stress in rat's brain and its amelioration by buffalo (bubalus bubalis) pineal proteins and melatonin, Biol. Trace Elem. Res., 130, 131, 10.1007\u002Fs12011-009-8320-2","http:\u002F\u002Fdx.doi.org\u002F10.1007\u002Fs12011-009-8320-2",{"doi":1895},"10.1007\u002Fs12011-009-8320-2",{"id":26,"text":1897,"url":1898,"identifiers":1899},"Basha, 2010, Pre and post natal exposure of fluoride induced oxidative macromolecular alterations in developing central nervous system of rat and amelioration by antioxidants, Neurochem. 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Free Rad. Biol. Med., 2, 211, 10.1016\u002FS8755-9668(86)80030-8",{"doi":1998},"10.1016\u002FS8755-9668(86)80030-8",{"id":26,"text":2000,"url":26,"identifiers":2001},"Kersten, 1971, Inhibition of RNA synthesis by quinone antibiotics, Prog. Mol. Subcell. Biol., 2, 48, 10.1007\u002F978-3-642-65141-0_6",{"doi":2002},"10.1007\u002F978-3-642-65141-0_6",{"id":26,"text":2004,"url":26,"identifiers":2005},"Olenick, 1974, Bactericidal action of a 2 hydroxy-3-alkyl-1,4 naphthoquinone, Ann. N.Y. Acad. Sci., 235, 542, 10.1111\u002Fj.1749-6632.1974.tb43289.x",{"doi":2006},"10.1111\u002Fj.1749-6632.1974.tb43289.x",{"id":26,"text":2008,"url":26,"identifiers":2009},"Rich, 1969, Quinones",{},{"id":26,"text":2011,"url":26,"identifiers":2012},"Martin, 1973, Relationship between physical properties and antimalarial activities of 1,4-naphthoquinone, J. Med. Chem., 16, 1089, 10.1021\u002Fjm00268a005",{"doi":2013},"10.1021\u002Fjm00268a005",{"id":26,"text":2015,"url":26,"identifiers":2016},"Eisner, 1977, Defense mechanisms of anthropods. 57. Chemistry of defensive secretions of bombardier beetles, J. Insect. Physiol., 23, 1383, 10.1016\u002F0022-1910(77)90162-7",{"doi":2017},"10.1016\u002F0022-1910(77)90162-7",{"id":26,"text":2019,"url":26,"identifiers":2020},"Driscoll, 1974, Structure-antitumor activity relations among quinone derivatives, Cancer Chemother., Rep., 4, 1",{},{"id":26,"text":2022,"url":26,"identifiers":2023},"Powis, 1989, Free radical formation by antitumor quinones, Free Rad. Biol. Med., 6, 63, 10.1016\u002F0891-5849(89)90162-7",{"doi":2024},"10.1016\u002F0891-5849(89)90162-7",{"id":26,"text":2026,"url":26,"identifiers":2027},"Powis, 1987, Metabolism and reactions of quinoid anticancer agents, Pharmacol. Ther., 35, 57, 10.1016\u002F0163-7258(87)90105-7",{"doi":2028},"10.1016\u002F0163-7258(87)90105-7",{"id":26,"text":2030,"url":26,"identifiers":2031},"Deeley, 1980, A clinical trial of synkavit in the treatment of carcinoma of the bronchus, Br. J. Cancer, 16, 387, 10.1038\u002Fbjc.1962.44",{"doi":2032},"10.1038\u002Fbjc.1962.44",{"id":26,"text":2034,"url":26,"identifiers":2035},"Beckman, 1985, Bactericidal agents generated by the peroxidase-catalyzed oxidation of para-hydroquinones, J. Biol. Chem., 260, 14604, 10.1016\u002FS0021-9258(17)38610-6",{"doi":2036},"10.1016\u002FS0021-9258(17)38610-6",{"id":26,"text":2038,"url":26,"identifiers":2039},"De Haan, 1969, The mechanism of uncoupling of oxidative phosphorylation by 2-methyl-1,4 naphthoquinone, Biochim. Biophys. Acta, 180, 417, 10.1016\u002F0005-2728(69)90127-3",{"doi":2040},"10.1016\u002F0005-2728(69)90127-3",{"id":26,"text":2042,"url":26,"identifiers":2043},"Cremer, 1987, Toward a rationalization of the sensitizing potency of substituted p-benzoquinones, J. Med. Chem., 30, 1678, 10.1021\u002Fjm00392a027",{"doi":2044},"10.1021\u002Fjm00392a027",{"id":26,"text":2046,"url":26,"identifiers":2047},"Nobbs, 1983, Soil tissue injury caused by antineoplastic drugs is inhibited by topical dimethylsulfoxide and 2-tocopherol, Br. J. Cancer, 48, 873, 10.1038\u002Fbjc.1983.281",{"doi":2048},"10.1038\u002Fbjc.1983.281",{"id":26,"text":2050,"url":26,"identifiers":2051},"Pascoe, 1988, Evidence for p-benzoquinone as a reactive intermediate in acetaminophen metabolism, Chem.-Biol. Interact., 68, 85, 10.1016\u002F0009-2797(88)90008-7",{"doi":2052},"10.1016\u002F0009-2797(88)90008-7",{"id":26,"text":2054,"url":26,"identifiers":2055},"Larsson, 1986, Cellular effects of N(4-ethoxyphenyl) p-benzoquinoneimine, a p-phenetidine metabolite formed during peroxidase reactions, Chem.-Biol. Interact., 60, 317, 10.1016\u002F0009-2797(86)90062-1",{"doi":2056},"10.1016\u002F0009-2797(86)90062-1",{"id":26,"text":2058,"url":26,"identifiers":2059},"Epe, 1987, Site-specific covalent binding of stilbene type and steroidal oestrogens to tubulin following metabolic activation in vitro, Carcinogenesis, 8, 1271, 10.1093\u002Fcarcin\u002F8.9.1271",{"doi":2060},"10.1093\u002Fcarcin\u002F8.9.1271",{"id":26,"text":2062,"url":26,"identifiers":2063},"Dugue, 1986, Covalent binding of ellipticinium acetate to nucleic acids of L1210 cells in culture, Cancer Res., 46, 3828",{},{"id":26,"text":2065,"url":26,"identifiers":2066},"Riley, 1985, Radicals and melanoma, Phil. Trans R. Soc. Lond., B311, 679, 10.1098\u002Frstb.1985.0173",{"doi":2067},"10.1098\u002Frstb.1985.0173",{"id":26,"text":2069,"url":26,"identifiers":2070},"Graham, 1978, Autoxidation versus covalent binding of quinones as the mechanism of toxicity of dopamine, 6-hydroxydopamine and related compounds toward neuroblastoma cells in vitro, Mol. Pharmacol., 14, 644",{},{"id":26,"text":2072,"url":26,"identifiers":2073},"Dexter, 1989, Increased signal iron content in Parkinson's disease, J. Neurochem., 52, 1830, 10.1111\u002Fj.1471-4159.1989.tb07264.x",{"doi":2074},"10.1111\u002Fj.1471-4159.1989.tb07264.x",{"id":26,"text":2076,"url":26,"identifiers":2077},"Graham, 1984, Catecholamine toxicity: a proposal for the molecular pathogenesis of manganese toxicity and Parkinson's disease, Neurotoxicology, 5, 83",{},{"id":26,"text":2079,"url":26,"identifiers":2080},"Singal, 1982, Role of free radicals in catecholamine induced cardiomyopathy, Can. J. Physiol. Pharmacol., 60, 1390, 10.1139\u002Fy82-207",{"doi":2081},"10.1139\u002Fy82-207",{"id":26,"text":2083,"url":26,"identifiers":2084},"Bruchelt, 1985, The role of reactive oxygen compounds derived from 6-hydroxydopamine for bone marrow purging from neuroblastoma cells, Biochem. Biophys. Res. Commun., 130, 168, 10.1016\u002F0006-291X(85)90397-3",{"doi":2085},"10.1016\u002F0006-291X(85)90397-3",{"id":26,"text":2087,"url":26,"identifiers":2088},"Dybing, 1976, Oxidation of 1-methyldopa and other catechols by cytochrome P-450 generated superoxide anion: Possible mechanism of methyldopa hepatitis, Mol. Pharmacol., 12, 911",{},{"id":26,"text":2090,"url":26,"identifiers":2091},"Uemura, 1980, NADPH-dependent melanin pigment formation from 5-hydroxyindolealkylamines by hepatic and cerebral microsomes, Biochem. Biophys. Res. Commun., 93, 1074, 10.1016\u002F0006-291X(80)90598-7",{"doi":2092},"10.1016\u002F0006-291X(80)90598-7",{"id":26,"text":2094,"url":26,"identifiers":2095},"Munday, 1988, Dilauric acid autoxidation effects of transition metals on the reaction rate and on the generation of ‘active oxygen’ species, Biochem. Pharmacol., 37, 409, 10.1016\u002F0006-2952(88)90207-9",{"doi":2096},"10.1016\u002F0006-2952(88)90207-9",{"id":26,"text":2098,"url":26,"identifiers":2099},"Winterbourn, 1986, Contributions of superoxide, hydrogen peroxide, and transition metals to autoxidation of favism-inducing pyrimidine aglycone, divicine, and its reaction with hemoglobin, Biochem. Pharmacol., 35, 2009, 10.1016\u002F0006-2952(86)90734-3",{"doi":2100},"10.1016\u002F0006-2952(86)90734-3",{"id":26,"text":2102,"url":26,"identifiers":2103},"Schlosser, 1989, Metabolic activation of hydroquinone by macrophage peroxidase, Chem.-Biol. Interact., 72, 191, 10.1016\u002F0009-2797(89)90027-6",{"doi":2104},"10.1016\u002F0009-2797(89)90027-6",{"id":26,"text":2106,"url":26,"identifiers":2107},"Post, 1985, Inhibition of RNA synthesis in lymphocytes by benzene and its metabolites, hydroquinone and p-benzoquinone, Toxicol. Lett., 29, 161, 10.1016\u002F0378-4274(85)90037-2",{"doi":2108},"10.1016\u002F0378-4274(85)90037-2",{"id":26,"text":2110,"url":26,"identifiers":2111},"Pellack-Walker, 1986, DNA damage in L5178YS cells following exposure to benzene metabolites, Mol. Pharmacol., 30, 42",{},{"id":26,"text":2113,"url":26,"identifiers":2114},"Lorentzen, 1979, Toxicity of metabolic benzo[a]pyrenediones to cultured cells and the dependence upon molecular oxygen, Cancer Res., 39, 3194",{},{"id":26,"text":2116,"url":26,"identifiers":2117},"Morrison, 1985, Induction of cell damage by menadione and benzo[a]pyrene-3,6-quinone in cultures of adult rat hepatocytes and human fibroblasts, Toxicol. Lett., 28, 37, 10.1016\u002F0378-4274(85)90007-4",{"doi":2118},"10.1016\u002F0378-4274(85)90007-4",{"id":26,"text":2120,"url":26,"identifiers":2121},"Chesis, 1984, Mutagenicity of quinones: Pathways of metabolic activation and detoxification, 81, 1696",{},{"id":26,"text":2123,"url":26,"identifiers":2124},"Leadon, 1988, Production of oxidative DNA damage during the metabolic activation of benzo(a)pyrene in human mammary epithelial cells correlates with cell killing, Prod. Natl. Acad. Sci., 85, 4365, 10.1073\u002Fpnas.85.12.4365",{"doi":2125},"10.1073\u002Fpnas.85.12.4365",{"id":26,"text":2127,"url":26,"identifiers":2128},"Buonarati, 1989, Glutathione depletion and cytotoxicity by naphthalene 1,2 oxide in isolated hepatocytes, Chem.-Biol. Interact., 71, 147, 10.1016\u002F0009-2797(89)90031-8",{"doi":2129},"10.1016\u002F0009-2797(89)90031-8",{"id":26,"text":2131,"url":26,"identifiers":2132},"Doherty, 1989, Mechanisms of toxic injury to isolated hepatocytes by 1-naphthol, Biochem. Pharmacol., 33, 543, 10.1016\u002F0006-2952(84)90305-8",{"doi":2133},"10.1016\u002F0006-2952(84)90305-8",{"id":26,"text":2135,"url":26,"identifiers":2136},"van Ommen, 1989, Possible reactive intermediates in the oxidative biotransformation of hexachlorobenzene, Drug Metab. Drug Interact., 7, 213, 10.1515\u002FDMDI.1989.7.2-3.213",{"doi":2137},"10.1515\u002FDMDI.1989.7.2-3.213",{"id":26,"text":2139,"url":26,"identifiers":2140},"Schnellman, 1989, 2-Bromohydroquinone-induced toxicity to rabbit renal proximal tubules, Toxicol. Appl. Pharmacol., 99, 19, 10.1016\u002F0041-008X(89)90107-5",{"doi":2141},"10.1016\u002F0041-008X(89)90107-5",{"id":26,"text":2143,"url":26,"identifiers":2144},"Gillette, 1974, Biochemical mechanisms of drug toxicity, Annu. Rev. Pharmacol. Toxicol., 14, 271, 10.1146\u002Fannurev.pa.14.040174.001415",{"doi":2145},"10.1146\u002Fannurev.pa.14.040174.001415",{"id":26,"text":2147,"url":26,"identifiers":2148},"Potter, 1987, Mechanisms of acetaminophen oxidation to N-acetyl-p-benzoquinone-imine by horse radish peroxidase and cytochrome P-450, J. Biol. Chem., 262, 966, 10.1016\u002FS0021-9258(19)75735-4",{"doi":2149},"10.1016\u002FS0021-9258(19)75735-4",{"id":26,"text":2151,"url":26,"identifiers":2152},"Hoffmann, 1985, Identification of the major covalent adduct formed in vitro and in vivo between acetaminophen and mouse liver proteins, Mol. Pharmacol., 27, 566",{},{"id":26,"text":2154,"url":26,"identifiers":2155},"Toranzo, 1977, Effect of substitutents on arene oxide-mediated liver toxicity among substituted bromobenzenes, Toxicol. Appl. Pharmacol., 40, 415, 10.1016\u002F0041-008X(77)90069-2",{"doi":2156},"10.1016\u002F0041-008X(77)90069-2",{"id":26,"text":2158,"url":26,"identifiers":2159},"Rush, 1984, Nephrotoxicity of phenolic bromobenzene metabolites, Toxicology, 30, 259, 10.1016\u002F0300-483X(84)90097-0",{"doi":2160},"10.1016\u002F0300-483X(84)90097-0",{"id":26,"text":2162,"url":26,"identifiers":2163},"Monks, 1985, Glutathione conjugates of 2-bromohydroquinone are nephrotoxic, Drug Metab. Dispos., 13, 553",{},{"id":26,"text":2165,"url":26,"identifiers":2166},"Monks, 1988, 2-Bromo (-diglutathione-s-yl) hydroquinone nephrotoxicity: Physiological, biochemical, and electrochemical determinants, Mol. Pharmacol., 34, 492",{},{"id":26,"text":2168,"url":26,"identifiers":2169},"Monks, 1988, Synthesis and nephrotoxicity of 6-Bromo-2,5-dihydroxy-thiophenol, Mol. Pharmacol., 34, 15",{},{"id":26,"text":2171,"url":26,"identifiers":2172},"Miller, 1978, Some current perspectives on chemical carcinogenesis on humans and experimental animals: Presidential address, Cancer Res., 38, 1479",{},{"id":26,"text":2174,"url":26,"identifiers":2175},"Gerson, 1985, Oxygen-mediated cell injury in the killing of cultured hepatocytes by acetaminophen, Biochem. Biophys. Res. Commun., 126, 1129, 10.1016\u002F0006-291X(85)90303-1",{"doi":2176},"10.1016\u002F0006-291X(85)90303-1",{"id":26,"text":2178,"url":26,"identifiers":2179},"Casini, 1982, Mechanisms of cell injury in the killing of cultured hepatocytes by bromobenzene, J. Biol. Chem., 257, 6721, 10.1016\u002FS0021-9258(18)34490-9",{"doi":2180},"10.1016\u002FS0021-9258(18)34490-9",{"id":26,"text":2182,"url":26,"identifiers":2183},"Labadarios, 1977, Paracetamol-induced hepatic necrosis in the mouse, Biochem. Pharmacol., 26, 31, 10.1016\u002F0006-2952(77)90126-5",{"doi":2184},"10.1016\u002F0006-2952(77)90126-5",{"id":26,"text":2186,"url":26,"identifiers":2187},"Tee, 1986, Reversal of acetaminophen toxicity in isolated hamster hepatocytes by dithiothreitol, Toxicol. Appl. Pharmacol., 83, 294, 10.1016\u002F0041-008X(86)90307-8",{"doi":2188},"10.1016\u002F0041-008X(86)90307-8",{"id":26,"text":2190,"url":26,"identifiers":2191},"Casini, 1987, Lipid peroxidation and protein thiols and calcium homeostasis in bromobenzene-induced liver damage, Biochem. Pharmacol., 36, 3689, 10.1016\u002F0006-2952(87)90021-9",{"doi":2192},"10.1016\u002F0006-2952(87)90021-9",{"id":26,"text":2194,"url":26,"identifiers":2195},"Fernando, 1980, Studies on the mechanism of toxicity of acetaminophen: Synthesis and reactions of N-acetyl-2,6-dimethyl-p-benzoquinone, J. Med. Chem., 23, 1153, 10.1021\u002Fjm00185a001",{"doi":2196},"10.1021\u002Fjm00185a001",{"id":26,"text":2198,"url":26,"identifiers":2199},"Rosen, 1983, Acetaminophen hepatotoxicity, an alternative mechanism, Biochem. Pharmacol., 32, 2053, 10.1016\u002F0006-2952(83)90426-4",{"doi":2200},"10.1016\u002F0006-2952(83)90426-4",{"id":26,"text":2202,"url":26,"identifiers":2203},"Heinz, 1890, Virchows Arch. Pathol. Anat. Physiol., 122, 100, 10.1007\u002FBF01922783",{"doi":2204},"10.1007\u002FBF01922783",{"id":26,"text":2206,"url":26,"identifiers":2207},"Hoppe-Seyler, 1885, Z. Physiol. Chem., 9, 34",{},{"id":26,"text":2209,"url":26,"identifiers":2210},"Agarwal, 1988, Susceptibility of glucose 6-phosphate dehydrogenase deficient red cells to primaquine enantiomers and two putative metabolites, Biochem. Pharmacol., 37, 4605, 10.1016\u002F0006-2952(88)90327-9",{"doi":2211},"10.1016\u002F0006-2952(88)90327-9",{"id":26,"text":2213,"url":26,"identifiers":2214},"Chevion, 1987, The chemistry of favism-inducing compounds, the properties of isouramil and divicine and their reaction with glutathione, Eur. J. Biochem., 127, 405, 10.1111\u002Fj.1432-1033.1982.tb06886.x",{"doi":2215},"10.1111\u002Fj.1432-1033.1982.tb06886.x",{"id":26,"text":2217,"url":26,"identifiers":2218},"Clark, 1989, Antimalarials",{},{"id":26,"text":2220,"url":26,"identifiers":2221},"Grankvist, 1981, Superoxide dismutase is a prophylactic against alloxan diabetes, Nature, 294, 158, 10.1038\u002F294158a0",{"doi":2222},"10.1038\u002F294158a0",{"id":26,"text":2224,"url":26,"identifiers":2225},"Grankvist, 1979, Superoxide dismutase and scavenger of hydroxyl radicals protect against the toxic action of alloxan on pancreatic islets cells in vitro, Biochem. J., 182, 17, 10.1042\u002Fbj1820017",{"doi":2226},"10.1042\u002Fbj1820017",{"id":26,"text":2228,"url":26,"identifiers":2229},"Grankvist, 1979, Influence of trace metals on alloxan cytotoxicity in pancreatic islets, FEBS Lett., 105, 15, 10.1016\u002F0014-5793(79)80877-7",{"doi":2230},"10.1016\u002F0014-5793(79)80877-7",{"id":26,"text":2232,"url":26,"identifiers":2233},"Cohen, 1964, Generation of hydrogen peroxide in erythrocytes by hemolytic agents, Biochemistry, 3, 895, 10.1021\u002Fbi00895a006",{"doi":2234},"10.1021\u002Fbi00895a006",{"id":26,"text":2236,"url":26,"identifiers":2237},"Mezick, 1970, Erythocyte membrane interactions with menadione and the mechanism of menadione-induced hemolysis, Biochim. Biophys. Acta, 219, 361, 10.1016\u002F0005-2736(70)90213-0",{"doi":2238},"10.1016\u002F0005-2736(70)90213-0",{"id":26,"text":2240,"url":26,"identifiers":2241},"Doroshow, 1986, Redox cycling of anthracyclines by cardiac mitochondria. II. Formation of superoxide anion, hydrogen peroxide and hydroxyl radical, J. Biol. Chem., 261, 3068, 10.1016\u002FS0021-9258(17)35747-2",{"doi":2242},"10.1016\u002FS0021-9258(17)35747-2",{"id":26,"text":2244,"url":26,"identifiers":2245},"Doroshow, 1980, Enzymatic defenses of the mouse heart against reactive oxygen metabolites. Alterations produced by doxorubicin, J. Clin. Invest., 65, 128, 10.1172\u002FJCI109642",{"doi":2246},"10.1172\u002FJCI109642",{"id":26,"text":2248,"url":26,"identifiers":2249},"Badr, 1989, Hepatotoxicity of menadione predominates in oxygen-rich zones of the liver lobule, J. Pharmacol. Exp. Ther., 248, 1317",{},{"id":26,"text":2251,"url":26,"identifiers":2252},"Ganey, 1988, Oxygen dependent hepatotoxicity due to doxorubicin; role of reducing equivalent supply in perfused rat liver, Mol. Pharmacol., 34, 695",{},{"id":26,"text":2254,"url":26,"identifiers":2255},"Wilson, 1987, Reactivity of thiols towards derivatives of 2- and 6-methyl-1,4-naphthoquinone bioreductive alkylating agents, Chem.-Biol. Interact., 61, 229, 10.1016\u002F0009-2797(87)90003-2",{"doi":2256},"10.1016\u002F0009-2797(87)90003-2",{"id":26,"text":2258,"url":26,"identifiers":2259},"Thor, 1982, The metabolism of menadione (2-methyl-1,4-naphthoquinone) by isolated hepatocytes. A study in the implication of oxidative stress in intact cells, J. Biol. Chem., 257, 12419, 10.1016\u002FS0021-9258(18)33730-X",{"doi":2260},"10.1016\u002FS0021-9258(18)33730-X",{"id":26,"text":2262,"url":26,"identifiers":2263},"Babson, 1981, Protective role of the glutathione redox cycle against adriamycin-mediated toxicity in isolated hepatocytes, Biochem. Pharmacol., 30, 2299, 10.1016\u002F0006-2952(81)90102-7",{"doi":2264},"10.1016\u002F0006-2952(81)90102-7",{"id":26,"text":2266,"url":26,"identifiers":2267},"Rossi, 1986, Quinone toxicity in hepatocytes without oxidative stress, Arch. Biochem. Biophys., 251, 25, 10.1016\u002F0003-9861(86)90047-0",{"doi":2268},"10.1016\u002F0003-9861(86)90047-0",{"id":26,"text":2270,"url":26,"identifiers":2271},"Moore, 1987, Quinone toxicity in hepatocytes: Studies on mitochondrial Ca2+ release induced by benzoquinone derivatives, Arch. Biochem. Biophys., 259, 283, 10.1016\u002F0003-9861(87)90495-4",{"doi":2272},"10.1016\u002F0003-9861(87)90495-4",{"id":26,"text":2274,"url":26,"identifiers":2275},"Moore, 1988, Role of sulfhydryl groups in benzoquinone-induced Ca2+ release by rat liver mitochondria, Arch. Biochem. Biophys., 267, 539, 10.1016\u002F0003-9861(88)90061-6",{"doi":2276},"10.1016\u002F0003-9861(88)90061-6",{"id":26,"text":2278,"url":26,"identifiers":2279},"Silva, 1989, Diaziquone-induced cytotoxicity in isolated rat hepatocytes, Cancer Res., 49, 5550",{},{"id":26,"text":2281,"url":26,"identifiers":2282},"Silva, 1989",{},{"id":26,"text":2284,"url":26,"identifiers":2285},"Bellomo, 1986, Formation and reduction of glutathione-protein mixed disulfides during oxidative stress. A study with isolated hepatocytes and menadione (2-methyl-1,4-naphthoquinone), Biochem. Pharmacol., 36, 1313, 10.1016\u002F0006-2952(87)90087-6",{"doi":2286},"10.1016\u002F0006-2952(87)90087-6",{"id":26,"text":2288,"url":26,"identifiers":2289},"Gant, 1988, Redox cycling and sulfhydryl arylation; their relative importance in the mechanism of quinone cytotoxicity to isolated hepatocytes, Chem.-Biol. Interact., 65, 157, 10.1016\u002F0009-2797(88)90052-X",{"doi":2290},"10.1016\u002F0009-2797(88)90052-X",{"id":26,"text":2292,"url":26,"identifiers":2293},"Pritsos, 1982, Involvement of superoxide in the interaction of 2,3-dichloro-1,4-naphthoquinone with mitochondrial membranes, Arch. Biochem. Biophys., 217, 98, 10.1016\u002F0003-9861(82)90483-0",{"doi":2294},"10.1016\u002F0003-9861(82)90483-0",{"id":26,"text":2296,"url":26,"identifiers":2297},"Pritsos, 1984, Biochem. Pharmacol., 33, 3771, 10.1016\u002F0006-2952(84)90039-X",{"doi":2298},"10.1016\u002F0006-2952(84)90039-X",{"id":26,"text":2300,"url":26,"identifiers":2301},"Powis, 1989, Role of metabolism and oxidation-reduction cycling in the cytotoxicity of antitumor quinoneimines and quinonediimines, Cancer Res., 47, 2363",{},{"id":26,"text":2303,"url":26,"identifiers":2304},"Nakamura, 1969, One-electron transfer reactions in biochemical systems. IV. A mixed mechanism in the reaction of milk xanthine oxidase with electron acceptors, Biochim. Biophys. Acta, 189, 29, 10.1016\u002F0005-2728(69)90221-7",{"doi":2305},"10.1016\u002F0005-2728(69)90221-7",{"id":26,"text":2307,"url":26,"identifiers":2308},"Prochaska, 1986, Purification and characterization of isofunctional forms of NAD(P)H; quinone reductase from mouse liver, J. Biol. Chem., 261, 1372, 10.1016\u002FS0021-9258(17)36101-X",{"doi":2309},"10.1016\u002FS0021-9258(17)36101-X",{"id":26,"text":2311,"url":26,"identifiers":2312},"Kumaki, 1977, Genetic differences in induction of cytosol reduced NAD(P): Menandione oxidoreductase and microsomal aryl hydrocarbon hydroxylase in the mouse, J. Biol. Chem., 252, 157, 10.1016\u002FS0021-9258(17)32810-7",{"doi":2313},"10.1016\u002FS0021-9258(17)32810-7",{"id":26,"text":2315,"url":26,"identifiers":2316},"Robertson, 1986, Menandione oxidoreductase novel purification of enzyme, cDNA and complete amino acid sequence, and gene regulation, J. Biol. Chem., 261, 15794, 10.1016\u002FS0021-9258(18)66789-4",{"doi":2317},"10.1016\u002FS0021-9258(18)66789-4",{"id":26,"text":2319,"url":26,"identifiers":2320},"Powis, 1980, Relationship of the single electron reduction potential of quinones to their reduction by flavoproteins, Biochem. Pharmacol., 29, 2567, 10.1016\u002F0006-2952(80)90068-4",{"doi":2321},"10.1016\u002F0006-2952(80)90068-4",{"id":26,"text":2323,"url":26,"identifiers":2324},"Ruzicka, 1970, Quinone interaction with the respiratory chain-linked NADH dehydrogenase of beef heart mitochondria, Biochim. Biophys. Acta, 226, 221, 10.1016\u002F0005-2728(71)90089-2",{"doi":2325},"10.1016\u002F0005-2728(71)90089-2",{"id":26,"text":2327,"url":26,"identifiers":2328},"Buffington, 1989, DT-diaphorase catalyzed reduction of 1,4-naphthoquinone derivatives and glutathionyl-quinone conjugates, Biochem. J., 257, 561, 10.1042\u002Fbj2570561",{"doi":2329},"10.1042\u002Fbj2570561",{"id":26,"text":2331,"url":26,"identifiers":2332},"Ernster, 1962, DT-diaphorase I. Purification from the soluble fraction of rat liver cytoplasm, and properties, Biochim. Biophys. Acta, 58, 171, 10.1016\u002F0006-3002(62)90997-6",{"doi":2333},"10.1016\u002F0006-3002(62)90997-6",{"id":26,"text":2335,"url":26,"identifiers":2336},"d'Arcy Doherty, 1987, Mechanisms of toxicity of 2- and 5-hydroxy-1,4-naphthoquinone: Absence of a role for redox cycling in the toxicity of 2-OH-1,4 naphthoquinone to isolated hepatocytes, J. Appl. Toxicol., 7, 123, 10.1002\u002Fjat.2550070209",{"doi":2337},"10.1002\u002Fjat.2550070209",{"id":26,"text":2339,"url":26,"identifiers":2340},"Talcott, 1983, Possible role of DT-diaphorase in the bioactivation of antitumor quinones, Biochem. Biophys. Res. Commun., 111, 346, 10.1016\u002FS0006-291X(83)80158-2",{"doi":2341},"10.1016\u002FS0006-291X(83)80158-2",{"id":26,"text":2343,"url":26,"identifiers":2344},"van de Straat, 1987, Role of hepatic microsomal and purified cytochrome P-450 in one-electron reduction of two quinoneimines and concomitant reduction of molecular oxygen, Biochem. Pharmacol., 36, 613, 10.1016\u002F0006-2952(87)90710-6",{"doi":2345},"10.1016\u002F0006-2952(87)90710-6",{"id":26,"text":2347,"url":26,"identifiers":2348},"Weiner, 1981, Microsomal and photochemical oxidation and reduction of 1-piperidinoanthraquinone, Biochim. Biophys. Acta, 714, 234, 10.1016\u002F0304-4165(82)90329-4",{"doi":2349},"10.1016\u002F0304-4165(82)90329-4",{"id":26,"text":2351,"url":26,"identifiers":2352},"Kennedy, 1982, Metabolic activation of mitomycin C by liver microsomes and nuclei, Biochem. Pharmacol., 31, 2011, 10.1016\u002F0006-2952(82)90414-2",{"doi":2353},"10.1016\u002F0006-2952(82)90414-2",{"id":26,"text":2355,"url":26,"identifiers":2356},"Nishibayashi, 1967, Specificity of naphthoquinones as cofactor for NADPH oxidation by liver microsomes, J. Biochem., 62, 215, 10.1093\u002Foxfordjournals.jbchem.a128651",{"doi":2357},"10.1093\u002Foxfordjournals.jbchem.a128651",{"id":26,"text":2359,"url":26,"identifiers":2360},"Heikkila, 1971, Further studies on the generation of hydrogen peroxide by 6-hydroxydopamine, Mol. Pharmacol, 8, 241",{},{"id":26,"text":2362,"url":26,"identifiers":2363},"Koch, 1979, Ascorbate anion potentiates cytotoxicity of nitroaromatic compounds under hypoxic and anoxic conditions, Br. J. Cancer., 39, 321, 10.1038\u002Fbjc.1979.56",{"doi":2364},"10.1038\u002Fbjc.1979.56",{"id":26,"text":2366,"url":26,"identifiers":2367},"Pethig, 1983, Ascorbate-quinone interactions: Electrochemical, free radical, and cytotoxic properties, 80, 129",{},{"id":26,"text":2369,"url":26,"identifiers":2370},"Land, 1983, Reduction of the napthazarin molecules: Studies by pulse radiolysis II. Second one-electron step, J. Chem. Soc. Faraday Trans I., 79, 405, 10.1039\u002Ff19837900405",{"doi":2371},"10.1039\u002Ff19837900405",{"id":26,"text":2373,"url":26,"identifiers":2374},"Rao, 1987, Generation of radical anions of nitrofurantoin, misonidazole by ascorbate, Arch. Biochem. Biophys., 255, 419, 10.1016\u002F0003-9861(87)90410-3",{"doi":2375},"10.1016\u002F0003-9861(87)90410-3",{"id":26,"text":2377,"url":26,"identifiers":2378},"Rao, 1975, Redox potentials of free radicals IV. Superoxide and hydroperoxy radicals O2• and HO2•, J. Phys. Chem., 79, 397, 10.1021\u002Fj100571a021",{"doi":2379},"10.1021\u002Fj100571a021",{"id":26,"text":2381,"url":26,"identifiers":2382},"Iyanagi, 1970, One-electron transfer reaction in biochemical system, Biochim. Biophys. Acta, 216, 282, 10.1016\u002F0005-2728(70)90220-3",{"doi":2383},"10.1016\u002F0005-2728(70)90220-3",{"id":26,"text":2385,"url":26,"identifiers":2386},"Powis, 1987, Quinoneimines as substrates for quinone reductase NAD(P)H (quinone-acceptor) oxidoreductase and the effect of dicoumarol on their cytotoxicity, Biochem. Pharmacol., 36, 2473, 10.1016\u002F0006-2952(87)90519-3",{"doi":2387},"10.1016\u002F0006-2952(87)90519-3",{"id":26,"text":2389,"url":26,"identifiers":2390},"Ollinger, 1989, Study of the redox properties of naphthazarin and its glutathionyl conjugate in biological reactions: one and two-electron enzymatic reaction, Arch. Biochem. Biophys., 275, 514, 10.1016\u002F0003-9861(89)90398-6",{"doi":2391},"10.1016\u002F0003-9861(89)90398-6",{"id":26,"text":2393,"url":26,"identifiers":2394},"Rao, 1988, Characterisation of a glutathione conjugate of the 1,4-benzosemiquinone free radical formed in rat hepatocytes, J. Biol. Chem., 263, 17981, 10.1016\u002FS0021-9258(19)81312-1",{"doi":2395},"10.1016\u002FS0021-9258(19)81312-1",{"id":26,"text":2397,"url":26,"identifiers":2398},"Board, 1981, Transport of glutathione S-conjugate from human erythrocytes, FEBS Lett., 124, 163, 10.1016\u002F0014-5793(81)80127-5",{"doi":2399},"10.1016\u002F0014-5793(81)80127-5",{"id":26,"text":2401,"url":26,"identifiers":2402},"Rose, 1984, Detection of superoxide generated by endothelial cells, 81, 7269",{},{"id":26,"text":2404,"url":26,"identifiers":2405},"Lau, 1988, Sequential oxidation and glutathione addition to 1,4-benzoquinone: Correlation of toxicity with increased glutathione, Mol. Pharmacol., 34, 829",{},{"id":26,"text":2407,"url":26,"identifiers":2408},"Ross, 1985, Interaction of menadione (2-methyl-1,4-naphthoquinone) with glutathione, Chem.-Biol. Interact., 55, 177, 10.1016\u002FS0009-2797(85)80126-5",{"doi":2409},"10.1016\u002FS0009-2797(85)80126-5",{"id":26,"text":2411,"url":26,"identifiers":2412},"Finley, 1974, The addition and substitution chemistry of quinones",{},{"id":26,"text":2414,"url":26,"identifiers":2415},"Brunmark, 1988, Reductive addition of glutathione to p-benzoquinone, 2-hydroxy-p-benzoquinone, and p-benzoquinone epoxides. Effect of the hydroxy- and glutathionyl-substituents on p-benzo hydroquinone autoxidation, Chem.-Biol. Interact., 68, 273, 10.1016\u002F0009-2797(88)90021-X",{"doi":2416},"10.1016\u002F0009-2797(88)90021-X",{"id":26,"text":2418,"url":26,"identifiers":2419},"Eckert, 1990, Activation and detoxification of aminophenols. III. Synthesis and structural elucidation of various glutathione addition products to 1,4-benzoquinone, Xenobiotica, 20, 351, 10.3109\u002F00498259009046852",{"doi":2420},"10.3109\u002F00498259009046852",{"id":26,"text":2422,"url":26,"identifiers":2423},"van Ommen, 1988, The oxidation of tetrachloro-1,4-hydroquinone by microsomes and purified cytochrome P-450b. Implications for covalent binding to protein and involvement of reactive oxygen species, Chem.-Biol. Interact., 65, 247, 10.1016\u002F0009-2797(88)90110-X",{"doi":2424},"10.1016\u002F0009-2797(88)90110-X",{"id":26,"text":2426,"url":26,"identifiers":2427},"van Ommen, 1986, The microsomal metabolism of hexachlorobenzene, Biochem. Pharmacol., 35, 3233, 10.1016\u002F0006-2952(86)90417-X",{"doi":2428},"10.1016\u002F0006-2952(86)90417-X",{"id":26,"text":2254,"url":26,"identifiers":2430},{"doi":2256},{"id":26,"text":2432,"url":26,"identifiers":2433},"Nickerson, 1963, Studies on quinone thioethers (I). Mechanism of formation and properties of thiodione, Biochemistry, 2, 537, 10.1021\u002Fbi00903a025",{"doi":2434},"10.1021\u002Fbi00903a025",{"id":26,"text":2436,"url":26,"identifiers":2437},"Gause, 1967, ESR studies of the chloranil-cysteine, dichlone-cysteine and dichlone-glutathione reactions, Biochim. Biophys. Acta, 141, 217, 10.1016\u002F0304-4165(67)90271-1",{"doi":2438},"10.1016\u002F0304-4165(67)90271-1",{"id":26,"text":2440,"url":26,"identifiers":2441},"Gant, 1986, Semiquinone anion radicals formed by the reaction of quinones with glutathione of amino acids, FEBS Lett., 201, 296, 10.1016\u002F0014-5793(86)80627-5",{"doi":2442},"10.1016\u002F0014-5793(86)80627-5",{"id":26,"text":2444,"url":26,"identifiers":2445},"Rosen, 1984, Reduction and glutathione conjugation reactions of N-acetyl-p-benzoquinoneimine and two dimethylated analogs, Mol. Pharmacol., 25, 151",{},{"id":26,"text":2447,"url":26,"identifiers":2448},"Rundgren, 1988, Comparative cytotoxic effects of N-acetyl-p-benzoquinone imine and two dimethylated analogues, Mol. Pharmacol., 34, 566",{},{"id":26,"text":2450,"url":26,"identifiers":2451},"Wardman, 1990, Bioreductive activation of quinones: Redox properties and thiol reactivity, Free Rad. Res. Commun., 10.3109\u002F10715769009053355",{"doi":2452},"10.3109\u002F10715769009053355",{"id":26,"text":2454,"url":26,"identifiers":2455},"Winterbourn, 1989, Inhibition of autoxidation of divicine and isouramil by the combination of superoxide dismutase and reduced glutathione, Arch. Biochem. Biophys., 271, 447, 10.1016\u002F0003-9861(89)90295-6",{"doi":2456},"10.1016\u002F0003-9861(89)90295-6",{"id":26,"text":2458,"url":26,"identifiers":2459},"Winterbourn, 1989, Glutathione-mediated redox cycling of alloxan. Mechanisms of superoxide dismutase inhibition and of metal-catalyzed hydroxy radical formation, Biochem. Pharmacol., 38, 271, 10.1016\u002F0006-2952(89)90037-3",{"doi":2460},"10.1016\u002F0006-2952(89)90037-3",{"id":26,"text":2462,"url":26,"identifiers":2463},"Fohe, 1972, Glutathione peroxidase, V. Kinetic mechanism, Hoppe-Seyles Z., Physiol. Chem., 353, 987, 10.1515\u002Fbchm2.1972.353.1.987",{"doi":2464},"10.1515\u002Fbchm2.1972.353.1.987",{"id":26,"text":2466,"url":26,"identifiers":2467},"Wefers, 1983, Hepatic low-level chemiluminescence during redox cycling of menadione and the menadione-glutathione conjugate: Relation to glutathione and NAD(P)H: Quinone reductase (DT-diaphorase) activity, Arch. Biochem. Biophys., 224, 568, 10.1016\u002F0003-9861(83)90244-8",{"doi":2468},"10.1016\u002F0003-9861(83)90244-8",{"id":26,"text":2470,"url":26,"identifiers":2471},"Wefers, 1986, Generation of photoemissive species during quinone redox cycling, Biochem. Pharmacol., 35, 22, 10.1016\u002F0006-2952(86)90548-4",{"doi":2472},"10.1016\u002F0006-2952(86)90548-4",{"id":26,"text":2474,"url":26,"identifiers":2475},"Prochaska, 1987, Direct protective effect of NAD(P)H: Quinone reductase against menadione-induced chemiluminescence of post-mitochondrial fractions of mouse liver, J. Biol. Chem., 262, 1931, 10.1016\u002FS0021-9258(18)61597-2",{"doi":2476},"10.1016\u002FS0021-9258(18)61597-2",{"id":26,"text":2258,"url":26,"identifiers":2478},{"doi":2260},{"id":26,"text":2480,"url":26,"identifiers":2481},"Coles, 1988, The spontaneous and enzymatic reaction of N-acetyl-p-benzoquinone-imine with glutathione: A stopped flow kinetic study, Arch. Biochem. Biophys., 264, 253, 10.1016\u002F0003-9861(88)90592-9",{"doi":2482},"10.1016\u002F0003-9861(88)90592-9",{"id":26,"text":2484,"url":26,"identifiers":2485},"Sato, 1988, Glutathione S-transferases and hepatocarcinogenesis, Jpn. J. Cancer Res. (Gann), 79, 556, 10.1111\u002Fj.1349-7006.1988.tb00022.x",{"doi":2486},"10.1111\u002Fj.1349-7006.1988.tb00022.x",{"id":26,"text":2488,"url":26,"identifiers":2489},"De Bault, 1973, Inhibition of growth by 6-hydroxydopamine in cultured cells of neuronal and non-neuronal origin, Cancer Res., 33, 745",{},{"id":26,"text":2491,"url":26,"identifiers":2492},"Heikkila, 1973, 6-hydroxydopamine: Evidence for superoxide radical as an oxidative intermediate, Science, 181, 456, 10.1126\u002Fscience.181.4098.456",{"doi":2493},"10.1126\u002Fscience.181.4098.456",{"id":26,"text":2495,"url":26,"identifiers":2496},"Heikkila, 1971, Further studies on the generation of hydrogen peroxide by 6-hydroxydopamine, Mol. Pharmacol., 8, 241",{},{"id":26,"text":2498,"url":26,"identifiers":2499},"Rotman, 1976, Oxygen-dependent reaction of 6-hydroxydopamine, 5,6-dihydroxy tryptamine, and related compounds with proteins in vitro: A model for cytotoxicity, Mol. Pharmacol., 12, 887",{},{"id":26,"text":2501,"url":26,"identifiers":2502},"Sachs, 1975, Mechanisms of action of 6-hydroxydopamine, Biochem. Pharmacol., 24, 1, 10.1016\u002F0006-2952(75)90304-4",{"doi":2503},"10.1016\u002F0006-2952(75)90304-4",{"id":26,"text":2069,"url":26,"identifiers":2505},{},{"id":26,"text":2507,"url":26,"identifiers":2508},"Liang, 1977, Isolation and identification of an in vivo reaction product of 6-hydroxydopamine, J. Med. Chem., 20, 581, 10.1021\u002Fjm00214a026",{"doi":2509},"10.1021\u002Fjm00214a026",{"id":26,"text":2511,"url":26,"identifiers":2512},"Borchardt, 1977, Effects of 2-and\u002For 5-methylated analogues of 6-hydroxydopamine on norepinephrine- and dopamine-containing neurons, Mol. Pharmacol., 13, 805",{},{"id":26,"text":2514,"url":26,"identifiers":2515},"Ito, 1987, Mechanism of selective toxicity of 4-cysteinylphenol and 4-S-cysteaminyl phenol to melanocytes, Biochem. Pharmacol., 36, 2007, 10.1016\u002F0006-2952(87)90501-6",{"doi":2516},"10.1016\u002F0006-2952(87)90501-6",{"id":26,"text":2518,"url":26,"identifiers":2519},"James, 1938, Oxidation processes XII. The autoxidation of hydroquinone and of the mono-, di-, and trimethyl hydroquinones, J. Am. Chem. Soc., 60, 2084, 10.1021\u002Fja01276a020",{"doi":2520},"10.1021\u002Fja01276a020",{"id":26,"text":2522,"url":26,"identifiers":2523},"James, 1938, Oxidation processes XI. The autoxidation of durohydroquinone, J. Am. Chem. Soc., 60, 98, 10.1021\u002Fja01268a032",{"doi":2524},"10.1021\u002Fja01268a032",{"id":26,"text":2526,"url":26,"identifiers":2527},"Greenlee, 1981, A proposed mechanism of benzene toxicity: Formation of reactive intermediates from polyphenol metabolites, Toxic. Appl. Pharmacol., 59, 187, 10.1016\u002F0041-008X(81)90189-7",{"doi":2528},"10.1016\u002F0041-008X(81)90189-7",{"id":26,"text":2530,"url":26,"identifiers":2531},"Gee, 1984, 6-Hydroxydopamine does not reduce molecular oxygen directly but requires a coreductant, Arch. Biochem. Biophys., 231, 164, 10.1016\u002F0003-9861(84)90373-4",{"doi":2532},"10.1016\u002F0003-9861(84)90373-4",{"id":26,"text":2534,"url":26,"identifiers":2535},"Nicotera, 1989, Ca2+ activated mechanisms in cell killing, Drug Metab. Rev., 20, 193, 10.3109\u002F03602538909103536",{"doi":2536},"10.3109\u002F03602538909103536",{"id":26,"text":2538,"url":26,"identifiers":2539},"Di Monte, 1984, Alterations in intracellular thiol homeostasis during the metabolism of menadione by isolated rat hepatocytes, Arch. Biochem. Biophys., 235, 334, 10.1016\u002F0003-9861(84)90206-6",{"doi":2540},"10.1016\u002F0003-9861(84)90206-6",{"id":26,"text":2542,"url":26,"identifiers":2543},"Winterbourn, 1989, Autooxidation of dialuric acid, divicine, and isouramil: superoxide dependent and independent mechanisms, Biochem. Pharmacol., 38, 611, 10.1016\u002F0006-2952(89)90206-2",{"doi":2544},"10.1016\u002F0006-2952(89)90206-2",{"id":26,"text":2546,"url":26,"identifiers":2547},"Monks, 1984, Formation of non-toxic reactive metabolites of p-bromophenol identification of a new glutathione conjugate, Drug Metab. Disp., 12, 437",{},{"id":26,"text":2549,"url":26,"identifiers":2550},"Scheulen, 1975, Irreversible binding of dopa and dopamine metabolites to proteins by rat liver microsomes, Biochem. Biophys. Res. Commun., 66, 1396, 10.1016\u002F0006-291X(75)90514-8",{"doi":2551},"10.1016\u002F0006-291X(75)90514-8",{"id":26,"text":2553,"url":26,"identifiers":2554},"Lunte, 1983, Detection and identification of sulphydryl conjugates of p-benzoquinone in microsomal incubations of benzene and phenol, Chem.-Biol. Interact., 47, 195, 10.1016\u002F0009-2797(83)90157-6",{"doi":2555},"10.1016\u002F0009-2797(83)90157-6",{"id":26,"text":2557,"url":26,"identifiers":2558},"Brodie, 1987, Reversible oxidation of glyceraldehyde 3-phosphate dehydrogenase thiols in human lung carcinoma cells by hydrogen peroxide, Biochem. Biophys. Res. Commun., 148, 120, 10.1016\u002F0006-291X(87)91084-9",{"doi":2559},"10.1016\u002F0006-291X(87)91084-9",{"id":26,"text":2561,"url":26,"identifiers":2562},"Chatham, 1989, The metabolic consequences of hydroperoxide perfusion on the isolated rat heart, Eur. J. Biochem., 184, 657, 10.1111\u002Fj.1432-1033.1989.tb15063.x",{"doi":2563},"10.1111\u002Fj.1432-1033.1989.tb15063.x",{"id":26,"text":2565,"url":26,"identifiers":2566},"Eckert, 1989, Depletion of mitochondrial coenzyme A and glutathione by 4-dimethylaminophenol and formation of mixed thietheo, Biochem.-Pharmacol., 38, 3252, 10.1016\u002F0006-2952(89)90622-9",{"doi":2567},"10.1016\u002F0006-2952(89)90622-9",{"id":26,"text":2569,"url":26,"identifiers":2570},"Stubberfield, 1989, Interconversions of NAD(H) to NADP(H). A cellular response to quinone-induced oxidative stress in isolated hepatocytes, Biochem.-Pharmacol., 38, 2631, 10.1016\u002F0006-2952(89)90548-0",{"doi":2571},"10.1016\u002F0006-2952(89)90548-0",{"id":26,"text":2573,"url":26,"identifiers":2574},"Thor, 1988, Alterations in hepatocyte cytoskeleton caused by redox cycling and alkylating quinones, Arch. Biochem. Biophys., 266, 397, 10.1016\u002F0003-9861(88)90271-8",{"doi":2575},"10.1016\u002F0003-9861(88)90271-8",{"id":26,"text":2577,"url":26,"identifiers":2578},"Nicotera, 1988, Ca2+ activated mechanisms in cell killing, Drug Metab. Rev., 20, 193, 10.3109\u002F03602538909103536",{"doi":2536},{"id":26,"text":2580,"url":26,"identifiers":2581},"Wardman, 1989, Reduction potentials of one-electron couples, J. Phys. Chem. Ref. Data, 18, 1645, 10.1063\u002F1.555843",{"doi":2582},"10.1063\u002F1.555843",{"id":26,"text":2584,"url":26,"identifiers":2585},"Prince, 1982, Quinones of value to electron-transfer studies; oxidation-reduction potentials of the first reduction step in a aprotic solvent, 29",{},{"id":26,"text":2587,"url":26,"identifiers":2588},"Bishop, 1965, Equilibria of substituted semiquinones at high pH, J. Am. Chem. Soc., 87, 501, 10.1021\u002Fja01081a018",{"doi":2589},"10.1021\u002Fja01081a018",{"id":26,"text":2591,"url":26,"identifiers":2592},"Rich, 1980, The kinetics and thermodynamics of the reduction of cytochrome C by substituted p-benzoquinols in solution, Biochim. Biophys. Acta, 592, 506, 10.1016\u002F0005-2728(80)90095-X",{"doi":2593},"10.1016\u002F0005-2728(80)90095-X",{"id":26,"text":2595,"url":26,"identifiers":2596},"Patel, 1973, Semiquinone free radicals and oxygen, Chem. Soc. J. (Faraday Trans.), 69, 814, 10.1039\u002Ff19736900814",{"doi":2597},"10.1039\u002Ff19736900814",{"id":26,"text":2599,"url":26,"identifiers":2600},"Butler, 1987, The reduction of anti-tumour diaziridinyl benzoquinones, Biochim. Biophys. Acta, 925, 144, 10.1016\u002F0304-4165(87)90103-6",{"doi":2601},"10.1016\u002F0304-4165(87)90103-6",{"id":26,"text":2603,"url":26,"identifiers":2604},"Butler, 1987, Are reduced quinones necessarily involved in the antitumour reactivity of quinone drugs?, Br. J. Cancer, 55, 53",{},{"id":26,"text":2606,"url":26,"identifiers":2607},"Mukherjee, 1987, One-electron reduction of juglone: A pulse radiolysis study, Int. J. Radiat. Appl. Instrum., 29, 455",{},{"id":2609,"createTime":2610,"updateTime":2610,"relativeEntities":2611,"slug":2612,"properties":2613,"entityType":781,"verifyStatus":25,"verifyTime":2626,"verifyNote":783,"syncStatus":28,"languages":2627,"translateLanguages":26,"viewCount":36,"primaryUrl":2628,"fullTextUrl":26,"authors":2629,"publicationType":837,"publisherRelationship":2652,"citationCount":2688,"citationInfo":2689,"publishDate":2691,"publishYear":2692,"citationAnalyzeStatus":28,"lastCitationAnalyze":26,"indexDatabases":26,"openAccess":26,"references":2693,"isForceReanalyzing":1904},"488472e1-4755-4f57-b45f-c62f4839ff01","2024-09-19T00:24:17.356+00:00",[],"Glutathione-an-overview-of-biosynthesis-and-modulation",{"mag":2614,"keywords":2616,"openalex":2617,"abstract":2619,"title":2620,"pm":2622,"doi":2624},{"VOID":2615},"1983480912",{},{"VOID":2618},"W1983480912",{},{"EN":2621},"Glutathione: an overview of biosynthesis and modulation",{"VOID":2623},"9679538",{"VOID":2625},"10.1016\u002Fs0009-2797(97)00146-4","2024-09-19T00:24:17.355+00:00",[102],"https:\u002F\u002Flinkinghub.elsevier.com\u002Fretrieve\u002Fpii\u002FS0009279797001464",[2630],{"id":2631,"sortIndex":36,"researcher":26,"roles":2632,"affiliations":2633,"properties":2645},"211893a7-789d-4a8b-93fd-539ab170ac90",[],[2634],{"id":2635,"sortIndex":36,"affiliation":2636,"properties":26},"b7641410-a238-4ba3-b68a-58e42e9ec19a",{"id":2637,"createTime":2638,"updateTime":2639,"relativeEntities":2640,"slug":2641,"properties":2642,"entityType":98,"verifyStatus":28,"verifyTime":26,"verifyNote":26,"syncStatus":28,"languages":26,"translateLanguages":26,"viewCount":36},"89537302-e8bd-4ec0-acb1-5a37897d8a36","2024-09-19T00:24:17.383+00:00","2024-10-11T19:23:32.862+00:00",[],"Department-of-Microbiology-and-Molecular-Cell-Sciences-University-of-Memphis-TN-38152-USA-",{"title":2643},{"EN":2644},"Department of Microbiology and Molecular Cell Sciences, University of Memphis, TN 38152, USA.",{"openalex":2646,"orcid":2648,"title":2650},{"VOID":2647},"A5015017352",{"VOID":2649},"https:\u002F\u002Forcid.org\u002F0000-0001-5342-530X",{"EN":2651},"Mary E. 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Meister. Metabolism and function of glutathione, in: D. Dolphin, R. Poulson, O. Avramovic (Eds.), Glutathione: Chemical, Biochemical and Medical Aspects, Wiley, New York, pp. 367–474.",{"doi":2697},"10.1016\u002F0968-0004(81)90084-0",{"id":26,"text":2699,"url":26,"identifiers":2700},"Meister, 1983, Glutathione, Ann. Rev. Biochem., 52, 711, 10.1146\u002Fannurev.bi.52.070183.003431",{"doi":2701},"10.1146\u002Fannurev.bi.52.070183.003431",{"id":26,"text":2703,"url":26,"identifiers":2704},"Anderson, 1997, Glutathione and Glutathione Delivery Compounds, Adv. Pharmacol., 38, 65, 10.1016\u002FS1054-3589(08)60979-5",{"doi":2705},"10.1016\u002FS1054-3589(08)60979-5",{"id":26,"text":2707,"url":26,"identifiers":2708},"M.E. Anderson, M.E. (1997) Modulation of Glutathione, in: L. Packer, E. Cadenas (Eds.), Handbook of Antioxidants, Marcel Dekker, New York, pp. 321–328.",{},{"id":26,"text":2710,"url":26,"identifiers":2711},"Meister, 1991, Glutathione deficiency produced by inhibition of its synthesis, and its reversal; applications in research and therapy, Pharmacol. Therapeut., 51, 155, 10.1016\u002F0163-7258(91)90076-X",{"doi":2712},"10.1016\u002F0163-7258(91)90076-X",{"id":26,"text":2714,"url":26,"identifiers":2715},"A. Meister, On the biochemistry of glutathione, in: N. Taniguchi, T. Higashi, Y. Sakamoto, A. Meister (Eds.), Glutathione Centennial: Molecular Perspectives and Clinical Implications; Academic Press, New York, 1989, pp. 1–21.",{"doi":2716},"10.1016\u002FB978-0-12-683275-4.50005-X",{"id":26,"text":2718,"url":26,"identifiers":2719},"Orlowski, 1970, The γ-glutamyl cycle: a possible transport system for amino acids, Proc. Natl. Acad. Sci. U.S.A., 67, 1248, 10.1073\u002Fpnas.67.3.1248",{"doi":2720},"10.1073\u002Fpnas.67.3.1248",{"id":26,"text":2722,"url":26,"identifiers":2723},"Thompson, 1976, Hydrolysis and transfer reactions catalyzed by γ- glutamyl transpeptidase; evidence for separate substrate sites and for high affinity of l-cystine, Biochem. Biophys. Res. Commun., 71, 32, 10.1016\u002F0006-291X(76)90245-X",{"doi":2724},"10.1016\u002F0006-291X(76)90245-X",{"id":26,"text":2726,"url":26,"identifiers":2727},"A. Meister, Glutathione Synthesis, in: P.B. Boyer (Ed.), The Enzymes, 3rd ed, vol 10, Academic Press, New York, pp. 671–697.",{"doi":2728},"10.1016\u002FS1874-6047(08)60154-7",{"id":26,"text":2730,"url":26,"identifiers":2731},"Yan, 1990, Amino acid sequence of rat kidney γ-glutamycysteine synthetase, J. Biol. Chem., 265, 1588, 10.1016\u002FS0021-9258(19)40057-4",{"doi":2732},"10.1016\u002FS0021-9258(19)40057-4",{"id":26,"text":2734,"url":26,"identifiers":2735},"Watanabe, 1986, The nucleotide sequence of the gene for γ-glutamylcysteine synthetase of Escherichia coli, Nucleic Acids Res, 14, 4393, 10.1093\u002Fnar\u002F14.11.4393",{"doi":2736},"10.1093\u002Fnar\u002F14.11.4393",{"id":26,"text":2738,"url":26,"identifiers":2739},"Gipp, 1992, Cloning and nucleotide sequence of a full-length cDNA for human γ-glutamylcysteine synthetase, Biochem. Biophys. Res. Commun., 185, 29, 10.1016\u002FS0006-291X(05)80950-7",{"doi":2740},"10.1016\u002FS0006-291X(05)80950-7",{"id":26,"text":2742,"url":26,"identifiers":2743},"Richman, 1973, Regulation of γ-glutamylcysteine synthetase by non-allosteric feedback inhibition by glutathione, J. Biol. Chem., 250, 1422, 10.1016\u002FS0021-9258(19)41830-9",{"doi":2744},"10.1016\u002FS0021-9258(19)41830-9",{"id":26,"text":2746,"url":26,"identifiers":2747},"Huang, 1988, On the active site thiol of γ-glutamylcysteine synthetase: relationships to catalysis, inhibition, and regulation, Proc. Natl. Acad. Sci. U.S.A., 85, 2464, 10.1073\u002Fpnas.85.8.2464",{"doi":2748},"10.1073\u002Fpnas.85.8.2464",{"id":26,"text":2750,"url":26,"identifiers":2751},"Griffith, 1979, Inhibition of glutathione biosynthesis by prothionine (S-n-propyl homocysteine sulfoximine), a selective inhibitor of γ-glutamylcysteine synthetase, J. Biol. Chem., 254, 1205, 10.1016\u002FS0021-9258(17)34188-1",{"doi":2752},"10.1016\u002FS0021-9258(17)34188-1",{"id":26,"text":2754,"url":26,"identifiers":2755},"Griffith, 1979, Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine), J. Biol. Chem., 254, 7558, 10.1016\u002FS0021-9258(18)35980-5",{"doi":2756},"10.1016\u002FS0021-9258(18)35980-5",{"id":26,"text":2758,"url":26,"identifiers":2759},"Griffith, 1977, Inhibition of γ-glutamylcysteine aciduria), Biochem. Biophys. Res. Commun., 79, 919, 10.1016\u002F0006-291X(77)91198-6",{"doi":2760},"10.1016\u002F0006-291X(77)91198-6",{"id":26,"text":2762,"url":26,"identifiers":2763},"Simondsen, 1986, Interaction of the d-isomer of γ-methylene glutamate with an active site thiol of γ-glutamylcysteine synthetase, J. Biol. Chem., 261, 17134, 10.1016\u002FS0021-9258(19)76009-8",{"doi":2764},"10.1016\u002FS0021-9258(19)76009-8",{"id":26,"text":2766,"url":26,"identifiers":2767},"Moore, 1987, Inactivation of γ-glutamylcysteine synthetase, but not of glutamine synthetase, by S-sulfocysteine and S-homocysteine, J. Biol. Chem., 262, 16771, 10.1016\u002FS0021-9258(18)45450-6",{"doi":2768},"10.1016\u002FS0021-9258(18)45450-6",{"id":26,"text":2770,"url":26,"identifiers":2771},"Sekura, 1977, Covalent interaction of l-2-amino-4-oxo-5 chloropentanoate at the glutamate binding site of γ-glutamylcysteine synthetase, J. Biol. Chem., 252, 2606, 10.1016\u002FS0021-9258(17)40501-1",{"doi":2772},"10.1016\u002FS0021-9258(17)40501-1",{"id":26,"text":2774,"url":26,"identifiers":2775},"Beamer, 1980, Interaction of l- and d-3-amino-1-chloro-2-pentanone with γ-glutamylcysteine synthetase, J. Biol. Chem., 255, 11721, 10.1016\u002FS0021-9258(19)70195-1",{"doi":2776},"10.1016\u002FS0021-9258(19)70195-1",{"id":26,"text":2778,"url":26,"identifiers":2779},"Seelig, 1984, Reversible dissociation of γ-glutamylcysteine synthetase into two subunits, J. Biol. Chem., 259, 9345, 10.1016\u002FS0021-9258(17)42703-7",{"doi":2780},"10.1016\u002FS0021-9258(17)42703-7",{"id":26,"text":2782,"url":26,"identifiers":2783},"Huang, 1993, Catalytic and regulatory properties of the heavy subunit of rat kidney γ-glutamylcysteine synthetase, J. Biol. Chem., 268, 19675, 10.1016\u002FS0021-9258(19)36569-X",{"doi":2784},"10.1016\u002FS0021-9258(19)36569-X",{"id":26,"text":2786,"url":26,"identifiers":2787},"Huang, 1993, Amino acid sequence and function of the light subunit of rat kidney γ-glutamylcysteine synthetase, J. Biol. Chem., 268, 20578, 10.1016\u002FS0021-9258(20)80764-9",{"doi":2788},"10.1016\u002FS0021-9258(20)80764-9",{"id":26,"text":2790,"url":26,"identifiers":2791},"Meister, 1985, Glutathione synthetase from rat kidney, Methods Enzymol., 113, 393, 10.1016\u002FS0076-6879(85)13052-1",{"doi":2792},"10.1016\u002FS0076-6879(85)13052-1",{"id":26,"text":2794,"url":26,"identifiers":2795},"Oppenheimer, 1979, Glutathione synthetase: purification from rat kidney and mapping of the substrate binding sites, J. Biol. Chem., 254, 5184, 10.1016\u002FS0021-9258(18)50577-9",{"doi":2796},"10.1016\u002FS0021-9258(18)50577-9",{"id":26,"text":2798,"url":26,"identifiers":2799},"Dodd Mooz, 1973, Glutathione biosynthesis, Methods Enzymol., 17B, 483",{},{"id":26,"text":2801,"url":26,"identifiers":2802},"Gushima, 1984, Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II, Nucleic Acid Res., 12, 9299, 10.1093\u002Fnar\u002F12.24.9299",{"doi":2803},"10.1093\u002Fnar\u002F12.24.9299",{"id":26,"text":2805,"url":26,"identifiers":2806},"Kato, 1988, Role of cysteine residues in glutathione synthetase from Escherichia coli B.: chemical modification and oligonucleotide site-directed mutagenesis, J. Biol. Chem., 263, 11646, 10.1016\u002FS0021-9258(18)37833-5",{"doi":2807},"10.1016\u002FS0021-9258(18)37833-5",{"id":26,"text":2809,"url":26,"identifiers":2810},"Kato, 1989, Crystallization and preliminary X-ray studies of glutathione synthetase from Escherichia coli B, J. Mol. Biol., 209, 503, 10.1016\u002F0022-2836(89)90015-6",{"doi":2811},"10.1016\u002F0022-2836(89)90015-6",{"id":26,"text":2813,"url":26,"identifiers":2814},"Yamaguchi, 1993, Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 A resolution, J. Mol. Biol., 229, 1000, 10.1006\u002Fjmbi.1993.1106",{"doi":2815},"10.1006\u002Fjmbi.1993.1106",{"id":26,"text":2817,"url":26,"identifiers":2818},"Tanaka, 1992, Mutational and proteolytic studies on a flexible loop in glutathione synthetase from Escherichia coli B: the loop and arginine 233 are critical for the catalytic reaction, Biochemistry, 31, 2259, 10.1021\u002Fbi00123a007",{"doi":2819},"10.1021\u002Fbi00123a007",{"id":26,"text":2821,"url":26,"identifiers":2822},"Tanaka, 1993, Flexibility impaired by mutations revealed the multifuctional roles of the loop in glutathione synthetase, Biochemistry, 32, 12398, 10.1021\u002Fbi00097a018",{"doi":2823},"10.1021\u002Fbi00097a018",{"id":26,"text":2825,"url":26,"identifiers":2826},"Kato, 1994, Flexible loop that is novel catalytic machinery in a ligase: atomic structure and function of the loopless glutathione synthetase, Biochemistry, 33, 4995, 10.1021\u002Fbi00183a001",{"doi":2827},"10.1021\u002Fbi00183a001",{"id":26,"text":2829,"url":26,"identifiers":2830},"Huang, 1995, Amino acid sequence of rat kidney glutathione synthetase, Proc. Natl. Acad. Sci. U.S.A., 92, 1232, 10.1073\u002Fpnas.92.4.1232",{"doi":2831},"10.1073\u002Fpnas.92.4.1232",{"id":26,"text":2833,"url":26,"identifiers":2834},"Mutoh, 1991, Cloning and sequencing of the gene encoding the large subunit of glutathione synthetase of Schizosaccharomyces pombe, Biochem. Biophys. Res. Comm., 181, 430, 10.1016\u002FS0006-291X(05)81437-8",{"doi":2835},"10.1016\u002FS0006-291X(05)81437-8",{"id":26,"text":2837,"url":26,"identifiers":2838},"Habennicht, 1993, Molecular cloning of the large subunit of glutathione synthetase from Xenopus laveus embryos, Biochim. Biophys. Acta, 1174, 295, 10.1016\u002F0167-4781(93)90202-O",{"doi":2839},"10.1016\u002F0167-4781(93)90202-O",{"id":26,"text":2841,"url":26,"identifiers":2842},"Gali, 1995, Sequencing and expression of a cDNA for human glutathione synthetase, Biochem. J., 310, 353, 10.1042\u002Fbj3100353",{"doi":2843},"10.1042\u002Fbj3100353",{"id":26,"text":2845,"url":26,"identifiers":2846},"Gali, 1997, Identification of an essential cysteine residue in human glutathione synthase, Biochem. J., 321, 207, 10.1042\u002Fbj3210207",{"doi":2847},"10.1042\u002Fbj3210207",{"id":26,"text":2849,"url":26,"identifiers":2850},"C.S. Huang, L.S. Chiang, A. Meister, M.E. Anderson, Mutations in a conserved domain of rat glutathione synthetase, (in preparation).",{},{"id":26,"text":2852,"url":26,"identifiers":2853},"A. Larsson, Hereditary disorders related to glutathione deficiency, in: D. Dolphin, R. Poulson, O. Avramovic (Eds.), Glutathione: Chemical, Biochemical and Medical Aspects, Wiley, New York, 1989, pp. 197–233.",{},{"id":26,"text":2855,"url":26,"identifiers":2856},"A. Meister, A. Larsson, Glutathione synthetase deficiency and other disorders of the γ-glutamyl cycle, in: C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.), The Metabolic Basis of Inherited Disease, 7th ed, McGraw Hill, New York, 1995, pp 1461–1477.",{},{"id":26,"text":2858,"url":26,"identifiers":2859},"Wellner, 1974, Glutathione synthetase deficiency: an inborn error of metabolism involving the γ-glutamyl cycle in patients with 5-oxoprolinuria (pyroglutamic aciduria), Proc. Natl. Acad. Sci. U.S.A, 71, 2969, 10.1073\u002Fpnas.71.6.2505",{"doi":2860},"10.1073\u002Fpnas.71.6.2505",{"id":26,"text":2862,"url":26,"identifiers":2863},"A. Larsson, L. Hagenfeldt, Hereditary glutathione synthetase deficiency in man, in: A. Larsson, S. Orrenius, A. Holmgren, B. Mannervik (Eds.), Functions of Glutathione—Biochemical, Physiological, Toxicological and Clinical Aspects, Raven Press, New York, 1983, pp. 317–324.",{},{"id":26,"text":2865,"url":26,"identifiers":2866},"Dahl, 1997, Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction, Human Mol. Genet., 6, 1147, 10.1093\u002Fhmg\u002F6.7.1147",{"doi":2867},"10.1093\u002Fhmg\u002F6.7.1147",{"id":26,"text":2869,"url":26,"identifiers":2870},"Rowe, 1973, Studies on the inhibition of glutamine synthetase by methionine sulfone, Biochemistry, 12, 1578, 10.1021\u002Fbi00732a018",{"doi":2871},"10.1021\u002Fbi00732a018",{"id":26,"text":2873,"url":26,"identifiers":2874},"Griffith, 1978, Differential inhibition of glutamine and γ-glutamylcysteine synthetases by α-alkyl analogs of methionine sulfoximine that induce convulsions, J. Biol. Chem., 253, 2333, 10.1016\u002FS0021-9258(17)38077-8",{"doi":2875},"10.1016\u002FS0021-9258(17)38077-8",{"id":26,"text":2877,"url":26,"identifiers":2878},"Suthanthiran, 1990, Glutathione regulates activation-dependent DNA synthesis in highly purified T-lymphocytes stimulated via CD2 and CD3 antigens, Proc. Natl. Acad. Sci. U.S.A., 87, 3343, 10.1073\u002Fpnas.87.9.3343",{"doi":2879},"10.1073\u002Fpnas.87.9.3343",{"id":26,"text":2881,"url":26,"identifiers":2882},"Calvin, 1986, Near-total glutathione depletion and age-specific cataracts induced by buthionine sulfoximine in mice, Science, 233, 553, 10.1126\u002Fscience.3726547",{"doi":2883},"10.1126\u002Fscience.3726547",{"id":26,"text":2885,"url":26,"identifiers":2886},"Griffith, 1985, Origin and turnover of mitochondrial glutathione, Proc. Natl. Acad. Sci. U.S.A., 82, 4668, 10.1073\u002Fpnas.82.14.4668",{"doi":2887},"10.1073\u002Fpnas.82.14.4668",{"id":26,"text":2889,"url":26,"identifiers":2890},"Martensson, 1989, Mitochondrial damage in muscle occurs after marked depletion of glutathione and is prevented by giving glutathione monoester, Proc. Natl. Acad. Sci. U.S.A., 867, 471, 10.1073\u002Fpnas.86.2.471",{"doi":2891},"10.1073\u002Fpnas.86.2.471",{"id":26,"text":2893,"url":26,"identifiers":2894},"Martensson, 1991, Inhibition of glutathione synthesis in the newborn rat: a model for endogenously produced oxidative stress, Proc. Natl. Acad. Sci. U.S.A., 88, 9360, 10.1073\u002Fpnas.88.20.9360",{"doi":2895},"10.1073\u002Fpnas.88.20.9360",{"id":26,"text":2897,"url":26,"identifiers":2898},"Martensson, 1989, Glutathione metabolism in the lung; mitochondrial defects, Proc. Natl. Acad. Sci. U.S.A., 86, 5296, 10.1073\u002Fpnas.86.14.5296",{"doi":2899},"10.1073\u002Fpnas.86.14.5296",{"id":26,"text":2901,"url":26,"identifiers":2902},"Martensson, 1990, Glutathione is required for intestinal function, Proc. Natl. Acad. Sci. U.S.A., 87, 7185, 10.1073\u002Fpnas.87.18.7185",{"doi":2903},"10.1073\u002Fpnas.87.18.7185",{"id":26,"text":2905,"url":26,"identifiers":2906},"Jain, 1992, Ascorbic acid prevents oxidative stress in glutathione-deficient mice: effects on lung type 2 cell lamellar bodies, lung surfactant, and skeletal muscle, Proc. Natl. Acad. Sci. U.S.A., 89, 5093, 10.1073\u002Fpnas.89.11.5093",{"doi":2907},"10.1073\u002Fpnas.89.11.5093",{"id":26,"text":2909,"url":26,"identifiers":2910},"Martensson, 1991, Glutathione deficiency decreases tissue ascorbate levels in newborn rats: ascorbate spares glutathione and protects, Proc. Natl. Acad. Sci. U.S.A., 88, 4656, 10.1073\u002Fpnas.88.11.4656",{"doi":2911},"10.1073\u002Fpnas.88.11.4656",{"id":26,"text":2913,"url":26,"identifiers":2914},"Meister, 1994, Glutathione-ascorbate acid antioxidant system in animals, J. Biol. Chem., 269, 9397, 10.1016\u002FS0021-9258(17)36891-6",{"doi":2915},"10.1016\u002FS0021-9258(17)36891-6",{"id":26,"text":2917,"url":26,"identifiers":2918},"A. Meister, Strategies for increasing cellular glutathione, in: L. Packer, E. Cadenas (Eds.), Biothiols in Health and Disease, Marcel Dekker, New York, 1995, pp. 165–188.",{},{"id":26,"text":2920,"url":26,"identifiers":2921},"White, 1994, Glutathione deficiency in human disease, J. Nutr. Biochem., 5, 218, 10.1016\u002F0955-2863(94)90039-6",{"doi":2922},"10.1016\u002F0955-2863(94)90039-6",{"id":26,"text":2924,"url":26,"identifiers":2925},"Nishiuch, 1976, Cytotoxicity of cysteine in culture media, In Vitro, 12, 635, 10.1007\u002FBF02797462",{"doi":2926},"10.1007\u002FBF02797462",{"id":26,"text":2928,"url":26,"identifiers":2929},"Olney, 1971, Cytotoxic effect of acid and sulphur containing amino acids on the infant mouse central nervous system, Brain Res., 14, 61",{},{"id":26,"text":2931,"url":26,"identifiers":2932},"Anderson, 1987, Intracellular delivery of cysteine, Methods Enzymol., 143, 313, 10.1016\u002F0076-6879(87)43059-0",{"doi":2933},"10.1016\u002F0076-6879(87)43059-0",{"id":26,"text":2935,"url":26,"identifiers":2936},"Cooper, 1982, On the chemistry and biochemistry of 3-mercaptopyruvate acid, the α-keto acid analog of cysteine, J. Biol. Chem., 257, 816, 10.1016\u002FS0021-9258(19)68270-0",{"doi":2937},"10.1016\u002FS0021-9258(19)68270-0",{"id":26,"text":2939,"url":26,"identifiers":2940},"Williamson, 1982, New substrates of 5-oxo-l-prolinase, J. Biol. Chem., 257, 12039, 10.1016\u002FS0021-9258(18)33673-1",{"doi":2941},"10.1016\u002FS0021-9258(18)33673-1",{"id":26,"text":2943,"url":26,"identifiers":2944},"Williamson, 1981, Stimulation of hepatic glutathione formation by administration of l-2-oxothiazolidine-4-carboxylate, a 5-oxo-l-prolinase substrate, Proc. Natl. Acad. Sci. U.S.A, 78, 936, 10.1073\u002Fpnas.78.2.936",{"doi":2945},"10.1073\u002Fpnas.78.2.936",{"id":26,"text":2947,"url":26,"identifiers":2948},"Williamson, 1982, Intracellular cysteine delivery system that protects against toxicity by promoting glutathione synthesis, Proc. Natl. Acad. Sci. U.S.A., 79, 6246, 10.1073\u002Fpnas.79.20.6246",{"doi":2949},"10.1073\u002Fpnas.79.20.6246",{"id":26,"text":2951,"url":26,"identifiers":2952},"Meister, 1986, Intracellular delivery of cysteine and glutathione delivery systems, J. Am. Coll. Nutr., 5, 137, 10.1080\u002F07315724.1986.10720121",{"doi":2953},"10.1080\u002F07315724.1986.10720121",{"id":26,"text":2955,"url":26,"identifiers":2956},"Anderson, 1989, Marked increase of cysteine levels in many regions of the brain after administration of 2-oxothiazolidine-4-carboxylate, FASEB J., 3, 1632, 10.1096\u002Ffasebj.3.5.2920877",{"doi":2957},"10.1096\u002Ffasebj.3.5.2920877",{"id":26,"text":2959,"url":26,"identifiers":2960},"Jain, 1995, l-2-oxothiazolidine-4-carboxylate, a cysteine precursor, stimulates growth and normalizes tissue glutathione concentrations in rats fed a sulfur amino acid deficient diet, J. Nutr., 125, 851",{},{"id":26,"text":2962,"url":26,"identifiers":2963},"Breborowicz, 1993, Enhancement of viability of human peritoneal mesothelial cells with glutathione precursor: l-2 oxothiazolidine-4-carboxylate, Adv. Peritoneal Dialysis, 9, 21",{},{"id":26,"text":2965,"url":26,"identifiers":2966},"Weitberg, 1987, The effect of l-2-oxothiazolidine on glutathione levels in cultured mammalian cells, Mutat. Res., 191, 189, 10.1016\u002F0165-7992(87)90152-7",{"doi":2967},"10.1016\u002F0165-7992(87)90152-7",{"id":26,"text":2969,"url":26,"identifiers":2970},"Shug, 1994, Protection of the ischemic rat heart by procysteine and amino acids, J. Nutr. Biochem., 5, 3356, 10.1016\u002F0955-2863(94)90066-3",{"doi":2971},"10.1016\u002F0955-2863(94)90066-3",{"id":26,"text":2973,"url":26,"identifiers":2974},"D.M. Wilson, R.D. White, L.E. Webb, J.G. Bender, L.L. Pippin, D.L. Goldberg, Amelioration of AZT-induced bone marrow hypoplasia in mice cotreated with glutathione prodrug, Procysteine™ (abstract)., 9th Int. Conf. AIDS, June 7–11, 1993, Berlin.",{},{"id":26,"text":2976,"url":26,"identifiers":2977},"S. Josephs, C. Asuncion, C. Sun, P. Jacobson, L. Webb, Procysteine (l-2 oxothiazolidine-4-carboxylic acid) reduces the toxicity of AZT (zidovudine) and enhances the antiviral activity of AZT in cultured peripheral blood mononuclear cells (PBMC), abstract 230. 10th Int. Conf. AIDS, June 6–11, 1993, Berlin.",{},{"id":26,"text":2979,"url":26,"identifiers":2980},"Lederman, 1995, l-2-oxothiazolidine-4-carboxylic acid (procysteine) inhibits expression of the human immunodeficiency virus and expression of the interleukin-2 receptor α-chain, J. Acq. Immune Def. Syndr., 8, 107",{},{"id":26,"text":2982,"url":26,"identifiers":2983},"Porta, 1991, l-2-oxothiazolidine-4 carboxylic acid, a cysteine prodrug: pharmacokinetics and effects on thiols in plasma and lymphocytes in human, J. Pharmacol. Exp. Ther., 257, 331",{},{"id":26,"text":2985,"url":26,"identifiers":2986},"Kalayjian, 1994, A phase I\u002FII trial of intravenous l-2-oxothiazolidine-4-carboxylic acid (procysteine) in asymptomatic HIV infected subjects, J. Acq. Immune Def. Syndr., 7, 369",{},{"id":26,"text":2988,"url":26,"identifiers":2989},"Anderson, 1983, Transport and direct utilization of γ- glutamylcyst(e)ine for glutathione synthesis, Proc. Natl. Acad. Sci. U.S.A., 80, 707, 10.1073\u002Fpnas.80.3.707",{"doi":2990},"10.1073\u002Fpnas.80.3.707",{"id":26,"text":2992,"url":26,"identifiers":2993},"Pileblad, 1992, Increase in rat brain glutathione following intracerebroventricular administration of γ-glutamylcysteine, Biochem. Pharmacol., 44, 895, 10.1016\u002F0006-2952(92)90121-X",{"doi":2994},"10.1016\u002F0006-2952(92)90121-X",{"id":26,"text":2996,"url":26,"identifiers":2997},"Puri, 1983, Transport of glutathione, as γ-glutamylcysteinylglycyl ester, into liver and kidney, Proc. Natl. Acad. Sci. U.S.A., 80, 5258, 10.1073\u002Fpnas.80.17.5258",{"doi":2998},"10.1073\u002Fpnas.80.17.5258",{"id":26,"text":3000,"url":26,"identifiers":3001},"Anderson, 1985, Glutathione monoethyl ester: preparation, uptake by tissues, and conversion to glutathione, Arch. Biochem. Biophys., 239, 538, 10.1016\u002F0003-9861(85)90723-4",{"doi":3002},"10.1016\u002F0003-9861(85)90723-4",{"id":26,"text":3004,"url":26,"identifiers":3005},"Anderson, 1989, Glutathione metabolism at the blood-cerebrospinal fluid barrier, FASEB J., 3, 2527, 10.1096\u002Ffasebj.3.13.2572501",{"doi":3006},"10.1096\u002Ffasebj.3.13.2572501",{"id":26,"text":3008,"url":26,"identifiers":3009},"Martensson, 1989, Glutathione ester prevents buthionine sulfoximine-induced cataracts and lens epithelial cell damage, Proc. Natl. Acad. Sci. 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Commun., 289, 712, 10.1006\u002Fbbrc.2001.6032",{"doi":3244},"10.1006\u002Fbbrc.2001.6032",{"id":26,"text":3246,"url":26,"identifiers":3247},"Prozorovski, 1992, Identification of reactive tyrosine residues in cysteine-reactive dehydrogenases: differences between liver sorbitol, liver alcohol and Drosophila alcohol dehydrogenases, FEBS Lett., 304, 46, 10.1016\u002F0014-5793(92)80586-6",{"doi":3248},"10.1016\u002F0014-5793(92)80586-6",{"id":26,"text":3250,"url":26,"identifiers":3251},"Krook, 1992, Short-chain dehydrogenases: proteolysis and chemical modification of prokaryotic 3 alpha\u002F20 beta-hydroxysteroid, insect alcohol and human 15-hydroxyprostaglandin dehydrogenases, Eur. J. Biochem., 209, 233, 10.1111\u002Fj.1432-1033.1992.tb17281.x",{"doi":3252},"10.1111\u002Fj.1432-1033.1992.tb17281.x",{"id":26,"text":3254,"url":26,"identifiers":3255},"Andersson, 1996, Crystal structure of the ternary complex of 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor, Structure, 4, 1161, 10.1016\u002FS0969-2126(96)00124-4",{"doi":3256},"10.1016\u002FS0969-2126(96)00124-4",{"id":26,"text":3258,"url":26,"identifiers":3259},"Zhou, 1999, Threonine 188 is critical for interaction with NAD+ in human NAD+-dependent 15-hydroxyprostaglandin dehydrogenase, Biochem. Biophys. Res. Commun., 257, 414, 10.1006\u002Fbbrc.1999.0356",{"doi":3260},"10.1006\u002Fbbrc.1999.0356",{"id":26,"text":3262,"url":26,"identifiers":3263},"J. Benach, C. Filling, U. Oppermann, R.P.G. Bricogne, K.D. Berndt, H. Jornvall, R. Ladenstein, Structure of bacterial 3b\u002F17b-hydroxysteroid dehydrogenase at 1.2 Å resolution: a model for multiple steroid recognitions, Biochemistry, in press.",{},{"id":26,"text":3265,"url":26,"identifiers":3266},"Ghosh, 2001, Molecular mechanisms of estrogen recognition and 17-keto reduction by human 17beta-hydroxysteroid dehydrogenase 1, Chem. Biol. Interact., 130–132, 637, 10.1016\u002FS0009-2797(00)00255-6",{"doi":3267},"10.1016\u002FS0009-2797(00)00255-6",{"id":26,"text":3269,"url":26,"identifiers":3270},"Ghosh, 2001, Porcine carbonyl reductase: structural basis for a functional monomer in short chain dehydrogenases\u002Freductases, J. Biol. Chem., 276, 18457, 10.1074\u002Fjbc.M100538200",{"doi":3271},"10.1074\u002Fjbc.M100538200",{"id":26,"text":3273,"url":26,"identifiers":3274},"Benach, 1998, The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 Å resolution, J. Mol. Biol., 282, 383, 10.1006\u002Fjmbi.1998.2015",{"doi":3275},"10.1006\u002Fjmbi.1998.2015",{"id":26,"text":3277,"url":26,"identifiers":3278},"Agarwal, 1995, Mutations in putative glycosylation sites of rat 11 beta-hydroxysteroid dehydrogenase affect enzymatic activity, Biochim. Biophys. Acta, 1248, 70, 10.1016\u002F0167-4838(95)00005-F",{"doi":3279},"10.1016\u002F0167-4838(95)00005-F",{"id":26,"text":3281,"url":26,"identifiers":3282},"Eklund, 1982, Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase, J. Biol. Chem., 257, 14349, 10.1016\u002FS0021-9258(19)45387-8",{"doi":3283},"10.1016\u002FS0021-9258(19)45387-8",{"id":26,"text":3285,"url":26,"identifiers":3286},"van Hylckama Vlieg, 2001, Halohydrin dehalogenases are structurally and mechanistically related to short-chain dehydrogenases\u002Freductases, J. Bacteriol., 183, 5058, 10.1128\u002FJB.183.17.5058-5066.2001",{"doi":3287},"10.1128\u002FJB.183.17.5058-5066.2001",{"id":26,"text":3289,"url":26,"identifiers":3290},"Gourley, 2001, Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites, Nat. Struct. Biol., 8, 521, 10.1038\u002F88584",{"doi":3291},"10.1038\u002F88584",{"id":26,"text":3293,"url":26,"identifiers":3294},"Pereira, 2001, Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme, Nat. Struct. Biol., 8, 215, 10.1038\u002F84948",{"doi":3295},"10.1038\u002F84948",{"id":26,"text":3297,"url":26,"identifiers":3298},"Stammers, 2001, The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase\u002Freductases, EMBO J., 20, 6619, 10.1093\u002Femboj\u002F20.23.6619",{"doi":3299},"10.1093\u002Femboj\u002F20.23.6619",{"id":26,"text":3301,"url":26,"identifiers":3302},"Nobel, 2001, Metabolic conversion as a pre-receptor control mechanism for lipophilic hormones, Eur. J. Biochem., 268, 4113, 10.1046\u002Fj.1432-1327.2001.02359.x",{"doi":3303},"10.1046\u002Fj.1432-1327.2001.02359.x",{"id":26,"text":3305,"url":26,"identifiers":3306},"Barf, 2002, Arylsulfonamidothiazoles as a new class of potential antidiabetic drugs: inhibitors of the 11beta hydroxysteroid dehydrogenase type 1, J. Med. Chem., 45, 3813, 10.1021\u002Fjm025530f",{"doi":3307},"10.1021\u002Fjm025530f",{"id":26,"text":3309,"url":26,"identifiers":3310},"Sandeep, 2001, Pathophysiology of modulation of local glucocorticoid levels by 11beta-hydroxysteroid dehydrogenases, Trends Endocrinol. Metab., 12, 446, 10.1016\u002FS1043-2760(01)00499-4",{"doi":3311},"10.1016\u002FS1043-2760(01)00499-4",{"id":26,"text":3313,"url":26,"identifiers":3314},"Kotelevtsev, 1997, 11beta-Hydroxysteroid dehydrogenase type 1 knockout mice show attenuated glucocorticoid-inducible responses and resist hyperglycemia on obesity or stress, Proc. Natl. Acad. Sci. USA, 94, 14924, 10.1073\u002Fpnas.94.26.14924",{"doi":3315},"10.1073\u002Fpnas.94.26.14924",{"id":26,"text":3317,"url":26,"identifiers":3318},"Masuzaki, 2001, A transgenic model of visceral obesity and the metabolic syndrome, Science, 294, 2166, 10.1126\u002Fscience.1066285",{"doi":3319},"10.1126\u002Fscience.1066285",{"id":26,"text":3321,"url":26,"identifiers":3322},"Davani, 2000, Type 1 11beta-hydroxysteroid dehydrogenase mediates glucocorticoid activation and insulin release in pancreatic islets, J. Biol. Chem., 275, 34841, 10.1074\u002Fjbc.C000600200",{"doi":3323},"10.1074\u002Fjbc.C000600200",{"id":26,"text":3325,"url":26,"identifiers":3326},"Duax, 2000, Steroid dehydrogenase structures, mechanism of action, and disease, Vitam. Horm., 58, 121, 10.1016\u002FS0083-6729(00)58023-6",{"doi":3327},"10.1016\u002FS0083-6729(00)58023-6",{"id":26,"text":3329,"url":26,"identifiers":3330},"Hoffren, 2001, Structure-based focusing using pharmacophores derived from the active site of 17beta-hydroxysteroid dehydrogenase, Curr. Pharm. Des., 7, 547, 10.2174\u002F1381612013397870",{"doi":3331},"10.2174\u002F1381612013397870",{"id":26,"text":3333,"url":26,"identifiers":3334},"Thompson, 1997, Trihydroxynaphthalene reductase from Magnaporthe grisea: realization of an active center inhibitor and elucidation of the kinetic mechanism, Biochemistry, 36, 1852, 10.1021\u002Fbi962355u",{"doi":3335},"10.1021\u002Fbi962355u",{"id":26,"text":3337,"url":26,"identifiers":3338},"Thompson, 2000, The second naphthol reductase of fungal melanin biosynthesis in Magnaporthe grisea: tetrahydroxynaphthalene reductase, J. Biol. Chem., 275, 34867, 10.1074\u002Fjbc.M006659200",{"doi":3339},"10.1074\u002Fjbc.M006659200",{"id":26,"text":3341,"url":26,"identifiers":3342},"Price, 2001, Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis, Biochemistry, 40, 12772, 10.1021\u002Fbi010737g",{"doi":3343},"10.1021\u002Fbi010737g",{"id":26,"text":3345,"url":26,"identifiers":3346},"Rozwarski, 1999, Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate, J. Biol. 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Appl. Toxicol., 20, 273, 10.1006\u002Ffaat.1993.1036",{"doi":3483},"10.1006\u002Ffaat.1993.1036",{"id":26,"text":3485,"url":26,"identifiers":3486},"Sultatos, 1983, Hepatic microsomal detoxification of the organophosphates paraoxon and chlorpyrifos oxon in the mouse, Drug Metab. Dispos., 11, 232",{},{"id":26,"text":3488,"url":26,"identifiers":3489},"Sultatos, 1983, Kinetic analyses of the microsomal biotransformation of the phosphorothioate insecticides chlorpyrifos and parathion, Fundam. Appl. Toxicol., 3, 16, 10.1016\u002FS0272-0590(83)80167-5",{"doi":3490},"10.1016\u002FS0272-0590(83)80167-5",{"id":26,"text":3492,"url":26,"identifiers":3493},"Miyazaki, 1972, Chronic toxicity of dursban and its metabolite, 3,5,6-trichloro-2-pyridinol in chickens, Toxicol. Appl. Pharmacol., 23, 391, 10.1016\u002F0041-008X(72)90041-5",{"doi":3494},"10.1016\u002F0041-008X(72)90041-5",{"id":26,"text":3496,"url":26,"identifiers":3497},"Goel, 2000, Protective effects of zinc in chlorpyrifos induced hepatotoxicity: a biochemical and trace elemental study, Biol. Trace Elem. Res., 74, 171, 10.1385\u002FBTER:74:2:171",{"doi":3498},"10.1385\u002FBTER:74:2:171",{"id":26,"text":3500,"url":26,"identifiers":3501},"Goel, 2001, Zinc supplementation prevents liver injury in chlorpyrifos-treated rats, Biol. Trace Elem. Res., 82, 185, 10.1385\u002FBTER:82:1-3:185",{"doi":3502},"10.1385\u002FBTER:82:1-3:185",{"id":26,"text":3504,"url":26,"identifiers":3505},"Bebe, 2003, Exposure to low doses of endosulfan and chlorpyrifos modifies endogenous antioxidants in tissues of rats, J. Environ. Sci. Health B, 38, 349, 10.1081\u002FPFC-120019901",{"doi":3506},"10.1081\u002FPFC-120019901",{"id":26,"text":3508,"url":26,"identifiers":3509},"Buckley, 2005, Oximes for acute organophosphate pesticide poisoning, Cochrane Database Syst. Rev., CD005085",{},{"id":26,"text":3511,"url":26,"identifiers":3512},"Cagen, 1979, Protection of carbon tetrachloride-induced hepatotoxicity by zinc: role of metallothionein, Toxicol. Appl. Pharmacol., 51, 107, 10.1016\u002F0041-008X(79)90013-9",{"doi":3513},"10.1016\u002F0041-008X(79)90013-9",{"id":26,"text":3515,"url":26,"identifiers":3516},"Chvapil, 1972, Effect of zinc on lipid peroxidation in liver microsomes and mitochondria, Proc. Soc. Exp. Biol. Med., 141, 150, 10.3181\u002F00379727-141-36734",{"doi":3517},"10.3181\u002F00379727-141-36734",{"id":26,"text":3519,"url":26,"identifiers":3520},"Cabre, 1999, Inhibition of hepatic cell nuclear DNA fragmentation by zinc in carbon tetrachloride-treated rats, J. Hepatol., 31, 228, 10.1016\u002FS0168-8278(99)80218-9",{"doi":3521},"10.1016\u002FS0168-8278(99)80218-9",{"id":26,"text":3523,"url":26,"identifiers":3524},"Sidhu, 2004, Protective effects of zinc on oxidative stress enzymes in liver of protein deficient rats, Nutr. Hosp., 19, 341",{},{"id":26,"text":3526,"url":26,"identifiers":3527},"Sidhu, 2004, Protective role of zinc in nickel induced hepatotoxicity in rats, Chem. Biol. Interact., 150, 199, 10.1016\u002Fj.cbi.2004.09.012",{"doi":3528},"10.1016\u002Fj.cbi.2004.09.012",{"id":26,"text":3530,"url":26,"identifiers":3531},"Sidhu, 2004, Role of zinc in regulating the levels of hepatic elements following nickel toxicity in rats, Biol. Trace Elem. Res., 102, 161, 10.1385\u002FBTER:102:1-3:161",{"doi":3532},"10.1385\u002FBTER:102:1-3:161",{"id":26,"text":3534,"url":26,"identifiers":3535},"Lowry, 1951, Protein measurement with the Folin phenol reagent, J. Biol. Chem., 193, 265, 10.1016\u002FS0021-9258(19)52451-6",{"doi":3536},"10.1016\u002FS0021-9258(19)52451-6",{"id":26,"text":3538,"url":26,"identifiers":3539},"Hochstein, 1964, Evidence for the involvement of iron in the ADP-activated peroxidation of lipids in microsomes and mitochondria, Biochem. Biophys. Res. Commun., 14, 323, 10.1016\u002FS0006-291X(64)80004-8",{"doi":3540},"10.1016\u002FS0006-291X(64)80004-8",{"id":26,"text":3542,"url":26,"identifiers":3543},"Luck, 1954, Quantitative determination of catalase activity of biological material, Enzymologia, 17, 31",{},{"id":26,"text":3545,"url":26,"identifiers":3546},"Kono, 1978, Generation of superoxide radical during autoxidation of hydroxylamine and an assay for superoxide dismutase, Arch. Biochem. Biophys., 186, 189, 10.1016\u002F0003-9861(78)90479-4",{"doi":3547},"10.1016\u002F0003-9861(78)90479-4",{"id":26,"text":3549,"url":26,"identifiers":3550},"Moron, 1979, Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver, Biochim. Biophys. Acta, 582, 67, 10.1016\u002F0304-4165(79)90289-7",{"doi":3551},"10.1016\u002F0304-4165(79)90289-7",{"id":26,"text":3553,"url":26,"identifiers":3554},"Williams, 1967, Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and thioredoxin, J. Biol. Chem., 242, 5226, 10.1016\u002FS0021-9258(18)99415-9",{"doi":3555},"10.1016\u002FS0021-9258(18)99415-9",{"id":26,"text":3557,"url":26,"identifiers":3558},"Habig, 1974, Glutathione S-transferases: the first enzymatic step in mercapturic acid formation, J. Biol. Chem., 249, 7130, 10.1016\u002FS0021-9258(19)42083-8",{"doi":3559},"10.1016\u002FS0021-9258(19)42083-8",{"id":26,"text":3561,"url":26,"identifiers":3562},"Flohe, 1984, Assays of glutathione peroxidase, Methods Enzymol., 105, 114, 10.1016\u002FS0076-6879(84)05015-1",{"doi":3563},"10.1016\u002FS0076-6879(84)05015-1",{"id":26,"text":3565,"url":26,"identifiers":3566},"Eaton, 1982, Evaluation of the Cd\u002Fhemoglobin affinity assay for the rapid determination of metallothionein in biological tissues, Toxicol. Appl. Pharmacol., 66, 134, 10.1016\u002F0041-008X(82)90068-0",{"doi":3567},"10.1016\u002F0041-008X(82)90068-0",{"id":26,"text":3569,"url":26,"identifiers":3570},"Abou-Donia, 1981, Organophosphorus ester-induced delayed neurotoxicity, Annu. Rev. Pharmacol. Toxicol., 21, 511, 10.1146\u002Fannurev.pa.21.040181.002455",{"doi":3571},"10.1146\u002Fannurev.pa.21.040181.002455",{"id":26,"text":3573,"url":26,"identifiers":3574},"Rahman, 1990, Haematological and hepatotoxic effects of isoprocarb in chicken, J. Appl. Toxicol., 10, 187, 10.1002\u002Fjat.2550100308",{"doi":3575},"10.1002\u002Fjat.2550100308",{"id":26,"text":3577,"url":26,"identifiers":3578},"Dhawan, 1994, Protective role of zinc on rat liver function in long-term toxicity induced by carbontetrachloride, J. Trace Elem. Exp. Med., 7, 1",{},{"id":26,"text":3580,"url":26,"identifiers":3581},"Dhawan, 1995, Further evidence for zinc as a hepatoprotective agent in rat liver toxicity, Exp. Mol. Pathol., 63, 110, 10.1006\u002Fexmp.1995.1035",{"doi":3582},"10.1006\u002Fexmp.1995.1035",{"id":26,"text":3584,"url":26,"identifiers":3585},"Gutteridge, 2000, Free radicals and antioxidants in the year 2000: a historical look to the future, Ann. N. Y. Acad. Sci., 899, 136, 10.1111\u002Fj.1749-6632.2000.tb06182.x",{"doi":3586},"10.1111\u002Fj.1749-6632.2000.tb06182.x",{"id":26,"text":3588,"url":26,"identifiers":3589},"Tappel, 1973, Lipid peroxidation damage to cell components, Fed. Proc., 32, 1870",{},{"id":26,"text":3591,"url":26,"identifiers":3592},"Bettger, 1981, A critical physiological role of zinc in the structure and function of biomembranes, Life Sci., 28, 1425, 10.1016\u002F0024-3205(81)90374-X",{"doi":3593},"10.1016\u002F0024-3205(81)90374-X",{"id":26,"text":3595,"url":26,"identifiers":3596},"Younes, 1981, Mechanistic aspects of enhanced lipid peroxidation following glutathione depletion in vivo, Chem. Biol. Interact., 34, 257, 10.1016\u002F0009-2797(81)90098-3",{"doi":3597},"10.1016\u002F0009-2797(81)90098-3",{"id":26,"text":3599,"url":26,"identifiers":3600},"Hayes, 2005, Glutathione transferases, Annu. Rev. Pharmacol. Toxicol., 45, 51, 10.1146\u002Fannurev.pharmtox.45.120403.095857",{"doi":3601},"10.1146\u002Fannurev.pharmtox.45.120403.095857",{"id":26,"text":3603,"url":26,"identifiers":3604},"Cathcart, 1985, Vitamin C: the nontoxic, nonrate-limited, antioxidant free radical scavenger, Med. Hypotheses, 18, 61, 10.1016\u002F0306-9877(85)90121-5",{"doi":3605},"10.1016\u002F0306-9877(85)90121-5",{"id":26,"text":3607,"url":26,"identifiers":3608},"Ludwig, 1980, Interaction of zinc ions with electron carrying coenzymes NADPH and NADH, Chem. Biol. Interact., 30, 25, 10.1016\u002F0009-2797(80)90111-8",{"doi":3609},"10.1016\u002F0009-2797(80)90111-8",{"id":26,"text":3611,"url":26,"identifiers":3612},"Kyle, 1987, Superoxide dismutase and catalase protect cultured hepatocytes from the cytotoxicity of acetaminophen, Biochem. Biophys. Res. Commun., 149, 889, 10.1016\u002F0006-291X(87)90491-8",{"doi":3613},"10.1016\u002F0006-291X(87)90491-8",{"id":26,"text":3615,"url":26,"identifiers":3616},"Mates, 1999, Antioxidant enzymes and their implications in pathophysiologic processes, Front. Biosci., 4, D339, 10.2741\u002FMates",{"doi":3617},"10.2741\u002FMates",{"id":26,"text":3619,"url":26,"identifiers":3620},"Mates, 1999, Antioxidant enzymes and human diseases, Clin. Biochem., 32, 595, 10.1016\u002FS0009-9120(99)00075-2",{"doi":3621},"10.1016\u002FS0009-9120(99)00075-2",{"id":26,"text":3623,"url":26,"identifiers":3624},"Yu, 1994, Cellular defenses against damage from reactive oxygen species, Physiol. Rev., 74, 139, 10.1152\u002Fphysrev.1994.74.1.139",{"doi":3625},"10.1152\u002Fphysrev.1994.74.1.139",{"id":26,"text":3627,"url":26,"identifiers":3628},"Sultatos, 1982, Factors involved in the differential acute toxicity of the insecticides chlorpyrifos and methyl chlorpyrifos in mice, Toxicol. Appl. Pharmacol., 65, 144, 10.1016\u002F0041-008X(82)90372-6",{"doi":3629},"10.1016\u002F0041-008X(82)90372-6",{"id":26,"text":3631,"url":26,"identifiers":3632},"Seagrave, 1983, Zinc effects on glutathione metabolism relationship to zinc-induced protection from alkylating agents, Biochem. Pharmacol., 32, 3017, 10.1016\u002F0006-2952(83)90243-5",{"doi":3633},"10.1016\u002F0006-2952(83)90243-5",{"id":26,"text":3635,"url":26,"identifiers":3636},"Taylor, 1988, Effect of dietary zinc or copper deficiency on the primary free radical defense system in rats, J. Nutr., 118, 613, 10.1093\u002Fjn\u002F118.5.613",{"doi":3637},"10.1093\u002Fjn\u002F118.5.613",{"id":26,"text":3639,"url":26,"identifiers":3640},"Sato, 1989, Effect of zinc deficiency on the accumulation of metallothionein and cadmium in the rat liver and kidney, Arch. Environ. Contam. Toxicol., 18, 587, 10.1007\u002FBF01055026",{"doi":3641},"10.1007\u002FBF01055026",{"id":26,"text":3643,"url":26,"identifiers":3644},"Liu, 1992, A multivariate study of protective effects of Zn and Cu against nephrotoxicity induced by cadmium metallothionein in rats, Toxicol. Appl. Pharmacol., 114, 239, 10.1016\u002F0041-008X(92)90074-3",{"doi":3645},"10.1016\u002F0041-008X(92)90074-3",{"id":26,"text":3647,"url":26,"identifiers":3648},"Durnam, 1981, Transcriptional regulation of the mouse metallothionein-I gene by heavy metals, J. Biol. 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Rev. Biochem. Mol. Biol., 27, 283, 10.3109\u002F10409239209082565",{"doi":3771},"10.3109\u002F10409239209082565",{"id":26,"text":3773,"url":26,"identifiers":3774},"Vasiliou, 2000, Polymorphisms of human aldehyde dehydrogenases: consequences for drug metabolism and disease, Pharmacology, 61, 192, 10.1159\u002F000028400",{"doi":3775},"10.1159\u002F000028400",{"id":26,"text":3777,"url":26,"identifiers":3778},"Duester, 2000, Families of retinoid dehydrogenases regulating vitamin A function: production of visual pigment and retinoic acid, Eur. J. Biochem., 267, 4315, 10.1046\u002Fj.1432-1327.2000.01497.x",{"doi":3779},"10.1046\u002Fj.1432-1327.2000.01497.x",{"id":26,"text":3781,"url":26,"identifiers":3782},"Mark, 1999, A genetic dissection of the retinoid signalling pathway in the mouse, Proc. Nutr. Soc., 58, 609, 10.1017\u002FS0029665199000798",{"doi":3783},"10.1017\u002FS0029665199000798",{"id":26,"text":3785,"url":26,"identifiers":3786},"Malcangio, 1996, GABA and its receptors in the spinal cord, Trends Pharmacol. Sci., 17, 457, 10.1016\u002FS0165-6147(96)01013-9",{"doi":3787},"10.1016\u002FS0165-6147(96)01013-9",{"id":26,"text":3789,"url":26,"identifiers":3790},"Seiler, 1975, 4-Aminobutyrate in mammalian putrescine catabolism, Biochem. J., 152, 201, 10.1042\u002Fbj1520201",{"doi":3791},"10.1042\u002Fbj1520201",{"id":26,"text":3793,"url":26,"identifiers":3794},"Seiler, 1974, Putrescine catabolism in mammalian brain, Biochem. J., 144, 29, 10.1042\u002Fbj1440029",{"doi":3795},"10.1042\u002Fbj1440029",{"id":26,"text":3797,"url":26,"identifiers":3798},"Kikonyogo, 1996, Aldehyde dehydrogenase from adult human brain that dehydrogenates γ-aminobutyraldehyde: purification, characterization, cloning and distribution, Biochem. J., 316, 317, 10.1042\u002Fbj3160317",{"doi":3799},"10.1042\u002Fbj3160317",{"id":26,"text":3801,"url":26,"identifiers":3802},"Nakajima, 1993, Cytochrome P450-related differences between rats and mice in the metabolism of benzene, toluene and trichloroethylene in liver microsomes, Biochem. Pharmacol., 45, 1079, 10.1016\u002F0006-2952(93)90252-R",{"doi":3803},"10.1016\u002F0006-2952(93)90252-R",{"id":26,"text":3805,"url":26,"identifiers":3806},"Fisher, 1998, A human physiologically based pharmacokinetic model for trichloroethylene and its metabolites, trichloroacetic acid and free trichloroethanol, Toxicol. Appl. Pharmacol., 152, 339, 10.1006\u002Ftaap.1998.8486",{"doi":3807},"10.1006\u002Ftaap.1998.8486",{"id":26,"text":3809,"url":26,"identifiers":3810},"Green, 1997, Tricholoethylene induced cancer in animals and its relevance to humans, J. Occup. Health, 39, 261, 10.1539\u002Fjoh.39.261",{"doi":3811},"10.1539\u002Fjoh.39.261",{"id":26,"text":3813,"url":26,"identifiers":3814},"Ashby, 1994, Mechanistically-based human hazard assessment of peroxisome proliferator-induced hepatocarcinogenesis, Hum. Exp. Toxicol., 13, S1, 10.1177\u002F096032719401300201",{"doi":3815},"10.1177\u002F096032719401300201",{"id":26,"text":3817,"url":26,"identifiers":3818},"Johnson, 1998, A review: trichloroethylene metabolites: potential cardiac teratogens, Environ. Health Perspect., 106, 995, 10.1289\u002Fehp.98106s4995",{"doi":3819},"10.1289\u002Fehp.98106s4995",{"id":26,"text":3821,"url":26,"identifiers":3822},"Johnson, 1998, Cardiac teratogenicity of trichloroethylene metabolites, J. Am. Coll. Cardiol., 32, 540, 10.1016\u002FS0735-1097(98)00232-0",{"doi":3823},"10.1016\u002FS0735-1097(98)00232-0",{"id":26,"text":3825,"url":26,"identifiers":3826},"Stauber, 1998, Dichloroacetate and trichloroacetate promote clonal expansion of anchorage-independent hepatocytes in vivo and in vitro, Toxicol. Appl. Pharmacol., 150, 287, 10.1006\u002Ftaap.1998.8417",{"doi":3827},"10.1006\u002Ftaap.1998.8417",{"id":26,"text":3829,"url":26,"identifiers":3830},"Sharpe, 1993, Substrate specificity of rat liver aldehyde dehydrogenase with chloroacetaldehydes, J. Biochem. Toxicol., 8, 155, 10.1002\u002Fjbt.2570080307",{"doi":3831},"10.1002\u002Fjbt.2570080307",{"id":26,"text":3833,"url":26,"identifiers":3834},"Pietruszko, 1999, Aldehyde inhibitors of aldehyde dehydrogenases, Adv. Exp. Med. Biol., 463, 79, 10.1007\u002F978-1-4615-4735-8_10",{"doi":3835},"10.1007\u002F978-1-4615-4735-8_10",{"id":26,"text":3837,"url":26,"identifiers":3838},"Dayhoff, 1976, The origin and evolution of protein superfamilies, Fed. Proc., 35, 2132",{},{"id":26,"text":3840,"url":26,"identifiers":3841},"Tatusov, 1997, A genomic prespective on protein families, Science, 278, 631, 10.1126\u002Fscience.278.5338.631",{"doi":3842},"10.1126\u002Fscience.278.5338.631",{"id":26,"text":3844,"url":26,"identifiers":3845},"N.A. Sophos, A. Pappa, T. Ziegler, V. Vasiliou, Aldehyde dehydrogenase gene superfamily: the 2000 update, Chem. Biol. Interact., in press.",{"doi":3846},"10.1016\u002FS0009-2797(00)00275-1",{"id":26,"text":3848,"url":26,"identifiers":3849},"Vasiliou, 1999, Eukaryotic aldehyde dehydrogenase (ALDH) genes: human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping, Pharmacogenetics, 9, 421",{},{"id":26,"text":3851,"url":26,"identifiers":3852},"Hsu, 1985, Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2, Proc. Natl. Acad. Sci. USA, 82, 3771, 10.1073\u002Fpnas.82.11.3771",{"doi":3853},"10.1073\u002Fpnas.82.11.3771",{"id":26,"text":3855,"url":26,"identifiers":3856},"Rongnoparut, 1991, Isolation and characterization of a cytosolic aldehyde dehydrogenase-encoding cDNA from mouse liver, Gene, 101, 261, 10.1016\u002F0378-1119(91)90421-7",{"doi":3857},"10.1016\u002F0378-1119(91)90421-7",{"id":26,"text":3859,"url":26,"identifiers":3860},"Bhat, 1995, Cloning of a cDNA encoding rat aldehyde dehydrogenase with high activity for retinal oxidation, Gene, 166, 303, 10.1016\u002F0378-1119(96)81752-5",{"doi":3861},"10.1016\u002F0378-1119(96)81752-5",{"id":26,"text":3863,"url":26,"identifiers":3864},"von Bahr-Lindstrom, 1984, The cytoplasmic isoenzyme of horse liver aldehyde dehydrogenase: relationship to the corresponding human isoenzyme, Eur. J. Biochem., 141, 37, 10.1111\u002Fj.1432-1033.1984.tb08152.x",{"doi":3865},"10.1111\u002Fj.1432-1033.1984.tb08152.x",{"id":26,"text":3867,"url":26,"identifiers":3868},"Stayner, 1995, Cloning and characterization of the cDNA for sheep liver cytosolic aldehyde dehydrogenase, Adv. Exp. Med. Biol., 372, 61, 10.1007\u002F978-1-4615-1965-2_8",{"doi":3869},"10.1007\u002F978-1-4615-1965-2_8",{"id":26,"text":3871,"url":26,"identifiers":3872},"Saari, 1995, Characterization and localization of an aldehyde dehydrogenase to amacrine cells of bovine retina, Vis. Neurosci., 12, 263, 10.1017\u002FS095252380000794X",{"doi":3873},"10.1017\u002FS095252380000794X",{"id":26,"text":3875,"url":26,"identifiers":3876},"Godbout, 1992, High levels of aldehyde dehydrogenase transcripts in the undifferentiated chick retina, Exp. Eye Res., 54, 297, 10.1016\u002FS0014-4835(05)80219-2",{"doi":3877},"10.1016\u002FS0014-4835(05)80219-2",{"id":26,"text":3879,"url":26,"identifiers":3880},"Ang, 1999, Stimulation of premature retinoic acid synthesis in Xenopus embryos following premature expression of aldehyde dehydrogenase ALDH1, Eur. J. Biochem., 260, 227, 10.1046\u002Fj.1432-1327.1999.00139.x",{"doi":3881},"10.1046\u002Fj.1432-1327.1999.00139.x",{"id":26,"text":3883,"url":26,"identifiers":3884},"Yoshida, 1992, Molecular genetics of human aldehyde dehydrogenase, Pharmacogenetics, 2, 139, 10.1097\u002F00008571-199208000-00001",{"doi":3885},"10.1097\u002F00008571-199208000-00001",{"id":26,"text":3887,"url":26,"identifiers":3888},"Yoshida, 1992, Retinal oxidation activity and biological role of human cytosolic aldehyde dehydrogenase, Enzyme, 46, 239, 10.1159\u002F000468794",{"doi":3889},"10.1159\u002F000468794",{"id":26,"text":3891,"url":26,"identifiers":3892},"McCaffery, 1999, Dorsal and ventral rentinoic territories defined by retinoic acid synthesis, break-down and nuclear receptor expression, Mech. Dev., 85, 203",{},{"id":26,"text":3894,"url":26,"identifiers":3895},"Chen, 1994, Enzymatic conversion of retinaldehyde to retinoic acid by cloned murine cytosolic and mitochondrial aldehyde dehydrogenases, Mol. Pharmacol., 46, 88",{},{"id":26,"text":3897,"url":26,"identifiers":3898},"Sladek, 1999, Aldehyde dehydrogenase-mediated cellular relative insensitivity to the oxazaphosphorines, Curr. Pharm. Des., 5, 607, 10.2174\u002F1381612805666230110215319",{"doi":3899},"10.2174\u002F1381612805666230110215319",{"id":26,"text":3901,"url":26,"identifiers":3902},"Wroczynski, 2000, Aromatic aldehydes as fluorogenic indicators for human aldehyde dehydrogenases and oxidases: substrate and isozyme specificity, Analyst, 125, 511, 10.1039\u002Fa906962c",{"doi":3903},"10.1039\u002Fa906962c",{"id":26,"text":3905,"url":26,"identifiers":3906},"Pereira, 1991, The 56 kDa androgen binding protein is an aldehyde dehydrogenase, Biochem. Biophys. Res. Commun., 175, 831, 10.1016\u002F0006-291X(91)91640-X",{"doi":3907},"10.1016\u002F0006-291X(91)91640-X",{"id":26,"text":3909,"url":26,"identifiers":3910},"Yamauchi, 1999, Xenopus cytosolic thyroid hormone-binding protein (xCTBP) is aldehyde dehydrogenase catalyzing the formation of retinoic acid, J. Biol. Chem., 274, 8460, 10.1074\u002Fjbc.274.13.8460",{"doi":3911},"10.1074\u002Fjbc.274.13.8460",{"id":26,"text":3913,"url":26,"identifiers":3914},"Schnier, 1999, Identification of cytosolic aldehyde dehydrogenase 1 from non-small cell lung carcinomas as a flavopiridol-binding protein, FEBS Lett., 454, 100, 10.1016\u002FS0014-5793(99)00773-5",{"doi":3915},"10.1016\u002FS0014-5793(99)00773-5",{"id":26,"text":3917,"url":26,"identifiers":3918},"Banfi, 1994, The daunorubicin-binding protein of Mr 54 000 is an aldehyde dehydrogenase and is down-regulated in mouse liver tumors and in tumor cell lines, Mol. Pharmacol., 46, 896",{},{"id":26,"text":3920,"url":26,"identifiers":3921},"Dragani, 1996, Down expression of aldehyde dehydrogenase 1 in murine lung tumors, Mol. Carcinog., 16, 123, 10.1002\u002F(SICI)1098-2744(199607)16:3\u003C123::AID-MC1>3.0.CO;2-I",{"doi":3922},"10.1002\u002F(SICI)1098-2744(199607)16:3\u003C123::AID-MC1>3.0.CO;2-I",{"id":26,"text":3924,"url":26,"identifiers":3925},"Napoli, 1999, Interactions of retinoid binding proteins and enzymes in retinoid metabolism, Biochim. Biophys. Acta, 1440, 139, 10.1016\u002FS1388-1981(99)00117-1",{"doi":3926},"10.1016\u002FS1388-1981(99)00117-1",{"id":26,"text":3928,"url":26,"identifiers":3929},"Zhao, 1996, Molecular identification of a major retinoic-acid-synthesizing enzyme, a retinaldehyde-specific dehydrogenase, Eur. J. Biochem., 240, 15, 10.1111\u002Fj.1432-1033.1996.0015h.x",{"doi":3930},"10.1111\u002Fj.1432-1033.1996.0015h.x",{"id":26,"text":3932,"url":26,"identifiers":3933},"Wang, 1996, Cloning of a cDNA encoding an aldehyde dehydrogenase and its expression in Escherichia coli. Recognition of retinal as substrate, J. Biol. Chem., 271, 16288, 10.1074\u002Fjbc.271.27.16288",{"doi":3934},"10.1074\u002Fjbc.271.27.16288",{"id":26,"text":3936,"url":26,"identifiers":3937},"Ono, 1998, TAL1 and LIM-only proteins synergistically induce retinaldehyde dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia by acting as cofactors for GATA3, Mol. Cell. Biol., 18, 6939, 10.1128\u002FMCB.18.12.6939",{"doi":3938},"10.1128\u002FMCB.18.12.6939",{"id":26,"text":3940,"url":26,"identifiers":3941},"Graham, 1996, A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens. Gene recruitment of eta-crystallin, J. Biol. Chem., 271, 15623, 10.1074\u002Fjbc.271.26.15623",{"doi":3942},"10.1074\u002Fjbc.271.26.15623",{"id":26,"text":3944,"url":26,"identifiers":3945},"Swindell, 1999, Complementary domains of retinoic acid production and degradation in the early chick embryo, Dev. Biol., 216, 282, 10.1006\u002Fdbio.1999.9487",{"doi":3946},"10.1006\u002Fdbio.1999.9487",{"id":26,"text":3948,"url":26,"identifiers":3949},"Penzes, 1997, Cloning of a rat cDNA encoding retinal dehydrogenase isozyme type I and its expression in E. coli, Gene, 191, 167, 10.1016\u002FS0378-1119(97)00054-1",{"doi":3950},"10.1016\u002FS0378-1119(97)00054-1",{"id":26,"text":3952,"url":26,"identifiers":3953},"Niederreither, 1999, Embryonic retinoic acid synthesis is essential for early mouse post-implantation development, Nat. Genet., 21, 444, 10.1038\u002F7788",{"doi":3954},"10.1038\u002F7788",{"id":26,"text":3956,"url":26,"identifiers":3957},"Yoshida, 1998, Human aldehyde dehydrogenase gene family, Eur. J. Biochem., 251, 549, 10.1046\u002Fj.1432-1327.1998.2510549.x",{"doi":3958},"10.1046\u002Fj.1432-1327.1998.2510549.x",{"id":26,"text":3960,"url":26,"identifiers":3961},"Hsu, 1994, Molecular cloning, genomic organization, and chromosomal localization of an additional human aldehyde dehydrogenase gene, ALDH6, Genomics, 24, 333, 10.1006\u002Fgeno.1994.1624",{"doi":3962},"10.1006\u002Fgeno.1994.1624",{"id":26,"text":3964,"url":26,"identifiers":3965},"Li, 2000, A retinoic acid synthesizing enzyme in ventral retina and telencephalon of the embryonic mouse, Mech. Dev., 95, 283, 10.1016\u002FS0925-4773(00)00352-X",{"doi":3966},"10.1016\u002FS0925-4773(00)00352-X",{"id":26,"text":3968,"url":26,"identifiers":3969},"Okamura, 1999, Identification of seven genes regulated by wild-type p53 in a colon cancer cell line carrying a well-controlled wild-type p53 expression system, Oncol. Res., 11, 281",{},{"id":26,"text":3971,"url":26,"identifiers":3972},"Hsu, 1991, Cloning and characterization of a new functional human aldehyde dehydrogenase gene, J. Biol. Chem., 266, 12257, 10.1016\u002FS0021-9258(18)98890-3",{"doi":3973},"10.1016\u002FS0021-9258(18)98890-3",{"id":26,"text":3975,"url":26,"identifiers":3976},"Stewart, 1995, The novel aldehyde dehydrogenase gene, ALDH5, encodes an active aldehyde dehydrogenase enzyme, Biochem. Biophys. Res. Commun., 211, 144, 10.1006\u002Fbbrc.1995.1789",{"doi":3977},"10.1006\u002Fbbrc.1995.1789",{"id":26,"text":3979,"url":26,"identifiers":3980},"Cook, 1991, Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase, J. Biol. Chem., 266, 4965, 10.1016\u002FS0021-9258(19)67743-4",{"doi":3981},"10.1016\u002FS0021-9258(19)67743-4",{"id":26,"text":3983,"url":26,"identifiers":3984},"Krupenko, 1997, Domain structure of rat 10-formyltetrahydrofolate dehydrogenase. Resolution of the amino-terminal domain as 10-formyltetrahydrofolate hydrolase, J. Biol. Chem., 272, 10273, 10.1074\u002Fjbc.272.15.10273",{"doi":3985},"10.1074\u002Fjbc.272.15.10273",{"id":26,"text":3987,"url":26,"identifiers":3988},"Krupenko, 1997, Expression, purification, and properties of the aldehyde dehydrogenase homologous carboxyl-terminal domain of rat 10-formyltetrahydrofolate dehydrogenase, J. Biol. Chem., 272, 10266, 10.1074\u002Fjbc.272.15.10266",{"doi":3989},"10.1074\u002Fjbc.272.15.10266",{"id":26,"text":3991,"url":26,"identifiers":3992},"Krupenko, 1995, Baculovirus expression and purification of rat 10-formyltetrahydrofolate dehydrogenase, Protein Exp. Purif., 6, 457, 10.1006\u002Fprep.1995.1061",{"doi":3993},"10.1006\u002Fprep.1995.1061",{"id":26,"text":3995,"url":26,"identifiers":3996},"Krupenko, 1995, Recombinant 10-formyltetrahydrofolate dehydrogenase catalyses both dehydrogenase and hydrolase reactions utilizing the synthetic substrate 10-formyl-5,8-dideazafolate, Biochem. J., 306, 651, 10.1042\u002Fbj3060651",{"doi":3997},"10.1042\u002Fbj3060651",{"id":26,"text":3999,"url":26,"identifiers":4000},"Krupenko, 1999, Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase, J. Biol. Chem., 274, 35777, 10.1074\u002Fjbc.274.50.35777",{"doi":4001},"10.1074\u002Fjbc.274.50.35777",{"id":26,"text":4003,"url":26,"identifiers":4004},"Tephly, 1991, The toxicity of methanol, Life Sci., 48, 1031, 10.1016\u002F0024-3205(91)90504-5",{"doi":4005},"10.1016\u002F0024-3205(91)90504-5",{"id":26,"text":4007,"url":26,"identifiers":4008},"Champion, 1994, Identification of a heritable deficiency of the folate-dependent enzyme 10-formyltetrahydrofolate dehydrogenase in mice, Proc. Natl. Acad. Sci. USA, 91, 11338, 10.1073\u002Fpnas.91.24.11338",{"doi":4009},"10.1073\u002Fpnas.91.24.11338",{"id":26,"text":4011,"url":26,"identifiers":4012},"Hsu, 1989, Genomic structure of the human cytosolic aldehyde dehydrogenase gene, Genomics, 5, 857, 10.1016\u002F0888-7543(89)90127-4",{"doi":4013},"10.1016\u002F0888-7543(89)90127-4",{"id":26,"text":4015,"url":26,"identifiers":4016},"Farres, 1989, Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences, Eur. J. Biochem., 180, 67, 10.1111\u002Fj.1432-1033.1989.tb14616.x",{"doi":4017},"10.1111\u002Fj.1432-1033.1989.tb14616.x",{"id":26,"text":4019,"url":26,"identifiers":4020},"Chang, 1994, Cloning and characterization of the gene encoding mouse mitochondrial aldehyde dehydrogenase, Gene, 148, 331, 10.1016\u002F0378-1119(94)90708-0",{"doi":4021},"10.1016\u002F0378-1119(94)90708-0",{"id":26,"text":4023,"url":26,"identifiers":4024},"Hjelmqvist, 1997, Class 2 aldehyde dehydrogenase. Characterization of the hamster enzyme, sensitive to daidzin and conserved within the family of multiple forms, FEBS Lett., 416, 99, 10.1016\u002FS0014-5793(97)01176-9",{"doi":4025},"10.1016\u002FS0014-5793(97)01176-9",{"id":26,"text":4027,"url":26,"identifiers":4028},"Johansson, 1988, Mitochondrial aldehyde dehydrogenase from horse liver. Correlations of the same species variants fror both the cytosolic and the mitochondrial forms of an enzyme, Eur. J. Biochem., 172, 527, 10.1111\u002Fj.1432-1033.1988.tb13920.x",{"doi":4029},"10.1111\u002Fj.1432-1033.1988.tb13920.x",{"id":26,"text":4031,"url":26,"identifiers":4032},"Harada, 1985, Aldehyde dehydrogenase polymorphism and alcohol metabolism in alcoholics, Alcohol, 2, 391, 10.1016\u002F0741-8329(85)90100-4",{"doi":4033},"10.1016\u002F0741-8329(85)90100-4",{"id":26,"text":4035,"url":26,"identifiers":4036},"Peng, 1999, Involvement of acetaldehyde for full protection against alcoholism by homozygosity of the variant allele of mitochondrial aldehyde dehydrogenase gene in Asians, Pharmacogenetics, 9, 463",{},{"id":26,"text":4038,"url":26,"identifiers":4039},"Yoshida, 1985, Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases, Alcohol, 2, 103, 10.1016\u002F0741-8329(85)90024-2",{"doi":4040},"10.1016\u002F0741-8329(85)90024-2",{"id":26,"text":4042,"url":26,"identifiers":4043},"Peterson, 1999, Effects of worldwide population subdivision on ALDH2 linkage disequilibrium, Genome Res., 9, 844, 10.1101\u002Fgr.9.9.844",{"doi":4044},"10.1101\u002Fgr.9.9.844",{"id":26,"text":4046,"url":26,"identifiers":4047},"Harada, 1996, Investigation of genetic risk factors associated with alcoholism, Alcohol Clin. Exp. Res., 20, 293A, 10.1111\u002Fj.1530-0277.1996.tb01795.x",{"doi":4048},"10.1111\u002Fj.1530-0277.1996.tb01795.x",{"id":26,"text":4050,"url":26,"identifiers":4051},"Muramatsu, 1996, Association between alcoholism and the dopamine D4 receptor gene, J. Med. Genet., 33, 113, 10.1136\u002Fjmg.33.2.113",{"doi":4052},"10.1136\u002Fjmg.33.2.113",{"id":26,"text":4054,"url":26,"identifiers":4055},"Yokoyama, 1999, Alcohol and aldehyde dehydrogenase gene polymorphisms influence susceptibility to esophageal cancer in Japanese alcoholics, Alcohol Clin. Exp. Res., 23, 1705, 10.1111\u002Fj.1530-0277.1999.tb04064.x",{"doi":4056},"10.1111\u002Fj.1530-0277.1999.tb04064.x",{"id":26,"text":4058,"url":26,"identifiers":4059},"Muto, 2000, Association of aldehyde dehydrogenase 2 gene polymorphism with multiple oesophageal dysplasia in head and neck cancer patients, Gut, 47, 256, 10.1136\u002Fgut.47.2.256",{"doi":4060},"10.1136\u002Fgut.47.2.256",{"id":26,"text":4062,"url":26,"identifiers":4063},"Murata, 1999, Genotype difference of aldehyde dehydrogenase 2 gene in alcohol drinkers influences the incidence of Japanese colorectal cancer patients, Jpn. J. Cancer Res., 90, 711, 10.1111\u002Fj.1349-7006.1999.tb00805.x",{"doi":4064},"10.1111\u002Fj.1349-7006.1999.tb00805.x",{"id":26,"text":4066,"url":26,"identifiers":4067},"Kamino, 2000, Deficiency in mitochondrial aldehyde dehydrogenase increases the risk for late-onset Alzheimer's disease in the Japanese population, Biochem. Biophys. Res. Commun., 273, 192, 10.1006\u002Fbbrc.2000.2923",{"doi":4068},"10.1006\u002Fbbrc.2000.2923",{"id":26,"text":4070,"url":26,"identifiers":4071},"Wong, 1998, Effects on sister chromatid exchange frequency of aldehyde dehydrogenase 2 genotype and smoking in vinyl chloride workers, Mutat. Res., 420, 99, 10.1016\u002FS1383-5718(98)00150-8",{"doi":4072},"10.1016\u002FS1383-5718(98)00150-8",{"id":26,"text":4074,"url":26,"identifiers":4075},"Farres, 1994, Effects of changing glutamate 487 to lysine in rat and human liver mitochondrial aldehyde dehydrogenase. A model to study human (Oriental type) class 2 aldehyde dehydrogenase, J. Biol. Chem., 269, 13854, 10.1016\u002FS0021-9258(17)36725-X",{"doi":4076},"10.1016\u002FS0021-9258(17)36725-X",{"id":26,"text":4078,"url":26,"identifiers":4079},"Spengler, 1988, Formation of interstrand cross-links in chloroacetaldehyde-treated DNA demonstrated by ethidium bromide fluorescence, Cancer Res., 48, 4804",{},{"id":26,"text":4081,"url":26,"identifiers":4082},"Kazmierczak, 1995, Description of a novel fusion transcript between HMGI-C, a gene encoding for a member of the high mobility group proteins, and the mitochondrial aldehyde dehydrogenase gene, Cancer Res., 55, 6038",{},{"id":26,"text":4084,"url":26,"identifiers":4085},"Landin, 1996, Identification of a 54-kDa mitochondrial acetaminophen-binding protein as aldehyde dehydrogenase, Toxicol. Appl. Pharmacol., 141, 299, 10.1016\u002FS0041-008X(96)80036-6",{"doi":4086},"10.1016\u002FS0041-008X(96)80036-6",{"id":26,"text":4088,"url":26,"identifiers":4089},"Lindahl, 1991, Lipid aldehyde oxidation as a physiological role for class 3 aldehyde dehydrogenases, Biochem. Pharmacol., 41, 1583, 10.1016\u002F0006-2952(91)90157-Z",{"doi":4090},"10.1016\u002F0006-2952(91)90157-Z",{"id":26,"text":4092,"url":26,"identifiers":4093},"Marselos, 1988, Substrate preference of a cytosolic aldehyde dehydrogenase inducible in rat liver by treatment with 3-methylcholanthrene, Toxicol. Appl. Pharmacol., 95, 339, 10.1016\u002F0041-008X(88)90170-6",{"doi":4094},"10.1016\u002F0041-008X(88)90170-6",{"id":26,"text":4096,"url":26,"identifiers":4097},"Vasiliou, 1999, Mouse cytosolic class 3 aldehyde dehydrogenase (Aldh3a1): gene structure and regulation of constitutive and dioxin-inducible expression, Pharmacogenetics, 9, 569, 10.1097\u002F00008571-199910000-00004",{"doi":4098},"10.1097\u002F00008571-199910000-00004",{"id":26,"text":4100,"url":26,"identifiers":4101},"Vasiliou, 1993, Mouse dioxin-inducible cytosolic aldehyde dehydrogenase-3: AHD4 cDNA sequence, genetic mapping, and differences in mRNA levels, Pharmacogenetics, 3, 281, 10.1097\u002F00008571-199312000-00002",{"doi":4102},"10.1097\u002F00008571-199312000-00002",{"id":26,"text":4104,"url":26,"identifiers":4105},"Asman, 1993, Organization and characterization of the rat class 3 aldehyde dehydrogenase gene, J. Biol. Chem., 268, 12530, 10.1016\u002FS0021-9258(18)31421-2",{"doi":4106},"10.1016\u002FS0021-9258(18)31421-2",{"id":26,"text":4108,"url":26,"identifiers":4109},"Hempel, 1989, Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol\u002Fmitochondria, Biochemistry, 28, 1160, 10.1021\u002Fbi00429a034",{"doi":4110},"10.1021\u002Fbi00429a034",{"id":26,"text":4112,"url":26,"identifiers":4113},"Cooper, 1991, Degenerate oligonucleotide sequence-directed cross-species PCR cloning of the BCP 54\u002FALDH 3 cDNA: priming from inverted repeats and formation of tandem primer arrays, PCR Methods Appl., 1, 57, 10.1101\u002Fgr.1.1.57",{"doi":4114},"10.1101\u002Fgr.1.1.57",{"id":26,"text":4116,"url":26,"identifiers":4117},"Hsu, 1992, Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli, J. Biol. Chem., 267, 3030, 10.1016\u002FS0021-9258(19)50690-1",{"doi":4118},"10.1016\u002FS0021-9258(19)50690-1",{"id":26,"text":4120,"url":26,"identifiers":4121},"Boesch, 1996, Constitutive expression of class 3 aldehyde dehydrogenase in cultured rat corneal epithelium, J. Biol. Chem., 271, 5150, 10.1074\u002Fjbc.271.9.5150",{"doi":4122},"10.1074\u002Fjbc.271.9.5150",{"id":26,"text":4124,"url":26,"identifiers":4125},"Vasiliou, 1989, Tissue distribution of inducible aldehyde dehydrogenase activity in the rat after treatment with phenobarbital or methylcholanthrene, Pharmacol. Toxicol., 64, 39, 10.1111\u002Fj.1600-0773.1989.tb00597.x",{"doi":4126},"10.1111\u002Fj.1600-0773.1989.tb00597.x",{"id":26,"text":4128,"url":26,"identifiers":4129},"Piatigorsky, 1998, Multifunctional lens crystallins and corneal enzymes. More than meets the eye, Ann. New York Acad. Sci., 842, 7, 10.1111\u002Fj.1749-6632.1998.tb09626.x",{"doi":4130},"10.1111\u002Fj.1749-6632.1998.tb09626.x",{"id":26,"text":4132,"url":26,"identifiers":4133},"Kays, 1997, Aldehyde dehydrogenase class 3 expression: identification of a cornea-preferred gene promoter in transgenic mice, Proc. Natl. Acad. Sci. USA, 94, 13594, 10.1073\u002Fpnas.94.25.13594",{"doi":4134},"10.1073\u002Fpnas.94.25.13594",{"id":26,"text":4136,"url":26,"identifiers":4137},"Vasiliou, 1999, The lack of AHD4 induction by TCDD in corneal cells may involve tissue-specific regulatory proteins, Adv. Exp. Med. Biol., 463, 181, 10.1007\u002F978-1-4615-4735-8_22",{"doi":4138},"10.1007\u002F978-1-4615-4735-8_22",{"id":26,"text":4140,"url":26,"identifiers":4141},"Uma, 1996, Effect of UVB radiation on corneal aldehyde dehydrogenase, Curr. Eye Res., 15, 685, 10.3109\u002F02713689609008910",{"doi":4142},"10.3109\u002F02713689609008910",{"id":26,"text":4144,"url":26,"identifiers":4145},"Abedinia, 1990, Bovine corneal aldehyde dehydrogenase: the major soluble corneal protein with a possible dual protective role for the eye, Exp. Eye Res., 51, 419, 10.1016\u002F0014-4835(90)90154-M",{"doi":4146},"10.1016\u002F0014-4835(90)90154-M",{"id":26,"text":4148,"url":26,"identifiers":4149},"Ruben, 1991, Isolation of a rel-related human cDNA that potentially encodes the 65-kDa subunit of NF-κ B, Science, 251, 1490, 10.1126\u002Fscience.2006423",{"doi":4150},"10.1126\u002Fscience.2006423",{"id":26,"text":4152,"url":26,"identifiers":4153},"Atherton, 1999, Fluorescence studies of lens epithelial cells and their constituents, Photochem. Photobiol., 70, 823, 10.1111\u002Fj.1751-1097.1999.tb08289.x",{"doi":4154},"10.1111\u002Fj.1751-1097.1999.tb08289.x",{"id":26,"text":4156,"url":26,"identifiers":4157},"King, 1993, Human corneal aldehyde dehydrogenase: purification, kinetic characterisation and phenotypic variation, Biochem. Mol. Biol. Int., 31, 49",{},{"id":26,"text":4159,"url":26,"identifiers":4160},"Marks-Hull, 1997, Expression of ALDH3 and NMO1 in human corneal epithelial and breast adenocarcinoma cells, Adv. Exp. Med. Biol., 414, 59, 10.1007\u002F978-1-4615-5871-2_8",{"doi":4161},"10.1007\u002F978-1-4615-5871-2_8",{"id":26,"text":4163,"url":26,"identifiers":4164},"A. Pappa, N.A. Sophos, V. Vasiliou, Corneal and stomach expression of aldehyde dhydrogenases: from fish to mammals. Chem. Biol. Interact. (2000), in press.",{"doi":4165},"10.1016\u002FS0009-2797(00)00233-7",{"id":26,"text":4167,"url":26,"identifiers":4168},"Shiao, 1999, Four amino acid changes are associated with the Aldh3a1 locus polymorphism in mice which may be responsible for corneal sensitivity to ultraviolet light, Pharmacogenetics, 9, 145",{},{"id":26,"text":4170,"url":26,"identifiers":4171},"Downes, 1997, A genetic basis for corneal sensitivity to ultraviolet light among recombinant SWXJ inbred strains of mice, Curr. Eye Res., 16, 539, 10.1076\u002Fceyr.16.6.539.5075",{"doi":4172},"10.1076\u002Fceyr.16.6.539.5075",{"id":26,"text":4174,"url":26,"identifiers":4175},"Xie, 1996, Characterization of the rat Class 3 aldehyde dehydrogenase gene promoter, Nucleic Acids Res., 24, 4185, 10.1093\u002Fnar\u002F24.21.4185",{"doi":4176},"10.1093\u002Fnar\u002F24.21.4185",{"id":26,"text":4178,"url":26,"identifiers":4179},"Hsu, 1996, The human aldehyde dehydrogenase 3 gene (ALDH3): identification of a new exon and diverse mRNA isoforms, and functional analysis of the promoter, Gene Exp., 6, 87",{},{"id":26,"text":4181,"url":26,"identifiers":4182},"Marselos, 1987, Changes in the pattern of aldehyde dehydrogenase activity in primary and metastatic adenocarcinomas of the human colon, Cancer Lett., 34, 27, 10.1016\u002F0304-3835(87)90070-X",{"doi":4183},"10.1016\u002F0304-3835(87)90070-X",{"id":26,"text":4185,"url":26,"identifiers":4186},"Shibuya, 1994, Immunohistochemical study of hepatocellular carcinoma-specific aldehyde dehydrogenase, Alcohol Alcohol, 29, 119",{},{"id":26,"text":4188,"url":26,"identifiers":4189},"Vasiliou, 1995, Response of [Ah] battery genes to compounds that protect against menadione toxicity, Biochem. Pharmacol., 50, 1885, 10.1016\u002F0006-2952(95)02083-7",{"doi":4190},"10.1016\u002F0006-2952(95)02083-7",{"id":26,"text":4192,"url":26,"identifiers":4193},"Liu, 1994, Regulation of [Ah] gene battery enzymes and glutathione levels by 5,10-dihydroindeno[1,2-b]indole in mouse hepatoma cell lines, Carcinogenesis, 15, 2347, 10.1093\u002Fcarcin\u002F15.10.2347",{"doi":4194},"10.1093\u002Fcarcin\u002F15.10.2347",{"id":26,"text":4196,"url":26,"identifiers":4197},"Sreerama, 1993, Overexpression or polycyclic aromatic hydrocarbon-mediated induction of an apparently novel class 3 aldehyde dehydrogenase in human breast adenocarcinoma cells and its relationship to oxazaphosphorine-specific acquired resistance, Adv. Exp. Med. Biol., 328, 99, 10.1007\u002F978-1-4615-2904-0_12",{"doi":4198},"10.1007\u002F978-1-4615-2904-0_12",{"id":26,"text":4200,"url":26,"identifiers":4201},"Rizzo, 1998, Inherited disorders of fatty alcohol metabolism, Mol. Genet. Metab., 65, 63, 10.1006\u002Fmgme.1998.2728",{"doi":4202},"10.1006\u002Fmgme.1998.2728",{"id":26,"text":4204,"url":26,"identifiers":4205},"Vasiliou, 1996, Mouse microsomal Class 3 aldehyde dehydrogenase: AHD3 cDNA sequence, inducibility by dioxin and clofibrate, and genetic mapping, DNA Cell Biol., 15, 235, 10.1089\u002Fdna.1996.15.235",{"doi":4206},"10.1089\u002Fdna.1996.15.235",{"id":26,"text":4208,"url":26,"identifiers":4209},"Miyauchi, 1991, Molecular cloning, sequencing, and expression of cDNA for rat liver microsomal aldehyde dehydrogenase, J. Biol. Chem., 266, 19536, 10.1016\u002FS0021-9258(18)55028-6",{"doi":4210},"10.1016\u002FS0021-9258(18)55028-6",{"id":26,"text":4212,"url":26,"identifiers":4213},"Rogers, 1997, Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH), Genomics, 39, 127, 10.1006\u002Fgeno.1996.4501",{"doi":4214},"10.1006\u002Fgeno.1996.4501",{"id":26,"text":4216,"url":26,"identifiers":4217},"De, 1996, Sjogren–Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene, Nat. Genet., 12, 52, 10.1038\u002Fng0196-52",{"doi":4218},"10.1038\u002Fng0196-52",{"id":26,"text":4220,"url":26,"identifiers":4221},"Masaki, 1996, Membrane topology and retention of microsomal aldehyde dehydrogenase in the endoplasmic reticulum, J. Biol. Chem., 271, 16939, 10.1074\u002Fjbc.271.28.16939",{"doi":4222},"10.1074\u002Fjbc.271.28.16939",{"id":26,"text":4224,"url":26,"identifiers":4225},"Masaki, 1994, Microsomal aldehyde dehydrogenase is localized to the endoplasmic reticulum via its carboxyl-terminal 35 amino acids, J. Cell Biol., 126, 1407, 10.1083\u002Fjcb.126.6.1407",{"doi":4226},"10.1083\u002Fjcb.126.6.1407",{"id":26,"text":4228,"url":26,"identifiers":4229},"Kelson, 1997, Human liver fatty aldehyde dehydrogenase: microsomal localization, purification, and biochemical characterization, Biochim. Biophys. Acta, 1335, 99, 10.1016\u002FS0304-4165(96)00126-2",{"doi":4230},"10.1016\u002FS0304-4165(96)00126-2",{"id":26,"text":4232,"url":26,"identifiers":4233},"Rizzo, 1999, The molecular basis of Sjogren–Larsson syndrome: mutation analysis of the fatty aldehyde dehydrogenase gene, Am. J. Hum. Genet., 65, 1547, 10.1086\u002F302681",{"doi":4234},"10.1086\u002F302681",{"id":26,"text":4236,"url":26,"identifiers":4237},"Hsu, 1994, Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde dehydrogenase family, Gene, 151, 285, 10.1016\u002F0378-1119(94)90672-6",{"doi":4238},"10.1016\u002F0378-1119(94)90672-6",{"id":26,"text":4240,"url":26,"identifiers":4241},"Hsu, 1997, Human aldehyde dehydrogenase genes, ALDH7 and ALDH8: genomic organization and gene structure comparison, Gene, 189, 89, 10.1016\u002FS0378-1119(96)00839-6",{"doi":4242},"10.1016\u002FS0378-1119(96)00839-6",{"id":26,"text":4244,"url":26,"identifiers":4245},"Forte-McRobbie, 1986, Purification and characterization of human liver ‘high Km’ aldehyde dehydrogenase and its identification as glutamic γ-semialdehyde dehydrogenase, J. Biol. Chem., 261, 2154, 10.1016\u002FS0021-9258(17)35911-2",{"doi":4246},"10.1016\u002FS0021-9258(17)35911-2",{"id":26,"text":4248,"url":26,"identifiers":4249},"Hu, 1996, Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase, J. Biol. Chem., 271, 9795, 10.1074\u002Fjbc.271.16.9795",{"doi":4250},"10.1074\u002Fjbc.271.16.9795",{"id":26,"text":4252,"url":26,"identifiers":4253},"Geraghty, 1998, Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia, Hum. Mol. Genet., 7, 1411, 10.1093\u002Fhmg\u002F7.9.1411",{"doi":4254},"10.1093\u002Fhmg\u002F7.9.1411",{"id":26,"text":4256,"url":26,"identifiers":4257},"Cohen, 1997, Proline-induced inhibition of glutamate release in hippocampal area CA1, Brain Res., 769, 333, 10.1016\u002FS0006-8993(97)00721-X",{"doi":4258},"10.1016\u002FS0006-8993(97)00721-X",{"id":26,"text":4260,"url":26,"identifiers":4261},"Cohen, 1997, Proline-induced potentiation of glutamate transmission, Brain Res., 761, 271, 10.1016\u002FS0006-8993(97)00352-1",{"doi":4262},"10.1016\u002FS0006-8993(97)00352-1",{"id":26,"text":4264,"url":26,"identifiers":4265},"Miltyk, 2000, Potential role of pyrroline 5-carboxylate in regulation of collagen biosynthesis in cultured human skin fibroblasts, Comp. Biochem. Physiol. A Mol. Integr. Physiol., 125, 265, 10.1016\u002FS1095-6433(99)00181-6",{"doi":4266},"10.1016\u002FS1095-6433(99)00181-6",{"id":26,"text":4268,"url":26,"identifiers":4269},"Yeh, 1984, The effect of pyrroline-5-carboxylic acid on nucleotide metabolism in erythrocytes from normal and glucose-6-phosphate dehydrogenase-deficient subjects, J. Biol. Chem., 259, 5454, 10.1016\u002FS0021-9258(18)91032-X",{"doi":4270},"10.1016\u002FS0021-9258(18)91032-X",{"id":26,"text":4272,"url":26,"identifiers":4273},"Chambliss, 1995, Enzymatic and immunologic identification of succinic semialdehyde dehydrogenase in rat and human neural and nonneural tissues, J. Neurochem., 65, 851, 10.1046\u002Fj.1471-4159.1995.65020851.x",{"doi":4274},"10.1046\u002Fj.1471-4159.1995.65020851.x",{"id":26,"text":4276,"url":26,"identifiers":4277},"Gibson, 1998, 4-Hydroxybutyric acid and the clinical phenotype of succinic semialdehyde dehydrogenase deficiency, an inborn error of GABA metabolism, Neuropediatrics, 29, 14, 10.1055\u002Fs-2007-973527",{"doi":4278},"10.1055\u002Fs-2007-973527",{"id":26,"text":4280,"url":26,"identifiers":4281},"Kedishvili, 1992, CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution, J. Biol. Chem., 267, 19724, 10.1016\u002FS0021-9258(18)41835-2",{"doi":4282},"10.1016\u002FS0021-9258(18)41835-2",{"id":26,"text":4284,"url":26,"identifiers":4285},"Chambliss, 2000, Molecular characterization of methylmalonate semialdehyde dehydrogenase deficiency, J. Inherit. Metab. Dis., 23, 497, 10.1023\u002FA:1005616315087",{"doi":4286},"10.1023\u002FA:1005616315087",{"id":26,"text":4288,"url":26,"identifiers":4289},"Roe, 1998, Methylmalonic semialdehyde dehydrogenase deficiency: psychomotor delay and methylmalonic aciduria without metabolic decompensation, Mol. Genet. Metab., 65, 35, 10.1006\u002Fmgme.1998.2737",{"doi":4290},"10.1006\u002Fmgme.1998.2737",{"id":26,"text":4292,"url":26,"identifiers":4293},"Lee, 1994, Homology between a human protein and a protein of the green garden pea, Genomics, 21, 371, 10.1006\u002Fgeno.1994.1279",{"doi":4294},"10.1006\u002Fgeno.1994.1279",{"id":26,"text":4296,"url":26,"identifiers":4297},"Skvorak, 1997, An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1), Genomics, 46, 191, 10.1006\u002Fgeno.1997.5026",{"doi":4298},"10.1006\u002Fgeno.1997.5026",{"id":26,"text":4300,"url":26,"identifiers":4301},"Vaz, 2000, Molecular and biochemical characterization of rat γ-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis, J. Biol. Chem., 275, 7390, 10.1074\u002Fjbc.275.10.7390",{"doi":4302},"10.1074\u002Fjbc.275.10.7390",{"id":26,"text":4304,"url":26,"identifiers":4305},"Izaguirre, 1997, Tissue distribution of human aldehyde dehydrogenase E3 (ALDH9): comparison of enzyme activity with E3 protein and mRNA distribution, Comp. Biochem. Physiol. B Biochem. Mol. Biol., 118, 59, 10.1016\u002FS0305-0491(97)00022-9",{"doi":4306},"10.1016\u002FS0305-0491(97)00022-9",{"id":4308,"createTime":4309,"updateTime":4310,"relativeEntities":4311,"slug":4312,"properties":4313,"entityType":781,"verifyStatus":25,"verifyTime":4322,"verifyNote":783,"syncStatus":28,"languages":26,"translateLanguages":26,"viewCount":36,"primaryUrl":4323,"fullTextUrl":26,"authors":4324,"publicationType":837,"publisherRelationship":4352,"citationCount":4387,"citationInfo":4388,"publishDate":3765,"publishYear":3766,"citationAnalyzeStatus":4390,"lastCitationAnalyze":4391,"indexDatabases":26,"openAccess":26,"references":26,"isForceReanalyzing":1904},"eefdce29-6d27-49dd-80fb-ef2b54f79e9a","2024-02-06T14:05:00.947+00:00","2026-06-17T04:18:53.144+00:00",[],"Carbonyl-reductase",{"references":4314,"title":4316,"doi":4318,"gsPaper":4320},{"VOID":4315},"Wermuth, 1992, Prostaglandins, 44, 5, 10.1016\u002F0090-6980(92)90102-Y\nKrook, 1993, FEBS Lett., 322, 139, 10.1016\u002F0014-5793(93)81554-D\nWermuth, 1985, Prog. Clin. Biol. Res., 174, 209\nFelsted, 1980, 1\nBaker, 1994, Biochem. J., 300, 605, 10.1042\u002Fbj3000605b\nZelinski, 1994, J. Biotechnol., 33, 283, 10.1016\u002F0168-1656(94)90076-0\nOppermann, 1998, Chem. Biol. Interact., 114, 211, 10.1016\u002FS0009-2797(98)00057-X\nOppermann, 1996, Eur. J. Biochem., 241, 744, 10.1111\u002Fj.1432-1033.1996.00744.x\nWada, 1998, Biosci. Biotechnol. Biochem., 62, 280, 10.1271\u002Fbbb.62.280\nPeters, 1993, Enzyme Microb. Technol., 15, 950, 10.1016\u002F0141-0229(93)90171-W\nGuan, 1999, Biochem. Biophys. Res. Commun., 255, 123, 10.1006\u002Fbbrc.1998.0127\nIwata, 1993, Biochem. Pharmacol., 45, 1711, 10.1016\u002F0006-2952(93)90313-L\nAhmed, 1978, Biochem. Pharmacol., 27, 2713, 10.1016\u002F0006-2952(78)90047-3\nFelsted, 1982, 291\nIwata, 1990, J. Biochem., 107, 209, 10.1093\u002Foxfordjournals.jbchem.a123027\nWermuth, 1981, J. Biol. Chem., 256, 1206, 10.1016\u002FS0021-9258(19)69950-3\nSawada, 1979, Biochem. Pharmacol., 28, 1089, 10.1016\u002F0006-2952(79)90310-1\nImamura, 1993, Arch. Biochem. Biophys., 300, 570, 10.1006\u002Fabbi.1993.1079\nAhmed, 1979, J. Pharmacol. Exp. Ther., 209, 12\nFelsted, 1980, 1\nHara, 1987, 401\nNakayama, 1986, Biochim. Biophys. Acta, 882, 220, 10.1016\u002F0304-4165(86)90158-3\nSawada, 1979, J. Biochem. (Tokyo), 86, 871, 10.1093\u002Foxfordjournals.jbchem.a132619\nLee, 1974, J. Biol. Chem., 249, 1369, 10.1016\u002FS0021-9258(19)42891-3\nLee, 1974, Biochem. Biophys. Res. Commun., 61, 14, 10.1016\u002F0006-291X(74)90527-0\nCagen, 1979, Biochim. Biophys. Acta, 573, 547, 10.1016\u002F0005-2760(79)90228-5\nTanaka, 1992, J. Biol. Chem., 267, 13451, 10.1016\u002FS0021-9258(18)42232-6\nHara, 1986, Arch. Biochem. Biophys., 244, 238, 10.1016\u002F0003-9861(86)90113-X\nMolowa, 1986, Arch. Biochem. Biophys., 251, 487, 10.1016\u002F0003-9861(86)90356-5\nNakayama, 1985, Biochem. Pharmacol., 34, 107, 10.1016\u002F0006-2952(85)90108-X\nWermuth, 1986, Biochem. Pharmacol., 35, 1277, 10.1016\u002F0006-2952(86)90271-6\nOhara, 1995, Biochem. Pharmacol., 50, 221, 10.1016\u002F0006-2952(95)00124-I\nMaser, 1995, Adv. Exp. Med. Biol., 372, 211, 10.1007\u002F978-1-4615-1965-2_27\nMaser, 1994, J. Steroid Biochem. Mol. Biol., 48, 257, 10.1016\u002F0960-0760(94)90153-8\nGonzales, 1995, Gene, 154, 297, 10.1016\u002F0378-1119(94)00843-H\nNakanishi, 1995, Eur. J. Biochem., 228, 381, 10.1111\u002Fj.1432-1033.1995.tb20274.x\nMatsuura, 1988, Biochem. J., 252, 17, 10.1042\u002Fbj2520017\nHara, 1992, Arch. Biochem. Biophys., 292, 548, 10.1016\u002F0003-9861(92)90029-V\nMatsuura, 1990, J. Histochem. Cytochem., 38, 217, 10.1177\u002F38.2.1688897\nMoxon, 1987, Prog. Clin. Biol. Res., 232, 383\nNakanishi, 1993, Biochem. Biophys. Res. Commun., 194, 1311, 10.1006\u002Fbbrc.1993.1967\nNakayama, 1988, Arch. Biochem. Biophys., 264, 492, 10.1016\u002F0003-9861(88)90314-1\nOritani, 1992, Arch. Biochem. Biophys., 292, 539, 10.1016\u002F0003-9861(92)90028-U\nImamura, 1999, Biol. Pharm. Bull., 22, 731, 10.1248\u002Fbpb.22.731\nImamura, 1999, J. Biochem. (Tokyo), 125, 41, 10.1093\u002Foxfordjournals.jbchem.a022266\nHiguchi, 1993, Biochim. Biophys. Acta, 1158, 23, 10.1016\u002F0304-4165(93)90091-L\nHara, 1982, J. Biochem. (Tokyo), 92, 1753, 10.1093\u002Foxfordjournals.jbchem.a134105\nSchieber, 1992, Eur. J. Biochem., 206, 491, 10.1111\u002Fj.1432-1033.1992.tb16952.x\nCromlish, 1985, J. Neurochem., 44, 1477, 10.1111\u002Fj.1471-4159.1985.tb08785.x\nIwata, 1990, Eur. J. Biochem., 193, 75, 10.1111\u002Fj.1432-1033.1990.tb19306.x\nAoki, 1997, Biochem. Biophys. Res. Commun., 230, 518, 10.1006\u002Fbbrc.1996.5995\nInazu, 1992, Biochim. Biophys. Acta, 1116, 50, 10.1016\u002F0304-4165(92)90127-G\nWermuth, 1995, Eur. J. Biochem., 228, 473, 10.1111\u002Fj.1432-1033.1995.tb20286.x\nIwata, 1989, J. Biochem. Tokyo, 105, 556, 10.1093\u002Foxfordjournals.jbchem.a122704\nToft, 1994, Biochem. Biophys. Res. Commun., 201, 149, 10.1006\u002Fbbrc.1994.1681\nWintergalen, 1995, Eur. J. Biochem., 234, 264, 10.1111\u002Fj.1432-1033.1995.264_c.x\nOppermann, 1991, Biochem. Pharmacol., 42, S189, 10.1016\u002F0006-2952(91)90409-X\nInazu, 1994, J. Biochem. (Tokyo), 115, 991, 10.1093\u002Foxfordjournals.jbchem.a124450\nMaser, 1992, Toxicology, 74, 45, 10.1016\u002F0300-483X(92)90042-D\nBachur, 1976, Science, 193, 595, 10.1126\u002Fscience.959821\nAhmed, 1981, Xenobiotica, 11, 131, 10.3109\u002F00498258109045283\nJarabak, 1993, Arch. Biochem. Biophys., 303, 394, 10.1006\u002Fabbi.1993.1300\nNakanishi, 1995, Biol. Pharm. Bull., 18, 1248, 10.1248\u002Fbpb.18.1248\nChung, 1987, Prostaglandins, 33, 383, 10.1016\u002F0090-6980(87)90020-7\nNakayama, 1982, Arch. Biochem. Biophys., 217, 564, 10.1016\u002F0003-9861(82)90538-0\nRis, 1973, Eur. J. Biochem., 37, 69, 10.1111\u002Fj.1432-1033.1973.tb02958.x\nWermuth, 1988, J. Biol. Chem., 263, 16185, 10.1016\u002FS0021-9258(18)37576-8\nJornvall, 1995, Biochemistry, 34, 6003, 10.1021\u002Fbi00018a001\nKrook, 1993, Proc. Natl. Acad. Sci. USA, 90, 502, 10.1073\u002Fpnas.90.2.502\nTanaka, 1996, Biochemistry, 35, 7715, 10.1021\u002Fbi951904d\nTanaka, 1995, J. Biochem. (Tokyo), 118, 871, 10.1093\u002Fjb\u002F118.5.871\nJez, 1997, Biochem. J., 326, 625, 10.1042\u002Fbj3260625\nWermuth, 1982, Prog. Clin. Biol. Res., 114, 261\nEspey, 2000, Biol. Reprod., 62, 390, 10.1095\u002Fbiolreprod62.2.390\nMaser, 1996, Eur. J. Biochem., 238, 484, 10.1111\u002Fj.1432-1033.1996.0484z.x\nMaser, 1994, Biochem. Pharmacol., 47, 1805, 10.1016\u002F0006-2952(94)90309-3\nMaser, 1999, Adv. Exp. Med. Biol., 463, 379, 10.1007\u002F978-1-4615-4735-8_47\nImamura, 1996, J. Biochem. Tokyo, 119, 648, 10.1093\u002Foxfordjournals.jbchem.a021291\nPark, 1991, Biochem. Biophys. Res. Commun., 175, 738, 10.1016\u002F0006-291X(91)91628-P\nIino, 2000, Arch. Biochem. Biophys., 373, 442, 10.1006\u002Fabbi.1999.1561\nIwata, 1989, Prog. Clin. Biol. Res., 290, 307\nWirth, 1985, FEBS Lett., 187, 280, 10.1016\u002F0014-5793(85)81259-X\nWirth, 1992, J. Histochem. Cytochem., 40, 1857, 10.1177\u002F40.12.1453004\nForrest, 1990, Biochim. Biophys. Acta., 1048, 149, 10.1016\u002F0167-4781(90)90050-C\nBohren, 1994, J. Mol. Biol., 244, 659, 10.1006\u002Fjmbi.1994.1762\nForrest, 1991, Mol. Pharmacol., 40, 502\nChung, 1987, Prostaglandins, 33, 391, 10.1016\u002F0090-6980(87)90021-9\nWermuth, 1993, FEBS Lett., 335, 151, 10.1016\u002F0014-5793(93)80719-B\nLemieux, 1993, Genomics, 15, 169, 10.1006\u002Fgeno.1993.1024\nAvramopoulos, 1992, Genomics, 13, 447, 10.1016\u002F0888-7543(92)90268-W\nWatanabe, 1998, Genomics, 52, 95, 10.1006\u002Fgeno.1998.5380\nDaumer-Haas, 1994, Am. J. Med. Genet., 53, 359, 10.1002\u002Fajmg.1320530411\nEpstein, 1991, Am. J. Hum. Genet., 49, 207\nKorenberg, 1994, Proc. Natl. Acad. Sci. USA, 91, 4997, 10.1073\u002Fpnas.91.11.4997\nHassold, 1984, Annu. Rev. Genet., 18, 69, 10.1146\u002Fannurev.ge.18.120184.000441\nMjaatvedt, 1993, Genomics, 17, 382, 10.1006\u002Fgeno.1993.1336\nWei, 1996, Genomics, 34, 147, 10.1006\u002Fgeno.1996.0255\nMalkinson, 1992, Cancer Res., 52, 4752\nBohren, 1989, J. Biol. Chem., 264, 9547, 10.1016\u002FS0021-9258(18)60566-6\nSchlager, 1990, Int. J. Cancer, 45, 403, 10.1002\u002Fijc.2910450304\nLopez de Cerain, 1999, Eur. J. Cancer., 35, 320, 10.1016\u002FS0959-8049(98)00372-4\nSuto, 1999, J. Cancer Res. Clin. Oncol., 125, 83, 10.1007\u002Fs004320050246\nKajihara-Kano, 1997, Biochem. J., 328, 473, 10.1042\u002Fbj3280473\nIsmail, 2000, Cancer Res., 60, 1173\nFulton, 1991, Cancer Res., 51, 2047\nAblin, 1986, Anticancer Res., 6, 327\nYoung, 1991, Invasion Metastasis, 11, 48\nErnster, 1986, Chemica Scripta, 27A, 1\nChesis, 1984, Proc. Natl. Acad. Sci. USA, 81, 1696, 10.1073\u002Fpnas.81.6.1696\nWefers, 1983, Arch. Biochem. Biophys., 224, 568, 10.1016\u002F0003-9861(83)90244-8\nChung, 1987, J. Biol. Chem., 262, 12448, 10.1016\u002FS0021-9258(18)45225-8\nJarabak, 1991, Arch. Biochem. Biophys., 291, 334, 10.1016\u002F0003-9861(91)90143-7\nKelner, 1997, Life Sci., 61, 2317, 10.1016\u002FS0024-3205(97)00935-1\nBus, 1984, Environ. Health Perspect., 55, 37, 10.1289\u002Fehp.845537\nAmes, 1975, Mutation Res., 31, 347, 10.1016\u002F0165-1161(75)90046-1\nGonzalez, 1995, Cancer Res., 55, 4646\nFelsted, 1974, J. Biol. Chem., 249, 3672, 10.1016\u002FS0021-9258(19)42527-1\nSchott, 1989, Biochem. Pharmacol., 38, 4069, 10.1016\u002F0006-2952(89)90688-6\nKuffel, 1992, Cancer Chemother. Pharmacol., 30, 51, 10.1007\u002FBF00686485\nKuffel, 1995, Cancer Chemother. Pharmacol., 36, 223, 10.1007\u002FBF00685850\nAhmed, 1985, Eur. J. Cancer Clin. Oncol., 21, 1209, 10.1016\u002F0277-5379(85)90017-3\nBachur, 1976, J. Med. Chem., 19, 651, 10.1021\u002Fjm00227a015\nAx, 2000, Biochem. 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Curr. Biotechnol., 3, 1",{},{"id":26,"text":4595,"url":26,"identifiers":4596},"Kim, 2010, Nanomedicine, N. Engl. J. Med., 363, 2434, 10.1056\u002FNEJMra0912273",{"doi":4597},"10.1056\u002FNEJMra0912273",{"id":26,"text":4599,"url":26,"identifiers":4600},"Akhtar, 2015, Biosynthesis and characterization of silver nanoparticles from methanol leaf extract of Cassia didymobotyra and assessment of their antioxidant and antibacterial activities, Nanosci. Nanotechnol., 15, 1",{},{"id":26,"text":4602,"url":26,"identifiers":4603},"Rudramurthy, 2016, Nanoparticles : alternatives against drug-resistant, Molecules, 21, 1, 10.3390\u002Fmolecules21070836",{"doi":4604},"10.3390\u002Fmolecules21070836",{"id":26,"text":4606,"url":26,"identifiers":4607},"Lee, 2011, Antibacterial activity of silver-nanoparticles against Staphylococcus aureus and Escherichia coli, Kor. J. Microbiol. Biotechnol., 39, 77",{},{"id":26,"text":4609,"url":26,"identifiers":4610},"Mohamed, 2017, Antibacterial effect of gold nanoparticles against Corynebacterium pseudotuberculosis, Int. J. Vet. Sci. Med, 5, 23, 10.1016\u002Fj.ijvsm.2017.02.003",{"doi":4611},"10.1016\u002Fj.ijvsm.2017.02.003",{"id":26,"text":4613,"url":26,"identifiers":4614},"Guajardo-pacheco, 2017, Antimicrobial properties of copper nanoparticles and amino acid chelated copper nanoparticles produced by using a soya extract, Bioinorgan. Chem. Appl., 2017, 15",{},{"id":26,"text":4616,"url":26,"identifiers":4617},"Naseem, 2015, Antibacterial activity of Green synthesis of iron nanoparticles using lawsonia inermis and gardenia jasminoides leaves extract, J. Chem., 1, 10.1155\u002F2015\u002F912342",{"doi":4618},"10.1155\u002F2015\u002F912342",{"id":26,"text":4620,"url":26,"identifiers":4621},"Jesline, 2015, Antimicrobial activity of zinc and titanium dioxide nanoparticles against biofilm-producing methicillin-resistant Staphylococcus aureus, Appl. Nanosci., 5, 157, 10.1007\u002Fs13204-014-0301-x",{"doi":4622},"10.1007\u002Fs13204-014-0301-x",{"id":26,"text":4624,"url":26,"identifiers":4625},"Ren, 2009, Characterisation of copper oxide nanoparticles for antimicrobial applications, Int. J. Antimicrob. Agents, 33, 587, 10.1016\u002Fj.ijantimicag.2008.12.004",{"doi":4626},"10.1016\u002Fj.ijantimicag.2008.12.004",{"id":26,"text":4628,"url":26,"identifiers":4629},"Ismail, 2015, Antibacterial activity of magnetic iron oxide nanoparticles synthesised by laser ablation in liquid, Mater. Sci. Eng. C, 10.1016\u002Fj.msec.2015.04.047",{"doi":4630},"10.1016\u002Fj.msec.2015.04.047",{"id":26,"text":4632,"url":26,"identifiers":4633},"Reddy, 2014, Antimicrobial activity of zinc oxide ( ZnO ) nanoparticle against Klebsiella pneumoniae, Pharm. Biol., 1",{},{"id":26,"text":4635,"url":26,"identifiers":4636},"Huang, 2010, Toxicity of transition metal oxide nanoparticles: recent insights from in vitro studies, Materials, 3, 4842, 10.3390\u002Fma3104842",{"doi":4637},"10.3390\u002Fma3104842",{"id":26,"text":4639,"url":26,"identifiers":4640},"Wang, 2017, Fabrication of antibacterial casein-based ZnO nanocomposite for fl exible coatings, Mater. Des., 113, 240, 10.1016\u002Fj.matdes.2016.09.082",{"doi":4641},"10.1016\u002Fj.matdes.2016.09.082",{"id":26,"text":4643,"url":26,"identifiers":4644},"Murali, 2017, Antibacterial and antioxidant properties of biosynthesized zinc oxide nanoparticles from Ceropegia candelabrum L. – an endemic species, Spectrochim. Acta Part A Mol. Biomol. Spectrosc, 179, 104, 10.1016\u002Fj.saa.2017.02.027",{"doi":4645},"10.1016\u002Fj.saa.2017.02.027",{"id":26,"text":4647,"url":26,"identifiers":4648},"Pandimurugan, 2016, Novel seaweed capped ZnO nanoparticles for effective dye photodegradation and antibacterial activity, Adv. Powder Technol., 27, 1062, 10.1016\u002Fj.apt.2016.03.014",{"doi":4649},"10.1016\u002Fj.apt.2016.03.014",{"id":26,"text":4651,"url":26,"identifiers":4652},"Raj, 2016, Anti-bacterial activity of zinc oxide nanoparticles prepared from brassica oleraceae leaves extract, Int. J. Adv. Res., 3, 322",{},{"id":26,"text":4654,"url":26,"identifiers":4655},"Basha, 2016, Sensing and Bio-Sensing Research Ammonia sensor and antibacterial activities of green zinc oxide nanoparticles, Sens. Bio-Sensing Res., 10, 34, 10.1016\u002Fj.sbsr.2016.08.007",{"doi":4656},"10.1016\u002Fj.sbsr.2016.08.007",{"id":26,"text":4658,"url":26,"identifiers":4659},"Pandimurugan, 2017, UV protection and antibacterial properties of seaweed capped ZnO nanoparticles coated cotton fabrics, Int. J. Biol. Macromol., 10.1016\u002Fj.ijbiomac.2017.07.097",{"doi":4660},"10.1016\u002Fj.ijbiomac.2017.07.097",{"id":26,"text":4662,"url":26,"identifiers":4663},"Savithramma, 2014, Biological Synthesis of Zinc oxide Nanoparticles from C atharanthus roseus (l.) G. Don. Leaf extract and validation for antibacterial activity, Int. J. Drug Dev. Res., 6, 208",{},{"id":26,"text":4665,"url":26,"identifiers":4666},"Shah, 2015, Synthesis and characterization of ZnO nanoparticles using leaf extract of camellia sinesis and evaluation of their antimicrobial efficacy, Int. J. Curr. Microbiol. Appl. Sci., 4, 444",{},{"id":26,"text":4668,"url":26,"identifiers":4669},"Gunalan, 2012, Green synthesized ZnO nanoparticles against bacterial and fungal pathogens, Prog. Nat. Sci. Mater. Int, 22, 693, 10.1016\u002Fj.pnsc.2012.11.015",{"doi":4670},"10.1016\u002Fj.pnsc.2012.11.015",{"id":26,"text":4672,"url":26,"identifiers":4673},"Sundrarajan, 2015, Plant-extract mediated synthesis of ZnO nanoparticles using Pongamia pinnata and their activity against pathogenic bacteria, Adv. Powder Technol., 26, 1294, 10.1016\u002Fj.apt.2015.07.001",{"doi":4674},"10.1016\u002Fj.apt.2015.07.001",{"id":26,"text":4676,"url":26,"identifiers":4677},"Patil, 2016, Limonia acidissima L. leaf mediated synthesis of zinc oxide nanoparticles : a potent tool against Mycobacterium tuberculosis, Int. J. Mycobacteriology, 5, 197, 10.1016\u002Fj.ijmyco.2016.03.004",{"doi":4678},"10.1016\u002Fj.ijmyco.2016.03.004",{"id":26,"text":4680,"url":26,"identifiers":4681},"Ali, 2016, Aloe vera extract functionalized zinc oxide nanoparticles as nanoantibiotics against multi-drug resistant clinical bacterial isolates, J. Colloid Interface Sci., 472, 145, 10.1016\u002Fj.jcis.2016.03.021",{"doi":4682},"10.1016\u002Fj.jcis.2016.03.021",{"id":26,"text":4684,"url":26,"identifiers":4685},"Vijayakumar, 2015, Plectranthus amboinicus leaf extract mediated synthesis of zinc oxide nanoparticles and its control of methicillin resistant Staphylococcus aureus biofilm and blood sucking mosquito larvae, Spectrochim. Acta Part A Mol. Biomol. Spectrosc, 137, 886, 10.1016\u002Fj.saa.2014.08.064",{"doi":4686},"10.1016\u002Fj.saa.2014.08.064",{"id":26,"text":4688,"url":26,"identifiers":4689},"Pati, 2014, Topical application of zinc oxide nanoparticles reduces bacterial skin infection in mice and exhibits antibacterial activity by inducing oxidative stress response and cell membrane disintegration in macrophages, Nanomed. Nanotechnol. Biol. Med., 10, 1195, 10.1016\u002Fj.nano.2014.02.012",{"doi":4690},"10.1016\u002Fj.nano.2014.02.012",{"id":26,"text":4692,"url":26,"identifiers":4693},"Suresh, 2015, Udayabhanu, H. Rajanaika, H. Nagabhushana, S.C. Sharma, Green synthesis of multifunctional zinc oxide (ZnO) nanoparticles using Cassia fistula plant extract and their photodegradative, antioxidant and antibacterial activities, Mater. Sci. Semicond. Process., 31, 446, 10.1016\u002Fj.mssp.2014.12.023",{"doi":4694},"10.1016\u002Fj.mssp.2014.12.023",{"id":26,"text":4696,"url":26,"identifiers":4697},"Santhoshkumar, 2017, Synthesis of zinc oxide nanoparticles using plant leaf extract against urinary tract infection pathogen, Resour. Technol, 0, 1",{},{"id":26,"text":4699,"url":26,"identifiers":4700},"Senthilkumar, 2014, Green tea (Camellia sinensis) mediated synthesis of zinc oxide (ZnO) nanoparticles and studies on their antimicrobial activities, Int. J. Pharm. Pharmaceut. Sci., 6, 461",{},{"id":26,"text":4702,"url":26,"identifiers":4703},"Madan, 2016, Facile green fabrication of nanostructure ZnO plates, bullets, flower, prismatic tip, closed pine cone: their antibacterial, antioxidant, photoluminescent and photocatalytic properties, Spectrochim. Acta. A. Mol. Biomol. Spectrosc, 152, 404, 10.1016\u002Fj.saa.2015.07.067",{"doi":4704},"10.1016\u002Fj.saa.2015.07.067",{"id":26,"text":4706,"url":26,"identifiers":4707},"Ambika, 2015, Antibacterial behaviour of Vitex negundo extract assisted ZnO nanoparticles against pathogenic bacteria, J. Photochem. Photobiol. B Biol., 146, 52, 10.1016\u002Fj.jphotobiol.2015.02.020",{"doi":4708},"10.1016\u002Fj.jphotobiol.2015.02.020",{"id":26,"text":4710,"url":26,"identifiers":4711},"Anbuvannan, 2015, Anisochilus carnosus leaf extract mediated synthesis of zinc oxide nanoparticles for antibacterial and photocatalytic activities, Mater. Sci. Semicond. Process., 39, 621, 10.1016\u002Fj.mssp.2015.06.005",{"doi":4712},"10.1016\u002Fj.mssp.2015.06.005",{"id":26,"text":4714,"url":26,"identifiers":4715},"Jafarirad, 2016, Biofabrication of zinc oxide nanoparticles using fruit extract of Rosa canina and their toxic potential against bacteria: a mechanistic approach, Mater. Sci. Eng. C, 59, 296, 10.1016\u002Fj.msec.2015.09.089",{"doi":4716},"10.1016\u002Fj.msec.2015.09.089",{"id":26,"text":4718,"url":26,"identifiers":4719},"Nagajyothi, 2014, Characterization, antibacterial, antioxidant, and cytotoxic activities of ZnO nanoparticles using Coptidis Rhizoma, Bioorg. Med. Chem. Lett, 24, 4298, 10.1016\u002Fj.bmcl.2014.07.023",{"doi":4720},"10.1016\u002Fj.bmcl.2014.07.023",{"id":26,"text":4722,"url":26,"identifiers":4723},"Elumalai, 2015, Green synthesis, characterization and antimicrobial activities of zinc oxide nanoparticles from the leaf extract of Azadirachta indica ( L.), Appl. Surf. Sci., 345, 329, 10.1016\u002Fj.apsusc.2015.03.176",{"doi":4724},"10.1016\u002Fj.apsusc.2015.03.176",{"id":26,"text":4726,"url":26,"identifiers":4727},"Jayaseelan, 2012, Novel microbial route to synthesize ZnO nanoparticles using Aeromonas hydrophila and their activity against pathogenic bacteria and fungi, Spectrochim. Acta Part A Mol. Biomol. Spectrosc, 90, 78, 10.1016\u002Fj.saa.2012.01.006",{"doi":4728},"10.1016\u002Fj.saa.2012.01.006",{"id":26,"text":4730,"url":26,"identifiers":4731},"Ramesh, 2015, Green synthesis of ZnO nanoparticles using Solanum nigrum leaf extract and their antibacterial activity, Spectrochim. Acta Part A Mol. Biomol. Spectrosc, 136, 864, 10.1016\u002Fj.saa.2014.09.105",{"doi":4732},"10.1016\u002Fj.saa.2014.09.105",{"id":26,"text":4734,"url":26,"identifiers":4735},"Suresh, 2015, Green synthesis of multifunctional zinc oxide ( ZnO ) nanoparticles using Cassia fistula plant extract and their photodegradative, antioxidant and antibacterial activities, Mater. Sci. Semicond. Process., 31, 446, 10.1016\u002Fj.mssp.2014.12.023",{"doi":4694},{"id":26,"text":4737,"url":26,"identifiers":4738},"Yuvakkumar, 2014, Novel green synthetic strategy to prepare ZnO nanocrystals using rambutan (Nephelium lappaceum L.) peel extract and its antibacterial applications, Mater. Sci. Eng. C, 41, 17, 10.1016\u002Fj.msec.2014.04.025",{"doi":4739},"10.1016\u002Fj.msec.2014.04.025",{"id":26,"text":4741,"url":26,"identifiers":4742},"Malaikozhundan, 2017, Biological therapeutics of Pongamia pinnata coated zinc oxide nanoparticles against clinically important pathogenic bacteria, fungi and MCF-7 breast cancer cells, Microb. Pathog., 104, 268, 10.1016\u002Fj.micpath.2017.01.029",{"doi":4743},"10.1016\u002Fj.micpath.2017.01.029",{"id":26,"text":4745,"url":26,"identifiers":4746},"Sathishkumar, 2017, Facile biosynthesis of antimicrobial zinc oxide ( ZnO ) nano fl akes using leaf extract of Couroupita guianensis, Aubl. Mater. Lett., 188, 383, 10.1016\u002Fj.matlet.2016.11.100",{"doi":4747},"10.1016\u002Fj.matlet.2016.11.100",{"id":26,"text":4749,"url":26,"identifiers":4750},"Madan, 2016, Facile green fabrication of nanostructure ZnO plates, bullets, flower, prismatic tip, closed pine cone : their antibacterial, antioxidant, photoluminescent and photocatalytic properties, Spectrochim. ACTA PART A Mol. Biomol. Spectrosc, 152, 404, 10.1016\u002Fj.saa.2015.07.067",{"doi":4704},{"id":26,"text":4752,"url":26,"identifiers":4753},"Sharma, 2016, ZnO nano-flowers from Carica papaya milk : degradation of Alizarin Red-S dye and antibacterial activity against Pseudomonas aeruginosa and Staphylococcus aureus, Opt. Int. J. Light Electron Opt, 127, 6498, 10.1016\u002Fj.ijleo.2016.04.036",{"doi":4754},"10.1016\u002Fj.ijleo.2016.04.036",{"id":26,"text":4756,"url":26,"identifiers":4757},"Salem, 2015, Antibacterial activity of silver and zinc nanoparticles against Vibrio cholerae and enterotoxic Escherichia coli, Int. J. Med. Microbiol., 305, 85, 10.1016\u002Fj.ijmm.2014.11.005",{"doi":4758},"10.1016\u002Fj.ijmm.2014.11.005",{"id":26,"text":4760,"url":26,"identifiers":4761},"St, 2016, Biosynthesis of zinc oxide nanoparticles using Aspergillus fumigatus JCF and its antibacterial activity, Int. J. Mod. Sci. Technol, 1, 52",{},{"id":26,"text":4763,"url":26,"identifiers":4764},"Cowan, 1999, Plant products as antimicrobial agents, Clin. Microbiol. Rev., 12, 564, 10.1128\u002FCMR.12.4.564",{"doi":4765},"10.1128\u002FCMR.12.4.564",{"id":26,"text":4767,"url":26,"identifiers":4768},"Choi, 2010, Potentiation of bacterial killing activity of zinc chloride by pyrrolidine dithiocarbamate, J. Microbiol., 48, 40, 10.1007\u002Fs12275-009-0049-2",{"doi":4769},"10.1007\u002Fs12275-009-0049-2",{"id":26,"text":4771,"url":26,"identifiers":4772},"Behlol, 2016, Future prospects of antibacterial metal nanoparticles as enzyme inhibitor, Mater. Sci. Eng. C",{},{"id":26,"text":4774,"url":26,"identifiers":4775},"Joe, 2016, Journal of industrial and engineering chemistry antibacterial mechanism of ZnO nanoparticles under dark conditions, J. Ind. Eng. Chem.",{},{"id":26,"text":4777,"url":26,"identifiers":4778},"Xie, 2011, Antibacterial activity and mechanism of action of zinc oxide nanoparticles against Campylobacter jejuni antibacterial activity and mechanism of action of zinc oxide nanoparticles against Campylobacter jejuni, Appl. Environ. Microbiol., 77, 2325, 10.1128\u002FAEM.02149-10",{"doi":4779},"10.1128\u002FAEM.02149-10",{"id":26,"text":4781,"url":26,"identifiers":4782},"Hood, 2012, Nutritional immunity : transition metals at the pathogen–host interface, Nat. Publ. Gr, 10, 525",{},{"id":26,"text":4784,"url":26,"identifiers":4785},"Kumar, 2011, Cellular uptake and mutagenic potential of metal oxide nanoparticles in bacterial cells, Chemosphere, 83, 1124, 10.1016\u002Fj.chemosphere.2011.01.025",{"doi":4786},"10.1016\u002Fj.chemosphere.2011.01.025",{"id":26,"text":4788,"url":26,"identifiers":4789},"Nikaido, 1983, vol. 153, 241",{},{"id":26,"text":4791,"url":26,"identifiers":4792},"Jayawardena, 2013, Maltoheptaose promotes nanoparticle internalization by Escherichia coli, Chem. Commun. (J. Chem. Soc. Sect. D), 3034, 10.1039\u002Fc3cc40491a",{"doi":4793},"10.1039\u002Fc3cc40491a",{"id":26,"text":4795,"url":26,"identifiers":4796},"Patra, 2017, Antibacterial activity and synergistic antibacterial potential of biosynthesized silver nanoparticles against foodborne pathogenic bacteria along with its anticandidal and antioxidant effects, Front. Microbiol., 8, 1, 10.3389\u002Ffmicb.2017.00167",{"doi":4797},"10.3389\u002Ffmicb.2017.00167",{"id":26,"text":4799,"url":26,"identifiers":4800},"Amro, 2000, High-resolution atomic force microscopy studies of the Escherichia coli outer Membrane : structural basis for permeability, Langmuir, 16, 2789, 10.1021\u002Fla991013x",{"doi":4801},"10.1021\u002Fla991013x",{"id":26,"text":4803,"url":26,"identifiers":4804},"Chen, 2006, Acute toxicological effects of copper nanoparticles in vivo, Toxicol. Lett., 163, 109, 10.1016\u002Fj.toxlet.2005.10.003",{"doi":4805},"10.1016\u002Fj.toxlet.2005.10.003",{"id":26,"text":4807,"url":26,"identifiers":4808},"Pal, 2007, Does the antibacterial activity of silver nanoparticles depend on the shape of the Nanoparticle ? A study of the gram-negative bacterium Escherichia coli, Appl. Environ. Microbiol., 73, 1712, 10.1128\u002FAEM.02218-06",{"doi":4809},"10.1128\u002FAEM.02218-06",{"id":26,"text":4811,"url":26,"identifiers":4812},"Brayner, 2006, Toxicological impact studies based on Escherichia coli bacteria in ultrafine ZnO nanoparticles colloidal medium, Nano Lett., 6, 866, 10.1021\u002Fnl052326h",{"doi":4813},"10.1021\u002Fnl052326h",{"id":26,"text":4815,"url":26,"identifiers":4816},"Warren, 2015, Cellular binding of nanoparticles disrupts the membrane potential, RSC Adv., 5, 13660, 10.1039\u002FC4RA15727C",{"doi":4817},"10.1039\u002FC4RA15727C",{"id":26,"text":4819,"url":26,"identifiers":4820},"Xia, 2006, Comparison of the abilities of ambient and manufactured nanoparticles to induce cellular toxicity according to an oxidative stress paradigm, Nano Lett., 6, 1794, 10.1021\u002Fnl061025k",{"doi":4821},"10.1021\u002Fnl061025k",{"id":26,"text":4823,"url":26,"identifiers":4824},"Halder, 2015, Alteration of Zeta potential and membrane permeability in bacteria : a study with cationic agents, SpringerPlus, 4, 672, 10.1186\u002Fs40064-015-1476-7",{"doi":4825},"10.1186\u002Fs40064-015-1476-7",{"id":26,"text":4827,"url":26,"identifiers":4828},"Neal, 2012, Can the soil bacterium Cupriavidus necator sense ZnO nanomaterials and aqueous Zn 2 + differentially ?, Nanotoxicology, 6, 371, 10.3109\u002F17435390.2011.579633",{"doi":4829},"10.3109\u002F17435390.2011.579633",{"id":26,"text":4831,"url":26,"identifiers":4832},"Cedervall, 2007, Understanding the nanoparticle – protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles, Proc. Natl. Acad. Sci. Unit. States Am., 104, 10.1073\u002Fpnas.0608582104",{"doi":4833},"10.1073\u002Fpnas.0608582104",{"id":26,"text":4835,"url":26,"identifiers":4836},"Azzam, 2015, Surface and antibacterial activity of synthesized nonionic surfactant assembled on metal nanoparticles, Egypt, J. Petrol.",{},{"id":26,"text":4838,"url":26,"identifiers":4839},"Wu, 2010, Bacterial responses to Cu-doped TiO 2 nanoparticles, Sci. Total Environ., 408, 1755, 10.1016\u002Fj.scitotenv.2009.11.004",{"doi":4840},"10.1016\u002Fj.scitotenv.2009.11.004",{"id":26,"text":4842,"url":26,"identifiers":4843},"Maret, 2013, Inhibitory zinc sites in enzymes, Biometals, 26, 197, 10.1007\u002Fs10534-013-9613-7",{"doi":4844},"10.1007\u002Fs10534-013-9613-7",{"id":26,"text":4846,"url":26,"identifiers":4847},"Chulhun, 1995, Identification of an essential second metal ion in the reaction mechanism of Escherichia coli adenyloscuccinate synthetase, J. Biol. Chem., 270, 15539, 10.1074\u002Fjbc.270.26.15539",{"doi":4848},"10.1074\u002Fjbc.270.26.15539",{"id":26,"text":4850,"url":26,"identifiers":4851},"Hendricks, 1971, Enteric bacterial metabolism of stream sediment eluates, Can. J. Microbiol., 17, 551, 10.1139\u002Fm71-090",{"doi":4852},"10.1139\u002Fm71-090",{"id":26,"text":4854,"url":26,"identifiers":4855},"Von Moos, 2013, Oxidative stress induced by inorganic nanoparticles in bacteria and aquatic microalgae – state of the art and knowledge gaps sation. At acidic pH, it is in equilibrium with its protonated, Nanotoxicology, 1",{},{"id":26,"text":4857,"url":26,"identifiers":4858},"Leung, 2016, Toxicity of ZnO and TiO 2 to Escherichia coli cells, Sci. Rep., 1",{},{"id":26,"text":4860,"url":26,"identifiers":4861},"Zhang, 2007, Investigation into the antibacterial behaviour of suspensions of ZnO nanoparticles (ZnO nanofluids), J. Nanoparticle Res., 9, 479, 10.1007\u002Fs11051-006-9150-1",{"doi":4862},"10.1007\u002Fs11051-006-9150-1",{"id":26,"text":4864,"url":26,"identifiers":4865},"Buzea, 2007, Nanomaterials and nanoparticles : sources and toxicity, Biointerphases, 2, 17, 10.1116\u002F1.2815690",{"doi":4866},"10.1116\u002F1.2815690",{"id":26,"text":4868,"url":26,"identifiers":4869},"Hafiz, 2011, Performance of an ultraviolet photoconductive sensor using well-aligned aluminium-doped zinc-oxide nanorod arrays annealed in an air and oxygen environment, Jpn. J. Appl. Phys., 5",{},{"id":26,"text":4871,"url":26,"identifiers":4872},"Messner, 1999, The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli *, J. Biol. Chem., 274, 10119, 10.1074\u002Fjbc.274.15.10119",{"doi":4873},"10.1074\u002Fjbc.274.15.10119",{"id":26,"text":4875,"url":26,"identifiers":4876},"Xia, 2008, Comparison of the mechanism of toxicity of zinc oxide and cerium oxide nanoparticles based on dissolution and oxidative stress properties, ACS Nano, 2, 2121, 10.1021\u002Fnn800511k",{"doi":4877},"10.1021\u002Fnn800511k",{"id":26,"text":4879,"url":26,"identifiers":4880},"Wang, 2008, Acute toxicological impact of nano- and submicro-scaled zinc oxide powder on healthy adult mice, J. Nanoparticle Res., 10, 263, 10.1007\u002Fs11051-007-9245-3",{"doi":4881},"10.1007\u002Fs11051-007-9245-3",{"id":26,"text":4883,"url":26,"identifiers":4884},"Choi, 2014, 261",{},{"id":26,"text":4886,"url":26,"identifiers":4887},"Paek, 2013, Modulation of the pharmacokinetics of zinc oxide nanoparticles and their fates in vivo, Nanoscale, 5, 11416, 10.1039\u002Fc3nr02140h",{"doi":4888},"10.1039\u002Fc3nr02140h",{"id":26,"text":4890,"url":26,"identifiers":4891},"Choi, 2012, Pharmacokinetics, tissue distribution, and excretion of zinc oxide nanoparticles, Int. J. Nanomed., 7, 3081, 10.2147\u002FIJN.S32593",{"doi":4892},"10.2147\u002FIJN.S32593",{"id":26,"text":4894,"url":26,"identifiers":4895},"Dakal, 2016, Mechanistic basis of antimicrobial actions of silver nanoparticles, Front. Microbiol., 7, 1, 10.3389\u002Ffmicb.2016.01831",{"doi":4896},"10.3389\u002Ffmicb.2016.01831",{"id":26,"text":4898,"url":26,"identifiers":4899},"Chen, 2002, Synthesis and characterization of truncated triangular silver nanoplates, Nano Lett., 2, 1003, 10.1021\u002Fnl025674h",{"doi":4900},"10.1021\u002Fnl025674h",{"id":26,"text":4902,"url":26,"identifiers":4903},"Leung, 2012, Antibacterial activity of ZnO nanoparticles with a modified surface under ambient illumination, Nanotechnology, 23, 10.1088\u002F0957-4484\u002F23\u002F47\u002F475703",{"doi":4904},"10.1088\u002F0957-4484\u002F23\u002F47\u002F475703",{"id":26,"text":4906,"url":26,"identifiers":4907},"Peng, 2011, Effect of morphology of ZnO nanostructures on their toxicity to marine algae, Aquat. Toxicol., 102, 186, 10.1016\u002Fj.aquatox.2011.01.014",{"doi":4908},"10.1016\u002Fj.aquatox.2011.01.014",{"id":26,"text":4910,"url":26,"identifiers":4911},"Webster, 2012, Antimicrobial applications of nanotechnology : methods and literature, Int. J. Nanomed., 7, 2767, 10.2147\u002FIJN.S24805",{"doi":4912},"10.2147\u002FIJN.S24805",{"id":26,"text":4914,"url":26,"identifiers":4915},"Vielkind, 2013, Zinc oxide nanoparticles in bacterial growth Medium : optimized dispersion and growth inhibition of Pseudomonas putida, Adv. Nanoparticles, 2, 287, 10.4236\u002Fanp.2013.24039",{"doi":4916},"10.4236\u002Fanp.2013.24039",{"id":26,"text":4918,"url":26,"identifiers":4919},"Raghupathi, 2011, Size-dependent bacterial growth inhibition and mechanism of antibacterial activity of zinc oxide nanoparticles, Langmuir, 4020, 10.1021\u002Fla104825u",{"doi":4920},"10.1021\u002Fla104825u",{"id":26,"text":4922,"url":26,"identifiers":4923},"Wang, 2017, The antimicrobial activity of nanoparticles: present situation and prospects for the future, Int. J. Nanomed., 12, 1227, 10.2147\u002FIJN.S121956",{"doi":4924},"10.2147\u002FIJN.S121956",{"id":26,"text":4926,"url":26,"identifiers":4927},"Emami-karvani, 2015, Antibacterial activity of ZnO nanoparticle on Gram-positive and Gram-negative bacteria Antibacterial activity of ZnO nanoparticle on gram- positive and gram-negative bacteria, Afr. J. Microbiol. Res., 5, 1368",{},{"id":26,"text":4929,"url":26,"identifiers":4930},"Dobrucka, 2016, Biosynthesis and antibacterial activity of ZnO nanoparticles using Trifolium pratense flower extract, Saudi J. Biol. Sci., 23, 517, 10.1016\u002Fj.sjbs.2015.05.016",{"doi":4931},"10.1016\u002Fj.sjbs.2015.05.016",{"id":26,"text":4933,"url":26,"identifiers":4934},"Saliani, 2015, Effects of pH and temperature on antibacterial activity of zinc oxide nanofluid against Escherichia coli O157 : H7 and Staphylococcus aureus, Microbiol. Res., 8",{},{"id":26,"text":4936,"url":26,"identifiers":4937},"Moreau, 2014, Extracellular proteins limit the dispersal of biogenic nanoparticles, Science (80-. ), 1600",{},{"id":26,"text":4939,"url":26,"identifiers":4940},"Iao, 2010, Zinc oxide – engineered nanoparticles  dissolution and toxicity to marine phytoplankton, Environ. Toxicol. Chem., 29, 2814, 10.1002\u002Fetc.340",{"doi":4941},"10.1002\u002Fetc.340",{"id":26,"text":4943,"url":26,"identifiers":4944},"Eed, 2012, Nanomaterials in the Environment solubility of nano-zinc oxide in environmentally and biologically important matrices, Environ. Toxicol. Chem., 31, 93, 10.1002\u002Fetc.708",{"doi":4945},"10.1002\u002Fetc.708",{"id":26,"text":4947,"url":26,"identifiers":4948},"Tayel, 2011, Antibacterial action of zinc oxide nanoparticles, J. Food Saf., 31, 211, 10.1111\u002Fj.1745-4565.2010.00287.x",{"doi":4949},"10.1111\u002Fj.1745-4565.2010.00287.x",{"id":26,"text":4951,"url":26,"identifiers":4952},"Bhuyan, 2015, Materials Science in Semiconductor Processing Biosynthesis of zinc oxide nanoparticles from Azadirachta indica for antibacterial and photocatalytic applications, Mater. Sci. Semicond. Process., 32, 55, 10.1016\u002Fj.mssp.2014.12.053",{"doi":4953},"10.1016\u002Fj.mssp.2014.12.053",{"id":26,"text":4955,"url":26,"identifiers":4956},"Shalumon, 2011, International Journal of Biological Macromolecules Sodium alginate\u002Fpoly ( vinyl alcohol )\u002Fnano ZnO composite nanofibers for antibacterial wound dressings, Int. J. Biol. Macromol., 49, 247, 10.1016\u002Fj.ijbiomac.2011.04.005",{"doi":4957},"10.1016\u002Fj.ijbiomac.2011.04.005",{"id":26,"text":4959,"url":26,"identifiers":4960},"Liu, 2012, Characterization and antibacterial properties of genipin-crosslinked chitosan\u002Fpoly ( ethylene glycol )\u002FZnO\u002FAg nanocomposites, 111",{},{"id":26,"text":4962,"url":26,"identifiers":4963},"Moritz, 2013, The newest achievements in synthesis, immobilization and practical applications of antibacterial nanoparticles, Chem. Eng. J., 228, 596, 10.1016\u002Fj.cej.2013.05.046",{"doi":4964},"10.1016\u002Fj.cej.2013.05.046",{"id":26,"text":4966,"url":26,"identifiers":4967},"Zheng, 2011, Effects of ZnO nanoparticles on wastewater biological nitrogen and phosphorus removal, Environ. Sci. Technol., 45, 2826, 10.1021\u002Fes2000744",{"doi":4968},"10.1021\u002Fes2000744",{"id":26,"text":4970,"url":26,"identifiers":4971},"Rajiv, 2013, Spectrochimica Acta Part A : molecular and Biomolecular Spectroscopy Bio-Fabrication of zinc oxide nanoparticles using leaf extract of Parthenium hysterophorus L. and its size-dependent antifungal activity against plant fungal pathogens, Spectrochim. Acta Part A Mol. Biomol. Spectrosc, 112, 384, 10.1016\u002Fj.saa.2013.04.072",{"doi":4972},"10.1016\u002Fj.saa.2013.04.072",{"id":26,"text":4974,"url":26,"identifiers":4975},"Kiselev, 2017, Transparent bactericidal coatings based on zinc and to appear in : ceramics International, Ceram. 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Asp. Med., 14, 287, 10.1016\u002F0098-2997(93)90002-U",{"doi":5062},"10.1016\u002F0098-2997(93)90002-U",{"id":26,"text":5064,"url":26,"identifiers":5065},"Loidl-Stahlhofen, 1994, Hydroxyaldehydes, products of lipid peroxidation, Biochim. Biophys. Acta, 1211, 156, 10.1016\u002F0005-2760(94)90264-X",{"doi":5066},"10.1016\u002F0005-2760(94)90264-X",{"id":26,"text":5068,"url":26,"identifiers":5069},"Wells-Knecht, 1995, Mechanism of autoxidative glycosylation: Identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose, J. Am. Chem. Soc., 34, 3702",{},{"id":26,"text":5071,"url":26,"identifiers":5072},"Glomb, 1995, Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction, J. Biol. Chem., 276, 10017, 10.1074\u002Fjbc.270.17.10017",{"doi":5073},"10.1074\u002Fjbc.270.17.10017",{"id":26,"text":5075,"url":26,"identifiers":5076},"Phillips, 1993, The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal, Eur. J. Biochem., 212, 101, 10.1111\u002Fj.1432-1033.1993.tb17638.x",{"doi":5077},"10.1111\u002Fj.1432-1033.1993.tb17638.x",{"id":26,"text":5079,"url":26,"identifiers":5080},"Pompliano, 1990, Stabilization of a reaction intermediate as a catalytic device: Definition of the functional role of the flexible loop in triosephosphate isomerase, Biochemistry, 29, 3186, 10.1021\u002Fbi00465a005",{"doi":5081},"10.1021\u002Fbi00465a005",{"id":26,"text":5083,"url":26,"identifiers":5084},"Ray, 1981, Isolation of methylglyoxal synthase goat liver, J. Biol. Chem., 256, 6230, 10.1016\u002FS0021-9258(19)69151-9",{"doi":5085},"10.1016\u002FS0021-9258(19)69151-9",{"id":26,"text":5087,"url":26,"identifiers":5088},"Koop, 1985, Identification of ethanol-inducible P-450 isozyme 3a as the acetone and acetol monooxygenase of rabbit microsomes, J. Biol. Chem., 260, 13607, 10.1016\u002FS0021-9258(17)38768-9",{"doi":5089},"10.1016\u002FS0021-9258(17)38768-9",{"id":26,"text":5091,"url":26,"identifiers":5092},"Lyles, 1992, The metabolism of aminoacetone to methylglyoxal by semicarbazide-sensitive amino oxidase in human umbilical artery, Biochem. Pharmacol., 43, 1409, 10.1016\u002F0006-2952(92)90196-P",{"doi":5093},"10.1016\u002F0006-2952(92)90196-P",{"id":26,"text":5095,"url":26,"identifiers":5096},"Jerzykowski, 1979, Dioxovalerate as a substrate for the glyoxalase enzyme system, Biochemistry, 135, 713, 10.1042\u002Fbj1350713",{"doi":5097},"10.1042\u002Fbj1350713",{"id":26,"text":5099,"url":26,"identifiers":5100},"Thornalley, 1996, Negative association of red blood cell reduced glutathione with diabetic complications, Clin. Sci., 91, 575, 10.1042\u002Fcs0910575",{"doi":5101},"10.1042\u002Fcs0910575",{"id":26,"text":5103,"url":26,"identifiers":5104},"McLellan, 1994, The glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications, Clin. Sci., 87, 21, 10.1042\u002Fcs0870021",{"doi":5105},"10.1042\u002Fcs0870021",{"id":26,"text":5107,"url":26,"identifiers":5108},"Papoulis, 1995, Identification of N2-(1-carboxyethyl)guanine (CEG) as a guanine advanced glycosylation endproduct, Biochemistry, 34, 648, 10.1021\u002Fbi00002a032",{"doi":5109},"10.1021\u002Fbi00002a032",{"id":26,"text":5111,"url":26,"identifiers":5112},"Vaca, 1994, Development of a 32P-postlabelling technique for the analysis of 2′-deoxyguanosine-3′-monophosphate and DNA of methylglyoxal, Carcinogenesis, 15, 1887, 10.1093\u002Fcarcin\u002F15.9.1887",{"doi":5113},"10.1093\u002Fcarcin\u002F15.9.1887",{"id":26,"text":5115,"url":26,"identifiers":5116},"Nukaya, 1993, Modification of the amino group of guanosine by methylglyoxal and other α-ketoaldehydes in the presence of H2O2, Chem. Pharm. Bull., 41, 649, 10.1248\u002Fcpb.41.649",{"doi":5117},"10.1248\u002Fcpb.41.649",{"id":26,"text":5119,"url":26,"identifiers":5120},"Thornalley, 1995, Crit. Rev. Oncol. Haematol., 20, 99, 10.1016\u002F1040-8428(94)00149-N",{"doi":5121},"10.1016\u002F1040-8428(94)00149-N",{"id":26,"text":5123,"url":26,"identifiers":5124},"Kang, 1996, Effect of methylglyoxal on human leukaemia 60 cell growth: modification of DNA, G1 growth arrest and induction of apoptosis, Leuk. Res., 20, 397, 10.1016\u002F0145-2126(95)00162-X",{"doi":5125},"10.1016\u002F0145-2126(95)00162-X",{"id":26,"text":5127,"url":26,"identifiers":5128},"Hiraku, 1997, Mechanism of oxidative DNA damage induced by δ-aminolevulinic acid in the presence of copper ion, Cancer Res., 56, 1786",{},{"id":26,"text":5130,"url":26,"identifiers":5131},"Vince, 1969, Glyoxalase inhibitors as potential anticancer agents, Biochem. Biophys. Res. Commun., 35, 593, 10.1016\u002F0006-291X(69)90445-8",{"doi":5132},"10.1016\u002F0006-291X(69)90445-8",{"id":26,"text":5134,"url":26,"identifiers":5135},"Lo, 1992, Inhibition of proliferation of human leukemia 60 cells by diethyl esters of glyoxalase inhibitors in vitro, Biochem. Pharmacol., 44, 2357, 10.1016\u002F0006-2952(92)90680-H",{"doi":5136},"10.1016\u002F0006-2952(92)90680-H",{"id":26,"text":5138,"url":26,"identifiers":5139},"Thornalley, 1996, Antitumour activity of S-p-bromobenzylglutathione diesters in vitro: a structure activity study, J. Med. Chem., 39, 3409, 10.1021\u002Fjm960129c",{"doi":5140},"10.1021\u002Fjm960129c",{"id":26,"text":5142,"url":26,"identifiers":5143},"Thornalley, 1996, Antitumour activity of S-p-bromobenzylglutathione cyclopentyl diester in vitro and in vivo. Inhibition of glyoxalase I and induction of apoptosis, Biochem. Pharmacol., 51, 1365, 10.1016\u002F0006-2952(96)00059-7",{"doi":5144},"10.1016\u002F0006-2952(96)00059-7",{"id":26,"text":5146,"url":26,"identifiers":5147},"Moldeus, 1994, N-Acetylcysteine, Methods Enzymol., 234, 482, 10.1016\u002F0076-6879(94)34119-2",{"doi":5148},"10.1016\u002F0076-6879(94)34119-2",{"id":26,"text":5150,"url":26,"identifiers":5151},"Thornalley, 1994, Anti-malarial activity in vitro of the glyoxalase I inhibitor diester, S-p-bromobenzylglutathione diethyl ester, Biochem. Pharmacol., 268, 14189",{},{"id":26,"text":5153,"url":26,"identifiers":5154},"Thornalley, 1988, Modification of the glyoxalase system in human red blood cells by glucose in vitro, Biochem. J., 254, 751, 10.1042\u002Fbj2540751",{"doi":5155},"10.1042\u002Fbj2540751",{"id":26,"text":5157,"url":26,"identifiers":5158},"Phillips, 1993, Modification of the glyoxalase system in streptozotocin-induced diabetic rats; effect of the aldose reductase inhibitor Statil, Biochem. Pharmacol., 46, 805, 10.1016\u002F0006-2952(93)90488-I",{"doi":5159},"10.1016\u002F0006-2952(93)90488-I",{"id":26,"text":5161,"url":26,"identifiers":5162},"Donnini, 1996, Glucose may induce cell death through a free radical-mediated mechanism, Biochem. Biophys. Res. Commun., 219, 412, 10.1006\u002Fbbrc.1996.0247",{"doi":5163},"10.1006\u002Fbbrc.1996.0247",{"id":26,"text":5165,"url":26,"identifiers":5166},"Shinohara, 1996, Overexpression of glyoxalase I inhibits intracellular advanced glycation endproduct (AGE) formation, Diabetes, 45, 126A",{},{"id":26,"text":5168,"url":26,"identifiers":5169},"Lo, 1994, Reaction of methylglyoxal with aminoguanidine under physiological conditions and prevention of methylglyoxal binding to plasma proteins, Biochem. Pharmacol., 48, 1865, 10.1016\u002F0006-2952(94)90584-3",{"doi":5170},"10.1016\u002F0006-2952(94)90584-3",{"id":26,"text":5172,"url":26,"identifiers":5173},"Thornalley, 1996, Advanced glycation and the development of diabetic complications. Unifying the involvement of glucose, methylglyoxal and oxidative stress, Endocrinol. Metab., 3, 149",{},{"id":26,"text":5175,"url":26,"identifiers":5176},"Lo, 1994, Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with Nα-acetylarginine, Nα-acetylcysteine, Nα-acetyl-lysine, and bovine serum albumin, J. Biol. Chem., 269, 32299, 10.1016\u002FS0021-9258(18)31635-1",{"doi":5177},"10.1016\u002FS0021-9258(18)31635-1",{"id":26,"text":5179,"url":26,"identifiers":5180},"Henle, 1994, Detection and identification of a protein-bound imidazolone resulting from the reaction of arginine residues and methylglyoxal, Z. Lebensm. Unters. Forsch, 199, 55, 10.1007\u002FBF01192954",{"doi":5181},"10.1007\u002FBF01192954",{"id":26,"text":5183,"url":26,"identifiers":5184},"Nagaraj, 1996, Protein cross-linking by the Maillard reaction. Isolation, characterization, and in vivo detection of a lysine–lysine cross-link derived from methylglyoxal, J. Biol. Chem., 271, 19338, 10.1074\u002Fjbc.271.32.19338",{"doi":5185},"10.1074\u002Fjbc.271.32.19338",{"id":26,"text":5187,"url":26,"identifiers":5188},"Ahmed, 1997, Nε-(2-Carboxyethyl)lysine, a product of chemical modification of proteins by methylglyoxal, increases with age in human lens proteins, Biochem. J., 324, 565, 10.1042\u002Fbj3240565",{"doi":5189},"10.1042\u002Fbj3240565",{"id":26,"text":5191,"url":26,"identifiers":5192},"Griffith, 1980, The apparent glutathione oxidase activity of gamma-glutamyl transpeptidase, J. Biol. Chem., 255, 5011, 10.1016\u002FS0021-9258(19)70739-X",{"doi":5193},"10.1016\u002FS0021-9258(19)70739-X",{"id":26,"text":5195,"url":26,"identifiers":5196},"McLellan, 1992, The assay of methylglyoxal in biological systems by derivatization with 1,2-diamino-4,5-dimethoxybenzene, Anal. Biochem., 206, 17, 10.1016\u002FS0003-2697(05)80005-3",{"doi":5197},"10.1016\u002FS0003-2697(05)80005-3",{"id":26,"text":5199,"url":26,"identifiers":5200},"Westwood, 1997, Methylglyoxal-modified arginine residues-a signal for receptor-mediated endocytosis and degradation of proteins by monocytic THP-1 cells, Biochim. Biophys. Acta, 1356, 84, 10.1016\u002FS0167-4889(96)00154-1",{"doi":5201},"10.1016\u002FS0167-4889(96)00154-1",{"id":26,"text":5203,"url":26,"identifiers":5204},"Westwood, 1996, Induction of synthesis and secretion of interleukin 1( in the human monocytic leukaemia THP-1 cells by human serum albumins modified with methylglyoxal and advanced glycation endproducts, Immunol. Lett., 50, 17, 10.1016\u002F0165-2478(96)02496-0",{"doi":5205},"10.1016\u002F0165-2478(96)02496-0",{"id":26,"text":5207,"url":26,"identifiers":5208},"Westwood, 1994, Receptor-mediated endocytic uptake of methylglyoxal-modified proteins, J. Biol. Chem., 269, 32293, 10.1016\u002FS0021-9258(18)31634-X",{"doi":5209},"10.1016\u002FS0021-9258(18)31634-X",{"id":26,"text":5211,"url":26,"identifiers":5212},"Shinoda, 1993, Uptake of proteins modified with 3-deoxyglucosone, a Maillard reaction intermediate, by the type I macrophage scavenger receptor, Biosci. Biotech. Biochem., 57, 1826, 10.1271\u002Fbbb.57.1826",{"doi":5213},"10.1271\u002Fbbb.57.1826",{"id":26,"text":5215,"url":26,"identifiers":5216},"Araki, 1995, Macrophage scavenger receptor mediates the endocytic uptake and degradation of advanced glycation end-products of the Maillard reaction, Eur. J. Biochem., 230, 408, 10.1111\u002Fj.1432-1033.1995.0408h.x",{"doi":5217},"10.1111\u002Fj.1432-1033.1995.0408h.x",{"id":26,"text":5219,"url":26,"identifiers":5220},"Schmidt, 1994, The endothelial cell binding site for advanced glycation endproducts consists of a complex: An integral membrane protein and a lactoferrin-like polypeptide, J. Biol. Chem., 269, 9882, 10.1016\u002FS0021-9258(17)36965-X",{"doi":5221},"10.1016\u002FS0021-9258(17)36965-X",{"id":26,"text":5223,"url":26,"identifiers":5224},"Abordo, 1996, Synthesis and secretion of macrophage colony stimulating factor by mature human monocytes and human monocytic THP-1 cells induced by human serum albumin derivatives modified with methylglyoxal and glucose-derived advanced glycation endproducts, Immunol. Lett., 53, 7, 10.1016\u002F0165-2478(96)02601-6",{"doi":5225},"10.1016\u002F0165-2478(96)02601-6",{"id":26,"text":5227,"url":26,"identifiers":5228},"Abordo, 1996, Human serum albumin minimally-modified by methylglyoxal but not by glucose-derived advanced glycation endproducts induced the synthesis and secretion of tumour necrosis factor-α (TNFα) by human monocytic THP-1 cells in vitro, Diabetes, 45, 129A",{},{"id":26,"text":5230,"url":26,"identifiers":5231},"McCance, 1993, Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus, J. Clin. Invest., 91, 2470, 10.1172\u002FJCI116482",{"doi":5232},"10.1172\u002FJCI116482",{"id":26,"text":5234,"url":26,"identifiers":5235},"Lyons, 1991, Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts, Diabetes, 40, 1010, 10.2337\u002Fdiab.40.8.1010",{"doi":5236},"10.2337\u002Fdiab.40.8.1010",{"id":26,"text":5238,"url":26,"identifiers":5239},"Vlassara, 1992, Exogenous advanced glycosylation end products induce complex vascular dysfunction in normal animals: A model for diabetic and aging complications, Proc. Natl. Acad. Sci. USA, 89, 12043, 10.1073\u002Fpnas.89.24.12043",{"doi":5240},"10.1073\u002Fpnas.89.24.12043",{"id":26,"text":5242,"url":26,"identifiers":5243},"Vitek, 1994, Advanced glycation end products contribute to amyloidosis in Alzheimer disease, Proc. Natl. Acad. Sci. USA, 91, 4766, 10.1073\u002Fpnas.91.11.4766",{"doi":5244},"10.1073\u002Fpnas.91.11.4766",{"id":26,"text":5246,"url":26,"identifiers":5247},"Miyata, 1993, β2-Microglobulin modified with advanced glycation end products is a major component of haemodialysis-associated amyloidosis, J. Clin. Invest., 92, 1243, 10.1172\u002FJCI116696",{"doi":5248},"10.1172\u002FJCI116696",{"id":26,"text":5250,"url":26,"identifiers":5251},"Monteiro, 1989, Free radical generation during δ-aminolevulinic acid autooxiadtion: induction by hemoglobin and connections with porphyrinopathies, Arch. Biochem. 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Biochem. Biophys., 241, 149, 10.1016\u002F0003-9861(85)90371-6",{"doi":5354},"10.1016\u002F0003-9861(85)90371-6",{"id":26,"text":5356,"url":26,"identifiers":5357},"Astrom, 1986, Subcellular and organ distribution of cholesterol epoxide hydrolase in the rat, Biochim. Biophys. Acta, 882, 359, 10.1016\u002F0304-4165(86)90259-X",{"doi":5358},"10.1016\u002F0304-4165(86)90259-X",{"id":26,"text":5360,"url":26,"identifiers":5361},"Finley, 1988, Increased cholesterol epoxide hydrolase activity in clofibrate-fed animals, Biochem. Pharmacol., 37, 3169, 10.1016\u002F0006-2952(88)90316-4",{"doi":5362},"10.1016\u002F0006-2952(88)90316-4",{"id":26,"text":5364,"url":26,"identifiers":5365},"Levin, 1983, Distinct rat hepatic microsomal epoxide hydrolases catalyze the hydration of cholesterol 5,6 α-oxide and certain xenobiotic alkene and arene oxides, Arch. Biochem. Biophys., 220, 485, 10.1016\u002F0003-9861(83)90439-3",{"doi":5366},"10.1016\u002F0003-9861(83)90439-3",{"id":26,"text":5368,"url":26,"identifiers":5369},"Muller, 1997, Visualization of a covalent intermediate between microsomal epoxide hydrolase, but not cholesterol epoxide hydrolase, and their substrates, Eur. J. Biochem., 245, 490, 10.1111\u002Fj.1432-1033.1997.00490.x",{"doi":5370},"10.1111\u002Fj.1432-1033.1997.00490.x",{"id":26,"text":5372,"url":26,"identifiers":5373},"Sevanian, 1986, Catalytic properties and inhibition of hepatic cholesterol-epoxide hydrolase, J. Biol. Chem., 261, 54, 10.1016\u002FS0021-9258(17)42429-X",{"doi":5374},"10.1016\u002FS0021-9258(17)42429-X",{"id":26,"text":5376,"url":26,"identifiers":5377},"Sevanian, 1984, Cholesterol epoxide is a direct-acting mutagen, Proc. Natl. Acad. Sci. USA, 81, 4198, 10.1073\u002Fpnas.81.13.4198",{"doi":5378},"10.1073\u002Fpnas.81.13.4198",{"id":26,"text":5380,"url":26,"identifiers":5381},"Sevanian, 1986, The cytotoxic and mutagenic properties of cholesterol oxidation products, Food Chem. Toxicol., 24, 1103, 10.1016\u002F0278-6915(86)90295-4",{"doi":5382},"10.1016\u002F0278-6915(86)90295-4",{"id":26,"text":5384,"url":26,"identifiers":5385},"Nashed, 1986, 7-Dehydrocholesterol 5,6 α-oxide as a mechanism-based inhibitor of microsomal cholesterol oxide hydrolase, J. Biol. Chem., 261, 2510, 10.1016\u002FS0021-9258(17)35815-5",{"doi":5386},"10.1016\u002FS0021-9258(17)35815-5",{"id":26,"text":5388,"url":26,"identifiers":5389},"Watabe, 1983, Mouse liver microsomal cholesterol epoxide hydrolase: a specific inhibition of its activity by 5,6 α-imino-5 α-cholestan-3 α-OL, Chem. Biol. Interact., 44, 143, 10.1016\u002F0009-2797(83)90136-9",{"doi":5390},"10.1016\u002F0009-2797(83)90136-9",{"id":26,"text":5392,"url":26,"identifiers":5393},"Pace-Asciak, 1989, Purification of hepoxilin epoxide hydrolase from rat liver, J. Biol. Chem., 264, 9310, 10.1016\u002FS0021-9258(18)60532-0",{"doi":5394},"10.1016\u002FS0021-9258(18)60532-0",{"id":26,"text":5396,"url":26,"identifiers":5397},"Pace-Asciak, 1994, Hepoxilins: a review on their cellular actions, Biochim. Biophys. Acta, 1215, 1, 10.1016\u002F0005-2760(94)90087-6",{"doi":5398},"10.1016\u002F0005-2760(94)90087-6",{"id":26,"text":5400,"url":26,"identifiers":5401},"Reynaud, 1994, Hepoxilin A3 formation in the rat pineal gland selectively utilizes (12S)-hydroperoxyeicosatetraenoic acid (HPETE), but not (12R)-HPETE, J. Biol. Chem., 269, 23976, 10.1016\u002FS0021-9258(19)51034-1",{"doi":5402},"10.1016\u002FS0021-9258(19)51034-1",{"id":26,"text":5404,"url":26,"identifiers":5405},"Laneuville, 1991, Hepoxilin A3 (HxA3) is formed by the rat aorta and is metabolized into HxA3-C, a glutathione conjugate, Biochim. Biophys. Acta, 1084, 60, 10.1016\u002F0005-2760(91)90056-N",{"doi":5406},"10.1016\u002F0005-2760(91)90056-N",{"id":26,"text":5408,"url":26,"identifiers":5409},"Reynaud, 1999, Hepoxilin signaling in intact human neutrophils: biphasic elevation of intracellular calcium by unesterified hepoxilin A3, FEBS Lett., 446, 236, 10.1016\u002FS0014-5793(99)00225-2",{"doi":5410},"10.1016\u002FS0014-5793(99)00225-2",{"id":26,"text":5412,"url":26,"identifiers":5413},"Margalit, 1993, Hepoxilin A3 is the endogenous lipid mediator opposing hypotonic swelling of intact human platelets, Proc. Natl. Acad. Sci. USA, 90, 2589, 10.1073\u002Fpnas.90.7.2589",{"doi":5414},"10.1073\u002Fpnas.90.7.2589",{"id":26,"text":5416,"url":26,"identifiers":5417},"Haeggstrom, 1994, Novel structural and functional properties of leukotriene A4 hydrolase. Implications for the development of enzyme inhibitors, Adv. Prostaglandin Thromb. Leukot. Res., 22, 3",{},{"id":26,"text":5419,"url":26,"identifiers":5420},"Mancini, 1995, Cloning and characterization of the human leukotriene A4 hydrolase gene, Eur. J. Biochem., 231, 65, 10.1111\u002Fj.1432-1033.1995.tb20671.x",{"doi":5421},"10.1111\u002Fj.1432-1033.1995.tb20671.x",{"id":26,"text":5423,"url":26,"identifiers":5424},"Jendraschak, 1996, The human leukotriene A4 hydrolase gene is expressed in two alternatively spliced mRNA forms, Biochem. J., 314, 733, 10.1042\u002Fbj3140733",{"doi":5425},"10.1042\u002Fbj3140733",{"id":26,"text":5427,"url":26,"identifiers":5428},"E. Jendraschak, W.E. Kaminski, Isolation of human promoter regions by Alu repeat consensus-based polymerase chain reaction, Genomics 50 (1998) 53–60.",{"doi":5429},"10.1006\u002Fgeno.1998.5290",{"id":26,"text":5431,"url":26,"identifiers":5432},"Fu, 1989, Leukotriene A4 hydrolase: analysis of some human tissues by radioimmunoassay, Biochim. Biophys. Acta, 1006, 121, 10.1016\u002F0005-2760(89)90332-9",{"doi":5433},"10.1016\u002F0005-2760(89)90332-9",{"id":26,"text":5435,"url":26,"identifiers":5436},"McGee, 1985, Enzymatic hydration of leukotriene A4. Purification and characterization of a novel epoxide hydrolase from human erythrocytes, J. Biol. Chem., 260, 12832, 10.1016\u002FS0021-9258(17)38953-6",{"doi":5437},"10.1016\u002FS0021-9258(17)38953-6",{"id":26,"text":5439,"url":26,"identifiers":5440},"Rybina, 1997, Regulation of leukotriene A4 hydrolase activity in endothelial cells by phosphorylation, J. Biol. Chem., 272, 31865, 10.1074\u002Fjbc.272.50.31865",{"doi":5441},"10.1074\u002Fjbc.272.50.31865",{"id":26,"text":5443,"url":26,"identifiers":5444},"Haeggstrom, 2000, Structure, function, and regulation of leukotriene A4 hydrolase, Am. J. Respir. Crit. Care Med., 161, S25, 10.1164\u002Fajrccm.161.supplement_1.ltta-6",{"doi":5445},"10.1164\u002Fajrccm.161.supplement_1.ltta-6",{"id":26,"text":5447,"url":26,"identifiers":5448},"Wetterholm, 1994, Zinc and other divalent cations inhibit purified leukotriene A4 hydrolase and leukotriene B4 biosynthesis in human polymorphonuclear leukocytes, Arch. Biochem. Biophys., 311, 263, 10.1006\u002Fabbi.1994.1236",{"doi":5449},"10.1006\u002Fabbi.1994.1236",{"id":26,"text":5451,"url":26,"identifiers":5452},"Yuan, 1993, Development of selective tight-binding inhibitors of leukotriene A4 hydrolase, J. Med. Chem., 36, 211, 10.1021\u002Fjm00054a004",{"doi":5453},"10.1021\u002Fjm00054a004",{"id":26,"text":5455,"url":26,"identifiers":5456},"Andberg, 2000, Leukotriene A4 hydrolase: a critical role of glutamic acid-296 for the binding of bestatin, Biochem. J., 345, 621, 10.1042\u002Fbj3450621",{"doi":5457},"10.1042\u002Fbj3450621",{"id":26,"text":5459,"url":26,"identifiers":5460},"G.M. Habib, A.A. Cuevas, R. Barrios, M.W. Lieberman, Mouse leukotriene A4 hydrolase is expressed at high levels in intestinal crypt cells and splenic lymphocytes, Gene 234 (1999) 249–255.",{"doi":5461},"10.1016\u002FS0378-1119(99)00175-4",{"id":26,"text":5463,"url":26,"identifiers":5464},"Blomster, 1995, Evidence for a catalytic role of tyrosine 383 in the peptidase reaction of leukotriene A4 hydrolase, Eur. J. Biochem., 231, 528, 10.1111\u002Fj.1432-1033.1995.0528d.x",{"doi":5465},"10.1111\u002Fj.1432-1033.1995.0528d.x",{"id":26,"text":5467,"url":26,"identifiers":5468},"Haeggstrom, 1993, Leukotriene A4 hydrolase: structural and functional properties of the active center, J. Lipid Mediat., 6, 1",{},{"id":26,"text":5470,"url":26,"identifiers":5471},"Andberg, 1999, Evidence for a carbocation intermediate in the enzymatic transformation of leukotriene A4 into leukotriene B4, Adv. Exp. Med. Biol., 469, 319, 10.1007\u002F978-1-4615-4793-8_47",{"doi":5472},"10.1007\u002F978-1-4615-4793-8_47",{"id":26,"text":5474,"url":26,"identifiers":5475},"Beetham, 1995, Gene evolution of epoxide hydrolases and recommended nomenclature, DNA Cell Biol., 14, 61, 10.1089\u002Fdna.1995.14.61",{"doi":5476},"10.1089\u002Fdna.1995.14.61",{"id":26,"text":5478,"url":26,"identifiers":5479},"Meijer, 1988, Cytosolic epoxide hydrolase, Chem. Biol. Interact., 64, 207, 10.1016\u002F0009-2797(88)90100-7",{"doi":5480},"10.1016\u002F0009-2797(88)90100-7",{"id":26,"text":5482,"url":26,"identifiers":5483},"Schladt, 1988, Purification and characterization of rat-liver cytosolic epoxide hydrolase, Eur. J. Biochem., 176, 31, 10.1111\u002Fj.1432-1033.1988.tb14247.x",{"doi":5484},"10.1111\u002Fj.1432-1033.1988.tb14247.x",{"id":26,"text":5486,"url":26,"identifiers":5487},"Schladt, 1988, Human liver cytosolic epoxide hydrolases, Eur. J. Biochem., 176, 715, 10.1111\u002Fj.1432-1033.1988.tb14335.x",{"doi":5488},"10.1111\u002Fj.1432-1033.1988.tb14335.x",{"id":26,"text":5490,"url":26,"identifiers":5491},"Beetham, 1993, cDNA cloning and expression of a soluble epoxide hydrolase from human liver, Arch. Biochem. Biophys., 305, 197, 10.1006\u002Fabbi.1993.1411",{"doi":5492},"10.1006\u002Fabbi.1993.1411",{"id":26,"text":5494,"url":26,"identifiers":5495},"Thomas, 1990, Rat and human liver cytosolic epoxide hydrolases: evidence for multiple forms at level of protein and mRNA, Environ. Health Perspect., 88, 49",{},{"id":26,"text":5497,"url":26,"identifiers":5498},"Schladt, 1986, Distribution and inducibility of cytosolic epoxide hydrolase in male Sprague–Dawley rats, Biochem. Pharmacol., 35, 3309, 10.1016\u002F0006-2952(86)90428-4",{"doi":5499},"10.1016\u002F0006-2952(86)90428-4",{"id":26,"text":5501,"url":26,"identifiers":5502},"Arand, 1991, An impaired peroxisomal targeting sequence leading to an unusual bicompartmental distribution of cytosolic epoxide hydrolase, FEBS Lett., 294, 19, 10.1016\u002F0014-5793(91)81333-4",{"doi":5503},"10.1016\u002F0014-5793(91)81333-4",{"id":26,"text":5505,"url":26,"identifiers":5506},"Eriksson, 1991, Studies on the intracellular distributions of soluble epoxide hydrolase and of catalase by digitonin-permeabilization of hepatocytes isolated from control and clofibrate-treated mice, Eur. J. Biochem., 198, 471, 10.1111\u002Fj.1432-1033.1991.tb16037.x",{"doi":5507},"10.1111\u002Fj.1432-1033.1991.tb16037.x",{"id":26,"text":5509,"url":26,"identifiers":5510},"Grant, 1993, Molecular cloning and expression of murine liver soluble epoxide hydrolase, J. Biol. Chem., 268, 17628, 10.1016\u002FS0021-9258(19)85378-4",{"doi":5511},"10.1016\u002FS0021-9258(19)85378-4",{"id":26,"text":5513,"url":26,"identifiers":5514},"Knehr, 1993, Isolation and characterization of a cDNA encoding rat liver cytosolic epoxide hydrolase and its functional expression in Escherichia coli, J. Biol. Chem., 268, 17623, 10.1016\u002FS0021-9258(19)85377-2",{"doi":5515},"10.1016\u002FS0021-9258(19)85377-2",{"id":26,"text":5517,"url":26,"identifiers":5518},"Sandberg, 1996, Structural characterization of the human soluble epoxide hydrolase gene (EPHX2), Biochem. Biophys. Res. Commun., 221, 333, 10.1006\u002Fbbrc.1996.0596",{"doi":5519},"10.1006\u002Fbbrc.1996.0596",{"id":26,"text":5521,"url":26,"identifiers":5522},"Stapleton, 1994, Cloning and expression of soluble epoxide hydrolase from potato, Plant J., 6, 251, 10.1046\u002Fj.1365-313X.1994.6020251.x",{"doi":5523},"10.1046\u002Fj.1365-313X.1994.6020251.x",{"id":26,"text":5525,"url":26,"identifiers":5526},"Vesell, 1991, Genetic factors that regulate cytosolic epoxide hydrolase activity in normal human lymphocytes, Ann. Genet., 34, 167",{},{"id":26,"text":5528,"url":26,"identifiers":5529},"M. Sandberg, C. Hassett, J. Meijer, E.T. Adman, C.J. Omiecinski, Identification and functional characterization of human soluble epoxide hydrolase genetic polymorphisms, J. Biol. Chem. 275 (2000) 28873–28881.",{"doi":5530},"10.1074\u002Fjbc.M001153200",{"id":26,"text":5532,"url":26,"identifiers":5533},"Johansson, 1995, Tissue specific basal expression of soluble murine epoxide hydrolase and effects of clofibrate on the mRNA levels in extrahepatic tissues and liver, Arch. Toxicol., 70, 61, 10.1007\u002Fs002040050250",{"doi":5534},"10.1007\u002Fs002040050250",{"id":26,"text":5536,"url":26,"identifiers":5537},"Lundgren, 1987, Induction of cytosolic and microsomal epoxide hydrolases and proliferation of peroxisomes and mitochondria in mouse liver after dietary exposure to p-chlorophenoxyacetic acid, 2,4-dichlorophenoxyacetic acid and 2,4,5-trichlorophenoxyacetic acid, Biochem. Pharmacol., 36, 815, 10.1016\u002F0006-2952(87)90169-9",{"doi":5538},"10.1016\u002F0006-2952(87)90169-9",{"id":26,"text":5540,"url":26,"identifiers":5541},"Lundgren, 1988, Induction of cytosolic and microsomal epoxide hydrolases in mouse liver by peroxisome proliferators, with special emphasis on structural analogues of 2-ethylhexanoic acid, Chem. Biol. Interact., 68, 219, 10.1016\u002F0009-2797(88)90018-X",{"doi":5542},"10.1016\u002F0009-2797(88)90018-X",{"id":26,"text":5544,"url":26,"identifiers":5545},"B. Lundgren, J.W. DePierre, Proliferation of peroxisomes and induction of cytosolic and microsomal epoxide hydrolases in different strains of mice and rats after dietary treatment with clofibrate, Xenobiotica 19 (1989) 867–881.",{"doi":5546},"10.3109\u002F00498258909043147",{"id":26,"text":5548,"url":26,"identifiers":5549},"Oesch, 1986, Rat cytosolic epoxide hydrolase, Adv. Exp. Med. Biol., 197, 195, 10.1007\u002F978-1-4684-5134-4_16",{"doi":5550},"10.1007\u002F978-1-4684-5134-4_16",{"id":26,"text":5552,"url":26,"identifiers":5553},"Zeldin, 1995, Metabolism of epoxyeicosatrienoic acids by cytosolic epoxide hydrolase: substrate structural determinants of asymmetric catalysis, Arch. Biochem. Biophys., 316, 443, 10.1006\u002Fabbi.1995.1059",{"doi":5554},"10.1006\u002Fabbi.1995.1059",{"id":26,"text":5556,"url":26,"identifiers":5557},"Borhan, 1995, Improved radiolabeled substrates for soluble epoxide hydrolase, Anal. Biochem., 231, 188, 10.1006\u002Fabio.1995.1520",{"doi":5558},"10.1006\u002Fabio.1995.1520",{"id":26,"text":5560,"url":26,"identifiers":5561},"Dietze, 1994, Spectrophotometric substrates for cytosolic epoxide hydrolase, Anal. Biochem., 216, 176, 10.1006\u002Fabio.1994.1023",{"doi":5562},"10.1006\u002Fabio.1994.1023",{"id":26,"text":5564,"url":26,"identifiers":5565},"Nourooz Zadeh, 1992, Characterization of the cytosolic epoxide hydrolase-catalyzed hydration products from 9,10:12,13-diepoxy stearic esters, Arch. Biochem. Biophys., 294, 675, 10.1016\u002F0003-9861(92)90741-E",{"doi":5566},"10.1016\u002F0003-9861(92)90741-E",{"id":26,"text":5568,"url":26,"identifiers":5569},"Zeldin, 1993, Regio- and enantiofacial selectivity of epoxyeicosatrienoic acid hydration by cytosolic epoxide hydrolase, J. Biol. Chem., 268, 6402, 10.1016\u002FS0021-9258(18)53266-X",{"doi":5570},"10.1016\u002FS0021-9258(18)53266-X",{"id":26,"text":5572,"url":26,"identifiers":5573},"Moghaddam, 1997, Bioactivation of leukotoxins to their toxic diols by epoxide hydrolase, Nat. Med., 3, 562, 10.1038\u002Fnm0597-562",{"doi":5574},"10.1038\u002Fnm0597-562",{"id":26,"text":5576,"url":26,"identifiers":5577},"Miyamoto, 1987, Inhibition of epoxide hydrolases and glutathione S-transferases by 2-, 3-, and 4-substituted derivatives of 4′-phenylchalcone and its oxide, Arch. Biochem. Biophys., 254, 203, 10.1016\u002F0003-9861(87)90096-8",{"doi":5578},"10.1016\u002F0003-9861(87)90096-8",{"id":26,"text":5580,"url":26,"identifiers":5581},"Dietze, 1991, Inhibition of cytosolic epoxide hydrolase by trans-3-phenylglycidols, Biochem. Pharmacol., 42, 1163, 10.1016\u002F0006-2952(91)90250-9",{"doi":5582},"10.1016\u002F0006-2952(91)90250-9",{"id":26,"text":5584,"url":26,"identifiers":5585},"Dietze, 1993, Inhibition of epoxide hydrolase from human, monkey, bovine, rabbit and murine liver by trans-3-phenylglycidols, Comp. Biochem. Physiol. B, 104, 309, 10.1016\u002F0305-0491(93)90373-D",{"doi":5586},"10.1016\u002F0305-0491(93)90373-D",{"id":26,"text":5588,"url":26,"identifiers":5589},"Morisseau, 1999, Potent urea and carbamate inhibitors of soluble epoxide hydrolases, Proc. Natl. Acad. Sci. USA, 96, 8849, 10.1073\u002Fpnas.96.16.8849",{"doi":5590},"10.1073\u002Fpnas.96.16.8849",{"id":26,"text":5592,"url":26,"identifiers":5593},"Draper, 1999, Inhibition of soluble and microsomal epoxide hydrolase by zinc and other metals, Toxicol. Sci., 52, 26, 10.1093\u002Ftoxsci\u002F52.1.26",{"doi":5594},"10.1093\u002Ftoxsci\u002F52.1.26",{"id":26,"text":5596,"url":26,"identifiers":5597},"Fisslthaler, 1999, Cytochrome P450 2C is an EDHF synthase in coronary arteries, Nature, 401, 493, 10.1038\u002F46816",{"doi":5598},"10.1038\u002F46816",{"id":26,"text":5600,"url":26,"identifiers":5601},"Fisslthaler, 2000, EDHF: a cytochrome P450 metabolite in coronary arteries, Semin. Perinatol., 24, 15, 10.1016\u002FS0146-0005(00)80048-8",{"doi":5602},"10.1016\u002FS0146-0005(00)80048-8",{"id":26,"text":5604,"url":26,"identifiers":5605},"Weintraub, 1999, Epoxide hydrolases regulate epoxyeicosatrienoic acid incorporation into coronary endothelial phospholipids, Am. J. Physiol., 277, H2098",{},{"id":26,"text":5607,"url":26,"identifiers":5608},"Arand, 1994, Sequence similarity of mammalian epoxide hydrolases to the bacterial haloalkane dehalogenase and other related proteins. Implication for the potential catalytic mechanism of enzymatic epoxide hydrolysis, FEBS Lett., 338, 251, 10.1016\u002F0014-5793(94)80278-5",{"doi":5609},"10.1016\u002F0014-5793(94)80278-5",{"id":26,"text":5611,"url":26,"identifiers":5612},"Pinot, 1995, Molecular and biochemical evidence for the involvement of the Asp-333-His-523 pair in the catalytic mechanism of soluble epoxide hydrolase, J. Biol. Chem., 270, 7968, 10.1074\u002Fjbc.270.14.7968",{"doi":5613},"10.1074\u002Fjbc.270.14.7968",{"id":26,"text":5615,"url":26,"identifiers":5616},"Borhan, 1995, Mechanism of soluble epoxide hydrolase. Formation of an alpha-hydroxy ester-enzyme intermediate through Asp-333, J. Biol. Chem., 270, 26923, 10.1074\u002Fjbc.270.45.26923",{"doi":5617},"10.1074\u002Fjbc.270.45.26923",{"id":26,"text":5619,"url":26,"identifiers":5620},"Arand, 1996, Asp333, Asp495, and His523 form the catalytic triad of rat soluble epoxide hydrolase, J. Biol. Chem., 271, 4223, 10.1074\u002Fjbc.271.8.4223",{"doi":5621},"10.1074\u002Fjbc.271.8.4223",{"id":26,"text":5623,"url":26,"identifiers":5624},"Argiriadi, 1999, Detoxification of environmental mutagens and carcinogens: structure, mechanism and evolution of liver epoxide hydrolase, Proc. Natl. Acad. Sci. USA, 96, 10637, 10.1073\u002Fpnas.96.19.10637",{"doi":5625},"10.1073\u002Fpnas.96.19.10637",{"id":26,"text":5627,"url":26,"identifiers":5628},"M. Shou, F.J. Gonzalez, H.V. Gelboin, Stereoselective epoxidation and hydration at the K-region of polycyclic aromatic hydrocarbons by cDNA-expressed cytochromes P450 1A1, 1A2, and epoxide hydrolase, Biochemistry 35 (1996) 15807–15813.",{"doi":5629},"10.1021\u002Fbi962042z",{"id":26,"text":5631,"url":26,"identifiers":5632},"F.P. Guengerich, Epoxide hydrolase: properties and metabolic roles, Rev. Biochem. Toxicol. 4 (1982) 5–30.",{},{"id":26,"text":5634,"url":26,"identifiers":5635},"Armstrong, 1987, Enzyme-catalyzed detoxication reactions: mechanisms and stereochemistry, CRC Crit. Rev. Biochem., 22, 39, 10.3109\u002F10409238709082547",{"doi":5636},"10.3109\u002F10409238709082547",{"id":26,"text":5638,"url":26,"identifiers":5639},"Omiecinski, 1993, Human peripheral lymphocytes as indicators of microsomal epoxide hydrolase activity in liver and lung, Pharmacogenetics, 3, 150, 10.1097\u002F00008571-199306000-00005",{"doi":5640},"10.1097\u002F00008571-199306000-00005",{"id":26,"text":5642,"url":26,"identifiers":5643},"Papadopoulos, 1994, Purification and initial characterization of microsomal epoxide hydrolase from the human adrenal gland, Biochim. Biophys. Acta, 1206, 253, 10.1016\u002F0167-4838(94)90216-X",{"doi":5644},"10.1016\u002F0167-4838(94)90216-X",{"id":26,"text":5646,"url":26,"identifiers":5647},"Hassett, 1989, Rabbit microsomal epoxide hydrolase: isolation and characterization of the xenobiotic metabolizing enzyme cDNA, Arch. Biochem. Biophys., 271, 380, 10.1016\u002F0003-9861(89)90287-7",{"doi":5648},"10.1016\u002F0003-9861(89)90287-7",{"id":26,"text":5650,"url":26,"identifiers":5651},"Skoda, 1988, Human microsomal xenobiotic epoxide hydrolase. Complementary DNA sequence, complementary DNA-directed expression in COS-1 cells, and chromosomal localization, J. Biol. Chem., 263, 1549, 10.1016\u002FS0021-9258(19)57339-2",{"doi":5652},"10.1016\u002FS0021-9258(19)57339-2",{"id":26,"text":5654,"url":26,"identifiers":5655},"Bulleid, 1986, Microsomal epoxide hydrolase of rat liver. Purification and characterization of enzyme fractions with different chromatographic characteristics, Biochem. J., 233, 607, 10.1042\u002Fbj2330607",{"doi":5656},"10.1042\u002Fbj2330607",{"id":26,"text":5658,"url":26,"identifiers":5659},"C. Hassett, K.B. Robinson, N.B. Beck, C.J. Omiecinski, The human microsomal epoxide hydrolase gene (EPHX1): complete nucleotide sequence and structural characterization, Genomics 23 (1994) 433–442.",{"doi":5660},"10.1006\u002Fgeno.1994.1520",{"id":26,"text":5662,"url":26,"identifiers":5663},"Wilson, 1989, Xenobiotic microsomal epoxide hydrolase: 5′ sequence of the human gene, Biochim. Biophys. Acta, 1008, 357, 10.1016\u002F0167-4781(89)90029-8",{"doi":5664},"10.1016\u002F0167-4781(89)90029-8",{"id":26,"text":5666,"url":26,"identifiers":5667},"Hassett, 1998, Effects of chemical inducers on human microsomal epoxide hydrolase in primary hepatocyte cultures, Biochem. Pharmacol., 55, 1059, 10.1016\u002FS0006-2952(97)00679-5",{"doi":5668},"10.1016\u002FS0006-2952(97)00679-5",{"id":26,"text":5670,"url":26,"identifiers":5671},"A. Astrom, S. Man'er, J.W. DePierre, Induction of liver microsomal epoxide hydrolase, UDP-glucuronyl transferase and cytosolic glutathione transferase in different rodent species by 2-acetylaminofluorene or 3-methylcholanthrene, Xenobiotica 17 (1987) 155–163.",{"doi":5672},"10.3109\u002F00498258709043925",{"id":26,"text":5674,"url":26,"identifiers":5675},"Cho, 1998, Differential induction of rat hepatic microsomal epoxide hydrolase and rGSTA2 by diazines: the role of cytochrome P450 2E1-mediated metabolic activation, Chem. Biol. Interact., 116, 229, 10.1016\u002FS0009-2797(98)00093-3",{"doi":5676},"10.1016\u002FS0009-2797(98)00093-3",{"id":26,"text":5678,"url":26,"identifiers":5679},"Craft, 1988, Induction of microsomal epoxide hydrolase by nitrosamines in rat liver. Effect on messenger ribonucleic acids, Biochem. Pharmacol., 37, 297, 10.1016\u002F0006-2952(88)90732-0",{"doi":5680},"10.1016\u002F0006-2952(88)90732-0",{"id":26,"text":5682,"url":26,"identifiers":5683},"A. Parkinson, P.E. Thomas, D.E. Ryan, W. Levin, T. Fujita, S. Safe, Induction of rat liver microsomal cytochrome P-450 isozymes and epoxide hydrolase by a series of 4′-substituted-2,3,4,5-tetrachlorobiphenyls, Toxicology 53 (1988) 289–300.",{"doi":5684},"10.1016\u002F0300-483X(88)90221-1",{"id":26,"text":5686,"url":26,"identifiers":5687},"Bell, 1990, Glucocorticoid repression and basal regulation of the epoxide hydrolase promoter, Arch. Biochem. Biophys., 279, 363, 10.1016\u002F0003-9861(90)90503-Q",{"doi":5688},"10.1016\u002F0003-9861(90)90503-Q",{"id":26,"text":5690,"url":26,"identifiers":5691},"Gaedigk, 1994, Characterization of the microsomal epoxide hydrolase gene in patients with anticonvulsant adverse drug reactions, Pharmacogenetics, 4, 142, 10.1097\u002F00008571-199406000-00005",{"doi":5692},"10.1097\u002F00008571-199406000-00005",{"id":26,"text":5694,"url":26,"identifiers":5695},"Hassett, 1994, Human microsomal epoxide hydrolase: genetic polymorphism and functional expression in vitro of amino acid variants, Hum. Mol. Genet., 3, 421, 10.1093\u002Fhmg\u002F3.3.421",{"doi":5696},"10.1093\u002Fhmg\u002F3.3.421",{"id":26,"text":5698,"url":26,"identifiers":5699},"Laurenzana, 1998, Post-transcriptional regulation of human microsomal epoxide hydrolase, Pharmacogenetics, 8, 157, 10.1097\u002F00008571-199804000-00008",{"doi":5700},"10.1097\u002F00008571-199804000-00008",{"id":26,"text":5702,"url":26,"identifiers":5703},"Hassett, 1997, Human hepatic microsomal epoxide hydrolase: comparative analysis of polymorphic expression, Arch. Biochem. Biophys., 337, 275, 10.1006\u002Fabbi.1996.9794",{"doi":5704},"10.1006\u002Fabbi.1996.9794",{"id":26,"text":5706,"url":26,"identifiers":5707},"S. Raaka, C. Hassett, C.J. Omiencinski, Human microsomal epoxide hydrolase: 5′-flanking region genetic polymorphisms, Carcinogenesis 19 (1998) 387–393.",{"doi":5708},"10.1093\u002Fcarcin\u002F19.3.387",{"id":26,"text":5710,"url":26,"identifiers":5711},"M.W. Himmelstein, M.J. Turner, B. Asgharian, J.A. Bond, Comparison of blood concentrations of 1,3-butadiene and butadiene epoxides in mice and rats exposed to 1,3-butadiene by inhalation, Carcinogenesis 15 (1994) 1479–1486.",{"doi":5712},"10.1093\u002Fcarcin\u002F15.8.1479",{"id":26,"text":5714,"url":26,"identifiers":5715},"Krause, 1997, Oxidation of butadiene monoxide to meso- and (+\u002F−)-diepoxybutane by cDNA-expressed human cytochrome P450s and by mouse, rat, and human liver microsomes: evidence for preferential hydration of meso-diepoxybutane in rat and human liver microsomes, Arch. Biochem. Biophys., 337, 176, 10.1006\u002Fabbi.1996.9781",{"doi":5716},"10.1006\u002Fabbi.1996.9781",{"id":26,"text":5718,"url":26,"identifiers":5719},"Krause, 1997, Epoxide hydrolase-dependent metabolism of butadiene monoxide to 3-butene-1,2-diol in mouse, rat, and human liver, Drug Metab. Dispos., 25, 1013",{},{"id":26,"text":5721,"url":26,"identifiers":5722},"Snyder, 1993, Toxicol. Appl. Pharmacol., 122, 172, 10.1006\u002Ftaap.1993.1185",{"doi":5723},"10.1006\u002Ftaap.1993.1185",{"id":26,"text":5725,"url":26,"identifiers":5726},"A.B. Lindstrom, K. Yeowell-O'Connell, S. Waidyanatha, B.T. Golding, V.R. Tornero, S.M. Rappaport, Measurement of benzene oxide in the blood of rats following administration of benzene, Carcinogenesis 18 (1997) 1637–1641.",{"doi":5727},"10.1093\u002Fcarcin\u002F18.8.1637",{"id":26,"text":5729,"url":26,"identifiers":5730},"Guengerich, 1998, Activation and detoxication of aflatoxin B1, Mutat. Res., 402, 121, 10.1016\u002FS0027-5107(97)00289-3",{"doi":5731},"10.1016\u002FS0027-5107(97)00289-3",{"id":26,"text":5733,"url":26,"identifiers":5734},"Guengerich, 1999, Kinetics of hydrolysis and reaction of aflatoxin B1 exo-8,9-epoxide and relevance to toxicity and detoxication, Drug Metab. Rev., 31, 141, 10.1081\u002FDMR-100101911",{"doi":5735},"10.1081\u002FDMR-100101911",{"id":26,"text":5737,"url":26,"identifiers":5738},"J.M. Walters, R.D. Combes, Activation of benzo[a]pyrene and aflatoxin B1 to mutagenic chemical species by microsomal preparations from rat liver and small intestine in relation to microsomal epoxide hydrolase, Mutagenesis 1 (1986) 45–48.",{"doi":5739},"10.1093\u002Fmutage\u002F1.1.45",{"id":26,"text":5741,"url":26,"identifiers":5742},"H. Glatt, C. Wameling, S. Elsberg, H. Thomas, H. Marquardt, A. Hewer, D.H. Phillips, F. Oesch, A. Seidel, Genotoxicity characteristics of reverse diol-epoxides of chrysene, Carcinogenesis 14 (1993) 11–19.",{"doi":5743},"10.1093\u002Fcarcin\u002F14.1.11",{"id":26,"text":5745,"url":26,"identifiers":5746},"Yang, 1987, Stereoselective formations of K-region and non-K-region epoxides in the metabolism of chrysene by rat liver microsomal cytochrome P-450 isozymes, Mol. Pharmacol., 32, 73",{},{"id":26,"text":5748,"url":26,"identifiers":5749},"R.H. Heflich, J.R. Thornton Manning, T. Kinouchi, F.A. Beland, Mutagenicity of oxidized microsomal metabolites of 1-nitropyrene in Chinese hamster ovary cells, Multagenesis 5 (1990) 151–157.",{"doi":5750},"10.1093\u002Fmutage\u002F5.2.151",{"id":26,"text":5752,"url":26,"identifiers":5753},"van Bladeren, 1985, Differential stereoselectivity of cytochromes P-450b and P-450c in the formation of naphthalene and anthracene 1,2-oxides. The role of epoxide hydrolase in determining the enantiomer composition of the 1,2-dihydrodiols formed, J. Biol. Chem., 260, 10226, 10.1016\u002FS0021-9258(17)39235-9",{"doi":5754},"10.1016\u002FS0021-9258(17)39235-9",{"id":26,"text":5756,"url":26,"identifiers":5757},"M. Hall, D.K. Parker, A.J. Hewer, D.H. Phillips, P.L. Grover, Further metabolism of diol-epoxides of chrysene and dibenz[a,c]anthracene to DNA binding species as evidenced by 32P-postlabelling analysis, Carcinogenesis 9 (1988) 865–868.",{"doi":5758},"10.1093\u002Fcarcin\u002F9.5.865",{"id":26,"text":5760,"url":26,"identifiers":5761},"Miyata, 1999, Targeted disruption of the microsomal epoxide hydrolase gene. Microsomal epoxide hydrolase is required for the carcinogenic activity of 7,12-dimethylbenz[a]anthracene, J. Biol. Chem., 274, 23963, 10.1074\u002Fjbc.274.34.23963",{"doi":5762},"10.1074\u002Fjbc.274.34.23963",{"id":26,"text":5764,"url":26,"identifiers":5765},"Bellucci, 1994, Kinetics and stereochemistry of the microsomal epoxide hydrolase-catalyzed hydrolysis of cis-stilbene oxides, Chirality, 6, 577, 10.1002\u002Fchir.530060711",{"doi":5766},"10.1002\u002Fchir.530060711",{"id":26,"text":5768,"url":26,"identifiers":5769},"Kitteringham, 1996, Interindividual and interspecies variation in hepatic microsomal epoxide hydrolase activity: studies with cis-stilbene oxide, carbamazepine 10, 11-epoxide and naphthalene, J. Pharmacol. Exp. Ther., 278, 1018",{},{"id":26,"text":5771,"url":26,"identifiers":5772},"Moody, 1987, Purification of microsomal epoxide hydrolase from liver of rhesus monkey: partial separation of cis- and trans-stilbene oxide hydrolase, Arch. Biochem. Biophys., 258, 156, 10.1016\u002F0003-9861(87)90332-8",{"doi":5773},"10.1016\u002F0003-9861(87)90332-8",{"id":26,"text":5775,"url":26,"identifiers":5776},"Carlson, 1998, Metabolism of styrene oxide to styrene glycol by mouse liver and lung, J. Toxicol. Environ. Health, 53, 19, 10.1080\u002F009841098159448",{"doi":5777},"10.1080\u002F009841098159448",{"id":26,"text":5779,"url":26,"identifiers":5780},"Gadberry, 1996, Pneumotoxicity and hepatotoxicity of styrene and styrene oxide, J. Toxicol. Environ. Health, 48, 273, 10.1080\u002F009841096161339",{"doi":5781},"10.1080\u002F009841096161339",{"id":26,"text":5783,"url":26,"identifiers":5784},"Herrero, 1997, Recombinant expression of human microsomal epoxide hydrolase protects V79 Chinese hamster cells from styrene oxide- but not from ethylene oxide-induced DNA strand breaks, Environ. Mol. Mutagen., 30, 429, 10.1002\u002F(SICI)1098-2280(1997)30:4\u003C429::AID-EM8>3.0.CO;2-D",{"doi":5785},"10.1002\u002F(SICI)1098-2280(1997)30:4\u003C429::AID-EM8>3.0.CO;2-D",{"id":26,"text":5787,"url":26,"identifiers":5788},"Hartsfield, 1995, Phenytoin embryopathy: effect of epoxide hydrolase inhibitor on phenytoin exposure in utero in C57BL\u002F6J mice, Biochem. Mol. Med., 56, 131, 10.1006\u002Fbmme.1995.1068",{"doi":5789},"10.1006\u002Fbmme.1995.1068",{"id":26,"text":5791,"url":26,"identifiers":5792},"Riley, 1988, An in vitro study of the microsomal metabolism and cellular toxicity of phenytoin, sorbinil and mianserin, Br. J. Clin. Pharmacol., 26, 577, 10.1111\u002Fj.1365-2125.1988.tb05298.x",{"doi":5793},"10.1111\u002Fj.1365-2125.1988.tb05298.x",{"id":26,"text":5795,"url":26,"identifiers":5796},"Van Dyke, 1991, Differences in phenytoin biotransformation and susceptibility to congenital malformations: a review, DICP, 25, 987, 10.1177\u002F106002809102500914",{"doi":5797},"10.1177\u002F106002809102500914",{"id":26,"text":5799,"url":26,"identifiers":5800},"Bellucci, 1987, The metabolism of carbamazepine in humans: steric course of the enzymatic hydrolysis of the 10,11-epoxide, J. Med. Chem., 30, 768, 10.1021\u002Fjm00388a004",{"doi":5801},"10.1021\u002Fjm00388a004",{"id":26,"text":5803,"url":26,"identifiers":5804},"Eugster, 1991, Heterologous expression of human microsomal epoxide hydrolase in Saccharomyces cerevisiae. Study of the valpromide–carbamazepine epoxide interaction, Biochem. Pharmacol., 42, 1367, 10.1016\u002F0006-2952(91)90447-D",{"doi":5805},"10.1016\u002F0006-2952(91)90447-D",{"id":26,"text":5807,"url":26,"identifiers":5808},"Vogel, 1982, Endogenous role of microsomal epoxide hydrolase. Ontogenesis, induction inhibition, tissue distribution, immunological behaviour and purification of microsomal epoxide hydrolase with 16α, 17α-epoxyandrostene-3-one as substrate, Eur. J. Biochem., 126, 425, 10.1111\u002Fj.1432-1033.1982.tb06797.x",{"doi":5809},"10.1111\u002Fj.1432-1033.1982.tb06797.x",{"id":26,"text":5811,"url":26,"identifiers":5812},"Papadopoulos, 1985, Subcellular distribution, catalytic properties and partial purification of epoxide hydrolase in the human adrenal gland, Chem. Biol. Interact., 55, 249, 10.1016\u002FS0009-2797(85)80133-2",{"doi":5813},"10.1016\u002FS0009-2797(85)80133-2",{"id":26,"text":5815,"url":26,"identifiers":5816},"Prestwich, 1985, Cyclopropyl oxiranes: reversible inhibitors of cytosolic and microsomal epoxide hydrolases, Arch. Biochem. Biophys., 237, 361, 10.1016\u002F0003-9861(85)90288-7",{"doi":5817},"10.1016\u002F0003-9861(85)90288-7",{"id":26,"text":5819,"url":26,"identifiers":5820},"Leeder, 1992, Human anti-cytochrome P450 antibodies in aromatic anticonvulsant-induced hypersensitivity reactions, J. Pharmacol. Exp. Ther., 263, 360",{},{"id":26,"text":5822,"url":26,"identifiers":5823},"Shear, 1988, Anticonvulsant hypersensitivity syndrome. In vitro assessment of risk, J. Clin. Invest., 82, 1826, 10.1172\u002FJCI113798",{"doi":5824},"10.1172\u002FJCI113798",{"id":26,"text":5826,"url":26,"identifiers":5827},"Green, 1995, Genetic analysis of microsomal epoxide hydrolase in patients with carbamazepine hypersensitivity, Biochem. Pharmacol., 50, 1353, 10.1016\u002F0006-2952(95)02009-8",{"doi":5828},"10.1016\u002F0006-2952(95)02009-8",{"id":26,"text":5830,"url":26,"identifiers":5831},"Leeder, 1996, Epitope mapping studies with human anti-cytochrome P450 3A antibodies, Mol. Pharmacol., 49, 234",{},{"id":26,"text":5833,"url":26,"identifiers":5834},"Benhamou, 1998, Association between lung cancer and microsomal epoxide hydrolase genotypes, Cancer Res., 58, 5291",{},{"id":26,"text":5836,"url":26,"identifiers":5837},"Hulla, 1999, Symposium overview: the role of genetic polymorphism and repair deficiencies in environmental disease, Toxicol. Sci., 47, 135, 10.1093\u002Ftoxsci\u002F47.2.135",{"doi":5838},"10.1093\u002Ftoxsci\u002F47.2.135",{"id":26,"text":5840,"url":26,"identifiers":5841},"Lin, 2000, Association of CYP1A1 and microsomal epoxide hydrolase polymorphisms with lung squamous cell carcinoma, Br. J. Cancer, 82, 852, 10.1054\u002Fbjoc.1999.1011",{"doi":5842},"10.1054\u002Fbjoc.1999.1011",{"id":26,"text":5844,"url":26,"identifiers":5845},"Harrison, 1999, Microsomal epoxide hydrolase gene polymorphism and susceptibility to colon cancer, Br. J. Cancer, 79, 168, 10.1038\u002Fsj.bjc.6690028",{"doi":5846},"10.1038\u002Fsj.bjc.6690028",{"id":26,"text":5848,"url":26,"identifiers":5849},"Hengstler, 1998, Polymorphisms of N-acetyltransferases, glutathione S-transferases, microsomal epoxide hydrolase and sulfotransferases: influence on cancer susceptibility, Recent Results Cancer Res., 154, 47, 10.1007\u002F978-3-642-46870-4_4",{"doi":5850},"10.1007\u002F978-3-642-46870-4_4",{"id":26,"text":5852,"url":26,"identifiers":5853},"L.T. Laughlin, H.F. Tzeng, S. Lin, R.N. Armstrong, Mechanism of microsomal epoxide hydrolase, semifunctional site-specific mutants affecting the alkylation half-reaction, Biochemistry 37 (1998) 2897–2904.",{"doi":5854},"10.1021\u002Fbi972737f",{"id":26,"text":5856,"url":26,"identifiers":5857},"Arand, 1999, Catalytic triad of microsomal epoxide hydrolase: replacement of Glu404 with Asp leads to a strongly increased turnover rate, Biochem. J., 337, 37, 10.1042\u002Fbj3370037",{"doi":5858},"10.1042\u002Fbj3370037",{"id":26,"text":5860,"url":26,"identifiers":5861},"Bell, 1993, Expression of rat microsomal epoxide hydrolase in Escherichia coli. Identification of a histidyl residue essential for catalysis, J. Biol. Chem., 268, 14011, 10.1016\u002FS0021-9258(19)85202-X",{"doi":5862},"10.1016\u002FS0021-9258(19)85202-X",{"id":26,"text":5864,"url":26,"identifiers":5865},"Lacourciere, 1994, Microsomal and soluble epoxide hydrolases are members of the same family of CX bond hydrolase enzymes, Chem. Res. Toxicol., 7, 121, 10.1021\u002Ftx00038a001",{"doi":5866},"10.1021\u002Ftx00038a001",{"id":26,"text":5868,"url":26,"identifiers":5869},"Arand, 1999, Cloning and molecular characterization of a soluble epoxide hydrolase from Aspergillus niger that is related to mammalian microsomal epoxide hydrolase, Biochem. J., 344, 273, 10.1042\u002Fbj3440273",{"doi":5870},"10.1042\u002Fbj3440273",{"id":26,"text":5872,"url":26,"identifiers":5873},"Zou, 2000, Structure of Aspergillus niger epoxide hydrolase at 1.8 A resolution: implications for the structure and function of the mammalian microsomal class of epoxide hydrolases. Structure, Fold Des., 8, 111, 10.1016\u002FS0969-2126(00)00087-3",{"doi":5874},"10.1016\u002FS0969-2126(00)00087-3"]