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Journal of Medicine and Pharmacy","Tạp chí Y Dược học Cần Thơ",{"EN":487,"VI":488},"\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">04\u002F10\u002F2015 Ministry of Information and Communications allowed Can Tho journal of medicine and pharmacy to operate (102 \u002FGP-BTTTT)\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">07\u002F16\u002F2015 Can Tho journal of medicine and pharmacy is internationally recognized: ISSN 2354-1210\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">In 2016, The journal has been included in the list of medical science journals by The State Council for professorship which is awarded a work score of 0-0.5 points for a published article.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Can Tho Journal of Medicine and Pharmacy welcome original works that haven’t been submitted or published in other medical journals. Posts must contain content related to one of the journal’s categories.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">The content published\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">The journal is divided into 3 categories:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Scientific research article: are valuable scientific works, which have been researched and accepted.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Overview of medicine, biology and pharmacy: serving the objective of continuing training in the fields of medicine, biology and pharmacy; to systematize classical and modern knowledge.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Update information on new knowledge about medicine, biology, pharmacy in the country and in the world.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Scope\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Publication and introduction of scientific research in the fields:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">+ Medicine (internal medicine, surgery, pediatrics, obstetrics and gynecology, odonto-stomatology, laboratory, oncology, traditional medicine, nursing).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">+ Biology (genetics, biotechnology).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">+ Pharmacology (pharmaceutics, drug quality analysis-control, synthetic pharmaceutical chemistry, biochemistry, pharmacognosy, botany, clinical pharmacy).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- To enhance the quality of undergraduate, postgraduate education, scientifically researching and meet the necessary treatment in hospital.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Introducing the updated domestic and oversea information about science technology to promote scientific research and exchanging technology in local, other universities.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Exchanging pharmaceutical and medical information for social health developing in the Mekong Delta and Vietnam.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">The object\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Postgraduate students, student of Can Tho University of Medicine and Pharmacy, scientists from schools, research institutes, hospitals, health centers, pharmaceutical companies of the Mekong Delta; 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. Danh sách bài báo theo số Tạp chí được in ấn và phát hành trong năm định kỳ được công bố chính thức trên website: https:\u002F\u002Ftapchi.ctump.edu.vn\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>",{"VOID":490},"wcQ1uqwAAAAJ","2023-05-30T08:17:21.868+00:00",[],[494],{"id":495,"createTime":28,"updateTime":28,"relativeEntities":496,"slug":28,"properties":497,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":507,"parentIds":508,"statistic":28},"6413896b-eca9-442b-a73f-182a58a0ce40",[],{"title":498,"address":501,"country":504,"abbreviation":505},{"EN":499,"VI":500},"Can Tho University of Medicine and Pharmacy","Trường Đại học Y Dược Cần Thơ",{"EN":502,"VI":503},"No 179, Nguyen Van Cu street, An Khanh ward, Ninh Kieu district, Can Tho city, Vietnam","Số 179, đường Nguyễn Văn Cừ, phường An Khánh, quận Ninh Kiều, thành phố Cần Thơ, Việt Nam",{"VOID":15},{"VOID":506},"ctump","http:\u002F\u002Fwww.ctump.edu.vn\u002F",[],[],"https:\u002F\u002Ftapchi.ctump.edu.vn\u002Findex.php\u002Fctump",{"impactFactor":32,"impactFactorByYear":512,"i10Index":32,"i10IndexLast5Year":32,"totalPublication":514,"totalPublicationByYear":515,"totalCitation":520,"totalCitationByYear":521,"totalCitationPerPublication":108,"totalCitationPerPublicationByYear":523,"hindexLast5Year":45,"hindex":45},{"2022":513,"2023":111,"2024":106},0.01,1556,{"2020":47,"2021":516,"2022":517,"2023":518,"2024":519,"2025":122},57,306,801,358,161,{"2021":146,"2022":280,"2023":522},99,{"2021":524,"2022":318,"2023":104},0.23,{"impactFactor":28,"impactFactorByYear":28,"i10Index":123,"i10IndexLast5Year":123,"totalPublication":526,"totalPublicationByYear":527,"totalCitation":526,"totalCitationByYear":528,"totalCitationPerPublication":40,"totalCitationPerPublicationByYear":531,"hindexLast5Year":49,"hindex":49},476,{"0":205,"2019":123,"2021":139,"2022":459,"2023":451,"2024":357,"2025":49,"2026":48},{"2021":42,"2022":123,"2023":161,"2024":529,"2025":360,"2026":530},136,83,{"2021":105,"2022":513,"2023":532,"2024":127,"2025":533,"2026":534},0.62,25.43,13.83,{"id":536,"createTime":537,"updateTime":382,"relativeEntities":538,"slug":539,"properties":540,"entityType":25,"verifyStatus":26,"verifyTime":28,"verifyNote":28,"languages":552,"translateLanguages":28,"viewCount":133,"subjectFields":553,"manageAffiliations":554,"indexDatabases":555,"url":556,"thumbnailPath":557,"statistic":558,"gsStatistic":594,"type":55,"analyzePriority":28},"6984a56a-db70-403b-9cc4-4013e1ceaffa","2023-05-09T06:47:40.346+00:00",[],"T%E1%BA%A1p%20ch%C3%AD%20Nghi%C3%AAn%20c%E1%BB%A9u%20n%C6%B0%E1%BB%9Bc%20ngo%C3%A0i",{"country":541,"issn":542,"title":544,"introduce":547,"gsId":550},{"VOID":15},{"VOID":543},"25252445",{"EN":545,"VI":546},"VNU Journal of Foreign Studies","Tạp chí Nghiên cứu nước ngoài",{"EN":548,"VI":549},"{\"ops\":[{\"insert\":\"\\n\\nThe \\n\"},{\"attributes\":{\"italic\":true},\"insert\":\"VNU Journal of Science\"},{\"insert\":\"\\n was established in 1985 for the publication of national and international research papers in all fields of natural sciences and technology, social sciences and humanities. 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is a toxic metal and poses a high environmental risk to animals and humans, alike. It is thus pertinent to search for medicinal plants in protecting against cadmium toxicity. This study aims at investigating the ability of aqueous extract of Persea americana seeds (AEPA) in ameliorating the toxic effects of cadmium in the kidneys of cadmium-exposed Wistar rats. Male Wistar rats were grouped into five, of six animals each. Different groups of animals received normal saline (control group), 200 mg\u002Fkg body weight AEPA, 400 mg\u002Fkg AEPA, and standard drug, Livolin Forte, respectively. A last group of animals was left untreated. To induce toxicity, all animals, except the control group, were exposed to cadmium (200 mg\u002FL, as CdCl2) in their main drinking water for 21 days. Biochemical analysis of serum kidney markers, oxidative stress and antioxidant status, as well as anti-inflammatory activities, was done using standard methods and kits. In silico analysis was performed on phytochemicals reported to be abundant in AEPA. Treatment with 400 mg\u002Fkg AEPA significantly reversed (P ≤ 0.05) the adverse effect of cadmium on serum creatinine, urea, uric acid and blood urea nitrogen, and restored (P ≤ 0.05) antioxidant status, evidenced by its significant effect on superoxide dismutase, catalase, glutathione-S-transferase, glutathione peroxidase, reduced glutathione, and lipid peroxidation activities. AEPA, at 400 mg\u002Fkg also exhibited significant anti-inflammatory effects, which was shown by reduced interleukin-2 and tumour necrosis factor α activities. Molecular docking of phytochemicals with the selected protein target also confirmed the therapeutic potential of AEPA. The study concluded that aqueous extract of AEPA protects against cadmium-induced kidney toxicity and inflammation.",{"EN":1036},"Nephroprotective and anti-inflammatory potential of aqueous extract from Persea americana seeds against cadmium-induced nephrotoxicity in Wistar rats",{"VOID":1038},"Abarikwu SO, Adebayo OL, Otuechere CA, Iserhienrhien BO, Badejo TA (2016) Selenium and rutin alone or in combination do not have stronger protective effects than their separate effects against cadmium-induced renal damage. Pharm Biol 54:896–904\nAdaramola B, Onigbinde A, Shokunbi O (2016) Physiochemical properties and antioxidant potential of Persea Americana seed oil. Chem Int 2:168–175\nAdaramoye OA, Akanni OO (2016) Modulatory effects of methanol extract of Artocarpus altilis (Moraceae) on cadmium-induced hepatic and renal toxicity in male Wistar rats. Pathophysiology 23:1–9\nAdi PJ, Burra SP, Vataparti AR, Matcha B (2016) Calcium, zinc and vitamin E ameliorate cadmium-induced renal oxidative damage in albino Wistar rats. Toxicol Rep 3:591–597\nAli S, Hussain S, Khan R, Mumtaz S, Ashraf N, Andleeb S, Shakir HA, Tahir HM, Khan MKA, Ulhaq M (2019) Renal toxicity of heavy metals (cadmium and mercury) and their amelioration with ascorbic acid in rabbits. Environ Sci Pollut Res 26:3909–3920\nAlkhalaf MI, Alansari WS, Ibrahim EA, ELhalwagy ME (2019) Anti-oxidant, anti-inflammatory and anti-cancer activities of avocado (Persea americana) fruit and seed extract. J King Saud Univ Sci 31:1358–1362\nAnsari MA, Raish M, Ahmad A, Alkharfy KM, Ahmad SF, Attia SM, Alsaad AMS, Bakheet SA (2017) Sinapic acid ameliorate cadmium-induced nephrotoxicity: In vivo possible involvement of oxidative stress, apoptosis, and inflammation via NF-κB downregulation. Environ Toxicol Pharmacol 51:100–107\nATSDR (2019) ATSDR’s substance priority list. CDC, Atlanta\nBabaknejad N, Moshtaghie AA, Nayeri H, Hani M, Bahrami S (2016) Protective role of zinc and magnesium against cadmium nephrotoxicity in male Wistar rats. Biol Trace Elem Res 174:112–120\nBartels H, Böhmer M, Heierli C (1972) Serum creatinine determination without protein precipitation. Clin Chim Acta 37:193–197\nBhuyan DJ, Alsherbiny MA, Perera S, Low M, Basu A, Devi OA, Barooah MS, Li CG, Papoutsis K (2019) The odyssey of bioactive compounds in avocado (Persea americana) and their health benefits. Antioxidants 8:426\nBove M, Cicero AFG, Borghi C (2017) The Effect of xanthine oxidase inhibitors on blood pressure and renal function. Curr Hypertens Rep 19:95\nBrzóska MM, Kamiński M, Dziki M, Moniuszko-Jakoniuk J (2004) Changes in the structure and function of the kidney of rats chronically exposed to cadmium. II. Histoenzymatic studies. Arch Toxicol 78:226–231\ndel Refugio Ramos M, Jerz G, Villanueva S, López-Dellamary F, Waibel R, Winterhalter P (2004) Two glucosylated abscisic acid derivates from avocado seeds (Persea americana Mill. Lauraceae cv. Hass). Phytochemistry 65:955–962\nDita MRA, Mukono IS, Rochmanti M (2019) Combination effect of the extract of avocado leaf and seed (Persea americana) on level of total cholesterol, LDL, and HDL in Mice (Mus musculus) with hypercholesterolemia. Biomol Health Sci J 2:44–47\nDkhil MA, Al-Quraishy S, Diab MMS, Othman MS, Aref AM, Abdel Moneim AE (2014) The potential protective role of Physalis peruviana L. fruit in cadmium-induced hepatotoxicity and nephrotoxicity. Food Chem Toxicol 74:98–106\nDkhil MA, Diab MSM, Lokman MS, El-Sayed H, Bauomy AA, Al-Shaebi EM, Al-Quraishy S (2020) Nephroprotective effect of Pleurotus ostreatus extract against cadmium chloride toxicity in rats. An Acad Bras Ciênc. https:\u002F\u002Fdoi.org\u002F10.1590\u002F0001-3765202020191121\nDraper HH, Hadley M (1990) Malondialdehyde determination as index of lipid Peroxidation. In: Methods enzymol. Academic Press, pp 421–431\nEjiofor C, Ezeagu I, Ayoola M (2018a) Hypoglycaemic and Biochemical effects of the aqueous and methanolic extract of Persea americana seeds on alloxan-induced albino rats. Eur J Med Plants 26:1–12\nEjiofor N, Ezeagu I, Ayoola M, Umera E (2018b) Determination of the chemical composition of avocado (Persea americana) seed. Adv Food Technol Nutr Sci SE:S51–S55\nEl-Boshy ME, Risha EF, Abdelhamid FM, Mubarak MS, Hadda TB (2015) Protective effects of selenium against cadmium induced hematological disturbances, immunosuppressive, oxidative stress and hepatorenal damage in rats. J Trace Elem Med Biol 29:104–110\nFawcett JK, Scott JE (1960) A rapid and precise method for the determination of urea. J Clin Pathol 13:156–159\nJahan S, Zahra A, Irum U, Iftikhar N, Ullah H (2014) Protective effects of different antioxidants against cadmium induced oxidative damage in rat testis and prostate tissues. Syst Biol Reprod Med 60:199–205\nJan AT, Azam M, Siddiqui K, Ali A, Choi I, Haq QMR (2015) Heavy metals and human health: mechanistic insight into toxicity and counter defense system of antioxidants. Int J Mol Sci 16:29592–29630\nJiménez-Arellanes A, Luna-Herrera J, Ruiz-Nicolás R, Cornejo-Garrido J, Tapia A, Yépez-Mulia L (2013) Antiprotozoal and antimycobacterial activities of Persea americana seeds. BMC Comp Altern Med 13:1–5\nJin X, Jia T, Liu R, Xu S (2018) The antagonistic effect of selenium on cadmium-induced apoptosis via PPAR-γ\u002FPI3K\u002FAkt pathway in chicken pancreas. J Hazard Mater 357:355–362\nKhaliq T, Mumtaz F, Javed I, Iftikhar A (2015) Nephroprotective potential of Rosa damascena Mill flowers, Cichorium intybus Linn roots and their mixtures on Gentamicin-induced toxicity in albino rabbits. Pak Vet J 35:43–47\nLacerda LG, da Silva Carvalho Filho MA, Bauab T, Demiate IM, Colman TAD, Andrade MMP, Schnitzler E (2015) The effects of heat-moisture treatment on avocado starch granules. J Therm Anal Calorim 120:387–393\nLiu L, Yang B, Cheng Y, Lin H (2015) Ameliorative effects of selenium on cadmium-induced oxidative stress and endoplasmic reticulum stress in the chicken kidney. Biol Trace Elem Res 167:308–319\nLiu J, Zhou H, Song L, Yang Z, Qiu M, Wang J, Shi S (2021) Anthocyanins: promising natural products with diverse pharmacological activities. Molecules 26:3807\nLuo Y, Zheng SG (2016) Hall of fame among pro-inflammatory cytokines: Interleukin-6 gene and its transcriptional regulation mechanisms. Front Immunol 7:604\nMakelele FB, Mukweke NL, Chasinge T, Murhula PH, Kadima JN (2020) Antiulcer effect of Persea americana seed against alcohol-induced peptic ulcer in guinea pig. J Pharmacogn Phytochem 9:1244–1249\nMorales AI, Vicente-Sánchez C, Sandoval JMS, Egido J, Mayoral P, Arévalo MA, Fernández-Tagarro M, López-Novoa JM, Pérez-Barriocanal F (2006) Protective effect of quercetin on experimental chronic cadmium nephrotoxicity in rats is based on its antioxidant properties. Food Chem Toxicol 44:2092–2100\nMorsy MA, Ibrahim SA, Amin EF, Kamel MY, Rifaai RA, Hassan MK (2013) Curcumin ameliorates methotrexate-induced nephrotoxicity in rats. Adv Pharmacol Sci 2013:387071–387071\nNwozo SO, Oyinloye BE (2011) Hepatoprotective effect of aqueous extract of Aframomum melegueta on ethanol-induced toxicity in rats. Acta Biochim Pol 58:355–358\nOjo OA, Ajiboye BO, Oyinloye BE, Ojo AB, Olarewaju OI (2014) Protective effect of Irvingia gabonensis stem bark extract on cadmiuminduced nephrotoxicity in rats. Interdiscip Toxicol 7:208–214\nOlubunmi OP, Yinka OS, Oladele OJ, Olubusayo FA, Afees OJ (2016) An assessment of renal function parameters on the ameliorative properties of Ginkgo biloba extract in cadmium-induced nephrotoxicity in adult Wistar rats model. Am J Clin Exp Med 4:112–117\nOrororo O, Asagba S, Tonukari N, Okandeji O, Mbanugo J (2018) Effects of Hibiscus Sabdarrifa L. anthocyanins on cadmium-induced oxidative stress in Wistar rats. J Appl Sci Environ Manag 22:465–470\nOyinloye BE, Adenowo AF, Osunsanmi FO, Ogunyinka BI, Nwozo SO, Kappo AP (2016) Aqueous extract of Monodora myristica ameliorates cadmium-induced hepatotoxicity in male rats. Springerplus 5:641\nRajakrishnan R, Lekshmi R, Benil PB, Thomas J, AlFarhan AH, Rakesh V, Khalaf S (2017) Phytochemical evaluation of roots of Plumbago zeylanica L. and assessment of its potential as a nephroprotective agent. Saudi J Biol Sci 24:760–766\nRaymond Chia TW, Dykes GA (2010) Antimicrobial activity of crude epicarp and seed extracts from mature avocado fruit (Persea americana) of three cultivars. Pharm Biol 48:753–756\nSatarug S, Garrett Scott H, Sens Mary A, Sens Donald A (2010) Cadmium, environmental exposure, and health outcomes. Environ Health Perspect 118:182–190\nTabeshpour J, Razavi BM, Hosseinzadeh H (2017) Effects of avocado (Persea americana) on metabolic syndrome: a comprehensive systematic review. Phytother Res 31:819–837\nThévenod F, Wolff NA (2016) Iron transport in the kidney: implications for physiology and cadmium nephrotoxicity. Metallomics 8:17–42\nTrott O, Olson AJ (2010) AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 31:455–461\nVeljkovic AR, Nikolic RS, Kocic GM, Pavlovic DD, Cvetkovic TP, Sokolovic DT, Jevtovic TM, Basic JT, Laketic DM, Marinkovic MR et al (2012) Protective effects of glutathione and lipoic acid against cadmium-induced oxidative stress in rat’s kidney. Ren Fail 34:1281–1287\nVo TS, Le PU, Ngo DH (2019) Free radical scavenging and anti-proliferative activities of avocado (Persea americana Mill.) seed extract. Asian Pac J Trop Biomed 9:91–97\nZhang C, Ge J, Lv M, Zhang Q, Talukder M, Li J-L (2020) Selenium prevent cadmium-induced hepatotoxicity through modulation of endoplasmic reticulum-resident selenoproteins and attenuation of endoplasmic reticulum stress. 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Adeola","ARTICLE",{"url":1042,"publisher":1150,"properties":1204},{"id":868,"createTime":869,"updateTime":870,"relativeEntities":1151,"slug":872,"properties":1152,"entityType":25,"verifyStatus":880,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":32,"subjectFields":1156,"manageAffiliations":1173,"indexDatabases":1184,"url":953,"thumbnailPath":28,"statistic":1199,"gsStatistic":28,"type":55,"analyzePriority":28},[],{"issn":1153,"title":1154,"eissn":1155},{"VOID":875},{"EN":877},{"VOID":879},[1157,1161,1165,1169],{"id":883,"createTime":28,"updateTime":28,"relativeEntities":1158,"label":1159,"description":1160,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":886},{},{"id":889,"createTime":28,"updateTime":28,"relativeEntities":1162,"label":1163,"description":1164,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":892},{},{"id":895,"createTime":28,"updateTime":28,"relativeEntities":1166,"label":1167,"description":1168,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":898},{},{"id":901,"createTime":28,"updateTime":28,"relativeEntities":1170,"label":1171,"description":1172,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":904},{},[1174,1179],{"id":908,"createTime":28,"updateTime":28,"relativeEntities":1175,"slug":28,"properties":1176,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1178,"statistic":28},[],{"title":1177},{"EN":912},[914],{"id":916,"createTime":28,"updateTime":28,"relativeEntities":1180,"slug":28,"properties":1181,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1183,"statistic":28},[],{"title":1182},{"EN":920},[],[1185,1192],{"id":924,"indexDatabase":1186,"url":28,"indexYears":28,"academicFieldIds":1191,"indexDatabaseRanking":28},{"id":926,"createTime":28,"updateTime":28,"relativeEntities":1187,"label":1188,"description":1189,"key":933,"publicationTags":1190,"standard":28},[],{"EN":929,"VI":929},{"EN":931,"VI":932},[935,813],[937],{"id":939,"indexDatabase":1193,"url":945,"indexYears":946,"academicFieldIds":1198,"indexDatabaseRanking":952},{"id":775,"createTime":28,"updateTime":28,"relativeEntities":1194,"label":1195,"description":1196,"key":781,"publicationTags":1197,"standard":28},[],{"EN":778,"VI":778},{"EN":778,"VI":780},[783],[948,949,950,951],{"impactFactor":32,"impactFactorByYear":1200,"i10Index":959,"i10IndexLast5Year":137,"totalPublication":960,"totalPublicationByYear":1201,"totalCitation":974,"totalCitationByYear":1202,"totalCitationPerPublication":998,"totalCitationPerPublicationByYear":1203,"hindexLast5Year":325,"hindex":325},{"2012":347,"2013":423,"2014":956,"2015":347,"2016":118,"2017":840,"2018":957,"2019":956,"2020":424,"2021":229,"2022":422,"2023":958},{"1988":122,"1989":69,"1990":358,"1991":208,"1992":50,"1993":353,"1994":325,"1995":354,"1996":329,"1997":434,"1998":156,"1999":962,"2000":207,"2001":436,"2002":160,"2003":600,"2004":963,"2005":530,"2006":964,"2007":965,"2008":600,"2009":966,"2010":613,"2011":967,"2012":968,"2013":969,"2014":575,"2015":212,"2016":212,"2017":563,"2018":970,"2019":971,"2020":207,"2021":972,"2022":603,"2023":973,"2024":196},{"1989":976,"1990":128,"1991":213,"1992":977,"1993":564,"1994":978,"1995":979,"1996":980,"2004":45,"2005":981,"2006":982,"2007":983,"2008":984,"2009":985,"2010":986,"2011":987,"2012":988,"2013":989,"2014":990,"2015":991,"2016":992,"2017":993,"2018":994,"2019":995,"2020":332,"2021":571,"2022":996,"2023":997},{"1989":1000,"1990":113,"1991":1001,"1992":1002,"1993":1003,"1994":1004,"1995":1005,"1996":1006,"2004":317,"2005":1007,"2006":1008,"2007":1009,"2008":1010,"2009":1011,"2010":1012,"2011":1013,"2012":1014,"2013":1015,"2014":1016,"2015":1017,"2016":1018,"2017":1019,"2018":1020,"2019":1021,"2020":1022,"2021":1023,"2022":177,"2023":166},{"pages":1205,"volume":1207},{"VOID":1206},"1141-1153",{"VOID":1208},"34","2021-08-07",2021,[935,952],false,{"id":1214,"createTime":1215,"updateTime":1216,"relativeEntities":1217,"slug":1218,"properties":1219,"entityType":1041,"verifyStatus":26,"verifyTime":1216,"verifyNote":1230,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":1231,"fullTextUrl":28,"authors":1232,"publicationType":1148,"publisherRelationship":1261,"citationCount":28,"citationInfo":28,"publishDate":1316,"publishYear":1317,"citationAnalyzeStatus":880,"lastCitationAnalyze":28,"indexDatabases":1318,"openAccess":28,"references":28,"isForceReanalyzing":1212},"0030bb71-3e3b-48c9-8f1b-65e7457a37be","2024-04-09T10:37:42.081+00:00","2024-12-25T06:39:36.266+00:00",[],"Methionine-sulfoxide-formation-in-proteins-NMR-study",{"abstract":1220,"title":1222,"keywords":1224,"references":1226,"doi":1228},{"EN":1221},"\n1H-NMR spectra of bovine pancreatic trypsin inhibitor (BPTI) both native and oxidized by chloramine T, are reported. The spectrum of the oxidized form is characterized by the appearance of two singlets for methyl group shifted 0.60 and 0.46 ppm downfield with respect to the native form.",{"EN":1223},"Methionine sulfoxide formation in proteins: NMR study",{"EN":1225},"",{"VOID":1227},"Concetti A, Angeletti M, Fioretti E, Ascoli F (1989) Selective oxidation of methionine residues in Kunitz-type protease inhibitors. Biol Chem Hoppe-Seyler 370:723–728\nDe Marco A, Tschesche H, Wagner G, Wüthrich K (1977)1HNMR studies at 360 MHz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI). Biophys Struct Mechanism 3:303–315\nSwaim MW, Pizzo S (1988) Methionine sulfoxide and the oxidative regulation of plasma proteinase inhibitors. J Leukocyte Biol 43:365–379",{"VOID":1229},"10.1007\u002FBF01179519","Auto Verify","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF01179519",[1233,1248],{"id":1234,"sortIndex":32,"researcher":28,"roles":1235,"affiliations":1236,"properties":1245},"aad1565b-387f-4910-9e6e-7c7b9dfff7ed",[1047],[1237],{"id":1238,"sortIndex":32,"affiliation":1239,"properties":28},"e3d0cca7-ea7f-4830-9c4c-e61ea5308425",{"id":1238,"createTime":28,"updateTime":28,"relativeEntities":1240,"slug":28,"properties":1241,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1244,"statistic":28},[],{"title":1242},{"VI":1243},"Department of Cell Biology and Department of Chemistry, University of Camerino, Camerino, Italy",[],{"title":1246},{"VI":1247},"Antonio 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exposure is related to several cardiovascular diseases, such as hypertension, atherosclerosis and endothelial dysfunction. However, the toxic effect of cadmium can be dependent on the sex when examined sex in experimental models. The aim of this study was to analyze the effects of cadmium exposure on the cardiovascular system of male and female rodents. The experiments were carried out on both-sexes Wistar at 4 months of age, where from 3 months onwards, cadmium (CdCl2 100 mg\u002Fl in placed the drinking water for 30 days) or vehicle delivered (distilled water) was ingested. Before and after 30 days of exposure to cadmium, systolic blood pressure was regularly measured. After exposure, blood was collected to measure dosage of cadmium, in male and female, and estrogen in females. Vascular reactivity to phenylephrine (Phe), acetylcholine (ACh), and sodium nitroprusside (SNP) was studied at respective isolated aortic segments. After the period to Cd-exposure, systolic blood pressure was increased only in the male rats. Males also had higher levels of plasma cadmium than those of female rats, and exposure to the metal did not affect the amount of estrogen produced in the female rats. Increased myeloperoxidase (MPO) activity was also observed in both the males and females that had been exposed to the metal. Moreover, exposure to the cadmium reduced the ACh relaxation and increased vascular reactivity to Phe, resulting in an imbalance between nitric oxide superoxide anion in the isolated aorta of male rats. In female rats, sub-chronic cadmium exposure did not modify the vascular reactivity to Phe and neither to the ACh. The present study revealed that the Cd exposure for 30 days induced sex-dependent cardiovascular abnormalities.",{"EN":1329},"Sex-dependent vascular effects of cadmium sub-chronic exposure on rats",{"VOID":1331},"Abu-Hayyeh S et al (2001) Cadmium accumulation in aortas of smokers. Arterioscler Thromb Vasc Biol 21(5):863–867. https:\u002F\u002Fdoi.org\u002F10.1161\u002F01.ATV.21.5.863\nAdams SV, Newcomb PA (2014) Cadmium blood and urine concentrations as measures of exposure: NHANES 1999–2010. J Exposure Sci Environ Epidemiol 24:163–170. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fjes.2013.55\nAfolabi OK et al (2012) Impaired lipid levels and inflammatory response in rats exposed to cadmium. Excli J 11:677–687\nAfridi HI et al (2010) Evaluation of cadmium, lead, nickel and zinc status in biological samples of smokers and nonsmokers hypertensive patients. J Hum Hypertens 24(1):34–43. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fjhh.2009.39\nAlmenara CCP et al (2013) Chronic cadmium treatment promotes oxidative stress and endothelial damage in isolated rat aorta. PLoS ONE 8(7):1–8. https:\u002F\u002Fdoi.org\u002F10.1371\u002Fjournal.pone.0068418\nAngeli JK et al (2013) Cadmium exposure induces vascular injury due to endothelial oxidative stress: the role of local angiotensin II and COX-2. Free Radical Biol Med 65:838–848. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.freeradbiomed.2013.08.167\nArdanaz N, Pagano PJ (2006) Minireview hydrogen peroxide as a paracrine vascular mediator: regulation and signaling leading to dysfunction. Exp Biol Med (maywood) 231:237–251\nAtaei N, Aghaei M, Panjehpour M (2018) The protective role of melatonin in cadmium-induced proliferation of ovarian cancer cells. Res Pharma Sci 13(2):159–167. https:\u002F\u002Fdoi.org\u002F10.4103\u002F1735-5362.223801\nBaron JA, Vecchia CL, Levi F (1990) Current development the antiestrogenic effect of cigarette smoking in women. Am J Obstet Gynecol 162(2):502–514. https:\u002F\u002Fdoi.org\u002F10.1016\u002F0002-9378(90)90420-C\nBarton M, Meyer MR, Prossnitz ER (2011) Estrogen-independent activation of estrogen receptors. Hypertension 57(6):1056–1057. https:\u002F\u002Fdoi.org\u002F10.1161\u002FHYPERTENSIONAHA.111.173427\nBergiund M et al (1994) Intestinal absorption of dietary cadmium in women depends on body iron stores and fiber intake. Environ Health Persp 102:1058–1066\nCasalino E et al (2002) Molecular inhibitory mechanisms of antioxidant enzymes in rat liver and kidney by cadmium. Toxicology 179:37–50\nChedrese HE (2004) Endocrine disruption by cadmium, a common environmental toxicant with paradoxical effects on reproduction. Exp Biol Med 229(3):383–392\nda Costa CS et al (2020) Subacute cadmium exposure disrupts the hypothalamic-pituitary-gonadal axis, leading to polycystic ovarian syndrome and premature ovarian failure features in female rats. Environ Pollut 269:116154. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.envpol.2020.116154\nDonpunha W et al (2011) Protective effect of ascorbic acid on cadmium-induced hypertension and vascular dysfunction in mice. Biometals 24(1):105–115. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs10534-010-9379-0\nEum KD, Lee MS, Paek D (2008) Cadmium in blood and hypertension. Sci Total Environ 407(1):147–153. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.scitotenv.2008.08.037\nFleming I (2010) Molecular mechanisms underlying the activation of eNOS. Pflugers Archiv Eur J Physiol 459:793–806. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs00424-009-0767-7\nFranceschini N et al (2017) Cadmium body burden and increased blood pressure in middle-aged American Indians: the strong heart study. J Hum Hypertens 31(3):225–230. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fjhh.2016.67\nGökalp O et al (2009) Impairment of endothelium-dependent vasorelaxation in cadmium-hypertensive rats. Toxicol Ind Health 25(7):447–453. https:\u002F\u002Fdoi.org\u002F10.1177\u002F0748233709106822\nGriendling KK, Sorescu D, Ushio-Fukai M (2000) NAD(P)H oxidase role in cardiovascular biology and disease. Circ Res 86:494–501\nGrizzo LT, Cordellini S (2008) Perinatal lead exposure affects nitric oxide and cyclooxygenase pathways in aorta of weaned rats. Toxicol Sci 103(1):207–214. https:\u002F\u002Fdoi.org\u002F10.1093\u002Ftoxsci\u002Fkfn018\nHart BA et al (1999) Characterization of cadmium-induced apoptosis in rat lung epithelial cells: evidence for the participation of oxidant stress. Toxicology 133:43–58\nHuang YH et al (2006) Effects of cadmium on structure and enzymatic activity of Cu, Zn-SOD and oxidative status in neural cells. J Cell Biochem 98(3):577–589. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fjcb.20772\nJamakala O, Rani UA (2015) Amelioration effect of zinc and iron supplementation on selected oxidative stress enzymes in liver and kidney of cadmium-treated male albino rat. Toxicol Int 22(1):1–9. https:\u002F\u002Fdoi.org\u002F10.4103\u002F0971-6580.172289\nJohnson MD et al (2003) Cadmium mimics the in vivo effects of estrogen in the uterus and mammary gland. Nat Med 9(8):1081–1084. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fnm902\nKataranovski M et al (2009) Gender differences in acute cadmium-induced systemic inflammation in rats. Biomed Environ Sci 22(1):1–7. https:\u002F\u002Fdoi.org\u002F10.1016\u002FS0895-3988(09)60014-3\nKataranovski M et al (2010) Gender differences in pulmonary inflammation following systemic cadmium administration in rats. Biomed Environ Sci 23:293–299\nKnoflach M et al (2011) Non-toxic cadmium concentrations induce vascular inflammation and promote atherosclerosis. Circ J 75(October):2491–2495. https:\u002F\u002Fdoi.org\u002F10.1253\u002Fcircj.CJ-11-0196\nLee J, Lim KT (2011) Inhibitory effect of plant-originated glycoprotein (27kDa) on expression of matrix metalloproteinase-9 in cadmium chloride-induced BNL CL.2 cells. J Trace Elem Med Biol 25(4):239–246. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jtemb.2011.08.142\nMartins AC et al (2020) Blood cadmium levels and sources of exposure in an adult urban population in southern Brazil. Environ Res. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.envres.2020.109618\nNoor N et al (2018) Urinary cadmium concentrations and metabolic syndrome in U.S. adults: the national health and nutrition examination survey 2001–2014. Environ Int 121:349–356. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.envint.2018.08.029\nNordberg GF, Nogawa K, Nordberg M (2015) Cadmium. Handbook on the toxicology of metals, 4th edn. Academic Press, pp 667–716\nNwokocha CR, Owu DU, Stephen Ufearo C (2011) Estimation of absorded cadmium in tissues of male and female albino rats through different routes of administration effect of chronic consumption of thermoxidized palm oil on the renal Na\u002FK ATPases view project effect of quercetin on cadmium chloride-induced reproductive toxicity in male and female rats view project. https:\u002F\u002Fwww.researchgate.net\u002Fpublication\u002F221815175.\nOliveira TF et al (2018) Chronic cadmium exposure accelerates the development of atherosclerosis and induces vascular dysfunction in the aorta of ApoE −\u002F− mice. Biol Trace Elem Res 187(1):163–171. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs12011-018-1359-1\nPaksy K, Varga B, Folly G (1990) Long-term effects of a single cadmium chloride injection on the ovulation, ovarian progesterone and estradiol-17 beta secretion in rats. Acta Physiol Hung 76(2):245–252\nSadeghi N et al (2014) The relationship between bone health and plasma zinc, copper lead and cadmium concentration in osteoporotic women. J Environ Health Sci Eng. https:\u002F\u002Fdoi.org\u002F10.1186\u002Fs40201-014-0125-3\nSantos Dos RL et al (2014) Sex hormones in the cardiovascular system. Horm Mol Biol Clin Invest 18(2):89–103. https:\u002F\u002Fdoi.org\u002F10.1515\u002Fhmbci-2013-0048\nShimada H et al (2012) Sexual dimorphism of cadmium-induced toxicity in rats: Involvement of sex hormones. Arch Toxicol 86(9):1475–1480. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs00204-012-0844-0\nSilva N et al (2013) Metalloestrogen cadmium stimulates proliferation of stromal cells derived from the eutopic endometrium of women with endometriosis. Taiwan J Obstet Gynecol 52(4):540–545. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.tjog.2013.10.015\nSompamit K et al (2010) Reversal of cadmium-induced vascular dysfunction and oxidative stress by meso-2,3-dimercaptosuccinic acid in mice. Toxicol Lett 198(1):77–82. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.toxlet.2010.04.007\nStockand J et al. (no date) Interactions of cadmium and nickel with K channels of vascular smooth muscle.\nStoica A, Katzenellenbogen BS, and Martin MB (2000) Activation of estrogen receptor-by the heavy metal cadmium. https:\u002F\u002Facademic.oup.com\u002Fmend\u002Farticle\u002F14\u002F4\u002F545\u002F2870457.\nTakahashi K et al (2003) Both estrogen and raloxifene cause G1 arrest of vascular smooth muscle cells. J Endocrinol. https:\u002F\u002Fdoi.org\u002F10.1677\u002Fjoe.0.1780319\nTellez-Plaza M et al (2008) Cadmium exposure and hypertension in the 1999–2004 national health and nutrition examination survey (NHANES). Environ Health Perspect 116(1):51–56. https:\u002F\u002Fdoi.org\u002F10.1289\u002Fehp.10764\nTellez-Plaza M et al (2013) Cadmium exposure and incident cardiovascular disease. Epidemiology 24(3):421–429. https:\u002F\u002Fdoi.org\u002F10.1097\u002FEDE.0b013e31828b0631\nThirumoorthy N et al (2011) A review of metallothionein isoforms and their role in pathophysiology. World J Surg Oncol. https:\u002F\u002Fdoi.org\u002F10.1186\u002F1477-7819-9-54\nWang L et al (2012) Endogenous sex hormones, blood pressure change, and risk of hypertension in postmenopausal women: the multi-ethnic study of atherosclerosis. Atherosclerosis 224(1):228–234. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.atherosclerosis.2012.07.005\nWhanger PD (1979) Cadmium effects in rats on tissue iron, selenium, and blood pressure; blood and hair cadmium in some Oregon residents. Environ Health Persp 28:115\nWu H et al (2016) Environmental exposure to cadmium: health risk assessment and its associations with hypertension and impaired kidney function. Sci Rep. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fsrep29989\nYu X et al (2011) Activation of G protein-coupled estrogen receptor induces endothelium-independent relaxation of coronary artery smooth muscle. Am J Physiol Endocrinol Metab 301:882–888. https:\u002F\u002Fdoi.org\u002F10.1152\u002Fajpendo.00037.2011.-Estrogens\nZhao Z et al (2006) Oral exposure to cadmium chloride triggers an acute inflammatory response in the intestines of mice, initiated by the over-expression of tissue macrophage inflammatory protein-2 mRNA. Toxicol Lett 164(2):144–154. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.toxlet.2005.12.004",{"VOID":1333},"10.1007\u002Fs10534-022-00470-w","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10534-022-00470-w",[1336,1351,1364,1379,1392,1407,1420,1435],{"id":1337,"sortIndex":32,"researcher":28,"roles":1338,"affiliations":1339,"properties":1348},"61e27b87-7d3f-4bdd-a3e8-498a30fa8bdb",[1047],[1340],{"id":1341,"sortIndex":32,"affiliation":1342,"properties":28},"d62044b6-fcbc-45d4-8645-01cfd14a3748",{"id":1341,"createTime":28,"updateTime":28,"relativeEntities":1343,"slug":28,"properties":1344,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1347,"statistic":28},[],{"title":1345},{"VI":1346},"Department of Physiological Sciences, Universidade Federal do Espírito Santo, Vitória, Brazil",[],{"title":1349},{"VI":1350},"Thiago Fernandes de 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complexes [Cu(H\n                           \n                    2\n                  \n                           O)\n                           \n                    2\n                  \n                           (L1)(phen)](ClO\n                           \n                    4\n                  \n                           ) (1) and [Cu(H\n                           \n                    2\n                  \n                           O)(L2)(phen)](ClO\n                           \n                    4\n                  \n                           ) (2) (HL1 = naringenin; HL2 = hesperetin) were obtained, in which an anionic flavonoid ligand is attached to the metal center along with 1,10-phenanthroline (phen) as co-ligand. Complexes (1) and (2) were assayed for their cytotoxic activity against A549 lung carcinoma and against normal lung fibroblasts (LL-24) and human umbilical vein endothelial cells (HUVEC). We found IC50 = 16.42 µM (1) and IC50 = 5.82 µM (2) against A549 tumor cells. Complexes (1) and (2) exhibited slight specificity, being more cytotoxic against malignant than against non-malignant cells. 1 and 2 induced apoptosis on A549 cells in a mitochondria-independent pathway, and showed antioxidant activity. The antioxidant effect of the complexes could possibly improve their apoptotic action, most likely by a PI3K-independent reduction of autophagy. Complexes (1) and (2) interact in vitro with calf thymus DNA by an intercalative binding mode. EPR data indicated that 1 and 2 interact with human serum albumin (HSA) forming mixed ligand species. \n                  \n                    \n                      \n                    \n                  \n                ",{"EN":1521},"Copper(II) complexes with naringenin and hesperetin: cytotoxic activity against A 549 human lung adenocarcinoma cells and investigation on the mode of action",{"VOID":1523},"Ali SMH, Yan YK, Lee PPF, Khong KZX, Sk MA, Hwa LK, Klejevskajac B, Vilarc R (2014) Copper(II) complexes of substituted salicylaldehyde dibenzyl semicarbazones: synthesis, cytotoxicity and interaction with quadruplex DNA. Dalton Trans 43:1449–1459\nBatista DGJ, Silva PB, Stivanin L, Lachter DR, Silva RS, Felcman J, Louro SRW, Teixeira LR, Soeiro MNC (2011) Co(II), Mn(II) and Cu(II) complexes of fluoroquinolones: synthesis, spectroscopical studies and biological evaluation against Trypanosoma cruzi. Polyhedron 30:1718–1725\nCavia-Saiz M, Busto MD, Pilar-Izquierdo MC, Ortega N, Perez-Mateos M, Muñiz P (2010) Antioxidant properties, radical scavenging activity and biomolecule protection capacity of flavonoid naringenin and its glycoside naringin: a comparative study. J Sci Food Agric 90:1238–1244\nConceição Filho JCC, Sarria ALF, Becceneri AB, Fuzer AM, Batalhão JR, Paranhos Da Silva CM, Carlos RM, Vieira PC, Fernandes JB, Cominetti MR (2014) Copper (II) and 2,2-bipyridine complexation improves chemopreventive effects of naringenin against breast tumor cells. PLoS ONE 9:e107058\nDa Silva JG, Recio-Despaigne AA, Louro SRW, Bandeira CC, Souza-Fagundes EM, Beraldo H (2013) Cytotoxic activity, albumin and DNA binding of new copper(II) complexes with chalcone-derived thiosemicarbazones. Eur J Med Chem 65:415–426\nDimiza F, Perdih F, Tangoulis V, Turel I, Kessissoglou DP, Psomas G (2011) Interaction of copper(II) with the non-steroidal anti-inflammatory drugs naproxen and diclofenac: synthesis, structure, DNA- and albumin-binding. J Inorg Biochem 105:476–489\nEaton SS, More KM, Sawant BM, Eaton GR (1983) Use of the ESR half-field transition to determine the interspin distance and the orientation of the interspin vector in systems with two unpaired electrons. J Am Chem Soc 105:6560–6567\nFasano M, Curry S, Terreno E, Galliano M, Fanali G, Narciso P, Notari S, Ascenzi P (2005) The extraordinary ligand binding properties of human serum albumin. IUBMB Life 57:787–796\nFilomeni G, De Zio D, Cecconi F (2015) Oxidative stress and autophagy: the clash between damage and metabolic needs. Cell Death Differ 22:377–388\nHegde AH, Sandhya B, Seetharamappa J (2011) Evaluation of binding and thermodynamic characteristics of interactions between a citrus flavonoid hesperitin with protein and effects of metal ions on binding. Mol Biol Rep 38:4921–4929\nİnci D, Aydın R, Yılmaz D, Gençkal HM, Vatan Ö, Çinkılıç N, Zorlu Y (2015) New water-soluble copper (II) complexes including 4,7-dimethyl-1,10-phenanthroline and l-tyrosine: synthesis, characterization, DNA interactions and cytotoxicities. Spectrochim Acta Part A Mol Biomol Spectrosc 136:761–770\nJanku F, McConkey DJ, Hong DS, Kurzrock R (2011) Autophagy as a target for anticancer therapy. Nat Rev Clin Oncol 8:528–539\nKrishnamoorthy P, Sathyadevi P, Cowley AH, Butorac RR, Dharmaraj N (2011) Evaluation of DNA binding, DNA cleavage, Protein binding and in vitro cytotoxic activities of bivalent transition metal hydrazone complexes. Eur J Med Chem 46:3376–3387\nKrishnapriya KR, Saravanakumar D, Arunkumar P, Kandaswamy M (2008) Synthesis of new oxamide-based ligand and its coordination behavior towards copper(II) ion: spectral and electrochemical studies. Spectrochim Acta Part A 69:1077–1081\nKumar P, Baidya B, Chaturvedi SK, Khan RH, Manna D, Mondal B (2011) DNA binding and nuclease activity of copper(II) complexes of tridentate ligands. Inorg Chim Acta 376:264–270\nLi TR, Yang ZY, Wang BD (2007) Synthesis, characterization and antioxidant activity of naringenin schiff base and its Cu(II), Ni(II), Zn(II) complexes. Chem Pharm Bull 55:26–28\nLu J, Sun Q, Li JL, Jiang L, Gu W, Liu X, Tian JL, Yan SP (2014) Two water-soluble copper(II) complexes: synthesis, characterization, DNA cleavage, protein binding activities and in vitro anticancer activity studies. J Inorg Biochem 137:46–56\nLushchak VI (2014) Free radicals, reactive oxygen species, oxidative stress and its classification. Chem Biol Interact 224:164–175\nMa T, Xu J, Wang Y, Yu H, Yang Y, Liu Y, Ding W, Zhu W, Chen R, Ge Z, Tan Y, Jia L, Zhu T (2015) Ternary copper(II) complexes with amino acid chains and heterocyclic bases: DNA binding, cytotoxic and cell apoptosis induction properties. J Inorg Biochem 144:38–46\nManikandamathavan VM, Kavitha M, Uma V, Parameswari RP, Vasanthi HR, Nair BU (2011) Cytotoxic copper(II) complex of tripyridoquinoxaline with DNA hydrolase activity. Polyhedron 30:1604–1611\nManikandamathavana VM, Parameswaric RP, Weyhermüller T, Vasanthic HR, Nair BU (2011) Cytotoxic copper(II) mixed ligand complexes: crystal structure and DNA cleavage activity. Eur J Med Chem 46:4537–4547\nMcPhail DB, Hartley RC, Gardner PT, Duthie GG (2003) Kinetic and stoichiometric assessment of the antioxidant activity of flavonoids by electron spin resonance Spectroscopy. J Agric Food Chem 51:1684–1690\nMjos KD, Orvig C (2014) Metallodrugs in medicinal inorganic chemistry. Chem Rev 114:4540–4563\nNakamoto K (1986) Infrared and Raman spectra of inorganic and coordination compounds. Wiley, New York\nPatel RN, Pandeya KB (2000) X-band electron paramagnetic resonance spectra of pig serum albumin-copper(II) and pig serum albumin-copper(II)-amino acid system. Indian J Biochem Biophys 37:251–255\nPoillet-Perez L, Despouy G, Delage-Mourroux R, Boyer-Guittaut M (2015) Interplay between ROS and autophagy in cancer cells, from tumor initiation to cancer therapy. Redox Biol 4:184–192\nPsomas G, Tarushi A, Efthimiadou EK, Sanakis Y, Raptopoulou CP, Katsaros N (2006) Synthesis, structure and biological activity of copper(II) complexes with oxolinic acid. J Inorg Biochem 100:1764–1773\nRaja DS, Bhuvanesh NSP, Natarajan K (2012) Structure-activity relationship study of copper(II) complexes with 2-oxo-1,2-dihydroquinoline-3-carbaldehyde (4′-methylbenzoyl) hydrazone: synthesis, structures, DNA and protein interaction studies, antioxidative and cytotoxic activity. J Biol Inorg Chem 17:223–237\nRakhit G, Antholine WE, Froncisz W, Hyde JS, Pilbrow JR, Sinclair GR, Sarker B (1985) Direct evidence of nitrogen coupling in the copper(II) complex of bovine serum albumin by S-band electron spin resonance technique. J Inorg Biochem 25:217–224\nRaninga PV, Di Trapani G, Tonissen KF (2014) Cross talk between two antioxidant systems, Thioredoxin and DJ-1: consequences for cancer. Oncoscience 1:95–110\nRecio Despaigne AA, Da Silva JG, Da Costa PR, Dos Santos RG, Beraldo H (2014) ROS-mediated cytotoxic effect of copper(II) hydrazone complexes against Human Glioma Cells. Molecules 19:17202–17220\nReichmann ME, Rice SA, Thomas CA, Doty P (1954) A further examination of the molecular weight and size of desoxypentose nucleic acid. J Am Chem Soc 76:3047–3053\nSadler PJ, Tucker A, Viles JH (1994) Involvement of a lysine residue in the N-terminal Ni2+ and Cu2+ binding site of serum albumins. Comparison with Co2+, Cd2+ and Al3+. Eur J Biochem 220:193–200\nSaha DK, Sandbhor U, Shirisha K, Padhye S, Deobagkar D, Anson CE, Powell AK (2004) A novel mixed-ligand antimycobacterial dimeric copper complex of ciprofloxacin and phenanthroline. Bioorg Med Chem Lett 14:3027–3032\nSelvaraj S, Krishnaswamy S, Devashya V, Sethuraman S, Krishnan UM (2012) Membrane fluidization & eryptotic properties of hesperidin-copper complex. RSC Adv 2:11138–11146\nStewart BW, Wild CP World Cancer Report (2014) IARC Nonserial Publication World Health Organization website http:\u002F\u002Fwww.who.int\u002Fmediacentre\u002Ffactsheets\u002Ffs297\u002Fen\u002F. Accessed on 9 Jan 2015\nStoll S, Schweiger A (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR. J Magn Reson 178:42–55\nSugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K (1999) Crystal structure of human serum albumin at 2.5 Å resolution. Protein Eng 12:439–446\nSui X, Chen R, Wang Z, Huang Z, Kong N, Zhang M, Han W, Lou F, Yang J, Zhang Q, Wang X, He C, Pan H (2013) Autophagy and chemotherapy resistance: a promising therapeutic target for cancer treatment. Cell Death Dis 4:e838\nTan J, Wang B, Zhu L (2009a) DNA binding and oxidative DNA damage induced by a quercetin copper(II) complex: potential mechanism of its antitumor properties. J Biol Inorg Chem 14:727–739\nTan M, Zhu J, Pan Y, Chen Z, Liang H, Liu H, Wang H (2009b) Synthesis, cytotoxic activity, and DNA binding properties of copper(II) complexes with Hesperetin, Naringenin, and Apigenin. Bioinorg Chem Appl. doi:10.1155\u002F2009\u002F347872\nWang HL, Yang ZY, Wang BD (2006) Synthesis, characterization and the antioxidative activity of copper(II), zinc(II) and nickel(II) complexes with naringenin. Trans Met Chem 31:470–474\nWeil JA, Bolton JR, Wertz JE (1993) Electron paramagnetic resonance, elementary theory and practical applications. Wiley, New York\nWong E, Giandomenico CM (1999) Current status of platinum-based antitumor drugs. Chem Rev 99:2451–2466\nYan LJ (2014) Positive oxidative stress in aging and aging-related disease tolerance. Redox Biol 2:165–169\nZang Y, Wilcox DE (2002) Thermodynamic and spectroscopic study of Cu(II) and Ni(II) binding to bovine serum albumin. J Biol Inorg Chem 7:327–337\nZgirski A, Frieden E (1990) Binding of Cu(II) to non-prosthetic sites in ceruloplasmin and bovine serum albumin. J Inorg Biochem 39:137–148",{"VOID":1525},"10.1007\u002Fs10534-015-9894-0","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10534-015-9894-0",[1528,1543,1556,1569,1582,1597,1610,1625,1647],{"id":1529,"sortIndex":32,"researcher":28,"roles":1530,"affiliations":1531,"properties":1540},"b1ae8ea7-d8da-4754-9ce1-c4d83744c903",[1047],[1532],{"id":1533,"sortIndex":32,"affiliation":1534,"properties":28},"6188edc5-a7d1-4cfb-bc69-f9767ad7aeee",{"id":1533,"createTime":28,"updateTime":28,"relativeEntities":1535,"slug":28,"properties":1536,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1539,"statistic":28},[],{"title":1537},{"VI":1538},"Departamento de Química, Universidade Federal de Minas Gerais, Belo Horizonte, Brazil",[],{"title":1541},{"VI":1542},"Lenka V. 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W. 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Groningen, The Netherlands",[],{},{"title":1645},{"VI":1646},"Adilson Kleber Ferreira",{"id":1648,"sortIndex":357,"researcher":28,"roles":1649,"affiliations":1650,"properties":1657},"acaa25d0-777e-4b69-bce0-e2811a1ddad2",[1047],[1651],{"id":1533,"sortIndex":32,"affiliation":1652,"properties":28},{"id":1533,"createTime":28,"updateTime":28,"relativeEntities":1653,"slug":28,"properties":1654,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1656,"statistic":28},[],{"title":1655},{"VI":1538},[],{"title":1658},{"VI":1659},"Heloisa 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0.2 % of all angiosperms are classified as metal hyperaccumulators based on their extraordinarily high leaf metal contents, for example >1 % zinc, >0.1 % nickel or >0.01 % cadmium (Cd) in dry biomass. So far, metal hyperaccumulation has been considered to be a taxon-wide, constitutively expressed trait, the extent of which depends solely on available metal concentrations in the soil. Here we show that in the facultative metallophyte Arabidopsis halleri, both insect herbivory and mechanical wounding of leaves trigger an increase specifically in leaf Cd accumulation. Moreover, the Cd concentrations accumulated in leaves can serve as an elemental defense against herbivory by larvae of the Brassicaceae specialist small white (Pieris rapae), thus allowing the plant to take advantage of this non-essential trace element and toxin. Metal homeostasis genes are overrepresented in the systemic transcriptional response of roots to the wounding of leaves in A. halleri, supporting that leaf Cd accumulation is preceded by systemic signaling events. A similar, but quantitatively less pronounced transcriptional response was observed in A. thaliana, suggesting that the systemically regulated modulation of metal homeostasis in response to leaf wounding also occurs in non-hyperaccumulator plants. This is the first report of an environmental stimulus influencing metal hyperaccumulation.",{"EN":1733},"Wounding of Arabidopsis halleri leaves enhances cadmium accumulation that acts as a defense against herbivory",{"VOID":1735},"Arrivault S, Senger T, Krämer U (2006) The Arabidopsis metal tolerance protein AtMTP3 maintains metal homeostasis by mediating Zn exclusion from the shoot under Fe deficiency and Zn oversupply. Plant J 46:861–879\nBaker AJM, Brooks RR (1989) Terrestrial higher plants which hyperaccumulate metallic elements—a review of their distribution, ecology and phytochemistry. Biorecovery 1:81–126\nBecher M, Talke IN, Krall L, Krämer U (2004) Cross-species microarray transcript profiling reveals high constitutive expression of metal homeostasis genes in shoots of the zinc hyperaccumulator Arabidopsis halleri. Plant J 37:251–268\nBovet L et al (2003) Transcript level of AtMRPs after cadmium treatment: induction of AtMRP3. Plant, Cell Environ 26:371–381\nBoyd RS (2007) The defense hypothesis of elemental hyperaccumulation: status, challenges and new directions. Plant Soil 293:153–176\nBoyd RS, Martens SN (1992) The raison d’être for metal hyperaccumulation in plants. In: Baker AJM, Proctor J, Reeves RD (eds) The vegetation of ultramafic (serpentine) soils. Intercept, Andover, pp 279–289\nBulgarelli D et al (2012) Revealing structure and assembly cues for Arabidopsis root-inhabiting bacterial microbiota. Nature 488:91–95. doi:10.1038\u002Fnature11336\nClemens S, Aarts MG, Thomine S, Verbruggen N (2013) Plant science: the key to preventing slow cadmium poisoning. Trends Plant Sci 18:92–99. doi:10.1016\u002Fj.tplants.2012.08.003\nColangelo EP, Guerinot ML (2004) The essential basic helix-loop-helix protein FIT1 is required for the iron deficiency response. Plant Cell 16:3400–3412\nDahmani-Muller H, Van Oort F, Gelie B, Balabane M (2000) Strategies of heavy metal uptake by three plant species growing near a metal smelter. Environ Pollut 109:231–238\nFarinati S et al (2009) Proteomic analysis of Arabidopsis halleri shoots in response to the heavy metals cadmium and zinc and rhizosphere microorganisms. Proteomics 9:4837–4850. doi:10.1002\u002Fpmic.200900036\nFarinati S, DalCrso G, Panigati M, Furini A (2011) Interaction between selected bacterial strains and Arabidopsis halleri modulates shoot proteome and cadmium and zinc accumulation. J Exp Bot 62:3433–3447. doi:10.1093\u002Fjxb\u002Ferr015\nGong Q, Li P, Ma S, Indu Rupassara S, Bohnert HJ (2005) Salinity stress adaptation competence in the extremophile Thellungiella halophila in comparison with its relative Arabidopsis thaliana. Plant J 44:826–839\nGravot A, Lieutaud A, Verret F, Auroy P, Vavasseur A, Richaud P (2004) AtHMA3, a plant P(1B)-ATPase, functions as a Cd\u002FPb transporter in yeast. FEBS Lett 561:22–28\nHanikenne M et al (2008) Evolution of metal hyperaccumulation required cis-regulatory changes and triplication of HMA4. Nature 453:391–395\nHilson P et al (2004) Versatile gene-specific sequence tags for Arabidopsis functional genomics: transcript profiling and reverse genetics applications. Genome Res 14:2176–2189\nHorton MW et al (2014) Genome-wide association study of Arabidopsis thaliana leaf microbial community Nat Commun 5:5320. doi:10.1038\u002Fncomms6320\nKazemi-Dinan A, Thomaschky S, Stein RJ, Krämer U, Müller C (2014) Zinc and cadmium hyperaccumulation act as deterrents towards specialist herbivores and impede the performance of a generalist herbivore. New Phytol 202:628–639. doi:10.1111\u002Fnph.12663\nKilian J et al (2007) The AtGenExpress global stress expression data set: protocols, evaluation and model data analysis of UV-B light, drought and cold stress responses. Plant J 50:347–363\nKrämer U (2010) Metal hyperaccumulation in plants. Annu Rev Plant Biol 61:517–534\nLundberg DS et al (2012) Defining the core Arabidopsis thaliana root microbiome. Nature 488:86–90. doi:10.1038\u002Fnature11237\nMassonneau A, Langlade N, Leon S, Smutny J, Vogt E, Neumann G, Martinoia E (2001) Metabolic changes associated with cluster root development in white lupin (Lupinus albus L.): relationship between organic acid excretion, sucrose metabolism and energy status. Planta 213:534–542\nMaurer F, Muller S, Bauer P (2011) Suppression of Fe deficiency gene expression by jasmonate. Plant Physiol Biochem 49:530–536. doi:10.1016\u002Fj.plaphy.2011.01.025\nMithofer A, Boland W (2012) Plant defense against herbivores: chemical aspects. Annu Rev Plant Biol 63:431–450. doi:10.1146\u002Fannurev-arplant-042110-103854\nMorel M, Crouzet J, Gravot A, Auroy P, Leonhardt N, Vavasseur A, Richaud P (2009) AtHMA3, a P1B-ATPase Allowing Cd\u002FZn\u002FCo\u002FPb Vacuolar Storage in Arabidopsis. Plant Physiol 149:894–904\nMousavi SA, Chauvin A, Pascaud F, Kellenberger S, Farmer EE (2013) GLUTAMATE RECEPTOR-LIKE genes mediate leaf-to-leaf wound signalling. Nature 500:422–426. doi:10.1038\u002Fnature12478\nMuehe EM, Weigold P, Adaktylou IJ, Planer-Friedrich B, Krämer U, Kappler A, Behrens S (2015) Rhizosphere microbial community composition affects cadmium and zinc uptake of the metal-hyperaccumulating plant Arabidopsis halleri. Appl Environ Microbiol. [Epub ahead of print]\nNemhauser JL, Hong F, Chory J (2006) Different plant hormones regulate similar processes through largely nonoverlapping transcriptional responses. Cell 126:467–475\nReymond P, Bodenhausen N, Van Poecke RM, Krishnamurthy V, Dicke M, Farmer EE (2004) A conserved transcript pattern in response to a specialist and a generalist herbivore Plant Cell 16:3132–3147\nTaki N et al (2005) 12-oxo-phytodienoic acid triggers expression of a distinct set of genes and plays a role in wound-induced gene expression in Arabidopsis. Plant Physiol 139:1268–1283\nTalke IN, Hanikenne M, Krämer U (2006) Zinc-dependent global transcriptional control, transcriptional deregulation, and higher gene copy number for genes in metal homeostasis of the hyperaccumulator Arabidopsis halleri. Plant Physiol 142:148–167\nUsadel B et al (2005) Extension of the visualization tool MapMan to allow statistical analysis of arrays, display of corresponding genes, and comparison with known responses. Plant Physiol 138:1195–1204\nVerbruggen N, Hermans C, Schat H (2009) Molecular mechanisms of metal hyperaccumulation in plants. New Phytol 181:759–776. doi:10.1111\u002Fj.1469-8137.2008.02748.x\nWeber M, Harada E, Vess C, Roepenack-Lahaye EV, Clemens S (2004) Comparative microarray analysis of Arabidopsis thaliana and Arabidopsis halleri roots identifies nicotianamine synthase, a ZIP transporter and other genes as potential metal hyperaccumulation factors. Plant J 37:269–281\nYang YH, Dudoit S, Luu P, Lin DM, Peng V, Ngai J, Speed TP (2002) Normalization for cDNA microarray data: a robust composite method addressing single and multiple slide systematic variation. 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là một nguyên tố thiết yếu cho vi sinh vật và nó có thể được thu nhận từ nhiều hợp chất, trong đó sulfate là nguồn ưu tiên. Bước đầu tiên trong việc sử dụng sulfate, thu nhận sulfate, đã được nghiên cứu ở một số loài vi khuẩn. Bài báo này tổng hợp các đặc điểm của các chất vận chuyển khác nhau ở vi khuẩn (và vi khuẩn cổ) cho sulfate, molybdate và các oxyanion liên quan. Việc thu nhận sulfate được thực hiện bởi các protein thấm sulfate thuộc các họ SulT (CysPTWA), SulP, CysP\u002F(PiT) và CysZ. Các oxyanion molybdate, tungstate, selenate và chromate có cấu trúc liên quan đến sulfate. Molybdate được vận chuyển chủ yếu bởi hệ thống ModABC có ái lực cao, trong khi tungstate được vận chuyển bởi các hệ thống TupABC và WtpABC. CysPTWA, ModABC, TupABC và WtpABC là các chất vận chuyển thuộc loại hộp đen liên kết ATP (ABC) có tổ chức và tính chất tương đồng. Việc thu nhận các oxyanion selenate và chromate chủ yếu diễn ra thông qua các protein thấm sulfate.","Sulfur is an essential element for microorganisms and it can be obtained from varied compounds, sulfate being the preferred source. The first step for sulfate assimilation, sulfate uptake, has been studied in several bacterial species. This article reviews the properties of different bacterial (and archaeal) transporters for sulfate, molybdate, and related oxyanions. Sulfate uptake is carried out by sulfate permeases that belong to the SulT (CysPTWA), SulP, CysP\u002F(PiT), and CysZ families. The oxyanions molybdate, tungstate, selenate and chromate are structurally related to sulfate. Molybdate is transported mainly by the high-affinity ModABC system and tungstate by the TupABC and WtpABC systems. CysPTWA, ModABC, TupABC, and WtpABC are homologous ATP-binding cassette (ABC)-type transporters with similar organization and properties. Uptake of selenate and chromate oxyanions occurs mainly through sulfate permeases.",{"EN":1988,"VI":1989},"Bacterial transport of sulfate, molybdate, and related oxyanions","Vận chuyển sulfate, molybdate và các oxyanion liên quan ở vi khuẩn",{"VI":1991},"sulfate, molybdate, oxyanion, vi khuẩn, vận chuyển",{"VOID":1993},"Aguilar-Barajas E, Paluscio E, Cervantes C, Rensing C (2008) Expression of chromate resistance genes from Shewanella sp. strain ANA-3 in Escherichia coli. FEMS Microbiol Lett 285:97–100\nAlvarez AH, Moreno-Sánchez R, Cervantes C (1999) Chromate efflux by means of the ChrA chromate resistance protein from Pseudomonas aeruginosa. J Bacteriol 181:7398–7400\nAnderson LA, Palmer T, Price NC, Bornemann S, Boxer DH, Pau RN (1997) Characterisation of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli. Eur J Biochem 246:119–126\nAndreesen JR, Makdessi K (2008) Tungsten, the surprisingly positively acting heavy metal element for prokaryotes. Ann NY Acad Sci 1125:215–219\nAvoscan L, Carrière M, Proux O, Sarret G, Degrouard J, Covès J, Gouget B (2009) Enhanced selenate accumulation in Cupriavidus metallidurans CH34 does not trigger a detoxification pathway. Appl Environ Microbiol 75:2250–2252\nBai L, Collins JF, Ghishan FK (2000) Cloning and characterization of a type III Na-dependent phosphate cotransporter from mouse intestine. Am J Physiol Cell Physiol 279:C1135–C1143\nBalan A, Santacruz CP, Moutran A, Ferreira RC, Medrano FJ, Pérez CA, Ramos CH, Ferreira LC (2006) The molybdate-binding protein (ModA) of the plant pathogen Xanthomonas axonopodis pv citri. Protein Expr Purif 50:215–222\nBalan A, Santacruz-Pérez C, Moutran A, Ferreira LC, Neshich G, Goncalves Barbosa JA (2008) Crystallographic structure and substrate-binding interactions of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv citri. Biochim Biophys Acta 1784:393–399\nBébien M, Kirsch J, Méjean V, Verméglio A (2002) Involvement of a putative molybdenum enzyme in the reduction of selenate by Escherichia coli. Microbiology 148:3865–3872\nBevers LE, Hagedoorn PL, Krijger GC, Hagen WR (2006) Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters. J Bacteriol 188:6498–6505\nBøttger P, Pedersen L (2005) Evolutionary and experimental analyses of inorganic phosphate transporter PiT family reveals two related signature sequences harboring highly conserved aspartic acids critical for sodium-dependent phosphate transport function of human PiT2. FEBS J 272:3060–3074\nBranco R, Chung AP, Johnston T, Gurel V, Morais P, Zhitkovich A (2008) The chromate-inducible chrBACF operon from the transposable element TnOtChr confers resistance to chromium(VI) and superoxide. J Bacteriol 190:6996–7003\nBritton P, Boronat A, Hartley DA, Jones-Mortimer MC, Kornberg HL, Parra F (1983) Phosphotransferase-mediated regulation of carbohydrate utilization in Escherichia coli K12: location of the gsr (tgs) and iex (crr) genes by specialized transduction. J Gen Microbiol 129:349–356\nBrown SD, Thompson MR, Verberkmoes NC, Chourey K, Shah M, Zhou J, Hettich RL, Thompson DK (2006) Molecular dynamics of the Shewanella oneidensis response to chromate stress. Mol Cell Proteomics 5:1054–1071\nByrne CR, Monroe RS, Ward KA, Kredich NM (1988) DNA Sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH. J Bacteriol 170:3150–3157\nCervantes C, Ohtake H, Chu L, Misra TK, Silver S (1990) Cloning, nucleotide sequence, and expression of the chromate resistance determinant of Pseudomonas aeruginosa plasmid pUM505. J Bacteriol 172:287–291\nCervantes C, Campos-García J, Devars S, Gutiérrez-Corona F, Loza-Tavera H, Torres-Guzmán JC, Moreno-Sánchez R (2001) Interactions of chromium with microorganisms and plants. FEMS Microbiol Rev 25:335–347\nChen Y, Holtman CK, Magnuson RD, Youderian PA, Golden SS (2008) The complete sequence and functional analysis of pANL, the large plasmid of the unicellular cyanobacterium Synechococcus elongatus PCC 7942. Plasmid 59:176–192\nCrooks GE, Hon G, Chandonia JM, Brenner SE (2004) WebLogo: a sequence logo generator. Genome Res 14:1188–1190\nDam P, Olman V, Harris K, Su Z, Xu Y (2007) Operon prediction using both genome-specific and general genomic information. Nucleic Acids Res 35:288–298\nDaram P, Brunner S, Rausch C, Steiner C, Amrhein N, Bucher M (1999) Pht2;1 encodes a low-affinity phosphate transporter from Arabidopsis. Plant Cell 11:2153–2166\nDelgado MJ, Tresierra-Ayala A, Talbi C, Bedmar EJ (2006) Functional characterization of the Bradyrhizobium japonicum modA and modB genes involved in molybdenum transport. Microbiology 152:199–207\nDetro-Dassen S, Schänzler M, Lauks H, Martin I, zu Berstenhorst SM, Nothmann D, Torres-Salazar D, Hidalgo P, Schmalzing G, Fahlke C (2008) Conserved dimeric subunit stoichiometry of SLC26 multifunctional anion exchangers. J Biol Chem 283:4177–4188\nDíaz-Magaña A, Aguilar-Barajas E, Moreno-Sánchez R, Ramírez-Díaz MI, Riveros-Rosas H, Vargas E, Cervantes C (2009) Short-chain chromate ion transporter proteins from Bacillus subtilis confer chromate resistance in Escherichia coli. 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function of ferritins is to store and release ferrous iron. During oxidative iron uptake, ferritin tends to lower Fe2+ concentration, thus competing with Fenton reactions and limiting hydroxy radical generation. When ferritin functions as a releasing iron agent, the oxidative damage is stimulated. The antioxidant versus pro-oxidant functions of ferritin are studied here in the presence of Fe2+, oxygen and reducing agents. The Fe2+-dependent radical damage is measured using supercoiled DNA as a target molecule. The relaxation of supercoiled DNA is quantitatively correlated to the concentration of exogenous Fe2+, providing an indirect assay for free Fe2+. After addition of ferrous iron to ferritin, Fe2+ is actively taken up and asymptotically reaches a stable concentration of 1–5μ\nm. Comparable equilibrium concentrations are found with plant or horse spleen ferritins, or their apoferritins. After addition of ascorbate, iron release is observed using ferrozine as an iron scavenger. Rates of iron release are dependent on ascorbate concentration. They are about 10 times larger with pea ferritin than with horse ferritin. In the absence of ferrozine, the reaction of ascorbate with ferritins produces a wave of radical damage; its amplitude increases with increased ascorbate concentrations with plant ferritin; the damage is weaker with horse ferritin and less dependent on ascorbate concentrations.",{"EN":2142},"Dynamic equilibria in iron uptake and release by ferritin",{"VOID":2144},"Ames BN, Cathcart R, Schwiers E, Hochstein P. 1981 Uric acid provides an antioxidant defense in humans against oxidant and radical-caused aging and cancer: a hypothesis.Proc Natl Acad Sci USA 78, 6858–6862.\nAndrews SC, Arosio P, Bottke W,et al. 1992 Structure, function, and evolution of ferritins.J Inorg Biochemistry 47, 161–174.\nAruoma OI, Halliwell B. 1987 Superoxide-dependent and ascorbatedependent formation of hydroxyl radicals from hydrogen peroxide in the presence of iron.Biochem J 241, 273–278.\nBalla G, Jacob HS, Balla J,et al. 1992 Ferritin: a cytoprotective antioxidant stratagem of endothelium.J Biol Chem 267, 18148–18153.\nBienfait HF, Van Den Breil ML. 1980 Rapid mobilisation of ferritin iron by ascorbate in the presence of oxygen.Biochem Biophys Acta 631, 507–510.\nBoyer RF, Clark HM, LaRoche AP. 1988 Reduction and release of ferritin iron by plant phenolics.J Inorg Biochem 32, 171–181.\nBriat JF, Labouré AM, Laulhère JP,et al. 1995 Molecular and cellular biology of plant ferritins. In: Abadia, J, ed.Iron Nutrition in Soils and Plants. Dordrecht: Kluwer.\nBridges KR, Hoffman KE. 1986 The effect of ascorbic acid on the intracellular metabolism of iron and ferritin.J Biol Chem 261, 14273–14277.\nCairo G, Tacchini L, Pogliaghi G, Anzon E, Tomasini A, Bernelli-Zazzera A. 1995 Induction of ferritin synthesis by oxidative stress. Transcriptional and post-transcriptional regulation by expansion of the ‘free’ iron pool.J Biol Chem 270, 700–703.\nCrichton RR. 1991Inorganic Biochemistry of Iron Metabolism. Chichester: Ellis Horwood; 190–212.\nFloyd RA. 1981 DNA-ferrous iron-catalysed hydroxyl free radical formation from hydrogen peroxide.Biochem Biophys Res Commun 99, 1209–1215.\nGrady JK, Chen Y, Chasteen ND, Harris DC. 1989 Hydroxyl radical production during oxidative deposition of iron in ferritin.J Biol Chem 264, 20224–20229.\nHalliwell B. 1987 Oxidative damage, lipid peroxidation and antioxidant protection in chloroplasts.Chem Phys Lipids 44, 327–340.\nHarrison PM, Lilley TH. 1989 Ferritin. In: Loehred TM, ed.Iron Carriers and Iron Proteins (Physical Bioinorganic Chemistry Series 5). Weinheim: VCH.\nLaulhère JP, Briat JF. 1993 Iron release and uptake by plant ferritin: effects of pH, reduction and chelation.Biochem J 290, 693–699.\nLaulhère JP, Lescure AM, Briat JF. 1988 Purification and characterisation of ferritin from maize, pea, and soyabean seeds.J Biol Chem 263, 10289–10294.\nLaulhère JP, Labouré AM, Briat JF. 1990 Mechanism of the transition from plant ferritin to phytosiderin.J Biol Chem 264, 3629–3635.\nLaw MY, Charles SA, Halliwell B. 1983 Gluthatione and ascorbic acid in spinach (Spinacia oleracea) chloroplasts. The effect of hydrogene peroxide and of paraquat.Biochem J 210, 899–903.\nLobréaux S, Briat JF. 1991 Ferritin accumulation in different organs of pea (Pisum sativum) during development.Biochem J 274, 601–606.\nLobréaux S, Yewdall SJ, Briat JF, Harrison PM. 1992 Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin.Biochem J 288, 931–939.\nMiller JPG, Perkins DJ. 1969 Model experiments for the study of iron transfer from transferrin to ferritin.Eur J Biochem 10, 146–151.\nRohrer JS, Joo MS, Dartyge E, Sayers DE, Fontaine A, Theil EC. 1987 Stabilization of iron in a ferrous form by ferritin.J Biol Chem 262, 13385–13387.\nRohrer JS, Frankel RB, Papaefthymiou GC, Theil EC. 1989 Protein coats of ferritin can sequester large amounts of ferrous iron.Inorg Chem 28, 3393–3395.\nSun S, Chasteen ND. 1992 Ferroxidase kinetics of horse spleen apoferritin.J Biol Chem 267, 25160–25166.\nToyokuni S, Sagripanti JL. 1992 Iron mediated DNA damage: sensitive detection of DNA strand breakage catalysed by iron.J Inorg Biochem 47, 241–248.\nTreffy A, Sowerby JM, Harrison PM. 1979 Oxidant specificity in ferritin formation.FEBS Lett 100, 33–36.\nvan der Mark F, de Lange T, Bienfait HF. 1981 The role of ferritin in developing primary bean leaves under various light conditions.Planta 153, 338–342.\nWade VJ, Teffry A, Laulhère JP,et al. 1993 Structure and composition of ferritin cores from pea seed (Pisum sativum).Biochem Biophys Acta 1161, 91–96.\nXu B, Chasteen ND, 1991 Iron oxidation chemistry in ferritin.J Biol Chem 266, 19965–19970.",{"VOID":2146},"10.1007\u002FBF00817931","http:\u002F\u002Flink.springer.com\u002F10.1007\u002FBF00817931",[2149,2164,2186],{"id":2150,"sortIndex":32,"researcher":28,"roles":2151,"affiliations":2152,"properties":2161},"e7ea61f8-be38-46c8-879e-ce9fcb9f0f14",[1047],[2153],{"id":2154,"sortIndex":32,"affiliation":2155,"properties":28},"bc0fe0e9-9f06-47ed-9c3f-eb590eb9ca11",{"id":2154,"createTime":28,"updateTime":28,"relativeEntities":2156,"slug":28,"properties":2157,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2160,"statistic":28},[],{"title":2158},{"VI":2159},"Chimie Bioinorganioque, LEDSS, Université J. Fourier, Grenoble, France",[],{"title":2162},{"VI":2163},"Jean Pierre Laulhére",{"id":2165,"sortIndex":40,"researcher":28,"roles":2166,"affiliations":2167,"properties":2183},"56f31714-ad90-4734-a851-2beb156c7f98",[1047],[2168,2174],{"id":2154,"sortIndex":32,"affiliation":2169,"properties":28},{"id":2154,"createTime":28,"updateTime":28,"relativeEntities":2170,"slug":28,"properties":2171,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2173,"statistic":28},[],{"title":2172},{"VI":2159},[],{"id":2175,"sortIndex":40,"affiliation":2176,"properties":2182},"7de85e7d-6634-4774-825d-bba1c2c436dd",{"id":2175,"createTime":28,"updateTime":28,"relativeEntities":2177,"slug":28,"properties":2178,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2181,"statistic":28},[],{"title":2179},{"VI":2180},"Biologia Fundamental y Ciencias de la Salud, Universitat de les Illes Balears, Palma de Mallorca, Spain",[],{},{"title":2184},{"VI":2185},"Francisca Barcelò",{"id":2187,"sortIndex":123,"researcher":28,"roles":2188,"affiliations":2189,"properties":2196},"c40cf055-f048-412e-873d-c71321da53c5",[1047],[2190],{"id":2154,"sortIndex":32,"affiliation":2191,"properties":28},{"id":2154,"createTime":28,"updateTime":28,"relativeEntities":2192,"slug":28,"properties":2193,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2195,"statistic":28},[],{"title":2194},{"VI":2159},[],{"title":2197},{"VI":2198},"Marc 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pronounced argyrosis caused by adding AgCl to the feed of laboratory rats efficiently mimics the deficiency of ceruloplasmin (CP) ferroxidase activity. Bringing the concentration of AgCl in the feedstuff of lactating rats to 250 mg % and keeping their progeny (Ag-rats) for 3 months on the same silver-containing feed provided the serum iron content 1.4 times lower than that in the control group. Besides, the ferroxidase activity of CP dropped to zero. In CP purified from sera of Ag-rats two copper ions were substituted with two silver ions. Using rat models of both post-hemorrhagic and hemolytic anemia we showed that the deficiency of CP ferroxidase activity in Ag-rats affects the iron content in serum, though does not prevent the recovery of hemoglobin level accompanied by exhaustion of iron caches in liver and spleen. When apo-lactoferrin (apo-LF) was administered to Ag-rats suffering from either post-hemorrhagic or hemolytic anemia, both hemoglobin and serum iron were restored more rapidly than in the control animals. In independent experiments Ag-rats were compared with those fed on regular diet and the former displayed a prolonged 3-day stabilization of hypoxia-inducible factors 1 and 2 alpha (HIF-1a and HIF-2a) along with an increased serum concentration of erythropoietin. Introduction to Ag-rats of active CP separately or together with apo-LF reduced that effect to 1 day only. It is concluded that saturation of apo-LF with iron, provided by active CP, can strongly affect its protective capacity.",{"EN":2270},"Functional link between ferroxidase activity of ceruloplasmin and protective effect of apo-lactoferrin: studying rats kept on a silver chloride diet",{"VOID":2272},"Aisen P, Listowsky I (1980) Iron transport and storage proteins. Annu Rev Biochem 49:357–393\nAnderson NL, Nance SL, Pearson TW et al (1982) Specific antiserum staining of two-dimensional electrophoretic patterns of human plasma proteins immobilized on nitrocellulose. Electrophoresis 3:135–142\nAnderson GJ, Murphy TL, Cowley L et al (1998) Mapping the gene for sex-linked anemia: an inherited defect of intestinal iron absorption in the mouse. Genomics 48:34–39\nBirgens HS (1994) The monocytic receptor for lactoferrin and its involvement in lactoferrin-mediated iron transport. Adv Exp Med Biol 357:99–109\nBradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254\nCervello V, Barabini E (1894) Sul potere ematogeno dei metallic pesanti. Tipogr Ed Tempo, Palermo\nCherukuri S, Potla R, Sarkar J et al (2005) Unexpected role of ceruloplasmin in intestinal iron absorption. Cell Metab 2:309–319\nCutone A, Frioni A, Berlutti F et al (2014) Lactoferrin prevents LPS-induced decrease of the iron exporter ferroportin in human monocytes\u002Fmacrophages. Biometals 27:807–813\nDavis BJ (1964) Disk elecrtophoresis. II. Method and application to human serum proteins. Ann N Y Acad Sci 121:404–427\nDe Domenico I, Ward DMcV, di Patti MCB et al (2007) Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin. EMBO J 26:2823–2831\nErel O (1998) Automated measurement of serum ferroxidase activity. Clin Chem 44:2313–2319\nFling SP, Gregerson DS (1986) Peptide and protein molecular weight determination by electrophoresis using a high-molarity tris buffer system without urea. Anal Biochem 155:83–88\nGruen LC (1975) Interaction of amino acids with silver(I) ions. Biochim Biophys Acta 386:270–274\nHarris ZL, Durley AP, Man TK et al (1999) Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. PNAS 96:10812–10817\nHart EB, Steenbock H, Waddell J et al (1928) Iron in nutrition. VII. Copper as a supplement to iron for hemoglobin building in the rat. J Biol Chem 77:97–812\nHodgson GS (1973) Properties of haemopoietic stem cells in phenylhydrazine treated mice. Cell Tissue Kinet 6:199–208\nJeong SY, David S (2003) GPI-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system. J Biol Chem 278:27144–27148\nLahey ME, Gubler CJ, Chase MS et al (1952) Studies on copper metabolism. II. Hematologic manifestations of copper deficiency in swine. Blood 7:1053–1074\nLaurell CB (1967) Quantitative estimation of proteins by electrophoresis in antibody-containing agarose gel. In: Peeters H (ed) Protides of the biological fluids. Elsevier, Amsterdam\nMasson PL (1970) In: Arscia SA (ed) Proteine des Secretions Externes et des Leucocytes Neutrophiles. La Lactoferrine, Brussels\nMendini L (1862) Di un rimedio per l’amenorrea et di altro per la sordita ipostenica. Gazz Med Ital Prov Venete 5:36–37\nNguyen DN, Jiang P, Stensballe A et al (2016) Bovine lactoferrin regulates cell survival, apoptosis and inflammation in intestinal epithelial cells and preterm pig intestine. J Proteom 139:95–102\nNoyer M, Dwulet FE, Hao YL, Putnam FW (1980) Purification and characterization of undergraded human ceruloplasmin. Anal Biochem 102:450–458\nPark Y-G, Moon J-H, Park S-Y (2014) Lactoferrin from bovine colostrum regulates prolyl hydroxylase 2 activity and prevents prion protein-mediated neuronal cell damage via cellular prion protein. Neuroscience 274:187–197\nPribyl T, Schreiber V, Jahodová J (1980) Inhibition of rat serum polyphenoloxidase activity by silver ions abolished by administration of copper ions. Folia Biol (Praha) 261:47–52\nPulina MO, Sokolov AV, Zakharova ET et al (2010) Effect of lactoferrin on consequences of acute experimental hemorrhagic anemia in rats. 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Gastroenterology 146:630–642\nShavlovski MM, Chebotar NA, Konopistseva LA et al (1995) Embryotoxicity of silver ions is diminished by ceruloplasmin—further evidence for its role in the transport of copper. Biometals 8:122–128\nSokolov AV, Pulina MO, Zakharova ET et al (2005a) Effect of lactoferrin on the ferroxidase activity of ceruloplasmin. Biochemistry (Moscow) 70:1015–1019\nSokolov AV, Zakharova ET, Shavlovskii MM et al (2005b) Isolation of stable human ceruloplasmin and its interaction with salmon protamine. Bioorg Khim 31:269–279\nSokolov AV, Pulina MO, Kristiyan AV et al (2006a) A study of recombinant human lactoferrin secreted in milk of transgenic mice. Dokl Biochem Biophys 411:336–368\nSokolov AV, Pulina MO, Zakharova ET et al (2006b) Identification and isolation from breast milk of ceruloplasmin–lactoferrin complex. Biochemistry (Mosc) 71:160–166\nSokolov AV, Ageeva KV, Pulina MO et al (2009) Effect of lactoferrin on oxidative features of ceruloplasmin. Biometals 22:521–529\nSokolov AV, Kostevich VA, Romanico DN et al (2012) Two-stage method for purification of ceruloplasmin based on its interaction with neomycin. Biochemistry (Mosc) 77:631–638\nTopham RW, Frieden E (1970) Identification and purification of a non-ceruloplasmin ferroxidase of human serum. J Biol Chem 245:6698–6705\nvan Snick JL, Masson PL, Heremans JF (1974) The involvement of lactoferrin in the hyposideremia of acute inflammation. J Exp Med 140:1068–1084\nVulpe CD, Kuo YM, Murphy TL et al (1999) Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat Genet 21:195–199\nWarnecke C, Zaborowska Z, Kurreck J et al (2004) Differentiating the functional role of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha (EPAS-1) by the use of RNA interference: erythropoietin is a HIF-2alpha target gene in Hep3B and Kelly cells. FASEB J 18:1462–1464\nYoshida K, Furihata K, Takeda S et al (1995) A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans. Nat Genet 9:267–272\nZaitsev VN, Zaitseva I, Papiz M et al (1999) An X-ray crystallographic study of the binding center of azide inhibitor and organic substrates of ceruloplasmin, a multi-copper oxidase in plasma. J Biol Inorg Chem 4:579–587\nZakharova ET, Vasil’ev VB, Gorbunova VN, Shavlovskiĭ MM (1983) Isolation and physico-chemical properties of rat ceruloplasmin. Biokhimiia 48:1709–1720\nZakharova ET, Shavlovski MM, Bass MG et al (2000) Interaction of lactoferrin with ceruloplasmin. Arch Biochem Biophys 374:222–228\nZakharova ET, Kostevich VA, Sokolov AV et al (2012) Human apo-lactoferrin as a physiological mimetic of hypoxia stabilizes hypoxia-inducible factor-1 alpha. 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this study, Ni–Ti alloy and stainless steal were exposed to artificial saliva containing fibrinogen, IgG or mucin, and the resultant corrosion behavior was studied. The purpose was to determine the mechanisms by which different types of protein contribute to corrosion. The effect of different proteins on the electrochemical resistance of Ni–Ti and SS was tested by potentiodynamic polarization, and the repair capacity of passivation film was tested by cyclic polarization measurements. The dissolved corrosion products were determined by ICP-OES, and the surface was analyzed by SEM and AFM. The results showed fibrinogen, IgG or mucin could have different influences on the susceptibility to corrosion of the same alloy. Adding protein lead to the decrease of corrosion resistance of SS, whereas protein could slow down the corrosion process of Ni–Ti. For Ni–Ti, adding mucin could enhance the corrosion stability and repair capacity of passivation film. The susceptibility to pitting corrosion of Ni–Ti and stainless steal in fibrinogen AS is not as high as mucin and IgG AS. There are different patterns of deposition formation on the metal surface by different types of protein, which is associated with their effects on the corrosion process of the alloys.",{"EN":2458},"The effect of mucin, fibrinogen and IgG on the corrosion behaviour of Ni–Ti alloy and stainless steel",{"VOID":2460},"ASTM Standard F 2129–06, ASTM International (2006) Standard test method for conducting cyclic potentiodynamic polarization measurements to determine the corrosion susceptibility of small implant devices, ASTM Standard F 2129–06, ASTM International, West Conshohocken, PA\nBelmar-Beiny MT, Fryer PJ (1993) Preliminary stages of fouling from whey protein solutions. J Dairy Res 60(4):467–483\nBlake DA, Jones RM, Ii RCB, Pavlov AR, Darwish IA, Yu H (2001) Antibody-based sensors for heavy metal ions. 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Mater Sci Eng 55:267–271",{"VOID":2462},"10.1007\u002Fs10534-017-0012-3","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10534-017-0012-3",[2465,2480,2493,2506],{"id":2466,"sortIndex":32,"researcher":28,"roles":2467,"affiliations":2468,"properties":2477},"e362bc07-c9c7-4f01-9ec3-1cd657aa67d8",[1047],[2469],{"id":2470,"sortIndex":32,"affiliation":2471,"properties":28},"eb64659e-8da8-432c-82bf-90bfd2246aa9",{"id":2470,"createTime":28,"updateTime":28,"relativeEntities":2472,"slug":28,"properties":2473,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2476,"statistic":28},[],{"title":2474},{"VI":2475},"The Stomatological Hospital of Southern Medical University, Guangdong Provincial Stomatological Hospital, Guangzhou, People’s Republic of China",[],{"title":2478},{"VI":2479},"Zhang 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(Cd) is a nephrotoxic environmental pollutant that causes insidious injury to the proximal tubule that results in severe polyuria and proteinuria. Cystatin C is a low molecular weight protein that is being evaluated as a serum and urinary biomarker for various types of ischemic and nephrotoxic renal injury. The objective of the present study was to determine if cystatin C might be a useful early biomarker of Cd nephrotoxicity. Male Sprague–Dawley rats were given daily injections of Cd for up to 12 weeks. At 3, 6, 9 and 12 weeks, urine samples were analyzed for cystatin C, protein, creatinine, β2 microglobulin and kidney injury molecule-1. The results showed that Cd caused a significant increase in the urinary excretion of cystatin C that occurred 3–4 weeks before the onset of polyuria and proteinuria. Serum levels of cystatin C were not altered by Cd. Immunolabeling studies showed that Cd caused the relocalization of cystatin C from the cytoplasm to the apical surface of the epithelial cells of the proximal tubule. The Cd-induced changes in cystatin C labelling paralleled those of the brush border transport protein, megalin, which has been implicated as a mediator of cystatin C uptake in the proximal tubule. These results indicate that Cd increases the urinary excretion of cystatin C, and they suggest that this effect may involve disruption of megalin-mediated uptake of cystatin C by epithelial cells of the proximal tubule.",{"EN":2592},"Evaluation of cystatin C as an early biomarker of cadmium nephrotoxicity in the rat",{"VOID":2594},"citation_journal_title=Environ Health Perspect; citation_title=Tubular and glomerular kidney effects in Swedish women with low environmental cadmium exposure; citation_author=A Akesson, T Lundh, M Vahter, P Bjellerup, J Lidfeldt, C Nerbrand, G Samsioe, U Stromberg, S Skerfving; citation_volume=113; citation_publication_date=2005; citation_pages=1627-1631; citation_doi=10.1289\u002Fehp.8033; citation_id=CR1\ncitation_journal_title=Int J Urol; citation_title=Cadmium nephrotoxicity and evacuation from the body in a rat modeled subchronic intoxication; citation_author=T Aoyagi, K Hayakawa, K Miyaji, H Ishikawa, M Hata; citation_volume=10; citation_publication_date=2003; 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