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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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Recently, various cellular pathogeneses, including tumorigenesis and metastasis, have been reported to be associated with mitochondrial homeostasis. Consequently, exploiting the correlation between dysfunctional mitochondria and tumor progression has been implicated in the understanding of tumorigenesis, tumor metastasis, and chemoresistance, along with novel strategies to develop cancer therapeutics. To comprehensively understand the role of the mitochondria in cancer metastasis, it is necessary to resolve thousands of mitochondrial proteins and their post-translational modifications with high-throughput global assessments. We introduce mitochondrial proteomic strategies in this review and a discussion on their recent findings related to cancer metastasis. Additionally, the mitochondrial respiratory chain is believed to be a major site for ROS production, and elevated ROS is likely a key source to trigger dysfunctional mitochondria and impaired mitochondrial metabolism that subsequently contribute to the development of cancer progression. Equipment-based metabolomic analysis now allows the monitoring of disease progression and diagnosis. These newly emerging techniques, including proteomics, redox-proteomics, and metabolomics, are described in this review.",{"EN":1019},"Targeting proteomics to investigate metastasis-associated mitochondrial proteins",{"VOID":1021},"Andreyev AY et al (2005) Mitochondrial metabolism of reactive oxygen species. Biochemistry (Mosc) 70:200–214\nBlagoev B et al (2003) A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat Biotechnol 21:315–318\nBoveris A, Chance B (1973) The mitochondrial generation of hydrogen peroxide. 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Cancer Res 67:1472–1486\nChen YW et al (2011) Mitochondrial proteomics analysis of tumorigenic and metastatic breast cancer markers. Funct Integr Genomics 11:225–239\nChou HC et al (2012) Proteomic and redox-proteomic analysis of berberine-induced cytotoxicity in breast cancer cells. J Proteomics 75:3158–3176\nDa Cruz S et al (2005) Building the mitochondrial proteome. Exp Rev Proteomics 2:541–551\nDeSouza L et al (2005) Search for cancer markers from endometrial tissues using differentially labeled tags iTRAQ and cICAT with multidimensional liquid chromatography and tandem mass spectrometry. J Proteome Res 4:377–386\nDunkley TP et al (2004) The use of isotope-coded affinity tags (ICAT) to study organelle proteomes in Arabidopsis thaliana. Biochem Soc Trans 32:520–523\nEvans C et al. (2012) An insight into iTRAQ: where do we stand now? Anal Bioanal Chem. doi:10.1007\u002Fs00216-012-5918-6\nFenn JB et al (1989) Electrospray ionization for mass spectrometry of large biomolecules. 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Analyst 137:293–300",{"VOID":1023},"10.1007\u002Fs10863-012-9466-8","PUBLICATION","Auto Verify","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10863-012-9466-8",[1028,1044],{"id":1029,"sortIndex":32,"researcher":28,"roles":1030,"affiliations":1032,"properties":1041,"displayName":1043,"givenName":28,"familyName":28},"f2d3f23f-694c-4be6-8f48-3ee243c4b729",[1031],"AUTHOR",[1033],{"id":1034,"sortIndex":32,"affiliation":1035,"properties":28},"98b86e5a-8464-4a52-9951-89b918526ec0",{"id":1034,"createTime":28,"updateTime":28,"relativeEntities":1036,"slug":28,"properties":1037,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1040,"statistic":28},[],{"title":1038},{"VI":1039},"Department of Applied Science, National Hsinchu University of Education, Hsinchu, Taiwan",[],{"title":1042},{"VI":1043},"Hsiu-Chuan Chou",{"id":1045,"sortIndex":40,"researcher":28,"roles":1046,"affiliations":1047,"properties":1056,"displayName":1058,"givenName":28,"familyName":28},"8e2b572d-a120-45c5-95e5-eecca298acb0",[1031],[1048],{"id":1049,"sortIndex":32,"affiliation":1050,"properties":28},"a87d037b-57cb-4bdd-a71e-f61201feafab",{"id":1049,"createTime":28,"updateTime":28,"relativeEntities":1051,"slug":28,"properties":1052,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1055,"statistic":28},[],{"title":1053},{"VI":1054},"Institute of Bioinformatics and Structural Biology, Department of Medical Science, National Tsing Hua University, Hsinchu, Taiwan",[],{"title":1057},{"VI":1058},"Hong-Lin Chan","ARTICLE",{"url":1026,"publisher":1061,"properties":1107},{"id":868,"createTime":869,"updateTime":870,"relativeEntities":1062,"slug":872,"properties":1063,"entityType":25,"verifyStatus":882,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":32,"subjectFields":1067,"manageAffiliations":1076,"indexDatabases":1087,"url":28,"thumbnailPath":28,"statistic":1102,"gsStatistic":28,"type":55,"analyzePriority":28},[],{"issn":1064,"title":1065,"eissn":1066},{"VOID":877},{"EN":879},{"VOID":875},[1068,1072],{"id":885,"createTime":28,"updateTime":28,"relativeEntities":1069,"label":1070,"description":1071,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":888},{},{"id":891,"createTime":28,"updateTime":28,"relativeEntities":1073,"label":1074,"description":1075,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":894},{},[1077,1082],{"id":898,"createTime":28,"updateTime":28,"relativeEntities":1078,"slug":28,"properties":1079,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1081,"statistic":28},[],{"title":1080},{"EN":902},[904],{"id":906,"createTime":28,"updateTime":28,"relativeEntities":1083,"slug":28,"properties":1084,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1086,"statistic":28},[],{"title":1085},{"EN":910},[904],[1088,1095],{"id":914,"indexDatabase":1089,"url":28,"indexYears":28,"academicFieldIds":1094,"indexDatabaseRanking":28},{"id":916,"createTime":28,"updateTime":28,"relativeEntities":1090,"label":1091,"description":1092,"key":923,"publicationTags":1093,"standard":28},[],{"EN":919,"VI":919},{"EN":921,"VI":922},[925,813],[927,928],{"id":930,"indexDatabase":1096,"url":936,"indexYears":937,"academicFieldIds":1101,"indexDatabaseRanking":941},{"id":775,"createTime":28,"updateTime":28,"relativeEntities":1097,"label":1098,"description":1099,"key":781,"publicationTags":1100,"standard":28},[],{"EN":778,"VI":778},{"EN":778,"VI":780},[783],[939,940],{"impactFactor":32,"impactFactorByYear":1103,"i10Index":570,"i10IndexLast5Year":48,"totalPublication":947,"totalPublicationByYear":1104,"totalCitation":949,"totalCitationByYear":1105,"totalCitationPerPublication":972,"totalCitationPerPublicationByYear":1106,"hindexLast5Year":206,"hindex":206},{"2012":440,"2013":440,"2014":582,"2015":224,"2016":221,"2017":691,"2018":944,"2019":945,"2020":289,"2021":946,"2022":368,"2023":171},{"1970":131,"1971":129,"1972":136,"1973":132,"1974":126,"1975":127,"1976":127,"1977":127,"1978":357,"1979":48,"1980":128,"1981":128,"1982":136,"1983":135,"1984":140,"1985":134,"1986":122,"1987":202,"1988":148,"1989":69,"1990":69,"1991":142,"1992":149,"1993":149,"1994":279,"1995":201,"1996":152,"1997":139,"1998":141,"1999":137,"2000":280,"2001":150,"2002":147,"2003":141,"2004":150,"2005":196,"2006":132,"2007":328,"2008":279,"2009":149,"2010":137,"2011":279,"2012":328,"2013":278,"2014":149,"2015":69,"2016":150,"2017":147,"2018":136,"2019":134,"2020":137,"2021":196,"2022":135,"2023":133,"2024":126},{"1970":951,"1971":131,"1972":129,"1973":952,"1974":357,"1975":202,"1976":46,"1977":137,"1978":352,"1979":127,"1980":435,"1982":325,"1983":49,"1984":215,"1985":132,"1986":830,"1987":149,"1988":953,"1989":954,"1990":955,"1991":956,"1992":957,"1993":958,"1994":959,"1995":960,"1996":961,"2005":962,"2006":963,"2007":964,"2008":965,"2009":966,"2010":967,"2011":437,"2012":968,"2013":969,"2014":361,"2015":358,"2016":970,"2017":971,"2018":135,"2019":599,"2020":161,"2021":600,"2022":133,"2023":357,"2024":40},{"1970":974,"1971":232,"1972":171,"1973":975,"1974":369,"1975":444,"1976":461,"1977":976,"1978":977,"1979":978,"1980":979,"1982":980,"1983":169,"1984":981,"1985":982,"1986":983,"1987":363,"1988":984,"1989":985,"1990":986,"1991":987,"1992":988,"1993":989,"1994":990,"1995":991,"1996":992,"2005":993,"2006":994,"2007":995,"2008":996,"2009":48,"2010":997,"2011":998,"2012":999,"2013":1000,"2014":1001,"2015":1002,"2016":1003,"2017":1004,"2018":698,"2019":636,"2020":191,"2021":191,"2022":370,"2023":316,"2024":105},{"pages":1108,"volume":1110},{"VOID":1109},"629-634",{"VOID":1111},"44","2012-08-14",2012,[925,941],false,{"id":1117,"createTime":1118,"updateTime":1119,"relativeEntities":1120,"slug":1121,"properties":1122,"entityType":1024,"verifyStatus":26,"verifyTime":1119,"verifyNote":1025,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":1131,"fullTextUrl":28,"authors":1132,"publicationType":1059,"publisherRelationship":1148,"citationCount":28,"citationInfo":28,"publishDate":1200,"publishYear":1201,"citationAnalyzeStatus":882,"lastCitationAnalyze":28,"indexDatabases":1202,"openAccess":28,"references":28,"isForceReanalyzing":1115},"01d74d70-a607-40db-8df0-f47285c614d7","2024-01-20T09:57:11.723+00:00","2024-12-23T07:58:31.418+00:00",[],"Functional-binding-of-cardiolipin-to-cytochromec-oxidase",{"abstract":1123,"title":1125,"references":1127,"doi":1129},{"EN":1124},"Bovine cytochromec oxidase usually contains 3–4 mol of tightly bound cardiolipin per cytochromeaa\n3 complex. At least two of these cardiolipins are required for full electron transport activity. Without the tightly bound cardiolipin, cytochromec oxidase has only 40–50% of its original activity when assayed in detergents that support activity, e.g., dodecyl maltoside. By measuring the restoration of electron transport activity, functional binding constants for cardiolipin and a number of cardiolipin analogues have been evaluated (K\n\nd,app=1 µM for cardiolipin). These binding constants agree reasonably well with direct measurement of the binding using [14C]-acetyl-cardiolipin (K\n\n                  d\n                \u003C0.1 µM) when the enzyme is solubilized with Triton X-100. These data are discussed in relationship to the wealth of data that is known about the association of cardiolipin with cytochromec oxidase and the other mitochrondrial electron transport complexes and transporters.",{"EN":1126},"Functional binding of cardiolipin to cytochromec oxidase",{"VOID":1128},"Adramovitch, D. A., Marsh, D., and Powell, G. L. (1990).Biochim. Biophys. Acta 1020 34–42.\nAl-Tai, W. F., Jones, M. G., Rashid, K., and Wilson, M. T. (1983).Biochem. J. 209 901–903.\nAl-Tai, W. F., Jones, M. G., and Wilson, M. T. (1984).Comp. Biochem. Physiol. 77B 609–616.\nAwasthi, Y. C., Chuang, T. F., Kennan, T. W., and Crane, F. L. (1971).Biochim. Biophys. Acta 226 42–52.\nBeleznai, Z., and Jancsik (1989).Biochem. Biophys. Res. Commun. 159 132–139.\nBeyer, K., and Klingenberg, M. (1985).Biochemistry 15 3821–3826.\nBligh, E. G., and Dyer, W. J. (1959).Can. J. Biochem. Physiol. 37 911–917.\nBrandolin, G., Doussiere, J., Gulik, A., Gulik-Krzywicki, T., Lauquin, G. J. M., and Vignais, P. V. (1980).Biochim. Biophys. Acta 592 592–614.\nBrierley, G. P., and Merola, A. J. (1962).Biochim. Biophys. Acta 64 205–217.\nCable, M. B., and Powell, G. L. (1980).Biochemistry 19 5679–5686.\ncheneval, D., and Carafoli, E. (1988).Eur. J. Biochem. 171 1–9.\nCheneval, D., Muller, M., and Carafoli, E. (1983).FEBS Lett. 159 123–126.\nCheneval, D., Muller, M., Toni, R., Ruetz, S., and Carafoli, E. (1985).J. Biol. Chem. 260 13003–13007.\nDale, M. P., and Robinson, N. C. (1988a).Biochemistry 27 8270–8275.\nDale, M., and Robinson, N. C. (1988b).FASEB J. 2, A774.\nDemant, E. J. F. (1983).Eur. J. Biochem. 137 113–118.\nDemant, E. J. F., and Jensen, P. K. (1983).Eur. J. Biochem. 132 551–556.\nDemel, R. A., Jordi, W., Lambrechts, H., van Damme, H., Hovius, R., and de Kruijff, B. (1989).J. Biol. Chem. 264 3988–3997.\nEilers, M., Endo, T., and Schatz, G. (1989).J. Biol. Chem. 264 2945–2950.\nFowler, W. T., Lambeth, J. D., and Powell, G. L. (1988).Chem. Phys. Lipids 47 261–271.\nFry, M., and Green, D. E. (1980).Biochem. Biophys. Res. Commun. 93 1238–1245.\nFry, M., and Green, D. E. (1981).J. Biol. Chem. 256 1874–1880.\nFry, M., Blondin, G. A., and Green, D. E. (1980).J. Biol. Chem. 255 9967–9970.\nGoormaghtigh, E., and Ruysschaert, J. (1984).Biochim. Biophys. Acta 779 271–288.\nGoormaghtigh, E., Chatelain, P., Caspers, J., and Ruysschaert, J. M. (1980).Biochim. Biophys. Acta 597 1–14.\nGoormaghtigh, E., Brasseur, R., and Ruysschaert, J. (1982).Biochem. Biophys. Res. Commun. 104 314–320.\nGoormaghtigh, E., Huart, P., Brasseur, R., and Ruysschaert, J.-M. (1986).Biochim. Biophys. Acta 861 83–94.\nHasinoff, B. B., and Davey, J. P. (1988).Biochem. J. 250 827–834.\nHill, B. C., Cook, K., and Robinson, N. C. (1988).Biochemistry 27 4741–4747.\nHoch, F. L. (1992).Biochim. Biophys. Acta 1113 71–133.\nIoannou, P. V., and Golding, B. T. (1979).J. Lipid Res. 17 279–318.\nKadenbach, B., Mende, P., Kolbe, H. V. J., Stipani, I., and Palmieri, F. (1982).FEBS Lett. 139 109–112.\nKadenbach, B., Jarausch, J., Hartmann, R., and Merle, P. (1983).Anal. Biochem.,129 517–521.\nKaplan, R. S., Pratt, R. D., and Pedersen, P. L. (1986).J. Biol. Chem. 261 12767–73.\nKnowles, P. F., Watts, A., and Marsh, D. (1981).Biochemistry 20 5888–5894.\nKramer, R., and Klingenberg, M. (1980).FEBS Lett. 119 257–260.\nKuppe, A., Mrsny, R. J., Shimizu, M., Firsan, S. J., Keana, J. F. W., and Griffith, O. H. (1987).Biochemistry 26 7693–7701.\nMahapatro, S. N., and Robinson, N. C. (1990).Biochemistry 29 764–770.\nMarsh, D., and Powell, G. L. (1988).Bioelectrochem. Bioenerg.,20 73–82.\nMende, P., Kolbe, H. V. J., Kadenbach, B., Stipani, I., and Palmieri, F. (1982).Eur. J. Biochem.,128 91–95.\nMende, P., Huther, J.-J., and Kadenbach, B. (1983).FEBS Lett. 158 331–334.\nMuller, M., Moser, R., Cheneval, D., and Carafoli, E. (1985).J. Biol. Chem.,260 3839–3843.\nMyers, M., Mayorga, O., Emtage, J., and Freire, E. (1987).Biochemistry 26 4309–4315.\nNalecz, K. A., Bolli, R., Wojtczak, L., and Azzi, A. (1986).Biochim. Biophys. Acta 851 29–37.\nNicolay, K., and deKruijff, B. (1987).Biochim. Biophys. Acta 892 320–330.\nNicolay, K., Timmers, R. J. M., Spoelstra, E., van der Neut, R., Fok, J. J., Huigen, Y., Verkleij, A. J., and de Kruijff, B. (1984).Biochim. Biophys. Acta 778 359–371.\nNishijima, S., Asami, Y., Uetake, N., Yamagoe, S., Ohta, A., and Shibuya, I. (1988).J. Bacteriol. 170 775–780.\nNoel, H., and Pande, S. V. (1986).Eur. J. Biochem. 155 99–102.\nOrtega-Lopez, J., and Robinson, N. C. (1993). unpublished data.\nOu, W.-J., Ito, A., Umeda, M., Inoue, K., and Omura, T. (1988).J. Biochem.,103 589–595.\nPowell, G. L., Knowles, P. F., and Marsh, D. (1985).Biochim. Biophys. Acta 816 191–194.\nPowell, G. L., Knowles, P. F., and Marsh, D. (1987).Biochemistry 26 8138–8145.\nRobinson, N. C. (1982).Biochemistry 21 184–188.\nRobinson, N. C. (1990).J. Lipid Res. 31 1513–1516.\nRobinson, N. C., and Capaldi, R. A. (1977).Biochemistry 16 375–380.\nRobinson, N. C., and Wiginton, D. (1985).J. Inorg. Biochem.,23 171–176.\nRobinson, N. C., Strey, F., and Talbert, L. (1980).Biochemistry 19 3656–3661.\nRobinson, N. C., Zborowski, J., and Talbert, L. H. (1990).Biochemistry 29 8962–8969.\nSpeck, S. H., Neu, C. A., Swanson, M. S., and Margoliash, E. (1983).FEBS Lett. 164 379–382.\nTamm, L. K. (1986).Biochemistry 25 7470–7476.\nThompson, D. A., and Ferguson-Miller, S. (1983).Biochemistry 22 3178–3187.\nVik, S. B., Georgevich, G., and Capaldi, R. A. (1981).Proc. Natl. Acad. Sci. USA 78 1456–1460.\nWatts, A., Marsh, D., and Knowles, P. F. (1978).Biochem. Biophys. Res. Commun. 81 403–409.\nYu, C., Yu, L., and King, T. E. (1975).J. Biol. Chem. 250 1383–1392.",{"VOID":1130},"10.1007\u002FBF00762857","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF00762857",[1133],{"id":1134,"sortIndex":32,"researcher":28,"roles":1135,"affiliations":1136,"properties":1145,"displayName":1147,"givenName":28,"familyName":28},"ca5c1a13-cc1c-434e-85a0-b75b93ea866d",[1031],[1137],{"id":1138,"sortIndex":32,"affiliation":1139,"properties":28},"662066b8-3420-4e88-91cc-60f31e3dccaf",{"id":1138,"createTime":28,"updateTime":28,"relativeEntities":1140,"slug":28,"properties":1141,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1144,"statistic":28},[],{"title":1142},{"VI":1143},"Department of Biochemistry, The University of Texas Health Science Center, San Antonio",[],{"title":1146},{"VI":1147},"Neal C. Robinson",{"url":1131,"publisher":1149,"properties":1195},{"id":868,"createTime":869,"updateTime":870,"relativeEntities":1150,"slug":872,"properties":1151,"entityType":25,"verifyStatus":882,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":32,"subjectFields":1155,"manageAffiliations":1164,"indexDatabases":1175,"url":28,"thumbnailPath":28,"statistic":1190,"gsStatistic":28,"type":55,"analyzePriority":28},[],{"issn":1152,"title":1153,"eissn":1154},{"VOID":877},{"EN":879},{"VOID":875},[1156,1160],{"id":885,"createTime":28,"updateTime":28,"relativeEntities":1157,"label":1158,"description":1159,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":888},{},{"id":891,"createTime":28,"updateTime":28,"relativeEntities":1161,"label":1162,"description":1163,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":894},{},[1165,1170],{"id":898,"createTime":28,"updateTime":28,"relativeEntities":1166,"slug":28,"properties":1167,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1169,"statistic":28},[],{"title":1168},{"EN":902},[904],{"id":906,"createTime":28,"updateTime":28,"relativeEntities":1171,"slug":28,"properties":1172,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1174,"statistic":28},[],{"title":1173},{"EN":910},[904],[1176,1183],{"id":914,"indexDatabase":1177,"url":28,"indexYears":28,"academicFieldIds":1182,"indexDatabaseRanking":28},{"id":916,"createTime":28,"updateTime":28,"relativeEntities":1178,"label":1179,"description":1180,"key":923,"publicationTags":1181,"standard":28},[],{"EN":919,"VI":919},{"EN":921,"VI":922},[925,813],[927,928],{"id":930,"indexDatabase":1184,"url":936,"indexYears":937,"academicFieldIds":1189,"indexDatabaseRanking":941},{"id":775,"createTime":28,"updateTime":28,"relativeEntities":1185,"label":1186,"description":1187,"key":781,"publicationTags":1188,"standard":28},[],{"EN":778,"VI":778},{"EN":778,"VI":780},[783],[939,940],{"impactFactor":32,"impactFactorByYear":1191,"i10Index":570,"i10IndexLast5Year":48,"totalPublication":947,"totalPublicationByYear":1192,"totalCitation":949,"totalCitationByYear":1193,"totalCitationPerPublication":972,"totalCitationPerPublicationByYear":1194,"hindexLast5Year":206,"hindex":206},{"2012":440,"2013":440,"2014":582,"2015":224,"2016":221,"2017":691,"2018":944,"2019":945,"2020":289,"2021":946,"2022":368,"2023":171},{"1970":131,"1971":129,"1972":136,"1973":132,"1974":126,"1975":127,"1976":127,"1977":127,"1978":357,"1979":48,"1980":128,"1981":128,"1982":136,"1983":135,"1984":140,"1985":134,"1986":122,"1987":202,"1988":148,"1989":69,"1990":69,"1991":142,"1992":149,"1993":149,"1994":279,"1995":201,"1996":152,"1997":139,"1998":141,"1999":137,"2000":280,"2001":150,"2002":147,"2003":141,"2004":150,"2005":196,"2006":132,"2007":328,"2008":279,"2009":149,"2010":137,"2011":279,"2012":328,"2013":278,"2014":149,"2015":69,"2016":150,"2017":147,"2018":136,"2019":134,"2020":137,"2021":196,"2022":135,"2023":133,"2024":126},{"1970":951,"1971":131,"1972":129,"1973":952,"1974":357,"1975":202,"1976":46,"1977":137,"1978":352,"1979":127,"1980":435,"1982":325,"1983":49,"1984":215,"1985":132,"1986":830,"1987":149,"1988":953,"1989":954,"1990":955,"1991":956,"1992":957,"1993":958,"1994":959,"1995":960,"1996":961,"2005":962,"2006":963,"2007":964,"2008":965,"2009":966,"2010":967,"2011":437,"2012":968,"2013":969,"2014":361,"2015":358,"2016":970,"2017":971,"2018":135,"2019":599,"2020":161,"2021":600,"2022":133,"2023":357,"2024":40},{"1970":974,"1971":232,"1972":171,"1973":975,"1974":369,"1975":444,"1976":461,"1977":976,"1978":977,"1979":978,"1980":979,"1982":980,"1983":169,"1984":981,"1985":982,"1986":983,"1987":363,"1988":984,"1989":985,"1990":986,"1991":987,"1992":988,"1993":989,"1994":990,"1995":991,"1996":992,"2005":993,"2006":994,"2007":995,"2008":996,"2009":48,"2010":997,"2011":998,"2012":999,"2013":1000,"2014":1001,"2015":1002,"2016":1003,"2017":1004,"2018":698,"2019":636,"2020":191,"2021":191,"2022":370,"2023":316,"2024":105},{"pages":1196,"volume":1198},{"VOID":1197},"153-163",{"VOID":1199},"25","1993-04-01",1993,[925,941],{"id":1204,"createTime":1205,"updateTime":1206,"relativeEntities":1207,"slug":1208,"properties":1209,"entityType":1024,"verifyStatus":26,"verifyTime":1206,"verifyNote":1025,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":1218,"fullTextUrl":28,"authors":1219,"publicationType":1059,"publisherRelationship":1248,"citationCount":28,"citationInfo":28,"publishDate":1300,"publishYear":1301,"citationAnalyzeStatus":882,"lastCitationAnalyze":28,"indexDatabases":1302,"openAccess":28,"references":28,"isForceReanalyzing":1115},"026c423a-ab60-4075-8dba-8eee76b1c8b9","2023-12-19T14:02:00.667+00:00","2024-12-23T01:27:13.999+00:00",[],"Synchronization-of-Na-K-pump-molecules-by-a-train-of-squared-pulses",{"abstract":1210,"title":1212,"references":1214,"doi":1216},{"EN":1211},"We experimentally studied the Na\u002FK pump currents evoked by a train of squared pulses whose pulse-duration is about the time course of Na-extrusion at physiological conditions. The magnitude of the measured pump current can be as much as three-fold of that induced by the traditional single pulse measurement. The increase in the pump current is directly dependent on the number of pre-pulses. The larger the number of the pre-pulses is, the higher the current magnitude can be obtained. At a particular number of pre-pulses, the pump current becomes saturated. These results suggest that a large number of pre-pulses may synchronize the pump molecules to work at the same pace. As a result, the pump molecules may extrude Na ions at the same time corresponding to the stimulation pulses, and pump in K ions at the same time during the pulse intervals. Therefore, the measured pump current is three-fold of that measured by a single pulse where the outward and inward pump currents are canceled each other.",{"EN":1213},"Synchronization of Na\u002FK pump molecules by a train of squared pulses",{"VOID":1215},"Apell HJ, Bersch B (1987) Oxonol VI as an optical indicator for membrane potentials in lipid vesicles. Biochim Biophys Acta 903:480–494\nAstumian RD (1997) Thermodynamics and Kinetics of a Brownian motor. Science 276:917–922\nAstumian (2003) Physical Review letter, Adiabatic pumping mechanism for ion motive ATPases V91(11)118102(4)\nBlank M, Soo L (1989) The effects of alternating currents on Na,K-ATPase function. Bioelectrchem Bioenerge 22:313–322\nBlank M, Soo L (1990) Ion activation of the Na,K-ATPase in alternating currents. Bioelectrochem Bioenergetics 24:51–61\nChen W, Wu W (2002) The asymmetric, rectifier-like I-V curve of the Na\u002FK pump transient currents in frog skeletal muscle fibers. Bioelectrochemistry 56:199–203\nChen W (2004) Supra-physiological membrane potential induced conformational changes in K channel conducting system of skeletal muscle fibers. Bioelectrochemistry 62:47–56\nChen W (2004) Evidence of electroconformational changes in membrane proteins: field-induced reductions in intra membrane nonlinear charge movement current. Bioelectrochemistry 63:333–335\nChen W (2005) Voltage dependence of the carrier-medicated ion transporters. Physics Review E, (in press)\nChen W (submitted) Synchronization modulation of the Na\\K pump molecules, Physical Review Letter\nDe Weer P, Gadsby DC, Rakowski RF (1989) Voltage dependence of the Na\u002FK pump. Annu. Rev. Physiol. 50:225–241\nDe Weer P, Gadsby DC, Rakowski RF (1989) Stoichiometry and voltage dependence of the Na\u002FK pump, In JC Skou, JG Norby, AB, Maunsbachy, M Esmann (eds.) The Na, K-ATPase, Part A: Molecular aspects, Progr. Clin. Biol. Res. 268A. A. R. Liss, New York, pp 421–434\nGadsby DC, Kimura J, Noma, A (1985) Voltage dependence of (Na\u002FK) pump current in isolated heart cells. Nature 315:63–65\nGadsby DC, Nakao M (1989) Steady-state current-voltage relationship of the Na\u002FK pump in guinea-pig ventricular myocytes. J Gen Physiol 94:511–537.\nGadsby DC, Bahinski A, Nakao M, Voltage dependence of Na\u002FK pump current (1989) Current topics in membrane and transport, (34):269–288\nHille B, Campbell DT (1976) An improved Vaseline gap voltage clamp for skeletal muscle fibers. J Gen Physiol 67:265–293\nHui CS, Chen W (1992) Separation of Q and Q charge components in frog twitch fibers with tetracaine. J Gen Physiol 99:985–1016\nHolmgren M, Wagg J, Bezanilla F, Rakowski RF, De Weer P, Gadsby DC (2000) Three distinct and sequential steps in the release of sodium ions by the Na+\u002FK+-ATPase. Nature Feb 24:403(6772):898–901\nIrving M, Maylie J, Sizto NL, Chandler WK (1987) Intrinsic optical and passive electrical properties of cut frog twitch fibers. J Gen Physiol 89:1–40\nKovacs L, Rios E, Schneider MF (1983) Measurement and modification of free calcium transients in frog skeletal muscle fibers by a metallochromic indicator dye. J Physiol 343:161–196\nLauger P, Apell H-J (1986) A microscopic model for the current-voltage behavior of the Na-K-pump. Eur Biophys J 13:309–321\nLauger P (1991) Electrogenic ion pumps, Sinauer Associates, Inc\nMarkin VS, Liu DS, Rosenberg MD, Tsong TY (1992) Resonance transduction of low level periodic signals by an enzyme: an oscillatory activation barrier model. Biophysical J 61(4):1045–1049\nNakao M, Gadsby DC (1989) [Na] and [K] dependence of the Na\u002FK pump current- voltage relationship in guinea pig ventricular myocytes. J Gen Physiol 94:539–565\nRakowski RF, Gadsby DC, De Weer P (1989) Stoichiometry and voltage–dependence of the sodium pump in voltage-champed, internally dialyzed squid giant axon. J Gen Physiol 93:903–941\nRakowski RF, Vasilets LA, Latona J, Schwarz W (1991) A negative slope in the current-voltage relationship of the Na+K+ pump in Xenopus oocytes produced by reduction of external [K]. J Membr Biol 121:177–187\nRakowski RF, Gadsby DC, DeWeer P (1997) Voltage dependence of the Na\u002FK pump. J Membrane Biol 155:105–112\nRobertson B, Astumian D (1991) Frequency dependence of catalyzed reactions in a weak oscillating field. J Chem Phys 94(11):7414–7419\nSerpersu EH, Tsong TY (1983) Stimulation of Rb-pumping activityof Na,K-ATPase in human erythrocytes with an external electric field. J Membrane Biol 74:191–201\nTeissie J, Tsong TY (1980) Evidence of voltage-induced channel opening in Na\u002FK ATPase of human erythrocyte membrane. J Membrane Biol 55:133–140\nTsong TY, Astumian RD (1986) Absorption and conversion of electric field energy by membrane bound ATPases. Bioelectrochem Bioenerg 15:457–476\nTsong TY, Astumian RD (1987) Electroconformational coupling and membrane protein function. Prog Biophys Molec Biol 50:1–45\nTsong TY (2002) Na,K-ATPase as a brownian motor: Electric field-induced conformational fluctuation leads to uphill pumping of cation in the absence of ATP. J Biol Phys V(28), 2:309–325\nXie TD, Chen YD, Marszalek P, Tsong TY (1994) Recognition and processing of randomly fluctuating electric signals by Na, K-ATPase. Biophys J 67:1247–1251\nXie TD, Marszalek P, Tsong TY (1997) Fluctuation-driven directional flow in biochemical cycle: further study of electric activation of Na, K pumps. Biophysical J (72):2496–2502",{"VOID":1217},"10.1007\u002Fs10863-006-9049-7","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10863-006-9049-7",[1220,1235],{"id":1221,"sortIndex":32,"researcher":28,"roles":1222,"affiliations":1223,"properties":1232,"displayName":1234,"givenName":28,"familyName":28},"b1327606-4ae8-45fe-af1e-d3342811e252",[1031],[1224],{"id":1225,"sortIndex":32,"affiliation":1226,"properties":28},"6095c04b-b49a-4c88-9a8d-fd5168e50762",{"id":1225,"createTime":28,"updateTime":28,"relativeEntities":1227,"slug":28,"properties":1228,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1231,"statistic":28},[],{"title":1229},{"VI":1230},"Center for Cellular and Molecular Biophysics, Department of Physics, University of South Florida, Tampa, USA",[],{"title":1233},{"VI":1234},"Wei 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1312,"gsPaper":1314,"references":1316,"doi":1318},{"EN":1311},"Thirteen different polypeptide subunits, each in one copy, five phosphatidyl ethanolamines and three phosphatidyl glycerols, two hemes A, three Cu ions, one Mg ion, and one Zn ion are detectable in the crystal structure of bovine heart cytochrome c oxidase in the fully oxidized form at 2.8 Å resolution. A propionate of hems a, a peptide unit (–CO–NH–), and an imidazole bound to CuA are hydrogen-bonded sequentially, giving a facile electron transfer path from CuA to heme a. The O2 binding and reduction site, heme a\n3, is 4.7 Å apart from CuB. Two possible proton transfer paths from the matrix side to the cytosolic side are located in subunit I, including hydrogen bonds and internal cavities likely to contain randomly oriented water molecules. Neither path includes the O2 reduction site. The O2 reduction site has a proton transfer path from the matrix side possibly for protons for producing water. The coordination geometry of CuB and the location of Tyr244 in subunit I at the end of the scalar proton path suggests a hydroperoxo species as the two electron reduced intermediate in the O2 reduction process.",{"EN":1313},"Crystal Structure of Bovine Heart Cytochrome c Oxidase at 2.8 Å Resolution",{"VOID":1315},"[\"239897252851903449\"]",{"VOID":1317},"Antholine, W. E., Kastran, D. H. 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Biochemistry 33, 3079-3086.\nWikström, M., Bogachev, A., Finel, M., Morgan, J. E., Puustinen, A., Raitio, M., Verkhovskaya, M., and Verkhovsky M. I. (1994). Biochim. Biophys. Acta 1187, 106-111.\nWilliams, R. J. P. (1995). Nature 376, 643.",{"VOID":1319},"10.1023\u002FA:1020595108560","2024-05-13T04:08:18.690+00:00","http:\u002F\u002Flink.springer.com\u002F10.1023\u002FA:1020595108560",[1323,1338,1351],{"id":1324,"sortIndex":32,"researcher":28,"roles":1325,"affiliations":1326,"properties":1335,"displayName":1337,"givenName":28,"familyName":28},"5c7b8fff-c09f-4e2a-a13d-a1a57f9bd748",[1031],[1327],{"id":1328,"sortIndex":32,"affiliation":1329,"properties":28},"9db3c12e-b359-4c3d-ac10-c711845d19b4",{"id":1328,"createTime":28,"updateTime":28,"relativeEntities":1330,"slug":28,"properties":1331,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1334,"statistic":28},[],{"title":1332},{"VI":1333},"Department of Life Science, Himeji Institute of Technology, Kamigohri, Japan",[],{"title":1336},{"VI":1337},"Shinya 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ofParacoccus-denitrificans",{"abstract":1429,"title":1432,"keywords":1435,"references":1437,"doi":1439},{"VI":1430,"EN":1431},"Paracoccus denitrificans là một loại vi khuẩn hiếm khí tùy thuận có khả năng điều chỉnh cơ sở hạ tầng trao đổi chất của nó, về số lượng và\u002Fhoặc chất lượng, phù hợp với điều kiện tăng trưởng hiện tại. Trong loại vi khuẩn này, hoạt động tương đối của các con đường dị hóa khác nhau chịu sự kiểm soát theo hệ thống thứ bậc. Trong sự hiện diện của oxy, hô hấp hiếu khí, cách chuyển điện tử hiệu quả nhất liên kết với phosphoryl hóa, là ưu tiên hàng đầu. Ở áp suất oxy cao, P. denitrificans tổng hợp một loại oxidase có ái lực tương đối thấp với oxy, trong khi تحت áp lực oxy, một oxidase có ái lực cao được hiện diện cụ thể. Trong điều kiện thiếu oxy, các con đường có hiệu suất chuyển đổi năng lượng tự do thấp hơn được kích thích. Trong sự hiện diện của nitrat, việc biểu hiện một số dehydrogenases đảm bảo sự tiếp tục của phosphoryl hóa oxy hóa thông qua quá trình khử nitrat. Sau khi xác định các thành phần cấu trúc liên quan đến cả mạng lưới hô hấp hiếu khí và kỵ khí của P. denitrificans, thách thức thú vị tiếp theo là tìm kiếm cái nhìn sâu sắc về sự điều hòa của nó. Hai điều hòa phiên mã gần đây đã được chứng minh là tham gia vào việc biểu hiện một số phức hợp hô hấp hiếu khí và\u002Fhoặc kỵ khí trong P. denitrificans. Việc hiểu biết về cơ chế điều hòa đang bắt đầu hình thành và hứa hẹn mang lại nhiều điều thú vị trong việc khám phá.","\nParacoccus denitrificans is a facultative anaerobic bacterium that has the capacity to adjust its metabolic infrastructure, quantitatively and\u002For qualitatively, to the prevailing growth condition. In this bacterium the relative activity of distinct catabolic pathways is subject to a hierarchical control. In the presence of oxygen the aerobic respiration, the most efficient way of electron transfer-linked phosphorylation, has priority. At high oxygen tensionsP. denitrificans synthesizes an oxidase with a relatively low affinity for oxygen, whereas under oxygen limitation a high-affinity oxidase appears specifically induced. During anaerobiosis, the pathways with lower free energy-transducing efficiency are induced. In the presence of nitrate, the expression of a number of dehydrogenases ensures the continuation of oxidative phosphorylation via denitrification. After identification of the structural components that are involved in both the aerobic and the anaerobic respiratory networks ofP. denitrificans, the intriguing next challenge is to get insight in its regulation. Two transcription regulators have recently been demonstrated to be involved in the expression of a number of aerobic and\u002For anaerobic respiratory complexes inP. denitrificans. Understanding of the regulation machinery is beginning to emerge and promises much excitement in discovery.",{"EN":1433,"VI":1434},"Regulation of oxidative phosphorylation: The flexible respiratory network ofParacoccus denitrificans","Điều hòa phosphoryl hóa oxy hóa: Mạng lưới hô hấp linh hoạt của Paracoccus denitrificans",{"VI":1436},"Paracoccus denitrificans, điều hòa hô hấp, phosphoryl hóa oxy hóa, vi khuẩn hiếm khí, mạng lưới trao đổi chất.",{"VOID":1438},"Adman, E. T. (1991).Adv. Protein Chem. 42, 145–197.\nBallard, A. L., and Ferguson, S. J. (1988).Eur. J. Biochem. 174, 207–212.\nBatut, J. and Boitard, P. (1994).Anton Leeuwenhoek Int. J. Gen. M. 66, 129–150.\nBell, L. C., Richardson, D. J., and Ferguson, S. J. (1990).FEBS Lett. 265, 85–87.\nBerks, B. C., Richardson, D. J., Robinson, C., Reilly, A., Aplin, R. T., and Ferguson, S. J. (1994).Eur. J. Biochem. 220, 117–124.\nBerks, B. C., Page, M. D., Richardson, D. J., Reilly, A., Cavill, A., Outen, F., and Ferguson, S. J. 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Although its molecular mechanism is largely unknown, recent biochemical, biophysical, and molecular biological studies have revealed that particular subunits and cofactors play an essential role in the energy-coupling reaction. Based on these latest experimental data, we exhaustively analyzed the sequence information available from evolutionarily related enzymes such as [NiFe] hydrogenases. We found significant and conserved sequence differences in the PSST\u002FNqo6\u002FNuoB, 49kDa\u002FNqo4\u002FNuoD, and ND1\u002FNqo8\u002FNuoH subunit homologs between complex I\u002FNDH-1 and [NiFe] hydrogenases. The alterations, especially in the postulated ligand motif for cluster N2 in the PSST\u002FNqo6\u002FNuoB subunits, appear to be evolutionarily important in determining the physiological function of complex I\u002FNDH-1. These observations led us to propose a hypothetical evolutionary scheme: during the course of evolution, drastic changes have occurred in the putative cluster N2 binding site in the PSST\u002FNqo6\u002FNuoB subunit and the progenitors of complex I\u002FNDH-1 have concurrently become to utilize a lipophilic electron\u002Fproton carrier such as Q as its physiological substrate. This scheme provides new insights into the structure and function relationship of complex I\u002FNDH-1 and may help us understand its energy-coupling mechanism.",{"EN":1714},"The Origin of Cluster N2 of the Energy-Transducing NADH–Quinone Oxidoreductase: Comparisons of Phylogenetically Related Enzymes",{"VOID":1716},"Ahlers, P. M., Zwicker, K., Kerscher, S., and Brandt, U. (2000). J. Biol. Chem. 275, 23577–23582.\nAlbracht, S. P. (1993). Biochim. Biophys. Acta 1144, 221–224.\nAndrews, S. C., Berks, B. C., McClay, J., Ambler, A., Quail, M. A., Golby, P., and Guest, J. R. (1997). 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Biochemistry 37, 11792–11796.",{"VOID":1718},"10.1023\u002FA:1010782903144","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1023\u002FA:1010782903144",[1721,1728],{"id":1722,"sortIndex":32,"researcher":28,"roles":1723,"affiliations":1724,"properties":1725,"displayName":1727,"givenName":28,"familyName":28},"6026b16a-30c7-49a8-8c49-49af7b715f51",[1031],[],{"title":1726},{"VI":1727},"Takahiro Yano",{"id":1729,"sortIndex":40,"researcher":28,"roles":1730,"affiliations":1731,"properties":1732,"displayName":1734,"givenName":28,"familyName":28},"e621ee8b-0ad0-4968-b37c-29cbfd62a467",[1031],[],{"title":1733},{"VI":1734},"Tomoko Ohnishi",{"url":1719,"publisher":1736,"properties":1782},{"id":868,"createTime":869,"updateTime":870,"relativeEntities":1737,"slug":872,"properties":1738,"entityType":25,"verifyStatus":882,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":32,"subjectFields":1742,"manageAffiliations":1751,"indexDatabases":1762,"url":28,"thumbnailPath":28,"statistic":1777,"gsStatistic":28,"type":55,"analyzePriority":28},[],{"issn":1739,"title":1740,"eissn":1741},{"VOID":877},{"EN":879},{"VOID":875},[1743,1747],{"id":885,"createTime":28,"updateTime":28,"relativeEntities":1744,"label":1745,"description":1746,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":888},{},{"id":891,"createTime":28,"updateTime":28,"relativeEntities":1748,"label":1749,"description":1750,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":894},{},[1752,1757],{"id":898,"createTime":28,"updateTime":28,"relativeEntities":1753,"slug":28,"properties":1754,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1756,"statistic":28},[],{"title":1755},{"EN":902},[904],{"id":906,"createTime":28,"updateTime":28,"relativeEntities":1758,"slug":28,"properties":1759,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1761,"statistic":28},[],{"title":1760},{"EN":910},[904],[1763,1770],{"id":914,"indexDatabase":1764,"url":28,"indexYears":28,"academicFieldIds":1769,"indexDatabaseRanking":28},{"id":916,"createTime":28,"updateTime":28,"relativeEntities":1765,"label":1766,"description":1767,"key":923,"publicationTags":1768,"standard":28},[],{"EN":919,"VI":919},{"EN":921,"VI":922},[925,813],[927,928],{"id":930,"indexDatabase":1771,"url":936,"indexYears":937,"academicFieldIds":1776,"indexDatabaseRanking":941},{"id":775,"createTime":28,"updateTime":28,"relativeEntities":1772,"label":1773,"description":1774,"key":781,"publicationTags":1775,"standard":28},[],{"EN":778,"VI":778},{"EN":778,"VI":780},[783],[939,940],{"impactFactor":32,"impactFactorByYear":1778,"i10Index":570,"i10IndexLast5Year":48,"totalPublication":947,"totalPublicationByYear":1779,"totalCitation":949,"totalCitationByYear":1780,"totalCitationPerPublication":972,"totalCitationPerPublicationByYear":1781,"hindexLast5Year":206,"hindex":206},{"2012":440,"2013":440,"2014":582,"2015":224,"2016":221,"2017":691,"2018":944,"2019":945,"2020":289,"2021":946,"2022":368,"2023":171},{"1970":131,"1971":129,"1972":136,"1973":132,"1974":126,"1975":127,"1976":127,"1977":127,"1978":357,"1979":48,"1980":128,"1981":128,"1982":136,"1983":135,"1984":140,"1985":134,"1986":122,"1987":202,"1988":148,"1989":69,"1990":69,"1991":142,"1992":149,"1993":149,"1994":279,"1995":201,"1996":152,"1997":139,"1998":141,"1999":137,"2000":280,"2001":150,"2002":147,"2003":141,"2004":150,"2005":196,"2006":132,"2007":328,"2008":279,"2009":149,"2010":137,"2011":279,"2012":328,"2013":278,"2014":149,"2015":69,"2016":150,"2017":147,"2018":136,"2019":134,"2020":137,"2021":196,"2022":135,"2023":133,"2024":126},{"1970":951,"1971":131,"1972":129,"1973":952,"1974":357,"1975":202,"1976":46,"1977":137,"1978":352,"1979":127,"1980":435,"1982":325,"1983":49,"1984":215,"1985":132,"1986":830,"1987":149,"1988":953,"1989":954,"1990":955,"1991":956,"1992":957,"1993":958,"1994":959,"1995":960,"1996":961,"2005":962,"2006":963,"2007":964,"2008":965,"2009":966,"2010":967,"2011":437,"2012":968,"2013":969,"2014":361,"2015":358,"2016":970,"2017":971,"2018":135,"2019":599,"2020":161,"2021":600,"2022":133,"2023":357,"2024":40},{"1970":974,"1971":232,"1972":171,"1973":975,"1974":369,"1975":444,"1976":461,"1977":976,"1978":977,"1979":978,"1980":979,"1982":980,"1983":169,"1984":981,"1985":982,"1986":983,"1987":363,"1988":984,"1989":985,"1990":986,"1991":987,"1992":988,"1993":989,"1994":990,"1995":991,"1996":992,"2005":993,"2006":994,"2007":995,"2008":996,"2009":48,"2010":997,"2011":998,"2012":999,"2013":1000,"2014":1001,"2015":1002,"2016":1003,"2017":1004,"2018":698,"2019":636,"2020":191,"2021":191,"2022":370,"2023":316,"2024":105},{"pages":1783,"volume":1785},{"VOID":1784},"213-222",{"VOID":1786},"33","2001-06-01",2001,[925,941],{"id":1791,"createTime":1792,"updateTime":1792,"relativeEntities":1793,"slug":28,"properties":1794,"entityType":1024,"verifyStatus":882,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":1803,"fullTextUrl":28,"authors":1804,"publicationType":1059,"publisherRelationship":1833,"citationCount":28,"citationInfo":28,"publishDate":1885,"publishYear":1886,"citationAnalyzeStatus":882,"lastCitationAnalyze":28,"indexDatabases":1887,"openAccess":28,"references":28,"isForceReanalyzing":1115},"02cb8623-7f65-47d6-b576-a0cdeb9213f2","2024-02-02T16:44:52.823+00:00",[],{"abstract":1795,"title":1797,"references":1799,"doi":1801},{"EN":1796},"Regularly arrayed surface (glyco)proteins—often referred to as S layers—are a common feature of the cell envelopes of almost all archaebacteria. We have selected some examples (Halobacterium, Sulfolobus, Thermoproteus, Pyrobaculum, Staphylothermus), and we describe the structure of their surface layers as revealed primarily by electron crystallography. In spite of a considerable diversity in shapes and dimensions, some common structural features emerge from the comparison. The glycoprotein arrays are composed of oligomeric units which are anchored in the plasma membrane; extended spacer or linker domains maintain the bulk of the more or less porous surface layers at a constant distance above the membrane surface, thus creating a quasi-periplasmic compartment. Functions ascribed to surface layers, such as compartmentalization, shape maintenance and determination, and adhesion are discussed.",{"EN":1798},"Structural features of archaebacterial cell envelopes",{"VOID":1800},"Achenbach-Richter, L., Stetter, K. O., and Woese, C. R. (1987).Nature (London) 327, 348–349.\nBaumeister, W., and Hegerl, R. (1986).FEMS Microbiol. Lett. 36, 119–125.\nBaumeister, W., Wildhaber, I., and Engelhardt, H. (1988).Biophys. Chem. 29, 39–49.\nBaumeister, W., Wildhaber, I., and Phipps, B. M. (1989).Can. J. Microbiol. 35, 215–227.\nBaumeister, W., Santarius, U., Volker, S., Dürr, R., Lembcke, G., and Englehardt, H. (1990).Syst. Appl. Microbiol. 13, 105–111.\nBaumeister, W., Volker, S., and Santarius, U. (1991).Syst. Appl. Microbiol. 14, 103–110.\nBeveridge, T. J., Patel, G. B., Harris, B. J., and Sprott, G. D. (1986).Can. J. Microbiol. 32, 112–120.\nBlaurock, A. E., Stoeckenius, W., Oesterhelt, D., and Scherphof, G. L. (1976).J. Cell Biol. 71, 1–22.\nBröckl, G., Behr, M., Fabry, S., Hensel, R., Kaudewitz, H., Biendl, E., and König, H. (1991).Eur. J. Biochem. 199, 147–152.\nCheong, G.-W., Cjeka, Z., Peters, J., Stetter, K. O., and Baumeister, W. (1991).Syst. Appl. Microbiol. 14, 209–217.\nCunningham, B. A., Hemperly, J. J., Murray, B. A., Prediger, E. A., Brackenbury, R., and Edelman, G. M. 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USA,89, 7645–7649.\nSearcy, D. G. (1987).Ann. N.Y. Acad. Sci. 503, 168–179.\nShaw, P. J., Hillis, G. J., Henwood, J. A., Harris, J. E., and Archer, D. B. (1985).J. Bacteriol. 161, 750–757.\nSumper, M. (1987).Biochim. Biophys. Acta 906, 69–79.\nSumper, M., Berg, E., Mengele, R., and Strobel, I. (1990).J. Bacteriol. 172, 7111–7118.\nTaylor, K. A., Deatherage, J. F., and Amos, L. A. (1982).Nature (London)229, 840–842.\nWeiss, R. L. (1974).J. Bacteriol. 118, 275–284.\nWildhaber, I., and Baumeister, W. (1987).EMBO J. 6, 1475–1480.\nWildhaber, I., Santarius, U., and Baumeister, W. (1987).J. Bacteriol. 169, 5563–5568.\nZeikus, J. G., and Bowen, V. G. (1975).J. Bacteriol. 121, 373–380.\nZillig, W., Stetter, K. O., Schäfer, W., Janekovic, D., Wunderl, S., Holz, I., and Palm, P. (1981).Zbl. Bakt. Hyg., I. Abt. Orig. C 2, 205–227.",{"VOID":1802},"10.1007\u002FBF00762349","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF00762349",[1805,1820],{"id":1806,"sortIndex":32,"researcher":28,"roles":1807,"affiliations":1808,"properties":1817,"displayName":1819,"givenName":28,"familyName":28},"04091794-d8cb-4ae8-bde7-b91dce3ae534",[1031],[1809],{"id":1810,"sortIndex":32,"affiliation":1811,"properties":28},"287b46af-cd80-4d9e-acba-307ca3294a37",{"id":1810,"createTime":28,"updateTime":28,"relativeEntities":1812,"slug":28,"properties":1813,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1816,"statistic":28},[],{"title":1814},{"VI":1815},"Department of Structural Biology, Max-Planck-Institut for Biochemistry, Martinsried, Germany",[],{"title":1818},{"VI":1819},"Wolfgang Baumeister",{"id":1821,"sortIndex":40,"researcher":28,"roles":1822,"affiliations":1823,"properties":1830,"displayName":1832,"givenName":28,"familyName":28},"a8c8652f-de34-4e76-8f20-42b05df96a7a",[1031],[1824],{"id":1810,"sortIndex":32,"affiliation":1825,"properties":28},{"id":1810,"createTime":28,"updateTime":28,"relativeEntities":1826,"slug":28,"properties":1827,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1829,"statistic":28},[],{"title":1828},{"VI":1815},[],{"title":1831},{"VI":1832},"Gisela 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ct":1895,"title":1897,"references":1899,"doi":1901},{"EN":1896},"Mitochondria from a variety of sources possess an inner membrane channel, the permeability transition pore. The pore is a voltage-dependent channel, activated by matrix Ca2+ and inhibited by matrix H+, which can be blocked by cyclosporin A, presumably after binding to mitochondrial cyclophilin. The physiological function of the permeability transition pore remains unknown. Here we evaluate its potential role as a fast Ca2+ release channel involved in mitochondrial and cellular Ca2+ homeostasis. We (i) discuss the theoretical and experimental reasons why mitochondria need a fast, inducible Ca2+ release channel; (ii) analyze the striking analogies between the mitochondrial permeability transition pore and the sarcoplasmic reticulum ryanodine receptor-Ca2+ release channel; (iii) argue that the permeability transition pore can act as a selective release channel for Ca2+ despite its apparent lack of selectivity for the transported speciesin vitro; and (iv) discuss the importance of mitochondria in cellular Ca2+ homeostasis, and how disruption of this function could impinge upon cell viability, particularly under conditions of oxidative stress.",{"EN":1898},"The permeability transition pore as a mitochondrial calcium release channel: A critical appraisal",{"VOID":1900},"Abramson, J. J., and Salama, G. (1989).J. Bioenerg. Biomembr. 21, 283–295.\nAzzone, G. F., Pozzan, T., Massari, S., Bragadin, M., and Dell'Antone, P. (1977).FEBS Lett,78, 21–24.\nBernardi, P. (1992).J. Biol. Chem. 267, 8334–8339.\nBernardi, P., Paradisi, V., Pozzzan, T., and Azzone, G. F. (1984).Biochemistry 23, 1645–1651.\nBernardi, P., Vassanelli, S., Veronese, P., Colonna, R., Szabó, I., and Zoratti, M. (1992)J. Biol. Chem. 267, 2934–2939.\nBernardi, P., Broekemeier, K. M., and Pfeiffer, D. R. (1994).J. Bioenerg. Biomembr. 26, 509–517.\nBrillantes, A., Ondrias, K., Scott, A., Kobrinsky, E., Ondriasova, E., Moschella, M. C., Jayaraman, T., Landers, M., Ehrlich, B. E. and Marks, A. R. (1994).Cell 77, 513–523.\nBroekemeier, K. M., Dempsey, M. E., and Pfeiffer, D. R. (1989).J. Biol. Chem. 264, 7829–7830.\nBroekemeier, K. M., Carpenter-Deyo, L., Reed, D. J., and Pfeiffer, D. R. (1992).FEBS Lett. 304, 192–194.\nCameron, A. M., Steiner, J. P., Sabatini, D. M., Kaplin, A. I., Walensky, L. D., and Snyder, S. H. (1995).Proc. Natl. Acad. Sci. USA 92, 1784–1788.\nChacon, E., Reece, J. M., Nieminen, A. L., Zahrebelski, G., Herman, B. and Lemasters, J. J. (1994).Biophys. J. 66, 942–952.\nConnem, C. 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Cardiol. 25, 1461–1469.\nGunter, T. E., and Pfeiffer, D. R. (1990).Am. J. Physiol. 258, C755-C786.\nGunter, T. E., Gunter, K. K., Sheu, S.-S., and Gavin, C. E. (1994).Am. J. Physiol. 267, C313-C339.\nHalestrap, A. P., and Davidson, A. M. (1990).Biochem. J. 268, 153–160.\nHaworth, R. A., and Hunter, D. R. (1979).Arch. Biochem. Biophys. 195, 460–467.\nHoek, J. B., Farber, J. L., Thomas, A. P., and Wang, X. L. (1995).Biochim. Biophys. Acta 1271, 93–102.\nHunter, D. R., Haworth, R. A. (1979).Arch. Biochem. Biophys. 195, 453–459.\nIchas, F., Jouaville, L. S., Sidash, S. S., Mazat, J.-P., and Holmuhamedov, E. L. (1994).FEBS Lett. 348, 211–215.\nIgbavboa, U., and Pfeiffer, D. R. (1991).J. Biol. Chem. 266, 4283–4287.\nImberti, R., Nieminen, A. L., Herman, B., and Lemasters, J. J. (1993).J. Pharmacol. Exp. Ther. 265, 392–400.\nJayaraman, T., Brillantes, A. M., Timerman, A. P., Fleischer, S., Erdjument-Bromage, H., Tempst, P., and Marks, A. (1992).J. Biol. Chem. 267, 9474–9477.\nJung, D. W., Baysal, K., and Brierley, G. P. (1995).J. Biol. Chem. 270, 672–678.\nKass, G. E. N., Juedes, M., and Orrenius, S. (1992).Biochem. Pharmacol. 44, 1995–2003.\nKinnally, K. W., Campo, M. L., and Tedeschi, H. (1989).J. Bioenerg. Biomembr. 21, 497–506.\nKreisel, W., Heildebrandt, H., Schiltz, E., Kohler, G., Spamer, C., Dietz, C., Mossner, W., and Heilmann, C. (1994).Acta Histochem. 96, 51–62.\nLai, F. A., and Meissner, G. (1989).J. Bioenerg. Biomembr. 21, 227–247.\nMa, J., Fill, M., Knudson, M., Campbell, K. P., and Coronado, R. (1988).Science 242, 99–102.\nMeissner, G. (1986).J. Biol. Chem. 261, 6300–6306.\nMitchell, P. (1966).Biol. Rev. 41, 445–501.\nNazareth, W., Yafei, N., and Crompton, M. (1991).J. Mol. Cell. Cardiol. 23, 1351–1354.\nNicolli, A., Petronilli, V., and Bernardi, P. (1993).Biochemistry 32, 4461–4465.\nPalade, P., Dettbarn, C., Brunder, D., Stein, P., and Hais, G. (1989).J. Bioenerg. Biomembr. 21, 295–320.\nPastorino, J. G., Snyder, J. W., Serroni, A., Hoek, J. 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(1993).J. Biol. Chem. 268, 22992–22999.\nYellen, G. (1993).Nature 366, 109–110.\nZoeteweij, J. P., Vandewater, B., Debont, H. J. G. M., Mulder, G. J. and Nagelkerke, J. F. (1993).J. Biol. Chem. 268, 3384–3388.\nZoratti, M., and Szabó, I. (1995).Biochim. Biophys. Acta,1241, 139–176.",{"VOID":1902},"10.1007\u002FBF02110643","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF02110643",[1905,1920],{"id":1906,"sortIndex":32,"researcher":28,"roles":1907,"affiliations":1908,"properties":1917,"displayName":1919,"givenName":28,"familyName":28},"579f588c-cbc2-4682-ace2-52319240e3c5",[1031],[1909],{"id":1910,"sortIndex":32,"affiliation":1911,"properties":28},"c4d2bca8-601b-4644-b1ff-d778f56eb08e",{"id":1910,"createTime":28,"updateTime":28,"relativeEntities":1912,"slug":28,"properties":1913,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1916,"statistic":28},[],{"title":1914},{"VI":1915},"CNR Unit for the Study of Biomembranes and the Laboratory of Biophysics and Membrane Biology, Department of Biomedical Sciences, University of Padova, Italy",[],{"title":1918},{"VI":1919},"Paolo 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scopic-and-Redox-Studies",{"abstract":1995,"title":1997,"keywords":1999,"doi":2001},{"EN":1996},"The membrane bound fumarate reductase (FRD) from the sulphate-reducer Desulfovibrio gigas was purified from cells grown on a fumarate\u002Fsulphate medium and extensively characterized. The FRD is isolated with three subunits of apparent molecular masses of 71, 31, and 22 kDa. The enzyme is capable of both fumarate reduction and succinate oxidation, exhibiting a higher specificity toward fumarate (K\nm for fumarate is 0.02 and for succinate 2 mM) and a reduction rate 30 times faster than that for oxidation. Studies by Visible and EPR spectroscopies allowed the identification of two B-type haems and the three iron–sulphur clusters usually found in FRDs and succinate dehydrogenases: [2Fe-2S]2+\u002F1+ (S1), [4Fe-4S]2+\u002F1+ (S2), and [3Fe-4S]1+\u002F0 (S3). The apparent macroscopic reduction potentials for the metal centers, at pH 7.6, were determined by redox titrations: −45 and −175 mV for the two haems, and +20 and −140 mV for the S3 and S1 clusters, respectively. The reduction potentials of the haem groups are pH dependent, supporting the proposal that fumarate reduction is associated with formation of the membrane proton gradient. Furthermore, co-reconstitution in liposomes of D. gigas FRD, duroquinone, and D. gigas cytochrome bd shows that this system is capable of coupling succinate oxidation with oxygen reduction to water.",{"EN":1998},"The Quinol:Fumarate Oxidoreductase from the Sulphate Reducing Bacterium Desulfovibrio gigas: Spectroscopic and Redox Studies",{"EN":2000},"",{"VOID":2002},"10.1023\u002FA:1013814619023","2025-02-04T11:37:32.090+00:00",[31],"https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1023\u002FA:1013814619023",[2007,2022,2035,2056,2069],{"id":2008,"sortIndex":32,"researcher":28,"roles":2009,"affiliations":2010,"properties":2019,"displayName":2021,"givenName":28,"familyName":28},"b567dd17-9dda-438e-8d87-276b9a2294d6",[],[2011],{"id":2012,"sortIndex":32,"affiliation":2013,"properties":28},"d67447b8-8eca-4597-98de-85bd43764419",{"id":2012,"createTime":28,"updateTime":28,"relativeEntities":2014,"slug":28,"properties":2015,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2018,"statistic":28},[],{"title":2016},{"VI":2017},"Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal",[],{"title":2020},{"EN":2021},"Rita S. Lemos",{"id":2023,"sortIndex":40,"researcher":28,"roles":2024,"affiliations":2025,"properties":2032,"displayName":2034,"givenName":28,"familyName":28},"1335ce1e-10ed-42a1-9de6-87bb93904408",[],[2026],{"id":2012,"sortIndex":32,"affiliation":2027,"properties":28},{"id":2012,"createTime":28,"updateTime":28,"relativeEntities":2028,"slug":28,"properties":2029,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2031,"statistic":28},[],{"title":2030},{"VI":2017},[],{"title":2033},{"EN":2034},"Cláudio M. Gomes",{"id":2036,"sortIndex":123,"researcher":28,"roles":2037,"affiliations":2038,"properties":2053,"displayName":2055,"givenName":28,"familyName":28},"60361be4-90d1-4afc-aaa2-660a13245314",[],[2039,2045],{"id":2012,"sortIndex":32,"affiliation":2040,"properties":28},{"id":2012,"createTime":28,"updateTime":28,"relativeEntities":2041,"slug":28,"properties":2042,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2044,"statistic":28},[],{"title":2043},{"VI":2017},[],{"id":2046,"sortIndex":40,"affiliation":2047,"properties":28},"0498bf60-c9f6-4f82-b12a-68a4284d5413",{"id":2046,"createTime":28,"updateTime":28,"relativeEntities":2048,"slug":28,"properties":2049,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2052,"statistic":28},[],{"title":2050},{"EN":2051},"Department of Biochemistry and Molecular Biology, University of Georgia, Athens",[],{"title":2054},{"EN":2055},"Jean LeGall",{"id":2057,"sortIndex":42,"researcher":28,"roles":2058,"affiliations":2059,"properties":2066,"displayName":2068,"givenName":28,"familyName":28},"abc51bd5-6bb1-4db5-bc65-b39e0bda4f02",[],[2060],{"id":2012,"sortIndex":32,"affiliation":2061,"properties":28},{"id":2012,"createTime":28,"updateTime":28,"relativeEntities":2062,"slug":28,"properties":2063,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2065,"statistic":28},[],{"title":2064},{"VI":2017},[],{"title":2067},{"EN":2068},"António V. 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