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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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SCIE","scie",[948,813],"SCIE",[950],"8eb75d88-0c7a-497c-a346-e729afc75040",{"impactFactor":32,"impactFactorByYear":952,"i10Index":32,"i10IndexLast5Year":32,"totalPublication":49,"totalPublicationByYear":953,"totalCitation":32,"totalCitationByYear":954,"totalCitationPerPublication":32,"totalCitationPerPublicationByYear":955,"hindexLast5Year":32,"hindex":32},{},{"1999":40,"2000":40,"2001":40,"2002":40,"2004":40,"2012":40,"2019":40},{},{},{"meta":957,"data":959},{"total":958},"8366",[960,1137,1301,1436,1648,1831,2003,2091,2167,2284],{"id":961,"createTime":962,"updateTime":963,"relativeEntities":964,"slug":965,"properties":966,"entityType":975,"verifyStatus":26,"verifyTime":963,"verifyNote":976,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":977,"fullTextUrl":28,"authors":978,"publicationType":1073,"publisherRelationship":1074,"citationCount":28,"citationInfo":28,"publishDate":1133,"publishYear":1134,"citationAnalyzeStatus":878,"lastCitationAnalyze":28,"indexDatabases":1135,"openAccess":28,"references":28,"isForceReanalyzing":1136},"0002727b-f93a-4808-adaa-d9800593582d","2024-01-14T01:29:55.825+00:00","2025-02-14T09:25:58.154+00:00",[],"Antiproliferative-and-antioxidant-potential-of-beta-ionone-against-benzo-a-pyrene-induced-lung-carcinogenesis-in-Swiss-albino-mice",{"abstract":967,"title":969,"references":971,"doi":973},{"EN":968},"Nowadays, in developing countries like India, incidence of lung cancer is increasing rapidly, and as a consequence it has become the most common cause of malignancy-associated death. This study is aimed to evaluate the therapeutic efficacy of beta-ionone (ION), a precursor for carotenoids against benzo(a)pyrene [B(a)P]-induced lung carcinogenesis. B(a)P (50 mg\u002Fkg body weight, orally twice a week for 4 successive weeks)-induced lung cancer in mice was assessed both in tissue and serum in terms of increase LPO and tissue marker enzymes, such as aryl hydrocarbon hydroxylase, γ-glutamyl transpeptidase, 5′-nucleotidase, and lactate dehydrogenase, and serum tumor markers such as carcinoembryonic antigen and neuron-specific enolase with concordant decrease in activities of tissue enzymic and non-enzymic antioxidants were observed on the treatment of ION (60 mg\u002Fkg body weight, orally twice a week for 16 weeks) significantly attenuated LPO and restored all cancer marker enzymes and antioxidants levels to near normal, which indicates the anticancer effect of ION. This was further confirmed by histological staining of argyrophilic nucleolar organizer region and histopathological analysis of lung tissue, immunohistochemical and immunoblot analysis of proliferating cell nuclear antigen. Overall findings suggested that the ION effectively ameliorated the lung carcinogenesis, which is attributed to the antiproliferative and antioxidant potential through free radical scavenging property.",{"EN":970},"Antiproliferative and antioxidant potential of beta-ionone against benzo(a)pyrene-induced lung carcinogenesis in Swiss albino mice",{"VOID":972},"Tang N, Wu Y, Ma J, Wang B, Yu R (2010) Coffee consumption and risk of lung cancer: a meta-analysis. Lung Cancer 67:17–22\nNational Cancer Institute SEER data. Available at: http:\u002F\u002Fseer.cancer.gov\u002Fstatistics\u002F. Accessed 20 June 2009\nDelgado-Saborit JM, Stark C, Harrison RM (2010) Carcinogenic potential, levels and sources of polycyclic aromatic hydrocarbon mixtures in indoor and outdoor environments and their implications for air quality standards. Environ Int 37:383–392\nAnandakumar P, Kamaraj S, Jagan S, Ramakrishnan G, Naveenkumar C, Asokkumar S et al. (2009) Capsaicin alleviates the imbalance in xenobiotic metabolizing enzymes and tumor markers during experimental lung tumorigenesis. Mol Cell Biochem. doi:10.1007\u002Fs11010-009-0151-0\nTsuji G, Takahara M, Uchi H, Takeuchi S, Mitoma C, Moroi Y, Furue M et al (2011) An environmental contaminant, benzo(a)pyrene, induces oxidative stress-mediated interleukin-8 production in human keratinocytes via the aryl hydrocarbon receptor signaling pathway. J Dermatol Sci 62(1):42–49\nKamaraj S, Anandakumar P, Jagan S, Ramakrishnan G, Devaki T (2010) Modulatory effect of hesperidin on benzo(a)pyrene induced experimental lung carcinogenesis with reference to COX-2, MMP-2 and MMP-9. Eur J Pharmacol. doi:10.1016\u002Fj.ejphar.2010.09.017\nHail N Jr, Cortes M, Drake EN, Spallholz JE (2008) Cancer chemoprevention: a radical perspective. Free Radic Biol Med 45:97–110\nMilner JA (2008) Nutrition and cancer: essential elements for a roadmap. Cancer Lett 269:189–198. doi:10.1016\u002Fj.canlet05.030\nCardozo MT, de Conti A, Ong TP, Scolastici C, Purgatto E, Horst MA et al. (2010) Chemopreventive effects of β-ionone and geraniol during rat hepatocarcinogenesis promotion: distinct actions on cell proliferation, apoptosis, HMGCoA reductase, and RhoA. J Nutr Biochem. doi:10.1016\u002Fj.jnutbio.2009.12.007\nKim MO, Moon DO, Kang CH, Kwon TK, Choi YH, Kim GY (2010) β-Ionone enhances TRAIL-induced apoptosis in hepatocellular carcinoma cells through Sp1-dependent upregulation of DR5 and downregulation of NF-κB Activity. Mol Cancer Ther 9:833. doi:10.1158\u002F1535-7163.MCT-09-061\nKamaraj S, Ramakrishnan G, Anandakumar P, Jagan S, Devaki T (2008) Antioxidant and anticancer efficacy of hesperidin in benzo(a)pyrene induced lung carcinogenesis in mice. Invest New Drugs. doi:10.1007\u002Fs10637-008-9159-7\nLowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275\nOhkawa H, Ohishi N, Yagi K (1979) Assay for lipid peroxidation in animal tissues by thiobarbituric acid reaction. Anal Biochem 95:351–358. doi:10.1016\u002F0003-2697(79)90738-3\nMarklund S, Marklund G (1974) Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 47:469–474. doi:10.1111\u002Fj.1432-1033.1974.tb03714.x\nSinha AK (1972) Colorimetric assay of catalase. Anal Biochem 47:389–394. doi:10.1016\u002F0003-2697(72)90132-7\nRotruck JT, Pope AL, Ganther HE, Swanson AB, Hafeman DG, Hoekstra WG (1973) Selenium: biochemical role as a component of glutathione peroxidase. Science 179:588–590\nMoron MS, Depierre JW, Mannervik B (1979) Levels of glutathione, glutathione reductase and glutathione S-transferase activities in rat lung and liver. Biochim Biophys Acta 582:67–78\nHorn HD, Burn FH (1978) In: Bergmeyer HV (ed) Methods in enzymology. Academic Press, New York, p 877\nDesai ID (1984) Vitamin E analysis methods for animal tissues. Methods Enzymol 105:138–147\nOmaye ST, Turnbull JD, Sauberlich HE (1979) Selected methods for the determination of ascorbic acid in animal cells, tissues, and fluids. Methods Enzymol 62:3–11\nRamakrishnan G, Elinos-Baez CM, Jagan S, Augustine TA, Kamaraj S, Anandakumar P et al (2008) Silymarin downregulates COX-2 expression and attenuates hyperlipidemia during NDEA-induced rat hepatocellular carcinoma. Mol Cell Biochem 313:53–61. doi:10.1007\u002Fs11010-008-9741-5\nPloton D, Menager M, Jeannesson P, Himber G, Pigeon F, Adnet JJ (1986) Improvement in the staining and in the visualization of the argyrophilic proteins of the nucleolar organizer regions at the optical level. Histochem J 18:5–14. doi:10.1007\u002FBF01676192\nSingh SV, Benson PJ, Hu X, Pal A, Xia H, Srivastava SK et al (1998) Gender-related differences in susceptibility of A\u002FJ mouse to benzo[a]pyrene-induced pulmonary and forestomach tumorigenesis. Cancer Lett 128:197–204\nKim HS, Kwack SJ, Lee BM (2000) Lipid peroxidation, antioxidant enzymes, and benzo[a]pyrene-quinones in the blood of rats treated with benzo[a]pyrene. Chem Biol Interact 127:139–150. doi:10.1016\u002FS0009-2797(00)00177-0\nLiu JR, Dong HW, Sun XR, Wang Q, Sun WG, Parry JW et al (2010) Effects of β-ionone on mammary carcinogenesis and antioxidant status in rats treated with DMBA. Nutr Cancer 62:58–65. doi:10.1080\u002F01635580903191510\nSirri V, Roussel P, Trerè D, Derenzini M, Hernandez-Verdun D (1995) Amount variability of total and individual Ag-NOR proteins in cells stimulated to proliferate. J Histochem Cytochem 43:887–893\nFeng Q, Kumagai T, Torii Y, Nakamura Y, Osawa T, Uchida K (2001) Anticarcinogenic antioxidants as inhibitors against intracellular oxidative stress. Free Radic Res 35:779–788\nGosset P, Garçon G, Casset A, Fleurisse L, Hannothiaux MH, Creusy C et al (2003) Benzo(a)pyrene-coated onto Fe2O3 particles-induced apoptotic events in the lungs of Sprague-Dawley rats. Toxicol Lett 143:223–232. doi:10.1016\u002FS0378-4274(03)00153-X\nde Zwart LL, Meerman JH, Commandeur JN, Vermeulen NP (1999) Biomarkers of free radical damage applications in experimental animals and in humans. Free Radic Biol Med 26:202–226. doi:10.1016\u002FS0891-5849(98)00196-8\nSorokina LV, Solyanik GI, Pyatchanina TV (2010) The evaluation of prooxidant and antioxidant state of two variants of lewis lung carcinoma: a comparative study. Exp Oncol 32(4):249–253\nGupta KB, Tandon S, Garg V, Lai H (2000) Plasma glutathione-S-transferase activity in lung malignancy. Ind J Tuberc 47:227\nAnandakumar P, Kamaraj S, Jagan S, Ramakrishnan G, Vinodhkumar R, Devaki T (2008) Stabilization of pulmonary mitochondrial enzyme system by capsaicin during benzo(a)pyrene induced experimental lung cancer. Biomed Pharmacother 62:390–394\nHanigan MH, Ricketts WA (1993) Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase. Biochemistry 32:6302–6306\nFoa P, Fornier M, Miceli R, Seregni E, Santambrogio L, Nosotti M et al (1994) Tumor markers CEA, NSE, SCC, TPA and CYFRA 21.1 in resectable non-small cell lung cancer. Anticancer Res 19:3613–3618\nRonkainen H, Soini Y, Vaarala MH, Kauppila S, Hirvikoski P (2010) Evaluation of neuroendocrine markers in renal cell carcinoma. Diagn Pathol 5:28\nKeshgegian AA, Cnaan A (1995) Proliferation markers in breast carcinoma. Mitotic figure count, S-phase fraction, proliferating cell nuclear antigen, Ki-67 and MIB-1. Am J Clin Pathol 104:42–49\nJagan S, Ramakrishnan G, Anandakumar P, Kamaraj S, Devaki T (2008) Antiproliferative potential of gallic acid against diethylnitrosamine-induced rat hepatocellular carcinoma. Mol Cell Biochem. doi:10.1007\u002Fs11010-008-9876-4\nOrellana-Bustos AI, Espinoza-Santander IL, Franco-Martínez ME, Lobos-James-Freyre N, Ortega-Pinto AV (2004) Evaluation of keratinization and AgNORs counts in exfoliative cytology of normal mucosa from smokers and non-smokers. Med Oral 9:197–203\nUno T, Hashimoto S, Shimono M (1998) A study of the proliferative activity of the long junctional epithelium using argyrophilic nucleolar organizer region (AgNORs) staining. J Periodont Res 33:298–309\nJanakiram NB, Cooma I, Mohammed A, Steele VE, Rao CV (2008) Beta-ionone inhibits colonic aberrant crypt foci formation in rats, suppresses cell growth, and induces retinoid X receptor-alpha in human colon cancer cells. 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most frequently reported symptom of exposure to high altitude is loss of body mass and decreased performance which has been attributed to altered protein metabolism affecting skeletal muscles mass. The present study explores the mechanism of chronic hypobaric hypoxia mediated skeletal muscle wasting by evaluating changes in protein turnover and various proteolytic pathways. Male Sprague–Dawley rats weighing about 200 g were exposed to hypobaric hypoxia (7,620 m) for different durations of exposure. Physical performance of rats was measured by treadmill running experiments. Protein synthesis, protein degradation rates were determined by 14C-Leucine incorporation and tyrosine release, respectively. Chymotrypsin-like enzyme activity of the ubiquitin–proteasome pathway and calpains were studied fluorimetrically as well as using western blots. Declined physical performance by more than 20%, in terms of time taken in exhaustion on treadmill, following chronic hypobaric hypoxia was observed. Compared to 1.5-fold increase in protein synthesis, the increase in protein degradation was much higher (five-folds), which consequently resulted in skeletal muscle mass loss. Myofibrillar protein level declined from 46.79 ± 1.49 mg\u002Fg tissue at sea level to 37.36 ± 1.153 (P \u003C 0.05) at high altitude. However, the reduction in sarcoplasmic proteins was less as compared to myofibrillar protein. Upregulation of Ub-proteasome pathway (five-fold over control) and calpains (three-fold) has been found to be important factors for the enhanced protein degradation rate. The study provided strong evidences suggesting that elevated protein turnover rate lead to skeletal muscle atrophy under chronic hypobaric hypoxia via ubiquitin–proteasome pathway and calpains.",{"EN":1147,"VI":1148},"Chronic hypobaric hypoxia mediated skeletal muscle atrophy: role of ubiquitin–proteasome pathway and calpains","Teo cơ xương qua trung gian thiếu oxy áp suất thấp mạn tính: Vai trò của con đường ubiquitin–proteasome và các calpain",{"VOID":1150},"Fulco CS, Friedlander AL, Muza SR, Rock PB, Robinson S, Lammi E, Baker R, Fulco CJ, Lewis SF, Cymerman A (2002) Energy intake deficit and physical performance at altitude. Aviat Space Environ Med 73:758–765\nBharadwaj H, Prasad J, Pramanik SN, Kishnani S, Zachariah T, Chaudhary KL, Sridharan K, Srivastava KK (2000) Effect of prolonged exposure to high altitude on skeletal muscles of Indian soldiers. Def Sci J 50:167–176\nMacdonald JH, Oliver SJ, Hillyer K, Sanders S, Smith Z, Williams C, Yates D, Ginnever H, Scanlon E, Roberts E, Murphy D, Lawley J, Chichester E (2009) Body composition at high altitude: a randomized placebo-controlled trial of dietary carbohydrate supplementation. Am J Clin Nutr 90:1193–1202\nSridharan K, Mukherjee AK, Grover SK, Kumaria MML, Arora BS, Rai RM (1987) Assessment of nutritional status and physical work capacity of road construction workers at altitude of 2150–2750 m on two different ration scales. Nutr Rep Int 35:1269–1277\nBrouns F (1992) Nutritional aspects of health and performance at lowland and altitude. Int J Sports Med 13:S100–S106\nSchols AM (2002) Pulmonary cachexia. Int J Cardiol 85:101–110\nHoppeler H, Vogt M (2001) Muscle tissue adaptations to hypoxia. J Exp Biol 204:3133–3139\nHoppeler H, Kleinert E, Schlegel C, Claassen H, Howald H, Kayar SR, Cerretelli P (1990) Muscular exercise at high altitude. II. Morphological adaptation of skeletal muscle to chronic hypoxia. Int J Sports Med 11:S3–S9\nMartinelli M, Winterhalder R, Cerretelli P, Howald H, Hoppeler H (1990) Muscle lipofuscin content and satellite cell volume is increased after high altitude exposure in humans. Experientia 46:672–676\nKung-tung C, Yu-yawn C, Huey-june W, Chen-kang C, Wen-tsung L, Yen-yuan L, Chieh-chung L, Rong-sen Y, Jung-charng L (2008) Decreased anaerobic performance and hormone adaptation after expedition to Peak Lenin. Chin Med J 121:2229–2233\nBigard AX, Douce P, Merino D, Lienhard F, Guezennec CY (1996) Changes in dietary protein intake fail to prevent decrease in muscle growth induced by severe hypoxia in rats. J Appl Physiol 80:208–215\nPreedy VR, Smith DM, Sugden PH (1985) The effects of 6 hr hypoxia on protein synthesis in rat tissue in vivo & in vitro. Biochem J 228:179–185\nPreedy VR, Sugden PH (1989) The effects of fasting or hypoxia on rates of protein synthesis in vivo in subcellular fractions of rat heart and gastrocnemius muscle. Biochem J 257:519–527\nIioka TK, Sugito K, Moriya T, Kuriyama T (2002) Effects of insulin like growth factor on nitrogen balance during hypoxic exposure. Eur Respir J 20:293–299\nVigano A, Ripamonti M, Palma SD, Capitanio D, Vasso M, Wait R, Lundby C, Cerretelli P, Gelfi C (2008) Proteins modulation in human skeletal muscle in the early phase of adaptation to hypobaric hypoxia. Proteomics 8:4668–4679\nImoberdorf R, Garlick PJ, McNurlan MA, Casella GA, Marini JC, Turgay M, Bartsch P, Ballmer PE (2006) Skeletal muscle protein synthesis after active or passive ascent to high altitude. Med Sci Sports Exerc 38:1082–1087\nHolm L, Haslund ML, Robach P, van Hall G, Calbet JA, Saltin B, Lundby C (2010) Skeletal muscle myofibrillar and sarcoplasmic protein synthesis rates are affected differently by altitude-induced hypoxia in native lowlanders. PLoS ONE 20:e15606\nRennie MJ (1985) Muscle protein turnover and the wasting due to injury and disease. Br Med Bull 41:257–264\nCai D, Lee KK, Li M, Tang MK, Chan KM (2004) Ubiquitin expression is upregulated in human and rat skeletal muscles during aging. Arch Biochem Biophys 425:42–50\nReid MB (2005) Response of the ubiquitin–proteasome pathway to changes in muscle activity. Am J Physiol Regul Integr Comp Physiol 288:R1423–R1431\nMammucari C, Milan G, Romanello V, Masiero E, Rudolf R, Piccolo PD, Burden SJ, Lisi RD, Sandri C, Zhao J, Goldberg AL, Schiaffino S, Sandri M (2007) FoxO3 controls autophagy in skeletal muscle in vivo. Cell Metab 6:458–471\nAttaix D, Mosoni L, Dardevet D, Combaret L, Mirand PP, Grizard J (2005) Altered responses in skeletal muscle protein turnover during aging in anabolic and catabolic periods. Int J Biochem Cell Biol 37:2098–2114\nEnns DL, Raastad T, Ugelstad I, Belcastro AN (2007) Calpain\u002Fcalpastatin activities and substrate depletion patterns during hindlimb unweighting and reweighting in skeletal muscle. Eur J Appl Physiol 100:445–455\nDardevet D, Sornet C, Vary T, Grizard J (1996) Phosphotidylinositol 3-kinase and p70 S6 kinase participate in the regulation of protein turnover in skeletal muscle by insulin and insulin-like growth factor I. Endocrinology 137:4089–4094\nVary TC, Dardevet D, Grizard J, Voisin L, Buffiere C, Denis P, Breuille D, Obled C (1998) Differential regulation of skeletal muscle protein turnover by insulin and IGF-1 after bacteremia. Am J Physiol Endocrinol Metab 275:E584–E593\nVentrucci G, Mello MAR, Marcondes G (2004) Proteasome activity is altered in skeletal muscle tissue of tumour-bearing rats fed a leucine-rich diet. Endocr Relat Cancer 11:887–895\nWaalkes TP, Udenfriend S (1957) A fluorimetric method for the estimation of tyrosine in plasma and tissues. J Lab Clin Med 50:733–736\nHepple RT, Qin M, Nakamoto H, Goto S (2008) Caloric restriction optimizes the proteasome activity. Am J Physiol Regul Integr Comp Physiol 295:R1231–R1237\nMastrocola R, Reffo P, Penna F, Tomasinelli CE, Boccuzzi G, Baccino FM, Aragno M, Costelli P (2008) Muscle wasting in diabetic and in tumor bearing rats: role of oxidative stress. Free Radic Biol Med 44:584–593\nOron U (1990) Proteolytic enzyme activity in rat hind limb muscle in fetus and during post natal development. Int J Dev Biol 34:457–460\nLowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193:265–275\nKoopman R, Gehrig SM, Leger B, Walrand S, Murphy KT, Lynch GS (2010) Cellular mechanisms underlying temporal changes in skeletal muscle protein synthesis and breakdown during chronic β-adrenoceptor stimulation in mice. J Physiol 588:4811–4823\nKvamme E, Torgner IA, Svenneby G (1985) Glutaminase from mammalian tissue. Methods Enzymol 113:241–244\nElliott WH (1955) Glutamine synthesis. In: Colowick SP, Kaplan NO (eds) Methods enzymol II. pp 337–339\nCathcart R, Schwiers E, Ames BN (1983) Detection of pico mole levels of hyderoperoxides using fluorescent dichlorofluoroscein assay. Anal Biochem 134:111–116\nBuege JA, Aust SD (1978) Microsomal lipid peroxidation. Methods Enzymol 52:302–310\nDutta A, Ray K, Singh VK, Vats P, Singh SN, Singh SB (2008) L-carnitine supplementation attenuates intermittent hypoxia-induced oxidative stress and delays muscle fatigue in rats. Exp Physiol 93:1139–1146\nTisdale MJ (2005) The Ub-proteasome pathway as a therapeutic target for muscle wasting. J Support Oncol 3:209–217\nHowald H, Pette D, Simoneau JA, Uber A, Hoppeler H, Cerretelli P (1990) Effect of chronic hypoxia on muscle enzyme activities. Int J Sports Med S10–S14\nVats P, Mukherjee AK, Kumria MM, Singh SN, Patil SK, Rangnathan S, Sridharan K (1999) Changes in activity levels of glutamine synthetase, glutaminase and glycogen synthetase in rats subjected to hypoxic stress. Int J Biometeorol 42:205–209\nShang F, Gong Taylor A (1997) Activity of ubiquitin-dependent pathway in response to oxidative stress. Ubiquitin-activating enzyme is transiently up-regulated. J Biol Chem 272:23086–23093\nFernandes R, Ramalho J, Pereira P (2006) Oxidative stress upregulates ubiquitin proteasome pathway in retinal endothelial cells. Mol Vis 12:1526–1535\nHermann J, Gulati R, Napoli C, Woodrum LLO, Porcel MR, Sica V, Simari RD, Ciechanover A, Lerman A (2003) Oxidative stress-related increase in ubiquitination in early coronary atherogenesis. FASEB 17:1730–1732\nGomes M, Maria CC, Tisdale MJ (2002) Induction of protein catabolism and the ubiquitin proteasome pathway by mild oxidative stress. Cancer Lett 180:69–74\nSagi SKS, Patir H, Mishra C, Pradhan G, Mastoori SR, Ilavazhagan G (2008) Role of oxidative stress and NFkB in hypoxia induced pulmonary edema. Exp Biol Med 233:1088–1098\nMarfella R, Amico MD, Filippo CD, Baldi A, Siniscalchi M, Sasso FC, Portoghese M, Carbonara O, Crescenzi B, Sangiuolo P, Nicoletti GF, Rossiello R, Ferraraccio F, Cacciapuoti F, Verza M, Coppola L, Rossi F, Paolisso G (2006) Increased activity of the ubiquitin-proteasome system in patients with symptomatic carotid disease is associated with enhanced inflammation and may destabilize the atherosclerotic plaque: effects of rosiglitazone treatment. JACC 47:2444–2455",{"VOID":1152},"10.1007\u002Fs11010-011-1210-x","2025-01-19T11:46:38.025+00:00",[30],"https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs11010-011-1210-x",[1157,1172,1185,1198,1211,1226],{"id":1158,"sortIndex":32,"researcher":28,"roles":1159,"affiliations":1160,"properties":1169,"displayName":1171,"givenName":28,"familyName":28},"1022e40c-72df-4b99-9434-4ae0e5be4da5",[982],[1161],{"id":1162,"sortIndex":32,"affiliation":1163,"properties":28},"0f576c1d-2dd9-4a77-8f0c-62f39a53fa5b",{"id":1162,"createTime":28,"updateTime":28,"relativeEntities":1164,"slug":28,"properties":1165,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1168,"statistic":28},[],{"title":1166},{"VI":1167},"Defence Institute of Physiology and Allied Sciences, New Delhi, India",[],{"title":1170},{"VI":1171},"Pooja Chaudhary",{"id":1173,"sortIndex":40,"researcher":28,"roles":1174,"affiliations":1175,"properties":1182,"displayName":1184,"givenName":28,"familyName":28},"156eea5b-d7c0-437c-8779-450ac462e415",[982],[1176],{"id":1162,"sortIndex":32,"affiliation":1177,"properties":28},{"id":1162,"createTime":28,"updateTime":28,"relativeEntities":1178,"slug":28,"properties":1179,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1181,"statistic":28},[],{"title":1180},{"VI":1167},[],{"title":1183},{"VI":1184},"Geetha 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Ali",{"id":1227,"sortIndex":46,"researcher":28,"roles":1228,"affiliations":1229,"properties":1236,"displayName":1238,"givenName":28,"familyName":28},"ac527b3d-e077-4483-bee9-86a5c0e53d34",[982],[1230],{"id":1162,"sortIndex":32,"affiliation":1231,"properties":28},{"id":1162,"createTime":28,"updateTime":28,"relativeEntities":1232,"slug":28,"properties":1233,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1235,"statistic":28},[],{"title":1234},{"VI":1167},[],{"title":1237},{"VI":1238},"Govindsamy Ilavazhagan",{"url":1155,"publisher":1240,"properties":1293},{"id":868,"createTime":869,"updateTime":870,"relativeEntities":1241,"slug":872,"properties":1242,"entityType":25,"verifyStatus":878,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":32,"subjectFields":1245,"manageAffiliations":1262,"indexDatabases":1273,"url":28,"thumbnailPath":28,"statistic":1288,"gsStatistic":28,"type":55,"analyzePriority":28},[],{"issn":1243,"title":1244},{"VOID":875},{"EN":877},[1246,1250,1254,1258],{"id":881,"createTime":28,"updateTime":28,"relativeEntities":1247,"label":1248,"description":1249,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":884},{},{"id":887,"createTime":28,"updateTime":28,"relativeEntities":1251,"label":1252,"description":1253,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":890},{},{"id":893,"createTime":28,"updateTime":28,"relativeEntities":1255,"label":1256,"description":1257,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":896},{},{"id":899,"createTime":28,"updateTime":28,"relativeEntities":1259,"label":1260,"description":1261,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":902},{},[1263,1268],{"id":906,"createTime":28,"updateTime":28,"relativeEntities":1264,"slug":28,"properties":1265,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1267,"statistic":28},[],{"title":1266},{"EN":910},[],{"id":913,"createTime":28,"updateTime":28,"relativeEntities":1269,"slug":28,"properties":1270,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1272,"statistic":28},[],{"title":1271},{"EN":917},[919],[1274,1281],{"id":922,"indexDatabase":1275,"url":928,"indexYears":929,"academicFieldIds":1280,"indexDatabaseRanking":935},{"id":786,"createTime":28,"updateTime":28,"relativeEntities":1276,"label":1277,"description":1278,"key":792,"publicationTags":1279,"standard":28},[],{"EN":789,"VI":789},{"EN":789,"VI":791},[794],[931,932,933,934],{"id":937,"indexDatabase":1282,"url":28,"indexYears":28,"academicFieldIds":1287,"indexDatabaseRanking":28},{"id":939,"createTime":28,"updateTime":28,"relativeEntities":1283,"label":1284,"description":1285,"key":946,"publicationTags":1286,"standard":28},[],{"EN":942,"VI":942},{"EN":944,"VI":945},[948,813],[950],{"impactFactor":32,"impactFactorByYear":1289,"i10Index":32,"i10IndexLast5Year":32,"totalPublication":49,"totalPublicationByYear":1290,"totalCitation":32,"totalCitationByYear":1291,"totalCitationPerPublication":32,"totalCitationPerPublicationByYear":1292,"hindexLast5Year":32,"hindex":32},{},{"1999":40,"2000":40,"2001":40,"2002":40,"2004":40,"2012":40,"2019":40},{},{},{"pages":1294,"volume":1296},{"VOID":1295},"101-113",{"VOID":1297},"364","2012-01-04",2012,[948,935],{"id":1302,"createTime":1303,"updateTime":1304,"relativeEntities":1305,"slug":1306,"properties":1307,"entityType":975,"verifyStatus":26,"verifyTime":1304,"verifyNote":976,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":1316,"fullTextUrl":28,"authors":1317,"publicationType":1073,"publisherRelationship":1374,"citationCount":28,"citationInfo":28,"publishDate":1433,"publishYear":1434,"citationAnalyzeStatus":878,"lastCitationAnalyze":28,"indexDatabases":1435,"openAccess":28,"references":28,"isForceReanalyzing":1136},"0016239e-8092-422f-9632-d5e373e5668f","2024-01-15T09:16:33.580+00:00","2025-01-05T23:10:22.246+00:00",[],"Intestinal-mucosal-lipid-peroxidation-and-absorptive-function-In-Salmonella-typhimurium-mediated-intestinal-infection",{"abstract":1308,"title":1310,"references":1312,"doi":1314},{"EN":1309},"S. typhimurium infection is associated with neutrophil infiltration within the intestinal mucosa. Neutrophil activation provides a major source of reactive oxygen species (ROS). The mucosal pathology of S. typhimurium infection may be in part due to the excessive production of these reactive species. This study was carried out to investigate if ROS play a role in mediating the changes in the structural components and functional properties of brush border membrane (BBM) in rats during S. typhimurium infection. This was done by determining the changes in the BBM extent of lipid peroxidation and absorptive function. A significant increase in the extent of lipid peroxidation of BBM during S. typhimurium infection was observed as judged by malondialdehyde (MDA) and conjugated diene formation and depletion of α-tocopherol and protein associated thiol groups. A significant decrease in the BBMV (brush border membrane vesicle) transport of amino acids was also observed. However there was no change in the transport of D-glucose. The decrease in amino acid transport further led to a significant decrease in the enterocyte level of protein synthesis. Exposure of BBMV to a free radical donor, cumene hydroperoxide, also led to an increase in the extent of lipid peroxidation and a decrease in the amino acid transport. Possibly ROS might play a significant role in mediating the mucosal damage during S. typhimurium infection.",{"EN":1311},"Intestinal mucosal lipid peroxidation and absorptive function In Salmonella typhimurium mediated intestinal infection",{"VOID":1313},"Wallis TS, Hauker RJH, Candy DCA, Qi GM, Clarke GJ, Worton KJ, Osborne MP, Stephen J: Quantification of the leukocyte influx into rabbit ileal loops induced by strains of Salmonella typhimurium of different virulence. J Med Microbiol 30: 149–156, 1989\nWallis TS, Vaughan ATM, Clarke GJ, Qi GM, Worton KJ, Candy DCA, Osborne MP, Stephen, J: The role of leukocytes in the induction of fluid secretion by Salmonella typhimurium. J Med Microbiol 31: 27–35, 1990\nMcCormick BA, Miller SI, Cornes D, Madara JL: Transepithelial signalling to neutrophils by Salmonellae: A novel virulence mechanism for gastroenteritis. Infect Immun 63: 2302–2309, 1995\nAruoma OJ, Halliwell B, Gajewski E, Dizdaraglu M: Copper-iron dependent damage to the bases in DNA in the presence of hydrogen peroxide. Biochem J 273: 2601–2604, 1991\nSmith S, Grisham M, Manci E, Granger N, Kvietys P: Gastric mucosal injury in the rat. Gastroenterology 92: 950–956, 1981\nOshitani N, Kitano A, Okabe H, Nakamura S, Matsumoto T, Kobayashi K: Location of superoxide anion generation in human colonic mucosa obtained by biopsy. Gut 34: 936–938, 1993\nPryor WA: Free radicals and lipid peroxidation: What they are and how they got that way. In: B Frei (ed). Natural Antioxidants in Human Health and Disease. Orlando, FL: Academic Press, 1994, 1–24\nNalini S, Ibrahim SA, Balasubramanian KA: Effect of oxidant exposure on monkey intestinal brush-border membrane. Biochim Biophys Acta 1147: 169–176, 1993\nJourdheuil D, Vaananen P, Meddings JB: Lipid peroxidation of the brush border membrane: membrane physical properties and glucose transport. Am J Physiol 264: G1009–G1015, 1993\nWallis TS, Starkey WG, Stephen J, Haddon SJ, Osborne MP, Candy DCA: Enterotoxin production by Salmonella typhimurium strains of different virulence. J Med Microbiol 21: 19–23, 1986\nHouston CW, Davis CP, Peterson JW: Salmonella toxin synthesis is unrelated to the presence of temperate bacteriophages. Infect Immun 35: 749–751, 1982\nDe SN, Chatterji DN: An experimental study on the mechanism of action of V. cholerae on the intestinal mucous membrane. J Pathol Bacteriol 66: 559–562, 1953\nEvans DG, Evans DJ, Gorbach SL: Identification of enterotoxigenic E. coli and serum antitoxin activity by the vascular permeability factor assay. Infect Immun 8: 731–735, 1973\nPeterson JW, Houston CW, Koo FCW: Influence of culture conditions on mitomycin C-mediated bacteriophage induction and release of Salmonella toxin. Infect Immun 32: 232–242, 1981\nKaur R, Ganguly NK, Kumar L, Walia BNS: Studies on the pathophysiological mechanism of Campylobacter jejuni induced fluid secretion in rat ileum. FEMS Microbiol Lett 111: 327–330, 1993\nKessler M, Acuto O, Sterelli C, Murer H, Mueller M, Semenza G: A modification procedure for the rapid preparation of efficiently transporting vesicles from small intestinal brush border membranes. Their use in investigating some properties of D-glucose and choline transport systems. Biochim Biophys Acta 506: 136–154, 1978\nLowry OH, Rosebrough NJ, Farr AL, Randall RJ: Protein measurement with the Folin phenol reagent. J Biol Chem 193: 265–275, 1953\nPinkus LM: Separation and use of enterocytes. Meth Enzymol 77: 154–162, 1981\nToyoda S, Lee PC, Labenthol E: Physiological factors controlling release of enterokinase from rat enterocytes. Dig Dis Sci 30: 1174–1180, 1985\nOhkawa H, Oshishi N, Yagi H: Reaction of linoleic and hydroperoxide with TBA. J Lipid Res 19: 1053–1057, 1979\nRecknagel RO, Glende EA: Spectrophometric determination of lipid conjugated dienes. Meth Enzymol 105: 331–337, 1984\nMoron MS, Depierre JW, Mannerick B: Levels of glutathione, glutathione reductase and glutathione-S-transferase activities in rat liver and lung. Biochim Biophys Acta 582: 67–78, 1979\nThurnham DI, Smith E, Flora SP: Concurrent liquid chromatographic assay of retinol, α-tocopherol, β-carotene, α-carotene, lycopene and β-cryptoxanthin in plasma with tocopherol acetate as internal standard. Clin Chem 34 (Part 1): 377–381, 1988\nHopfer U: Isolated membrane vesicles as tools for analysis of epithelial transport. Am J Physiol 233: E445–E449, 1977\nKoo FCW, Peterson JW, Houston CW, Molina N: Pathogenesis of experimental salmonellosis. Inhibition of protein synthesis by cytotoxin. Infec Immun 43: 93–100, 1984\nPhull PS, Green CJ, Jacyna MR: A radical view of the stomach, the role of oxygen derived free radicals and antioxidants in gastroduodenal disease. Eur J Gastroenterol Hepatol 327: 265–274, 1995\nParks DA: Oxygen radicals: mediators of gastrointestinal pathophysiology. Gut 30: 293–298, 1989\nOtamiri T: Oxygen radicals, lipid peroxidation, and neutrophil infiltration after small intestinal ischemia and reperfusion. Surgery 105: 593–597, 1989\nKelly F: Glutathione content of the small intestine: regulation and function. Br J Nutr 69: 589–596, 1993\nJankowski J, Bridges AB, Scott N et al.: Circulating free radical markers and peptic ulcer disease. Eur J Gastroenterol Hepatol 3: 823–828, 1991\nHamilton R, Macleod J, Butler D: Functional and structural response of the intestine to enteric infections. In: S Tzipori (ed). Infectious Diarrhoea in the Young. Elsevier Science Publishers, B.V. 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growth factor (EGF) in high concentrations induces apoptosis of the tumor cells which express high levels of epidermal growth factor receptor. However, the precise mechanism for this induction is not clear. Galectin-3 is the most probable candidate for mediating this effect, as it is known to induce anti-apoptotic activity in a variety of tumor cells exposed to diverse apoptotic stimuli. In this study, we determined whether galectin-3 plays a role in high concentrations of EGF-induced apoptosis of HepG2 cells. We found that EGF in high concentrations led to the growth inhibition of HepG2 cells, which were associated with promotion of cell death. High concentrations of EGF suppressed cytoplasmic expression of galectin-3. Moreover, we demonstrated overexpression of galectin-3 could reduce EGF-induced apoptosis in HepG2 cells. Our study demonstrated for the first time that downregulation of cytoplasmic galectin-3 was essential for high concentrations of EGF-induced apoptosis in HepG2 cells.",{"EN":1446},"Downregulation of galectin-3 by EGF mediates the apoptosis of HepG2 cells",{"VOID":1448},"Schlessinger J (2000) Cell signaling by receptor tyrosine kinases. Cell 103:211–225\nMarmor MD, Skaria KB, Yarden Y (2004) Signal transduction and oncogenesis by ErbB\u002FHER receptors. Int J Radiat Oncol Biol Phys 58:903–913\nMilanezi F, Carvalho S, Schmitt FC (2008) EGFR\u002FHER2 in breast cancer: a biological approach for molecular diagnosis and therapy. Expert Rev Mol Diagn 8:417–434\nMarais R, Marshall CJ (1996) Control of the ERK MAP kinase cascade by Ras and Raf. Cancer Surv 27:101–125\nNormanno N, Lua AD, Bianco C, Strizzi L, Mancino M, Maiello MR, Carotenuto A, De Feo G, Caponigro F, Salomon DS (2006) Epidermal growth factor receptor (EGFR) signaling in cancer. Gene 366:2–16\nLurje G, Lenze HJ (2009) EGFR signaling and drug discovery. Oncology 77:400–410\nKawamoto T, Mendelsohn J, Le A, Sato GH, Lazar CS, Gill GN (1984) Relation of epidermal growth factor receptor concentration to growth of human epidermoid carcinoma A431 cells. J Biol Chem 259:7761–7766\nArmstrong DK, Kaufmann SH, Ottaviano YL, Furuya Y, Buckley JA, Isaacs JT, Davidson NE (1994) Epidermal growth factor-mediated apoptosis of MDA-MB-468 human breast cancer cells. Cancer Res 54:5280–5283\nGarcia R, Franklin RA, McCubrey JA (2006) Cell death of MCF-7 human breast cancer cells induced by EGFR activation in the absence of other growth factors. Cell Cycle 5:1840–1846\nGrudinkin PS, Zenin VV, Kropotov AV, Dorosh VN, Nikolsky NN (2007) EGF-induced apoptosis in A431 cells is dependent on STAT1, but not on STAT3. Eur J Cell Biol 86:591–603\nLeffler H, Carlsson S, Hedlund M, Qian Y, Poirier F (2004) Introduction to galectins. Glycoconj J 19:433–440\nVan de Brule F, Califices S, Castronovo V (2004) Expression of galectins in cancer: a critical review. Glycoconj J 19:537–542\nLiu FT, Patterson RJ, Wang JL (2002) Intracellular functions of galectins. Biochim Biophys Acta 1572:263–273\nHoyer KK, Pang M, Gui D, Shintaku IP, Kuwabara I, Liu FT, Said JW, Baum LG, Teitell MA (2004) An anti-apoptotic role for galectin-3 in diffuse large B-cell lymphomas. Am J Pathol 164:893–902\nTakenaka Y, Fukumori T, Yoshii T, Oka N, Inohara H, Kim HR, Bresalier RS, Raz A (2004) Nuclear export of phodphorylated galectin-3 regulates its antiapoptotic activity in response to chemotherapeutic drugs. Mol Cell Biol 24:4395–4406\nYu F, Finley RL, Kim HR (2002) Galectin-3 translocates to the perinuclear membranes and inhibits cytochrome c release from the mitochondria. A role for synexin in galectin-3 translocation. J Biol Chem 277:15819–15827\nLiu FT, Rabinovich GA (2005) Galectins as modulators of tumor progression. Nat Rev Cancer 5:29–39\nElad-Sfadia G, Haklai R, Ballan E, Kloog Y (2004) Galectin-3 augments K-Ras activation and triggers a Ras signal that attenuates ERK but not phodphoinositide 3-kinase activity. J Biol Chem 279:34922–34930\nKrall JA, Beyer EM, MacBeath G (2011) High- and low-affinity epidermal growth factor receptor-ligand interactions activate distinct signaling pathways. PLoS One 6:e15945\nYang EB, Wang DF, Mack P, Cheng LY (1996) EGF receptor in human Chang liver and hepatoma HepG2 cells. Mol Biol Int 38:813–820\nYamauchi K, Pessin JE (1995) Epidermal growth factor-induced association of the SHPTP2 protein tyrosine phosphatase with a 115-kDa phosphotyrosine protein. J Biol Chem 270:14871–14874\nShirako E, Hirayama N, Sukada YI, Tanaka T, Kitamura N (2008) Up-regulation of p21CIP1 expression mediated by ERK-dependent and -independent pathways contributes to hepatocyte growth factor-induced inhibition of HepG2 hepatoma cell proliferation. J Cell Biochem 204:176–188\nZhuge J, Cederbaum AI (2006) Serum deprivation-induced HepG2 cell death is potentiated by CYP2E1. Free Radic Biol Med 40:63–74\nSchamberger CJ, Gerner C, Cerni C (2005) Caspase-9 plays a marginal role in serum starvation-induced apoptosis. Exp Cell Res 302:115–128\nTakehara T, Liu X, Fujimoto J, Friedman SL, Takahashi H (2001) Expression and role of Bcl-xL in human hepatocellular carcinomas. Hepatology 34:55–61\nWu X, Daniels T, Molinaro C, Lilly MB, Casiano CA (2002) Caspase cleavage of the nuclear autoantigen LEDGF\u002Fp75 abrogates its prosurvival function: implications for autoimmunity in atopic disorders. Cell Death Differ 9:915–925\nKang S, Song J, Kang H, Kim S, Lee Y, Park D (2003) Insulin can block apoptosis by decreasing oxidative stress via phosphatidylinositol 3-kinase- and extracellular signal-regulated protein kinase-dependent signaling pathways in HepG2 cells. Eur J Endocrinol 148:147–155\nHsu DK, Liu FT (2004) Regulation of cellular homeostasis by galectins. Glycoconj J 19:507–515\nNakahara S, Oka N, Raz A (2005) On the role of galectin-3 in cancer apoptosis. Apoptosis 10:267–275\nKolch W (2000) Meaningful relationships: the regulation of the Ras\u002FRaf\u002FMEK\u002FERK pathway by protein interactions. Biochem J 351:289–305\nMcCubrey JA, Steelman LS, Abrams SL (2006) Roles of the RAF\u002FMEK\u002FERK and PI3K\u002FPETN\u002FAKT pathways in malignant transformation and drug resistance. Adv Enzyme Regul 46:249–279\nKim HR, Lin HM, Briliran H, Raz A (1999) Cell cycle arrest and inhibition of anoikis by galectin-3 in human breast epithelial cells. Cancer Res 59:148–4154\nLin HM, Pestell G, Raz A, Kim HR (2002) Galectin-3 enhanced cyclin D, promoter activity through SP1 and a cAMP-responsive element in human breast epithelial cells. Oncogene 21:8001–8010\nChin YE, Kitagawa M, Su W, You ZH, Iwamoto Y, Fu XY (1996) Cell growth arrest and induction of cyclin-dependent kinase inhibitor p21WAF1\u002FCIP1 mediated by STAT. Science 272:719–722\nAnto RJ, Venkatraman M, Karunagaran D (2003) Inhibition of NF-κB sensitizes A431 cells to epidermal growth factor-induced apoptosis, whereas its activation by ectopic expression of RelA confers resistance. J Biol Chem 278:25490–25498\nCalifice S, Castronovo V, Bracke M, Van Den Brule F (2004) Dual activities of galectin-3 in human prostate cancer: tumor suppression of nuclear galectin-3 vs tumor promotion of cytoplasmic galectin-3. Oncogene 23:7527–7536\nParon I (2003) Nuclear localization of galectin-3 in transformed thyroid cells: a role in transcriptional regulation. 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Feng",{"url":1451,"publisher":1588,"properties":1641},{"id":868,"createTime":869,"updateTime":870,"relativeEntities":1589,"slug":872,"properties":1590,"entityType":25,"verifyStatus":878,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":32,"subjectFields":1593,"manageAffiliations":1610,"indexDatabases":1621,"url":28,"thumbnailPath":28,"statistic":1636,"gsStatistic":28,"type":55,"analyzePriority":28},[],{"issn":1591,"title":1592},{"VOID":875},{"EN":877},[1594,1598,1602,1606],{"id":881,"createTime":28,"updateTime":28,"relativeEntities":1595,"label":1596,"description":1597,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":884},{},{"id":887,"createTime":28,"updateTime":28,"relativeEntities":1599,"label":1600,"description":1601,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":890},{},{"id":893,"createTime":28,"updateTime":28,"relativeEntities":1603,"label":1604,"description":1605,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":896},{},{"id":899,"createTime":28,"updateTime":28,"relativeEntities":1607,"label":1608,"description":1609,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":902},{},[1611,1616],{"id":906,"createTime":28,"updateTime":28,"relativeEntities":1612,"slug":28,"properties":1613,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1615,"statistic":28},[],{"title":1614},{"EN":910},[],{"id":913,"createTime":28,"updateTime":28,"relativeEntities":1617,"slug":28,"properties":1618,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1620,"statistic":28},[],{"title":1619},{"EN":917},[919],[1622,1629],{"id":922,"indexDatabase":1623,"url":928,"indexYears":929,"academicFieldIds":1628,"indexDatabaseRanking":935},{"id":786,"createTime":28,"updateTime":28,"relativeEntities":1624,"label":1625,"description":1626,"key":792,"publicationTags":1627,"standard":28},[],{"EN":789,"VI":789},{"EN":789,"VI":791},[794],[931,932,933,934],{"id":937,"indexDatabase":1630,"url":28,"indexYears":28,"academicFieldIds":1635,"indexDatabaseRanking":28},{"id":939,"createTime":28,"updateTime":28,"relativeEntities":1631,"label":1632,"description":1633,"key":946,"publicationTags":1634,"standard":28},[],{"EN":942,"VI":942},{"EN":944,"VI":945},[948,813],[950],{"impactFactor":32,"impactFactorByYear":1637,"i10Index":32,"i10IndexLast5Year":32,"totalPublication":49,"totalPublicationByYear":1638,"totalCitation":32,"totalCitationByYear":1639,"totalCitationPerPublication":32,"totalCitationPerPublicationByYear":1640,"hindexLast5Year":32,"hindex":32},{},{"1999":40,"2000":40,"2001":40,"2002":40,"2004":40,"2012":40,"2019":40},{},{},{"pages":1642,"volume":1644},{"VOID":1643},"157-165",{"VOID":1645},"369","2012-07-04",[948,935],{"id":1649,"createTime":1650,"updateTime":1651,"relativeEntities":1652,"slug":1653,"properties":1654,"entityType":975,"verifyStatus":26,"verifyTime":1651,"verifyNote":976,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":1663,"fullTextUrl":28,"authors":1664,"publicationType":1073,"publisherRelationship":1769,"citationCount":28,"citationInfo":28,"publishDate":1828,"publishYear":1829,"citationAnalyzeStatus":878,"lastCitationAnalyze":28,"indexDatabases":1830,"openAccess":28,"references":28,"isForceReanalyzing":1136},"002e69e0-bb33-4a1b-9361-58555ae34d2d","2023-11-24T22:35:51.478+00:00","2025-01-01T07:59:37.776+00:00",[],"Role-of-extracellular-matrix-proteins-in-heart-function",{"abstract":1655,"title":1657,"references":1659,"doi":1661},{"EN":1656},"The cardiac interstitium is populated by nonmyocyte cell types including transcriptionally active cardiac fibroblasts and endothelial cells. Since these cells are the source of many components of the cardiac extracellular matrix, and because changes in cardiac extracellular matrix are suspected of contributing to the genesis of cardiovascular complications in disease states such as diabetes, hypertension, cardiac hypertrophy and congestive heart failure, interest in the mechanisms of activation of fibroblasts and endothelial cells has led to progress in understanding these processes. Recent work provides evidence for the role of the renin-angiotensin-aldosterone system in the pathogenesis of abnormal deposition of extracellular matrix in the cardiac interstitium during the development of inappropriate cardiac hypertrophy and failure. The cardiac extracellular matrix is also known to change in response to altered cardiac performance associated with post-natal aging, and in response to environmental stimuli including intermittent hypoxia and abnormal nutrition. It is becoming clear that the extracellular matrix mainly consists of molecules of collagen types I and III; they form fibrils and provide most of the connective material for tying together myocytes and other structures in the myocardium and thus is involved in the transmission of developed mechanical force. The data available in the literature support the view that the extracellular matrix is a dynamic entity and alterations in this structure result in the development of heart dysfunction.",{"EN":1658},"Role of extracellular matrix proteins in heart function",{"VOID":1660},"Swynghedauw B: Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles. Physiol Rev 66: 710–771, 1986\nBaldwin KM, Cooke DA, Cheadle WG: Enzyme alteration in neonatal muscle during development. J Mol Cell Cardiol 8: 651–660, 1977\nBrooks WW, Bing OH, Blaustein AS, Allen PD: Comparison of contractile state and myosin isoenzymes of rat right and left ventricular myocardium. 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Dhalla",{"url":1663,"publisher":1770,"properties":1823},{"id":868,"createTime":869,"updateTime":870,"relativeEntities":1771,"slug":872,"properties":1772,"entityType":25,"verifyStatus":878,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":32,"subjectFields":1775,"manageAffiliations":1792,"indexDatabases":1803,"url":28,"thumbnailPath":28,"statistic":1818,"gsStatistic":28,"type":55,"analyzePriority":28},[],{"issn":1773,"title":1774},{"VOID":875},{"EN":877},[1776,1780,1784,1788],{"id":881,"createTime":28,"updateTime":28,"relativeEntities":1777,"label":1778,"description":1779,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":884},{},{"id":887,"createTime":28,"updateTime":28,"relativeEntities":1781,"label":1782,"description":1783,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":890},{},{"id":893,"createTime":28,"updateTime":28,"relativeEntities":1785,"label":1786,"description":1787,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":896},{},{"id":899,"createTime":28,"updateTime":28,"relativeEntities":1789,"label":1790,"description":1791,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":902},{},[1793,1798],{"id":906,"createTime":28,"updateTime":28,"relativeEntities":1794,"slug":28,"properties":1795,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1797,"statistic":28},[],{"title":1796},{"EN":910},[],{"id":913,"createTime":28,"updateTime":28,"relativeEntities":1799,"slug":28,"properties":1800,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1802,"statistic":28},[],{"title":1801},{"EN":917},[919],[1804,1811],{"id":922,"indexDatabase":1805,"url":928,"indexYears":929,"academicFieldIds":1810,"indexDatabaseRanking":935},{"id":786,"createTime":28,"updateTime":28,"relativeEntities":1806,"label":1807,"description":1808,"key":792,"publicationTags":1809,"standard":28},[],{"EN":789,"VI":789},{"EN":789,"VI":791},[794],[931,932,933,934],{"id":937,"indexDatabase":1812,"url":28,"indexYears":28,"academicFieldIds":1817,"indexDatabaseRanking":28},{"id":939,"createTime":28,"updateTime":28,"relativeEntities":1813,"label":1814,"description":1815,"key":946,"publicationTags":1816,"standard":28},[],{"EN":942,"VI":942},{"EN":944,"VI":945},[948,813],[950],{"impactFactor":32,"impactFactorByYear":1819,"i10Index":32,"i10IndexLast5Year":32,"totalPublication":49,"totalPublicationByYear":1820,"totalCitation":32,"totalCitationByYear":1821,"totalCitationPerPublication":32,"totalCitationPerPublicationByYear":1822,"hindexLast5Year":32,"hindex":32},{},{"1999":40,"2000":40,"2001":40,"2002":40,"2004":40,"2012":40,"2019":40},{},{},{"pages":1824,"volume":1826},{"VOID":1825},"101-120",{"VOID":1827},"129","1993-12-01",1993,[948,935],{"id":1832,"createTime":1833,"updateTime":1834,"relativeEntities":1835,"slug":1836,"properties":1837,"entityType":975,"verifyStatus":26,"verifyTime":1834,"verifyNote":976,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":1846,"fullTextUrl":28,"authors":1847,"publicationType":1073,"publisherRelationship":1941,"citationCount":28,"citationInfo":28,"publishDate":2000,"publishYear":2001,"citationAnalyzeStatus":878,"lastCitationAnalyze":28,"indexDatabases":2002,"openAccess":28,"references":28,"isForceReanalyzing":1136},"005a3ae0-4c7c-46ca-951f-84d2f976ae0b","2023-12-29T13:55:17.300+00:00","2025-01-04T04:58:40.107+00:00",[],"The-role-of-GTPase-activating-protein-ARHGAP26-in-human-cancers",{"abstract":1838,"title":1840,"references":1842,"doi":1844},{"EN":1839},"Rho GTPases are molecular switches that play an important role in regulating the behavior of a variety of tumor cells. RhoA GTPase-activating protein 26 (ARHGAP26) is a GTPase-activating protein and inhibits the activity of Rho GTPases by promoting the hydrolytic ability of Rho GTPases. It also affects tumorigenesis and progression of various tumors through several methods, including formation of abnormal fusion genes and circular RNA. This review summarizes the biological functions and molecular mechanisms of ARHGAP26 in different tumors, proposes the potential clinical value of ARHGAP26 in cancer treatment, and discusses current issues that need to be addressed.",{"EN":1841},"The role of GTPase-activating protein ARHGAP26 in human cancers",{"VOID":1843},"Hildebrand JD, Taylor JM, Parsons JT (1996) An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase. 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Nature 420:629–35. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fnature01148\nOhta K, Goto H, Matsumoto Y, Yumine N, Tsurudome M, Nishio M (2016) Graf1 controls the growth of human parainfluenza virus type 2 through Inactivation of RhoA signaling. J Virol 90:9394–405. https:\u002F\u002Fdoi.org\u002F10.1128\u002FJVI.01471-16\nLucken-Ardjomande Häsler S, Vallis Y, Jolin HE, McKenzie AN, McMahon HT (2014) GRAF1a is a brain-specific protein that promotes lipid droplet clustering and growth, and is enriched at lipid droplet junctions. J Cell Sci 127:4602–19. https:\u002F\u002Fdoi.org\u002F10.1242\u002Fjcs.147694\nShibata H, Oishi K, Yamagiwa A, Matsumoto M, Mukai H, Ono Y (2001) PKNbeta interacts with the SH3 domains of Graf and a novel Graf related protein, Graf2, which are GTPase activating proteins for Rho family. 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history of the development of the ideas and research of organized metabolic systems during last three decades is shortly reviewed. The cell cytoplasm is crowded with solutes, soluble macromolecules such as enzymes, nucleic acids, structural proteins and membranes. The high protein density within the large compartments of the cells predominantly determines the major characteristics of cellular environment such as viscosity, diffusion and inhomogeneity. The fact that the solvent viscosity of cytoplasm is not substantially different from the water is explained by intracellular structural heterogeneity: the intrinsic macromolecular density is relatively low within the interstitial voids in the cell because many soluble enzymes are apparently integral parts of the insoluble cytomatrix and are not distributed homogeneously. The molecular crowding and sieving restrict the mobility of very large solutes, binding severely restrict the mobility of smaller solutes. One of consequence of molecular crowding and hindered diffusion is the need to compartmentalize metabolic pathway to overcome diffusive barriers. Although the movement of small molecules is slowed down in the cytoplasm, the metabolism can successfully proceed and even be facilitated by metabolite channeling which directly transfers the intermediate from one enzyme to an adjacent enzyme without the need of free aqueous-phase diffusion. The enhanced probability for intermediates to be transfered from one active site to the other by sequential enzymes requires stable or transient interactions of the relevant enzymes, which associate physically in non-dissociable, static multienzyme complexes – metabolones, particles containing enzymes of a part or whole metabolic systems. Therefore, within the living cell the metabolism depends on the structural organization of enzymes forming microcompartments. Since cells contain many compartments and microenvironments, the measurement of the concentration of metabolites in whole cells or tissues gives an average cellular concentration and not that which is actually sensed by the active site of a specific enzyme. Thus, the microcompartmentation could provide a mechanism which can control metabolic pathways. Independently and in parallel to the developments described above, the ideas of compartmentation came into existence from the necessity to explain important physiological phenomena, in particular in heart research and in cardiac electrophysiology. These phenomena demonstrated the physiological importance of the biophysical and biochemical mechanisms described in this review.",{"EN":2177},"On the origin of intracellular compartmentation and organized metabolic systems",{"VOID":2179},"Srere PA: Enzyme concentrations in tissues. Science 158: 936–937, 1967\nFulton AB: How crowded is the cytoplasm? 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Kluwer Academic Publishers, Dordrecht, 1994, pp 1–348\nSaks VA, Ventura, Clapier R, Leverve X, Rossi A, Rigoulet M (eds): Mol Cell Biochem 184: 3–9, 1998\nSaks VA, Veksler VI, Kuznetsov AV, Kay L, Sikk P, Tiivel T, Tranqui L, Olivares J, Winkler K, Wiedemann F, Kunz WS: Permeabilized cell and skinned fiber techniques in studies of mitochondrial function in vivo. Mol Cell Biochem 184: 81–100, 1998\nPucar D, Dzeja PP, Bast P, Juranic N, Macura S, Terzik A: Cellular energetics in the preconditioned state. Protective role for phosphotransfer reactions captured by 18O-assisted 31PNMR. J Biol Chem 276: 44812–44819, 2001\nJoubert F, Hoerter JA, Mazet JL: Discrimination of cardiac subcellular creatine kinase fluxes by NMR spectroscopy: A new method of analysis. Biophys J 81: 2995–3004, 2001\nAliev MK, Saks VA: Compartmentalised energy transfer in cardio-myocytes. Use of mathematical modeling for analysis of in vivo regulation of respiration. 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Biophys Chem 54: 137–142\nSaks VA, Kuznetsov AV, Kupriyanov VV, Miceli MV, Jacobus WJ: Creatine kinase of rat heart mitochondria. The demonstration of functional coupling to oxidative phosphorylation in an inner membrane-matrix preparation. J Biol Chem 260: 7757–7764, 1985\nSeppet E, Kaambre T, Sikk P, Tiivel T, Vija H, Kay L, Appaix F, Tonkonogi M, Sahlin K, Saks VA: Functional complexes of mitochondria with MgATPases of myofibrils and sarcoplasmic reticulum in muscle cells. Biochim Biophys Acta 1504: 379–395, 2001\nSaks VA, Kaambre T, Sikk P, Eimre M, Orlova E, Paju K, Piirsoo A, Appaix F, Kay L, Regiz-Zagrosek V, Fleck E, Seppet E: Intracellular energetic units in red muscle cells. Biochem J 356: 643–657, 2001\nKaasik A, Veksler V, Boehm E, Novotova M, Minajeva A, Ventura-Clapier R: Energetic crosstalk between organelles. Architectural integration of energy production and utilization. Circ Res 89: 153–159, 2001\nBricknell OL, Opie LH: A relationship between adenosine triphosphate, glycolysis and ischemic contracture in the isolated rat heart. J Mol Cell Cardiol 13: 941–945, 1981\nMercer RW, Dunham PB: Membrane-bound ATP fuels the Na\u002FK pump. Studies on membrane-bound glycolytic enzymes on inside-out vesicles from human red cell membranes. J Gen Physiol 78: 547–568, 1981\nWeiss JN, Lamp ST: Glycolysis preferentially inhibits ATP-sensitive K-channels in isolated guinea-pig cardiac myocytes. Science 238: 67–69, 1987\nHan JW, Thieleczek R, Varsany M, Heimeyer LMG: Compartmentalized ATP synthesis in skeletal muscle triads. Biochemistry 31: 377–384, 1992\nJurevicius J, Fischmeister R: cAMP compartmentation is responsible for a local activation of cardiac Ca2+ channels by α-adrenergic agonists. Proc Natl Acad Sci USA 93: 295–299, 1996\nCarmeliet E: A fuzzy subsarcolemmal space for intracellular Na+ in cardiac cells? 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Ann Rev Physiol 61: 311–335, 1999",{"VOID":2181},"10.1023\u002FB:MCBI.0000009855.14648.2c","http:\u002F\u002Flink.springer.com\u002F10.1023\u002FB:MCBI.0000009855.14648.2c",[2184,2199],{"id":2185,"sortIndex":32,"researcher":28,"roles":2186,"affiliations":2187,"properties":2196,"displayName":2198,"givenName":28,"familyName":28},"98ddf509-00de-493e-96ed-e5c9cae2c109",[982],[2188],{"id":2189,"sortIndex":32,"affiliation":2190,"properties":28},"a2f15107-b2a7-4739-85ef-87b918e9a558",{"id":2189,"createTime":28,"updateTime":28,"relativeEntities":2191,"slug":28,"properties":2192,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2195,"statistic":28},[],{"title":2193},{"VI":2194},"Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary",[],{"title":2197},{"VI":2198},"Judit Ovádi",{"id":2200,"sortIndex":40,"researcher":28,"roles":2201,"affiliations":2202,"properties":2220,"displayName":2222,"givenName":28,"familyName":28},"2443a3d7-d604-4248-b7e8-3fdf20d248a1",[982],[2203,2211],{"id":2204,"sortIndex":32,"affiliation":2205,"properties":28},"ca6a6334-f565-4990-9c2b-b493d03dee8c",{"id":2204,"createTime":28,"updateTime":28,"relativeEntities":2206,"slug":28,"properties":2207,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2210,"statistic":28},[],{"title":2208},{"VI":2209},"Laboratory of Fundamental and Applied Bioenergetics, INSERM E0221, Joseph Fourier University, Grenoble, France",[],{"id":2212,"sortIndex":40,"affiliation":2213,"properties":2219},"79ce5d30-86c4-4e37-9640-a2abe285e357",{"id":2212,"createTime":28,"updateTime":28,"relativeEntities":2214,"slug":28,"properties":2215,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2218,"statistic":28},[],{"title":2216},{"VI":2217},"Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia",[],{},{"title":2221},{"VI":2222},"Valdur Saks",{"url":2182,"publisher":2224,"properties":2277},{"id":868,"createTime":869,"updateTime":870,"relativeEntities":2225,"slug":872,"properties":2226,"entityType":25,"verifyStatus":878,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":32,"subjectFields":2229,"manageAffiliations":2246,"indexDatabases":2257,"url":28,"thumbnailPath":28,"statistic":2272,"gsStatistic":28,"type":55,"analyzePriority":28},[],{"issn":2227,"title":2228},{"VOID":875},{"EN":877},[2230,2234,2238,2242],{"id":881,"createTime":28,"updateTime":28,"relativeEntities":2231,"label":2232,"description":2233,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":884},{},{"id":887,"createTime":28,"updateTime":28,"relativeEntities":2235,"label":2236,"description":2237,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":890},{},{"id":893,"createTime":28,"updateTime":28,"relativeEntities":2239,"label":2240,"description":2241,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":896},{},{"id":899,"createTime":28,"updateTime":28,"relativeEntities":2243,"label":2244,"description":2245,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":902},{},[2247,2252],{"id":906,"createTime":28,"updateTime":28,"relativeEntities":2248,"slug":28,"properties":2249,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2251,"statistic":28},[],{"title":2250},{"EN":910},[],{"id":913,"createTime":28,"updateTime":28,"relativeEntities":2253,"slug":28,"properties":2254,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2256,"statistic":28},[],{"title":2255},{"EN":917},[919],[2258,2265],{"id":922,"indexDatabase":2259,"url":928,"indexYears":929,"academicFieldIds":2264,"indexDatabaseRanking":935},{"id":786,"createTime":28,"updateTime":28,"relativeEntities":2260,"label":2261,"description":2262,"key":792,"publicationTags":2263,"standard":28},[],{"EN":789,"VI":789},{"EN":789,"VI":791},[794],[931,932,933,934],{"id":937,"indexDatabase":2266,"url":28,"indexYears":28,"academicFieldIds":2271,"indexDatabaseRanking":28},{"id":939,"createTime":28,"updateTime":28,"relativeEntities":2267,"label":2268,"description":2269,"key":946,"publicationTags":2270,"standard":28},[],{"EN":942,"VI":942},{"EN":944,"VI":945},[948,813],[950],{"impactFactor":32,"impactFactorByYear":2273,"i10Index":32,"i10IndexLast5Year":32,"totalPublication":49,"totalPublicationByYear":2274,"totalCitation":32,"totalCitationByYear":2275,"totalCitationPerPublication":32,"totalCitationPerPublicationByYear":2276,"hindexLast5Year":32,"hindex":32},{},{"1999":40,"2000":40,"2001":40,"2002":40,"2004":40,"2012":40,"2019":40},{},{},{"pages":2278,"volume":2280},{"VOID":2279},"5-12",{"VOID":2281},"256","2004-01-01",[948,935],{"id":2285,"createTime":2286,"updateTime":2287,"relativeEntities":2288,"slug":2289,"properties":2290,"entityType":975,"verifyStatus":26,"verifyTime":2287,"verifyNote":976,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":2299,"fullTextUrl":28,"authors":2300,"publicationType":1073,"publisherRelationship":2373,"citationCount":28,"citationInfo":28,"publishDate":2432,"publishYear":1134,"citationAnalyzeStatus":878,"lastCitationAnalyze":28,"indexDatabases":2433,"openAccess":28,"references":28,"isForceReanalyzing":1136},"006b3fb4-112c-40d6-9de4-7af81de1634c","2024-01-14T14:14:22.558+00:00","2025-01-18T20:02:08.464+00:00",[],"New-insights-into-the-Orange-domain-of-E-spl-M8-and-the-roles-of-the-C-terminal-domain-in-autoinhibition-and-Groucho-recruitment",{"abstract":2291,"title":2293,"references":2295,"doi":2297},{"EN":2292},"CK2 is a Ser\u002FThr protein kinase that regulates the activity of the Drosophila basic-helix-loop-helix (bHLH) repressor M8 encoded by the Enhancer of split Complex (E(spl)C) during neurogenesis. Specifically, phosphorylation appears to elicit a conformational change in an autoinhibited state of M8 to one that is permissive for repression. We describe biochemical and molecular modeling studies that provide new insights into repression by M8. Our studies implicate the phosphorylation domain in autoinhibition, and indicate that binding of the co-repressor Groucho (Gro) is context-dependent. Molecular modeling indicates that the Orange domain, proposed to be a specificity-determinant, may instead play a structural role, and that a conformational rearrangement of this domain may be necessary for repression. This model also provides a structural mechanism for the behavior of mutant alleles of the m8 gene. The insights gained from these studies should be applicable to the conserved metazoan bHLH repressors of the Hairy and Enhancer of Split (HES) family that are related to Drosophila M8.",{"EN":2294},"New insights into the Orange domain of E(spl)-M8, and the roles of the C-terminal domain in autoinhibition and Groucho recruitment",{"VOID":2296},"Bose A, Kahali B, Zhang S, Lin J-M, Allada R, Karandikar U, Bidwai A (2006) Drosophila CK2 regulates lateral-inhibition during eye and bristle development. Mech Dev 123:649–664\nKarandikar U, Trott RL, Yin J, Bishop CP, Bidwai AP (2004) Drosophila CK2 regulates eye morphogenesis via phosphorylation of E(spl)M8. Mech Dev 121:273–286\nGomez-Skarmeta JL, Campuzano S, Modolell J (2003) Half a century of neural prepatterning: the story of a few bristles and many genes. Nat Rev Neurosci 4:587–598\nCagan R (2009) Principles of Drosophila eye differentiation. Curr Top Dev Biol 89:115–135\nKiefer JC (2005) Proneural factors and neurogenesis. 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