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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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1621, 10.1084\u002Fjem.20130498\nCyr, 1994, Dnaj-like proteins – molecular chaperones and specific regulators of Hsp70, Trends Biochem Sci, 19, 176, 10.1016\u002F0968-0004(94)90281-X\nDemarco, 2006, Monitoring dynamic protein interactions with photoquenching FRET, Nat Methods, 3, 519, 10.1038\u002Fnmeth889\nDephoure, 2008, A quantitative atlas of mitotic phosphorylation, Proc Natl Acad Sci U S A, 105, 10762, 10.1073\u002Fpnas.0805139105\nDorval, 2005, Transcriptional activity of the paired-like homeodomain proteins CHX10 and VSX1, J Biol Chem, 280, 10100, 10.1074\u002Fjbc.M412676200\nDöppler, 2005, A phosphorylatin state-specific antibody recognizes Hsp27, a novel substrate of protein kinase D, J Biol Chem, 280, 15013, 10.1074\u002Fjbc.C400575200\nEdwards, 2012, PKA phosphorylation of the small heat-shock protein Hsp20 enhances its cardioprotective effects, Biochem Soc Trans, 40, 210, 10.1042\u002FBST20110673\nEllis, 1987, Proteins as molecular chaperones, Nature, 328, 378, 10.1038\u002F328378a0\nEvans, 2001, Phosphorylation of cysteine string protein by protein kinase A: implications for the modulation of exocytosis, J Biol Chem, 276, 47877, 10.1074\u002Fjbc.M108186200\nFan, 2003, Mechanisms for regulation of Hsp70 function by Hsp40, Cell Stress Chaperones, 8, 309, 10.1379\u002F1466-1268(2003)008\u003C0309:MFROHF>2.0.CO;2\nGaestel, 2006, MAPKAP kinases – MKs – two's company, three's a crowd, Nat Rev Mol Cell Biol, 7, 120, 10.1038\u002Fnrm1834\nGarrido, 2012, The small heat shock proteins family: the long forgotten chaperones, Int J Biochem Cell Biol, 44, 1588, 10.1016\u002Fj.biocel.2012.02.022\nGerits, 2007, Modulation of F-actin rearrangement by the cyclicAMP\u002FcAMP-dependent protein kinase (PKA) pathway is mediated by MAPK-activated protein kinase 5 and requires PKA-induced nuclear export of MK5, J Biol Chem, 282, 37232, 10.1074\u002Fjbc.M704873200\nGötz, 2009, The ER-membrane-resident Hsp40 ERj1 is a novel substrate for protein kinase CK2, Biochem 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10.1242\u002Fjcs.109.7.1787\nChen, 1996, Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase, J Biol Chem, 271, 26329, 10.1074\u002Fjbc.271.42.26329\nChen, 2010, TRPM7 regulates the migration of human nasopharyngeal carcinoma cell by mediating Ca(2+) influx, Cell Calcium, 47, 425, 10.1016\u002Fj.ceca.2010.03.003\nDauphinee, 2013, SASH1 is a scaffold molecule in endothelial TLR4 signaling, J Immunol, 191, 892, 10.4049\u002Fjimmunol.1200583\nDauphinee, 2006, Lipopolysaccharide signaling in endothelial cells, Lab Invest, 86, 9, 10.1038\u002Flabinvest.3700366\nDimmeler, 1995, Endotoxin-induced changes of endothelial cell viability and permeability: protective effect of a 21-aminosteroid, Eur J Pharmacol, 287, 257, 10.1016\u002F0014-2999(95)00499-8\nEcheverria, 2014, Endotoxin Induces Fibrosis in Vascular Endothelial Cells through a Mechanism Dependent on Transient Receptor Protein Melastatin 7 Activity, PLoS One, 9, e94146, 10.1371\u002Fjournal.pone.0094146\nEcheverria, 2013, Lipopolysaccharide induces a fibrotic-like phenotype in endothelial cells, J Cell Mol Med, 17, 800, 10.1111\u002Fjcmm.12066\nEide, 1995, Identification of Tyr-397 as the primary site of tyrosine phosphorylation and pp60src association in the focal adhesion kinase, pp125FAK, Mol Cell Biol, 15, 2819, 10.1128\u002FMCB.15.5.2819\nGoumans, 2008, Transforming growth factor beta-induced endothelial-to-mesenchymal transition: a switch to cardiac fibrosis, Trends Cardiovasc Med, 18, 293, 10.1016\u002Fj.tcm.2009.01.001\nGrandel, 2003, Endothelial responses to bacterial toxins in sepsis, Crit Rev Immunol, 23, 267, 10.1615\u002FCritRevImmunol.v23.i4.20\nHermosura, 2002, Dissociation of the store-operated calcium current I(CRAC) and the Mg-nucleotide-regulated metal ion current MagNuM, J Physiol, 539, 445, 10.1113\u002Fjphysiol.2001.013361\nHotchkiss, 2003, The pathophysiology and treatment of sepsis, N Engl J Med, 348, 138, 10.1056\u002FNEJMra021333\nHuet, 2011, Oxidative stress and endothelial dysfunction during sepsis, Front Biosci, 16, 1986, 10.2741\u002F3835\nInoue, 2010, Zinc-induced neurotoxicity mediated by transient receptor potential melastatin 7 channels, J Biol Chem, 285, 7430, 10.1074\u002Fjbc.M109.040485\nKimura, 2001, Alterations of Ca2+ mobilizing properties in migrating endothelial cells, Am J Physiol Heart Circ Physiol, 281, H745, 10.1152\u002Fajpheart.2001.281.2.H745\nKizu, 2009, Endothelial-mesenchymal transition as a novel mechanism for generating myofibroblasts during diabetic nephropathy, Am J Pathol, 175, 1371, 10.2353\u002Fajpath.2009.090698\nKovacs, 2012, Inhibition of the human epithelial calcium channel TRPV6 by 2-aminoethoxydiphenyl borate (2-APB), Cell Calcium, 52, 468, 10.1016\u002Fj.ceca.2012.08.005\nKozak, 2003, MIC channels are inhibited by internal divalent cations but not ATP, Biophys J, 84, 922, 10.1016\u002FS0006-3495(03)74909-1\nLappas, 2012, Anti-inflammatory properties of sirtuin 6 in human umbilical vein endothelial cells, Mediators Inflamm, 2012, 597514, 10.1155\u002F2012\u002F597514\nLivasy, 2004, Focal adhesion kinase overexpression in endometrial neoplasia, Appl Immunohistochem Mol Morphol, 12, 342, 10.1097\u002F00129039-200412000-00009\nMartini, 2010, Angiotensin II regulates endothelial cell migration through calcium influx via T-type calcium channel in human umbilical vein endothelial cells, Acta Physiol (Oxf), 198, 449, 10.1111\u002Fj.1748-1716.2009.02070.x\nMitra, 2005, Focal adhesion kinase: in command and control of cell motility, Nat Rev Mol Cell Biol, 6, 56, 10.1038\u002Fnrm1549\nMonteilh-Zoller, 2003, TRPM7 provides an ion channel mechanism for cellular entry of trace metal ions, J Gen Physiol, 121, 49, 10.1085\u002Fjgp.20028740\nNadler, 2001, LTRPC7 is a Mg.ATP-regulated divalent cation channel required for cell viability, Nature, 411, 590, 10.1038\u002F35079092\nNilius, 2007, Transient receptor potential cation channels in 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activity of macrophage migration inhibitory factor",{"VOID":1724},"Bacher, 1998, MIF expression in the rat brain: Implications for neuronal function, Molecular Medicine, 4, 217, 10.1007\u002FBF03401919\nBaugh, 2003, Macrophage migration inhibitory factor: A neuroendocrine modulator of chronic inflammation, Journal of Endocrinology, 179, 15, 10.1677\u002Fjoe.0.1790015\nBeissinger, 1998, How chaperones fold proteins, Biological Chemistry, 379, 245\nBendrat, 1997, Biochemical and mutational investigations of the enzymatic activity of macrophage migration inhibitory factor, Biochemistry, 36, 15356, 10.1021\u002Fbi971153a\nBen-Zvi, 1998, Minimal and optimal mechanisms for GroEL-mediated protein folding, Proceedings of the National Academy of Sciences of the United States of America, 95, 15275, 10.1073\u002Fpnas.95.26.15275\nBen-Zvi, 2002, Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones, The Journal of Biological Chemistry, 277, 49422, 10.1074\u002Fjbc.M209163200\nBernhagen, 1993, Macrophage migration inhibitory factor (MIF) is a pituitary-derived cytokine that potentiates lethal endotoxaemia, Nature, 365, 756, 10.1038\u002F365756a0\nBernhagen, 1994, Purification, bioactivity, and secondary structure analysis of mouse and human macrophage migration inhibitory factor (MIF), Biochemistry, 33, 14144, 10.1021\u002Fbi00251a025\nBhattacharyya, 2003, A peptide sequence YSGVCHTDLHAWHGDWPLPVK [40–60] in yeast alcohol dehydrogenase prevents the aggregation of denatured substrate proteins, Biochemical and Biophysical Research Communication, 307, 1, 10.1016\u002FS0006-291X(03)01116-1\nBischofberger, 2003, d-Peptides as inhibitors of the DnaK\u002FDnaJ\u002FGrpE chaperone system, The Journal of Biological Chemistry, 278, 19044, 10.1074\u002Fjbc.M300922200\nBloom, 1966, Mechanism of a reaction in vitro associated with delayed-type hypersensitivity, Science, 153, 80, 10.1126\u002Fscience.153.3731.80\nBradford, 1976, A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein–dye binding, Analytical Biochemistry, 72, 248, 10.1016\u002F0003-2697(76)90527-3\nBuchner, 1996, Supervising the fold: Functional principles of molecular chaperones, FASEB Journal, 10, 10, 10.1096\u002Ffasebj.10.1.8566529\nCalandra, 1994, The macrophage is an important and previously unrecognized source of macrophage migration inhibitory factor, Journal of Experimental Medicine, 179, 1895, 10.1084\u002Fjem.179.6.1895\nCherepkova, 2004, Macrophage migration inhibitory factor (MIF): Identification of the 30kDa MIF-related protein in bovine brain, Neurochemical Research, 29, 1391, 10.1023\u002FB:NERE.0000026403.06238.73\nDiamant, 2000, Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery, The Journal of Biological Chemistry, 275, 21107, 10.1074\u002Fjbc.M001293200\nDonn, 2004, Macrophage migration inhibitory factor: Molecular, cellular and genetic aspects of a key neuroendocrine molecule, Journal of Endocrinology, 182, 1, 10.1677\u002Fjoe.0.1820001\nDonnelly, 1997, Macrophage migration inhibitory factor: A regulator of glucocorticoid activity with a critical role in inflammatory disease, Molecular Medicine Today, 3, 502, 10.1016\u002FS1357-4310(97)01133-7\nFrydman, 2001, Folding of newly translated proteins in vivo: The role of molecular chaperones, Annual Review of Biochemistry, 70, 603, 10.1146\u002Fannurev.biochem.70.1.603\nFrydman, 1997, Chaperones get in touch: The hip-hop connection, Trends in Biochemical Sciences, 22, 87, 10.1016\u002FS0968-0004(97)01005-0\nGalat, 1993, Purification of macrophage migration inhibitory factor (MIF) from bovine brain cytosol, FEBS Letters, 319, 233, 10.1016\u002F0014-5793(93)80553-7\nGalat, 1994, A diversified family of 12kDa proteins with a high amino acid sequence similarity to macrophage migration inhibitory factor (MIF), European Journal of Biochemistry, 224, 417, 10.1111\u002Fj.1432-1033.1994.00417.x\n1997\nGurvits, 2004, Chaperone-like activity of macrophage migration inhibitory factor (MIF) from bovine brain, Journal of Neurochemistry, 88, 60\nGurvits, 2003, The brain pool of immunologically active heat-stable proteins in relation to adaptation to heat shock and other kinds of stress, Journal of Neurochemistry, 87, 152\nGurvits, 2000, Identification of macrophage migration inhibitory factor isoforms in bovine brain, Neurochemical Research, 25, 1125, 10.1023\u002FA:1007678214348\nHartman, 1993, Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro, Proceedings of the National Academy of Sciences of the United States of America, 90, 2276, 10.1073\u002Fpnas.90.6.2276\nHendrick, 1993, Molecular chaperone functions of heat-shock proteins, Annual Review of Biochemistry, 62, 349, 10.1146\u002Fannurev.bi.62.070193.002025\nHuang, 2002, Chaperone and antichaperone activities of trigger factor, European Journal of Biochemistry, 269, 4516, 10.1046\u002Fj.1432-1033.2002.03145.x\nHudson, 1999, A proinflammatory cytokine inhibits p53 tumor suppressor activity, Journal of Experimental Medicine, 190, 1375, 10.1084\u002Fjem.190.10.1375\nKleemann, 1998, Disulfide analysis reveals a role for macrophage migration inhibitory factor (MIF) as thiol–protein oxidoreductase, Journal of Molecular Biology, 280, 85, 10.1006\u002Fjmbi.1998.1864\nKnox, 1957, Enzymatic catalysis of the keto–enol tautomerisation of phenylpyruvic acids, The Journal of Biological Chemistry, 225, 675, 10.1016\u002FS0021-9258(18)64866-5\nLaemmli, 1970, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature, 227, 680, 10.1038\u002F227680a0\nMacRae, 2000, Structure and function of small heat shock\u002Falpha-crystallin proteins: Established concepts and emerging ideas, Cellular and Molecular Life Sciences, 57, 899, 10.1007\u002FPL00000733\nManna, 2001, Chaperone-like activity of tubulin: Binding and reactivation of unfolded substrate enzymes, The Journal of Biological Chemistry, 276, 39742, 10.1074\u002Fjbc.M104061200\nMischke, 1998, Cross-linking and mutational analysis of the oligomerization state of the cytokine macrophage migration inhibitory factor (MIF), FEBS Letters, 427, 85, 10.1016\u002FS0014-5793(98)00400-1\nMuhlhahn, 1996, NMR characterization of structure, backbone dynamics, and glutathione binding of the human macrophage migration inhibitory factor, Protein Science, 5, 2095, 10.1002\u002Fpro.5560051016\nNishihira, 1995, The structure and physicochemical properties of rat liver macrophage migration inhibitory factor, Biochimica et Biophysica Acta, 1247, 159, 10.1016\u002F0167-4838(94)00215-3\nNishino, 1995, Localization of MIF in secretory granules within the corticotropic thyrotropic cells of the pituitary gland, Molecular Medicine, 1, 781, 10.1007\u002FBF03401892\nNishio, 1999, Identification of macrophage migration inhibitory factor (MIF) in rat peripheral nerves: Its possible involvement in nerve regeneration, Biochimica et Biophysica Acta, 1453, 74, 10.1016\u002FS0925-4439(98)00086-6\nPhilo, 2004, Re-examining the oligomerization state of macrophage migration inhibitory factor (MIF) in solution, Biophysical Chemistry, 108, 77, 10.1016\u002Fj.bpc.2003.10.010\nPotolicchio, 2003, Molecular interaction and enzymatic activity of macrophage migration inhibitory factor (MIF) with immunorelevant peptides, The Journal of Biological Chemistry, 278, 30889, 10.1074\u002Fjbc.M302854200\nRosengren, 1997, The macrophage migration inhibitory factor (MIF) is a phenylpyruvate tautomerase, FEBS Letters, 417, 85, 10.1016\u002FS0014-5793(97)01261-1\nRossi, 1998, Human circulating eosinophils secrete macrophage migration inhibitory factor (MIF), Journal of Clinical Investigation, 101, 2869, 10.1172\u002FJCI1524\nSoman, 1983, Effect of oxyanions of the early transition metals on rabbit skeletal muscle phosphorylase, Biochemistry, 22, 4994, 10.1021\u002Fbi00290a018\nStromer, 2004, Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: The N-terminal domain is important for oligomer assembly and the binding of unfolding proteins, The Journal of Biological Chemistry, 279, 11222, 10.1074\u002Fjbc.M310149200\nSugimoto, 1996, Crystal structure of macrophage migration inhibitory factor from human lymphocyte at 2.1Å resolution, FEBS Letters, 389, 145, 10.1016\u002F0014-5793(96)00553-4\nSugrobova, 1983, Turbidimetric method for determination of glycogen phosphorylase activity and its use for estimation of equilibrium position of enzymic reaction, Journal of Biochemical and Biophysical Methods, 8, 299, 10.1016\u002F0165-022X(83)90004-0\nSun, 1996, Crystal structure at 2.6Å resolution of human macrophage migration inhibitory factor, Proceedings of the National Academy of Sciences of the United States of America, 93, 5191, 10.1073\u002Fpnas.93.11.5191\nSuzuki, 1996, Crystal structure of the macrophage migration inhibitory factor from rat liver, Nature Structural Biology, 3, 259, 10.1038\u002Fnsb0396-259\nSwope, 1998, Direct link between cytokine activity and a catalytic site for macrophage migration inhibitory factor, EMBO Journal, 17, 3534, 10.1093\u002Femboj\u002F17.13.3534\nWelsh, 1998, Small heat-shock protein family: Function in health and disease, Annual of New York Academy of Sciences, 851, 28, 10.1111\u002Fj.1749-6632.1998.tb08973.x\nYunis, 1962, Comparative studies on glycogen phosphorylase. 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Death. Dis., 6, e1766, 10.1038\u002Fcddis.2015.123\nBartel, 2004, MicroRNAs: genomics, biogenesis, mechanism, and function, Cell, 116, 281, 10.1016\u002FS0092-8674(04)00045-5\nBoll, 2013, MiR-130a, miR-203 and miR-205 jointly repress key oncogenic pathways and are downregulated in prostate carcinoma, Oncogene, 32, 277, 10.1038\u002Fonc.2012.55\nBouyssou, 2014, Regulation of microRNAs in cancer metastasis, Biochim. Biophys. Acta, 1845, 255\nChen, 2016, MicroRNA-130a promotes the metastasis and epithelial-mesenchymal transition of osteosarcoma by targeting PTEN, Oncol. Rep., 35, 3285, 10.3892\u002For.2016.4719\nCosta, 2015, MicroRNAs in glioblastoma: role in pathogenesis and opportunities for targeted therapies, CNS Neurol. Disord. 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A-I concentrations in early- and late-onset Alzheimer's disease, Neurosci Lett, 231, 175, 10.1016\u002FS0304-3940(97)00558-2\nSorci-Thomas, 2002, The effects of altered apolipoprotein A–I structure on plasma HDL concentration, Trends Cardiovasc Med, 3, 121, 10.1016\u002FS1050-1738(01)00163-3\nSoreghan, 1994, Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation, J Biol Chem, 269, 28551, 10.1016\u002FS0021-9258(19)61939-3\nTabner, 2005, Hydrogen peroxide is generated during the very early stages of aggregation of the amyloid peptides implicated in Alzheimer disease and familial British dementia, J Biol Chem, 280, 35789, 10.1074\u002Fjbc.C500238200\nTricerri, 1994, A rapid and efficient procedure for the purification of human apolipoprotein A–I by using gel filtration HPLC, Int J Biochromatog, 1, 159\nVollbach, 2005, APOA1 polymorphism influences risk for early-onset nonfamiliar AD, Ann Neurol, 58, 436, 10.1002\u002Fana.20593\nWilbur, 1949, The 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