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other provinces and regions in Vietnam and other country.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Address\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Headquarters of Can Tho Journal of Medicine and Pharmacy, located Scientific Research and International Cooperation Office: 179 Nguyen Van Cu Street, An Khanh Ward, Ninh Kieu District, Can Tho City, Vietnam.\u003C\u002Fspan>\u003C\u002Fp>","\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Ngày 16\u002F7\u002F2015, Tạp chí Y Dược học Cần Thơ được cấp chỉ số quốc tế: ISSN 2354-1210.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Từ tháng 4\u002F2016, Tạp chí đã được Hội đồng Giáo sư ngành Y đưa vào danh sách các tạp chí khoa học Y học được tính điểm công trình 0-0,5 điểm cho một bài báo đăng.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Năm 2020 Tạp chí Y Dược học Cần Thơ đã được phê duyệt vào danh mục của các Hội đồng Giáo sư ngành Dược học được tính điểm công trình 0-0,5 điểm cho một bài báo đăng.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ ra 12 số\u002Fnăm, 180-200 trang\u002Fsố.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Từ tháng 12\u002F2022 Tạp chí Y Dược học Cần Thơ là thành viên của hệ thống Crossref và từ tháng 01\u002F2023 tạp chí thực hiện bình duyệt online kín 2 chiều nhằm tăng tính minh bạch, tin cậy của các công trình nghiên cứu khoa học và đảm bảo tốt nhất chất lượng khoa học của bài viết.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tôn chỉ, mục đích và phạm vi của tạp chí\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tôn chỉ và mục đích hoạt động của tạp chí: xuất bản nhằm mục đích phổ biến kết quả từ các đề tài nghiên cứu khoa học; giao lưu trao đổi khoa học, chia sẻ kinh nghiệm, học tập, đồng thời cập nhật thông tin khoa học mới trong các lĩnh vực y, sinh, dược học trong và ngoài nước.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Phạm vi của tạp chí: Tạp chí xuất bản được chia thành 3 chuyên mục: (i) Bài báo nghiên cứu khoa học là kết quả công trình nghiên cứu khoa học có giá trị đã được triển khai nghiên cứu, (ii) Bài tổng quan y, sinh, dược học: phục vụ mục tiêu đào tạo liên tục trong lĩnh vực y, sinh, dược học; nhằm hệ thống hóa những kiến thức kinh điển và hiện đại; (iii) Thông tin cập nhật kiến thức mới về y, sinh, dược học trong nước và trên thế giới.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Chính sách truy cập mở\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ áp dụng chính sách truy cập mở đối với các bài báo đã xuất bản đến với độc giả, nhằm mở rộng cơ hội tiếp cận các kết quả nghiên cứu chất lượng cao và tăng cường trao đổi kiến thức. Tạp chí đăng tải trực tuyến (miễn phí) toàn văn các bài báo được công bố trên website của Tạp chí (https:\u002F\u002Ftapchi.ctump.edu.vn).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Đạo đức xuất bản\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ cam kết tuân thủ đạo đức xuất bản phù hợp với các hướng dẫn và tiêu chuẩn của the Committee on Publication Ethics (COPE), tuân thủ các nguyên tắc của COPE’s Core Practices, Best Practices Guidelines for Journal Editors và Guidelines on Good Publication Practices.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Bản thảo bài báo chỉ được chấp nhận khi được tác giả chịu trách nhiệm chính cam kết các nội dung sau: Các nội dung của bản thảo chưa được đăng tải toàn bộ hoặc một phần ở các tạp chí khác; Tất cả các tác giả đều có đóng góp một cách đáng kể vào quá trình nghiên cứu hoặc chuẩn bị bản thảo và cùng chịu trách nhiệm về các nội dung của bản thảo; Tuân thủ các biện pháp đảm bảo đạo đức nghiên cứu (ví dụ thỏa thuận đồng ý tham gia nghiên cứu).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Cam kết bảo mật\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí cam kết thực hiện và tuân thủ các quy định của luật và các văn bản hướng dẫn liên quan đến bảo mật thông tin cá nhân trên không gian mạng. Các thông tin mà người dùng (tác giả, độc giả, biên tập viên, người phản biện) nhập vào các biểu mẫu trên Hệ thống Quản lý xuất bản trực tuyến của tạp chí chỉ được sử dụng vào các mục đích đã được tuyên bố rõ ràng và sẽ không được cung cấp cho bất kỳ bên thứ ba nào khác, hay dùng vào bất kỳ mục đích nào khác.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Phí gửi bài\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Lệ phí gửi đăng bài: 1.000.000đ\u002Fbài báo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Lệ phí gửi đăng nhanh: 1.500.000đ\u002Fbài báo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Đối với tác giả là cán bộ viên chức thuộc Trường Đại học Y Dược Cần Thơ thì được hỗ trợ 50% lệ phí gửi đăng bài.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Đối với sinh viên thực hiện đề tài nghiên cứu khoa học cấp trường được hỗ trợ 100% lệ phí đăng bài ( Tác giả gửi đính kèm “ Quyết định về việc giao tổ chức thực hiện đề tài nghiên cứu khoa học cấp Trường của sinh viên”).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Hình thức nộp lệ phí:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Tiền mặt:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Nộp trực tiếp tại Phòng Tài chính - Kế toán, Trường Đại học Y Dược Cần Thơ, số 179 Nguyễn Văn Cừ, P. An Khánh, Q. Ninh Kiều, thành phố Cần Thơ.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Chuyển khoản:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tên Tài khoản: Trường ĐHYD Cần Thơ, Số TK: 0111000115668, tại ngân hàng Vietcombank chi nhánh Cần Thơ.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Thời gian: Áp dụng từ ngày 01\u002F02\u002F2023.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">* Phí gửi bài không được hoàn trả khi bài viết bị từ chối hoặc tác giả xin rút bài viết.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Quy trình phản biện bài báo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ thực hiện quy trình phản biện kín hai chiều nghiêm ngặt. Danh tính của những người phản biện không được tiết lộ cho các tác giả và ngược lại. Quy trình thẩm định bài báo đăng gồm các bước sau:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tiếp nhận bản thảo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tác giả liên hệ gửi bản thảo đến Tạp chí qua hệ thống trực tuyến tại website: https:\u002F\u002Ftapchi.ctump.edu.vn. Hướng dẫn về cách đăng ký, gửi bài và chuẩn bị bản thảo được cung cấp trên website của Tạp chí.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Sàng lọc sơ bộ\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Sau khi Tòa soạn nhận được bài báo của tác giả, Ban Thư ký sẽ tiến hành kiểm tra sơ bộ bài báo (các yêu cầu về nội dung và hình thức). Những bài báo không đúng quy cách hoặc có nội dung không phù hợp hoặc vi phạm bản quyền sẽ bị từ chối (Ban Thư ký thông báo phản hồi đến tác giả trong vòng 1 tuần). Những bài báo đủ điều kiện, được Ban Thư ký tòa soạn chuyển đến Ban Biên tập có cùng chuyên môn với nội dung bài báo để đề xuất người phản biện. Thời gian kể từ khi Ban Biên tập nhận bài báo đến khi đề xuất người phản biện bài báo chậm nhất là 5 ngày.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Vòng phản biện\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Ban Thư ký gửi bài và yêu cầu phản biện đến 02 phản biện độc lập.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Các phản biện gởi nhận xét cho Ban Thư ký. Thời gian từ khi gửi bài cho phản biện đến khi nhận ý kiến của phản biện tối đa là 20 ngày.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Xử ký kết quả phản biện\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Nếu ý kiến đồng ý cho đăng và không cần chỉnh sửa, Ban Thư ký tiếp tục đăng bài theo qui trình.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Nếu ý kiến đồng ý đăng và cần chỉnh sửa, Ban Thư ký sẽ thông tin đến tác giả chỉnh sửa theo yêu cầu của người phản biện. Thời gian chỉnh sửa và gửi lại kéo dài không quá 2 tuần, từ khi tác giả bài báo nhận được thông tin (Quá trình này có thể lặp lại tối đa 2 lần\u002F1 bài báo). Khi có sự thống nhất, đồng ý của người phản biện; bài báo được tiếp tục đăng theo qui trình.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">3. Những bài báo có chất lượng không đạt yêu cầu, cả 2 phản biện không đồng ý cho đăng sẽ bị Tòa soạn từ chối đăng.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Xuất bản\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Ban Thư ký tổng hợp các bản thảo đã được tác giả hoàn thiện sau thẩm định trình Ban Biên tập xem xét, Tổng Biên tập phê duyệt, quyết định bài đăng theo các tiêu chí: sự phù hợp nội dung với tôn chỉ và mục đích, thể loại bài viết (ưu tiên các bài có bài có nghiên cứu chuyên sâu, hàm lượng khoa học cao), đóng góp mới bài báo, bài báo được ưu tiên đăng trong số gần nhất của Tạp chí theo thứ tự: tính thời sự, chất lượng bài báo và thời gian gửi bài.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Ban Biên tập và Ban Thư ký biên tập bản thảo, chế bản, đọc rà soát lỗi. Thời gian hoàn thành từ 10-15 ngày.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">3. Ban Thư ký có trách nhiệm thông báo cho tác giả bài báo (bằng e-mail) về tình hình phê duyệt bài báo, thời gian, số kỳ, tập xuất bản bài báo theo qui định.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">4. 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The main objectives of the journal include: providing an intellectual platform for Vietnamese and international scholars; promoting interdisciplinary studies in social sciences and humanities; becoming the leading journal in social sciences and humanities in Vietnam; being indexed by worldwide databases and having academic recognition internationally in the near future.\\nThe journal is currently indexed by Google Scholar, WorldCat, Open Archives, Cosmos Impact Factor, Advanced Sciences Index, Scientific Indexing Services, CrossRef, EBSCO Information Services and Vietnam National University’s digital archive.\\n\"},{\"attributes\":{\"bold\":true},\"insert\":\"Journal of Social Sciences and Humanities-Vietnam\"},{\"insert\":\"\\n\"},{\"attributes\":{\"bold\":true},\"insert\":\"ISSN 2354-1172, email: tapchikhxhnv@gmail.com, tckhxhnv@vnu.edu.vn\"},{\"insert\":\"\\n\"}]}","{\"ops\":[{\"insert\":\"Được thành lập ngày 31\u002F8\u002F2015 (giấy phép hoạt động số 155\u002FGP-BVHTT ngày 11 tháng 5 năm 2015 của Bộ Thông tin và Truyền thông, mã số tiêu chuẩn quốc tế ISSN 2354-1172), Tạp chí Khoa học Xã hội và Nhân văn (Journal of Social Sciences and Humanities) là ấn phẩm khoa học chính thức, duy nhất của Trường Đại học Khoa học Xã hội và Nhân văn, ĐHQG Hà Nội, phát triển và kế thừa Chuyên san Khoa học Xã hội và Nhân văn, Tạp chí Khoa học, ĐHQG Hà Nội.\\nTạp chí xuất bản định kỳ (04 số tiếng Việt\u002Fnăm và 02 số tiếng Anh\u002Fnăm), có nhiệm vụ \"},{\"attributes\":{\"italic\":true},\"insert\":\"công bố, giới thiệu các công trình nghiên cứu khoa học khoa học xã hội và nhân văn của các tác giả là các nhà khoa học trong và ngoài nước, phục vụ giảng dạy, học tập và nghiên cứu khoa học\"},{\"insert\":\". 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Tạp chí công bố các công trình nghiên cứu liên quan đến mô hình bệnh tật, các phương pháp chẩn đoán, điều trị, dự phòng và phục hồi chức năng các bệnh thuộc chuyên ngành da liễu. Ngoài ra, tạp chí còn đăng tải các bài tổng quan, cập nhật thông tin, kiến thức, hướng dẫn chẩn đoán, điều trị trong chuyên ngành da liễu trong nước và quốc tế; đăng tải các bài ca lâm sàng đặc biệt trong chuyên ngành da liễu.\\nTạp chí Da liễu học Việt Nam được biết tới là một tạp chí chuyên ngành có uy tín trong lĩnh vực da liễu. Các bài báo về nghiên cứu khoa học đăng trong Tạp chí được bình duyệt một cách nghiêm ngặt bởi ít nhất 2 chuyên gia. Hội đồng biên tập tạp chí bao gồm các nhà khoa học có uy tín (Giáo sư, Phó Giáo sư, Tiến sĩ, Bác sĩ…) trong chuyên ngành da liễu nhằm đảm bảo chất lượng và tính khách quan, khoa học cho các bài viết đăng trên Tạp chí.\\n\"}]}",{"EN":556,"VI":557},"Vietnamese Journal of Dermatology and Venereology","Tạp chí Da liễu học Việt Nam","Admin Import",[],[],[],"https:\u002F\u002Fvjdv.vn\u002Findex.php\u002Fvjdv","\u002Fapi\u002Fpublic\u002Ffile\u002Fpublisher\u002F6ec01bd0-15c0-469a-86ac-41339076ae0a\u002F3cbc81720e58429dc7b1c4d7ab1935ca.jpg",{"impactFactor":36,"impactFactorByYear":565,"i10Index":36,"i10IndexLast5Year":36,"totalPublication":566,"totalPublicationByYear":567,"totalCitation":116,"totalCitationByYear":570,"totalCitationPerPublication":109,"totalCitationPerPublicationByYear":571,"hindexLast5Year":115,"hindex":115},{"2023":38,"2024":230},182,{"2022":568,"2023":45,"2024":569},69,56,{"2022":52,"2023":115},{"2022":40,"2023":229},{"id":573,"createTime":574,"updateTime":575,"relativeEntities":576,"slug":577,"properties":578,"entityType":24,"verifyStatus":25,"verifyTime":26,"verifyNote":27,"syncStatus":28,"languages":587,"translateLanguages":26,"viewCount":283,"subjectFields":588,"manageAffiliations":589,"indexDatabases":647,"url":648,"thumbnailPath":649,"statistic":650,"gsStatistic":26,"type":26,"analyzePriority":26},"19221551-7519-47ff-a892-331d1139c64b","2023-09-12T07:03:05.744+00:00","2026-01-24T20:54:40.144+00:00",[],"T%E1%BA%A1p-ch%C3%AD-Khoa-h%E1%BB%8Dc-S%E1%BB%A9c-kho%E1%BA%BB-%C4%90%E1%BA%A1i-h%E1%BB%8Dc-Qu%E1%BB%91c-gia-Th%C3%A0nh-ph%E1%BB%91-H%E1%BB%93-Ch%C3%AD-Minh",{"country":579,"issn":580,"introduce":582,"title":584},{"VOID":15},{"VOID":581},"27349446",{"EN":583},"{\"ops\":[{\"attributes\":{\"bold\":true},\"insert\":\"1. History\"},{\"attributes\":{\"align\":\"justify\"},\"insert\":\"\\n\"},{\"attributes\":{\"bold\":true},\"insert\":\"Science and Technology Development Journal\"},{\"insert\":\" (STDJ) (ISSN 2734-9446), Vietnam National University - Ho Chi Minh City (VNU-HCM) was established in 1997. And the first issue was published in January 1998 with ISSN 1859-0128. Since then, STDJ has become the most important scientific forum of scientists from VNU-HCM as well as other universities. The magazine has undergone 20 years of development and has become a bridge for scientific exchanges, as well as enriching reference materials for the faculty, doctoral students, students of VNU-HCM in particular and other universities, institutes...\"},{\"attributes\":{\"align\":\"justify\"},\"insert\":\"\\n\"},{\"insert\":\"Science and Technology Development Journal - Health Sciences (STDJ-HS) is a subjournal of Science and Technology Development Journal since 2020.\"},{\"attributes\":{\"align\":\"justify\"},\"insert\":\"\\n\"},{\"insert\":\" \"},{\"attributes\":{\"align\":\"justify\"},\"insert\":\"\\n\"},{\"attributes\":{\"bold\":true},\"insert\":\"2. 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Science Publishing",[],[],[],{"meta":673,"data":675},{"total":674},"58",[676,770,833,927,996,1094,1203,1284,1356,1419],{"id":677,"createTime":678,"updateTime":678,"relativeEntities":679,"slug":680,"properties":681,"entityType":695,"verifyStatus":28,"verifyTime":678,"verifyNote":696,"syncStatus":28,"languages":697,"translateLanguages":26,"viewCount":36,"primaryUrl":698,"fullTextUrl":26,"authors":699,"publicationType":747,"publisherRelationship":748,"citationCount":763,"citationInfo":764,"publishDate":766,"publishYear":767,"citationAnalyzeStatus":28,"lastCitationAnalyze":26,"indexDatabases":26,"openAccess":26,"references":768,"isForceReanalyzing":769},"a2d42f96-55e8-4b2c-ae68-48063903e8f5","2024-08-30T09:56:46.829+00:00",[],"Jack-bean-urease-EC-3-5-1-5-V-On-the-mechanism-of-action-of-urease-on-urea-formamide-acetamide-i-N-i-methylurea-and-related-compounds",{"mag":682,"keywords":684,"openalex":685,"abstract":687,"title":689,"pm":691,"doi":693},{"VOID":683},"2103875315",{},{"VOID":686},"W2103875315",{"EN":688},"\u003Cjats:p> Acetamide and N-methylurea have been shown for the first time to be substrates for jack bean urease. In the enzymatic hydrolysis of urea, formamide, acetamide, and N-methylurea at pH 7.0 and 38 °C, k\u003Cjats:sub>cat\u003C\u002Fjats:sub> has the values 5870, 85, 0.55, and 0.075 s\u003Cjats:sup>−1\u003C\u002Fjats:sup>, respectively. The urease-catalyzed hydrolysis of all these substrates involves the active-site nickel ion(s). Enzymatic hydrolysis of the following compounds could not be detected: phenyl formate, p-nitroformanilide, trifluoroacetamide, p-nitrophenyl carbamate, thiourea, and O-methylisouronium ion. In the enzymatic hydrolysis of urea, the pH dependence of k\u003Cjats:sub>cat\u003C\u002Fjats:sub> between pH 3.4 and 7.8 indicates that at least two prototropic forms are active. Enzymatic hydrolysis of urea in the presence of methanol gave no detectable methyl carbamate. A mechanism of action for urease is proposed which involves initially an O-bonded complex between urea and an active-site Ni\u003Cjats:sup>2+\u003C\u002Fjats:sup> ion and subsequently an O-bonded carbamato–enzyme intermediate. \u003C\u002Fjats:p>",{"EN":690},"Jack bean urease (EC 3.5.1.5). V. On the mechanism of action of urease on urea, formamide, acetamide, \u003Ci>N\u003C\u002Fi>-methylurea, and related compounds",{"VOID":692},"6788353",{"VOID":694},"10.1139\u002Fo80-181","PUBLICATION","Author affiliation is blank",[102],"http:\u002F\u002Fwww.nrcresearchpress.com\u002Fdoi\u002F10.1139\u002Fo80-181",[700,709,720,729,738],{"id":701,"sortIndex":115,"researcher":26,"roles":702,"affiliations":703,"properties":704},"85af638c-8dd9-4fd2-9dc6-13c56840c88a",[],[],{"openalex":705,"title":707},{"VOID":706},"A5012043340",{"EN":708},"Peter W. Riddles",{"id":710,"sortIndex":36,"researcher":26,"roles":711,"affiliations":712,"properties":713},"2438a81f-291e-4550-bcd7-8d428e8bb2f0",[],[],{"openalex":714,"orcid":716,"title":718},{"VOID":715},"A5011359890",{"VOID":717},"https:\u002F\u002Forcid.org\u002F0000-0002-5958-6945",{"EN":719},"Nicholas E. Dixon",{"id":721,"sortIndex":114,"researcher":26,"roles":722,"affiliations":723,"properties":724},"901e2ef9-f4a9-40e9-a3e4-4f73e6583118",[],[],{"openalex":725,"title":727},{"VOID":726},"A5069933660",{"EN":728},"Carlo Gazzola",{"id":730,"sortIndex":111,"researcher":26,"roles":731,"affiliations":732,"properties":733},"ed1ea2a4-7696-4278-b6b6-d5bb27966625",[],[],{"openalex":734,"title":736},{"VOID":735},"A5026933642",{"EN":737},"Burt Zerner",{"id":739,"sortIndex":59,"researcher":26,"roles":740,"affiliations":741,"properties":742},"bc0fd6bb-d47e-471c-9b25-5c7c910e4198",[],[],{"openalex":743,"title":745},{"VOID":744},"A5013150962",{"EN":746},"Robert L. Blakeley","ARTICLE",{"url":26,"publisher":749,"properties":757},{"id":659,"createTime":660,"updateTime":661,"relativeEntities":750,"slug":663,"properties":751,"entityType":24,"verifyStatus":28,"verifyTime":26,"verifyNote":26,"syncStatus":28,"languages":26,"translateLanguages":26,"viewCount":36,"subjectFields":754,"manageAffiliations":755,"indexDatabases":756,"url":26,"thumbnailPath":26,"statistic":26,"gsStatistic":26,"type":26,"analyzePriority":26},[],{"issn":752,"title":753},{"VOID":666},{"EN":668},[],[],[],{"volume":758,"pages":759,"issue":761},{"VOID":674},{"VOID":760},"1335-1344",{"VOID":762},"12",213,{"total":763,"publishYear":26,"statisticByYear":765},{"2012":135,"2013":158,"2014":111,"2015":111,"2016":114,"2017":111,"2018":158,"2019":50,"2020":52,"2021":50,"2022":52,"2023":59,"2024":158},"1980-12-01",1980,[],false,{"id":771,"createTime":772,"updateTime":772,"relativeEntities":773,"slug":774,"properties":775,"entityType":695,"verifyStatus":28,"verifyTime":772,"verifyNote":696,"syncStatus":28,"languages":789,"translateLanguages":26,"viewCount":36,"primaryUrl":790,"fullTextUrl":26,"authors":791,"publicationType":747,"publisherRelationship":812,"citationCount":629,"citationInfo":828,"publishDate":830,"publishYear":831,"citationAnalyzeStatus":28,"lastCitationAnalyze":26,"indexDatabases":26,"openAccess":26,"references":832,"isForceReanalyzing":769},"8bab47bf-0a70-4610-b154-720c01202d86","2024-09-20T14:22:31.126+00:00",[],"A-Cytokinin-Oxidase-in-i-Zea-mays-i-",{"mag":776,"keywords":778,"openalex":779,"abstract":781,"title":783,"pm":785,"doi":787},{"VOID":777},"1992372626",{},{"VOID":780},"W1992372626",{"EN":782},"\u003Cjats:p> An enzyme activity that catalyzes conversion of N\u003Cjats:sup>6\u003C\u002Fjats:sup>-(Δ\u003Cjats:sup>2\u003C\u002Fjats:sup>-isopentenyl)adenosine (i\u003Cjats:sup>6\u003C\u002Fjats:sup>Ado) to adenosine was detected in cultured tobacco tissue by Pačes et al. (1971) (Plant Physiol. 48, 775–778). Purification and characteristics of this enzyme in corn kernels have been studied. Only the naturally occurring cytokinins i\u003Cjats:sup>6\u003C\u002Fjats:sup>Ado and ribosylzeatin serve as substrates; the nucleoside or free base works equally as well. The reaction requires oxygen. An unstable intermediate appears to be the primary reaction product. This product decomposes to adenosine.The enzyme activity is greatest at pH 5–7. It is independent of added magnesium. The molecular weight of the enzyme is about 88 000. The activity of the enzyme in corn kernels increases from the time of pollination to about 21 days.A nucleoside hydrolase is isolated with i\u003Cjats:sup>6\u003C\u002Fjats:sup>Ado oxidase. The activities can be partially separated by G-150 gel filtration. The hydrolase is less stable than the i\u003Cjats:sup>6\u003C\u002Fjats:sup>Ado oxidase and frozen preparations lose their activity after 2 months, whereas i\u003Cjats:sup>6\u003C\u002Fjats:sup>Ado oxidase is stable under these conditions. \u003C\u002Fjats:p>",{"EN":784},"A Cytokinin Oxidase in \u003Ci>Zea mays\u003C\u002Fi>",{"VOID":786},"4214594",{"VOID":788},"10.1139\u002Fo74-112",[102],"http:\u002F\u002Fwww.nrcresearchpress.com\u002Fdoi\u002F10.1139\u002Fo74-112",[792,803],{"id":793,"sortIndex":115,"researcher":26,"roles":794,"affiliations":795,"properties":796},"094b361a-a469-4d29-98ce-d43a34bdf8a6",[],[],{"openalex":797,"orcid":799,"title":801},{"VOID":798},"A5006924147",{"VOID":800},"https:\u002F\u002Forcid.org\u002F0000-0001-8587-8696",{"EN":802},"Ross H. Hall",{"id":804,"sortIndex":36,"researcher":26,"roles":805,"affiliations":806,"properties":807},"e13b1441-f13a-4192-956b-e04092bd3ea4",[],[],{"openalex":808,"title":810},{"VOID":809},"A5051140016",{"EN":811},"Ciara Whitty",{"url":26,"publisher":813,"properties":821},{"id":659,"createTime":660,"updateTime":661,"relativeEntities":814,"slug":663,"properties":815,"entityType":24,"verifyStatus":28,"verifyTime":26,"verifyNote":26,"syncStatus":28,"languages":26,"translateLanguages":26,"viewCount":36,"subjectFields":818,"manageAffiliations":819,"indexDatabases":820,"url":26,"thumbnailPath":26,"statistic":26,"gsStatistic":26,"type":26,"analyzePriority":26},[],{"issn":816,"title":817},{"VOID":666},{"EN":668},[],[],[],{"volume":822,"pages":824,"issue":826},{"VOID":823},"52",{"VOID":825},"789-799",{"VOID":827},"9",{"total":629,"publishYear":26,"statisticByYear":829},{"2012":111,"2013":111,"2014":59,"2015":59,"2016":59,"2017":114,"2018":114,"2019":114,"2020":115,"2021":59,"2022":114,"2023":115},"1974-09-01",1974,[],{"id":834,"createTime":835,"updateTime":835,"relativeEntities":836,"slug":837,"properties":838,"entityType":695,"verifyStatus":28,"verifyTime":852,"verifyNote":696,"syncStatus":28,"languages":853,"translateLanguages":26,"viewCount":36,"primaryUrl":854,"fullTextUrl":26,"authors":855,"publicationType":747,"publisherRelationship":905,"citationCount":921,"citationInfo":922,"publishDate":924,"publishYear":925,"citationAnalyzeStatus":28,"lastCitationAnalyze":26,"indexDatabases":26,"openAccess":26,"references":926,"isForceReanalyzing":769},"07d39325-323e-4d0b-b702-ae769d5b801a","2024-10-04T03:54:03.222+00:00",[],"Structural-determination-of-the-polysaccharide-antigens-of-i-Neisseria-meningitidis-i-serogroups-Y-W-135-and-BO",{"mag":839,"keywords":841,"openalex":842,"abstract":844,"title":846,"pm":848,"doi":850},{"VOID":840},"2053163557",{},{"VOID":843},"W2053163557",{"EN":845},"\u003Cjats:p> The purified high molecular weight serogoup Y meningococcal polysaccharide contains equimolar proportions of D-glucose and N-acetylneuraminic acid and is partially O-acetylated. Carbon-13 nuclear magnetic resonance (NMR) studies, together with other chemical data, have indicated that the polysaccharide is linked only at C-6 of the D-glucose and C-4 of the sialic acid residues, all the linkages being in the α-configuration. The \u003Cjats:sup>13\u003C\u002Fjats:sup>C NMR data also indicated that the Y polysaccharide is composed of an alternating sequence of these two different residues, and this was confirmed by its autohydrolysis where the major product was 4-O-α-D-glucopyranosyl-β-D-N-acetylneuraminic acid. The W-135 polysaccharide differs from that of Y only in the absence of O-acetylation and in the configuration of one hydroxyl group of the disaccharide repeating unit. In this case autohydrolysis yielded 4-O-α-D-galactopyranosyl-β-D-N-acetylneuraminic acid as the major product. Structural evidence indicates that the BO and Y polysaccharides are identical.Methanolysis of the Y polysaccharide yielded in addition to the methyl glycosides of glucose and sialic acid, a 9-O-acetyl derivative of the latter. This derivative was formed during the re-N-acetylation process and its formation was mainly due to the presence of sodium ions in the original polysaccharide. \u003C\u002Fjats:p>",{"EN":847},"Structural determination of the polysaccharide antigens of \u003Ci>Neisseria meningitidis\u003C\u002Fi> serogroups Y, W-135, and BO",{"VOID":849},"814976",{"VOID":851},"10.1139\u002Fo76-001","2024-10-04T03:54:03.221+00:00",[102],"http:\u002F\u002Fwww.nrcresearchpress.com\u002Fdoi\u002F10.1139\u002Fo76-001",[856,865,874,883,894],{"id":857,"sortIndex":36,"researcher":26,"roles":858,"affiliations":859,"properties":860},"5017da1c-ba52-4544-8153-d97cd6f7109b",[],[],{"openalex":861,"title":863},{"VOID":862},"A5059617699",{"EN":864},"Apurba K. Bhattacharjee",{"id":866,"sortIndex":115,"researcher":26,"roles":867,"affiliations":868,"properties":869},"1edec816-cc01-4154-8658-456cd3a440b2",[],[],{"openalex":870,"title":872},{"VOID":871},"A5031462808",{"EN":873},"Harold J. Jennings",{"id":875,"sortIndex":114,"researcher":26,"roles":876,"affiliations":877,"properties":878},"91321f09-9d44-4954-b559-9c8ad4246a2b",[],[],{"openalex":879,"title":881},{"VOID":880},"A5066114097",{"EN":882},"C. P. Kenny",{"id":884,"sortIndex":111,"researcher":26,"roles":885,"affiliations":886,"properties":887},"05e7f796-8be7-49c9-a793-15e256a7c652",[],[],{"openalex":888,"orcid":890,"title":892},{"VOID":889},"A5103171807",{"VOID":891},"https:\u002F\u002Forcid.org\u002F0000-0001-5269-1710",{"EN":893},"Ian C. P. Smith",{"id":895,"sortIndex":59,"researcher":26,"roles":896,"affiliations":897,"properties":898},"df853ca2-3e08-4163-b60e-bfb6b741a536",[],[],{"openalex":899,"orcid":901,"title":903},{"VOID":900},"A5021206154",{"VOID":902},"https:\u002F\u002Forcid.org\u002F0000-0001-7826-5939",{"EN":904},"Andrew Martin",{"url":26,"publisher":906,"properties":914},{"id":659,"createTime":660,"updateTime":661,"relativeEntities":907,"slug":663,"properties":908,"entityType":24,"verifyStatus":28,"verifyTime":26,"verifyNote":26,"syncStatus":28,"languages":26,"translateLanguages":26,"viewCount":36,"subjectFields":911,"manageAffiliations":912,"indexDatabases":913,"url":26,"thumbnailPath":26,"statistic":26,"gsStatistic":26,"type":26,"analyzePriority":26},[],{"issn":909,"title":910},{"VOID":666},{"EN":668},[],[],[],{"volume":915,"pages":917,"issue":919},{"VOID":916},"54",{"VOID":918},"1-8",{"VOID":920},"1",145,{"total":921,"publishYear":26,"statisticByYear":923},{"2012":114,"2013":59,"2014":135,"2015":114,"2017":114,"2018":111,"2020":114,"2021":114,"2022":115,"2023":115,"2024":115},"1976-01-01",1976,[],{"id":928,"createTime":929,"updateTime":929,"relativeEntities":930,"slug":931,"properties":932,"entityType":695,"verifyStatus":28,"verifyTime":929,"verifyNote":696,"syncStatus":28,"languages":946,"translateLanguages":26,"viewCount":36,"primaryUrl":947,"fullTextUrl":26,"authors":948,"publicationType":747,"publisherRelationship":976,"citationCount":991,"citationInfo":992,"publishDate":994,"publishYear":831,"citationAnalyzeStatus":28,"lastCitationAnalyze":26,"indexDatabases":26,"openAccess":26,"references":995,"isForceReanalyzing":769},"ed2c6683-6a38-4082-94a7-fd9e8710efc3","2024-12-10T16:15:57.510+00:00",[],"Identification-and-Distribution-of-Tryptamine-in-the-Rat",{"mag":933,"keywords":935,"openalex":936,"abstract":938,"title":940,"pm":942,"doi":944},{"VOID":934},"2009506204",{},{"VOID":937},"W2009506204",{"EN":939},"\u003Cjats:p> A procedure for the quantitative measurement of tryptamine in mammalian tissues is described. The amine is isolated by ion-exchange chromatography, converted to its dansyl derivative, further purified by thin-layer chromatography, and quantitated by the mass-spectrometric integrated ion current technique using an isotopically labelled internal standard.The concentrations of tryptamine in some tissues of male Wistar rats were (ng\u002Fg ± S.D.): brain 0.50 ± 0.07, heart 0.62 ± 0.10, kidney 8.04 ± 2.10, liver 0.73 ± 0.07, lung 0.54 ± 0.18, and spleen 0.43 ± 0.14. In the brain, the hypothalamus contained 0.94 ± 0.22, the cerebellum 0.27 ± 0.02, the stem 0.24 ± 0.06, the caudate nucleus 2.93 ± 1.14, and the \"rest\" 0.32 ± 0.05 ng\u002Fg (mean ± mean deviation). \u003C\u002Fjats:p>",{"EN":941},"Identification and Distribution of Tryptamine in the Rat",{"VOID":943},"4844280",{"VOID":945},"10.1139\u002Fo74-068",[102],"http:\u002F\u002Fwww.nrcresearchpress.com\u002Fdoi\u002F10.1139\u002Fo74-068",[949,958,967],{"id":950,"sortIndex":115,"researcher":26,"roles":951,"affiliations":952,"properties":953},"f03b7827-df25-4412-8c35-50c225074fb4",[],[],{"openalex":954,"title":956},{"VOID":955},"A5013705148",{"EN":957},"D. A. Burden",{"id":959,"sortIndex":114,"researcher":26,"roles":960,"affiliations":961,"properties":962},"37048253-fbd3-4553-816a-58bad67d8905",[],[],{"openalex":963,"title":965},{"VOID":964},"A5111803542",{"EN":966},"A. A. Boulton",{"id":968,"sortIndex":36,"researcher":26,"roles":969,"affiliations":970,"properties":971},"dda49269-6cca-42a1-ae2a-74880ba7b515",[],[],{"openalex":972,"title":974},{"VOID":973},"A5114251977",{"EN":975},"S. R. Philips",{"url":26,"publisher":977,"properties":985},{"id":659,"createTime":660,"updateTime":661,"relativeEntities":978,"slug":663,"properties":979,"entityType":24,"verifyStatus":28,"verifyTime":26,"verifyNote":26,"syncStatus":28,"languages":26,"translateLanguages":26,"viewCount":36,"subjectFields":982,"manageAffiliations":983,"indexDatabases":984,"url":26,"thumbnailPath":26,"statistic":26,"gsStatistic":26,"type":26,"analyzePriority":26},[],{"issn":980,"title":981},{"VOID":666},{"EN":668},[],[],[],{"volume":986,"pages":987,"issue":989},{"VOID":823},{"VOID":988},"447-451",{"VOID":990},"6",135,{"total":991,"publishYear":26,"statisticByYear":993},{"2014":115,"2016":114,"2021":115},"1974-06-01",[],{"id":997,"createTime":998,"updateTime":998,"relativeEntities":999,"slug":1000,"properties":1001,"entityType":695,"verifyStatus":28,"verifyTime":998,"verifyNote":696,"syncStatus":28,"languages":1015,"translateLanguages":26,"viewCount":36,"primaryUrl":1016,"fullTextUrl":26,"authors":1017,"publicationType":747,"publisherRelationship":1076,"citationCount":1090,"citationInfo":1091,"publishDate":766,"publishYear":767,"citationAnalyzeStatus":28,"lastCitationAnalyze":26,"indexDatabases":26,"openAccess":26,"references":1093,"isForceReanalyzing":769},"56074a06-4b05-4961-99cf-5fc705777fb0","2024-09-30T13:24:09.573+00:00",[],"Jack-bean-urease-EC-3-5-1-5-IV-The-molecular-size-and-the-mechanism-of-inhibition-by-hydroxamic-acids-Spectrophotometric-titration-of-enzymes-with-reversible-inhibitors",{"mag":1002,"keywords":1004,"openalex":1005,"abstract":1007,"title":1009,"pm":1011,"doi":1013},{"VOID":1003},"2030029696",{},{"VOID":1006},"W2030029696",{"EN":1008},"\u003Cjats:p> Kinetic, spectral, and other studies establish that hydroxamic acids bind reversibly to active-site nickel ion in jack bean urease. Equilibrium ultracentrifugation studies establish that the molecular weight of native urease is 590 000 ± 30 000 while that of the subunit formed in 6 M guanidinium chloride in the presence of β-mercaptoethanol is ~95 000. Essentially the same subunit molecular weight (~93 000) is found by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, subsequent to denaturation in a guanidinium chloride – β-mercaptoethanol system at various temperatures. Coupled with an equivalent weight of 96 600 for binding of the inhibitors acetohydroxamic acid and phosphoramidate, these results establish securely that urease is a hexamer with one active site per 96 600-dalton subunit. Consistent values for the equivalent weight are obtained by a routine spectrophotometric titration of the active site of freshly prepared urease with trans-cinnamoylhydroxamic acid. General equations are derived which describe spectrophotometric titrations of binding sites of any enzyme with a reversible inhibitor. These equations allow the evaluation of the difference spectrum of the protein–inhibitor complex even when the binding sites cannot readily be saturated with the inhibitor or vice versa. \u003C\u002Fjats:p>",{"EN":1010},"Jack bean urease (EC 3.5.1.5). IV. The molecular size and the mechanism of inhibition by hydroxamic acids. Spectrophotometric titration of enzymes with reversible inhibitors",{"VOID":1012},"7248834",{"VOID":1014},"10.1139\u002Fo80-180",[102],"http:\u002F\u002Fwww.nrcresearchpress.com\u002Fdoi\u002F10.1139\u002Fo80-180",[1018,1025,1034,1041,1049,1058,1069],{"id":1019,"sortIndex":135,"researcher":26,"roles":1020,"affiliations":1021,"properties":1022},"82f7202a-30a2-47b9-aadc-769949a9cee3",[],[],{"openalex":1023,"title":1024},{"VOID":735},{"EN":737},{"id":1026,"sortIndex":115,"researcher":26,"roles":1027,"affiliations":1028,"properties":1029},"93b62fa5-7bda-448f-8006-7775294ec0e3",[],[],{"openalex":1030,"title":1032},{"VOID":1031},"A5080277658",{"EN":1033},"John A. 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Using this reagent, a more sensitive assay for peptidase activity has been developed, and its use in column fractionation of peptidase activity is described.The ϵ values for peptides, obtained with the modified reagent, are compared to those obtained with the conventional ninhydrin–hydrindantin reagent. The formation of Ruhmann's Purple by the modified reagent is inhibited by Tris buffer. No inhibition occurs with the ninhydrin–hydrandantin reagent. The absorption spectra of the two reaction mixtures indicate that Tris reacts in a different manner with the two reagents.\u003C\u002Fjats:p>",{"EN":1108},"A MODIFIED YEMM AND COCKING NINHYDRIN REAGENT FOR PEPTIDASE ASSAY",{"VOID":1110},"10.1139\u002Fo64-010",[102],"http:\u002F\u002Fwww.nrcresearchpress.com\u002Fdoi\u002F10.1139\u002Fo64-010",[1114,1123],{"id":1115,"sortIndex":115,"researcher":26,"roles":1116,"affiliations":1117,"properties":1118},"fb624639-3e1c-41b2-b235-2e30b2c477a5",[],[],{"openalex":1119,"title":1121},{"VOID":1120},"A5075925772",{"EN":1122},"B. Tattrie",{"id":1124,"sortIndex":36,"researcher":26,"roles":1125,"affiliations":1126,"properties":1127},"0134b0fe-2a23-4a8a-a85a-7ce6e53713cc",[],[],{"openalex":1128,"title":1130},{"VOID":1129},"A5069202838",{"EN":1131},"A. T. Matheson",{"url":26,"publisher":1133,"properties":1141},{"id":659,"createTime":660,"updateTime":661,"relativeEntities":1134,"slug":663,"properties":1135,"entityType":24,"verifyStatus":28,"verifyTime":26,"verifyNote":26,"syncStatus":28,"languages":26,"translateLanguages":26,"viewCount":36,"subjectFields":1138,"manageAffiliations":1139,"indexDatabases":1140,"url":26,"thumbnailPath":26,"statistic":26,"gsStatistic":26,"type":26,"analyzePriority":26},[],{"issn":1136,"title":1137},{"VOID":666},{"EN":668},[],[],[],{"volume":1142,"pages":1144,"issue":1146},{"VOID":1143},"42",{"VOID":1145},"95-103",{"VOID":920},{"total":248,"publishYear":26,"statisticByYear":1148},{"2013":115},"1964-01-01",1964,[1152,1156,1160,1164,1168,1172,1176,1179,1183,1187,1191,1195,1199],{"id":26,"text":1153,"url":26,"identifiers":1154},"'I' AKTZ, 1950, J. Biol. Chem., 184, 197, 10.1016\u002FS0021-9258(19)51139-5",{"doi":1155},"10.1016\u002FS0021-9258(19)51139-5",{"id":26,"text":1157,"url":26,"identifiers":1158},"'T, 1963, Can. J. Biochein. Physiol., 41, 1741, 10.1139\u002Fy63-199",{"doi":1159},"10.1139\u002Fy63-199",{"id":26,"text":1161,"url":26,"identifiers":1162},"YASARI J ., 1956, Biol. Chein., 220, 683, 10.1016\u002FS0021-9258(18)65293-7",{"doi":1163},"10.1016\u002FS0021-9258(18)65293-7",{"id":26,"text":1165,"url":26,"identifiers":1166},"COCKING., 1955, Analyst, 80, 209, 10.1039\u002Fan9558000209",{"doi":1167},"10.1039\u002Fan9558000209",{"id":26,"text":1169,"url":26,"identifiers":1170},"IATHESOX E., 1961, Can. J. Biochein. Physiol., 39, 417, 10.1139\u002Fo61-040",{"doi":1171},"10.1139\u002Fo61-040",{"id":26,"text":1173,"url":26,"identifiers":1174},"ROSES, 1957, Arch. Biochein. Biophys., 67, 10, 10.1016\u002F0003-9861(57)90241-2",{"doi":1175},"10.1016\u002F0003-9861(57)90241-2",{"id":26,"text":1177,"url":26,"identifiers":1178},"KE IT., 1954, STEIN. J. Biol. Chein., 211, 907",{},{"id":26,"text":1180,"url":26,"identifiers":1181},"COTSELL G. H., 1955, Can. J. Biochen. Physiol., 33, 416, 10.1139\u002Fo55-055",{"doi":1182},"10.1139\u002Fo55-055",{"id":26,"text":1184,"url":26,"identifiers":1185},"RE W. H., 1948, STEIN. J. Biol. Chem., 176, 367, 10.1016\u002FS0021-9258(18)51034-6",{"doi":1186},"10.1016\u002FS0021-9258(18)51034-6",{"id":26,"text":1188,"url":26,"identifiers":1189},"TROLL R. K., 1953, CANNAN. J. Biol. Chem., 200, 803, 10.1016\u002FS0021-9258(18)71428-2",{"doi":1190},"10.1016\u002FS0021-9258(18)71428-2",{"id":26,"text":1192,"url":26,"identifiers":1193},"DOWJIOST J ., 1952, FRUTON. J. Biol. Chern., 197, 271, 10.1016\u002FS0021-9258(18)55676-3",{"doi":1194},"10.1016\u002FS0021-9258(18)55676-3",{"id":26,"text":1196,"url":26,"identifiers":1197},"SAIDEL J ., 1957, Biol. Chein., 224, 445, 10.1016\u002FS0021-9258(18)65043-4",{"doi":1198},"10.1016\u002FS0021-9258(18)65043-4",{"id":26,"text":1200,"url":26,"identifiers":1201},"'I' C., 1958, J. Org. Chein., 23, 145, 10.1021\u002Fjo01095a641",{"doi":1202},"10.1021\u002Fjo01095a641",{"id":1204,"createTime":1205,"updateTime":1205,"relativeEntities":1206,"slug":1207,"properties":1208,"entityType":695,"verifyStatus":28,"verifyTime":1205,"verifyNote":696,"syncStatus":28,"languages":1222,"translateLanguages":26,"viewCount":36,"primaryUrl":1223,"fullTextUrl":26,"authors":1224,"publicationType":747,"publisherRelationship":1263,"citationCount":1278,"citationInfo":1279,"publishDate":1281,"publishYear":1282,"citationAnalyzeStatus":28,"lastCitationAnalyze":26,"indexDatabases":26,"openAccess":26,"references":1283,"isForceReanalyzing":769},"24d41d61-8b85-49a2-beeb-29f76ad29a5d","2024-11-25T15:49:59.343+00:00",[],"Purification-and-Properties-of-Rat-Liver-Nuclear-Protein-Kinases",{"mag":1209,"keywords":1211,"openalex":1212,"abstract":1214,"title":1216,"pm":1218,"doi":1220},{"VOID":1210},"2142898783",{},{"VOID":1213},"W2142898783",{"EN":1215},"\u003Cjats:p> Two protein kinases, designated NI and NII, have been isolated from rat liver nuclei. These enzymes have a similar pH optimum and phosphorylate phosvitin and casein more readily than histone. Both enzymes require magnesium for activity. In the absence of Mg\u003Cjats:sup>2+\u003C\u002Fjats:sup>, other divalent cations such as Ca\u003Cjats:sup>2+\u003C\u002Fjats:sup>, Co\u003Cjats:sup>2+\u003C\u002Fjats:sup>, and Mn\u003Cjats:sup>2+\u003C\u002Fjats:sup> can substitute partially for Mg\u003Cjats:sup>2+\u003C\u002Fjats:sup> when the reaction is catalyzed by NI. With NII, only Co\u003Cjats:sup>2+\u003C\u002Fjats:sup> showed any activity in the absence of Mg\u003Cjats:sup>2+\u003C\u002Fjats:sup>. Magnesium decreased the apparent K\u003Cjats:sub>m\u003C\u002Fjats:sub> for ATP of protein kinase NI without changing the V\u003Cjats:sub>max\u003C\u002Fjats:sub> of the reaction, and decreased the apparent K\u003Cjats:sub>m\u003C\u002Fjats:sub>'s for both ATP and casein, while increasing the V\u003Cjats:sub>max\u003C\u002Fjats:sub> of the reaction threefold with protein kinase NII. Both enzymes are stimulated about twofold by low concentrations (0.1–0.3 M) of NaCl, KCl, and sodium acetate, whereas higher concentrations (> 0.5 M) inhibit their activities. Both enzymes are inhibited by low concentrations of NaF (0.02 M) and (NH\u003Cjats:sub>4\u003C\u002Fjats:sub>)\u003Cjats:sub>2\u003C\u002Fjats:sub>SO\u003Cjats:sub>4\u003C\u002Fjats:sub> (0.1 M). NI and NII were found to have sedimentation coefficients of 3.6 S and 10.8 S, respectively. The nuclear protein kinases are not activated by cyclic AMP or cyclic GMP, and are not inhibited by the heat-stable cyclic AMP-dependent protein kinase inhibitor. \u003C\u002Fjats:p>",{"EN":1217},"Purification and Properties of Rat Liver Nuclear Protein Kinases",{"VOID":1219},"4345911",{"VOID":1221},"10.1139\u002Fo72-170",[102],"http:\u002F\u002Fwww.nrcresearchpress.com\u002Fdoi\u002F10.1139\u002Fo72-170",[1225,1234,1243,1254],{"id":1226,"sortIndex":59,"researcher":26,"roles":1227,"affiliations":1228,"properties":1229},"efde2883-e931-4351-b945-b95562e26d09",[],[],{"openalex":1230,"title":1232},{"VOID":1231},"A5112200476",{"EN":1233},"A. G. Gornall",{"id":1235,"sortIndex":115,"researcher":26,"roles":1236,"affiliations":1237,"properties":1238},"12061d66-9619-4dcd-aa31-4c896802e4f0",[],[],{"openalex":1239,"title":1241},{"VOID":1240},"A5110256118",{"EN":1242},"Peter F. Lue",{"id":1244,"sortIndex":114,"researcher":26,"roles":1245,"affiliations":1246,"properties":1247},"c6d641c6-788e-4551-b18a-f2325be1eb48",[],[],{"openalex":1248,"orcid":1250,"title":1252},{"VOID":1249},"A5011345433",{"VOID":1251},"https:\u002F\u002Forcid.org\u002F0000-0002-9908-0391",{"EN":1253},"Choong‐Chin Liew",{"id":1255,"sortIndex":36,"researcher":26,"roles":1256,"affiliations":1257,"properties":1258},"f6d6fca6-4d90-4e21-b8a8-544db23c2454",[],[],{"openalex":1259,"title":1261},{"VOID":1260},"A5073384511",{"EN":1262},"Paul Desjardins",{"url":26,"publisher":1264,"properties":1272},{"id":659,"createTime":660,"updateTime":661,"relativeEntities":1265,"slug":663,"properties":1266,"entityType":24,"verifyStatus":28,"verifyTime":26,"verifyNote":26,"syncStatus":28,"languages":26,"translateLanguages":26,"viewCount":36,"subjectFields":1269,"manageAffiliations":1270,"indexDatabases":1271,"url":26,"thumbnailPath":26,"statistic":26,"gsStatistic":26,"type":26,"analyzePriority":26},[],{"issn":1267,"title":1268},{"VOID":666},{"EN":668},[],[],[],{"volume":1273,"pages":1275,"issue":1277},{"VOID":1274},"50",{"VOID":1276},"1249-1259",{"VOID":762},112,{"total":1278,"publishYear":26,"statisticByYear":1280},{"2018":114,"2020":115,"2024":115},"1972-12-01",1972,[],{"id":1285,"createTime":1286,"updateTime":1286,"relativeEntities":1287,"slug":1288,"properties":1289,"entityType":695,"verifyStatus":28,"verifyTime":1286,"verifyNote":696,"syncStatus":28,"languages":1303,"translateLanguages":26,"viewCount":36,"primaryUrl":1304,"fullTextUrl":26,"authors":1305,"publicationType":747,"publisherRelationship":1335,"citationCount":1350,"citationInfo":1351,"publishDate":1353,"publishYear":1354,"citationAnalyzeStatus":28,"lastCitationAnalyze":26,"indexDatabases":26,"openAccess":26,"references":1355,"isForceReanalyzing":769},"3e415316-b6ea-4913-8a9a-62baef3d752e","2024-09-22T10:27:24.224+00:00",[],"Amino-acid-sequence-alignment-of-bacterial-and-mammalian-pancreatic-serine-proteases-based-on-topological-equivalences",{"mag":1290,"keywords":1292,"openalex":1293,"abstract":1295,"title":1297,"pm":1299,"doi":1301},{"VOID":1291},"2084164139",{},{"VOID":1294},"W2084164139",{"EN":1296},"\u003Cjats:p> The three-dimensional structures of the bacterial serine proteases SGPA, SGPB, and α-lytic protease have been compared with those of the pancreatic enzymes α-chymotrypsin and elastase. This comparison shows that ~60% (55–64%) of the α-carbon atom positions of the bacterial serine proteases are topologically equivalent to the α-carbon atom positions of the pancreatic enzymes. The corresponding value for a comparison of the bacterial enzymes among themselves is ~84%. The results of these topological comparisons have been used to deduce an experimentally sound sequence alignment for these several enzymes. This alignment shows that there is extensive tertiary structural homology among the bacterial and pancreatic enzymes without significant primary sequence identity (<21%). The acquisition of a zymogen function by the pancreatic enzymes is accompanied by two major changes to the bacterial enzymes' architecture: an insertion of 9 residues to increase the length of the N-terminal loop, and one of 12 residues to a loop near the activation salt bridge. In addition, in these two enzyme families, the methionine loop (residues 164–182) adopts very different conformations which are associated with their altered substrate specificities. \u003C\u002Fjats:p>",{"EN":1298},"Amino acid sequence alignment of bacterial and mammalian pancreatic serine proteases based on topological equivalences",{"VOID":1300},"96920",{"VOID":1302},"10.1139\u002Fo78-062",[102],"http:\u002F\u002Fwww.nrcresearchpress.com\u002Fdoi\u002F10.1139\u002Fo78-062",[1306,1315,1324],{"id":1307,"sortIndex":115,"researcher":26,"roles":1308,"affiliations":1309,"properties":1310},"3f051bfa-c60e-4dc6-ace1-af7df518e830",[],[],{"openalex":1311,"title":1313},{"VOID":1312},"A5032035309",{"EN":1314},"Louis T. J. Delbaere",{"id":1316,"sortIndex":114,"researcher":26,"roles":1317,"affiliations":1318,"properties":1319},"00a09a17-d25b-425d-abcb-4d0f9bd3e869",[],[],{"openalex":1320,"title":1322},{"VOID":1321},"A5105688985",{"EN":1323},"Gary D. Brayer",{"id":1325,"sortIndex":36,"researcher":26,"roles":1326,"affiliations":1327,"properties":1328},"d5078eef-806e-4ba3-89b1-1561e284f060",[],[],{"openalex":1329,"orcid":1331,"title":1333},{"VOID":1330},"A5062362734",{"VOID":1332},"https:\u002F\u002Forcid.org\u002F0000-0002-5978-4562",{"EN":1334},"Michael N.G. James",{"url":26,"publisher":1336,"properties":1344},{"id":659,"createTime":660,"updateTime":661,"relativeEntities":1337,"slug":663,"properties":1338,"entityType":24,"verifyStatus":28,"verifyTime":26,"verifyNote":26,"syncStatus":28,"languages":26,"translateLanguages":26,"viewCount":36,"subjectFields":1341,"manageAffiliations":1342,"indexDatabases":1343,"url":26,"thumbnailPath":26,"statistic":26,"gsStatistic":26,"type":26,"analyzePriority":26},[],{"issn":1339,"title":1340},{"VOID":666},{"EN":668},[],[],[],{"volume":1345,"pages":1347,"issue":1349},{"VOID":1346},"56",{"VOID":1348},"396-402",{"VOID":990},96,{"total":1350,"publishYear":26,"statisticByYear":1352},{"2013":162,"2016":115,"2019":115,"2021":115},"1978-06-01",1978,[],{"id":1357,"createTime":1358,"updateTime":1358,"relativeEntities":1359,"slug":1360,"properties":1361,"entityType":695,"verifyStatus":28,"verifyTime":1358,"verifyNote":696,"syncStatus":28,"languages":1375,"translateLanguages":26,"viewCount":36,"primaryUrl":1376,"fullTextUrl":26,"authors":1377,"publicationType":747,"publisherRelationship":1398,"citationCount":1413,"citationInfo":1414,"publishDate":1416,"publishYear":1417,"citationAnalyzeStatus":28,"lastCitationAnalyze":26,"indexDatabases":26,"openAccess":26,"references":1418,"isForceReanalyzing":769},"21a45069-8708-472a-a467-c038ffb0abfd","2024-09-19T18:32:54.858+00:00",[],"Evidence-for-albumin-Cu-II-amino-acid-ternary-complex",{"mag":1362,"keywords":1364,"openalex":1365,"abstract":1367,"title":1369,"pm":1371,"doi":1373},{"VOID":1363},"2048606424",{},{"VOID":1366},"W2048606424",{"EN":1368},"\u003Cjats:p> Commercially obtained pure human serum albumin (HSA) was shown to contain molecular aggregates and was significantly contaminated with Cu(II). A solution of commercial HSA was first passed through a Sephadex G-200 column to obtain pure monomeric HSA. The monomer of HSA was subsequently passed through Chelex-100 resin to free it from Cu(II). All Cu(II)-binding studies were conducted with monomeric and copper-free HSA. The first Cu(II)-binding site on HSA appears to be stronger than the second and the subsequent binding sites. Significant amounts of L-histidine and L-threonine were bound to HSA when Cu(II) was added in the form of Cu(II) – amino acid complexes. In the absence of Cu(II), free L-histidine or L-threonine do not bind to HSA at pH 7.4. It is concluded that, in the presence of either L-histidine or L-threonine, ternary complex formation is involved both at the first and the subsequent binding sites for Cu(II) on HSA. In view of this finding, it appears that the equilibrium between HSA–Cu(II) and Cu(II) – amino acid complex is mediated through a ternary complex HSA – Cu(II) – amino acid. \u003C\u002Fjats:p>",{"EN":1370},"Evidence for albumin – Cu(II) – amino acid ternary complex",{"VOID":1372},"5660417",{"VOID":1374},"10.1139\u002Fo68-092",[102],"http:\u002F\u002Fwww.nrcresearchpress.com\u002Fdoi\u002F10.1139\u002Fo68-092",[1378,1389],{"id":1379,"sortIndex":36,"researcher":26,"roles":1380,"affiliations":1381,"properties":1382},"70dc9562-7cc1-4215-a92b-352db9ed832f",[],[],{"openalex":1383,"orcid":1385,"title":1387},{"VOID":1384},"A5091378879",{"VOID":1386},"https:\u002F\u002Forcid.org\u002F0000-0002-6309-5081",{"EN":1388},"Bibudhendra Sarkar",{"id":1390,"sortIndex":115,"researcher":26,"roles":1391,"affiliations":1392,"properties":1393},"5882b29f-7cce-40e3-85d9-0a6b315ecf83",[],[],{"openalex":1394,"title":1396},{"VOID":1395},"A5017755098",{"EN":1397},"Yuk Y. Wigfield",{"url":26,"publisher":1399,"properties":1407},{"id":659,"createTime":660,"updateTime":661,"relativeEntities":1400,"slug":663,"properties":1401,"entityType":24,"verifyStatus":28,"verifyTime":26,"verifyNote":26,"syncStatus":28,"languages":26,"translateLanguages":26,"viewCount":36,"subjectFields":1404,"manageAffiliations":1405,"indexDatabases":1406,"url":26,"thumbnailPath":26,"statistic":26,"gsStatistic":26,"type":26,"analyzePriority":26},[],{"issn":1402,"title":1403},{"VOID":666},{"EN":668},[],[],[],{"volume":1408,"pages":1410,"issue":1412},{"VOID":1409},"46",{"VOID":1411},"601-607",{"VOID":990},80,{"total":1413,"publishYear":26,"statisticByYear":1415},{"2012":115,"2013":115,"2014":59,"2019":115,"2023":115,"2024":115},"1968-06-01",1968,[],{"id":1420,"createTime":1421,"updateTime":1421,"relativeEntities":1422,"slug":1423,"properties":1424,"entityType":695,"verifyStatus":28,"verifyTime":1421,"verifyNote":696,"syncStatus":28,"languages":1438,"translateLanguages":26,"viewCount":36,"primaryUrl":1439,"fullTextUrl":26,"authors":1440,"publicationType":747,"publisherRelationship":1463,"citationCount":1477,"citationInfo":1478,"publishDate":1480,"publishYear":1150,"citationAnalyzeStatus":28,"lastCitationAnalyze":26,"indexDatabases":26,"openAccess":26,"references":1481,"isForceReanalyzing":769},"68deddcf-8c2f-4431-9a6c-49d90f1bc505","2024-10-10T06:46:33.176+00:00",[],"STUDIES-ON-THE-LIPID-METABOLISM-OF-THE-CHICK-EMBRYO",{"mag":1425,"keywords":1427,"openalex":1428,"abstract":1430,"title":1432,"pm":1434,"doi":1436},{"VOID":1426},"1992476890",{},{"VOID":1429},"W1992476890",{"EN":1431},"\u003Cjats:p>A study was made of the amounts and fatty acid compositions of the cholesterol esters, phospholipids, and triglycerides present in the yolk of the fertile unincubated egg and in the yolk, liver, and extrahepatic tissues of the chick embryo at various stages of development. Esterification of cholesterol, mainly with oleic acid, occurred in the yolk during incubation. There appeared to be a preferential absorption from the yolk sac of phospholipids rich in docosahexaenoic acid. Considerable amounts of cholesterol esters, of which 80% was cholesterol oleate, accumulated in the embryonic liver. The liver phospholipids contained more stearic, arachidonic, and docosahexaenoic acids, and less palmitic and oleic acids, than did the yolk phospholipids. Docosahexaenoic acid occurred in a surprisingly high concentration in the liver triglycerides. The extrahepatic triglycerides contained more palmitic and C\u003Cjats:sub>18\u003C\u002Fjats:sub>polyunsaturated acids, but less docosahexaenoic acid, than did the liver triglycerides. The concentration of oleic acid in the extrahepatic cholesterol esters was much less than in the liver cholesterol esters. The extrahepatic phospholipids contained more arachidonic and docosahexaenoic acids, but less oleic acid, than did the yolk phospholipids. The implications of these findings are discussed in relation to the general lipid metabolism of the chick embryo.\u003C\u002Fjats:p>",{"EN":1433},"STUDIES ON THE LIPID METABOLISM OF THE CHICK EMBRYO",{"VOID":1435},"14241607",{"VOID":1437},"10.1139\u002Fo64-184",[102],"http:\u002F\u002Fwww.nrcresearchpress.com\u002Fdoi\u002F10.1139\u002Fo64-184",[1441,1452],{"id":1442,"sortIndex":36,"researcher":26,"roles":1443,"affiliations":1444,"properties":1445},"ff526038-3dce-433f-8b2d-e9f1da3edccc",[],[],{"openalex":1446,"orcid":1448,"title":1450},{"VOID":1447},"A5065341278",{"VOID":1449},"https:\u002F\u002Forcid.org\u002F0000-0002-8060-4669",{"EN":1451},"R. C. Noble",{"id":1453,"sortIndex":115,"researcher":26,"roles":1454,"affiliations":1455,"properties":1456},"fae5cbef-bb21-4947-b66e-eeebe058f074",[],[],{"openalex":1457,"orcid":1459,"title":1461},{"VOID":1458},"A5022391836",{"VOID":1460},"https:\u002F\u002Forcid.org\u002F0000-0002-9696-233X",{"EN":1462},"John H. 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J., 84, 506, 10.1042\u002Fbj0840506",{"doi":1485},"10.1042\u002Fbj0840506",{"id":26,"text":1487,"url":26,"identifiers":1488},"MOORE R. M., 1961, DORAN. Biochim. Biophys. Acta, 49, 617, 10.1016\u002F0006-3002(61)90271-2",{"doi":1489},"10.1016\u002F0006-3002(61)90271-2",{"id":26,"text":1491,"url":26,"identifiers":1492},"FOLCH M., 1957, J. Biol. Chem., 226, 497, 10.1016\u002FS0021-9258(18)64849-5",{"doi":1493},"10.1016\u002FS0021-9258(18)64849-5",{"id":26,"text":1495,"url":26,"identifiers":1496},"MANGOLD J., 1961, Soc., 38, 708",{},{"id":26,"text":1498,"url":26,"identifiers":1499},"STOFFEL F., 1959, JR. Anal. Chem., 31, 307, 10.1021\u002Fac60146a047",{"doi":1500},"10.1021\u002Fac60146a047",{"id":26,"text":1502,"url":26,"identifiers":1503},"MOORE D. L., 1963, Can. J. Riochem. Physiol., 41, 1821, 10.1139\u002Fy63-206",{"doi":1504},"10.1139\u002Fy63-206",{"id":26,"text":1506,"url":26,"identifiers":1507},"MOORE D. L., 1964, Biochim. Biophys. 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