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Journal of Medicine and Pharmacy","Tạp chí Y Dược học Cần Thơ",{"EN":487,"VI":488},"\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">04\u002F10\u002F2015 Ministry of Information and Communications allowed Can Tho journal of medicine and pharmacy to operate (102 \u002FGP-BTTTT)\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">07\u002F16\u002F2015 Can Tho journal of medicine and pharmacy is internationally recognized: ISSN 2354-1210\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">In 2016, The journal has been included in the list of medical science journals by The State Council for professorship which is awarded a work score of 0-0.5 points for a published article.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Can Tho Journal of Medicine and Pharmacy welcome original works that haven’t been submitted or published in other medical journals. Posts must contain content related to one of the journal’s categories.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">The content published\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">The journal is divided into 3 categories:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Scientific research article: are valuable scientific works, which have been researched and accepted.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Overview of medicine, biology and pharmacy: serving the objective of continuing training in the fields of medicine, biology and pharmacy; to systematize classical and modern knowledge.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Update information on new knowledge about medicine, biology, pharmacy in the country and in the world.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Scope\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Publication and introduction of scientific research in the fields:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">+ Medicine (internal medicine, surgery, pediatrics, obstetrics and gynecology, odonto-stomatology, laboratory, oncology, traditional medicine, nursing).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">+ Biology (genetics, biotechnology).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">+ Pharmacology (pharmaceutics, drug quality analysis-control, synthetic pharmaceutical chemistry, biochemistry, pharmacognosy, botany, clinical pharmacy).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- To enhance the quality of undergraduate, postgraduate education, scientifically researching and meet the necessary treatment in hospital.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Introducing the updated domestic and oversea information about science technology to promote scientific research and exchanging technology in local, other universities.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Exchanging pharmaceutical and medical information for social health developing in the Mekong Delta and Vietnam.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">The object\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Postgraduate students, student of Can Tho University of Medicine and Pharmacy, scientists from schools, research institutes, hospitals, health centers, pharmaceutical companies of the Mekong Delta; other provinces and regions in Vietnam and other country.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Address\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Headquarters of Can Tho Journal of Medicine and Pharmacy, located Scientific Research and International Cooperation Office: 179 Nguyen Van Cu Street, An Khanh Ward, Ninh Kieu District, Can Tho City, Vietnam.\u003C\u002Fspan>\u003C\u002Fp>","\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Ngày 16\u002F7\u002F2015, Tạp chí Y Dược học Cần Thơ được cấp chỉ số quốc tế: ISSN 2354-1210.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Từ tháng 4\u002F2016, Tạp chí đã được Hội đồng Giáo sư ngành Y đưa vào danh sách các tạp chí khoa học Y học được tính điểm công trình 0-0,5 điểm cho một bài báo đăng.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Năm 2020 Tạp chí Y Dược học Cần Thơ đã được phê duyệt vào danh mục của các Hội đồng Giáo sư ngành Dược học được tính điểm công trình 0-0,5 điểm cho một bài báo đăng.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ ra 12 số\u002Fnăm, 180-200 trang\u002Fsố.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Từ tháng 12\u002F2022 Tạp chí Y Dược học Cần Thơ là thành viên của hệ thống Crossref và từ tháng 01\u002F2023 tạp chí thực hiện bình duyệt online kín 2 chiều nhằm tăng tính minh bạch, tin cậy của các công trình nghiên cứu khoa học và đảm bảo tốt nhất chất lượng khoa học của bài viết.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tôn chỉ, mục đích và phạm vi của tạp chí\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tôn chỉ và mục đích hoạt động của tạp chí: xuất bản nhằm mục đích phổ biến kết quả từ các đề tài nghiên cứu khoa học; giao lưu trao đổi khoa học, chia sẻ kinh nghiệm, học tập, đồng thời cập nhật thông tin khoa học mới trong các lĩnh vực y, sinh, dược học trong và ngoài nước.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Phạm vi của tạp chí: Tạp chí xuất bản được chia thành 3 chuyên mục: (i) Bài báo nghiên cứu khoa học là kết quả công trình nghiên cứu khoa học có giá trị đã được triển khai nghiên cứu, (ii) Bài tổng quan y, sinh, dược học: phục vụ mục tiêu đào tạo liên tục trong lĩnh vực y, sinh, dược học; nhằm hệ thống hóa những kiến thức kinh điển và hiện đại; (iii) Thông tin cập nhật kiến thức mới về y, sinh, dược học trong nước và trên thế giới.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Chính sách truy cập mở\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ áp dụng chính sách truy cập mở đối với các bài báo đã xuất bản đến với độc giả, nhằm mở rộng cơ hội tiếp cận các kết quả nghiên cứu chất lượng cao và tăng cường trao đổi kiến thức. Tạp chí đăng tải trực tuyến (miễn phí) toàn văn các bài báo được công bố trên website của Tạp chí (https:\u002F\u002Ftapchi.ctump.edu.vn).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Đạo đức xuất bản\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ cam kết tuân thủ đạo đức xuất bản phù hợp với các hướng dẫn và tiêu chuẩn của the Committee on Publication Ethics (COPE), tuân thủ các nguyên tắc của COPE’s Core Practices, Best Practices Guidelines for Journal Editors và Guidelines on Good Publication Practices.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Bản thảo bài báo chỉ được chấp nhận khi được tác giả chịu trách nhiệm chính cam kết các nội dung sau: Các nội dung của bản thảo chưa được đăng tải toàn bộ hoặc một phần ở các tạp chí khác; Tất cả các tác giả đều có đóng góp một cách đáng kể vào quá trình nghiên cứu hoặc chuẩn bị bản thảo và cùng chịu trách nhiệm về các nội dung của bản thảo; Tuân thủ các biện pháp đảm bảo đạo đức nghiên cứu (ví dụ thỏa thuận đồng ý tham gia nghiên cứu).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Cam kết bảo mật\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí cam kết thực hiện và tuân thủ các quy định của luật và các văn bản hướng dẫn liên quan đến bảo mật thông tin cá nhân trên không gian mạng. Các thông tin mà người dùng (tác giả, độc giả, biên tập viên, người phản biện) nhập vào các biểu mẫu trên Hệ thống Quản lý xuất bản trực tuyến của tạp chí chỉ được sử dụng vào các mục đích đã được tuyên bố rõ ràng và sẽ không được cung cấp cho bất kỳ bên thứ ba nào khác, hay dùng vào bất kỳ mục đích nào khác.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Phí gửi bài\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Lệ phí gửi đăng bài: 1.000.000đ\u002Fbài báo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Lệ phí gửi đăng nhanh: 1.500.000đ\u002Fbài báo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Đối với tác giả là cán bộ viên chức thuộc Trường Đại học Y Dược Cần Thơ thì được hỗ trợ 50% lệ phí gửi đăng bài.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Đối với sinh viên thực hiện đề tài nghiên cứu khoa học cấp trường được hỗ trợ 100% lệ phí đăng bài ( Tác giả gửi đính kèm “ Quyết định về việc giao tổ chức thực hiện đề tài nghiên cứu khoa học cấp Trường của sinh viên”).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Hình thức nộp lệ phí:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Tiền mặt:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Nộp trực tiếp tại Phòng Tài chính - Kế toán, Trường Đại học Y Dược Cần Thơ, số 179 Nguyễn Văn Cừ, P. An Khánh, Q. Ninh Kiều, thành phố Cần Thơ.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Chuyển khoản:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tên Tài khoản: Trường ĐHYD Cần Thơ, Số TK: 0111000115668, tại ngân hàng Vietcombank chi nhánh Cần Thơ.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Thời gian: Áp dụng từ ngày 01\u002F02\u002F2023.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">* Phí gửi bài không được hoàn trả khi bài viết bị từ chối hoặc tác giả xin rút bài viết.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Quy trình phản biện bài báo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ thực hiện quy trình phản biện kín hai chiều nghiêm ngặt. Danh tính của những người phản biện không được tiết lộ cho các tác giả và ngược lại. Quy trình thẩm định bài báo đăng gồm các bước sau:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tiếp nhận bản thảo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tác giả liên hệ gửi bản thảo đến Tạp chí qua hệ thống trực tuyến tại website: https:\u002F\u002Ftapchi.ctump.edu.vn. Hướng dẫn về cách đăng ký, gửi bài và chuẩn bị bản thảo được cung cấp trên website của Tạp chí.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Sàng lọc sơ bộ\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Sau khi Tòa soạn nhận được bài báo của tác giả, Ban Thư ký sẽ tiến hành kiểm tra sơ bộ bài báo (các yêu cầu về nội dung và hình thức). Những bài báo không đúng quy cách hoặc có nội dung không phù hợp hoặc vi phạm bản quyền sẽ bị từ chối (Ban Thư ký thông báo phản hồi đến tác giả trong vòng 1 tuần). Những bài báo đủ điều kiện, được Ban Thư ký tòa soạn chuyển đến Ban Biên tập có cùng chuyên môn với nội dung bài báo để đề xuất người phản biện. Thời gian kể từ khi Ban Biên tập nhận bài báo đến khi đề xuất người phản biện bài báo chậm nhất là 5 ngày.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Vòng phản biện\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Ban Thư ký gửi bài và yêu cầu phản biện đến 02 phản biện độc lập.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Các phản biện gởi nhận xét cho Ban Thư ký. Thời gian từ khi gửi bài cho phản biện đến khi nhận ý kiến của phản biện tối đa là 20 ngày.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Xử ký kết quả phản biện\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Nếu ý kiến đồng ý cho đăng và không cần chỉnh sửa, Ban Thư ký tiếp tục đăng bài theo qui trình.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Nếu ý kiến đồng ý đăng và cần chỉnh sửa, Ban Thư ký sẽ thông tin đến tác giả chỉnh sửa theo yêu cầu của người phản biện. Thời gian chỉnh sửa và gửi lại kéo dài không quá 2 tuần, từ khi tác giả bài báo nhận được thông tin (Quá trình này có thể lặp lại tối đa 2 lần\u002F1 bài báo). Khi có sự thống nhất, đồng ý của người phản biện; bài báo được tiếp tục đăng theo qui trình.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">3. Những bài báo có chất lượng không đạt yêu cầu, cả 2 phản biện không đồng ý cho đăng sẽ bị Tòa soạn từ chối đăng.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Xuất bản\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Ban Thư ký tổng hợp các bản thảo đã được tác giả hoàn thiện sau thẩm định trình Ban Biên tập xem xét, Tổng Biên tập phê duyệt, quyết định bài đăng theo các tiêu chí: sự phù hợp nội dung với tôn chỉ và mục đích, thể loại bài viết (ưu tiên các bài có bài có nghiên cứu chuyên sâu, hàm lượng khoa học cao), đóng góp mới bài báo, bài báo được ưu tiên đăng trong số gần nhất của Tạp chí theo thứ tự: tính thời sự, chất lượng bài báo và thời gian gửi bài.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Ban Biên tập và Ban Thư ký biên tập bản thảo, chế bản, đọc rà soát lỗi. Thời gian hoàn thành từ 10-15 ngày.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">3. Ban Thư ký có trách nhiệm thông báo cho tác giả bài báo (bằng e-mail) về tình hình phê duyệt bài báo, thời gian, số kỳ, tập xuất bản bài báo theo qui định.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">4. Danh sách bài báo theo số Tạp chí được in ấn và phát hành trong năm định kỳ được công bố chính thức trên website: https:\u002F\u002Ftapchi.ctump.edu.vn\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>",{"VOID":490},"wcQ1uqwAAAAJ","2023-05-30T08:17:21.868+00:00",[],[494],{"id":495,"createTime":28,"updateTime":28,"relativeEntities":496,"slug":28,"properties":497,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":507,"parentIds":508,"statistic":28},"6413896b-eca9-442b-a73f-182a58a0ce40",[],{"title":498,"address":501,"country":504,"abbreviation":505},{"EN":499,"VI":500},"Can Tho University of Medicine and Pharmacy","Trường Đại học Y Dược Cần Thơ",{"EN":502,"VI":503},"No 179, Nguyen Van Cu street, An Khanh ward, Ninh Kieu district, Can Tho city, Vietnam","Số 179, đường Nguyễn Văn Cừ, phường An Khánh, quận Ninh Kiều, thành phố Cần Thơ, Việt Nam",{"VOID":15},{"VOID":506},"ctump","http:\u002F\u002Fwww.ctump.edu.vn\u002F",[],[],"https:\u002F\u002Ftapchi.ctump.edu.vn\u002Findex.php\u002Fctump",{"impactFactor":32,"impactFactorByYear":512,"i10Index":32,"i10IndexLast5Year":32,"totalPublication":514,"totalPublicationByYear":515,"totalCitation":520,"totalCitationByYear":521,"totalCitationPerPublication":108,"totalCitationPerPublicationByYear":523,"hindexLast5Year":45,"hindex":45},{"2022":513,"2023":111,"2024":106},0.01,1556,{"2020":47,"2021":516,"2022":517,"2023":518,"2024":519,"2025":122},57,306,801,358,161,{"2021":146,"2022":280,"2023":522},99,{"2021":524,"2022":318,"2023":104},0.23,{"impactFactor":28,"impactFactorByYear":28,"i10Index":123,"i10IndexLast5Year":123,"totalPublication":526,"totalPublicationByYear":527,"totalCitation":526,"totalCitationByYear":528,"totalCitationPerPublication":40,"totalCitationPerPublicationByYear":531,"hindexLast5Year":49,"hindex":49},476,{"0":205,"2019":123,"2021":139,"2022":459,"2023":451,"2024":357,"2025":49,"2026":48},{"2021":42,"2022":123,"2023":161,"2024":529,"2025":360,"2026":530},136,83,{"2021":105,"2022":513,"2023":532,"2024":127,"2025":533,"2026":534},0.62,25.43,13.83,{"id":536,"createTime":537,"updateTime":382,"relativeEntities":538,"slug":539,"properties":540,"entityType":25,"verifyStatus":26,"verifyTime":28,"verifyNote":28,"languages":552,"translateLanguages":28,"viewCount":133,"subjectFields":553,"manageAffiliations":554,"indexDatabases":555,"url":556,"thumbnailPath":557,"statistic":558,"gsStatistic":594,"type":55,"analyzePriority":28},"6984a56a-db70-403b-9cc4-4013e1ceaffa","2023-05-09T06:47:40.346+00:00",[],"T%E1%BA%A1p%20ch%C3%AD%20Nghi%C3%AAn%20c%E1%BB%A9u%20n%C6%B0%E1%BB%9Bc%20ngo%C3%A0i",{"country":541,"issn":542,"title":544,"introduce":547,"gsId":550},{"VOID":15},{"VOID":543},"25252445",{"EN":545,"VI":546},"VNU Journal of Foreign Studies","Tạp chí Nghiên cứu nước ngoài",{"EN":548,"VI":549},"{\"ops\":[{\"insert\":\"\\n\\nThe \\n\"},{\"attributes\":{\"italic\":true},\"insert\":\"VNU Journal of Science\"},{\"insert\":\"\\n was established in 1985 for the publication of national and international research papers in all fields of natural sciences and technology, social sciences and humanities. 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SCIE","scie",[940,813],"SCIE","https:\u002F\u002Fmjl.clarivate.com\u002Fsearch-results?issn=1478-6354",[943],"fd7e3bd4-9e39-4f09-954f-650cca734d91","https:\u002F\u002Flink.springer.com\u002Fjournal\u002F13075",{"impactFactor":32,"impactFactorByYear":946,"i10Index":948,"i10IndexLast5Year":32,"totalPublication":949,"totalPublicationByYear":950,"totalCitation":958,"totalCitationByYear":959,"totalCitationPerPublication":969,"totalCitationPerPublicationByYear":970,"hindexLast5Year":564,"hindex":564},{"2012":947,"2013":367,"2014":171,"2015":286,"2016":693,"2017":341},0.93,315,2939,{"1999":49,"2000":40,"2001":47,"2002":129,"2003":951,"2004":571,"2005":952,"2006":433,"2007":218,"2008":218,"2009":216,"2010":953,"2011":954,"2012":955,"2013":956,"2014":830,"2015":957,"2016":205,"2017":145,"2018":357,"2019":48,"2020":205,"2021":205,"2022":47,"2023":145},265,264,180,186,368,207,254,19559,{"2005":158,"2007":960,"2008":961,"2009":962,"2010":963,"2011":964,"2012":965,"2013":966,"2014":967,"2015":968},826,1656,3167,2339,1796,2599,1792,1568,1998,6.65,{"2005":168,"2007":971,"2008":972,"2009":973,"2010":974,"2011":975,"2012":976,"2013":977,"2014":978,"2015":979},5.36,10.75,15.45,12.99,9.66,7.06,8.66,7.96,7.87,{"meta":981,"data":983},{"total":982},"2967",[984,1159,1310,1473,1613,1703,1817,1947,2044,2160],{"id":985,"createTime":986,"updateTime":987,"relativeEntities":988,"slug":989,"properties":990,"entityType":999,"verifyStatus":26,"verifyTime":987,"verifyNote":1000,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":1001,"fullTextUrl":28,"authors":1002,"publicationType":1099,"publisherRelationship":1100,"citationCount":28,"citationInfo":28,"publishDate":1155,"publishYear":1156,"citationAnalyzeStatus":878,"lastCitationAnalyze":28,"indexDatabases":1157,"openAccess":28,"references":28,"isForceReanalyzing":1158},"001611a7-44ae-4763-9ed8-f3950114a3f3","2024-02-08T09:59:06.032+00:00","2025-01-20T11:45:59.617+00:00",[],"Degradation-of-small-leucine-rich-repeat-proteoglycans-by-matrix-metalloprotease-13-identification-of-a-new-biglycan-cleavage-site",{"abstract":991,"title":993,"references":995,"doi":997},{"EN":992},"A major and early feature of cartilage degeneration is proteoglycan breakdown. Matrix metalloprotease (MMP)-13 plays an important role in cartilage degradation in osteoarthritis (OA). This MMP, in addition to initiating collagen fibre cleavage, acts on several proteoglycans. One of the proteoglycan families, termed small leucine-rich proteoglycans (SLRPs), was found to be involved in collagen fibril formation\u002Finteraction, with some members playing a role in the OA process. We investigated the ability of MMP-13 to cleave members of two classes of SLRPs: biglycan and decorin; and fibromodulin and lumican. SLRPs were isolated from human normal and OA cartilage using guanidinium chloride (4 mol\u002Fl) extraction. Digestion products were examined using Western blotting. The identities of the MMP-13 degradation products of biglycan and decorin (using specific substrates) were determined following electrophoresis and microsequencing. We found that the SLRPs studied were cleaved to differing extents by human MMP-13. Although only minimal cleavage of decorin and lumican was observed, cleavage of fibromodulin and biglycan was extensive, suggesting that both molecules are preferential substrates. In contrast to biglycan, decorin and lumican, which yielded a degradation pattern similar for both normal and OA cartilage, fibromodulin had a higher level of degradation with increased cartilage damage. Microsequencing revealed a novel major cleavage site (... G177\u002FV178) for biglycan and a potential cleavage site for decorin upon exposure to MMP-13. We showed, for the first time, that MMP-13 can degrade members from two classes of the SLRP family, and identified the site at which biglycan is cleaved by MMP-13. MMP-13 induced SLRP degradation may represent an early critical event, which may in turn affect the collagen network by exposing the MMP-13 cleavage site in this macromolecule. Awareness of SLRP degradation products, especially those of biglycan and fibromodulin, may assist in early detection of OA cartilage degradation.",{"EN":994},"Degradation of small leucine-rich repeat proteoglycans by matrix metalloprotease-13: identification of a new biglycan cleavage site",{"VOID":996},"Heinegard D, Bayliss M, Lorenzo P: Pathogenesis of structural changes in the osteoarthritic joint. Osteoarthritis. Edited by: Brandt KD, Doherty M, Lohmander SL. 2003, New York: Oxford University Press Inc, 73-92.\nKjellen L, Lindahl U: Proteoglycans: structures and interactions. Annu Rev Biochem. 1991, 60: 443-475. 10.1146\u002Fannurev.bi.60.070191.002303.\nPoole AR: Cartilage in Health and Disease. Arthritis and Allied Conditions. Edited by: Koopman WJ, Moreland LW. 2005, Philadelphia: Lippincott, Williams & Wilkins, 223-269.\nBech-Hansen NT, Naylor MJ, Maybaum TA, Sparkes RL, Koop B, Birch DG, Bergen AA, Prinsen CF, Polomeno RC, Gal A, et al: Mutations in NYX, encoding the leucine-rich proteoglycan nyctalopin, cause X-linked complete congenital stationary night blindness. Nat Genet. 2000, 26: 319-323. 10.1038\u002F81619.\nKnudson CB, Knudson W: Cartilage proteoglycans. Semin Cell Dev Biol. 2001, 12: 69-78. 10.1006\u002Fscdb.2000.0243.\nHedlund H, Mengarelli-Widholm S, Heinegard D, Reinholt FP, Svensson O: Fibromodulin distribution and association with collagen. Matrix Biol. 1994, 14: 227-232. 10.1016\u002F0945-053X(94)90186-4.\nLorenzo P, Aspberg A, Onnerfjord P, Bayliss MT, Neame PJ, Heinegard D: Identification and characterization of asporin. A novel member of the leucine-rich repeat protein family closely related to decorin and biglycan. J Biol Chem. 2001, 276: 12201-12211. 10.1074\u002Fjbc.M010932200.\nSztrolovics R, White RJ, Poole AR, Mort JS, Roughley PJ: Resistance of small leucine-rich repeat proteoglycans to proteolytic degradation during interleukin-1-stimulated cartilage catabolism. Biochem J. 1999, 339: 571-577. 10.1042\u002F0264-6021:3390571.\nBengtsson E, Morgelin M, Sasaki T, Timpl R, Heinegard D, Aspberg A: The leucine-rich repeat protein PRELP binds perlecan and collagens and may function as a basement membrane anchor. J Biol Chem. 2002, 277: 15061-15068. 10.1074\u002Fjbc.M108285200.\nMansson B, Wenglen C, Morgelin M, Saxne T, Heinegard D: Association of chondroadherin with collagen type II. J Biol Chem. 2001, 276: 32883-32888. 10.1074\u002Fjbc.M101680200.\nYoung AA, Smith MM, Smith SM, Cake MA, Ghosh P, Read RA, Melrose J, Sonnabend DH, Roughley PJ, Little CB: Regional assessment of articular cartilage gene expression and small proteoglycan metabolism in an animal model of osteoarthritis. Arthritis Res Ther. 2005, 7: R852-R861. 10.1186\u002Far1756.\nKizawa H, Kou I, Iida A, Sudo A, Miyamoto Y, Fukuda A, Mabuchi A, Kotani A, Kawakami A, Yamamoto S, et al: An aspartic acid repeat polymorphism in asporin inhibits chondrogenesis and increases susceptibility to osteoarthritis. Nat Genet. 2005, 37: 138-144. 10.1038\u002Fng1496.\nBock HC, Michaeli P, Bode C, Schultz W, Kresse H, Herken R, Miosge N: The small proteoglycans decorin and biglycan in human articular cartilage of late-stage osteoarthritis. Osteoarthritis Cartilage. 2001, 9: 654-663. 10.1053\u002Fjoca.2001.0420.\nMelching LI, Roughley PJ: The synthesis of dermatan sulphate proteoglycans by fetal and adult human articular cartilage. Biochem J. 1989, 261: 501-508.\nImai K, Hiramatsu A, Fukushima D, Pierschbacher MD, Okada Y: Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release. Biochem J. 1997, 322: 809-814.\nWinnemoller M, Schon P, Vischer P, Kresse H: Interactions between thrombospondin and the small proteoglycan decorin: interference with cell attachment. Eur J Cell Biol. 1992, 59: 47-55.\nWinnemoller M, Schmidt G, Kresse H: Influence of decorin on fibroblast adhesion to fibronectin. Eur J Cell Biol. 1991, 54: 10-17.\nIozzo RV: Matrix proteoglycans: from molecular design to cellular function. Annu Rev Biochem. 1998, 67: 609-652. 10.1146\u002Fannurev.biochem.67.1.609.\nPoole AR, Rosenberg LC, Reiner A, Ionescu M, Bogoch E, Roughley PJ: Contents and distributions of the proteoglycans decorin and biglycan in normal and osteoarthritic human articular cartilage. J Orthop Res. 1996, 14: 681-689. 10.1002\u002Fjor.1100140502.\nHeathfield TF, Onnerfjord P, Dahlberg L, Heinegard D: Cleavage of fibromodulin in cartilage explants involves removal of the N-terminal tyrosine sulfate-rich region by proteolysis at a site that is sensitive to matrix metalloproteinase-13. J Biol Chem. 2004, 279: 6286-6295. 10.1074\u002Fjbc.M307765200.\nChakravarti S, Stallings RL, SundarRaj N, Cornuet PK, Hassell JR: Primary structure of human lumican (keratan sulfate proteoglycan) and localization of the gene (LUM) to chromosome 12q21.3-q22. Genomics. 1995, 27: 481-488. 10.1006\u002Fgeno.1995.1080.\nIozzo RV, Murdoch AD: Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J. 1996, 10: 598-614.\nHocking AM, Shinomura T, McQuillan DJ: Leucine-rich repeat glycoproteins of the extracellular matrix. Matrix Biol. 1998, 17: 1-19. 10.1016\u002FS0945-053X(98)90121-4.\nGrover J, Chen XN, Korenberg JR, Roughley PJ: The human lumican gene. Organization, chromosomal location, and expression in articular cartilage. J Biol Chem. 1995, 270: 21942-21949. 10.1074\u002Fjbc.270.37.21942.\nSvensson L, Narlid I, Oldberg A: Fibromodulin and lumican bind to the same region on collagen type I fibrils. FEBS Lett. 2000, 470: 178-182. 10.1016\u002FS0014-5793(00)01314-4.\nChakravarti S, Magnuson T, Lass JH, Jepsen KJ, LaMantia C, Carroll H: Lumican regulates collagen fibril assembly: skin fragility and corneal opacity in the absence of lumican. J Cell Biol. 1998, 141: 1277-1286. 10.1083\u002Fjcb.141.5.1277.\nLi Y, Aoki T, Mori Y, Ahmad M, Miyamori H, Takino T, Sato H: Cleavage of lumican by membrane-type matrix metalloproteinase-1 abrogates this proteoglycan-mediated suppression of tumor cell colony formation in soft agar. Cancer Res. 2004, 64: 7058-7064. 10.1158\u002F0008-5472.CAN-04-1038.\nKashiwagi M, Enghild JJ, Gendron C, Hughes C, Caterson B, Itoh Y, Nagase H: Altered proteolytic activities of ADAMTS-4 expressed by C-terminal processing. J Biol Chem. 2004, 279: 10109-10119. 10.1074\u002Fjbc.M312123200.\nFosang AJ, Last K, Knauper V, Murphy G, Neame PJ: Degradation of cartilage aggrecan by collagenase-3 (MMP-13). FEBS Lett. 1996, 380: 17-20. 10.1016\u002F0014-5793(95)01539-6.\nAltman RD, Asch E, Bloch DA, Bole G, Borenstein D, Brandt KD, Christy W, Cooke TD, Greenwald R, Hochberg M, et al: Development of criteria for the classification and reporting of osteoarthritis. Classification of osteoarthritis of the knee. Arthritis Rheum. 1986, 29: 1039-1049.\nMankin HJ, Dorfman H, Lippiello L, Zarins A: Biochemical and metabolic abnormalities in articular cartilage from osteoarthritic human hips. II. Correlation of morphology with biochemical and metabolic data. J Bone Joint Surg Am. 1971, 53: 523-537.\nPelletier JP, Martel-Pelletier J, Howell DS, Ghandur-Mnaymneh L, Enis JE, Woessner JF: Collagenase and collagenolytic activity in human osteoarthritic cartilage. 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Nature. 1990, 346: 281-284. 10.1038\u002F346281a0.\nTardif G, Pelletier JP, Dupuis M, Geng C, Cloutier JM, Martel-Pelletier J: Collagenase 3 production by human osteoarthritic chondrocytes in response to growth factors and cytokines is a function of the physiological state of the cells. Arthritis Rheum. 1999, 42: 1147-1158. 10.1002\u002F1529-0131(199906)42:6\u003C1147::AID-ANR11>3.0.CO;2-Y.\nMoldovan F, Pelletier JP, Hambor J, Cloutier JM, Martel-Pelletier J: Collagenase-3 (matrix metalloprotease 13) is preferentially localized in the deep layer of human arthritic cartilage in situ : In vitro mimicking effect by transforming growth factor beta. Arthritis Rheum. 1997, 40: 1653-1661.\nSvensson L, Heinegard D, Oldberg A: Decorin-binding sites for collagen type I are mainly located in leucine-rich repeats 4–5. J Biol Chem. 1995, 270: 20712-20716. 10.1074\u002Fjbc.270.35.20712.\nScott PG, McEwan PA, Dodd CM, Bergmann EM, Bishop PN, Bella J: Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan. Proc Natl Acad Sci USA. 2004, 101: 15633-15638. 10.1073\u002Fpnas.0402976101.\nKojoh K, Fukuda E, Matsuzawa H, Wakagi T: Zinc-coordination of aspartic acid-76 in Sulfolobus ferredoxin is not required for thermal stability of the molecule. J Inorg Biochem. 2002, 89: 69-73. 10.1016\u002FS0162-0134(01)00410-X.\nReboul P, Pelletier JP, Tardif G, Cloutier JM, Martel-Pelletier J: The new collagenase, collagenase-3, is expressed and synthesized by human chondrocytes but not by synoviocytes: A role in osteoarthritis. J Clin Invest. 1996, 97: 2011-2019.",{"VOID":998},"10.1186\u002Far1873","PUBLICATION","Auto Verify","https:\u002F\u002Farthritis-research.biomedcentral.com\u002Farticles\u002F10.1186\u002Far1873",[1003,1019,1032,1045,1058,1073,1086],{"id":1004,"sortIndex":32,"researcher":28,"roles":1005,"affiliations":1007,"properties":1016,"displayName":1018,"givenName":28,"familyName":28},"e5499045-f9f3-4181-82dd-387995d3fbb5",[1006],"AUTHOR",[1008],{"id":1009,"sortIndex":32,"affiliation":1010,"properties":28},"46ab7f4f-8d6a-4d85-b071-d11f38bce303",{"id":1009,"createTime":28,"updateTime":28,"relativeEntities":1011,"slug":28,"properties":1012,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1015,"statistic":28},[],{"title":1013},{"VI":1014},"Osteoarthritis Research Unit, University of Montreal Hospital Centre, Notre-Dame Hospital, Montreal, Canada",[],{"title":1017},{"VI":1018},"Jordi Monfort",{"id":1020,"sortIndex":40,"researcher":28,"roles":1021,"affiliations":1022,"properties":1029,"displayName":1031,"givenName":28,"familyName":28},"c18173c2-cb4a-4e47-bdb7-8011b5463478",[1006],[1023],{"id":1009,"sortIndex":32,"affiliation":1024,"properties":28},{"id":1009,"createTime":28,"updateTime":28,"relativeEntities":1025,"slug":28,"properties":1026,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1028,"statistic":28},[],{"title":1027},{"VI":1014},[],{"title":1030},{"VI":1031},"Ginette 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Reboul",{"id":1046,"sortIndex":42,"researcher":28,"roles":1047,"affiliations":1048,"properties":1055,"displayName":1057,"givenName":28,"familyName":28},"fbcac469-296b-4f72-a8b2-be5ddf4693f7",[1006],[1049],{"id":1009,"sortIndex":32,"affiliation":1050,"properties":28},{"id":1009,"createTime":28,"updateTime":28,"relativeEntities":1051,"slug":28,"properties":1052,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1054,"statistic":28},[],{"title":1053},{"VI":1014},[],{"title":1056},{"VI":1057},"François Mineau",{"id":1059,"sortIndex":45,"researcher":28,"roles":1060,"affiliations":1061,"properties":1070,"displayName":1072,"givenName":28,"familyName":28},"b70f41c0-b4e9-49fb-aad2-9e3cdcd1936e",[1006],[1062],{"id":1063,"sortIndex":32,"affiliation":1064,"properties":28},"8cb11f7b-7de8-4c4d-90e8-55abcebbd6e6",{"id":1063,"createTime":28,"updateTime":28,"relativeEntities":1065,"slug":28,"properties":1066,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1069,"statistic":28},[],{"title":1067},{"VI":1068},"Genetics Unit, Shriner's Hospital for Children, Montreal, Canada",[],{"title":1071},{"VI":1072},"Peter 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descriptions of gout have noted the tendency to hypertrophic bone changes. The aim of this study was to characterize the features of new bone formation (NBF) in gout, and to determine the relationship between NBF and other radiographic features of disease, particularly erosion and tophus. Paired plain radiographs (XR) and computed tomography (CT) scans of 798 individual hand and wrist joints from 20 patients with gout were analyzed. Following a structured review of a separate set of images, films were scored for the presence of the following features of NBF: spur, osteophyte, periosteal NBF, ankylosis and sclerosis. The relationship between NBF and other radiographic features was analyzed. The most frequent forms of NBF were bone sclerosis and osteophyte. Spur and periosteal NBF were less common, and ankylosis was rare. On both XR and CT, joints with bone erosion were more likely to have NBF; for CT, if erosion was present, the odds ratios (OR) was 45.1 for spur, 3.3 for osteophyte, 16.6 for periosteal NBF, 26.6 for ankylosis and 32.3 for sclerosis, P for all \u003C 0.01. Similarly, on CT, joints with intraosseous tophus were more likely to have NBF; if tophus was present, the OR was 48.4 for spur, 3.3 for osteophyte, 14.5 for periosteal NBF, 35.1 for ankylosis and 39.1 for sclerosis; P for all \u003C 0.001. This detailed quantitative analysis has demonstrated that NBF occurs more frequently in joints affected by other features of gout. This work suggests a connection between bone loss, tophus, and formation of new bone during the process of joint remodelling in gout.",{"EN":1169},"Characterization of new bone formation in gout: a quantitative site-by-site analysis using plain radiography and computed tomography",{"VOID":1171},"Resnick D, Broderick TW: Intraosseous calcifications in tophaceous gout. AJR Am J Roentgenol. 1981, 137: 1157-1161.\nWatt I, Middlemiss H: The radiology of gout. Review article. Clin Radiol. 1975, 26: 27-36.\nBarthelemy CR, Nakayama DA, Carrera GF, Lightfoot RW, Wortmann RL: Gouty arthritis: a prospective radiographic evaluation of sixty patients. Skeletal Radiol. 1984, 11: 1-8. 10.1007\u002FBF00361124.\nBloch C, Hermann G, Yu TF: A radiologic reevaluation of gout: a study of 2,000 patients. AJR Am J Roentgenol. 1980, 134: 781-787.\nGerster JC, Landry M, Duvoisin B, Rappoport G: Computed tomography of the knee joint as an indicator of intraarticular tophi in gout. Arthritis Rheum. 1996, 39: 1406-1409. 10.1002\u002Fart.1780390820.\nDalbeth N, Clark B, Gregory K, Gamble GD, Doyle A, McQueen FM: Computed tomography measurement of tophus volume: comparison with physical measurement. Arthritis Rheum. 2007, 57: 461-465. 10.1002\u002Fart.22612.\nDalbeth N, Clark B, Gregory K, Gamble G, Sheehan T, Doyle A, McQueen FM: Mechanisms of bone erosion in gout: a quantitative analysis using plain radiography and computed tomography. Ann Rheum Dis. 2009, 68: 1290-1295. 10.1136\u002Fard.2008.094201.\nRahman P, Gladman DD, Cook RJ, Zhou Y, Young G, Salonen D: Radiological assessment in psoriatic arthritis. Br J Rheumatol. 1998, 37: 760-765. 10.1093\u002Frheumatology\u002F37.7.760.\nTaylor WJ, Porter GG, Helliwell PS: Operational definitions and observer reliability of the plain radiographic features of psoriatic arthritis. J Rheumatol. 2003, 30: 2645-2658.\nOstergaard M, McQueen F, Wiell C, Bird P, Boyesen P, Ejbjerg B, Peterfy C, Gandjbakhch F, Duer-Jensen A, Coates L, Haavardsholm EA, Hermann KG, Lassere M, O'Connor P, Emery P, Genant H, Conaghan PG: The OMERACT psoriatic arthritis magnetic resonance imaging scoring system (PsAMRIS): definitions of key pathologies, suggested MRI sequences, and preliminary scoring system for PsA Hands. J Rheumatol. 2009, 36: 1816-1824. 10.3899\u002Fjrheum.090352.\nWendling D, Toussirot E, Streit G, Prati C: Imaging study scores for ankylosing spondylitis. Joint Bone Spine. 2006, 73: 655-660. 10.1016\u002Fj.jbspin.2006.03.007.\nBuckland-Wright C: Subchondral bone changes in hand and knee osteoarthritis detected by radiography. Osteoarthritis Cartilage. 2004, 12 (Suppl A): S10-19.\nResnick D: Diagnosis of Bone and Joint Disorders. 2002, Philadelphia: Saunders, 4\nDalbeth N, Collis J, Gregory K, Clark B, Robinson E, McQueen FM: Tophaceous joint disease strongly predicts hand function in patients with gout. Rheumatology (Oxford). 2007, 46: 1804-1807. 10.1093\u002Frheumatology\u002Fkem246.\nWallace SL, Robinson H, Masi AT, Decker JL, McCarty DJ, Yu TF: Preliminary criteria for the classification of the acute arthritis of primary gout. Arthritis Rheum. 1977, 20: 895-900. 10.1002\u002Fart.1780200320.\nDalbeth N, Clark B, McQueen F, Doyle A, Taylor W: Validation of a radiographic damage index in chronic gout. Arthritis Rheum. 2007, 57: 1067-1073. 10.1002\u002Fart.22891.\nDalbeth N, Pool B, Gamble GD, Smith T, Callon KE, McQueen FM, Cornish J: Cellular characterization of the gouty tophus: a quantitative analysis. Arthritis Rheum. 2010, 62: 1549-1556. 10.1002\u002Fart.27356.\nLee SJ, Nam KI, Jin HM, Cho YN, Lee SE, Kim TJ, Lee SS, Kee SJ, Lee KB, Kim N, Park YW: Bone destruction by receptor activator of nuclear factor kappaB ligand-expressing T cells in chronic gouty arthritis. Arthritis Res Ther. 2011, 13: R164-10.1186\u002Far3483.\nDalbeth N, Smith T, Nicolson B, Clark B, Callon K, Naot D, Haskard DO, McQueen FM, Reid IR, Cornish J: Enhanced osteoclastogenesis in patients with tophaceous gout: urate crystals promote osteoclast development through interactions with stromal cells. Arthritis Rheum. 2008, 58: 1854-1865. 10.1002\u002Fart.23488.\nBouchard L, de Medicis R, Lussier A, Naccache PH, Poubelle PE: Inflammatory microcrystals alter the functional phenotype of human osteoblast-like cells in vitro: synergism with IL-1 to overexpress cyclooxygenase-2. J Immunol. 2002, 168: 5310-5317.\nChhana A, Callon KE, Pool B, Naot D, Watson M, Gamble GD, McQueen FM, Cornish J, Dalbeth N: Monosodium urate monohydrate crystals inhibit osteoblast viability and function: implications for development of bone erosion in gout. Ann Rheum Dis. 2011, 70: 1684-1691. 10.1136\u002Fard.2010.144774.\nPalmer DG, Highton J, Hessian PA: Development of the gout tophus. An hypothesis. Am J Clin Pathol. 1989, 91: 190-195.\nSchweyer S, Hemmerlein B, Radzun HJ, Fayyazi A: Continuous recruitment, co-expression of tumour necrosis factor-alpha and matrix metalloproteinases, and apoptosis of macrophages in gout tophi. Virchows Arch. 2000, 437: 534-539. 10.1007\u002Fs004280000282.\nJoyce ME, Roberts AB, Sporn MB, Bolander ME: Transforming growth factor-beta and the initiation of chondrogenesis and osteogenesis in the rat femur. J Cell Biol. 1990, 110: 2195-2207. 10.1083\u002Fjcb.110.6.2195.\nFujimori Y, Nakamura T, Ijiri S, Shimizu K, Yamamuro T: Heterotopic bone formation induced by bone morphogenetic protein in mice with collagen-induced arthritis. Biochem Biophys Res Commun. 1992, 186: 1362-1367. 10.1016\u002FS0006-291X(05)81556-6.\nLories RJ, Derese I, Luyten FP: Modulation of bone morphogenetic protein signaling inhibits the onset and progression of ankylosing enthesitis. J Clin Invest. 2005, 115: 1571-1579. 10.1172\u002FJCI23738.\nDiarra D, Stolina M, Polzer K, Zwerina J, Ominsky MS, Dwyer D, Korb A, Smolen J, Hoffmann M, Scheinecker C, van der Heide D, Landewe R, Lacey D, Richards WG, Schett G: Dickkopf-1 is a master regulator of joint remodeling. Nat Med. 2007, 13: 156-163. 10.1038\u002Fnm1538.\nPedersen SJ, Chiowchanwisawakit P, Lambert RG, Ostergaard M, Maksymowych WP: Resolution of inflammation following treatment of ankylosing spondylitis is associated with new bone formation. J Rheumatol. 2011, 38: 1349-1354. 10.3899\u002Fjrheum.100925.\nMaksymowych WP, Chiowchanwisawakit P, Clare T, Pedersen SJ, Ostergaard M, Lambert RG: Inflammatory lesions of the spine on magnetic resonance imaging predict the development of new syndesmophytes in ankylosing spondylitis: evidence of a relationship between inflammation and new bone formation. Arthritis Rheum. 2009, 60: 93-102. 10.1002\u002Fart.24132.\nDalbeth N, Horne A, Gamble GD, Ames R, Mason B, McQueen FM, Bolland MJ, Grey A, Reid IR: The effect of calcium supplementation on serum urate: analysis of a randomized controlled trial. Rheumatology (Oxford). 2009, 48: 195-197.\nNabipour I, Sambrook PN, Blyth FM, Janu MR, Waite LM, Naganathan V, Handelsman DJ, Le Couteur DG, Cumming RG, Seibel MJ: Serum uric acid is associated with bone health in older men: a cross-sectional population-based study. J Bone Miner Res. 2011, 26: 955-964. 10.1002\u002Fjbmr.286.\nRoddy E, Zhang W, Doherty M: Are joints affected by gout also affected by osteoarthritis?. Ann Rheum Dis. 2007, 66: 1374-1377. 10.1136\u002Fard.2006.063768.\nChoi HK, Al-Arfaj AM, Eftekhari A, Munk PL, Shojania K, Reid G, Nicolaou S: Dual energy computed tomography in tophaceous gout. Ann Rheum Dis. 2009, 68: 1609-1612. 10.1136\u002Fard.2008.099713.",{"VOID":1173},"10.1186\u002Far3913","2025-01-01T20:26:01.610+00:00","http:\u002F\u002Farthritis-research.biomedcentral.com\u002Farticles\u002F10.1186\u002Far3913",[1177,1192,1207,1222,1237],{"id":1178,"sortIndex":32,"researcher":28,"roles":1179,"affiliations":1180,"properties":1189,"displayName":1191,"givenName":28,"familyName":28},"41ef2d19-d4a8-4e57-b5fd-11663c77674b",[1006],[1181],{"id":1182,"sortIndex":32,"affiliation":1183,"properties":28},"6ba2ccc3-cc0e-4270-9ff7-113b226a3c67",{"id":1182,"createTime":28,"updateTime":28,"relativeEntities":1184,"slug":28,"properties":1185,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1188,"statistic":28},[],{"title":1186},{"VI":1187},"Department of Medicine, University of Auckland, Grafton, New Zealand",[],{"title":1190},{"VI":1191},"Nicola 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necrosis factor (TNF) is considered to be a major factor in chronic synovial inflammation and is an inducer of mitogen-activated protein kinase (MAPK) signalling. In the present study we investigated the ability of TNF to activate MAPKs in the synovial membrane in vivo. We studied human TNF transgenic mice – an in vivo model of TNF-induced arthritis – to examine phosphorylation of extracellular signal-regulated kinase (ERK), c-Jun amino terminal kinase (JNK) and p38MAPKα in the inflamed joints by means of immunoblot and immunohistochemistry. In addition, the effects of systemic blockade of TNF, IL-1 and receptor activator of nuclear factor-κB (RANK) ligand on the activation of MAPKs were assessed. In vivo, overexpression of TNF induced activation of p38MAPKα and ERK in the synovial membrane, whereas activation of JNK was less pronounced and rarely observed on immunohistochemical analysis. Activated p38MAPKα was predominantly found in synovial macrophages, whereas ERK activation was present in both synovial macrophages and fibroblasts. T and B lymphocytes did not exhibit major activation of any of the three MAPKs. Systemic blockade of TNF reduced activation of p38MAPKα and ERK, whereas inhibition of IL-1 only affected p38MAPKα and blockade of RANK ligand did not result in any decrease in MAPK activation in the synovial membrane. These data indicate that TNF preferentially activates p38MAPKα and ERK in synovial membrane exposed to TNF. This not only suggests that targeted inhibition of p38MAPKα and ERK is a feasible strategy for blocking TNF-mediated effects on joints, but it also shows that even currently available methods to block TNF effectively reduce activation of these two MAPKs.",{"EN":1320},"Tumour necrosis factor activates the mitogen-activated protein kinases p38α and ERK in the synovial membrane in vivo",{"VOID":1322},"Firestein GS: Evolving concepts of rheumatoid arthritis. Nature. 2003, 423: 356-361. 10.1038\u002Fnature01661.\nFeldmann M, Brennan FM, Maini RN: Role of cytokines in rheumatoid arthritis. Annu Rev Immunol. 1996, 14: 397-440. 10.1146\u002Fannurev.immunol.14.1.397.\nBathon JM, Martin RW, Fleischmann RM, Tesser JR, Schiff MH, Keystone EC, Genovese MC, Wasko MC, Moreland LW, Weaver AL, et al: A comparison of etanercept and methotrexate in patients with early rheumatoid arthritis. N Engl J Med. 2000, 343: 1586-1593. 10.1056\u002FNEJM200011303432201.\nLipsky PE, van der Heijde DM, St Clair EW, Furst DE, Breedveld FC, Kalden JR, Smolen JS, Weisman M, Emery P, Feldmann M, et al: Infliximab and methotrexate in the treatment of rheumatoid arthritis. Anti-Tumor Necrosis Factor Trial in Rheumatoid Arthritis with Concomitant Therapy Study Group. N Engl J Med. 2000, 343: 1594-1602. 10.1056\u002FNEJM200011303432202.\nWeinblatt ME, Kremer JM, Bankhurst AD, Bulpitt KJ, Fleischmann RM, Fox RI, Jackson CG, Lange M, Burge DJ: A trial of etanercept, a recombinant tumor necrosis factor receptor:Fc fusion protein, in patients with rheumatoid arthritis receiving methotrexate. N Engl J Med. 1999, 340: 253-259. 10.1056\u002FNEJM199901283400401.\nWeinblatt ME, Keystone EC, Furst DE, Moreland LW, Weisman MH, Birbara CA, Teoh LA, Fischkoff SA, Chartash EK: Adalimumab, a fully human anti-tumor necrosis factor alpha monoclonal antibody, for the treatment of rheumatoid arthritis in patients taking concomitant methotrexate: the ARMADA trial. Arthritis Rheum. 2003, 48: 35-45. 10.1002\u002Fart.10697.\nKeffer J, Probert L, Cazlaris H, Georgopoulos S, Kaslaris E, Kioussis D, Kollias G: Transgenic mice expressing human tumour necrosis factor: a predictive genetic model of arthritis. EMBO J. 1991, 10: 4025-4031.\nDeleuren BW, Chu CG, Field M, Brennan FM, Katsikis P, Feldmann M, Maini RN: Localization of interleukin-1 alpha, type 1 interleukin-1 receptor and interleukin-1 receptor antagonist in the synovial membrane and cartilage\u002Fpannus junction in rheumatoid arthritis. Br J Rheumatol. 1992, 31: 801-809.\nAlsalameh S, Winter K, Al-Ward R, Wendler J, Kalden JR, Kinne RW: Distribution of TNF-α, TNF-R55 and TNF-R75 in the rheumatoid synovial membrane: TNF receptors are localized preferentially in the lining layer; TNF-α is distributed mainly in the vicinity of TNF receptors in the deeper layers. Scand J Immunol. 1999, 49: 278-285. 10.1046\u002Fj.1365-3083.1999.00458.x.\nVasquez-Del Mercado M, Delgado-Rizo V, Munoz-Valle JF, Orozco-Alcala J, Volk HD, Armendariz-Borunda J: Expression of interleukin-1 beta, tumor necrosis factor alpha, interleukin-6, -10 and -4 and metalloproteases by freshly isolated mononuclear cells from early never-treated and non-acute treated rheumatoid arthritis patients. Clin Exp Rheumatol. 1999, 17: 575-583.\nBaud V, Karin M: Signal transduction by tumor necrosis factor and its relatives. Trends Cell Biol. 2001, 11: 372-377. 10.1016\u002FS0962-8924(01)02064-5.\nJohnson GL, Lapadat R: Mitogen-activated protein kinase pathways mediated by ERK, JNK and p38 protein kinases. Science. 2002, 298: 1911-1912. 10.1126\u002Fscience.1072682.\nEnglish LM, Cobb MH: Pharmacological inhibitors of MAPK pathways. Trends Pharmacol Sci. 2002, 23: 40-45. 10.1016\u002FS0165-6147(00)01865-4.\nBadger AM, Griswold DE, Kapadia R, Blake S, Swift BA, Hoffmann SJ, Stroup GB, Webb E, Rieman DJ, Gowen M, et al: Disease-modifying activity of SB 242235, a selective inhibitor of p38 mitogen-activated protein kinase, in rat adjuvant arthritis. Arthritis Rheum. 2000, 43: 175-183. 10.1002\u002F1529-0131(200001)43:1\u003C175::AID-ANR22>3.0.CO;2-S.\nNishikawa M, Myoui A, Tomita T, Takahi K, Nampei A, Yishikawa H: Prevention of the onset and progression of collagen-induced arthritis in rats by the potent p38 mitogen-activated protein kinase inhibitor FR167653. Arthritis Rheum. 2003, 48: 2670-2681. 10.1002\u002Fart.11227.\nPargellis C, Regan J: Inhibitors of p38 mitogen-activated protein kinase for the treatment of rheumatoid arthritis. Curr Opin Investig Drugs. 2003, 45: 566-571.\nSweeney SE, Firestein G: Signal transduction in rheumatoid arthritis. Curr Opin Rheumatol. 2004, 16: 231-237. 10.1097\u002F00002281-200405000-00011.\nSchett G, Tohidast-Akrad M, Smolen JS, Schmid BJ, Steiner CW, Bitzan P, Zenz P, Redlich K, Xu Q, Steiner G: Activation, differential localization, and regulation of the stress-activated protein kinases, extracellular signal-regulated kinase, c-JUN N-terminal kinase, and p38 mitogen-activated protein kinase in synovial tissue and cells in rheumatoid arthritis. Arthritis Rheum. 2000, 43: 2501-2512. 10.1002\u002F1529-0131(200011)43:11\u003C2501::AID-ANR18>3.0.CO;2-K.\nZwerina J, Hayer S, Tohidast-Akrad M, Bergmeister H, Redlich K, Feige U, Dunstan C, Kollias G, Steiner G, Smolen JS, Schett G: Single and combined inhibition of TNF, IL-1 and RANKL pathways in TNF-induced arthritis: effects on synovial inflammation, bone erosion and cartilage destruction. Arthritis Rheum. 2004, 50: 277-290. 10.1002\u002Fart.11487.\nRedlich K, Hayer S, Maier A, Dunstan CR, Tohidast-Akrad M, Lang S, Turk B, Pietschmann P, Woloszczuk W, Haralambous S, et al: Tumor necrosis factor α-mediated joint destruction is inhibited by targeting osteoclasts with osteoprotegerin. Arthritis Rheum. 2002, 46: 785-792. 10.1002\u002Fart.10097.\nSchett G, Steiner CW, Xu Q, Smolen JS, Steiner G: TNFalpha mediates susceptibility to heat-induced apoptosis by protein phosphatase-mediated inhibition of the HSF1\u002Fhsp70 stress response. Cell Death Differ. 2003, 10: 1126-1136. 10.1038\u002Fsj.cdd.4401276.\nAggarwal BB: Tumor necrosis factors receptor associated signaling molecules and their role in activation of apoptosis, JNK and NF-kappaB. Ann Rheum Dis. 2000, 59 (Suppl 1): i6-i16. 10.1136\u002Fard.59.suppl_1.i6.\nSuzuki M, Tetsuka T, Yoshida S, Watanabe N, Kobayashi M, Matsui N, Okamoto T: The role of p38 mitogen-activated protein kinase in IL-6 and IL-8 production from the TNF-alpha- or IL-1beta-stimulated rheumatoid synovial fibroblasts. FEBS Lett. 2000, 465: 23-27. 10.1016\u002FS0014-5793(99)01717-2.\nLiacini A, Sylvester J, Li WQ, Huang W, Dehnade F, Ahmad M, Zafarullah M: Induction of matrix metalloproteinase-13 gene expression by TNF-alpha is mediated by MAP kinases, AP-1, and NF-kappaB transcription factors in articular chondrocytes. Exp Cell Res. 2003, 288: 208-217. 10.1016\u002FS0014-4827(03)00180-0.\nVanden Berghe W, Plaisance S, Boone E, De Bosscher K, Schmitz ML, Fiers W, Haegeman G: P38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-κB p65 transactivation mediated by tumor necrosis factor. J Biol Chem. 1998, 273: 3285-3290. 10.1074\u002Fjbc.273.6.3285.\nPelletier JP, Fernandes JC, Brunet J, Moldovan F, Schrier D, Flory C, Martel-Pelletier J: In vivo selective inhibition of mitogen-activated protein kinase kinase 1\u002F2 in rabbit experimental osteoarthritis is associated with a reduction in the development of structural changes. Arthritis Rheum. 2003, 48: 1582-1593. 10.1002\u002Fart.11014.\nHammaker DR, Boyle DL, Chabaud-Riou M, Firestein GS: Regulation of c-Jun N-terminal kinase by MEKK-2 and mitogen-activated protein kinase kinase kinases in rheumatoid arthritis. J Immunol. 2004, 172: 1612-1618.\nSundarrajan M, Boyle DL, Chabaud-Riou M, Hammaker D, Firestein GS: Expression of the MAPK kinases MKK-4 and MKK-7 in rheumatoid arthritis and their role as key regulators of JNK. Arthritis Rheum. 2003, 48: 2450-2460. 10.1002\u002Fart.11228.\nFanger GR, Johnson NL, Johnson GL: MEK kinases are regulated by EGF and selectively interact with Rac\u002FCdc42. EMBO J. 1997, 16: 4961-4972. 10.1093\u002Femboj\u002F16.16.4961.\nGarrington TP, Ishizuka T, Papst PJ, Chayama K, Webb S, Yujiri T, Sun W, Sather S, Russell DM, Gibson SB, et al: MEKK2 gene disruption causes loss of cytokine production in response to IgE and c-Kit ligand stimulation of ES cell-derived mast cells. EMBO J. 2000, 19: 5387-5395. 10.1093\u002Femboj\u002F19.20.5387.\nHan Z, Boyle DL, Chang L, Bennett B, Karin M, Yang L, Manning AM, Firestein GS: C-Jun N-terminal kinase is required for metalloproteinase expression and joint destruction in inflammatory arthritis. J Clin Invest. 2001, 108: 73-81. 10.1172\u002FJCI200112466.\nHan Z, Chang L, Yamanishi Y, Karin M, Firestein GS: Joint damage and inflammation in c-Jun N-terminal kinase 2 knockout mice with passive murine collagen-induced arthritis. Arthritis Rheum. 2002, 46: 818-823. 10.1002\u002Fart.10104.\nNeidhart M, Rethage J, Kuchen S, Kunzler P, Crowl RM, Billingham ME, Gay RE, Gay S: Retrotransposable L1 elements expressed in rheumatoid arthritis synovial tissue: association with genomic hypomethylation and influence on gene expression. Arthritis Rheum. 2000, 43: 2634-2647. 10.1002\u002F1529-0131(200012)43:12\u003C2634::AID-ANR3>3.0.CO;2-1.\nRidley SH, Sarsfield SJ, Lee JC, Bigg HF, Cawston TE, Taylor DJ, Witt DL, Saklatvala J: Actions of IL-1 are selectively controlled by p38 mitogen-activated protein kinase: regulation of prostaglandin H synthase-2, metalloproteinases, and IL-6 at different levels. J Immunol. 1997, 158: 3165-3173.\nKong YY, Feige U, Sarosi I, Bolon B, Tafuri A, Morony S, Capparelli C, Li J, Elliott R, McCabe S, et al: Activated T cells regulate bone loss and joint destruction in adjuvant arthritis through osteoprotegerin ligand. Nature. 1999, 402: 304-309. 10.1038\u002F46303.\nRomas E, Sims NA, Hards DK, Lindsay M, Quinn JW, Ryan PF, Dunstan CR, Martin TJ, Gillespie MT: Osteoprotegerin reduces osteoclast numbers and prevents bone erosion in collagen-induced arthritis. Am J Pathol. 2002, 161: 1419-1427.",{"VOID":1324},"10.1186\u002Far1797","http:\u002F\u002Farthritis-research.biomedcentral.com\u002Farticles\u002F10.1186\u002Far1797",[1327,1351,1364,1377,1390,1403],{"id":1328,"sortIndex":32,"researcher":28,"roles":1329,"affiliations":1330,"properties":1348,"displayName":1350,"givenName":28,"familyName":28},"900ef833-84ab-4a79-a7f3-42fc1f7fba2a",[1006],[1331,1339],{"id":1332,"sortIndex":32,"affiliation":1333,"properties":28},"5d145979-1700-4341-9625-e1a6b3598930",{"id":1332,"createTime":28,"updateTime":28,"relativeEntities":1334,"slug":28,"properties":1335,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1338,"statistic":28},[],{"title":1336},{"VI":1337},"Division of Rheumatology, Department of Internal Medicine III, University of Vienna, Vienna, 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transduction pathways regulate the production and function of many cytokines implicated in immune-mediated diseases. Targeting these enzymes with small molecule inhibitors represents a fertile field for the treatment of rheumatoid arthritis. Recent successes with compounds that block upstream kinases suggest that proximal members of the signaling cascades, such as Rac and other Rho family enzymes, might have therapeutic potential. Balancing efficacy and toxicity, however, remains a significant challenge that will require careful evaluation.",{"EN":1623},"'Rac'-ing upstream to treat rheumatoid arthritis",{"VOID":1625},"Abreu JRF, de Launay D, van Hennik PB, van Stalborgh AM, ten Klooster JP, Sanders MW, Reedquist KA, Vervoordeldonk MJ, Hordijk PL, Tak PP: A Rac1 inhibitory peptide suppresses antibody production and paw swelling in the murine collagen-induced arthritis model of rheumatoid arthritis. Arthritis Res Ther. 2010, 12: R2-10.1186\u002Far2900.\nHammaker D, Firestein GS: 'Go upstream, young man': lessons learned from the p38 saga. Ann Rheum Dis. 2010, 69 (Suppl 1): i77-i82. 10.1136\u002Fard.2009.119479.\nDamjanov N, Kauffman RS, Spencer-Green GT: Efficacy, pharmacodynamics, and safety of VX-702, a novel p38 MAPK inhibitor, in rheumatoid arthritis: results of two randomized, double-blind, placebo-controlled clinical studies. Arthritis Rheum. 2009, 60: 1232-1241. 10.1002\u002Fart.24485.\nWeinblatt ME, Kavanaugh A, Burgos-Vargas R, Dikranian AH, Medrano-Ramirez G, Morales-Torres JL, Murphy FT, Musser TK, Straniero N, Vicente-Gonzales AV, Grossbard E: Treatment of rheumatoid arthritis with a Syk kinase inhibitor: a twelve-week, randomized, placebo-controlled trial. Arthritis Rheum. 2008, 58: 3309-3318. 10.1002\u002Fart.23992.\nKremer JM, Bloom BJ, Breedveld FC, Coombs JH, Fletcher MP, Gruben D, Krishnaswami S, Burgos-Vargas R, Wilkinson B, Zerbini CA, Zwillich SH: The safety and efficacy of a JAK inhibitor in patients with active rheumatoid arthritis: results of a double-blind, placebo-controlled phase IIa trial of three dosage levels of CP-690,550 versus placebo. Arthritis Rheum. 2009, 60: 1895-1905. 10.1002\u002Fart.24567.\nHeasman SJ, Ridley AJ: Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat Rev Mol Cell Biol. 2008, 9: 690-701. 10.1038\u002Fnrm2476.\nYamanishi Y, Boyle DL, Pinkoski MJ, Mahboubi A, Lin T, Han Z, Zvaifler NJ, Green DR, Firestein GS: Regulation of joint destruction and inflammation by p53 in collagen-induced arthritis. Am J Pathol. 2002, 160: 123-130.\nFukushima A, Boyle DL, Corr M, Firestein GS: Kinetic analysis of synovial signaling and gene expression in animal models of arthritis. Ann Rheum Dis. 2010. 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focus of the present review is on the extent to which epigenetic alterations influence the development of systemic lupus erythematosus. Lupus is a systemic autoimmune disease characterized by the production of autoantibodies directed at nuclear self-antigens. A DNA methylation defect in CD4+ T cells has long been observed in idiopathic and drug-induced lupus. Recent studies utilizing high-throughput technologies have further characterized the nature of the DNA methylation defect in lupus CD4+ T cells. Emerging evidence in the literature is revealing an increasingly interconnected network of epigenetic dysregulation in lupus. Recent reports describe variable expression of a number of regulatory microRNAs in lupus CD4+ T cells, some of which govern the expression of DNA methyltransferase 1. While studies to date have revealed a significant role for epigenetic defects in the pathogenesis of lupus, the causal nature of epigenetic variation in lupus remains elusive. Future longitudinal epigenetic studies in lupus are therefore needed.",{"EN":1827},"The role of epigenetic variation in the pathogenesis of systemic lupus erythematosus",{"VOID":1829},"International Consortium for Systemic Lupus Erythematosus Genetics (SLEGEN), Harley JB, Alarcón-Riquelme ME, Criswell LA, Jacob CO, Kimberly RP, Moser KL, Tsao BP, Vyse TJ, Langefeld CD, Nath SK, Guthridge JM, Cobb BL, Mirel DB, Marion MC, Williams AH, Divers J, Wang W, Frank SG, Namjou B, Gabriel SB, Lee AT, Gregersen PK, Behrens TW, Taylor KE, Fernando M, Zidovetzki R, Gaffney PM, Edberg JC, Rioux JD, et al: Genome-wide association scan in women with systemic lupus erythematosus identifies susceptibility variants in ITGAM, PXK, KIAA1542 and other loci. Nat Genet. 2008, 40: 204-210. 10.1038\u002Fng.81.\nKozyrev SV, Abelson AK, Wojcik J, Zaghlool A, Linga Reddy MV, Sanchez E, Gunnarsson I, Svenungsson E, Sturfelt G, Jönsen A, Truedsson L, Pons-Estel BA, Witte T, D'Alfonso S, Barizzone N, Danieli MG, Gutierrez C, Suarez A, Junker P, Laustrup H, González-Escribano MF, Martin J, Abderrahim H, Alarcón-Riquelme ME: Functional variants in the B-cell gene BANK1 are associated with systemic lupus erythematosus. Nat Genet. 2008, 40: 211-216. 10.1038\u002Fng.79.\nHom G, Graham RR, Modrek B, Taylor KE, Ortmann W, Garnier S, Lee AT, Chung SA, Ferreira RC, Pant PV, Ballinger DG, Kosoy R, Demirci FY, Kamboh MI, Kao AH, Tian C, Gunnarsson I, Bengtsson AA, Rantapää-Dahlqvist S, Petri M, Manzi S, Seldin MF, Rönnblom L, Syvänen AC, Criswell LA, Gregersen PK, Behrens TW: Association of systemic lupus erythematosus with C8orf13-BLK and ITGAM-ITGAX. 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evidence implicates intervertebral disc degeneration as a major cause of low back pain, although its pathogenesis is poorly understood. Numerous characteristic features of disc degeneration mimic those seen during ageing but appear to occur at an accelerated rate. We hypothesised that this is due to accelerated cellular senescence, which causes fundamental changes in the ability of disc cells to maintain the intervertebral disc (IVD) matrix, thus leading to IVD degeneration. Cells isolated from non-degenerate and degenerate human tissue were assessed for mean telomere length, senescence-associated β-galactosidase (SA-β-gal), and replicative potential. Expression of P16INK4A(increased in cellular senescence) was also investigated in IVD tissue by means of immunohistochemistry. RNA from tissue and cultured cells was used for real-time polymerase chain reaction analysis for matrix metalloproteinase-13, ADAMTS 5 (a disintegrin and metalloprotease with thrombospondin motifs 5), and P16INK4A. Mean telomere length decreased with age in cells from non-degenerate tissue and also decreased with progressive stages of degeneration. In non-degenerate discs, there was an age-related increase in cellular expression of P16INK4A. Cells from degenerate discs (even from young patients) exhibited increased expression of P16INK4A, increased SA-β-gal staining, and a decrease in replicative potential. Importantly, there was a positive correlation between P16INK4Aand matrix-degrading enzyme gene expression. Our findings indicate that disc cell senescence occurs in vivo and is accelerated in IVD degeneration. Furthermore, the senescent phenotype is associated with increased catabolism, implicating cellular senescence in the pathogenesis of IVD degeneration.",{"EN":2054},"Accelerated cellular senescence in degenerate intervertebral discs: a possible role in the pathogenesis of intervertebral disc degeneration",{"VOID":2056},"Luoma K, Riihimaki H, Luukkonen R, Raininko R, Viikari-Juntura E, Lamminen A: Low back pain in relation to lumbar disc degeneration. Spine. 2000, 25: 487-492. 10.1097\u002F00007632-200002150-00016.\nMiller JA, Schmatz C, Schultz AB: Lumbar disc degeneration: correlation with age, sex, and spine level in 600 autopsy specimens. Spine. 1988, 13: 173-178. 10.1097\u002F00007632-198802000-00008.\nRoughley PJ, Alini M, Antoniou J: The role of proteoglycans in aging, degeneration and repair of the intervertebral disc. Biochem Soc Trans. 2002, 30: 869-874. 10.1042\u002FBST0300869.\nRoughley PJ: Biology of intervertebral disc aging and degeneration: involvement of the extracellular matrix. Spine. 2004, 29: 2691-2699. 10.1097\u002F01.brs.0000146101.53784.b1.\nLe Maitre CL, Freemont AJ, Hoyland JA: Localization of degradative enzymes and their inhibitors in the degenerate human intervertebral disc. J Pathol. 2004, 204: 47-54. 10.1002\u002Fpath.1608.\nBoos N, Weissbach S, Rohrbach H, Weiler C, Spratt KF, Nerlich AG: Classification of age-related changes in lumbar intervertebral discs: 2002 Volvo Award in basic science. Spine. 2002, 27: 2631-2644. 10.1097\u002F00007632-200212010-00002.\nWeiler C, Nerlich A, Zipperer J, Bachmeier BE, Boos N: 2002 SSE Award Competition in Basic Science: expression of major matrix metalloproteinases is associated with intervertebral disc degradation and resorption. Eur Spine J. 2002, 11: 308-320. 10.1007\u002Fs00586-002-0472-0.\nSive JI, Baird P, Jeziorsk M, Watkins A, Hoyland JA, Freemont AJ: Expression of chondrocyte markers by cells of normal and degenerate intervertebral discs. Mol Pathol. 2002, 55: 91-97. 10.1136\u002Fmp.55.2.91.\nLe Maitre CL, Freemont AJ, Hoyland JA: The role of interleukin-1 in the pathogenesis of human intervertebral disc degeneration. Arthritis Res Ther. 2005, 7: R732-R745. 10.1186\u002Far1732.\nGruber HE, Hanley EN: Analysis of aging and degeneration of the human intervertebral disc. Comparison of surgical specimens with normal controls [see comments]. Spine. 1998, 23: 751-757. 10.1097\u002F00007632-199804010-00001.\nCampisi J, Kim SH, Lim CS, Rubio M: Cellular senescence, cancer and aging: the telomere connection. Exp Gerontol. 2001, 36: 1619-1637. 10.1016\u002FS0531-5565(01)00160-7.\nRoberts S, Evans EH, Kletsas D, Jaffray DC, Eisenstein SM: Senescence in human intervertebral discs. Eur Spine J. 2006, 15 (Suppl 3): S312-S316. 10.1007\u002Fs00586-006-0126-8.\nGruber HE, Ingram JA, Norton HJ, Hanley EN: Senescence in cells of the aging and degenerating intervertebral disc: immunolocalization of senescence-associated beta-galactosidase in human and sand rat discs. Spine. 2007, 32: 321-327. 10.1097\u002F01.brs.0000253960.57051.de.\nMartin JA, Buckwalter JA: Aging, articular cartilage chondrocyte senescence and osteoarthritis. Biogerontology. 2002, 3: 257-264. 10.1023\u002FA:1020185404126.\nMartin JA, Buckwalter JA: The role of chondrocyte senescence in the pathogenesis of osteoarthritis and in limiting cartilage repair. J Bone Joint Surg Am. 2003, 85-A (Suppl 2): 106-110.\nPfaffl MW: Quantification strategies in real time PCR. A-Z of Quantitative PCR. Edited by: Bustin SA. 2004, La Jolla, CA: International University Line, 87-112.\nCampisi J: Replicative senescence and immortalization. The Molecular Basis of Cell Cycle and Growth Control. Edited by: Stein GS. 1999, New York: Wiley-Liss, 348-373.\nToussaint O, Medrano EE, von Zglinicki T: Cellular and molecular mechanisms of stress-induced premature senescence (SIPS) of human diploid fibroblasts and melanocytes. Exp Gerontol. 2000, 35: 927-945. 10.1016\u002FS0531-5565(00)00180-7.\nYudoh K, Nguyen T, Nakamura H, Hongo-Masuko K, Kato T, Nishioka K: Potential involvement of oxidative stress in cartilage senescence and development of osteoarthritis: oxidative stress induces chondrocyte telomere instability and downregulation of chondrocyte function. Arthritis Res Ther. 2005, 7: R380-R391. 10.1186\u002Far1499.\nHoyland JA, Freemont AJ, Jayson MI: Age related changes in the structures within and bordering the intervertebral foramen: associations with low back pain. The Ageing Spine. Edited by: Hukins DW, Nelson MA. 1987, Manchester: Manchester University Press, 94-110.\nFreemont AJ, Watkins A, Le Maitre C, Baird P, Jeziorska M, Knight MT, Ross ER, O'Brien JP, Hoyland JA: Nerve growth factor expression and innervation of the painful intervertebral disc. J Pathol. 2002, 197: 286-292. 10.1002\u002Fpath.1108.\nCoates PJ: Markers of senescence?. J Pathol. 2002, 196: 371-373. 10.1002\u002Fpath.1073.\nDuan J, Duan J, Zhang Z, Tong T: Irreversible cellular senescence induced by prolonged exposure to H2O2 involves DNA-damage-and-repair genes and telomere shortening. Int J Biochem Cell Biol. 2005, 37: 1407-1420. 10.1016\u002Fj.biocel.2005.01.010.\nDumont P, Balbeur L, Remacle J, Toussaint O: Appearance of biomarkers of in vitro ageing after successive stimulation of WI-38 fibroblasts with IL-1alpha and TNF-alpha: senescence associated beta-galactosidase activity and morphotype transition. J Anat. 2000, 197 (Pt 4): 529-537. 10.1046\u002Fj.1469-7580.2000.19740529.x.\nvon Zglinicki T, Martin-Ruiz CM: Telomeres as biomarkers for ageing and age-related diseases. Curr Mol Med. 2005, 5: 197-203. 10.2174\u002F1566524053586545.\nParsch D, Brummendorf TH, Richter W, Fellenberg J: Replicative aging of human articular chondrocytes during ex vivo expansion. Arthritis Rheum. 2002, 46: 2911-2916. 10.1002\u002Fart.10626.\nMartin JA, Buckwalter JA: Telomere erosion and senescence in human articular cartilage chondrocytes. J Gerontol A Biol Sci Med Sci. 2001, 56: B172-B179.\nChang E, Harley CB: Telomere length and replicative aging in human vascular tissues. Proc Natl Acad Sci USA. 1995, 92: 11190-11194. 10.1073\u002Fpnas.92.24.11190.\nAnderson DG, Tannoury C: Molecular pathogenic factors in symptomatic disc degeneration. Spine J. 2005, 5: 260S-266S. 10.1016\u002Fj.spinee.2005.02.010.\nHayflick L: The limited in vitro lifetime of human diploid cell strains. Exp Cell Res. 1965, 37: 614-636. 10.1016\u002F0014-4827(65)90211-9.\nCampisi J: Cancer, aging and cellular senescence. In Vivo. 2000, 14: 183-188.\nKrishnamurthy J, Torrice C, Ramsey MR, Kovalev GI, Al-Regaiey K, Su L, Sharpless NE: Ink4a\u002FArf expression is a biomarker of aging. J Clin Invest. 2004, 114: 1299-1307. 10.1172\u002FJCI200422475.\nSatyanarayana A, Rudolph KL: p16 and ARF: activation of teenage proteins in old age. J Clin Invest. 2004, 114: 1237-1240. 10.1172\u002FJCI200423437.\nSherr CJ, Roberts JM: CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev. 1999, 13: 1501-1512.\nZhou HW, Lou SQ, Zhang K: Recovery of function in osteoarthritic chondrocytes induced by p16INK4a-specific siRNA in vitro. Rheumatology (Oxford). 2004, 43: 555-568. 10.1093\u002Frheumatology\u002Fkeh127.\nDimri GP, Lee X, Basile G, Acosta M, Scott G, Roskelley C, Medrano EE, Linskens M, Rubelj I, Pereira-Smith O, et al: A biomarker that identifies senescent human cells in culture and in aging skin in vivo. Proc Natl Acad Sci USA. 1995, 92: 9363-9367. 10.1073\u002Fpnas.92.20.9363.\nPrice JS, Waters JG, Darrah C, Pennington C, Edwards DR, Donell ST, Clark IM: The role of chondrocyte senescence in osteoarthritis. Aging Cell. 2002, 1: 57-65. 10.1046\u002Fj.1474-9728.2002.00008.x.\nForeman KE, Tang J: Molecular mechanisms of replicative senescence in endothelial cells. Exp Gerontol. 2003, 38: 1251-1257. 10.1016\u002Fj.exger.2003.09.005.\nLe Maitre CL, Freemont A, Hoyland J: Human disc degeneration is associated with increased MMP 7 expression. Biotech Histochem. 2006, 81: 125-131. 10.1080\u002F10520290601005298.\nPiera-Velazquez S, Jimenez SA, Stokes D: Increased life span of human osteoarthritic chondrocytes by exogenous expression of telomerase. Arthritis Rheum. 2002, 46: 683-693. 10.1002\u002Fart.10116.\nShay JW, Wright WE: Use of telomerase to create bioengineered tissues. 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immunodominant epitope of bovine type II collagen (CII256–270) in Aq mice carries a hydroxylysine-264 linked galactose (Gal-Hyl264), the recognition of which is central to the development of collagen-induced arthritis. This study explores the molecular interactions involved in the engagement of T-cell receptors (TCRs) with such epitopes. Responses of three anti-CII T-cell hybridomas and clone A9.2 (all sharing close TCR sequences) to a panel of CII256–270 analogues incorporating Gal-Hyl264 with a modified side chain were determined. Recognition of naturally occurring CII256–270 peptides by either group of T cells depended strictly upon the presence of the carbohydrate and, more precisely, its intact HO-4 group. Modifications of primary amino group on the hydroxylysine side chain eliminated T-cell reactivity, notwithstanding the presence of the galactosyl moiety. Moderate stereochemical changes, such as altered sugar orientation and methylation at the galactose anchor position, were still permissive. Conversely, robust transformations affecting the relative positions of the key elements were detrimental to TCR recognition. To conclude, these data provide strong new experimental evidence that integrity of both galactose HO-4 and hydroxylysine side chain primary amino groups are mandatory for activation of anti-Gal-Hyl264 TCRs. They also indicate that there is a certain degree of TCR plasticity in peptide-TCR interactions.",{"EN":2170},"Insights into spatial configuration of a galactosylated epitope required to trigger arthritogenic T-cell receptors specific for the sugar moiety",{"VOID":2172},"Doyle HA, Mamula MJ: Post-translational protein modifications in antigen recognition and autoimmunity. Trends Immunol. 2001, 22: 443-449. 10.1016\u002FS1471-4906(01)01976-7.\nRudd PM, Elliott T, Cresswell P, Wilson IA, Dwek RA: Glycosylation and the immune system. Science. 2001, 291: 2370-2376. 10.1126\u002Fscience.291.5512.2370.\nSebbag M, Moinard N, Auger I, Clavel C, Arnaud J, Nogueira L, Roudier J, Serre G: Epitopes of human fibrin recognized by the rheumatoid arthritis-specific autoantibodies to citrullinated proteins. Eur J Immunol. 2006, 36: 2250-2263. 10.1002\u002Feji.200535790.\nvan Gaalen F, Ioan-Facsinay A, Huizinga TW, Toes RE: The devil in the details: the emerging role of anticitrulline autoimmunity in rheumatoid arthritis. J Immunol. 2005, 175: 5575-5580.\nKim WU, Cho ML, Jung YO, Min SY, Park SW, Min DJ, Yoon JH, Kim HY: Type II collagen autoimmunity in rheumatoid arthritis. Am J Med Sci. 2004, 327: 202-211. 10.1097\u002F00000441-200404000-00006.\nCathcart ES, Hayes KC, Gonnerman WA, Lazzari AA, Franzblau C: Experimental arthritis in a nonhuman primate. I. Induction by bovine type II collagen. Lab Invest. 1986, 54: 26-31.\nCourtenay JS, Dallman MJ, Dayan AD, Martin A, Mosedale B: Immunisation against heterologous type II collagen induces arthritis in mice. Nature. 1980, 283: 666-668. 10.1038\u002F283666a0.\nDehm P, Prockop DJ: Biosynthesis of cartilage procollagen. Eur J Biochem. 1973, 35: 159-166. 10.1111\u002Fj.1432-1033.1973.tb02821.x.\nMichaëlsson E, Malmström V, Reis S, Engström A, Burkhardt H, Holmdahl R: T cell recognition of carbohydrates on type II collagen. J Exp Med. 1994, 180: 745-749. 10.1084\u002Fjem.180.2.745.\nMyers LK, Myllyharju J, Nokelainen M, Brand DD, Cremer MA, Stuart JM, Bodo M, Kivirikko KI, Kang AH: Relevance of posttranslational modifications for the arthritogenicity of type II collagen. J Immunol. 2004, 172: 2970-2975.\nBäcklund J, Treschow A, Bockermann R, Holm B, Holm L, Issazadeh-Navikas S, Kihlberg J, Holmdahl R: Glycosylation of type II collagen is of major importance for T cell tolerance and pathology in collagen-induced arthritis. Eur J Immunol. 2002, 32: 3776-3784. 10.1002\u002F1521-4141(200212)32:12\u003C3776::AID-IMMU3776>3.0.CO;2-A.\nCorthay A, Bäcklund J, Broddefalk J, Michaëlsson E, Goldschmidt TJ, Kihlberg J, Holmdahl R: Epitope glycosylation plays a critical role for T cell recognition of type II collagen in collagen-induced arthritis. Eur J Immunol. 1998, 28: 2580-2590. 10.1002\u002F(SICI)1521-4141(199808)28:08\u003C2580::AID-IMMU2580>3.0.CO;2-X.\nBäcklund J, Carlsen S, Höger T, Holm B, Fugger L, Kihlberg J, Burkhardt H, Holmdahl R: Predominant selection of T cells specific for the glycosylated collagen type II epitope (263–270) in humanized transgenic mice and in rheumatoid arthritis. Proc Natl Acad Sci USA. 2002, 99: 9960-9965. 10.1073\u002Fpnas.132254199.\nChiocchia G, Manoury-Schwartz B, Boissier MC, Gahery H, Marche PN, Fournier C: T cell regulation of collagen-induced arthritis in mice. III. Is T cell vaccination a valuable therapy?. Eur J Immunol. 1994, 24: 2775-2783. 10.1002\u002Feji.1830241130.\nDoncarli A, Chiocchia G, Stasiuk LM, Herbage D, Boutillon MM, Fournier C, Abehsira-Amar O: A recurrent valpha17\u002Fvbeta10 TCR-expressing T cell clone is involved in the pathogenicity of collagen-induced arthritis in DBA\u002F1 mice. Eur J Immunol. 1999, 29: 3636-3642. 10.1002\u002F(SICI)1521-4141(199911)29:11\u003C3636::AID-IMMU3636>3.0.CO;2-3.\nChiocchia G, Boissier MC, Ronziere MC, Herbage D, Fournier C: T cell regulation of collagen-induced arthritis in mice. I. Isolation of Type II collagen-reactive T cell hybridomas with specific cytotoxic function. J Immunol. 1990, 145: 519-525.\nChiocchia G, Manoury B, Boissier MC, Fournier C: T cell-targeted immunotherapy in murine collagen-induced arthritis. Clin Exp Rheumatol. 1993, S15-S17. Suppl 9\nMarin J, Blaton MA, Briand JP, Chiocchia G, Fournier C, Guichard G: Synthesis of glycopeptides from type II collagen-incorporating galactosylated hydroxylysine mimetics and their use in studying the fine specificity of arthritogenic T cells. Chembiochem. 2005, 6: 1796-1804. 10.1002\u002Fcbic.200500075.\nMarin J, Didierjean C, Aubry A, Casimir JR, Briand JP, Guichard G: Synthesis of enantiopure 4-hydroxypipecolate and 4-hydroxylysine derivatives from a common 4,6-dioxopiperidinecarboxylate precursor. J Org Chem. 2004, 69: 130-141. 10.1021\u002Fjo0353886.\nManoury-Schwartz B, Chiocchia G, Lotteau V, Fournier C: Selective increased presentation of type II collagen by leupeptin. Int Immunol. 1997, 9: 581-589. 10.1093\u002Fintimm\u002F9.4.581.\nRosloniec EF, Whittington KB, Brand DD, Myers LK, Stuart JM: Identification of MHC class II and TCR binding residues in the type II collagen immunodominant determinant mediating collagen-induced arthritis. Cell Immunol. 1996, 172: 21-28. 10.1006\u002Fcimm.1996.0210.\nKjéllen P, Brunsberg U, Broddefalk J, Hansen B, Vestberg M, Ivarsson I, Engström A, Svejgaard A, Kihlberg J, Fugger L, Holmdahl R: The structural basis of MHC control of collagen-induced arthritis; binding of the immunodominant type II collagen 256–270 glycopeptide to H-2Aq and H-2Ap molecules. Eur J Immunol. 1998, 28: 755-767. 10.1002\u002F(SICI)1521-4141(199802)28:02\u003C755::AID-IMMU755>3.0.CO;2-2.\nFerlin WG, Mougneau E, Hugues S, Appel H, Jang MH, Cazareth J, Beaudoin L, Schricke C, Lehuen A, Wucherpfennig KW, Glaichenhaus N: Self-peptides that bind with low affinity to the diabetes-associated I-A(g7) molecule readily induce T cell tolerance in non-obese diabetic mice. Eur J Immunol. 2004, 34: 2656-2663. 10.1002\u002Feji.200425413.\nHe XL, Radu C, Sidney J, Sette A, Ward ES, Garcia KC: Structural snapshot of aberrant antigen presentation linked to autoimmunity: the immunodominant epitope of MBP complexed with I-Au. Immunity. 2002, 17: 83-94. 10.1016\u002FS1074-7613(02)00340-0.\nBoissier MC, Feng XZ, Carlioz A, Roudier R, Fournier C: Experimental autoimmune arthritis in mice. I. Homologous type II collagen is responsible for self-perpetuating chronic polyarthritis. Ann Rheum Dis. 1987, 46: 691-700.\nHolm B, Bäcklund J, Recio MA, Holmdahl R, Kihlberg J: Glycopeptide specificity of helper T cells obtained in mouse models for rheumatoid arthritis. Chembiochem. 2002, 3: 1209-1222. 10.1002\u002F1439-7633(20021202)3:12\u003C1209::AID-CBIC1209>3.0.CO;2-0.\nMaynard J, Petersson K, Wilson DH, Adams EJ, Blondelle SE, Boulanger MJ, Wilson DB, Garcia KC: Structure of an autoimmune T cell receptor complexed with class II peptide-MHC: insights into MHC bias and antigen specificity. 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