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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",[931,813],"SCIE","https:\u002F\u002Fmjl.clarivate.com\u002Fsearch-results?issn=0919-9268",[934],"e93c2eb9-09a3-4b7d-8b40-15b2fb7ed703",{"impactFactor":32,"impactFactorByYear":936,"i10Index":937,"i10IndexLast5Year":42,"totalPublication":938,"totalPublicationByYear":939,"totalCitation":944,"totalCitationByYear":945,"totalCitationPerPublication":955,"totalCitationPerPublicationByYear":956,"hindexLast5Year":278,"hindex":278},{"2012":109,"2013":168,"2014":121,"2015":318,"2016":320,"2017":318,"2018":52,"2019":118,"2020":524,"2021":524,"2022":681,"2023":113},141,1632,{"1997":123,"1998":123,"2004":40,"2005":940,"2006":941,"2007":940,"2008":362,"2009":942,"2010":600,"2011":611,"2012":154,"2013":826,"2014":329,"2015":151,"2016":157,"2017":161,"2018":943,"2019":332,"2020":689,"2021":325,"2022":325,"2023":160,"2024":128},121,113,108,84,4555,{"1997":946,"1998":323,"2004":133,"2005":947,"2006":948,"2007":949,"2008":950,"2009":951,"2010":837,"2011":836,"2012":952,"2013":607,"2014":953,"2015":954,"2016":209,"2017":830,"2018":215,"2019":689,"2020":161,"2021":51,"2022":135,"2023":42,"2024":40},241,649,448,459,319,446,408,151,190,2.79,{"1997":957,"1998":49,"2004":133,"2005":958,"2006":959,"2007":960,"2008":465,"2009":637,"2010":961,"2011":962,"2012":963,"2013":237,"2014":193,"2015":964,"2016":175,"2017":965,"2018":344,"2019":286,"2020":585,"2021":121,"2022":696,"2023":106,"2024":165},120.5,5.36,3.96,3.79,2.13,2.47,3.89,2.92,2.9,{"meta":967,"data":969},{"total":968},"1655",[970,1084,1231,1368,1488,1599,1734,1889,2144,2240],{"id":971,"createTime":972,"updateTime":973,"relativeEntities":974,"slug":975,"properties":976,"entityType":985,"verifyStatus":26,"verifyTime":973,"verifyNote":986,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":987,"fullTextUrl":28,"authors":988,"publicationType":1031,"publisherRelationship":1032,"citationCount":28,"citationInfo":28,"publishDate":1080,"publishYear":1081,"citationAnalyzeStatus":882,"lastCitationAnalyze":28,"indexDatabases":1082,"openAccess":28,"references":28,"isForceReanalyzing":1083},"0001c6ac-ce53-4acb-948d-26f80cc4b747","2024-01-03T04:51:48.807+00:00","2025-01-03T08:42:19.934+00:00",[],"Reproductive-characteristics-of-the-orbiculate-cardinalfish-Sphaeramia-orbicularis-in-the-Chuuk-Lagoon-Micronesia",{"abstract":977,"title":979,"references":981,"doi":983},{"EN":978},"Detailed knowledge of the reproductive characteristics of fish in tropical areas is currently lacking. We have performed a histological study of the reproductive aspects of Sphaeramia orbicularis, a tropical fish found on the Weno Islands of the Chuuk Lagoon, Micronesia, and further estimated the gonadosomatic indices (GSI) of this fish. The sex ratio was approximately 1:1. The standard length of males and females at 50% maturity was 49.0 and 46.9 mm, respectively. Histological observation of S. orbicularis ovaries and testes revealed that the fish exhibits multiple spawner characteristics, including coexistence of primary yolk stages, migratory nucleus or mature stages, and asynchronism of the spermatogenesis process. Monthly variations in the GSI and gonadal maturity stages demonstrated that reproductive activity occurs throughout the year. The findings in this study provide important information on the spawning activity and season of S. orbicularis in Micronesia.",{"EN":980},"Reproductive characteristics of the orbiculate cardinalfish Sphaeramia orbicularis in the Chuuk Lagoon, Micronesia",{"VOID":982},"Hilder ML, Pankhurst NM (2003) Evidence that temperature change cues reproductive developmental in the spiny damselfish, Acanthochromis polyacanthus. Environ Biol Fish 66:187–196\nTyler WA, Stanton FG (1995) Potential influence of food abundance on spawning patterns in a damselfish, Abudefduf abdominalis. Bull Mar Sci 57:610–623\nSrinivasan M, Jones GP (2006) Extended breeding and recruitment periods of fishes on a low latitude coral reef. Coral Reefs 25:673–682\nRobertson DR, Peterson CE, Brawn JD (1990) Lunar reproductive cycles of benthic-brooding reef fishes: reflection of larval biology or adult biology? Ecol Monogr 60:311–329\nRobertson DR (1991) The role of adult biology in the timing of spawning of tropical reef fishes. In: Sale PF (ed) The ecology of coral reef fishes. Academic Press, New York, pp 356–386\nThresher RE (1984) Reproduction of reef fishes. TFH Publ, Neptune City\nNelson JS (1994) Fishes of the world, 3rd edn. Wiley, New York\nThacker CE, Roje DM (2009) Phylogeny of cardinalfishes (Teleostei; Gobiiformes: Apogonidae) and the evolution of visceral bioluminescence. Mol Phylogenet Evol 52:735–745\nBellwood DR, Wainwright PC (2002) The history and biogeography of fishes on coral reefs. In: Sale PF (ed) Coral reef fishes: dynamics and diversity in a complex ecosystem. Academic Press, San Diego, pp 33–55\nBlumer LS (1982) A bibliography and categorization of bony fishes exhibiting parental care. Zool J Linn Soc 76:1–22\nAllen GR (1972) Observation on a commensal relationship between Siphamia fuscolineata (Apogonidae) and the crown-of-thorns starfish. Acanthaster planci. Copeia 1972:595–597\nOkuda N, Ohnishi N (2001) Nocturnal hatching timing of mouthbrooding male cardinalfish Apogon niger. Ichthyol Res 48:207–212\nVagelli AA, Volpedo AV (2004) Reproductive ecology of Pterapogon kauderni, an endemic apogonid from Indonesia with direct development. Environ Biol Fish 70:235–245\nJohannes RE (1978) Reproductive strategies of coastal marine fishes in tropics. Environ Biol Fish 3:65–84\nAllen GR (1975) The biology and taxonomy of the cardinalfish, Sphaermia orbicularis (Pisces; Apogonidae). J Roy Soc West Aust 58:86–92\nShao K-T, Chen J-P (1986) Ten new records of cardinalfishes from Taiwan, with synopsis of the family Apogonidae. J Taiwan Mus 39:61–104\nMees J, Mwamsojo GU, Wakwabi EO (1998) Aspects of the biology and feeding ecology of the orbiculate cardinalfish Sphaeramia orbicularis (CUVIER, 1828) (TELEOSTEL: APOGONIDAE) in a KENYAN mangrove forest. Biol Jaarb Dodonaea 66:134–145\nGarcía del Moral R (1993) Técnicas de laboratorio de anatomĺa patólogica. Interamericana-McGraw Hill, Madrid, Spain, pp 405–425\nYamamoto A, Yamazaki F (1961) Rhythm of development in the oocyte of the gold fish, Carassius auratus. Bull Fac Fish Hokkaido Univ 12:93–110\nKume G, Yamaguchi A, Aoki I, Taniuchi T (2000) Reproductive biology of the cardinalfish Apogon lineatus in Tokyo Bay, Japan. Fish Sci 66:947–954\nYoneda M, Futagawa K, Tokimura M, Horikawa Matsuura H, Matsuyama SM (2002) Reproductive cycle, spawning frequency and batch fecundity of the female whitefin jack Kaiwarinus equula in the East China Sea. Fish Res 57:297–309\nNielson LA, Johnson DL (1983) Fisheries techniques. American Fisheries Society, Bethesda\nReay PJ (1989) Reproductive tactics: a non-event in aquaculture? In: Potts GW, Wooton MN (eds) Fish reproduction: strategies and tactics. Academic Press, London, pp 291–309\nKvarnemo C, Ahbnesjö I (1996) The dynamics of operational sex ratios and competition for mates. Trends Ecol Evol 11:404–408\nOkuda N, Yanagisawa Y (1996) Filial cannibalism in a paternal mouthbrooding fish in relation to mate availability. Anim Behav 52:307–314\nOkuda N (2000) Interspecific differences in male cannibalistic behavior between two sympatric cardinalfishes (Pisces: Apogonidae). J Ethol 18:5–10\nHunter JR, Goldberg SR (1980) Spawning incidence and batch fecundity in northern anchovy Engraulis mordax. Fish Bull 77:641–652\nTakemura A, Rahman SMD, Nakamura S, Park YJ, Takano K (2004) Lunar cycles and reproductive activity in reef fishes with particular attention to rabbitfishes. Fish Fish 5:317–328\nDoherty PJ (1983) Diel, lunar and seasonal rhythms in the reproduction of two tropical damselfishes: Pomacentrus flavicauda and P. wardi. Mar Biol 75:215–222\nFoster SA (1987) Diel and lunar patterns of reproduction in the Caribbean and Pacific sergeant major damselfishes Abudefduf saxatilis and A. troschelii. Mar Biol 95:215–222\nCollin PL, Shapiro DY, Weiler D (1987) Aspects of the reproductive of two groupers, Epinephelus guttatus and E. striatus in the West Indies. Bull Mar Sci 40:220–230\nFerreira BP (1995) Reproduction of the common coral trout Plectropomus leopardus (Serranidae: Epinephelinae) from the central and northern Great Barrier Reef, Australia. Bull Mar Sci 56:653–669",{"VOID":984},"10.1007\u002Fs12562-012-0473-9","PUBLICATION","Auto Verify","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs12562-012-0473-9",[989,1005,1018],{"id":990,"sortIndex":32,"researcher":28,"roles":991,"affiliations":993,"properties":1002,"displayName":1004,"givenName":28,"familyName":28},"ee4fe8f3-a6e5-4cdd-8269-0d18d6121882",[992],"AUTHOR",[994],{"id":995,"sortIndex":32,"affiliation":996,"properties":28},"008715ca-c1c4-4a6b-aa61-2128d9ceebe7",{"id":995,"createTime":28,"updateTime":28,"relativeEntities":997,"slug":28,"properties":998,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1001,"statistic":28},[],{"title":999},{"VI":1000},"Korea Ocean Research and Development Institute (KORDI), Seoul, Republic of Korea",[],{"title":1003},{"VI":1004},"Young-Ung Choi",{"id":1006,"sortIndex":40,"researcher":28,"roles":1007,"affiliations":1008,"properties":1015,"displayName":1017,"givenName":28,"familyName":28},"d4ff9c14-138a-46db-837f-f72e22de3300",[992],[1009],{"id":995,"sortIndex":32,"affiliation":1010,"properties":28},{"id":995,"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":1014,"statistic":28},[],{"title":1013},{"VI":1000},[],{"title":1016},{"VI":1017},"Heung-Sik 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Heo","ARTICLE",{"url":987,"publisher":1033,"properties":1075},{"id":868,"createTime":869,"updateTime":870,"relativeEntities":1034,"slug":872,"properties":1035,"entityType":25,"verifyStatus":882,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":32,"subjectFields":1039,"manageAffiliations":1044,"indexDatabases":1055,"url":28,"thumbnailPath":28,"statistic":1070,"gsStatistic":28,"type":55,"analyzePriority":28},[],{"issn":1036,"title":1037,"eissn":1038},{"VOID":877},{"EN":879},{"VOID":875},[1040],{"id":885,"createTime":28,"updateTime":28,"relativeEntities":1041,"label":1042,"description":1043,"parentId":28,"standard":28,"scholarHubFieldId":28},[],{"EN":888},{},[1045,1050],{"id":892,"createTime":28,"updateTime":28,"relativeEntities":1046,"slug":28,"properties":1047,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1049,"statistic":28},[],{"title":1048},{"EN":896},[898],{"id":900,"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},{"EN":904},[898],[1056,1063],{"id":908,"indexDatabase":1057,"url":914,"indexYears":915,"academicFieldIds":1062,"indexDatabaseRanking":918},{"id":775,"createTime":28,"updateTime":28,"relativeEntities":1058,"label":1059,"description":1060,"key":781,"publicationTags":1061,"standard":28},[],{"EN":778,"VI":778},{"EN":778,"VI":780},[783],[917],{"id":920,"indexDatabase":1064,"url":932,"indexYears":28,"academicFieldIds":1069,"indexDatabaseRanking":28},{"id":922,"createTime":28,"updateTime":28,"relativeEntities":1065,"label":1066,"description":1067,"key":929,"publicationTags":1068,"standard":28},[],{"EN":925,"VI":925},{"EN":927,"VI":928},[931,813],[934],{"impactFactor":32,"impactFactorByYear":1071,"i10Index":937,"i10IndexLast5Year":42,"totalPublication":938,"totalPublicationByYear":1072,"totalCitation":944,"totalCitationByYear":1073,"totalCitationPerPublication":955,"totalCitationPerPublicationByYear":1074,"hindexLast5Year":278,"hindex":278},{"2012":109,"2013":168,"2014":121,"2015":318,"2016":320,"2017":318,"2018":52,"2019":118,"2020":524,"2021":524,"2022":681,"2023":113},{"1997":123,"1998":123,"2004":40,"2005":940,"2006":941,"2007":940,"2008":362,"2009":942,"2010":600,"2011":611,"2012":154,"2013":826,"2014":329,"2015":151,"2016":157,"2017":161,"2018":943,"2019":332,"2020":689,"2021":325,"2022":325,"2023":160,"2024":128},{"1997":946,"1998":323,"2004":133,"2005":947,"2006":948,"2007":949,"2008":950,"2009":951,"2010":837,"2011":836,"2012":952,"2013":607,"2014":953,"2015":954,"2016":209,"2017":830,"2018":215,"2019":689,"2020":161,"2021":51,"2022":135,"2023":42,"2024":40},{"1997":957,"1998":49,"2004":133,"2005":958,"2006":959,"2007":960,"2008":465,"2009":637,"2010":961,"2011":962,"2012":963,"2013":237,"2014":193,"2015":964,"2016":175,"2017":965,"2018":344,"2019":286,"2020":585,"2021":121,"2022":696,"2023":106,"2024":165},{"pages":1076,"volume":1078},{"VOID":1077},"515-523",{"VOID":1079},"78","2012-02-19",2012,[918,931],false,{"id":1085,"createTime":1086,"updateTime":1087,"relativeEntities":1088,"slug":1089,"properties":1090,"entityType":985,"verifyStatus":26,"verifyTime":1087,"verifyNote":986,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":1099,"fullTextUrl":28,"authors":1100,"publicationType":1031,"publisherRelationship":1180,"citationCount":28,"citationInfo":28,"publishDate":1228,"publishYear":1229,"citationAnalyzeStatus":882,"lastCitationAnalyze":28,"indexDatabases":1230,"openAccess":28,"references":28,"isForceReanalyzing":1083},"000fef7c-0262-465b-a0bc-d63d6a47db70","2024-02-06T04:14:46.830+00:00","2025-01-23T17:00:34.412+00:00",[],"Effect-of-starvation-on-biochemical-composition-and-gametogenesis-in-the-Pacific-oyster-Crassostrea-gigas",{"abstract":1091,"title":1093,"references":1095,"doi":1097},{"EN":1092},"The effects of starvation on biochemical composition and gametogenesis were investigated in the Pacific oyster Crassostrea gigas. Histological analysis, combined with oocyte examination and measurements of protein, glycogen and lipid levels and RNA\u002FDNA ratio from gonad, adductor muscle and mantle tissue of each sex were performed. In the starved groups, C. gigas showed gonad development, but the progress was delayed during the experiment. Glycogen was the first substrate used by C. gigas for dealing with lack of food. While glycogen was rapidly consumed, protein and lipid contents decreased gradually. A decrease in the RNA\u002FDNA ratio in the starved groups in all the body components was found during starvation, illustrating that RNA\u002FDNA ratio was a valid indicator of nutritional condition in C. gigas. A significant increase in water and ash contents and a corresponding decrease in condition index were observed in the starved groups, showing that the water and ash content and condition index were related to the usage of glycogen, lipid and protein reserves in body composition. During starvation, energy reserves were mobilized for survival and gonad development, but spawning was arrested. The information obtained in this study is useful for broodstock management in the Pacific oyster industry.",{"EN":1094},"Effect of starvation on biochemical composition and gametogenesis in the Pacific oyster Crassostrea gigas",{"VOID":1096},"Dridi S, Romdhane MS, Elcafsi M (2007) Seasonal variation in weight and biochemical composition of the Pacific oyster, Crassostrea gigas in relation to the gametogenic cycle and environmental conditions of the Bizert lagoon, Tunisia. Aquaculture 263:238–248\nBayne BL (1976) Aspects of reproduction in bivalve molluscs. In: Wiley ML (ed) Estuarine processes. Academic Press, New York\nLiu WG, Li Q, Yuan YD, Zhang SH (2008) Seasonal variations in reproductive activity and biochemical composition of the Cockle Fulvia mutica (Reeve) from eastern coast of China. J Shellfish Res 27:1–7\nTaylor AC, Venn TJ (1979) Seasonal variation in weight and biochemical composition of the tissues of the queen scallop Chlamys opercularis from the Clyde sea area. J Mar Biol Assoc UK 59:605–621\nBarber BJ, Blake NJ (1981) Energy storage and utilization in relation to gametogenesis in Argopecten irradians concentricus (Say). J Exp Mar Biol Ecol 52:121–134\nMartinez G (1991) Seasonal variation in biochemical composition of three size classes of the Chilean scallop Argopecten purpuratus Lamarck, 1819. Veliger 34:335–343\nThompson RJ (1977) Blood chemistry, biochemical composition, and the annual reproductive cycle in the giant scallop, Placopecten magellanicus, from southeast Newfoundland. J Fish Res Board Can 34:2104–2116\nFAO (2008) World aquaculture production of fish, crustaceans, molluscs, etc., by principal species. FAO, Rome\nDOF (Department of Fisheries) (2007) China fisheries statistic yearbook. China Agriculture Press, Beijing\nPernet F, Bricelj VM, Cartier S (2006) Lipid class dynamics during larval ontogeny of sea scallops, Placopecten magellanicus, in relation to metamorphic success and response to antibiotics. J Exp Mar Biol Ecol 329:265–280\nPernet F, Tremblay R, Langdon C, Bourget E (2004) Effect of additions of dietary triacylglycerol microspheres on growth, survival, and settlement of mussel (Mytilus sp.) larvae. Mar Biol 144:693–703\nPronker AE, Nevejan NM, Peene F, Geijsen P, Sorgeloos P (2008) Hatchery broodstock conditioning of the blue mussel Mytilus edulis (Linnaeus 1758). Part I. Impact of different micro-algae mixtures on broodstock performance. Aquacult Int 16:297–307\nKang CK, Park MS, Lee PY, Choi WJ, Lee WC (2000) Seasonal variations in condition, reproductive activity, and biochemical composition of the oyster, Crassostrea gigas (Thunberg), in suspended culture in two coastal bays of Korea. J Shellfish Res 19:771–778\nRuiz C, Abad M, Sedano F, Garcia-Martin LO, López JLS (1992) Influence of seasonal environmental changes on the gamete production and biochemical composition of Crassostrea gigas (Thunberg) in suspended culture in El Grove, Galicia, Spain. J Exp Mar Biol Ecol 155:249–262\nRen JS, Marsden ID, Ross AH, Schiel DR (2003) Seasonal variation in the reproductive activity and biochemical composition of the Pacific oyster (Crassostrea gigas) from the Marlborough Sounds, New Zealand. N Z J Mar Freshw Res 37:171–182\nStephen D (1980) The reproductive biology of the Indian oyster Crassotrea madrasensis (Preston). II. Gametogenic cycle and biochemical levels. Aquaculture 21:147–153\nFolch J, Lees M, Stanley-Sloane GH (1957) A simple method for the isolation purification of total lipids from animal tissues. J Biol Chem 226:497–507\nHorikoshi H (1958) Glycogen (in Japanese). Chem Field 34:36–39\nNakano H (1988) Techniques for studying on the early life history of fishes (in Japanese). Aquabiology 10:23–26\nWalne PR (1976) Experiments on the culture in the sea of the butterfish Venerupis decussata L. Aquaculture 8:371–381\nDinamani P (1987) Gametogenic patterns in populations of Pacific oyster Crassostrea gigas in Northland, New Zealand. Aquaculture 64:65–76\nAlbentosa MM, Fernández-Reiriz J, Labarta U, Pérez-Camacho A (2007) Response of two species of clams, Ruditapes decussatus and Venerupis pullastra, to starvation: physiological and biochemical parameters. Comp Biochem Physiol B 146:241–249\nLi Y, Qin JG, Li XX, Benkendorff K (2009) Spawning-dependent stress response to food deprivation in Pacific oyster Crassostrea gigas. Aquaculture 286:309–317\nCarefoot TH, Qian PY, Taylor BE, West T, Osborne J (1993) Effect of starvation on energy reserves and metabolism in the Northern abalone, Haliotis kamtschatkana. Aquaculrure 118:315–325\nLaing I (1993) The response of Manila clam, Tapes phillippinarum, juveniles to nutritive stress. J Exp Mar Biol Ecol 173:111–121\nLane JM (1986) Allometric and biochemical studies on starved and unstarved clams, Rangza Cuneata (Sowerby, 1831). J Exp Mar Biol Ecol 95:131–143\nLi Q, Osada M, Mori K (2000) Seasonal biochemical variations in Pacific oyster gonadal tissue during sexual maturation. Fish Sci 66:502–508\nBeninger PG, Lucas A (1984) Seasonal variations in condition, reproductive activity, and gross biochemical composition of two species of adult clam reared in a common habitat: Tapes decussatus L. (Jeffreys) and Tapes philippinarum (Adams & Reeve). J Exp Mar Biol Ecol 79:19–37\nSánchez-Paz A, García-Carreño F, Hernández-López J, Muhlia-Almazan A, Yepiz-Plascencia G (2007) Effect of short-term starvation on hepatopancreas and plasma energy reserves of the Pacific white shrimp (Litopenaeus vannamei). J Exp Mar Biol Ecol 340:184–193\nRiley RT (1976) Changes in the total protein, lipid, carbohydrate, and extracellular body fluid free amino acids of the Pacific oyster Crassostrea gigas, during starvation. Proc Natl Shellfish Assoc 65:84–90\nDu SB, Mai KS (2004) Effects of starvation on energy reserves in young juveniles of abalone Haliotis discus hannai Ino. J Shellfish Res 23:1037–1039\nCaers M, Coutteau P, Sorgeloos P (2000) Impact of starvation and of feeding algal and artificial diets on the lipid content and composition of juvenile oysters (Crassostrea gigas) and clams (Tapes philippinarum). Mar Biol 136:891–899\nRiley RT (1980) The effect of prolonged starvation on the relative free amino acid composition of the extracellular body fluids and protein bound amino acids in the oyster, Crassostrea gigas. Comp Biochem Physiol A 67:279–281\nWagner M, Durbin E, Buckley L (1998) RNA:DNA ratios as indicators of nutritional condition in the copepod Calanus fimarchicus. Mar Ecol Progr Ser 162:173–181\nVidal ÉAG, DiMarco P, Lee P (2006) Effects of starvation and recovery on the survival, growth and RNA\u002FDNA ratio in loliginid squid paralarvae. Aquaculture 260:94–105\nClemmesen C (1994) The effect of food availability, age or size on the RNA\u002FDNA ratio of individually measured herring larvae: laboratory calibration. Mar Biol 118:377–382\nWright DA, Hetzel EW (1985) Use of RNA:DNA ratios as an indicator of nutritional stress in the American oyster Crassostrea virginica. Mar Ecol Progr Ser 25:199–206\nFerron A, Leggett WC (1994) An appraisal of condition measures for marine fish larvae. In: Blaxter JHS, Southward AJ (eds) Advances in marine biology. Academic Press, London\nWhyte JNC, Englaf JR, Carswell BL (1990) Biochemical composition and energy reserves in Crassostrea gigas exposed to different levels of nutrition. Aquaculture 90:157–172",{"VOID":1098},"10.1007\u002Fs12562-010-0274-y","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs12562-010-0274-y",[1101,1116,1140,1160],{"id":1102,"sortIndex":32,"researcher":28,"roles":1103,"affiliations":1104,"properties":1113,"displayName":1115,"givenName":28,"familyName":28},"85ed1689-c7c2-4598-a8cc-b9eb34a95e93",[992],[1105],{"id":1106,"sortIndex":32,"affiliation":1107,"properties":28},"3888d32f-6f1c-42a9-aa82-f8ef09eca532",{"id":1106,"createTime":28,"updateTime":28,"relativeEntities":1108,"slug":28,"properties":1109,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1112,"statistic":28},[],{"title":1110},{"EN":1111},"Key Laboratory of Marine Bio-resources Sustainable Utilization, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou, China",[],{"title":1114},{"VI":1115},"Wenguang 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a dult maturing and immature female Japanese flounder Paralichthys olivaceus were collected in June 2004 and January 2005, respectively, to clarify a possible role of gonadotropin-releasing hormones (GnRHs) in reproduction. Levels of salmon GnRH (sGnRH), chicken GnRH-II (cGnRH-II) and sea bream GnRH (sbGnRH) in the brain and pituitary were examined by time-resolved fluoroimmunoassay. Three forms of GnRHs were detected in the discrete brain at various levels. In the pituitary of both maturing and immature fish, sbGnRH was abundant together with a pronounced amount of sGnRH, whereas cGnRH-II was almost below the detectable limit. In maturing fish, levels of sbGnRH were high in the telencephalon, hypothalamus and pituitary, while levels of sbGnRH of immature fish were very low in these regions. These results indicate that sbGnRH is mainly responsible for gonadotropin secretion, and that sb GnRH in the anterior part of the brain is associated with gonadal maturation in the Japanese flounder.",{"EN":1241},"Distribution of three GnRHs in the brain and pituitary of the wild Japanese flounder Paralichthys olivaceus",{"VOID":1243},"Lethimonier C, Madigou T, Munoz-Cueto JA, Lareyre JJ, Kah O. Evolutionary aspects of GnRHs, GnRH neuronal systems and GnRH receptors in teleost fish. Gen. Comp. Endocrinol. 2004; 135: 1–16.\nSherwood NM. Three forms of gonadotropin-releasing hormone characterized from brains of one species. Proc. Natl. Acad. Sci. U.S.A. 1994; 91: 12081–12085.\nYu KL, Sherwood NM Peter RE. Differential distribution of two molecular forms of gonadotropin-releasing hormone in discrete brain areas of goldfish, Carassius auratus. Peptides 1988; 9: 625–630.\nOkuzawa K, Amano M, Kobayashi M, Aida K, Hanyu I, Hasegawa Y, Miyamoto K. Differences in salmon GnRH and chicken GnRH-II contents in discrete brain areas of male and female rainbow trout according to age and stage of maturity. Gen. Comp. Endocrinol. 1990; 80: 116–126.\nAmano M, Oka Y, Aida K, Okumoto N, Kawashima S, Hasegawa Y. Immunocytochemical demonstration of salmon GnRH and chicken GnRH-II in the brain of masu salmon. Oncorhynchus masou. J. Comp. Neurol. 1991; 314: 587–597.\nPowell JFF, Zohar Y, Elizur A, Park M, Fischer WH, Craig AG, Rivier JE, Lovejoy DA, Sherwood NM. Three forms of gonadotropin-releasing hormone characterized from brains of one species. Proc. Natl. Acad. Sci. U.S.A. 1994; 91: 12081–12085.\nWhite SA, Kasten TL, Bond CT, Adelman JP, Fernald RD. Three gonadotropin-releasing hormone genes in one organism suggest novel roles for an ancient peptide. Proc. Natl. Acad. Sci. U.S.A. 1995; 92: 8363–8367.\nPowell JFF, Standen EM, Carolsfeld J, Borella MI, Gazola R, Fischer WH, Park M, Craig AG, Warby CM, Rivier JE, Val-Sella MV, Sherwood NM. Primary structure of three forms of gonadotropin-releasing hormone (GnRH) from the pacu brain. Regul. Pept. 1997; 68: 189–195.\nChow MM, Kight KE, Gothilf Y, Alok D, Stubblefield J. Zohar Y. Multiple GnRHs present in a teleost species are encoded by separate genes: analysis of the sbGnRH and cGnRH-II genes from the striped bass, Morone saxatilis. J. Mol. Endocrinol. 1998; 21: 277–289.\nSenthilkumaran B, Okuzawa K, General K, Ookura T, Kagawa H. Distribution and seasonal variations in levels of three native GnRHs in the brain and pituitary of perciform fish. J. Neuroendocrinol. 1999; 11: 181–186.\nGonzález-Martínez D, Zmora N, Anglade I, Madigou T, Zanuy S, Muñoz-Cueto JA, Zohar Y, Elizur A, Kah O. Differential expression of three GnRH forms in the brain of the sea bass (Dicentrarchus labrax): An in situ hybridisation study. Proceedings of the 6th International Symposium on Reproductive Physiology of Fish, University of Bergen, Norway, 2000.\nAnderson E, Fjelldal, PG, Klenke U, Vikingstad E, Taranger GL, Zohar Y, Stefansson SO. Three forms of GnRH in the brain and pituitary of the turbot, Scophthalmus maximus: immunological characterization and seasonal variation. Comp. Biochem. Physiol. B. Biochem. Mol. Biol. 2001; 129: 551–558.\nAmano M, Oka Y, Yamanome T, Okuzawa K, Yamamori K. Three GnRH systems in the brain and pituitary of a pleuronectiform fish, the barfin flounder, Verasper moseri. Cell Tissue Res. 2002; 309: 323–329.\nCarolsfeld J, Powell JF, Park M, Fischer WH, Craig AG, Chang JP, Rivier JE, Sherwood NM. Primary structure and function of three gonadotropin-releasing hormones, including a novel form, from an ancient teleost, herring. Endocrinology 2000; 141: 505–512.\nOkubo K, Amano M, Yoshiura Y, Suetake H, Aida K. A novel form of gonadotropin-releasing hormone in the medaka, Oryzias latipes. Biochem. Biophys. Res. Commun. 2000; 276: 298–303.\nAdams BA, Vickers ED, Warby C, Park M, Fischer WH, Grey Craig A, Rivier JE, Sherwood NM. Three forms of gonadotropin-releasing hormone, including a novel form, in a basal salmonid, Coregonus clupeaformis. Biol. Reprod. 2002; 67: 232–239.\nHolland MC, Gothilf Y, Meiri I, King JA, Okuzawa K, Elizur A, Zohar Y. Levels of the native forms of GnRH in the pituitary of the gilthead seabream, Sparus aurata, at several characteristic stages of the gonadal cycles. Gen. Comp. Endocrinol. 1998; 112: 394–405.\nRodriguez L, Carrillo M, Sorbera LA, Soubrier MA, Mananos E, Holland MC, Zohar Y, Zanuy S. Pituitary levels of three forms of GnRH in the male European sea bass (Dicentrarchus labrax, L.) during sex differentiation and first spawning season. Gen. Comp. Endocrinol. 2000; 120: 67–74.\nHolland MC, Hassin S, Zohar Y. Seasonal fluctuations in pituitary levels of the three forms of gonadotropin-releasing hormone in striped bass, Morone saxatilis (Teleostei), during juvenile and pubertal development. J. Endocriol.. 2001; 169: 527–538.\nOkuzawa K, Kobayashi M. Gonadotropin-releasing hormone neuronal systems in the teleostean brain and functional significance. In: Prasada Rao PD, Peter RE (eds). Neural Regulation in the Vertebrate Endocrine System. Kluwer Academic\u002FPlenum Publishers, New York. 1999; 85–100.\nMinami T. The early life history of Japanese flounder Paralichthys olivaceus. Nippon Suisan Gakkaishi 1982; 48: 1551–1588.\nFujii T, Sudo H, Azeta M, Tanaka M. Settling process of larvae and juveniles of Japanese flounder Paralichthys olivaceus in Shijiki Bay, Hirado Island. Nippon Suisan Gakkaisi 1989; 55: 17–23.\nTanaka M, Goto T, Tomiyama M, Sudo H. Immigration, settlement and mortality of flounder Paralichthys olivaceus larvae and juveniles in a nursery ground, Shijiki Bay, Japan. Neth. J. Sea. Res.. 1989; 24: 57–67.\nOkuzawa K, Amano M, Aida K, Hasegawa Y, Tanaka H, Kagawa H. Chromatographic and immunological identification of gonadotropin-releasing hormone in five marine teleosts. Fish Physiol. Biochem. 1993; 12: 337–345.\nKajimura S, Yoshiura Y, Suzuki M, Aida K. cDNA cloning of two gonadotropin β subunits (GTH-Iβ and GTH-IIβ) and their expression profiles during gametogenesis in the Japanese flounder, Paralichthys olivaceus. Gen. Comp. Endocrinol. 2001; 122: 117–129.\nMatsuyama M, Yoneda M, Takeuchi H, Kagawa H, Kashiwagi M, Tabata K, Nagahama Y, Ijiri S, Yamauchi K. Diurnal periodicity in testicular activity in the Japanese flounder Paralichthys olivaceus. Fish. Sci. 1995; 61: 17–23.\nYamamoto E. Studies on sex-manipulation and production of cloned populations in hirame flounder, Paralichthys olivaceus (Temminck et Schlegel). Bull. Tottori. Pref. Fish. Exp. Stn. 1995; 34: 1–145.\nYamada H, Amano M, Okuzawa K, Chiba H, Iwata M. Maturational changes in brain contents of salmon GnRH in rainbow trout as measured by a newly developed timeresolved fluoroimmunoassay. Gen. Comp. Endocrinol. 2002; 126: 136–143.\nAmano M, Yamanome T, Yamada H, Okuzawa K, Yamamori K. Effects of photoperiod on gonadotropin-releasing hormone levels in the brain and pituitary of underyearling male barfin flounder. Fish. Sci. 2004; 70: 812–818\nZohar Y, Elizur A, Sherwood NM, Powell JF, Rivier JE, Zmora, N. Gonadotropin-releasing activities of the three native forms of gonadotropin-releasing hormone present in the brain of gilthead seabream, Sparus aurata. Gen. Comp. Endocrinol., 1995; 97: 289–299.\nForniés MA, Carrillo M, Mañanós E, Sorbera LA, Zohar Y, Zanuy S. Relative potency of the forms of GnRH and their analogs on LH release in sea bass. J. Fish. Biol. 2003; 63: 73–89.\nSchulz RW, Bosma PT, Zandbergen MA, Van der Sanden MC, Van Dijk W, Peute J, Bogerd J, Goos HJT. Two gonadotropin-releasing hormones in the African catfish, Clarias gariepinus: localization, pituitary receptor binding, and gonadotropin releasing activity. Endocrinology, 1993; 133: 1569–1577.\nAmano M, Aida K, Okumoto N, Hasegawa Y. Changes in salmon GnRH and chicken GnRH-II contents in the brain and pituitary, and GTH contents in the pituitary in female masu salmon, Oncorhynchus masou, from hatching through oyulation. Zool. Sci. 1992; 9: 375–386.\nOka Y. GnRH neuronal system of fish brain as a model system for the study of peptidergic neuromodulation. In: Parhar IS, Sakuma Y (eds). GnRH Neurons: Gene to Behavior. Brain Shuppan, Tokyo, 1997; 245–276.",{"VOID":1245},"10.1111\u002Fj.1444-2906.2006.01121.x","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1111\u002Fj.1444-2906.2006.01121.x",[1248,1263,1276,1289,1304],{"id":1249,"sortIndex":32,"researcher":28,"roles":1250,"affiliations":1251,"properties":1260,"displayName":1262,"givenName":28,"familyName":28},"bb3989d6-ae48-4821-b64f-6b0d8050539b",[992],[1252],{"id":1253,"sortIndex":32,"affiliation":1254,"properties":28},"8250795e-05fd-4273-8041-acdabe020c1e",{"id":1253,"createTime":28,"updateTime":28,"relativeEntities":1255,"slug":28,"properties":1256,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1259,"statistic":28},[],{"title":1257},{"VI":1258},"School of Fisheries Sciences, Kitasato University, Ofunato, Iwate, Japan",[],{"title":1261},{"VI":1262},"Ky Xuan 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investigate the effect of oxidative stress on the survival of two Brachionus species of rotifer, we examined the effective dose of juglone, which generates reactive oxygen species, and compared survival times between the two species. First, we observed that juglone affected survival in the rotifers in a dose-dependent manner between 0.02 to 20 μM, and that treatment at above 2 μM showed acute toxicity causing the animals to die within a few hours. Next, we found the difference in survival time between the two species exposed to 20 μM juglone: B. rotundiformis was significantly more tolerant against the substance than the allied species B. plicatilis. The findings suggest that exploring the basis of species-specific abilities to persist under oxidative stress will be of great interest to uncover the underlying mechanisms governing the stress resistance of the rotifer, as well as contributing to their stable mass production for aquaculture.",{"EN":1376},"Effect of juglone on the survival time of two Brachionus species (Rotifera): species-specific tolerance against oxidative stress",{"VOID":1378},"Hagiwara A, Gallardo WG, Assavaaree M, Kotani T, de Araujo AB (2001) Live food production in Japan: recent progress and future aspects. Aquaculture 200:111–127\nYoshinaga T, Kaneko G, Kinoshita S, Tsukamoto K, Watabe S (2003) The molecular mechanisms of life history alterations in a rotifer: a novel approach in population dynamics. Comp Biochem Physiol (B) 136:715–722\nGuarente L, Kenyon C (2000) Genetic pathways that regulate ageing in model organisms. Nature 408:255–262\nKaneko G, Yoshinaga T, Kinoshita S, Yanagawa Y, Tsukamoto K, Watabe S (2005) Molecular characterization of Mn-superoxide dismutase and gene expression studies in dietary restricted Brachionus plicatilis rotifers. Hydrobiologia 546:117–123\nYoshinaga T, Kaneko G, Kinoshita S, Furukawa S, Tsukamoto K, Watabe S (2005) Insulin-like signaling pathway may involved in regulating longevity of rotifer. Hydrobiologia 546:347–352\nHonda Y, Honda S (1999) The daf-2 gene network for longevity regulates oxidative stress resistance and Mn-superoxide dismutase gene expression in Caenorhabditis elegans. FASEB J 13:1385–1393\nFinkel T, Holbrook NJ (2000) Oxidants, oxidative stress and the biology of ageing. Nature 408:239–247\nMallavadhani UV, Panda AK, Rao YR (1998) Pharmacology and chemotaxonomy of Diospyros. Phytochemistry 49:901–951\nDe Castro E, De Castro SH, Johnson TE (2004) Isolation of long-lived mutants in Caenorhabditis elegans using selection for resistance to juglone. Free Rad Biol Med 37:139–145\nPrzybysz AJ, Choe KP, Strange K, Roberts LJ (2007) Ageing inhibits the adaptive response of Caenorhabditis elegans to the reactive oxygen species-generating compound juglone. Free Rad Biol Med 43:158\nCypser JR, Johnson TE (2002) Multiple stressors in Caenorhabditis elegans induce stress hormesis and extended longevity. J Gerontol 57:109–114\nKampkötter A, Volkmann TE, de Castro SH, Leiers B, Klotz L-O, Johnson TE, Link CD, Henkle-Dührsen K (2003) Functional analysis of the glutathione S-transferase 3 from Onchocerca volvulus (Ov-GST-3): a parasite GST confers increased resistance to oxidative stress in Caenorhabditis elegans. J Mol Biol 325:25–37\nYoshinaga T, Hagiwara A, Tsukamoto K (1999) Effect of conditioned media on the asexual reproduction of the monogonont rotifer Brachionus plicatilis O. F. Müller. Hydrobiologia 412:103–110\nYoshinaga T, Minegishi Y, Rumengan IFM, Kaneko G, Furukawa S, Yanagawa Y, Tsukamoto K, Watabe S (2004) Molecular phylogeny of the rotifers with two Indonesian Brachionus lineages. Coast Mar Sci 29:45–56\nHennig L, Christner C, Kipping M, Schelbert B, Rucknagel KP, Grabley S, Kullertz G, Fischer G (1998) Selective inactivation of parvulin-like peptidyl-prolyl cist\u002Ftrans isomerases by juglone. Biochemistry 37:5953–5960\nChao SH, Greenleaf AL, Price DH (2001) Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription. Nuc Acids Res 29:767–773\nHagiwara A, Kotani T, Snell TW, Assavaaree M, Hirayama K (1995) Morphology, reproduction, genetics and mating behavior of small, tropical marine rotifer Brachionus strains (Rotifera). J Exp Mar Biol Ecol 194:25–37\nHagiwara A, Suga K, Akazawa A, Kotani T, Sakakura Y (2007) Development of rotifer strains with useful traits for rearing fish larvae. Aquaculture 268:44–52\nGallardo WG, Tomita Y, Hagiwara A, Soyano K, Snell TW (1997) Effect of dimethysulfoxide (DMSO), sodium hydroxide (NaOH), acetone, and ethanol on the population growth, mictic female production, and body size of the rotifer Brachionus plicatilis Muller. Bull Fac Fish Nagasaki Univ 78:15–22",{"VOID":1380},"10.1007\u002Fs12562-008-0009-5","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs12562-008-0009-5",[1383,1398,1411,1424],{"id":1384,"sortIndex":32,"researcher":28,"roles":1385,"affiliations":1386,"properties":1395,"displayName":1397,"givenName":28,"familyName":28},"08fb9089-edfa-4f54-8ca9-ec65b429cd36",[992],[1387],{"id":1388,"sortIndex":32,"affiliation":1389,"properties":28},"e11aeaf3-0d00-4a39-9b2b-8757f1aa5f17",{"id":1388,"createTime":28,"updateTime":28,"relativeEntities":1390,"slug":28,"properties":1391,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1394,"statistic":28},[],{"title":1392},{"EN":1393},"School of Marine Biosciences, Kitasato University, Ofunato, Japan",[],{"title":1396},{"VI":1397},"Chikaya 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study assessed the stock-recruitment relationship (SRR) for the Japanese sardine Sardinops melanostictus in the North-western Pacific. Of the 20 SRR models investigated, the Akaike information criterion (AIC) was the minimum (AIC=551.2) when the data were separated into two groups (A and B) and the log-normal distribution was applied as the error term. Group A was constructed with SRR data from 1976–1987 and 1992–2004. Group B consisted of data from 1988–1991. The AIC minimum model was R=22.8 S × eε for Group A, where R, S, and ε denote the recruitment of sardine (individual number of 0-year old fish), spawning stock biomass (SSB), and error term, respectively. This model indicated that recruitment was proportional to the SSB and that no density-dependent effect operated over the range of SSB investigated (51000–11.3 million t). Recruitment was markedly higher (lower) when the sea surface temperature (SST) of the Kuroshio Extension area in February was low (high). The essential SRR can simply be expressed as R=22.8 S × e\n                ε with the level of recruitment deviating from the model to a greater or lesser degree depending on the environmental conditions.",{"EN":1498},"Proposal for stock-recruitment relationship for Japanese sardine Sardinops melanostictus in North-Western Pacific",{"VOID":1500},"Zenitani H, Ishida M, Konishi Y, Goto T, Watanabe Y, Kimura R (eds) Distributions of eggs and larvae of Japanese sardine, Japanese anchovy, mackerels, round herring, Japanese horse mackerel, and Japanese common squid in waters around Japan, 1991 through 1993. National Research Institute of Fisheries Science, Kanagawa. 1995; 1–368.\nKubota H, Oozeki Y, Ishida M, Konishi Y, Goto T, Zenitani H, Kimura R (eds) Distributions of eggs and larvae of Japanese Sardine, Japanese anchovy, mackerels, round herring, jack mackerel and Japanese common squid in the waters around Japan, 1994 through 1996. National Research Institute of Fisheries Science, Kanagawa. 1999: 1–352.\nSugisaki H, Matsuo Y, Yokouchi K, Takahashi Y. Distribution of larvae and juveniles of Japanese sardine Sardinops melanostictus off the east coast of Honshu Island, Japan. Bull. Jpn. Soc. Fish. Oceanogr. 1994; 58: 336–338.\nKuroda K. Studies on the recruitment process focusing on the early life history of the Japanese sardine Sardinops melanostictus (SCHLEGEL). Bull. Natl. Res. Inst. Fish. Sci. 1991; 3: 25–278.\nSakuramoto K. How to manage pelagic fish when its stock size is low. Mar. Sci. Monthly 2006; 38: 231–235.\nJacobson LD, MacCall AD. Stock-recruitment models for Pacific sardine Sardinops sagax. Can. J. Fish. Aquat. Sci. 1995; 52: 566–577.\nNoto M, Yasuda I. Population decline of the Japanese sardine in relation to sea surface temperature in the Kuroshio Extension. Can. J. Fish. Aquat. Sci. 1999; 56: 973–983.\nWada T, Jacobson LD. Regime and stock-recruitment relationships in Japanese sardine Sardinops melanostictus, 1951–1995. Can. J. Fish. Aquat. Sci. 1998; 55: 2445–2463.\nRicker WE. Stock and recruitment. J. Fish. Res. Bd. Can. 1995; 11: 559–623.\nBeverton RJH, Holt SJ. On the dynamics of exploited fish populations. Fish. Invest. U. K. Ser. II 1957; 19: 43–75.\nSakuramoto K. Does the Ricker or Beverton and Holt type of stock-recruitment relationship truly exist? Fish. Sci. 2005; 71: 577–592.\nNishida H, Yatsu A, Ishida M, Noto M, Katsukawa Y. Stock assessment and evaluation for Pacific stock of sardine (fiscal year 2005). In: Nishida H, Yatsu A, Ishida M, Noto M, Katsukawa Y (eds). Marine fisheries stock assessment and evaluation for Japanese waters (fiscal year 2005\u002F2006). Fisheries Agency and Fisheries Research Agency of Japan, Tokyo. 2006; 11–45.",{"VOID":1502},"10.1111\u002Fj.1444-2906.2007.01433.x","http:\u002F\u002Flink.springer.com\u002F10.1111\u002Fj.1444-2906.2007.01433.x",[1505,1520,1535],{"id":1506,"sortIndex":32,"researcher":28,"roles":1507,"affiliations":1508,"properties":1517,"displayName":1519,"givenName":28,"familyName":28},"7b486d32-1bd7-4482-8140-a994bdbdf54a",[992],[1509],{"id":1510,"sortIndex":32,"affiliation":1511,"properties":28},"29b945b0-eb09-4e15-81d1-976f37c610bc",{"id":1510,"createTime":28,"updateTime":28,"relativeEntities":1512,"slug":28,"properties":1513,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1516,"statistic":28},[],{"title":1514},{"VI":1515},"Survey Research Center Co., Ltd., Arakawa, Tokyo, Japan",[],{"title":1518},{"VI":1519},"Satomi 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digestion by Corbicula japonica was investigated according to the hypothesis that without any symbiotic aid, this organism can utilize cellulose as a carbon source. Enzymatic studies revealed the complete cellulase activity of this species, and molecular cloning resulted in the isolation of cDNA with an ORF encoding a 596-amino-acid protein that shares significant homology with abalone and termite cellulases with an amino acid identity of 52.2% and 50.5%, respectively. The isolated cellulase had a carbohydrate-binding module at the N-terminal region that was also reportedly present in abalone cellulase, and its mRNA were specifically expressed in the digestive gland. These findings strongly support the assumption that C. japonica has an endogenous cellulose, as well as abalones and termites. It is further believed that C. japonica plays an important roll in decomposing cellulose, and consequently contributes to the carbon-cycle in the aquatic environment, as termites do in terrestrial forests.",{"EN":1609},"Cellulose digestion by common Japanese freshwater clam Corbicula japonica",{"VOID":1611},"Tomme P, Warren RA, Gilkes NR. Cellulose hydrolysis by bacteria and fungi. Adv. Microb. Physiol. 1995; 37: 1–81.\nPesis E, Fuchs Y, Zauberman G. Cellulase activity and fruit softening in avocado. Plant Physiol. 1978; 61: 416–419.\nPotts RC, Hewitt PH. Distribution of intestinal bacteria and cellulase activity in harvester termite Trinervitermes-Trinervoides (Nasutitermitinae). Insectes Sociaux 1973; 20: 215–220.\nMarshall JJ. Purification of α-1,4-glucan hydrolase (cellulase) from the snail, Helix pomatia. Comp. Biochem. Physiol. B 1973; 44: 981–988.\nWatanabe H, Tokuda G. Animal cellulases. Cell. Mol. Life Sci. 2001; 58: 1167–1178.\nSmant G, Stokkermans JP, Yan Y, de Boer JM, Baum TJ, Wang X, Hussey RS, Gommers FJ, Henrissat B, Davis EL, Helder J, Schots A, Baker J. Endogenous cellulases in animals: isolation of beta-1, 4-endoglucanase genes from two species of plant-parasitic cyst nematodes. Proc. Natl. Acad. Sci. USA 1998; 95: 4906–4911.\nMatthysse AG, Deschet K, Williams M, Marry M, White AR, Smith WC. A functional cellulose synthase from ascidian epidermis. Proc. Natl Acad. Sci. USA 2004; 101: 986–991.\nXu B, Janson JC, Sellos D. Cloning and sequencing of a molluscan endo-beta-1,4-glucanase gene from the blue mussel, Mytilus edulis. Eur. J. Biochem. 2001; 268: 3718–3727.\nWang J, Ding M, Li YH, Chen QX, Xu GJ, Zhao FK. Isolation of a multi-functional endogenous cellulase gene from mollusc, Ampullaria crossean. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 2003; 35: 941–946.\nWatanabe H, Noda H, Tokuda G, Lo N. A cellulase gene of termite origin. Nature 1998; 394: 330–331.\nDavison A, Blaxter M. Ancient origin of glycosyl hydrolase family 9 cellulase genes. Mol. Biol. Evol. 2005; 22: 1273–1284.\nSugimura M, Watanabe H, Lo N, Saito H. Purification, characterization, cDNA cloning and nucleotide sequencing of a cellulase from the yellow-spotted longicorn beetle, Psacothea hilaris. Eur. J. Biochem. 2003; 270: 3455–3460.\nSuzuki K, Ojima T, Nishita K. Purification and cDNA cloning of a cellulase from abalone Haliotis discus hannai. Eur. J. Biochem. 2003; 270: 771–778.\nDonald SM, Michael E. The Estuarine Ecosystem, Ecology. Threats and Management. Oxford University Press, Oxford 2004.\nBrock V, Kennedy VS. Quantitative-analysis of crystalline style carbohydrases in 5 suspension-feeding and deposit-feeding bivalves. J. Exp. Mar. Biol. Ecol. 1992; 159: 51–58.\nXu B, Hellman U, Ersson B, Janson JC. Purification, characterization and amino-acid sequence analysis of a thermostable, low molecular mass endo-beta-1,4-glucanase from blue mussel, Mytilus edulis. Eur.. J. Biochem. 2000; 267: 4970–4977.\nGosling E. Bivalve Mollusc Biology, Ecology and Culture. Blackwell Publishing, Oxford, 2003.\nNakamura M. Corbicula Fisheries in Japan. Tatara Shobo, Yonago. 2000 (in Japanese).\nFry B, Sherr EB. Delta-C-13 measurements as indicators of carbon flow in marine and fresh-water ecosystems. Contrib. Mar. Sci. 1984; 27: 13–47.\nKasai A, Nakata A. Utilization of terrestrial organic matter by the bivalve Corbicula japonica estimated from stable isotope analysis. Fish. Sci. 2005; 71: 151–158.\nBeguin P. Detection of cellulase activity in polyacrylamide gels using Congo red-stained agar replicas. Anal. Biochem. 1983; 131: 333–336.\nBradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976; 72: 248–254.\nJue CK, Lipke PN. Determination of reducing sugars in the nanomole range with tetrazolium blue. J. Biochem. Biophys. Methods 1985; 11: 109–115.\nByrne KA, Lehnert SA, Johnson SE, Moore SS. Isolation of a cDNA encoding a putative cellulase in the red claw crayfish Cherax quadricarinatus. Gene 1999; 239: 317–324.\nSakon J, Irwin D, Wilson DB, Karplus PA. Structure and mechanism of endo\u002Fexocellulase E4 from Thermomonospora fusca. Nat. Struct. Biol. 1997; 4: 810–818.\nSambrook J, David WR. Molecular Cloning: A Laboratory Manual. 3rd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 1989.\nTomme P, Chauvaux S, Beguin P, Millet J, Aubert JP, Claeyssens M. Identification of a histidyl residue in the active center of endoglucanase D from Clostridium thermocellum. J. Biol. Chem. 1991; 266: 10313–10318.\nTomme P, van Beeumen J, Claeyssens M. Modification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum. Biochem. J. 1992; 285: 319–324.\nvon Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 1986; 14: 4683–4690.\nSimpson PJ, Xie H, Bolam DN, Gilbert HJ, Williamson MP, The structural basis for the ligand specificity of family 2 carbohydrate-binding modules. J. Biol. Chem. 2000; 275: 41137–41142.\nKleman-Leyer KM, Siika-Aho M, Teeri TT, Kirk TK. The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synergistically to solubilize native cotton cellulose but not to decrease its molecular size. Appl. Environ. Microbiol. 1996; 62: 2883–2887.\nMartin MM. The evolution of cellulose digestion in insects. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 1991; 333: 281–288.",{"VOID":1613},"10.1111\u002Fj.1444-2906.2007.01381.x","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1111\u002Fj.1444-2906.2007.01381.x",[1616,1631,1646,1659,1672],{"id":1617,"sortIndex":32,"researcher":28,"roles":1618,"affiliations":1619,"properties":1628,"displayName":1630,"givenName":28,"familyName":28},"80d272dc-dfec-465e-ac9a-070134ee2a84",[992],[1620],{"id":1621,"sortIndex":32,"affiliation":1622,"properties":28},"88076f2d-45ae-48f2-8ba4-2f19d7d0465c",{"id":1621,"createTime":28,"updateTime":28,"relativeEntities":1623,"slug":28,"properties":1624,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1627,"statistic":28},[],{"title":1625},{"VI":1626},"Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan",[],{"title":1629},{"VI":1630},"Kentaro 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was extracted from several tissues (muscle, skin, bone, alimentary tract, gill, fin, hepatopancreas, and air bladder) of the tiger pufferfish Takifugu rubripes, and the content and solubility of the collagen extracted from each tissue were examined. Collagen content in ordinary muscle was 0.95 ± 0.07 % of wet tissue, which is lower than that reported for other fish species even though tiger pufferfish meat has a tough texture. The solubility of collagen extracted from the muscle and skin was relatively high, and collagen accounted for 47.2 ± 7.8 and 70.8 ± 8.1 % of wet tissue, respectively. In contrast, the solubility of the collagen extracted from bone was the lowest of all the tissues examined, being only 5.7 ± 0.8 % of total wet tissue. The extent of hydroxylation of proline and lysine residues was also examined. In most tissues, the extent of hydroxylation of the lysine residue in insoluble collagen was higher than that of acid-soluble collagen, indicating that hydroxylysine contributes to the stability of collagen. This is the first report of collagen contents, solubility, and extent of hydroxylation of proline and lysine residues in collagen extracted from different tissues of one organism. It is possible that hydroxylysine-derived collagen cross-links play a critical role in the stability of collagen in dilute acetic acid.",{"EN":1744},"Isolation of collagen from tiger pufferfish parts and its solubility in dilute acetic acid",{"VOID":1746},"citation_journal_title=Nippon Suisan Gakkaishi; citation_title=Collagen content in the muscle of fishes in association with their swimming movement and meat texture; citation_author=K Sato, R Yoshinaka, M Sato, Y Shimizu; citation_volume=52; citation_publication_date=1986; citation_pages=1595-1600; citation_doi=10.2331\u002Fsuisan.52.1595; citation_id=CR1\ncitation_journal_title=Nippon Suisan Gakkaishi; citation_title=Contribution of the connective tissue on the texture difference of various fish species; citation_author=K Hatae, A Tobimatsu, M Takeyama, J Matsumoto; citation_volume=52; citation_publication_date=1986; citation_pages=2001-2007; citation_doi=10.2331\u002Fsuisan.52.2001; citation_id=CR2\ncitation_journal_title=Biosci Biotechnol Biochem; 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study aimed to evaluate the effect of Lactococcus lactis K-C2 on the growth performance, microbial diversity, and release of free amino acids in the intestinal tract and the edible parts of young amberjack, Seriola dumerili. Fish were fed a diet with or without strain K-C2 (2 × 1010 cfu\u002Fg feed) for 25 days. The results indicated that the growth performance of fish in the treated group was significantly higher than those in the control group (p \u003C 0.05). The amount of five amino acids (aspartate, sarcosine, taurine, alanine, and arginine) in the gut content and 13 of 21 amino acids in the edible parts of fish in the treated group were significantly higher (p \u003C 0.05) than those in the control group. Sphingomonas, Propionibacterium, and Mycobacterium were observed in gut microflora of fish in both the control and treated groups. Staphylococcus and Kocuria were detected in one sample from the control and treated groups; Acinetobacter and Acidobacteria were found in one sample from the control group. L. lactis was only found in one sample in the treated group. In conclusion, the dietary administration of probiotic L. lactis stimulated growth, reduced feed consumption, and improved the nutritional value of cultured amberjack.",{"EN":1898},"Effect of Lactococcus lactis K-C2 on the growth performance, amino acid content and gut microflora of amberjack Seriola 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J Appl Microbiol 96:117–132",{"id":28,"text":2069,"url":28,"identifiers":28},"Itano T, Kawakami H, Kono T, Sakai M (2006) Live vaccine trials against nocardiosis in yellowtail Seriola quinqueradiata. Aquaculture 261:1175–1180",{"id":28,"text":2071,"url":28,"identifiers":28},"Kanehisa M, Goto S (2000) KEGG: Kyoto encyclopedia of genes and genomes. Nucleic Acids Res 28:27–30",{"id":28,"text":2073,"url":28,"identifiers":28},"Kato G, Kato K, Saito K, Pe Y, Kondo H, Aoki T, Hirono I (2011) Vaccine efficacy of Mycobacterium bovis BCG against Mycobacterium sp. infection in amberjack Seriola dumerili. Fish Shellfish Immunol 30:467–472",{"id":28,"text":2075,"url":28,"identifiers":28},"Kielak AM, Barreto CC, Kowalchuk GA, Veen JA, Kuramae EE (2016) The ecology of Acidobacteria: moving beyond genes and genomes. 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FAO Fisheries Technical Paper, pp 199–215",{"id":28,"text":2093,"url":28,"identifiers":28},"Nakajima N, Kawanishi M, Imamura S, Hirano F, Uchiyama M, Yamamoto K, Nagai H, Futami K, Katagiri T, Maita M, Kijima M (2014) Development of a serology-based assay for efficacy evaluation of a lactococcicosis vaccine in Seriola fish. Fish Shellfish Immunol 38:135–139",{"id":28,"text":2095,"url":28,"identifiers":28},"Nayak SK (2010) Role of gastrointestinal microbiota in fish. Aquac Res 41:1553–1573",{"id":28,"text":2097,"url":28,"identifiers":28},"Nguyen TL, Park C-I, Kim D-H (2017) Improved growth rate and disease resistance in olive flounder, Paralichthys olivaceus, by probiotic Lactococcus lactis WFLU12 isolated from wild marine fish. Aquaculture 471:113–120",{"id":28,"text":2099,"url":28,"identifiers":28},"Nomura M, Kimoto H, Someya Y (1999) Novel characteristic for distinguishing Lactococcus lactis subsp. lactis from subsp. cremoris. 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The effect of fish meal, standard soybean meal and a bioprocessed soybean meal. Aquaculture 261:829–841",{"id":28,"text":2111,"url":28,"identifiers":28},"Ringø E, Zhou Z, Vecino JLG, Wadsworth S, Romero J, Krogdahl A, Olsen RE, Dimitroglou A, Foey A, Davies S, Owen M, Lauzon HL, Martinsen LL, De Schryver P, Bossier P, Sperstad S, Merrifield DL (2016) Effect of dietary components on the gut microbiota of aquatic animals. A never-ending story? Aquac Nutr 22:219–282",{"id":28,"text":2113,"url":28,"identifiers":28},"Saeedi M, Shahidi F, Mortazavi SA, Milani E, Yazdi FT (2015) Isolation and identification of lactic acid bacteria in winter salad (Local Pickle) during fermentation using 16S rRNA gene sequence analysis. J Food Saf 35:287–294",{"id":28,"text":2115,"url":28,"identifiers":28},"Saini VP, Ojha ML, Gupta MC, Nair P, Sharma A, Luhar V (2014) Effect of dietary probiotic on growth performance and disease resistance in Labeo rohita (Ham.) fingerlings. Int J Fish Aquat Stud 1:7–11",{"id":28,"text":2117,"url":28,"identifiers":28},"Salze GP, Davis DA (2015) Taurine: a critical nutrient for future fish feeds. Aquaculture 437:215–229",{"id":28,"text":2119,"url":28,"identifiers":28},"Schmitz A, Riesner D (2006) Purification of nucleic acids by selective precipitation with polyethylene glycol 6000. Anal Biochem 354:311–313",{"id":28,"text":2121,"url":28,"identifiers":28},"Sequeiros C, Garces ME, Vallejo M, Marguet ER, Olivera NL (2015) Potential aquaculture probiont Lactococcus lactis TW34 produces nisin Z and inhibits the fish pathogen Lactococcus garvieae. Arch Microbiol 197:449–458",{"id":28,"text":2123,"url":28,"identifiers":28},"Soltani M, Masouleh AS, Ahmadi M, Pourkazemi M, Taherimirghaed A (2016) Antibacterial activity, antibiotic susceptibility and probiotic use of lactic acid bacteria (LAB) in Persian sturgeon (Acipenser persicus). Iran J Aquat Anim Heal 2:54–65",{"id":28,"text":2125,"url":28,"identifiers":28},"Sperandio B, Polard P, Ehrlich DS, Renault P, Guédon E (2005) Sulfur amino acid metabolism and its control in Lactococcus lactis IL1403. J Bacteriol 187:3762–3778",{"id":28,"text":2127,"url":28,"identifiers":28},"Sun Y, Yang H, Ma R, Zhai S (2012) Does dietary administration of Lactococcus lactis modulate the gut microbiota of grouper, Epinephelus coioides. J World Aquac Soc 43:198–207",{"id":28,"text":2129,"url":28,"identifiers":28},"Tanaka R, Miyamoto H, Kodama H, Kawachi N, Udagawa M, Miyamoto H, Matsushita T (2010) Feed additives with thermophile-fermented compost enhance concentrations of free amino acids in the muscle of the flatfish Paralichthys olivaceus. J Gen Appl Microbiol 56:61–65",{"id":28,"text":2131,"url":28,"identifiers":28},"Tanaka R, Miyamoto H, Inoue SI, Shigeta K, Kondo M, Ito T, Kodama H, Miyamoto H, Matsushita T (2016) Thermophile-fermented compost as a fish feed additive modulates lipid peroxidation and free amino acid contents in the muscle of the carp, Cyprinus carpio. J Biosci Bioeng 121:530–535",{"id":28,"text":2133,"url":28,"identifiers":28},"Wang Y-B, Tian Z-Q, Yao J-T, Li W-F (2008) Effect of probiotics, Enteroccus faecium, on tilapia (Oreochromis niloticus) growth performance and immune response. Aquaculture 277:203–207",{"id":28,"text":2135,"url":28,"identifiers":28},"Wong S, Rawls JF (2012) Intestinal microbiota composition in fishes is influenced by host ecology and environment. Mol Ecol 21:3100–3102",{"id":28,"text":2137,"url":28,"identifiers":28},"Wu G (2013) Functional amino acids in nutrition and health. Amino Acids 45:407–411",{"id":28,"text":2139,"url":28,"identifiers":28},"Wu S, Wang G, Angert ER, Wang W, Li W, Zou H (2012) Composition, diversity, and origin of the bacterial community in grass carp intestine. PLoS ONE 7(2):e30440. https:\u002F\u002Fdoi.org\u002F10.1371\u002Fjournal.pone.0030440",{"id":28,"text":2141,"url":28,"identifiers":28},"Yabuuchi E, Yano I, Oyaizu H, Hashimoto Y, Ezaki T, Yamamoto H (1990) Proposals of Sphingomonas paucimobilis sp. nov. and comb. nov, Shingomonas parapaucimobilis sp. nov., Sphingomonas yanoikuyae sp. nov., Sphingomonas adhaesiva sp. nov., Sphingomonas capsulata comb. nov., and two genospecies of the genus Sphingomonas. Microbiol Immunol 34:99–119",{"id":28,"text":2143,"url":28,"identifiers":28},"Zhou X, Wang Y, Yao J, Li W (2010) Inhibition ability of probiotic, Lactococcus lactis, against A. hydrophila and study of its immunostimulatory effect in tilapia (Oreochromis niloticus). Int J Eng Sci Technol 2:73–80",{"id":2145,"createTime":2146,"updateTime":2147,"relativeEntities":2148,"slug":2149,"properties":2150,"entityType":985,"verifyStatus":26,"verifyTime":2147,"verifyNote":986,"languages":28,"translateLanguages":28,"viewCount":32,"primaryUrl":2159,"fullTextUrl":28,"authors":2160,"publicationType":1031,"publisherRelationship":2189,"citationCount":28,"citationInfo":28,"publishDate":2237,"publishYear":2238,"citationAnalyzeStatus":882,"lastCitationAnalyze":28,"indexDatabases":2239,"openAccess":28,"references":28,"isForceReanalyzing":1083},"011864c1-2f8a-4ca4-98ef-3888f67fc262","2024-02-05T12:13:54.481+00:00","2025-01-10T14:29:53.646+00:00",[],"Temporal-and-spatial-distributions-of-Biwa-salmon-Oncorhynchus-masou-subsp-by-ultrasonic-telemetry-in-Lake-Biwa-Japan",{"abstract":2151,"title":2153,"references":2155,"doi":2157},{"EN":2152},"Biwa salmon Oncorhynchus masou subsp. were tagged with ultrasonic transmitters and released in Lake Biwa, Japan. The temporal and spatial distributions were investigated by using two types of ultrasonic telemetry system, active tracking and passive monitoring. Biwa salmon cruised throughout the north basin horizontally and were distributed from the surface to the bottom vertically in the lake. An individual monitored for over 1 year showed the diurnal patterns of vertical distribution and the seasonal patterns of horizontal distribution. The vertical distribution of the fish during daytime in the stratified period was bimodal, suggesting a feeding strategy targeting both fish near the thermocline and the amphipods near the bottom. During the night, however, the fish maintained a fixed depth range. The fish were distributed over a wider horizontal area in the mixed period than in the stratified period. Three individuals swam in shallower water and experienced higher water temperatures during the spawning season than before moving between offshore and coastal areas.",{"EN":2154},"Temporal and spatial distributions of Biwa salmon Oncorhynchus masou subsp. by ultrasonic telemetry in Lake Biwa, Japan",{"VOID":2156},"Kaneo S (2012) Fish. In: Naito et al (eds) BIWAKO handbook. Shiga Prefecture, pp 176–177\nFujioka Y (1990) Biwa salmon: its ecological and morphological characteristics. Fish Egg 159:25–38 (in Japanese with English abstract)\nKikko T, Nishimori K, Ide A, Seki S, Ninomiya K, Sugahara K (2009) Introduction of notification for the Biwa Salmon trolling angler in Lake Biwa. Nippon Suisan Gakkaishi 75:1102–1105 (in Japanese)\nOda M (2010) Spawning redds distributions of Biwa salmon Oncorhynchus masou subsp. in some inlet streams of Lake Biwa, central Japan. Nippon Suisan Gakkaishi 76:123–215 (in Japanese)\nSugahara K, Ide A, Sakai A, Suzuki T, Kume H, Kikko T, Nishimori K, Seki S (2014) The present status of trolling of the Biwa salmon Oncorhynchus masou subsp. Lake Biwa, assessed by obligatory reporting by recreational anglers. Nippon Suisan Gakkaishi 80:45–52 (in Japanese with English abstract)\nFujioka Y (1987) Parr-smolt transformation in Biwa salmon Oncorhynchus rhodurus reared in pond. Nippon Suisan Gakkaishi 53:253–260 (in Japanese with English abstract)\nFujioka Y, Fushiki S (1988) Downstream migration and body silvering in underyearling Biwa salmon Oncorhynchus rhodurus. Nippon Suisan Gakkaishi 54:1889–1897 (in Japanese with English abstract)\nFujioka Y, Uenishi M (2006) Change in habitat and food with growth of Biwa salmon. Rep Shiga Prefecture Fish Exp Stn 51:51–63 (in Japanese with English abstract)\nKuwahara M, Iguchi K (1994) Occurrence of mature stream resident male Biwa Salmon, Oncorhynchus masou subsp. J Ichthyol 40:495–497\nTanaka H (2011) Studies on the resource structure of Biwa salmon, Oncorhynchus masou rhodurus in Lake Biwa. Rep Shiga Prefect Fish Exp Stn 54:7–61 (in Japanese)\nLucas MC, Baras E (2000) Methods for studying spatial behavior of freshwater fishes in the natural environment. Fish Fish 1:283–316\nMitsunaga Y, Kawai S, Komeyama K, Matsuda M, Yamane T (2005) Habitat utilization of largemouth bass around a set net. Fish Engin 41:251–255\nTsujimura S, Tsukada H, Nakahara H, Nakajima T, Nishino M (2000) Seasonal variations of Microcystis populations in sediments of Lake Biwa, Japan. Hydrobiologia 434:183–192\nOokubo K, Muramoto Y, Kataoka K (1982) A study on the thermally induced currents in lakes. Disaster Prev Res Inst Ann 25:615–642\nOgura M, Ishida Y (1992) Swimming behavior of coho salmon, Oncorhynchus kisutch, in the open sea as determined by ultrasonic telemetry. Can J Fish Aquat Sci 49:453–457\nBevelhimer MS, Adams SM (1993) A bioenergetics analysis of diel vertical migration by kokanee salmon, Oncorhynchus nerka. Can J Fish Aquat Sci 50:2336–2349\nWarner EJ, Quinn TP (1995) Horizontal and vertical movements of telemetered rainbow trout (Oncorhynchus mykiss) in Lake Washington. Can J Zool 73:146–153\nCandy JR, Quinn TP (1999) Behavior of adult Chinook salmon (Oncorhynchus tshawytscha) in British Columbia coastal waters determined from ultrasonic telemetry. Can J Zool 77:1161–1169\nWalker RV, Myers KW, Davis ND, Aydin KY, Friedland KD, Carlson HR, Boehlert GW, Urawa S, Ueno Y, Anma G (2000) Diurnal variation in thermal environment experienced by salmonids in the North Pacific as indicated by data storage tags. Fish Oceanogr 9:171–186\nIshida Y, Yano A, Ban M, Ogura M (2001) Vertical movement of a chum salmon Oncorhynchus Keta in the western North Pacific Ocean as determined by a depth-recording archival tag. Fish Sci 67:1030–1035\nBaldwin CM, Beauchamp DA (2002) Seasonal and diel distribution and movement of cutthroat trout from ultrasonic telemetry. Trans Am Fish Soc 131:143–158\nNowak GM, Quinn TP (2002) Diel and seasonal patterns of horizontal and vertical movements of telemetered cutthroat trout in Lake Washington, Washington. Trans Am Fish Soc 131:452–462\nAzuma T, Ishida Y (2005) Mechanism of body cavity temperature regulation of chum salmon (Oncorhynchus keta) during homing migration in the North Pacific Ocean. Fish Oceanogr 14:81–96\nHinke JT, Watters GM, Boehlert GW, Zedonis P (2005) Ocean habitat use in autumn by Chinook salmon in coastal waters of Oregon and California. Mar Ecol Prog Ser 285:181–192\nTanaka H, Naito Y, Davis ND, Urawa S, Ueda H, Fukuwaka M (2005) First record of the at sea swimming speed of a Pacific salmon during its oceanic migration. Mar Ecol Prog Ser 291:307–312\nWalker RV, Sviridov VV, Urawa S, Azuma T (2007) Spatio–temporal variation in vertical distribution of Pacific salmon in the ocean. North Pac Anadromous Fish Comm 4:193–201\nDwyer WP, Kramer RH (1975) The influence of temperature on scope for activity in cutthroat trout, Salmo clarki. Trans Am Fish Soc 104:552–554\nSims DW, Wearmouth VJ, Southall EJ, Hill JM, Moore P, Rawlinson K, Hutchinson N, Budd GC, Righton D, Metcalfe JD, Nash JP, Morritt D (2006) Hunt warm, rest cool: bioenergetic strategy underlying diel vertical migration of a benthic shark. J Anim Ecol 75:176–190\nHenderson MA, Northcote TG (1985) Visual prey detection and foraging in sympatric cutthroat trout (Salmo clarki clarki) and Dolly Varden (Salvelinus malma). Can J Fish Aquat Sci 42:785–790\nShirakihara K, Yoshida M, Nishino M, Takao Y, Sawada K (2001) Acoustic evaluation of the vertical distribution of dwarf ayu Plecoglossus altivelis altivelis in Lake Biwa. Fish Sci 67:430–435\nGodo M, Ban S (2007) Effect of temperature on metabolic and horizontal distributions an endemic amphipod Jesogammarus annandalei in Lake Biwa. Jpn J Limnol 68:375–389 (in Japanese with English abstract)\nBrett JR (1971) Energetic responses of salmon to temperature. A study of some thermal relations in the physiology and freshwater ecology of sockeye salmon (Oncorhynchus nerka). Am Zool 11:99–118\nUeda H, Kaeriyama M, Mukasa K, Urano A, Kudo H, Shoji T, Tokumitsu Y, Yamauchi K, Kurihara K (1998) Lacustrine sockeye salmon return to their natal area from open water using both visual and olfactory cues. Chem Senses 23:207–212\nKitamura S (2000) Telemetric observation on the homing migration of sockeye salmon in Lake Chuzenji. Nippon Suisan Gakkaishi 66:919–920 (in Japanese)\nUeda H (2004) Recent biotelemetry research on lacustrine salmon homing migration. Natl Inst Polar Res 58:80–88\nUeda H (2005) Physiological and ecological studies on mechanisms of salmon homing. Nippon Suisan Gakkaishi 71:282–285 (in Japanese)\nUeda H, Yamamoto Y, Hino H (2007) Physiological mechanisms of homing ability in sockeye salmon: from behavior to molecules using a lacustrine model. Am Fish Soc Symp 54:5–16\nSchmidt-Nielsen K (1990) Temperature. In: Schmidt-Nielsen K (ed) Animal physiology: adaptation and environment. Cambridge University Press, New York, pp 217–239\nNaito Y, Tanaka H, Ueda H (2000) Preliminary report of swimming behavior and the response temperature of lacustrine masu salmon, Oncorhynchus masou Brevoort, monitored by data logger during spawning migration in Lake Toya. Polar Biosci 13:87–94\nWinter JD (1983) Underwater biotelemetry. In: Nielsen LA, Johnson DL (eds) Fisheries techniques. American Fisheries Society, Maryland, pp 371–395",{"VOID":2158},"10.1007\u002Fs12562-014-0772-4","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs12562-014-0772-4",[2161,2176],{"id":2162,"sortIndex":32,"researcher":28,"roles":2163,"affiliations":2164,"properties":2173,"displayName":2175,"givenName":28,"familyName":28},"8ac4a0e3-9de2-41da-907f-4d601b5b2c07",[992],[2165],{"id":2166,"sortIndex":32,"affiliation":2167,"properties":28},"98398948-0583-475b-8575-6e4be20e7d3a",{"id":2166,"createTime":28,"updateTime":28,"relativeEntities":2168,"slug":28,"properties":2169,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2172,"statistic":28},[],{"title":2170},{"VI":2171},"Department of Fisheries, Faculty of Agriculture, Kinki University, Nara, Japan",[],{"title":2174},{"VI":2175},"Hiroyuki Kamimura",{"id":2177,"sortIndex":40,"researcher":28,"roles":2178,"affiliations":2179,"properties":2186,"displayName":2188,"givenName":28,"familyName":28},"946e67c1-28c8-4da0-b00b-56e8bc849d0b",[992],[2180],{"id":2166,"sortIndex":32,"affiliation":2181,"properties":28},{"id":2166,"createTime":28,"updateTime":28,"relativeEntities":2182,"slug":28,"properties":2183,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2185,"statistic":28},[],{"title":2184},{"VI":2171},[],{"title":2187},{"VI":2188},"Yasushi 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catalyze the hydrolysis of starch material and play important roles in the regulation of many physiological processes. Here, we report an amylase gene denoted Pc-Amy in the crayfish Procambarus clarkii (Decapoda: Cambaridae). The Pc-Amy gene encodes a polypeptide of 514 amino acids, and the deduced amylase protein is highly homologous to those from crustaceans. Real-time quantitative reverse transcription PCR (qRT-PCR) analysis showed that Pc-Amy is highly expressed in hepatopancreas during the intermolt period. SDS-PAGE and western blot analysis demonstrated that a 58-kDa recombinant protein is successfully expressed in Escherichia coli cells. The expression of Pc-Amy was significantly downregulated in hepatopancreas at 48 h after ecdysteroid induction, as confirmed by qRT-PCR and western blot analyses. In addition, RNA interference with the ecdysteroid receptor had an impact on the expression of Pc-Amy. These results suggest that Pc-Amy is an ecdysteroid-responsive gene which plays a role in the developmental process of P. clarkii.",{"EN":2250},"Identification and expression of an ecdysteroid-responsive amylase from red crayfish Procambarus clarkii",{"VOID":2252},"Prakash O, Jaiswal N (2010) α-Amylase: an ideal representative of thermostable enzymes. Appl Biochem Biotechnol 160:2401–2414\nPictet R, McDonald RJ, Swain WF, Grebar MM, Hobart PM, Crawform R, Shen LD, Bell G, Rutter WJ (1981) Differentiation of the pancreas: an analysis of the structure of the amylase and insulin genes. Fortsh Zool B 26:227–245\nKumari A, Singh K, Kayastha AM (2012) α-Amylase: general properties, mechanism and biotechnological applications—a review. Curr Biotechnol 1:98–107\nSvensson B (1994) Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol Biol 25:141–157\nBoel E, Brady L, Brzozowski AM, Derewenda Z, Dodson GG, Jensen VJ, Petersen SB, Swif H, Thim L, Woldike HF (1990) Calcium binding in α-amylases: an X-ray diffraction study at 2.1 Å resolution of two enzymes from Aspergillus. Biochem 29:6244–6249\nMachius M, Declerck N, Huber R, Wiegand G (1998) Activation of Bacillus licheniformis α-amylase through a disorder–order transition of the substrate-binding site mediated by a calcium–sodium–calcium metal triad. Structure 6:281–292\nBuisson G, Duee E, Haser R, Payan F (1987) Three-dimensional structure of porcine pancreatic α-amylase at 2.9 Å resolution. Role of calcium in structure and activity. EMBO J 6:3909–3916\nJespersen HM, MacGregor EA, Henrissat B, Sieks MR, Svensson B (1993) Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (β\u002Fα)8-barrel domain and evolutionary relationship of other amylolytic enzymes. J Protein Chem 12:791–805\nJanecek S, Svensson B, MacGregor EA (2003) Relation between domain evolution, specificity, and taxonomy of the α-amylase family members containing a C-terminal starch-binding domain. Eur J Biochem 270:635–645\nVan Wormhoudt A, Bourreau G, Le Moullac G (1995) Amylase polymorphism in Crustacea Decapoda: electrophoretic and immunological studies. Biochem System Ecol 23:139–149\nFernandez I, Moyano FJ, Diaz M, Martinez T (2001) Characterization of α-amylase activity in five species of Mediterranean sparid fishes (Sparidae, Teleostei). J Exp Mar Biol Ecol 262:1–12\nVan Wormhoudt A, Sellos D (2003) Highly variable polymorphism of the α-amylase gene family in Litopenaeus vannamei (Crustacea Decapoda). J Mol Evol 57:659–671\nCastro PF, Freitas ACV, Santana WM, Costa HMS, Carvalho LB, Bezerra RS (2012) Comparative study of amylases from the midgut gland of three species of penaeid shrimp. J Crust Biol 32:607–613\nDonal AH, Bernhard FB, Poppo HB, Genest Y, Abukashawa S, Ben-David G (1987) Enzyme-coding genes as molecular clocks: the molecular evolution of animal alpha-amylases. J Mol Evol 26:252–256\nFernandez I, Oliva M, Carrillo O, Van Wormhoudt A (1997) Digestive enzyme activities of Penaeus notialis during reproduction and moulting cycle. Comp Biochem Physiol Part A Physiol 118:1267–1271\nXin JJ, Liu XL, Li XL, Wang XZ, Huang H, Xiang JH (2011) PCR-RFLP polymorphism of alpha amylase gene and its association with growth traits of Litopenaeus vannamei. Acta Oceanol Sin 33:124–130\nKumari A, Singh K, Kayastha AM (2012) α-Amylase: general properties, mechanism and biotechnological applications—a review. Curr Biotechnol 1:98–107\nFurukawa A, Nakada-Tsukui K, Nozaki T (2013) Cysteine protease-binding protein family 6 mediates the trafficking of amylases to phagosomes in the enteric protozoan Entamoeba histolytica. Infect Immun 81:1820–1829\nSlater EP, Hesse H, Müller JM, Beato M (1993) Glucocorticoid receptor binding site in the mouse alpha-amylase 2 gene mediates response to the hormone. Mol Endocrinol 7:907–914\nAragon-Axomulco H, Chiappa-Carrara X, Soto L, Cuzon G, Arena L, Maldonado C, Cardenas R, Gaxiola G (2012) Seasonal variability in trypsin and alpha-amylase activities caused by the molting cycle and feeding habits of juvenile pink shrimp Farfantepenaeus duorarum (Burkenroad, 1939). J Crustacean Biol 32:89\nCharron L, Geffard O, Chaumot A, Coulaud R, Jaffal A, Gaillet V, Dedourge-Geffard O, Geffard A (2014) Influence of molting and starvation on digestive enzyme activities and energy storage in Gammarus fossarum. PLoS One 9:e96393\nGaxiola G, Cuzon G, García T, Taboada G, Brito R, Chimal ME, Paredes A, Soto L, Rosas C, van Wormhoudt A (2005) Factorial effects of salinity, dietary carbohydrate and moult cycle on digestive carbohydrases and hexokinases in Litopenaeus vannamei (Boone, 1931). Comp Biochem Physiol A Mol Integr Physiol 140:29–39\nShechter A, Tom M, Yudkovski Y, Weil S, Chang SA, Chang ES, Chalifa-Caspi V, Berman A, Sagi A (2007) Search for hepatopancreatic ecdysteroid-responsive genes during the crayfish molt cycle: from a single gene to multigenicity. J Exp Biol 210:3525–3537\nVan Wormhoudt A, Sellos D (1996) Cloning and sequencing analysis of three amylase cDNAs in the shrimp Penaeus vannamei (Crustacea Decapoda): evolutionary aspects. J Mol Evol 42:543–551\nHuvet A, Jeffroy F, Fabioux C, Daniel JY, Quillien V, Van Wormhoudt A, Moal J, Samain JF, Boudry P, Pouvreau S (2008) Association among growth, food consumption-related traits and amylase gene polymorphism in the Pacific oyster Crassostrea gigas. Anim Genet 39:662–665\nFernandez GAV, Garcia-Carre FL, Navarrete Del Toro MA, Fenucci JL (2001) Digestive proteinases of red shrimp Pleoticus muelleri (Decapoda, Penaeoidea): partial characterization and relationship with molting. Comp Biochem Physiol Part B Biochem Mol Biol 130:331–338\nMeng-Shun Hsieh MS, Yin LJ, Jiang ST (2008) Purification and characterization of the amylase from a small abalone Haliotis sieboldii. Fish Sci 74:425–432\nTamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28:2731–2739\nBradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein–dye binding. Anal Biochem 72:248–254\nHarlow E, Lane D (1999) Immunizations. In: Harlow E, Lane D (eds) Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, New York, pp 92–119\nBernfeld P (1951) Enzymes of starch degradation and synthesis. Adv Enzymol Relat Subj Biochem 12:379–428\nLowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275\nLivak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real time quantitative PCR and the 2-[Delta] [Delta] CT method. Methods 25:402–408\nAltschul SF, Gish W, Miller W, Myers EW, Lipman DJ (1990) Basic local alignment search tool. J Mol Biol 215:403–410\nJanecek S (1997) α-Amylase family: molecular biology and evolution. Prog Biophys Mol Biol 67:67–97\nAsazuma H, Nagata S, Kono M, Nagasawa H (2007) Molecular cloning and expression analysis of ecdysone receptor and retinoid X receptor from the kuruma prawn, Marsupenaeus japonicus. Comp Biochem Physiol Part B Biochem Mol Biol 148:139–150\nBagamasbad P, Denve RJ (2011) Mechanisms and significance of nuclear receptor auto-and cross-regulation. Gen Comp Endocrinol 170:3–17\nTesteniere O, Hecker A, Le Gurun S, Quennedey B, Graf F, Luquet G (2002) Characterization and spatiotemporal expression of orchestin, a gene encoding an ecdysone-inducible protein from a crustacean organic matrix. Biochem J 361:327–335\nRewitz K, Styrishave B, Andersen O (2003) CYP330A1 and CYP4C39 enzymes in the shore crab Carcinus maenas: sequence and expression regulation by ecdysteroids and xenobiotics. Biochem Biophs Res Commun 310:252–260\nKim HW, Lee SG, Mykles DL (2005) Ecdysteroid-responsive genes, RXR and E75, in the tropical land crab, Gecarcinus lateralis: differential tissue expression of multiple RXR isoforms generated at three alternative splicing sites in the hinge and ligand-binding domains. Mol Cell Endocrinol 242:80–95\nDouglas CW (1990) Characterization of the alpha-amylase receptor of Streptococcus gordonii NCTC 7868. J Dent Res 69:1746–1752\nFernandez-Luna MT, Lanz-Mendoza H, Gill SS, Bravo A, Soberon M, Miranda-Rios J (2010) An alpha-amylase is a novel receptor for Bacillus thuringiensis ssp. israelensis Cry4Ba and Cry11Aa toxins in the malaria vector mosquito Anopheles albimanus (Diptera: Culicidae). Environ Microbiol 12:746–757",{"VOID":2254},"10.1007\u002Fs12562-015-0854-y","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs12562-015-0854-y",[2257,2272,2285,2298,2311],{"id":2258,"sortIndex":32,"researcher":28,"roles":2259,"affiliations":2260,"properties":2269,"displayName":2271,"givenName":28,"familyName":28},"79c69a72-608b-4f64-a66f-1745705a2e2b",[992],[2261],{"id":2262,"sortIndex":32,"affiliation":2263,"properties":28},"74cc7ad7-0cd8-4907-9f32-4dbc2c2b6c27",{"id":2262,"createTime":28,"updateTime":28,"relativeEntities":2264,"slug":28,"properties":2265,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2268,"statistic":28},[],{"title":2266},{"VI":2267},"College of Life Sciences, Anhui Agricultural University, Hefei, People’s Republic of China",[],{"title":2270},{"VI":2271},"Tao Peng",{"id":2273,"sortIndex":40,"researcher":28,"roles":2274,"affiliations":2275,"properties":2282,"displayName":2284,"givenName":28,"familyName":28},"48f9c100-2f11-4b3e-bebf-bf8c369d3d70",[992],[2276],{"id":2262,"sortIndex":32,"affiliation":2277,"properties":28},{"id":2262,"createTime":28,"updateTime":28,"relativeEntities":2278,"slug":28,"properties":2279,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2281,"statistic":28},[],{"title":2280},{"VI":2267},[],{"title":2283},{"VI":2284},"Daojun 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