tailieunhanh - Báo cáo y học: " Mutations affecting cleavage at the p10-capsid protease cleavage site block Rous sarcoma virus replication"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: Mutations affecting cleavage at the p10-capsid protease cleavage site block Rous sarcoma virus replication | Retrovirology BioMed Central Short report Open Access Mutations affecting cleavage at the pl0-capsid protease cleavage site block Rous sarcoma virus replication Marcy L Vana1 Aiping Chen1 Peter Boross2 3 Irene Weber2 Dalbinder Colman4 Eric Barklis4 and Jonathan Leis 1 Address Department of Microbiology and Immunology Feinberg School of Medicine Northwestern University Chicago Illinois 60611 USA 2Department of Biology Georgia State University Atlanta GA 30303 USA 3Biochemistry and Molecular Biology Department Medical and Health Sciences Center University of Debrecen Debrecen Hungary and 4Vollum Institute and Department of Microbiology Oregon Health and Science University Portland OR 97201 USA Email Marcy L Vana - mvana@ Aiping Chen - a-chen2@ Peter Boross - biopib@ Irene Weber - iweber@ Dalbinder Colman - colmand@ Eric Barklis - barklis@ Jonathan Leis - j-leis@ Corresponding author Published 27 September 2005 Received 01 February 2005 Accepted 27 September 2005 Retrovirology 2005 2 58 doi l 742-4690-2-58 This article is available from http content 2 1 58 2005 Vana et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract A series of amino acid substitutions M239F M239G P240F V241G were placed in the p10-CA protease cleavage site VVAM PVVI to change the rate of cleavage of the junction. The effects of these substitutions on p10-CA cleavage by RSV PR were confirmed by measuring the kinetics of cleavage of model peptide substrates containing the wild type and mutant pl0-CA sites. The effects of these substitutions on processing of the Gag polyprotein were determined by labeling Gag transfected COS-1 cells with .

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