tailieunhanh - Báo cáo y học: " The host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminus"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học 'Respiratory Research cung cấp cho các bạn kiến thức về ngành y đề tài: " The host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminus. | Retrovirology BioMed Central Research The host protein Staufenl interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminus Laurent Chatel-Chaix1 2 Karine Boulay1 Andrew J Mouland2 3 4 and Luc DesGroseillers 1 Address Departementde biochimie Université de Montreal Montreal Qc Canada 2HIV-1 RNA Trafficking Laboratory Lady Davis Institute for Medical Research-Sir Mortimer B. Davis Jewish General Hospital Montreal Qc Canada 3Department of Medicine McGill University Montreal Qc Canada and 4Department of Microbiology Immunology McGill University Montreal Qc Canada Email Laurent Chatel-Chaix - Karine Boulay - Andrew J Mouland - Luc DesGroseillers - Corresponding author Open Access Published 22 May 2008 Received 17 January 2008 Retrovirology 2008 5 41 doi 1742-4690-5-41 Accepted 22 May 2008 This article is available from http content 5 1 41 2008 Chatel-Chaix 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_ Background The formation of new infectious human immunodeficiency type 1 virus HIV-1 mainly relies on the homo-multimerization of the viral structural polyprotein Pr55Gag and on the recruitment of host factors. We have previously shown that the double-stranded RNA-binding protein Staufen 1 Stau1 likely through an interaction between its third double-stranded RNA-binding domain dsRBD3 and the nucleocapsid NC domain of Pr55Gag participates in HIV-1 assembly by influencing Pr55Gag multimerization. Results We now report the fine mapping of Stau 1 Pr55Gag association .

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