Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: Comparison of p53 and the PDZ domain containing protein MAGI-3 regulation by the E6 protein from high-risk human papillomaviruses | Virology Journal BioMed Central Open Access Comparison of p53 and the PDZ domain containing protein MAGI-3 regulation by the E6 protein from high-risk human papillomaviruses Julia Ainsworth1 Miranda Thomas2 Lawrence Banks2 Francois Coutlee3 and Greg Matlashewski 1 4 Address Department of Microbiology and Immunology McGill University Montreal QC. Canada international Centre for Genetic Engineering and Biotechnology Padriciano 99 Trieste I-34012 Italy 3Department de Microbiologie et Immunologie University de Montreal QC. Canada and 4Department of Microbiology and Immunology McGill University Montreal H3A 2B4 514-398-3914 Canada Email Julia Ainsworth - Miranda Thomas - Thomas@ Lawrence Banks - banks@ Francois Coutlee - Greg Matlashewski - Corresponding author Published 2 June 2008 Received 22 April 2008 Accepted 2 June 2008 Virology Journal 2008 5 67 doi 186 1743-422X-5-67 This article is available from http content 5 1 67 2008 Ainsworth 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 Central to cellular transformation caused by human papillomaviruses HPVs is the ability of E6 proteins to target cellular p53 and proteins containing PDZ domains including MAGI-3 for degradation. The aim of this study was to compare E6-mediated degradation of p53 and MAGI-3 under parallel experimental conditions and further with respect to the involvement of proteasomes and ubiquitination. We also compared the degradation of p53 and MAGI-3 by E6 from several HPV types including different variants from HPV-33. All of the E6 genes from different HPV types displayed similar abilities to mediate the .
