Tham khảo tài liệu 'báo cáo hóa học: " viroporin potential of the lentivirus lytic peptide (llp) domains of the hiv-1 gp41 protein"', luận văn - báo cáo phục vụ nhu cầu học tập, nghiên cứu và làm việc hiệu quả | Virology Journal BioMed Central Research Open Access Viroporin potential of the lentivirus lytic peptide LLP domains of the HIV-1 gp41 protein Joshua M Costin 1 Joshua M Rausch2 Robert F Garry3 and William C Wimley4 Address Biotechnology Research Group Department of Biology Florida Gulf Coast University 10501 FGCU Blvd. S. Fort Myers FL 33965 USA 2Department of Neurobiology and Physiology Northwestern University 2205 Tech Dr. Hogan 2-160 Evanston IL 60208 USA 3Department of Microbiology and Immunology Tulane University Health Sciences Center 1430 Tulane Avenue New Orleans LA 70112 USA and 4Department of Biochemistry Tulane University Tulane University Health Sciences Center 1430 Tulane Avenue New Orleans LA 70112 USA Email Joshua M Costin - jcostin@ Joshua M Rausch - j-rausch@ Robert F Garry - rfgarry@ William C Wimley - wwimley@ Corresponding author Published 20 November 2007 Virology Journal 2007 4 123 doi l743-422X-4-l23 Received 19 October 2007 Accepted 20 November 2007 This article is available from http content 4 l 123 2007 Costin 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 Mechanisms by which HIV-l mediates reductions in CD4 cell levels in infected persons are being intensely investigated and have broad implications for AIDS drug and vaccine development. Virally induced changes in membrane ionic permeability induced by lytic viruses of many families contribute to cytopathogenesis. HIV-l induces disturbances in plasma membrane ion transport. The carboxyl terminus of TM gp4l contains potential amphipathic a-helical motifs identified through their structural similarities to naturally occurring cytolytic peptides. These .
