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10.1016/j.virol.2015.03.043 http://scihub22266oqcxt.onion/10.1016/j.virol.2015.03.043 C4424100!4424100 !25866377     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25866377 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Virology 2015 ; 479-480 (ä): 498-507 Nephropedia Template TP {{tp|p=25866377 |t=2015. Viral membrane fusion |pdf=|usr=}}{{25866377 }} gab.com Text Viral membrane fusion JO: Virology http://www.kidney.de/pget.php?&tw=1&pmid=25866377 #FOAvip Membrane fusion is an essential step when enveloped viruses enter cells. Lipid bilayer fusion requires catalysis to overcome a high kinetic barrier; viral fusion proteins are the agents that fulfill this catalytic function. Despite a variety of molecular architectures, these proteins facilitate fusion by essentially the same generic mechanism. Stimulated by a signal associated with arrival at the cell to be infected (e.g., receptor or co-receptor binding, proton binding in an endosome), they undergo a series of conformational changes. A hydrophobic segment (a "fusion loop" or "fusion peptide") engages the target-cell membrane and collapse of the bridging intermediate thus formed draws the two membranes (virus and cell) together. We know of three structural classes for viral fusion proteins. Structures for both pre- and postfusion conformations of illustrate the beginning and end points of a process that can be probed by single-virion measurements of fusion kinetics. Twit Text FOAVip Viral membrane fusion ????Virology http://www.kidney.de/pget.php?&tw=1&pmid=25866377 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25866377 #FOAvip English Wikipedia <ref>{{Cite pmid|25866377 }}</ref> Viral membrane fusion #MMPMID25866377 Harrison SC Virology 2015[May]; 479-480 (ä): 498-507 PMID25866377 show ga Membrane fusion is an essential step when enveloped viruses enter cells. Lipid bilayer fusion requires catalysis to overcome a high kinetic barrier; viral fusion proteins are the agents that fulfill this catalytic function. Despite a variety of molecular architectures, these proteins facilitate fusion by essentially the same generic mechanism. Stimulated by a signal associated with arrival at the cell to be infected (e.g., receptor or co-receptor binding, proton binding in an endosome), they undergo a series of conformational changes. A hydrophobic segment (a "fusion loop" or "fusion peptide") engages the target-cell membrane and collapse of the bridging intermediate thus formed draws the two membranes (virus and cell) together. We know of three structural classes for viral fusion proteins. Structures for both pre- and postfusion conformations of illustrate the beginning and end points of a process that can be probed by single-virion measurements of fusion kinetics. |*Host-Pathogen Interactions [MESH] |*Virus Internalization [MESH] |Protein Conformation [MESH]Viral membrane fusion (epmc).pdf DeepDyve Pubget Overpricing