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10.1038/nrm.2016.65 http://scihub22266oqcxt.onion/10.1038/nrm.2016.65 C5471617!5471617 !27301672     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27301672 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27301672 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Rev+Mol+Cell+Biol 2016 ; 17 (8 ): 465-79 Nephropedia Template TP {{tp|p=27301672 |t=2016. Chaperoning SNARE assembly and disassembly |pdf=|usr=}}{{27301672 }} gab.com Text Chaperoning SNARE assembly and disassembly JO: Nat Rev Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=27301672 #FOAvip Intracellular membrane fusion is mediated in most cases by membrane-bridging complexes of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). However, the assembly of such complexes in vitro is inefficient, and their uncatalysed disassembly is undetectably slow. Here, we focus on the cellular machinery that orchestrates assembly and disassembly of SNARE complexes, thereby regulating processes ranging from vesicle trafficking to organelle fusion to neurotransmitter release. Rapid progress is being made on many fronts, including the development of more realistic cell-free reconstitutions, the application of single-molecule biophysics, and the elucidation of X-ray and high-resolution electron microscopy structures of the SNARE assembly and disassembly machineries 'in action'. Twit Text FOAVip Chaperoning SNARE assembly and disassembly ????Nat Rev Mol Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=27301672 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27301672 #FOAvip English Wikipedia <ref>{{Cite pmid|27301672 }}</ref> Chaperoning SNARE assembly and disassembly #MMPMID27301672 Baker RW ; Hughson FM Nat Rev Mol Cell Biol 2016[Aug]; 17 (8 ): 465-79 PMID27301672 show ga Intracellular membrane fusion is mediated in most cases by membrane-bridging complexes of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). However, the assembly of such complexes in vitro is inefficient, and their uncatalysed disassembly is undetectably slow. Here, we focus on the cellular machinery that orchestrates assembly and disassembly of SNARE complexes, thereby regulating processes ranging from vesicle trafficking to organelle fusion to neurotransmitter release. Rapid progress is being made on many fronts, including the development of more realistic cell-free reconstitutions, the application of single-molecule biophysics, and the elucidation of X-ray and high-resolution electron microscopy structures of the SNARE assembly and disassembly machineries 'in action'. |Animals [MESH] |Humans [MESH] |Molecular Chaperones/*metabolism [MESH]Chaperoning SNARE assembly and disassembly (epmc).pdf DeepDyve Pubget Overpricing