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10.1038/cr.2015.47 http://scihub22266oqcxt.onion/10.1038/cr.2015.47 C4423085!4423085!25906996     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25906996&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 Deprecated: Implicit conversion from float 215.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Res 2015 ; 25 (5): 551-60 Nephropedia Template TP {{tp|p=25906996|t=2015. Cryo-EM structure of SNAP-SNARE assembly in 20S particle |pdf=|usr=}}{{25906996}} gab.com Text Cryo-EM structure of SNAP-SNARE assembly in 20S particle JO: Cell Res http://www.kidney.de/pget.php?&tw=1&pmid=25906996 #FOAvip N-ethylmaleimide-sensitive factor (NSF) and ? soluble NSF attachment proteins (?-SNAPs) work together within a 20S particle to disassemble and recycle the SNAP receptor (SNARE) complex after intracellular membrane fusion. To understand the disassembly mechanism of the SNARE complex by NSF and ?-SNAP, we performed single-particle cryo-electron microscopy analysis of 20S particles and determined the structure of the ?-SNAP-SNARE assembly portion at a resolution of 7.35 Å. The structure illustrates that four ?-SNAPs wrap around the single left-handed SNARE helical bundle as a right-handed cylindrical assembly within a 20S particle. A conserved hydrophobic patch connecting helices 9 and 10 of each ?-SNAP forms a chock protruding into the groove of the SNARE four-helix bundle. Biochemical studies proved that this structural element was critical for SNARE complex disassembly. Our study suggests how four ?-SNAPs may coordinate with the NSF to tear the SNARE complex into individual proteins. Twit Text FOAVip Cryo-EM structure of SNAP-SNARE assembly in 20S particle ????Cell Res http://www.kidney.de/pget.php?&tw=1&pmid=25906996 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25906996 #FOAvip English Wikipedia <ref>{{Cite pmid|25906996}}</ref> Cryo-EM structure of SNAP-SNARE assembly in 20S particle #MMPMID25906996 Zhou Q; Huang X; Sun S; Li X; Wang HW; Sui SF Cell Res 2015[May]; 25 (5): 551-60 PMID25906996show ga N-ethylmaleimide-sensitive factor (NSF) and ? soluble NSF attachment proteins (?-SNAPs) work together within a 20S particle to disassemble and recycle the SNAP receptor (SNARE) complex after intracellular membrane fusion. To understand the disassembly mechanism of the SNARE complex by NSF and ?-SNAP, we performed single-particle cryo-electron microscopy analysis of 20S particles and determined the structure of the ?-SNAP-SNARE assembly portion at a resolution of 7.35 Å. The structure illustrates that four ?-SNAPs wrap around the single left-handed SNARE helical bundle as a right-handed cylindrical assembly within a 20S particle. A conserved hydrophobic patch connecting helices 9 and 10 of each ?-SNAP forms a chock protruding into the groove of the SNARE four-helix bundle. Biochemical studies proved that this structural element was critical for SNARE complex disassembly. Our study suggests how four ?-SNAPs may coordinate with the NSF to tear the SNARE complex into individual proteins. äCryo-EM structure of SNAP-SNARE assembly in 20S particle (epmc).pdf DeepDyve Pubget Overpricing