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10.1038/nsmb.3038 http://scihub22266oqcxt.onion/10.1038/nsmb.3038 C4809529!4809529!26030875     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Struct+Mol+Biol 2015 ; 22 (7): 547-54 Nephropedia Template TP {{tp|p=26030875|t=2015. Syntaxin Opening by the MUN Domain Underlies the Function of Munc13 in Synaptic Vesicle Priming |pdf=|usr=}}{{26030875}} gab.com Text Syntaxin Opening by the MUN Domain Underlies the Function of Munc13 in Synaptic Vesicle Priming JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=26030875 #FOAvip UNC-13-Munc13s play a central function in synaptic vesicle priming through their MUN domains. However, it is unclear whether this function arises from the ability of the MUN domain to mediate the transition from the Munc18-1?closed syntaxin-1 complex to the SNARE complex in vitro. The crystal structure of rat Munc13-1 MUN domain now reveals an elongated, arch-shaped architecture formed by ?-helical bundles, with a highly conserved hydrophobic pocket in the middle. Mutation of two residues (NF) in this pocket abolishes the stimulation caused by the Munc13-1 MUN domain on SNARE complex assembly and on SNARE-dependent proteoliposome fusion in vitro. Moreover, the same mutation in UNC-13 abrogates synaptic vesicle priming in C. elegans neuromuscular junctions. These results strongly support the notion that orchestration of syntaxin-1 opening and SNARE complex assembly underlies the central role of UNC-13-Munc13s in synaptic vesicle priming. Twit Text FOAVip Syntaxin Opening by the MUN Domain Underlies the Function of Munc13 in Synaptic Vesicle Priming ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=26030875 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26030875 #FOAvip English Wikipedia <ref>{{Cite pmid|26030875}}</ref> Syntaxin Opening by the MUN Domain Underlies the Function of Munc13 in Synaptic Vesicle Priming #MMPMID26030875 Yang X; Wang S; Sheng Y; Zhang M; Zou W; Wu L; Kang L; Rizo J; Zhang R; Xu T; Ma C Nat Struct Mol Biol 2015[Jul]; 22 (7): 547-54 PMID26030875show ga UNC-13-Munc13s play a central function in synaptic vesicle priming through their MUN domains. However, it is unclear whether this function arises from the ability of the MUN domain to mediate the transition from the Munc18-1?closed syntaxin-1 complex to the SNARE complex in vitro. The crystal structure of rat Munc13-1 MUN domain now reveals an elongated, arch-shaped architecture formed by ?-helical bundles, with a highly conserved hydrophobic pocket in the middle. Mutation of two residues (NF) in this pocket abolishes the stimulation caused by the Munc13-1 MUN domain on SNARE complex assembly and on SNARE-dependent proteoliposome fusion in vitro. Moreover, the same mutation in UNC-13 abrogates synaptic vesicle priming in C. elegans neuromuscular junctions. These results strongly support the notion that orchestration of syntaxin-1 opening and SNARE complex assembly underlies the central role of UNC-13-Munc13s in synaptic vesicle priming. äSyntaxin Opening by the MUN Domain Underlies the Function of Munc13 in(epmc).pdf DeepDyve Pubget Overpricing