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10.1038/s41594-017-0016-2 http://scihub22266oqcxt.onion/10.1038/s41594-017-0016-2 C5971111!5971111 !29335562     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29335562 &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       Nat+Struct+Mol+Biol 2018 ; 25 (2 ): 139-146 Nephropedia Template TP {{tp|p=29335562 |t=2018. Cryo-EM structure of the exocyst complex |pdf=|usr=}}{{29335562 }} gab.com Text Cryo-EM structure of the exocyst complex JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=29335562 #FOAvip The exocyst is an evolutionarily conserved octameric protein complex that mediates the tethering of post-Golgi secretory vesicles to the plasma membrane during exocytosis and is implicated in many cellular processes such as cell polarization, cytokinesis, ciliogenesis and tumor invasion. Using cryo-EM and chemical cross-linking MS (CXMS), we solved the structure of the Saccharomyces cerevisiae exocyst complex at an average resolution of 4.4?Å. Our model revealed the architecture of the exocyst and led to the identification of the helical bundles that mediate the assembly of the complex at its core. Sequence analysis suggests that these regions are evolutionarily conserved across eukaryotic systems. Additional cell biological data suggest a mechanism for exocyst assembly that leads to vesicle tethering at the plasma membrane. Twit Text FOAVip Cryo-EM structure of the exocyst complex ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=29335562 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29335562 #FOAvip English Wikipedia <ref>{{Cite pmid|29335562 }}</ref> Cryo-EM structure of the exocyst complex #MMPMID29335562 Mei K ; Li Y ; Wang S ; Shao G ; Wang J ; Ding Y ; Luo G ; Yue P ; Liu JJ ; Wang X ; Dong MQ ; Wang HW ; Guo W Nat Struct Mol Biol 2018[Feb]; 25 (2 ): 139-146 PMID29335562 show ga The exocyst is an evolutionarily conserved octameric protein complex that mediates the tethering of post-Golgi secretory vesicles to the plasma membrane during exocytosis and is implicated in many cellular processes such as cell polarization, cytokinesis, ciliogenesis and tumor invasion. Using cryo-EM and chemical cross-linking MS (CXMS), we solved the structure of the Saccharomyces cerevisiae exocyst complex at an average resolution of 4.4?Å. Our model revealed the architecture of the exocyst and led to the identification of the helical bundles that mediate the assembly of the complex at its core. Sequence analysis suggests that these regions are evolutionarily conserved across eukaryotic systems. Additional cell biological data suggest a mechanism for exocyst assembly that leads to vesicle tethering at the plasma membrane. |*Exocytosis [MESH] |Amino Acid Motifs [MESH] |Biological Transport [MESH] |Cell Membrane/metabolism [MESH] |Cross-Linking Reagents [MESH] |Cryoelectron Microscopy/*methods [MESH] |Cytoplasm/metabolism [MESH] |Golgi Apparatus/metabolism [MESH] |Image Processing, Computer-Assisted [MESH] |Mass Spectrometry [MESH] |Protein Binding [MESH] |Protein Multimerization [MESH] |Saccharomyces cerevisiae Proteins/metabolism [MESH] |Saccharomyces cerevisiae/*metabolism [MESH] |Secretory Vesicles/*metabolism [MESH]Cryo-EM structure of the exocyst complex (epmc).pdf DeepDyve Pubget Overpricing