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10.1073/pnas.2112703118 http://scihub22266oqcxt.onion/10.1073/pnas.2112703118 34782481!8640741!34782481     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\34782481.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (48): ä Nephropedia Template TP {{tp|p=34782481|t=2021. Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein |pdf=|usr=}}{{34782481}} gab.com Text Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=34782481 #FOAvip The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates membrane fusion to allow entry of the viral genome into host cells. To understand its detailed entry mechanism and develop a specific entry inhibitor, in situ structural information on the SARS-CoV-2 spike protein in different states is urgent. Here, by using cryo-electron tomography, we observed both prefusion and postfusion spikes in beta-propiolactone-inactivated SARS-CoV-2 virions and solved the in situ structure of the postfusion spike at nanometer resolution. Compared to previous reports, the six-helix bundle fusion core, the glycosylation sites, and the location of the transmembrane domain were clearly resolved. We observed oligomerization patterns of the spikes on the viral membrane, likely suggesting a mechanism of fusion pore formation. Twit Text FOAVip Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=34782481 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34782481 #FOAvip English Wikipedia <ref>{{Cite pmid|34782481}}</ref> Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein #MMPMID34782481 Tai L; Zhu G; Yang M; Cao L; Xing X; Yin G; Chan C; Qin C; Rao Z; Wang X; Sun F; Zhu Y Proc Natl Acad Sci U S A 2021[Nov]; 118 (48): ä PMID34782481show ga The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates membrane fusion to allow entry of the viral genome into host cells. To understand its detailed entry mechanism and develop a specific entry inhibitor, in situ structural information on the SARS-CoV-2 spike protein in different states is urgent. Here, by using cryo-electron tomography, we observed both prefusion and postfusion spikes in beta-propiolactone-inactivated SARS-CoV-2 virions and solved the in situ structure of the postfusion spike at nanometer resolution. Compared to previous reports, the six-helix bundle fusion core, the glycosylation sites, and the location of the transmembrane domain were clearly resolved. We observed oligomerization patterns of the spikes on the viral membrane, likely suggesting a mechanism of fusion pore formation. |Amino Acid Motifs[MESH] |Animals[MESH] |Chlorocebus aethiops[MESH] |Cryoelectron Microscopy[MESH] |Electron Microscope Tomography[MESH] |Glycosylation[MESH] |Protein Domains[MESH] |Protein Multimerization[MESH] |SARS-CoV-2/*ultrastructure[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/metabolism[MESH]Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion sp(epmc).pdf DeepDyve Pubget Overpricing