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10.1038/s41586-020-2665-2 http://scihub22266oqcxt.onion/10.1038/s41586-020-2665-2 32805734!7116492!32805734     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       Nature 2020 ; 588 (7838): 498-502 Nephropedia Template TP {{tp|p=32805734|t=2020. Structures and distributions of SARS-CoV-2 spike proteins on intact virions |pdf=|usr=}}{{32805734}} gab.com Text Structures and distributions of SARS-CoV-2 spike proteins on intact virions JO: Nature http://www.kidney.de/pget.php?&tw=1&pmid=32805734 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude(1). Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells(2-6). S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes(2,7,8). The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy(2,7,9-12), but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination. Twit Text FOAVip Structures and distributions of SARS-CoV-2 spike proteins on intact virions ????Nature http://www.kidney.de/pget.php?&tw=1&pmid=32805734 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32805734 #FOAvip English Wikipedia <ref>{{Cite pmid|32805734}}</ref> Structures and distributions of SARS-CoV-2 spike proteins on intact virions #MMPMID32805734 Ke Z; Oton J; Qu K; Cortese M; Zila V; McKeane L; Nakane T; Zivanov J; Neufeldt CJ; Cerikan B; Lu JM; Peukes J; Xiong X; Krausslich HG; Scheres SHW; Bartenschlager R; Briggs JAG Nature 2020[Dec]; 588 (7838): 498-502 PMID32805734show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude(1). Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells(2-6). S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes(2,7,8). The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy(2,7,9-12), but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination. |*Cryoelectron Microscopy[MESH] |Antibodies, Neutralizing/immunology[MESH] |COVID-19 Vaccines/immunology[MESH] |COVID-19/immunology[MESH] |Cell Line, Tumor[MESH] |Humans[MESH] |Models, Molecular[MESH] |Pliability[MESH] |Protein Conformation[MESH] |Protein Multimerization[MESH] |SARS-CoV-2/chemistry/isolation & purification/*metabolism/*ultrastructure[MESH] |Spike Glycoprotein, Coronavirus/*analysis/chemistry/isolation & purification/*ultrastructure[MESH]Structures and distributions of SARS-CoV-2 spike proteins on intact vi(epmc).pdf DeepDyve Pubget Overpricing