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10.1016/j.celrep.2022.110428 http://scihub22266oqcxt.onion/10.1016/j.celrep.2022.110428 35172173!8818377!35172173     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=35172173&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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\35172173.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Rep 2022 ; 38 (9): 110428 Nephropedia Template TP {{tp|p=35172173|t=2022. Cryo-EM structure of the SARS-CoV-2 Omicron spike |pdf=|usr=}}{{35172173}} gab.com Text Cryo-EM structure of the SARS-CoV-2 Omicron spike JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=35172173 #FOAvip The recently reported B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) includes 34 mutations in the spike protein relative to the Wuhan strain, including 15 mutations in the receptor-binding domain (RBD). Functional studies have shown Omicron to substantially escape the activity of many SARS-CoV-2-neutralizing antibodies. Here, we report a 3.1 A-resolution cryoelectron microscopy (cryo-EM) structure of the Omicron spike protein ectodomain. The structure depicts a spike that is exclusively in the 1-RBD-up conformation with high mobility of RBD. Many mutations cause steric clashes and/or altered interactions at antibody-binding surfaces, whereas others mediate changes of the spike structure in local regions to interfere with antibody recognition. Overall, the structure of the Omicron spike reveals how mutations alter its conformation and explains its extraordinary ability to evade neutralizing antibodies. Twit Text FOAVip Cryo-EM structure of the SARS-CoV-2 Omicron spike ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=35172173 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35172173 #FOAvip English Wikipedia <ref>{{Cite pmid|35172173}}</ref> Cryo-EM structure of the SARS-CoV-2 Omicron spike #MMPMID35172173 Cerutti G; Guo Y; Liu L; Liu L; Zhang Z; Luo Y; Huang Y; Wang HH; Ho DD; Sheng Z; Shapiro L Cell Rep 2022[Mar]; 38 (9): 110428 PMID35172173show ga The recently reported B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) includes 34 mutations in the spike protein relative to the Wuhan strain, including 15 mutations in the receptor-binding domain (RBD). Functional studies have shown Omicron to substantially escape the activity of many SARS-CoV-2-neutralizing antibodies. Here, we report a 3.1 A-resolution cryoelectron microscopy (cryo-EM) structure of the Omicron spike protein ectodomain. The structure depicts a spike that is exclusively in the 1-RBD-up conformation with high mobility of RBD. Many mutations cause steric clashes and/or altered interactions at antibody-binding surfaces, whereas others mediate changes of the spike structure in local regions to interfere with antibody recognition. Overall, the structure of the Omicron spike reveals how mutations alter its conformation and explains its extraordinary ability to evade neutralizing antibodies. |*Cryoelectron Microscopy[MESH] |Antibodies, Neutralizing/chemistry/metabolism[MESH] |Humans[MESH] |Immune Evasion/genetics[MESH] |Models, Molecular[MESH] |Mutation[MESH] |Neutralization Tests[MESH] |Protein Binding[MESH] |Protein Structure, Quaternary[MESH] |SARS-CoV-2/*chemistry/genetics/ultrastructure[MESH]Cryo-EM structure of the SARS-CoV-2 Omicron spike (epmc).pdf DeepDyve Pubget Overpricing