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10.1038/s41594-020-0480-y http://scihub22266oqcxt.onion/10.1038/s41594-020-0480-y 32737466!ä!32737466 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 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       Nat+Struct+Mol+Biol 2020 ; 27 (10): 950-958 Nephropedia Template TP {{tp|p=32737466|t=2020. Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient |pdf=|usr=}}{{32737466}} gab.com Text Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=32737466 #FOAvip The COVID-19 pandemic has had an unprecedented health and economic impact and there are currently no approved therapies. We have isolated an antibody, EY6A, from an individual convalescing from COVID-19 and have shown that it neutralizes SARS-CoV-2 and cross-reacts with SARS-CoV-1. EY6A Fab binds the receptor binding domain (RBD) of the viral spike glycoprotein tightly (K(D) of 2 nM), and a 2.6-A-resolution crystal structure of an RBD-EY6A Fab complex identifies the highly conserved epitope, away from the ACE2 receptor binding site. Residues within this footprint are key to stabilizing the pre-fusion spike. Cryo-EM analyses of the pre-fusion spike incubated with EY6A Fab reveal a complex of the intact spike trimer with three Fabs bound and two further multimeric forms comprising the destabilized spike attached to Fab. EY6A binds what is probably a major neutralizing epitope, making it a candidate therapeutic for COVID-19. Twit Text FOAVip Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=32737466 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32737466 #FOAvip English Wikipedia <ref>{{Cite pmid|32737466}}</ref> Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient #MMPMID32737466 Zhou D; Duyvesteyn HME; Chen CP; Huang CG; Chen TH; Shih SR; Lin YC; Cheng CY; Cheng SH; Huang YC; Lin TY; Ma C; Huo J; Carrique L; Malinauskas T; Ruza RR; Shah PNM; Tan TK; Rijal P; Donat RF; Godwin K; Buttigieg KR; Tree JA; Radecke J; Paterson NG; Supasa P; Mongkolsapaya J; Screaton GR; Carroll MW; Gilbert-Jaramillo J; Knight ML; James W; Owens RJ; Naismith JH; Townsend AR; Fry EE; Zhao Y; Ren J; Stuart DI; Huang KA Nat Struct Mol Biol 2020[Oct]; 27 (10): 950-958 PMID32737466show ga The COVID-19 pandemic has had an unprecedented health and economic impact and there are currently no approved therapies. We have isolated an antibody, EY6A, from an individual convalescing from COVID-19 and have shown that it neutralizes SARS-CoV-2 and cross-reacts with SARS-CoV-1. EY6A Fab binds the receptor binding domain (RBD) of the viral spike glycoprotein tightly (K(D) of 2 nM), and a 2.6-A-resolution crystal structure of an RBD-EY6A Fab complex identifies the highly conserved epitope, away from the ACE2 receptor binding site. Residues within this footprint are key to stabilizing the pre-fusion spike. Cryo-EM analyses of the pre-fusion spike incubated with EY6A Fab reveal a complex of the intact spike trimer with three Fabs bound and two further multimeric forms comprising the destabilized spike attached to Fab. EY6A binds what is probably a major neutralizing epitope, making it a candidate therapeutic for COVID-19. |Adult[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Animals[MESH] |Antibodies, Neutralizing/immunology[MESH] |Antibodies, Viral/*chemistry/immunology/metabolism[MESH] |Betacoronavirus/*chemistry/immunology/metabolism[MESH] |Binding Sites[MESH] |COVID-19[MESH] |Chlorocebus aethiops[MESH] |Coronavirus Infections/*immunology[MESH] |Cross Reactions[MESH] |Cryoelectron Microscopy[MESH] |Crystallography, X-Ray[MESH] |Epitopes[MESH] |Humans[MESH] |Immunoglobulin Fab Fragments/chemistry/metabolism[MESH] |Male[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/metabolism[MESH] |Pneumonia, Viral/*immunology[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |SARS-CoV-2[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/immunology/metabolism[MESH]Structural basis for the neutralization of SARS-CoV-2 by an antibody f(epmc).pdf DeepDyve Pubget Overpricing