Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1126/science.abi9745 http://scihub22266oqcxt.onion/10.1126/science.abi9745 34168070!9245151!34168070     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       Science 2021 ; 373 (6555): 642-648 Nephropedia Template TP {{tp|p=34168070|t=2021. Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants |pdf=|usr=}}{{34168070}} gab.com Text Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=34168070 #FOAvip Several fast-spreading variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have become the dominant circulating strains in the COVID-19 pandemic. We report here cryo-electron microscopy structures of the full-length spike (S) trimers of the B.1.1.7 and B.1.351 variants, as well as their biochemical and antigenic properties. Amino acid substitutions in the B.1.1.7 protein increase both the accessibility of its receptor binding domain and the binding affinity for receptor angiotensin-converting enzyme 2 (ACE2). The enhanced receptor engagement may account for the increased transmissibility. The B.1.351 variant has evolved to reshape antigenic surfaces of the major neutralizing sites on the S protein, making it resistant to some potent neutralizing antibodies. These findings provide structural details on how SARS-CoV-2 has evolved to enhance viral fitness and immune evasion. Twit Text FOAVip Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants ????Science http://www.kidney.de/pget.php?&tw=1&pmid=34168070 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34168070 #FOAvip English Wikipedia <ref>{{Cite pmid|34168070}}</ref> Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants #MMPMID34168070 Cai Y; Zhang J; Xiao T; Lavine CL; Rawson S; Peng H; Zhu H; Anand K; Tong P; Gautam A; Lu S; Sterling SM; Walsh RM Jr; Rits-Volloch S; Lu J; Wesemann DR; Yang W; Seaman MS; Chen B Science 2021[Aug]; 373 (6555): 642-648 PMID34168070show ga Several fast-spreading variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have become the dominant circulating strains in the COVID-19 pandemic. We report here cryo-electron microscopy structures of the full-length spike (S) trimers of the B.1.1.7 and B.1.351 variants, as well as their biochemical and antigenic properties. Amino acid substitutions in the B.1.1.7 protein increase both the accessibility of its receptor binding domain and the binding affinity for receptor angiotensin-converting enzyme 2 (ACE2). The enhanced receptor engagement may account for the increased transmissibility. The B.1.351 variant has evolved to reshape antigenic surfaces of the major neutralizing sites on the S protein, making it resistant to some potent neutralizing antibodies. These findings provide structural details on how SARS-CoV-2 has evolved to enhance viral fitness and immune evasion. |*Immune Evasion[MESH] |Amino Acid Substitution[MESH] |Angiotensin-Converting Enzyme 2/metabolism[MESH] |Antibodies, Viral/immunology[MESH] |Antigens, Viral/immunology[MESH] |COVID-19/*virology[MESH] |Cryoelectron Microscopy[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Models, Molecular[MESH] |Mutation[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Protein Interaction Domains and Motifs[MESH] |Protein Subunits/chemistry[MESH] |Receptors, Coronavirus/metabolism[MESH] |SARS-CoV-2/*chemistry/genetics/immunology/*pathogenicity[MESH]Structural basis for enhanced infectivity and immune evasion of SARS-C(epmc).pdf DeepDyve Pubget Overpricing