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10.3389/fmicb.2020.02112 http://scihub22266oqcxt.onion/10.3389/fmicb.2020.02112 33042039!7527407!33042039     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33042039&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       Front+Microbiol 2020 ; 11 (?): 2112 Nephropedia Template TP {{tp|p=33042039|t=2020. Flexible, Functional, and Familiar: Characteristics of SARS-CoV-2 Spike Protein Evolution |pdf=|usr=}}{{33042039}} gab.com Text Flexible, Functional, and Familiar: Characteristics of SARS-CoV-2 Spike Protein Evolution JO: Front Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=33042039 #FOAvip The SARS-CoV-2 S protein is a major point of interaction between the virus and the human immune system. As a consequence, the S protein is not a static target but undergoes rapid molecular evolution. In order to more fully understand the selection pressure during evolution, we examined residue positions in the S protein that vary greatly across closely related viruses but are conserved in the subset of viruses that infect humans. These "evolutionarily important" residues were not distributed evenly across the S protein but were concentrated in two domains: the N-terminal domain and the receptor-binding domain, both of which play a role in host cell binding in a number of related viruses. In addition to being localized in these two domains, evolutionary importance correlated with structural flexibility and inversely correlated with distance from known or predicted host receptor-binding residues. Finally, we observed a bias in the composition of the amino acids that make up such residues toward more human-like, rather than virus-like, sequence motifs. Twit Text FOAVip Flexible, Functional, and Familiar: Characteristics of SARS-CoV-2 Spike Protein Evolution ????Front Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=33042039 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33042039 #FOAvip English Wikipedia <ref>{{Cite pmid|33042039}}</ref> Flexible, Functional, and Familiar: Characteristics of SARS-CoV-2 Spike Protein Evolution #MMPMID33042039 Saputri DS; Li S; van Eerden FJ; Rozewicki J; Xu Z; Ismanto HS; Davila A; Teraguchi S; Katoh K; Standley DM Front Microbiol 2020[]; 11 (?): 2112 PMID33042039show ga The SARS-CoV-2 S protein is a major point of interaction between the virus and the human immune system. As a consequence, the S protein is not a static target but undergoes rapid molecular evolution. In order to more fully understand the selection pressure during evolution, we examined residue positions in the S protein that vary greatly across closely related viruses but are conserved in the subset of viruses that infect humans. These "evolutionarily important" residues were not distributed evenly across the S protein but were concentrated in two domains: the N-terminal domain and the receptor-binding domain, both of which play a role in host cell binding in a number of related viruses. In addition to being localized in these two domains, evolutionary importance correlated with structural flexibility and inversely correlated with distance from known or predicted host receptor-binding residues. Finally, we observed a bias in the composition of the amino acids that make up such residues toward more human-like, rather than virus-like, sequence motifs. ?Flexible, Functional, and Familiar: Characteristics of SARS-CoV-2 Spik(epmc).pdf DeepDyve Pubget Overpricing