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.

10.1021/acsinfecdis.1c00237 http://scihub22266oqcxt.onion/10.1021/acsinfecdis.1c00237 34437808!8424689!34437808     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Infect+Dis 2021 ; 7 (9): 2591-2595 Nephropedia Template TP {{tp|p=34437808|t=2021. Recognition of Divergent Viral Substrates by the SARS-CoV-2 Main Protease |pdf=|usr=}}{{34437808}} gab.com Text Recognition of Divergent Viral Substrates by the SARS-CoV-2 Main Protease JO: ACS Infect Dis http://www.kidney.de/pget.php?&tw=1&pmid=34437808 #FOAvip The main protease (M(pro)) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the cause of coronavirus disease (COVID-19), is an ideal target for pharmaceutical inhibition. M(pro) is conserved among coronaviruses and distinct from human proteases. Viral replication depends on the cleavage of the viral polyprotein at multiple sites. We present crystal structures of SARS-CoV-2 M(pro) bound to two viral substrate peptides. The structures show how M(pro) recognizes distinct substrates and how subtle changes in substrate accommodation can drive large changes in catalytic efficiency. One peptide, constituting the junction between viral nonstructural proteins 8 and 9 (nsp8/9), has P1' and P2' residues that are unique among the SARS-CoV-2 M(pro) cleavage sites but conserved among homologous junctions in coronaviruses. M(pro) cleaves nsp8/9 inefficiently, and amino acid substitutions at P1' or P2' can enhance catalysis. Visualization of M(pro) with intact substrates provides new templates for antiviral drug design and suggests that the coronavirus lifecycle selects for finely tuned substrate-dependent catalytic parameters. Twit Text FOAVip Recognition of Divergent Viral Substrates by the SARS-CoV-2 Main Protease ????ACS Infect Dis http://www.kidney.de/pget.php?&tw=1&pmid=34437808 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34437808 #FOAvip English Wikipedia <ref>{{Cite pmid|34437808}}</ref> Recognition of Divergent Viral Substrates by the SARS-CoV-2 Main Protease #MMPMID34437808 MacDonald EA; Frey G; Namchuk MN; Harrison SC; Hinshaw SM; Windsor IW ACS Infect Dis 2021[Sep]; 7 (9): 2591-2595 PMID34437808show ga The main protease (M(pro)) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the cause of coronavirus disease (COVID-19), is an ideal target for pharmaceutical inhibition. M(pro) is conserved among coronaviruses and distinct from human proteases. Viral replication depends on the cleavage of the viral polyprotein at multiple sites. We present crystal structures of SARS-CoV-2 M(pro) bound to two viral substrate peptides. The structures show how M(pro) recognizes distinct substrates and how subtle changes in substrate accommodation can drive large changes in catalytic efficiency. One peptide, constituting the junction between viral nonstructural proteins 8 and 9 (nsp8/9), has P1' and P2' residues that are unique among the SARS-CoV-2 M(pro) cleavage sites but conserved among homologous junctions in coronaviruses. M(pro) cleaves nsp8/9 inefficiently, and amino acid substitutions at P1' or P2' can enhance catalysis. Visualization of M(pro) with intact substrates provides new templates for antiviral drug design and suggests that the coronavirus lifecycle selects for finely tuned substrate-dependent catalytic parameters. |*COVID-19[MESH] |*SARS-CoV-2[MESH] |Antiviral Agents[MESH] |Coronavirus 3C Proteases/*metabolism[MESH] |Humans[MESH] |Peptide Hydrolases[MESH]Recognition of Divergent Viral Substrates by the SARS-CoV-2 Main Prote(epmc).pdf DeepDyve Pubget Overpricing