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10.1038/s41467-021-21060-3 http://scihub22266oqcxt.onion/10.1038/s41467-021-21060-3 33531496!7854729!33531496     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2021 ; 12 (1): 743 Nephropedia Template TP {{tp|p=33531496|t=2021. Structure of papain-like protease from SARS-CoV-2 and its complexes with non-covalent inhibitors |pdf=|usr=}}{{33531496}} gab.com Text Structure of papain-like protease from SARS-CoV-2 and its complexes with non-covalent inhibitors JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=33531496 #FOAvip The pandemic caused by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) continues to expand. Papain-like protease (PLpro) is one of two SARS-CoV-2 proteases potentially targetable with antivirals. PLpro is an attractive target because it plays an essential role in cleavage and maturation of viral polyproteins, assembly of the replicase-transcriptase complex, and disruption of host responses. We report a substantive body of structural, biochemical, and virus replication studies that identify several inhibitors of the SARS-CoV-2 enzyme. We determined the high resolution structure of wild-type PLpro, the active site C111S mutant, and their complexes with inhibitors. This collection of structures details inhibitors recognition and interactions providing fundamental molecular and mechanistic insight into PLpro. All compounds inhibit the peptidase activity of PLpro in vitro, some block SARS-CoV-2 replication in cell culture assays. These findings will accelerate structure-based drug design efforts targeting PLpro to identify high-affinity inhibitors of clinical value. Twit Text FOAVip Structure of papain-like protease from SARS-CoV-2 and its complexes with non-covalent inhibitors ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=33531496 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33531496 #FOAvip English Wikipedia <ref>{{Cite pmid|33531496}}</ref> Structure of papain-like protease from SARS-CoV-2 and its complexes with non-covalent inhibitors #MMPMID33531496 Osipiuk J; Azizi SA; Dvorkin S; Endres M; Jedrzejczak R; Jones KA; Kang S; Kathayat RS; Kim Y; Lisnyak VG; Maki SL; Nicolaescu V; Taylor CA; Tesar C; Zhang YA; Zhou Z; Randall G; Michalska K; Snyder SA; Dickinson BC; Joachimiak A Nat Commun 2021[Feb]; 12 (1): 743 PMID33531496show ga The pandemic caused by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) continues to expand. Papain-like protease (PLpro) is one of two SARS-CoV-2 proteases potentially targetable with antivirals. PLpro is an attractive target because it plays an essential role in cleavage and maturation of viral polyproteins, assembly of the replicase-transcriptase complex, and disruption of host responses. We report a substantive body of structural, biochemical, and virus replication studies that identify several inhibitors of the SARS-CoV-2 enzyme. We determined the high resolution structure of wild-type PLpro, the active site C111S mutant, and their complexes with inhibitors. This collection of structures details inhibitors recognition and interactions providing fundamental molecular and mechanistic insight into PLpro. All compounds inhibit the peptidase activity of PLpro in vitro, some block SARS-CoV-2 replication in cell culture assays. These findings will accelerate structure-based drug design efforts targeting PLpro to identify high-affinity inhibitors of clinical value. |Antiviral Agents/pharmacology[MESH] |Humans[MESH] |Mutation[MESH] |Papain/*metabolism[MESH] |Peptide Hydrolases/*metabolism[MESH] |Polyproteins/metabolism[MESH] |SARS-CoV-2/*drug effects/*enzymology[MESH] |Substrate Specificity[MESH]Structure of papain-like protease from SARS-CoV-2 and its complexes wi(epmc).pdf DeepDyve Pubget Overpricing