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10.1128/AAC.00872-20 http://scihub22266oqcxt.onion/10.1128/AAC.00872-20 32669265!7449189!32669265     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32669265&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 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\32669265.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Antimicrob+Agents+Chemother 2020 ; 64 (9): ä Nephropedia Template TP {{tp|p=32669265|t=2020. Discovery of M Protease Inhibitors Encoded by SARS-CoV-2 |pdf=|usr=}}{{32669265}} gab.com Text Discovery of M Protease Inhibitors Encoded by SARS-CoV-2 JO: Antimicrob Agents Chemother http://www.kidney.de/pget.php?&tw=1&pmid=32669265 #FOAvip The coronavirus (CoV) disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome CoV-2 (SARS-CoV-2) is a health threat worldwide. Viral main protease (M(pro), also called 3C-like protease [3CL(pro)]) is a therapeutic target for drug discovery. Herein, we report that GC376, a broad-spectrum inhibitor targeting M(pro) in the picornavirus-like supercluster, is a potent inhibitor for the M(pro) encoded by SARS-CoV-2, with a half-maximum inhibitory concentration (IC(50)) of 26.4 +/- 1.1 nM. In this study, we also show that GC376 inhibits SARS-CoV-2 replication with a half-maximum effective concentration (EC(50)) of 0.91 +/- 0.03 muM. Only a small portion of SARS-CoV-2 M(pro) was covalently modified in the excess of GC376 as evaluated by mass spectrometry analysis, indicating that improved inhibitors are needed. Subsequently, molecular docking analysis revealed that the recognition and binding groups of GC376 within the active site of SARS-CoV-2 M(pro) provide important new information for the optimization of GC376. Given that sufficient safety and efficacy data are available for GC376 as an investigational veterinary drug, expedited development of GC376, or its optimized analogues, for treatment of SARS-CoV-2 infection in human is recommended. Twit Text FOAVip Discovery of M Protease Inhibitors Encoded by SARS-CoV-2 ????Antimicrob Agents Chemother http://www.kidney.de/pget.php?&tw=1&pmid=32669265 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32669265 #FOAvip English Wikipedia <ref>{{Cite pmid|32669265}}</ref> Discovery of M Protease Inhibitors Encoded by SARS-CoV-2 #MMPMID32669265 Hung HC; Ke YY; Huang SY; Huang PN; Kung YA; Chang TY; Yen KJ; Peng TT; Chang SE; Huang CT; Tsai YR; Wu SH; Lee SJ; Lin JH; Liu BS; Sung WC; Shih SR; Chen CT; Hsu JT Antimicrob Agents Chemother 2020[Aug]; 64 (9): ä PMID32669265show ga The coronavirus (CoV) disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome CoV-2 (SARS-CoV-2) is a health threat worldwide. Viral main protease (M(pro), also called 3C-like protease [3CL(pro)]) is a therapeutic target for drug discovery. Herein, we report that GC376, a broad-spectrum inhibitor targeting M(pro) in the picornavirus-like supercluster, is a potent inhibitor for the M(pro) encoded by SARS-CoV-2, with a half-maximum inhibitory concentration (IC(50)) of 26.4 +/- 1.1 nM. In this study, we also show that GC376 inhibits SARS-CoV-2 replication with a half-maximum effective concentration (EC(50)) of 0.91 +/- 0.03 muM. Only a small portion of SARS-CoV-2 M(pro) was covalently modified in the excess of GC376 as evaluated by mass spectrometry analysis, indicating that improved inhibitors are needed. Subsequently, molecular docking analysis revealed that the recognition and binding groups of GC376 within the active site of SARS-CoV-2 M(pro) provide important new information for the optimization of GC376. Given that sufficient safety and efficacy data are available for GC376 as an investigational veterinary drug, expedited development of GC376, or its optimized analogues, for treatment of SARS-CoV-2 infection in human is recommended. |Amino Acid Motifs[MESH] |Animals[MESH] |Antiviral Agents/*chemistry/pharmacology[MESH] |Betacoronavirus/*drug effects/pathogenicity[MESH] |Catalytic Domain[MESH] |Chlorocebus aethiops[MESH] |Coronavirus 3C Proteases[MESH] |Cysteine Endopeptidases/*chemistry/genetics/metabolism[MESH] |Gene Expression[MESH] |Molecular Docking Simulation[MESH] |Protease Inhibitors/*chemistry/pharmacology[MESH] |Protein Binding[MESH] |Protein Conformation, alpha-Helical[MESH] |Protein Conformation, beta-Strand[MESH] |Protein Interaction Domains and Motifs[MESH] |Pyrrolidines/*chemistry/pharmacology[MESH] |Recombinant Proteins/chemistry/genetics/metabolism[MESH] |SARS-CoV-2[MESH] |Sulfonic Acids[MESH] |Thermodynamics[MESH] |Vero Cells[MESH] |Viral Nonstructural Proteins/antagonists & inhibitors/*chemistry/genetics/metabolism[MESH]Discovery of M Protease Inhibitors Encoded by SARS-CoV-2 (epmc).pdf DeepDyve Pubget Overpricing