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10.1126/science.abb4489 http://scihub22266oqcxt.onion/10.1126/science.abb4489 32321856!7179937!32321856     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2020 ; 368 (6497): 1331-1335 Nephropedia Template TP {{tp|p=32321856|t=2020. Structure-based design of antiviral drug candidates targeting the SARS-CoV-2 main protease |pdf=|usr=}}{{32321856}} gab.com Text Structure-based design of antiviral drug candidates targeting the SARS-CoV-2 main protease JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32321856 #FOAvip SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) is the etiological agent responsible for the global COVID-19 (coronavirus disease 2019) outbreak. The main protease of SARS-CoV-2, M(pro), is a key enzyme that plays a pivotal role in mediating viral replication and transcription. We designed and synthesized two lead compounds (11a and 11b) targeting M(pro) Both exhibited excellent inhibitory activity and potent anti-SARS-CoV-2 infection activity. The x-ray crystal structures of SARS-CoV-2 M(pro) in complex with 11a or 11b, both determined at a resolution of 1.5 angstroms, showed that the aldehyde groups of 11a and 11b are covalently bound to cysteine 145 of M(pro) Both compounds showed good pharmacokinetic properties in vivo, and 11a also exhibited low toxicity, which suggests that these compounds are promising drug candidates. Twit Text FOAVip Structure-based design of antiviral drug candidates targeting the SARS-CoV-2 main protease ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32321856 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32321856 #FOAvip English Wikipedia <ref>{{Cite pmid|32321856}}</ref> Structure-based design of antiviral drug candidates targeting the SARS-CoV-2 main protease #MMPMID32321856 Dai W; Zhang B; Jiang XM; Su H; Li J; Zhao Y; Xie X; Jin Z; Peng J; Liu F; Li C; Li Y; Bai F; Wang H; Cheng X; Cen X; Hu S; Yang X; Wang J; Liu X; Xiao G; Jiang H; Rao Z; Zhang LK; Xu Y; Yang H; Liu H Science 2020[Jun]; 368 (6497): 1331-1335 PMID32321856show ga SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) is the etiological agent responsible for the global COVID-19 (coronavirus disease 2019) outbreak. The main protease of SARS-CoV-2, M(pro), is a key enzyme that plays a pivotal role in mediating viral replication and transcription. We designed and synthesized two lead compounds (11a and 11b) targeting M(pro) Both exhibited excellent inhibitory activity and potent anti-SARS-CoV-2 infection activity. The x-ray crystal structures of SARS-CoV-2 M(pro) in complex with 11a or 11b, both determined at a resolution of 1.5 angstroms, showed that the aldehyde groups of 11a and 11b are covalently bound to cysteine 145 of M(pro) Both compounds showed good pharmacokinetic properties in vivo, and 11a also exhibited low toxicity, which suggests that these compounds are promising drug candidates. |*Drug Design[MESH] |Animals[MESH] |Antiviral Agents/*chemistry/pharmacology[MESH] |Betacoronavirus/drug effects/*enzymology[MESH] |COVID-19[MESH] |Catalytic Domain[MESH] |Chlorocebus aethiops[MESH] |Coronavirus 3C Proteases[MESH] |Coronavirus Infections/drug therapy[MESH] |Cysteine Endopeptidases[MESH] |Dogs[MESH] |Drug Evaluation, Preclinical[MESH] |Female[MESH] |Humans[MESH] |Male[MESH] |Mice[MESH] |Molecular Structure[MESH] |Pandemics[MESH] |Pneumonia, Viral/drug therapy[MESH] |Protein Structure, Tertiary[MESH] |Rats, Sprague-Dawley[MESH] |SARS-CoV-2[MESH] |Toxicity Tests[MESH] |Vero Cells[MESH]Structure-based design of antiviral drug candidates targeting the SARS(epmc).pdf DeepDyve Pubget Overpricing