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.

10.7150/ijbs.59191 http://scihub22266oqcxt.onion/10.7150/ijbs.59191 33907519!8071767!33907519     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Int+J+Biol+Sci 2021 ; 17 (6): 1555-1564 Nephropedia Template TP {{tp|p=33907519|t=2021. In silico structure-based discovery of a SARS-CoV-2 main protease inhibitor |pdf=|usr=}}{{33907519}} gab.com Text In silico structure-based discovery of a SARS-CoV-2 main protease inhibitor JO: Int J Biol Sci http://www.kidney.de/pget.php?&tw=1&pmid=33907519 #FOAvip The Coronavirus Disease 2019 (COVID-19) pandemic caused by the novel lineage B betacoroanvirus severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in significant mortality, morbidity, and socioeconomic disruptions worldwide. Effective antivirals are urgently needed for COVID-19. The main protease (M(pro)) of SARS-CoV-2 is an attractive antiviral target because of its essential role in the cleavage of the viral polypeptide. In this study, we performed an in silico structure-based screening of a large chemical library to identify potential SARS-CoV-2 M(pro) inhibitors. Among 8,820 compounds in the library, our screening identified trichostatin A, a histone deacetylase inhibitor and an antifungal compound, as an inhibitor of SARS-CoV-2 M(pro) activity and replication. The half maximal effective concentration of trichostatin A against SARS-CoV-2 replication was 1.5 to 2.7microM, which was markedly below its 50% effective cytotoxic concentration (75.7microM) and peak serum concentration (132microM). Further drug compound optimization to develop more stable analogues with longer half-lives should be performed. This structure-based drug discovery platform should facilitate the identification of additional enzyme inhibitors of SARS-CoV-2. Twit Text FOAVip In silico structure-based discovery of a SARS-CoV-2 main protease inhibitor ????Int J Biol Sci http://www.kidney.de/pget.php?&tw=1&pmid=33907519 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33907519 #FOAvip English Wikipedia <ref>{{Cite pmid|33907519}}</ref> In silico structure-based discovery of a SARS-CoV-2 main protease inhibitor #MMPMID33907519 Wen L; Tang K; Chik KK; Chan CC; Tsang JO; Liang R; Cao J; Huang Y; Luo C; Cai JP; Ye ZW; Yin F; Chu H; Jin DY; Yuen KY; Yuan S; Chan JF Int J Biol Sci 2021[]; 17 (6): 1555-1564 PMID33907519show ga The Coronavirus Disease 2019 (COVID-19) pandemic caused by the novel lineage B betacoroanvirus severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in significant mortality, morbidity, and socioeconomic disruptions worldwide. Effective antivirals are urgently needed for COVID-19. The main protease (M(pro)) of SARS-CoV-2 is an attractive antiviral target because of its essential role in the cleavage of the viral polypeptide. In this study, we performed an in silico structure-based screening of a large chemical library to identify potential SARS-CoV-2 M(pro) inhibitors. Among 8,820 compounds in the library, our screening identified trichostatin A, a histone deacetylase inhibitor and an antifungal compound, as an inhibitor of SARS-CoV-2 M(pro) activity and replication. The half maximal effective concentration of trichostatin A against SARS-CoV-2 replication was 1.5 to 2.7microM, which was markedly below its 50% effective cytotoxic concentration (75.7microM) and peak serum concentration (132microM). Further drug compound optimization to develop more stable analogues with longer half-lives should be performed. This structure-based drug discovery platform should facilitate the identification of additional enzyme inhibitors of SARS-CoV-2. |Animals[MESH] |Caco-2 Cells[MESH] |Chlorocebus aethiops[MESH] |Computer Simulation[MESH] |Coronavirus 3C Proteases/*antagonists & inhibitors[MESH] |Drug Discovery[MESH] |Drug Evaluation, Preclinical[MESH] |Humans[MESH] |Molecular Docking Simulation[MESH] |Molecular Structure[MESH] |Protease Inhibitors/chemistry/*pharmacology[MESH]In silico structure-based discovery of a SARS-CoV-2 main protease inhi(epmc).pdf DeepDyve Pubget Overpricing