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10.1038/s41594-020-0440-6 http://scihub22266oqcxt.onion/10.1038/s41594-020-0440-6 32382072!ä!32382072 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Struct+Mol+Biol 2020 ; 27 (6): 529-532 Nephropedia Template TP {{tp|p=32382072|t=2020. Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur |pdf=|usr=}}{{32382072}} gab.com Text Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=32382072 #FOAvip The antineoplastic drug carmofur is shown to inhibit the SARS-CoV-2 main protease (M(pro)). Here, the X-ray crystal structure of M(pro) in complex with carmofur reveals that the carbonyl reactive group of carmofur is covalently bound to catalytic Cys145, whereas its fatty acid tail occupies the hydrophobic S2 subsite. Carmofur inhibits viral replication in cells (EC(50) = 24.30 muM) and is a promising lead compound to develop new antiviral treatment for COVID-19. Twit Text FOAVip Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=32382072 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32382072 #FOAvip English Wikipedia <ref>{{Cite pmid|32382072}}</ref> Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur #MMPMID32382072 Jin Z; Zhao Y; Sun Y; Zhang B; Wang H; Wu Y; Zhu Y; Zhu C; Hu T; Du X; Duan Y; Yu J; Yang X; Yang X; Yang K; Liu X; Guddat LW; Xiao G; Zhang L; Yang H; Rao Z Nat Struct Mol Biol 2020[Jun]; 27 (6): 529-532 PMID32382072show ga The antineoplastic drug carmofur is shown to inhibit the SARS-CoV-2 main protease (M(pro)). Here, the X-ray crystal structure of M(pro) in complex with carmofur reveals that the carbonyl reactive group of carmofur is covalently bound to catalytic Cys145, whereas its fatty acid tail occupies the hydrophobic S2 subsite. Carmofur inhibits viral replication in cells (EC(50) = 24.30 muM) and is a promising lead compound to develop new antiviral treatment for COVID-19. |Animals[MESH] |Betacoronavirus/drug effects/*enzymology[MESH] |COVID-19[MESH] |Chlorocebus aethiops[MESH] |Coronavirus 3C Proteases[MESH] |Coronavirus Infections/virology[MESH] |Cysteine Endopeptidases/*chemistry/genetics/metabolism[MESH] |Fluorouracil/*analogs & derivatives/chemistry/pharmacology[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Pneumonia, Viral/virology[MESH] |SARS-CoV-2[MESH] |Vero Cells[MESH]Structural basis for the inhibition of SARS-CoV-2 main protease by ant(epmc).pdf DeepDyve Pubget Overpricing