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10.1038/s41467-020-18709-w http://scihub22266oqcxt.onion/10.1038/s41467-020-18709-w 33028810!7542442!33028810     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 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       Nat+Commun 2020 ; 11 (1): 5047 Nephropedia Template TP {{tp|p=33028810|t=2020. Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease |pdf=|usr=}}{{33028810}} gab.com Text Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=33028810 #FOAvip COVID-19, caused by SARS-CoV-2, lacks effective therapeutics. Additionally, no antiviral drugs or vaccines were developed against the closely related coronavirus, SARS-CoV-1 or MERS-CoV, despite previous zoonotic outbreaks. To identify starting points for such therapeutics, we performed a large-scale screen of electrophile and non-covalent fragments through a combined mass spectrometry and X-ray approach against the SARS-CoV-2 main protease, one of two cysteine viral proteases essential for viral replication. Our crystallographic screen identified 71 hits that span the entire active site, as well as 3 hits at the dimer interface. These structures reveal routes to rapidly develop more potent inhibitors through merging of covalent and non-covalent fragment hits; one series of low-reactivity, tractable covalent fragments were progressed to discover improved binders. These combined hits offer unprecedented structural and reactivity information for on-going structure-based drug design against SARS-CoV-2 main protease. Twit Text FOAVip Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=33028810 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33028810 #FOAvip English Wikipedia <ref>{{Cite pmid|33028810}}</ref> Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease #MMPMID33028810 Douangamath A; Fearon D; Gehrtz P; Krojer T; Lukacik P; Owen CD; Resnick E; Strain-Damerell C; Aimon A; Abranyi-Balogh P; Brandao-Neto J; Carbery A; Davison G; Dias A; Downes TD; Dunnett L; Fairhead M; Firth JD; Jones SP; Keeley A; Keseru GM; Klein HF; Martin MP; Noble MEM; O'Brien P; Powell A; Reddi RN; Skyner R; Snee M; Waring MJ; Wild C; London N; von Delft F; Walsh MA Nat Commun 2020[Oct]; 11 (1): 5047 PMID33028810show ga COVID-19, caused by SARS-CoV-2, lacks effective therapeutics. Additionally, no antiviral drugs or vaccines were developed against the closely related coronavirus, SARS-CoV-1 or MERS-CoV, despite previous zoonotic outbreaks. To identify starting points for such therapeutics, we performed a large-scale screen of electrophile and non-covalent fragments through a combined mass spectrometry and X-ray approach against the SARS-CoV-2 main protease, one of two cysteine viral proteases essential for viral replication. Our crystallographic screen identified 71 hits that span the entire active site, as well as 3 hits at the dimer interface. These structures reveal routes to rapidly develop more potent inhibitors through merging of covalent and non-covalent fragment hits; one series of low-reactivity, tractable covalent fragments were progressed to discover improved binders. These combined hits offer unprecedented structural and reactivity information for on-going structure-based drug design against SARS-CoV-2 main protease. |Betacoronavirus/*chemistry/enzymology[MESH] |Binding Sites[MESH] |Catalytic Domain[MESH] |Coronavirus 3C Proteases[MESH] |Crystallography, X-Ray[MESH] |Cysteine Endopeptidases/*chemistry/metabolism[MESH] |Drug Design[MESH] |Mass Spectrometry[MESH] |Models, Molecular[MESH] |Peptide Fragments/*chemistry/metabolism[MESH] |Protein Conformation[MESH] |SARS-CoV-2[MESH] |Small Molecule Libraries/chemistry/metabolism[MESH] |Static Electricity[MESH]Crystallographic and electrophilic fragment screening of the SARS-CoV-(epmc).pdf DeepDyve Pubget Overpricing