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10.1126/sciadv.abf8711 http://scihub22266oqcxt.onion/10.1126/sciadv.abf8711 33853786!8046379!33853786     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 261.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 261.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 261.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 261.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Adv 2021 ; 7 (16): ä Nephropedia Template TP {{tp|p=33853786|t=2021. Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking |pdf=|usr=}}{{33853786}} gab.com Text Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking JO: Sci Adv http://www.kidney.de/pget.php?&tw=1&pmid=33853786 #FOAvip The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) macrodomain within the nonstructural protein 3 counteracts host-mediated antiviral adenosine diphosphate-ribosylation signaling. This enzyme is a promising antiviral target because catalytic mutations render viruses nonpathogenic. Here, we report a massive crystallographic screening and computational docking effort, identifying new chemical matter primarily targeting the active site of the macrodomain. Crystallographic screening of 2533 diverse fragments resulted in 214 unique macrodomain-binders. An additional 60 molecules were selected from docking more than 20 million fragments, of which 20 were crystallographically confirmed. X-ray data collection to ultra-high resolution and at physiological temperature enabled assessment of the conformational heterogeneity around the active site. Several fragment hits were confirmed by solution binding using three biophysical techniques (differential scanning fluorimetry, homogeneous time-resolved fluorescence, and isothermal titration calorimetry). The 234 fragment structures explore a wide range of chemotypes and provide starting points for development of potent SARS-CoV-2 macrodomain inhibitors. Twit Text FOAVip Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking ????Sci Adv http://www.kidney.de/pget.php?&tw=1&pmid=33853786 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33853786 #FOAvip English Wikipedia <ref>{{Cite pmid|33853786}}</ref> Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking #MMPMID33853786 Schuller M; Correy GJ; Gahbauer S; Fearon D; Wu T; Diaz RE; Young ID; Carvalho Martins L; Smith DH; Schulze-Gahmen U; Owens TW; Deshpande I; Merz GE; Thwin AC; Biel JT; Peters JK; Moritz M; Herrera N; Kratochvil HT; Aimon A; Bennett JM; Brandao Neto J; Cohen AE; Dias A; Douangamath A; Dunnett L; Fedorov O; Ferla MP; Fuchs MR; Gorrie-Stone TJ; Holton JM; Johnson MG; Krojer T; Meigs G; Powell AJ; Rack JGM; Rangel VL; Russi S; Skyner RE; Smith CA; Soares AS; Wierman JL; Zhu K; O'Brien P; Jura N; Ashworth A; Irwin JJ; Thompson MC; Gestwicki JE; von Delft F; Shoichet BK; Fraser JS; Ahel I Sci Adv 2021[Apr]; 7 (16): ä PMID33853786show ga The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) macrodomain within the nonstructural protein 3 counteracts host-mediated antiviral adenosine diphosphate-ribosylation signaling. This enzyme is a promising antiviral target because catalytic mutations render viruses nonpathogenic. Here, we report a massive crystallographic screening and computational docking effort, identifying new chemical matter primarily targeting the active site of the macrodomain. Crystallographic screening of 2533 diverse fragments resulted in 214 unique macrodomain-binders. An additional 60 molecules were selected from docking more than 20 million fragments, of which 20 were crystallographically confirmed. X-ray data collection to ultra-high resolution and at physiological temperature enabled assessment of the conformational heterogeneity around the active site. Several fragment hits were confirmed by solution binding using three biophysical techniques (differential scanning fluorimetry, homogeneous time-resolved fluorescence, and isothermal titration calorimetry). The 234 fragment structures explore a wide range of chemotypes and provide starting points for development of potent SARS-CoV-2 macrodomain inhibitors. |COVID-19 Drug Treatment[MESH] |Catalytic Domain/genetics/*physiology[MESH] |Crystallography, X-Ray[MESH] |Humans[MESH] |Models, Molecular[MESH] |Molecular Docking Simulation[MESH] |Protein Binding/*physiology[MESH] |Protein Conformation[MESH] |SARS-CoV-2/genetics/physiology[MESH]Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified thro(epmc).pdf DeepDyve Pubget Overpricing