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10.1126/science.abc1560 http://scihub22266oqcxt.onion/10.1126/science.abc1560 32358203!7199908!32358203     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 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2020 ; 368 (6498): 1499-1504 Nephropedia Template TP {{tp|p=32358203|t=2020. Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir |pdf=|usr=}}{{32358203}} gab.com Text Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32358203 #FOAvip The pandemic of coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has become a global crisis. Replication of SARS-CoV-2 requires the viral RNA-dependent RNA polymerase (RdRp) enzyme, a target of the antiviral drug remdesivir. Here we report the cryo-electron microscopy structure of the SARS-CoV-2 RdRp, both in the apo form at 2.8-angstrom resolution and in complex with a 50-base template-primer RNA and remdesivir at 2.5-angstrom resolution. The complex structure reveals that the partial double-stranded RNA template is inserted into the central channel of the RdRp, where remdesivir is covalently incorporated into the primer strand at the first replicated base pair, and terminates chain elongation. Our structures provide insights into the mechanism of viral RNA replication and a rational template for drug design to combat the viral infection. Twit Text FOAVip Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32358203 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32358203 #FOAvip English Wikipedia <ref>{{Cite pmid|32358203}}</ref> Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir #MMPMID32358203 Yin W; Mao C; Luan X; Shen DD; Shen Q; Su H; Wang X; Zhou F; Zhao W; Gao M; Chang S; Xie YC; Tian G; Jiang HW; Tao SC; Shen J; Jiang Y; Jiang H; Xu Y; Zhang S; Zhang Y; Xu HE Science 2020[Jun]; 368 (6498): 1499-1504 PMID32358203show ga The pandemic of coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has become a global crisis. Replication of SARS-CoV-2 requires the viral RNA-dependent RNA polymerase (RdRp) enzyme, a target of the antiviral drug remdesivir. Here we report the cryo-electron microscopy structure of the SARS-CoV-2 RdRp, both in the apo form at 2.8-angstrom resolution and in complex with a 50-base template-primer RNA and remdesivir at 2.5-angstrom resolution. The complex structure reveals that the partial double-stranded RNA template is inserted into the central channel of the RdRp, where remdesivir is covalently incorporated into the primer strand at the first replicated base pair, and terminates chain elongation. Our structures provide insights into the mechanism of viral RNA replication and a rational template for drug design to combat the viral infection. |Adenosine Monophosphate/*analogs & derivatives/chemistry/metabolism/pharmacology[MESH] |Alanine/*analogs & derivatives/chemistry/metabolism/pharmacology[MESH] |Antiviral Agents/*chemistry/metabolism/pharmacology[MESH] |Betacoronavirus/drug effects/*enzymology/physiology[MESH] |Catalytic Domain[MESH] |Coronavirus RNA-Dependent RNA Polymerase[MESH] |Cryoelectron Microscopy[MESH] |Enzyme Inhibitors/chemistry/metabolism/pharmacology[MESH] |Models, Molecular[MESH] |Multiprotein Complexes/chemistry[MESH] |Protein Conformation[MESH] |RNA, Viral/chemistry/metabolism[MESH] |RNA-Dependent RNA Polymerase/*antagonists & inhibitors/*chemistry/metabolism[MESH] |SARS-CoV-2[MESH] |Viral Nonstructural Proteins/*antagonists & inhibitors/*chemistry/metabolism[MESH]Structural basis for inhibition of the RNA-dependent RNA polymerase fr(epmc).pdf DeepDyve Pubget Overpricing