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10.1038/s41594-021-00570-0 http://scihub22266oqcxt.onion/10.1038/s41594-021-00570-0 33674802!ä!33674802 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 2021 ; 28 (3): 319-325 Nephropedia Template TP {{tp|p=33674802|t=2021. Structural basis for inhibition of the SARS-CoV-2 RNA polymerase by suramin |pdf=|usr=}}{{33674802}} gab.com Text Structural basis for inhibition of the SARS-CoV-2 RNA polymerase by suramin JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=33674802 #FOAvip The COVID-19 pandemic caused by nonstop infections of SARS-CoV-2 has continued to ravage many countries worldwide. Here we report that suramin, a 100-year-old drug, is a potent inhibitor of the SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) and acts by blocking the binding of RNA to the enzyme. In biochemical assays, suramin and its derivatives are at least 20-fold more potent than remdesivir, the currently approved nucleotide drug for treatment of COVID-19. The 2.6 A cryo-electron microscopy structure of the viral RdRp bound to suramin reveals two binding sites. One site directly blocks the binding of the RNA template strand and the other site clashes with the RNA primer strand near the RdRp catalytic site, thus inhibiting RdRp activity. Suramin blocks viral replication in Vero E6 cells, although the reasons underlying this effect are likely various. Our results provide a structural mechanism for a nonnucleotide inhibitor of the SARS-CoV-2 RdRp. Twit Text FOAVip Structural basis for inhibition of the SARS-CoV-2 RNA polymerase by suramin ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=33674802 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33674802 #FOAvip English Wikipedia <ref>{{Cite pmid|33674802}}</ref> Structural basis for inhibition of the SARS-CoV-2 RNA polymerase by suramin #MMPMID33674802 Yin W; Luan X; Li Z; Zhou Z; Wang Q; Gao M; Wang X; Zhou F; Shi J; You E; Liu M; Wang Q; Jiang Y; Jiang H; Xiao G; Zhang L; Yu X; Zhang S; Eric Xu H Nat Struct Mol Biol 2021[Mar]; 28 (3): 319-325 PMID33674802show ga The COVID-19 pandemic caused by nonstop infections of SARS-CoV-2 has continued to ravage many countries worldwide. Here we report that suramin, a 100-year-old drug, is a potent inhibitor of the SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) and acts by blocking the binding of RNA to the enzyme. In biochemical assays, suramin and its derivatives are at least 20-fold more potent than remdesivir, the currently approved nucleotide drug for treatment of COVID-19. The 2.6 A cryo-electron microscopy structure of the viral RdRp bound to suramin reveals two binding sites. One site directly blocks the binding of the RNA template strand and the other site clashes with the RNA primer strand near the RdRp catalytic site, thus inhibiting RdRp activity. Suramin blocks viral replication in Vero E6 cells, although the reasons underlying this effect are likely various. Our results provide a structural mechanism for a nonnucleotide inhibitor of the SARS-CoV-2 RdRp. |Animals[MESH] |Antiviral Agents/chemistry/metabolism/*pharmacology[MESH] |Binding Sites[MESH] |Catalytic Domain[MESH] |Chlorocebus aethiops[MESH] |Coronavirus RNA-Dependent RNA Polymerase/*antagonists & inhibitors/*chemistry/metabolism[MESH] |Cryoelectron Microscopy[MESH] |Enzyme Inhibitors/chemistry/metabolism/*pharmacology[MESH] |Protein Conformation[MESH] |RNA, Viral/chemistry/metabolism[MESH] |SARS-CoV-2/drug effects[MESH] |Suramin/chemistry/metabolism/*pharmacology[MESH] |Vero Cells[MESH]Structural basis for inhibition of the SARS-CoV-2 RNA polymerase by su(epmc).pdf DeepDyve Pubget Overpricing