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10.1016/j.xinn.2021.100080 http://scihub22266oqcxt.onion/10.1016/j.xinn.2021.100080 33521757!7834001!33521757     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Innovation+(Camb) 2021 ; 2 (1): 100080 Nephropedia Template TP {{tp|p=33521757|t=2021. Structural Basis of SARS-CoV-2 Polymerase Inhibition by Favipiravir |pdf=|usr=}}{{33521757}} gab.com Text Structural Basis of SARS-CoV-2 Polymerase Inhibition by Favipiravir JO: Innovation (Camb) http://www.kidney.de/pget.php?&tw=1&pmid=33521757 #FOAvip The outbreak of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has developed into an unprecedented global pandemic. Nucleoside analogs, such as Remdesivir and Favipiravir, can serve as the first-line broad-spectrum antiviral drugs by targeting the viral polymerases. However, the underlying mechanisms for the antiviral efficacies of these drugs are far from well understood. Here, we reveal that Favipiravir, as a pyrazine derivative, could be incorporated into the viral RNA products by mimicking both adenine and guanine nucleotides. This drug thus inhibits viral replication mainly by inducing mutations in progeny RNAs, different from Remdesivir or other RNA-terminating nucleoside analogs that impair the elongation of RNA products. We further determined the cryo-EM structure of Favipiravir bound to the replicating polymerase complex of SARS-CoV-2 in the pre-catalytic state. This structure provides a missing snapshot for visualizing the catalysis dynamics of coronavirus polymerase, and reveals an unexpected base-pairing pattern between Favipiravir and pyrimidine residues that may explain its capacity for mimicking both adenine and guanine nucleotides. These findings shed light on the mechanism of coronavirus polymerase catalysis and provide a rational basis for developing antiviral drugs to combat the SARS-CoV-2 pandemic. Twit Text FOAVip Structural Basis of SARS-CoV-2 Polymerase Inhibition by Favipiravir ????Innovation (Camb) http://www.kidney.de/pget.php?&tw=1&pmid=33521757 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33521757 #FOAvip English Wikipedia <ref>{{Cite pmid|33521757}}</ref> Structural Basis of SARS-CoV-2 Polymerase Inhibition by Favipiravir #MMPMID33521757 Peng Q; Peng R; Yuan B; Wang M; Zhao J; Fu L; Qi J; Shi Y Innovation (Camb) 2021[Feb]; 2 (1): 100080 PMID33521757show ga The outbreak of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has developed into an unprecedented global pandemic. Nucleoside analogs, such as Remdesivir and Favipiravir, can serve as the first-line broad-spectrum antiviral drugs by targeting the viral polymerases. However, the underlying mechanisms for the antiviral efficacies of these drugs are far from well understood. Here, we reveal that Favipiravir, as a pyrazine derivative, could be incorporated into the viral RNA products by mimicking both adenine and guanine nucleotides. This drug thus inhibits viral replication mainly by inducing mutations in progeny RNAs, different from Remdesivir or other RNA-terminating nucleoside analogs that impair the elongation of RNA products. We further determined the cryo-EM structure of Favipiravir bound to the replicating polymerase complex of SARS-CoV-2 in the pre-catalytic state. This structure provides a missing snapshot for visualizing the catalysis dynamics of coronavirus polymerase, and reveals an unexpected base-pairing pattern between Favipiravir and pyrimidine residues that may explain its capacity for mimicking both adenine and guanine nucleotides. These findings shed light on the mechanism of coronavirus polymerase catalysis and provide a rational basis for developing antiviral drugs to combat the SARS-CoV-2 pandemic. äStructural Basis of SARS-CoV-2 Polymerase Inhibition by Favipiravir (epmc).pdf DeepDyve Pubget Overpricing