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10.1021/acs.jpclett.0c00571 http://scihub22266oqcxt.onion/10.1021/acs.jpclett.0c00571 32392072!ä!32392072 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Phys+Chem+Lett 2020 ; 11 (11): 4430-4435 Nephropedia Template TP {{tp|p=32392072|t=2020. Novel Coronavirus Polymerase and Nucleotidyl-Transferase Structures: Potential to Target New Outbreaks |pdf=|usr=}}{{32392072}} gab.com Text Novel Coronavirus Polymerase and Nucleotidyl-Transferase Structures: Potential to Target New Outbreaks JO: J Phys Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=32392072 #FOAvip The pandemic outbreak of a new coronavirus (CoV), SARS-CoV-2, has captured the world's attention, demonstrating that CoVs represent a continuous global threat. As this is a highly contagious virus, it is imperative to understand RNA-dependent-RNA-polymerase (RdRp), the key component in virus replication. Although the SARS-CoV-2 genome shares 80% sequence identity with severe acute respiratory syndrome SARS-CoV, their RdRps and nucleotidyl-transferases (NiRAN) share 98.1% and 93.2% identity, respectively. Sequence alignment of six coronaviruses demonstrated higher identity among their RdRps (60.9%-98.1%) and lower identity among their Spike proteins (27%-77%). Thus, a 3D structural model of RdRp, NiRAN, non-structural protein 7 (nsp7), and nsp8 of SARS-CoV-2 was generated by modeling starting from the SARS counterpart structures. Furthermore, we demonstrate the binding poses of three viral RdRp inhibitors (Galidesivir, Favipiravir, and Penciclovir), which were recently reported to have clinical significance for SARS-CoV-2. The network of interactions established by these drug molecules affirms their efficacy to inhibit viral RNA replication and provides an insight into their structure-based rational optimization for SARS-CoV-2 inhibition. Twit Text FOAVip Novel Coronavirus Polymerase and Nucleotidyl-Transferase Structures: Potential to Target New Outbreaks ????J Phys Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=32392072 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32392072 #FOAvip English Wikipedia <ref>{{Cite pmid|32392072}}</ref> Novel Coronavirus Polymerase and Nucleotidyl-Transferase Structures: Potential to Target New Outbreaks #MMPMID32392072 Zhang WF; Stephen P; Theriault JF; Wang R; Lin SX J Phys Chem Lett 2020[Jun]; 11 (11): 4430-4435 PMID32392072show ga The pandemic outbreak of a new coronavirus (CoV), SARS-CoV-2, has captured the world's attention, demonstrating that CoVs represent a continuous global threat. As this is a highly contagious virus, it is imperative to understand RNA-dependent-RNA-polymerase (RdRp), the key component in virus replication. Although the SARS-CoV-2 genome shares 80% sequence identity with severe acute respiratory syndrome SARS-CoV, their RdRps and nucleotidyl-transferases (NiRAN) share 98.1% and 93.2% identity, respectively. Sequence alignment of six coronaviruses demonstrated higher identity among their RdRps (60.9%-98.1%) and lower identity among their Spike proteins (27%-77%). Thus, a 3D structural model of RdRp, NiRAN, non-structural protein 7 (nsp7), and nsp8 of SARS-CoV-2 was generated by modeling starting from the SARS counterpart structures. Furthermore, we demonstrate the binding poses of three viral RdRp inhibitors (Galidesivir, Favipiravir, and Penciclovir), which were recently reported to have clinical significance for SARS-CoV-2. The network of interactions established by these drug molecules affirms their efficacy to inhibit viral RNA replication and provides an insight into their structure-based rational optimization for SARS-CoV-2 inhibition. |Adenine/analogs & derivatives/chemistry/metabolism[MESH] |Adenosine/analogs & derivatives[MESH] |Amides/chemistry/metabolism[MESH] |Antiviral Agents/chemistry/metabolism[MESH] |Betacoronavirus/*enzymology/isolation & purification[MESH] |Binding Sites[MESH] |COVID-19[MESH] |Coronavirus Infections/epidemiology/pathology/virology[MESH] |Humans[MESH] |Molecular Docking Simulation[MESH] |Nucleotidyltransferases/*chemistry/metabolism[MESH] |Pandemics[MESH] |Pneumonia, Viral/epidemiology/pathology/virology[MESH] |Protein Structure, Tertiary[MESH] |Pyrazines/chemistry/metabolism[MESH] |Pyrrolidines/chemistry/metabolism[MESH] |RNA-Dependent RNA Polymerase/*chemistry/metabolism[MESH]Novel Coronavirus Polymerase and Nucleotidyl-Transferase Structures: P(epmc).pdf DeepDyve Pubget Overpricing