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10.1002/btpr.3110 http://scihub22266oqcxt.onion/10.1002/btpr.3110 33314794!7883068!33314794     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 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 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 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biotechnol+Prog 2021 ; 37 (2): e3110 Nephropedia Template TP {{tp|p=33314794|t=2021. Computational drug repurposing study of the RNA binding domain of SARS-CoV-2 nucleocapsid protein with antiviral agents |pdf=|usr=}}{{33314794}} gab.com Text Computational drug repurposing study of the RNA binding domain of SARS-CoV-2 nucleocapsid protein with antiviral agents JO: Biotechnol Prog http://www.kidney.de/pget.php?&tw=1&pmid=33314794 #FOAvip The recent outbreak of coronavirus disease (COVID-19) in China caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has led to worldwide human infections and deaths. The nucleocapsid (N) protein of coronaviruses (CoVs) is a multifunctional RNA binding protein necessary for viral RNA replication and transcription. Therefore, it is a potential antiviral drug target, serving multiple critical functions during the viral life cycle. This study addresses the potential to repurpose antiviral compounds approved or in development for treating human CoV induced infections against SARS-CoV-2 N. For this purpose, we used the docking methodology to better understand the inhibitory mechanism of this protein with the existing 34 antiviral compounds. The results of this analysis indicate that rapamycin, saracatinib, camostat, trametinib, and nafamostat were the top hit compounds with binding energy (-11.87, -10.40, -9.85, -9.45, -9.35 kcal/mol, respectively). This analysis also showed that the most common residues that interact with the compounds are Phe66, Arg68, Gly69, Tyr123, Ile131, Trp132, Val133, and Ala134. Subsequently, protein-ligand complex stability was examined with molecular dynamics simulations for these five compounds, which showed the best binding affinity. According to the results of this study, the interaction between these compounds and crucial residues of the target protein were maintained. These results suggest that these residues are potential drug targeting sites for the SARS-CoV-2 N protein. This study information will contribute to the development of novel compounds for further in vitro and in vivo studies of SARS-CoV-2, as well as possible new drug repurposing strategies to treat COVID-19 disease. Twit Text FOAVip Computational drug repurposing study of the RNA binding domain of SARS-CoV-2 nucleocapsid protein with antiviral agents ????Biotechnol Prog http://www.kidney.de/pget.php?&tw=1&pmid=33314794 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33314794 #FOAvip English Wikipedia <ref>{{Cite pmid|33314794}}</ref> Computational drug repurposing study of the RNA binding domain of SARS-CoV-2 nucleocapsid protein with antiviral agents #MMPMID33314794 Tatar G; Ozyurt E; Turhan K Biotechnol Prog 2021[Mar]; 37 (2): e3110 PMID33314794show ga The recent outbreak of coronavirus disease (COVID-19) in China caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has led to worldwide human infections and deaths. The nucleocapsid (N) protein of coronaviruses (CoVs) is a multifunctional RNA binding protein necessary for viral RNA replication and transcription. Therefore, it is a potential antiviral drug target, serving multiple critical functions during the viral life cycle. This study addresses the potential to repurpose antiviral compounds approved or in development for treating human CoV induced infections against SARS-CoV-2 N. For this purpose, we used the docking methodology to better understand the inhibitory mechanism of this protein with the existing 34 antiviral compounds. The results of this analysis indicate that rapamycin, saracatinib, camostat, trametinib, and nafamostat were the top hit compounds with binding energy (-11.87, -10.40, -9.85, -9.45, -9.35 kcal/mol, respectively). This analysis also showed that the most common residues that interact with the compounds are Phe66, Arg68, Gly69, Tyr123, Ile131, Trp132, Val133, and Ala134. Subsequently, protein-ligand complex stability was examined with molecular dynamics simulations for these five compounds, which showed the best binding affinity. According to the results of this study, the interaction between these compounds and crucial residues of the target protein were maintained. These results suggest that these residues are potential drug targeting sites for the SARS-CoV-2 N protein. This study information will contribute to the development of novel compounds for further in vitro and in vivo studies of SARS-CoV-2, as well as possible new drug repurposing strategies to treat COVID-19 disease. |*Drug Design[MESH] |*Drug Repositioning[MESH] |Amino Acid Sequence[MESH] |Antiviral Agents/*chemistry[MESH] |Binding Sites[MESH] |Coronavirus Nucleocapsid Proteins/*chemistry[MESH] |Molecular Docking Simulation[MESH] |Molecular Dynamics Simulation[MESH] |Phosphoproteins/chemistry[MESH] |Protein Domains[MESH]Computational drug repurposing study of the RNA binding domain of SARS(epmc).pdf DeepDyve Pubget Overpricing