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10.1016/j.bpc.2020.106425 http://scihub22266oqcxt.onion/10.1016/j.bpc.2020.106425 32663708!7836334!32663708     free     free     free 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 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 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 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 Deprecated: Implicit conversion from float 284.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 284.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 284.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+Chem 2020 ; 264 (ä): 106425 Nephropedia Template TP {{tp|p=32663708|t=2020. Reckoning a fungal metabolite, Pyranonigrin A as a potential Main protease (M(pro)) inhibitor of novel SARS-CoV-2 virus identified using docking and molecular dynamics simulation |pdf=|usr=}}{{32663708}} gab.com Text Reckoning a fungal metabolite, Pyranonigrin A as a potential Main protease (M(pro)) inhibitor of novel SARS-CoV-2 virus identified using docking and molecular dynamics simulation JO: Biophys Chem http://www.kidney.de/pget.php?&tw=1&pmid=32663708 #FOAvip The novel SARS-CoV-2 is the etiological agent causing the Coronavirus disease 2019 (COVID-19), which continues to become an inevitable pandemic outbreak. Over a short span of time, the structures of therapeutic target proteins for SARS-CoV-2 were identified based on the homology modelled structure of similar SARS-CoV transmission of 2003. Since the onset of the disease, the research community has been looking for a potential drug lead. Out of all the known resolved structures related to SARS-CoV, Main protease (M(pro)) is considered an attractive anti-viral drug target on the grounds of its role in viral replication and probable non-interactive competency to bind to any viral host protein. To the best of our knowledge, till date only one compound has been identified and tested in-vivo as a potent inhibitor of M(pro) protein, addressed as N3 (PubChem Compound CID: 6323191) and is known to bind irreversibly to M(pro) suppressing its activity. Using computational approach, we intend to identify a probable natural fungal metabolite to interact and inhibit M(pro). After screening various small molecules for molecular docking and dynamics simulation, we propose Pyranonigrin A, a secondary fungal metabolite to possess potent inhibitory potential against the Main protease (M(pro)) expressed in SARS-CoV-2 virus. Twit Text FOAVip Reckoning a fungal metabolite, Pyranonigrin A as a potential Main protease (M(pro)) inhibitor of novel SARS-CoV-2 virus identified using docking and molecular dynamics simulation ????Biophys Chem http://www.kidney.de/pget.php?&tw=1&pmid=32663708 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32663708 #FOAvip English Wikipedia <ref>{{Cite pmid|32663708}}</ref> Reckoning a fungal metabolite, Pyranonigrin A as a potential Main protease (M(pro)) inhibitor of novel SARS-CoV-2 virus identified using docking and molecular dynamics simulation #MMPMID32663708 Rao P; Shukla A; Parmar P; Rawal RM; Patel B; Saraf M; Goswami D Biophys Chem 2020[Sep]; 264 (ä): 106425 PMID32663708show ga The novel SARS-CoV-2 is the etiological agent causing the Coronavirus disease 2019 (COVID-19), which continues to become an inevitable pandemic outbreak. Over a short span of time, the structures of therapeutic target proteins for SARS-CoV-2 were identified based on the homology modelled structure of similar SARS-CoV transmission of 2003. Since the onset of the disease, the research community has been looking for a potential drug lead. Out of all the known resolved structures related to SARS-CoV, Main protease (M(pro)) is considered an attractive anti-viral drug target on the grounds of its role in viral replication and probable non-interactive competency to bind to any viral host protein. To the best of our knowledge, till date only one compound has been identified and tested in-vivo as a potent inhibitor of M(pro) protein, addressed as N3 (PubChem Compound CID: 6323191) and is known to bind irreversibly to M(pro) suppressing its activity. Using computational approach, we intend to identify a probable natural fungal metabolite to interact and inhibit M(pro). After screening various small molecules for molecular docking and dynamics simulation, we propose Pyranonigrin A, a secondary fungal metabolite to possess potent inhibitory potential against the Main protease (M(pro)) expressed in SARS-CoV-2 virus. |Antiviral Agents/*chemistry[MESH] |Betacoronavirus/*enzymology/pathogenicity[MESH] |Binding Sites[MESH] |Coronavirus 3C Proteases[MESH] |Crystallography, X-Ray[MESH] |Cysteine Endopeptidases/chemistry/genetics/metabolism[MESH] |Drug Discovery[MESH] |Gene Expression[MESH] |Hydrogen Bonding[MESH] |Molecular Docking Simulation[MESH] |Molecular Dynamics Simulation[MESH] |Protease Inhibitors/*chemistry[MESH] |Protein Binding[MESH] |Protein Conformation, alpha-Helical[MESH] |Protein Conformation, beta-Strand[MESH] |Protein Interaction Domains and Motifs[MESH] |Pyrones/*chemistry[MESH] |Pyrroles/*chemistry[MESH] |SARS-CoV-2[MESH] |Sequence Homology, Amino Acid[MESH] |Thermodynamics[MESH]Reckoning a fungal metabolite, Pyranonigrin A as a potential Main prot(epmc).pdf DeepDyve Pubget Overpricing