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10.1080/07391102.2020.1799865 http://scihub22266oqcxt.onion/10.1080/07391102.2020.1799865 32729392!ä!32729392 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biomol+Struct+Dyn 2021 ; 39 (17): 6676-6688 Nephropedia Template TP {{tp|p=32729392|t=2021. Antiviral potential of some novel structural analogs of standard drugs repurposed for the treatment of COVID-19 |pdf=|usr=}}{{32729392}} gab.com Text Antiviral potential of some novel structural analogs of standard drugs repurposed for the treatment of COVID-19 JO: J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=32729392 #FOAvip SARS-CoV-2 pandemic has claimed millions of lives across the world. As of June 2020, there is no FDA approved antiviral therapy to eradicate this dreadful virus. In this study, drug re-purposing and computational approaches were employed to identify high affinity inhibitors of SARS-CoV-2 Main protease (3CLpro), Papain-like protease (PLpro) and the receptor domain of Spike protein. Molecular docking on 40 derivatives of standard drugs (Remdesivir, Lopinavir and Theophylline) led to the identification of R10, R2 and L9 as potential inhibitors of 3CLpro, PLpro and Spike protein, respectively. The binding affinity of R10, R2 and L9 towards 3CLpro, PLpro and Spike protein were 4.03 x 10(6), 3.72 x 10(4) and 1.31 x 10(4)M(-1), respectively. These inhibitors interact with the active site or catalytic amino acid residues of 3CLpro, PLpro and Spike protein. We also examined the stability and dynamic behavior of protein-inhibitor complex by employing molecular dynamics simulation. RMSDs, RMSFs and variation in secondary structure of target proteins alone or in complex with their respective inhibitors were used to ascertain the integrity of proteins' structure during simulation. Moreover, physicochemical and ADMET properties of R10, R2 and L9 along with Remdesivir, Lopinavir and Theophylline were determined. In vitro and In vivo studies are needed to further validate the potential of these derivatives before they can be developed into potential drug molecules.Communicated by Ramaswamy H. Sarma. Twit Text FOAVip Antiviral potential of some novel structural analogs of standard drugs repurposed for the treatment of COVID-19 ????J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=32729392 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32729392 #FOAvip English Wikipedia <ref>{{Cite pmid|32729392}}</ref> Antiviral potential of some novel structural analogs of standard drugs repurposed for the treatment of COVID-19 #MMPMID32729392 AlAjmi MF; Azhar A; Owais M; Rashid S; Hasan S; Hussain A; Rehman MT J Biomol Struct Dyn 2021[Oct]; 39 (17): 6676-6688 PMID32729392show ga SARS-CoV-2 pandemic has claimed millions of lives across the world. As of June 2020, there is no FDA approved antiviral therapy to eradicate this dreadful virus. In this study, drug re-purposing and computational approaches were employed to identify high affinity inhibitors of SARS-CoV-2 Main protease (3CLpro), Papain-like protease (PLpro) and the receptor domain of Spike protein. Molecular docking on 40 derivatives of standard drugs (Remdesivir, Lopinavir and Theophylline) led to the identification of R10, R2 and L9 as potential inhibitors of 3CLpro, PLpro and Spike protein, respectively. The binding affinity of R10, R2 and L9 towards 3CLpro, PLpro and Spike protein were 4.03 x 10(6), 3.72 x 10(4) and 1.31 x 10(4)M(-1), respectively. These inhibitors interact with the active site or catalytic amino acid residues of 3CLpro, PLpro and Spike protein. We also examined the stability and dynamic behavior of protein-inhibitor complex by employing molecular dynamics simulation. RMSDs, RMSFs and variation in secondary structure of target proteins alone or in complex with their respective inhibitors were used to ascertain the integrity of proteins' structure during simulation. Moreover, physicochemical and ADMET properties of R10, R2 and L9 along with Remdesivir, Lopinavir and Theophylline were determined. In vitro and In vivo studies are needed to further validate the potential of these derivatives before they can be developed into potential drug molecules.Communicated by Ramaswamy H. Sarma. |*COVID-19[MESH] |*Pharmaceutical Preparations[MESH] |Antiviral Agents/pharmacology[MESH] |Humans[MESH] |Molecular Docking Simulation[MESH]Antiviral potential of some novel structural analogs of standard drugs(epmc).pdf DeepDyve Pubget Overpricing