Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1080/07391102.2020.1791958 http://scihub22266oqcxt.onion/10.1080/07391102.2020.1791958 32684114!7441803!32684114     free     free     free 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 (15): 5756-5767 Nephropedia Template TP {{tp|p=32684114|t=2021. In-silico drug repurposing and molecular dynamics puzzled out potential SARS-CoV-2 main protease inhibitors |pdf=|usr=}}{{32684114}} gab.com Text In-silico drug repurposing and molecular dynamics puzzled out potential SARS-CoV-2 main protease inhibitors JO: J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=32684114 #FOAvip Herein, the DrugBank database which contains 10,036 approved and investigational drugs was explored deeply for potential drugs that target SARS-CoV-2 main protease (M(pro)). Filtration process of the database was conducted using three levels of accuracy for molecular docking calculations. The top 35 drugs with docking scores > -11.0 kcal/mol were then subjected to 10 ns molecular dynamics (MD) simulations followed by molecular mechanics-generalized Born surface area (MM-GBSA) binding energy calculations. The results showed that DB02388 and Cobicistat (DB09065) exhibited potential binding affinities towards M(pro) over 100 ns MD simulations, with binding energy values of -49.67 and -46.60 kcal/mol, respectively. Binding energy and structural analyses demonstrated the higher stability of DB02388 over Cobicistat. The potency of DB02388 and Cobicistat is attributed to their abilities to form several hydrogen bonds with the essential amino acids inside the active site of M(pro). Compared to DB02388 and Cobicistat, Darunavir showed a much lower binding affinity of -34.83 kcal/mol. The present study highlights the potentiality of DB02388 and Cobicistat as anti-COVID-19 drugs for clinical trials. Communicated by Ramaswamy H. Sarma. Twit Text FOAVip In-silico drug repurposing and molecular dynamics puzzled out potential SARS-CoV-2 main protease inhibitors ????J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=32684114 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32684114 #FOAvip English Wikipedia <ref>{{Cite pmid|32684114}}</ref> In-silico drug repurposing and molecular dynamics puzzled out potential SARS-CoV-2 main protease inhibitors #MMPMID32684114 Ibrahim MAA; Abdelrahman AHM; Hegazy MF J Biomol Struct Dyn 2021[Sep]; 39 (15): 5756-5767 PMID32684114show ga Herein, the DrugBank database which contains 10,036 approved and investigational drugs was explored deeply for potential drugs that target SARS-CoV-2 main protease (M(pro)). Filtration process of the database was conducted using three levels of accuracy for molecular docking calculations. The top 35 drugs with docking scores > -11.0 kcal/mol were then subjected to 10 ns molecular dynamics (MD) simulations followed by molecular mechanics-generalized Born surface area (MM-GBSA) binding energy calculations. The results showed that DB02388 and Cobicistat (DB09065) exhibited potential binding affinities towards M(pro) over 100 ns MD simulations, with binding energy values of -49.67 and -46.60 kcal/mol, respectively. Binding energy and structural analyses demonstrated the higher stability of DB02388 over Cobicistat. The potency of DB02388 and Cobicistat is attributed to their abilities to form several hydrogen bonds with the essential amino acids inside the active site of M(pro). Compared to DB02388 and Cobicistat, Darunavir showed a much lower binding affinity of -34.83 kcal/mol. The present study highlights the potentiality of DB02388 and Cobicistat as anti-COVID-19 drugs for clinical trials. Communicated by Ramaswamy H. Sarma. |*COVID-19[MESH] |*Protease Inhibitors[MESH] |Drug Repositioning[MESH] |Humans[MESH] |Molecular Docking Simulation[MESH] |Molecular Dynamics Simulation[MESH]In-silico drug repurposing and molecular dynamics puzzled out potentia(epmc).pdf DeepDyve Pubget Overpricing