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10.1080/07391102.2020.1752310 http://scihub22266oqcxt.onion/10.1080/07391102.2020.1752310 32362235!7212547!32362235     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32362235&cmd=llinks): Failed to open stream: HTTP request failed! 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Understanding the binding affinity of noscapines with protease of SARS-CoV-2 for COVID-19 using MD simulations at different temperatures |pdf=|usr=}}{{32362235}} gab.com Text Understanding the binding affinity of noscapines with protease of SARS-CoV-2 for COVID-19 using MD simulations at different temperatures JO: J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=32362235 #FOAvip The current outbreak of a novel coronavirus, named as SARS-CoV-2 causing COVID-19 occurred in 2019, is in dire need of finding potential therapeutic agents. Recently, ongoing viral epidemic due to coronavirus (SARS-CoV-2) primarily affected mainland China that now threatened to spread to populations in most countries of the world. In spite of this, there is currently no antiviral drug/ vaccine available against coronavirus infection, COVID-19. In the present study, computer-aided drug design-based screening to find out promising inhibitors against the coronavirus (SARS-CoV-2) leads to infection, COVID-19. The lead therapeutic molecule was investigated through docking and molecular dynamics simulations. In this, binding affinity of noscapines(23B)-protease of SARS-CoV-2 complex was evaluated through MD simulations at different temperatures. Our research group has established that noscapine is a chemotherapeutic agent for the treatment of drug resistant cancers; however, noscapine was also being used as anti-malarial, anti-stroke and cough-suppressant. This study suggests for the first time that noscapine exerts its antiviral effects by inhibiting viral protein synthesis. Twit Text FOAVip Understanding the binding affinity of noscapines with protease of SARS-CoV-2 for COVID-19 using MD simulations at different temperatures ????J Biomol Struct Dyn http://www.kidney.de/pget.php?&tw=1&pmid=32362235 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32362235 #FOAvip English Wikipedia <ref>{{Cite pmid|32362235}}</ref> Understanding the binding affinity of noscapines with protease of SARS-CoV-2 for COVID-19 using MD simulations at different temperatures #MMPMID32362235 Kumar D; Kumari K; Jayaraj A; Kumar V; Kumar RV; Dass SK; Chandra R; Singh P J Biomol Struct Dyn 2021[Apr]; 39 (7): 2659-2672 PMID32362235show ga The current outbreak of a novel coronavirus, named as SARS-CoV-2 causing COVID-19 occurred in 2019, is in dire need of finding potential therapeutic agents. Recently, ongoing viral epidemic due to coronavirus (SARS-CoV-2) primarily affected mainland China that now threatened to spread to populations in most countries of the world. In spite of this, there is currently no antiviral drug/ vaccine available against coronavirus infection, COVID-19. In the present study, computer-aided drug design-based screening to find out promising inhibitors against the coronavirus (SARS-CoV-2) leads to infection, COVID-19. The lead therapeutic molecule was investigated through docking and molecular dynamics simulations. In this, binding affinity of noscapines(23B)-protease of SARS-CoV-2 complex was evaluated through MD simulations at different temperatures. Our research group has established that noscapine is a chemotherapeutic agent for the treatment of drug resistant cancers; however, noscapine was also being used as anti-malarial, anti-stroke and cough-suppressant. This study suggests for the first time that noscapine exerts its antiviral effects by inhibiting viral protein synthesis. |*COVID-19[MESH] |*Noscapine[MESH] |Antiviral Agents/pharmacology[MESH] |Cysteine Endopeptidases[MESH] |Humans[MESH] |Molecular Docking Simulation[MESH] |Peptide Hydrolases[MESH] |Protease Inhibitors/pharmacology[MESH] |SARS-CoV-2[MESH] |Temperature[MESH]Understanding the binding affinity of noscapines with protease of SARS(epmc).pdf DeepDyve Pubget Overpricing