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10.1016/j.compbiomed.2021.104315 http://scihub22266oqcxt.onion/10.1016/j.compbiomed.2021.104315 33705994!7935700!33705994     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Comput+Biol+Med 2021 ; 132 (ä): 104315 Nephropedia Template TP {{tp|p=33705994|t=2021. A hijack mechanism of Indian SARS-CoV-2 isolates for relapsing contemporary antiviral therapeutics |pdf=|usr=}}{{33705994}} gab.com Text A hijack mechanism of Indian SARS-CoV-2 isolates for relapsing contemporary antiviral therapeutics JO: Comput Biol Med http://www.kidney.de/pget.php?&tw=1&pmid=33705994 #FOAvip Coronavirus disease (COVID-19) rapidly expands to a global pandemic and its impact on public health varies from country to country. It is caused by a new virus severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). It is imperative for relapsing current antiviral therapeutics owing to randomized genetic drift in global SARS-CoV-2 isolates. A molecular mechanism behind the emerging genomic variants is not yet understood for the prioritization of selective antivirals. The present computational study was aimed to repurpose existing antivirals for Indian SARS-CoV-2 isolates by uncovering a hijack mechanism based on structural and functional characteristics of protein variants. Forty-one protein mutations were identified in 12 Indian SARS-CoV-2 isolates by analysis of genome variations across 460 genome sequences obtained from 30 geographic sites in India. Two unique mutations such as W6152R and N5928H found in exonuclease of Surat (GBRC275b) and Gandhinagar (GBRC239) isolates. We report for the first time the impact of folding rate on stabilizing/retaining a sequence-structure-function-virulence link of emerging protein variants leading to accommodate hijack ability from current antivirals. Binding affinity analysis revealed the effect of point mutations on virus infectivity and the drug-escaping efficiency of Indian isolates. Emodin and artinemol suggested herein as repurposable antivirals for the treatment of COVID-19 patients infected with Indian isolates. Our study concludes that a protein folding rate is a key structural and evolutionary determinant to enhance the receptor-binding specificity and ensure hijack ability from the prevalent antiviral therapeutics. Twit Text FOAVip A hijack mechanism of Indian SARS-CoV-2 isolates for relapsing contemporary antiviral therapeutics ????Comput Biol Med http://www.kidney.de/pget.php?&tw=1&pmid=33705994 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33705994 #FOAvip English Wikipedia <ref>{{Cite pmid|33705994}}</ref> A hijack mechanism of Indian SARS-CoV-2 isolates for relapsing contemporary antiviral therapeutics #MMPMID33705994 Prathiviraj R; Saranya S; Bharathi M; Chellapandi P Comput Biol Med 2021[May]; 132 (ä): 104315 PMID33705994show ga Coronavirus disease (COVID-19) rapidly expands to a global pandemic and its impact on public health varies from country to country. It is caused by a new virus severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). It is imperative for relapsing current antiviral therapeutics owing to randomized genetic drift in global SARS-CoV-2 isolates. A molecular mechanism behind the emerging genomic variants is not yet understood for the prioritization of selective antivirals. The present computational study was aimed to repurpose existing antivirals for Indian SARS-CoV-2 isolates by uncovering a hijack mechanism based on structural and functional characteristics of protein variants. Forty-one protein mutations were identified in 12 Indian SARS-CoV-2 isolates by analysis of genome variations across 460 genome sequences obtained from 30 geographic sites in India. Two unique mutations such as W6152R and N5928H found in exonuclease of Surat (GBRC275b) and Gandhinagar (GBRC239) isolates. We report for the first time the impact of folding rate on stabilizing/retaining a sequence-structure-function-virulence link of emerging protein variants leading to accommodate hijack ability from current antivirals. Binding affinity analysis revealed the effect of point mutations on virus infectivity and the drug-escaping efficiency of Indian isolates. Emodin and artinemol suggested herein as repurposable antivirals for the treatment of COVID-19 patients infected with Indian isolates. Our study concludes that a protein folding rate is a key structural and evolutionary determinant to enhance the receptor-binding specificity and ensure hijack ability from the prevalent antiviral therapeutics. |*COVID-19[MESH] |*SARS-CoV-2[MESH] |Antiviral Agents/pharmacology/therapeutic use[MESH] |Humans[MESH] |Mutation[MESH]A hijack mechanism of Indian SARS-CoV-2 isolates for relapsing contemp(epmc).pdf DeepDyve Pubget Overpricing