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10.1016/j.bbrc.2021.03.118 http://scihub22266oqcxt.onion/10.1016/j.bbrc.2021.03.118 33813274!7997393!33813274     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+Biophys+Res+Commun 2021 ; 555 (ä): 147-153 Nephropedia Template TP {{tp|p=33813274|t=2021. Targeted design of drug binding sites in the main protease of SARS-CoV-2 reveals potential signatures of adaptation |pdf=|usr=}}{{33813274}} gab.com Text Targeted design of drug binding sites in the main protease of SARS-CoV-2 reveals potential signatures of adaptation JO: Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=33813274 #FOAvip Several existing drugs are currently being tested worldwide to treat COVID-19 patients. Recent data indicate that SARS-CoV-2 is rapidly evolving into more transmissible variants. It is therefore highly possible that SARS-CoV-2 can accumulate adaptive mutations modulating drug susceptibility and hampering viral antigenicity. Thus, it is vital to predict potential non-synonymous mutation sites and predict the evolution of protein structural modifications leading to drug tolerance. As two FDA-approved anti-hepatitis C virus (HCV) drugs, boceprevir, and telaprevir, have been shown to effectively inhibit SARS-CoV-2 by targeting the main protease (M(pro)), here we used a high-throughput interface-based protein design strategy to identify mutational hotspots and potential signatures of adaptation in these drug binding sites of M(pro). Several mutants exhibited reduced binding affinity to these drugs, out of which hotspot residues having a strong tendency to undergo positive selection were identified. The data further indicated that these anti-HCV drugs have larger footprints in the mutational landscape of M(pro) and hence encompass the highest potential for positive selection and adaptation. These findings are crucial in understanding the potential structural modifications in the drug binding sites of M(pro) and thus its signatures of adaptation. Furthermore, the data could provide systemic strategies for robust antiviral design and discovery against COVID-19 in the future. Twit Text FOAVip Targeted design of drug binding sites in the main protease of SARS-CoV-2 reveals potential signatures of adaptation ????Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=33813274 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33813274 #FOAvip English Wikipedia <ref>{{Cite pmid|33813274}}</ref> Targeted design of drug binding sites in the main protease of SARS-CoV-2 reveals potential signatures of adaptation #MMPMID33813274 Padhi AK; Tripathi T Biochem Biophys Res Commun 2021[May]; 555 (ä): 147-153 PMID33813274show ga Several existing drugs are currently being tested worldwide to treat COVID-19 patients. Recent data indicate that SARS-CoV-2 is rapidly evolving into more transmissible variants. It is therefore highly possible that SARS-CoV-2 can accumulate adaptive mutations modulating drug susceptibility and hampering viral antigenicity. Thus, it is vital to predict potential non-synonymous mutation sites and predict the evolution of protein structural modifications leading to drug tolerance. As two FDA-approved anti-hepatitis C virus (HCV) drugs, boceprevir, and telaprevir, have been shown to effectively inhibit SARS-CoV-2 by targeting the main protease (M(pro)), here we used a high-throughput interface-based protein design strategy to identify mutational hotspots and potential signatures of adaptation in these drug binding sites of M(pro). Several mutants exhibited reduced binding affinity to these drugs, out of which hotspot residues having a strong tendency to undergo positive selection were identified. The data further indicated that these anti-HCV drugs have larger footprints in the mutational landscape of M(pro) and hence encompass the highest potential for positive selection and adaptation. These findings are crucial in understanding the potential structural modifications in the drug binding sites of M(pro) and thus its signatures of adaptation. Furthermore, the data could provide systemic strategies for robust antiviral design and discovery against COVID-19 in the future. |*Drug Design[MESH] |*Mutation[MESH] |Adaptation, Physiological/*genetics[MESH] |Amino Acid Sequence[MESH] |Antiviral Agents/*chemistry/pharmacology[MESH] |Binding Sites/drug effects/genetics[MESH] |COVID-19 Drug Treatment[MESH] |Coronavirus 3C Proteases/antagonists & inhibitors/*chemistry/genetics/metabolism[MESH] |Drug Resistance, Viral/*genetics[MESH] |Genetic Fitness/genetics[MESH] |Hepacivirus/drug effects/enzymology[MESH] |Ligands[MESH] |Models, Molecular[MESH] |Oligopeptides/chemistry/pharmacology[MESH] |Proline/analogs & derivatives/chemistry/pharmacology[MESH] |Reproducibility of Results[MESH] |SARS-CoV-2/drug effects/*enzymology/*genetics[MESH] |Selection, Genetic/genetics[MESH]Targeted design of drug binding sites in the main protease of SARS-CoV(epmc).pdf DeepDyve Pubget Overpricing