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10.1021/acs.jpclett.0c02706 http://scihub22266oqcxt.onion/10.1021/acs.jpclett.0c02706 33147968!ä!33147968 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 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 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Phys+Chem+Lett 2020 ; 11 (22): 9781-9787 Nephropedia Template TP {{tp|p=33147968|t=2020. In Silico Antibody Mutagenesis for Optimizing Its Binding to Spike Protein of Severe Acute Respiratory Syndrome Coronavirus 2 |pdf=|usr=}}{{33147968}} gab.com Text In Silico Antibody Mutagenesis for Optimizing Its Binding to Spike Protein of Severe Acute Respiratory Syndrome Coronavirus 2 JO: J Phys Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=33147968 #FOAvip Coronavirus disease 2019 (COVID-19) is an ongoing global pandemic, and there are currently no FDA-approved medicines for treatment or prevention. Inspired by promising outcomes for convalescent plasma treatment, the development of antibody drugs (biologics) to block SARS-CoV-2 infection has been the focus of drug discovery, along with tremendous efforts in repurposing small-molecule drugs. In the past several months, experimentally, many human neutralizing monoclonal antibodies (mAbs) were successfully extracted from plasma of recovered COVID-19 patients. Currently, several mAbs targeting the SARS-CoV-2's spike glycoprotein (S-protein) are in clinical trials. With known atomic structures of the mAb and S-protein complex, it becomes possible to investigate in silico the molecular mechanism of mAb's binding with S-protein and to design more potent mAbs through protein mutagenesis studies, complementary to existing experimental efforts. Leveraging today's superb computing power, we propose a fully automated in silico protocol for quickly identifying possible mutations in a mAb (e.g., CB6) to enhance its binding affinity for S-protein for the design of more efficacious therapeutic mAbs. Twit Text FOAVip In Silico Antibody Mutagenesis for Optimizing Its Binding to Spike Protein of Severe Acute Respiratory Syndrome Coronavirus 2 ????J Phys Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=33147968 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33147968 #FOAvip English Wikipedia <ref>{{Cite pmid|33147968}}</ref> In Silico Antibody Mutagenesis for Optimizing Its Binding to Spike Protein of Severe Acute Respiratory Syndrome Coronavirus 2 #MMPMID33147968 Luan B; Huynh T J Phys Chem Lett 2020[Nov]; 11 (22): 9781-9787 PMID33147968show ga Coronavirus disease 2019 (COVID-19) is an ongoing global pandemic, and there are currently no FDA-approved medicines for treatment or prevention. Inspired by promising outcomes for convalescent plasma treatment, the development of antibody drugs (biologics) to block SARS-CoV-2 infection has been the focus of drug discovery, along with tremendous efforts in repurposing small-molecule drugs. In the past several months, experimentally, many human neutralizing monoclonal antibodies (mAbs) were successfully extracted from plasma of recovered COVID-19 patients. Currently, several mAbs targeting the SARS-CoV-2's spike glycoprotein (S-protein) are in clinical trials. With known atomic structures of the mAb and S-protein complex, it becomes possible to investigate in silico the molecular mechanism of mAb's binding with S-protein and to design more potent mAbs through protein mutagenesis studies, complementary to existing experimental efforts. Leveraging today's superb computing power, we propose a fully automated in silico protocol for quickly identifying possible mutations in a mAb (e.g., CB6) to enhance its binding affinity for S-protein for the design of more efficacious therapeutic mAbs. |Antibodies, Monoclonal/genetics/*immunology/metabolism[MESH] |Antibodies, Neutralizing/genetics/*immunology/metabolism[MESH] |Molecular Dynamics Simulation[MESH] |Mutagenesis[MESH] |Mutation[MESH] |Protein Binding/genetics[MESH] |Protein Domains[MESH] |SARS-CoV-2/*chemistry[MESH] |Spike Glycoprotein, Coronavirus/chemistry/*immunology[MESH]In Silico Antibody Mutagenesis for Optimizing Its Binding to Spike Pro(epmc).pdf DeepDyve Pubget Overpricing