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10.1021/acs.jpcb.0c03716 http://scihub22266oqcxt.onion/10.1021/acs.jpcb.0c03716 32790379!?!32790379 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32790379&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       J+Phys+Chem+B 2020 ; 124 (38): 8201-8208 Nephropedia Template TP {{tp|p=32790379|t=2020. Interdiction of Protein Folding for Therapeutic Drug Development in SARS CoV-2 |pdf=|usr=}}{{32790379}} gab.com Text Interdiction of Protein Folding for Therapeutic Drug Development in SARS CoV-2 JO: J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=32790379 #FOAvip In this article, we predict the folding initiation events of the ribose phosphatase domain of protein Nsp3 and the receptor binding domain of the spike protein from the severe acute respiratory syndrome (SARS) coronavirus-2. The calculations employ the sequential collapse model and the crystal structures to identify the segments involved in the initial contact formation events of both viral proteins. The initial contact locations may provide good targets for therapeutic drug development. The proposed strategy is based on a drug binding to the contact location, thereby aiming to prevent protein folding. Peptides are suggested as a natural choice for such protein folding interdiction drugs. Twit Text FOAVip Interdiction of Protein Folding for Therapeutic Drug Development in SARS CoV-2 ????J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=32790379 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32790379 #FOAvip English Wikipedia <ref>{{Cite pmid|32790379}}</ref> Interdiction of Protein Folding for Therapeutic Drug Development in SARS CoV-2 #MMPMID32790379 Bergasa-Caceres F; Rabitz HA J Phys Chem B 2020[Sep]; 124 (38): 8201-8208 PMID32790379show ga In this article, we predict the folding initiation events of the ribose phosphatase domain of protein Nsp3 and the receptor binding domain of the spike protein from the severe acute respiratory syndrome (SARS) coronavirus-2. The calculations employ the sequential collapse model and the crystal structures to identify the segments involved in the initial contact formation events of both viral proteins. The initial contact locations may provide good targets for therapeutic drug development. The proposed strategy is based on a drug binding to the contact location, thereby aiming to prevent protein folding. Peptides are suggested as a natural choice for such protein folding interdiction drugs. |Adaptor Proteins, Signal Transducing/*drug effects[MESH] |Antiviral Agents/*pharmacology/*therapeutic use[MESH] |Betacoronavirus/drug effects[MESH] |COVID-19[MESH] |Coronavirus Infections/*drug therapy[MESH] |Humans[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Pneumonia, Viral/*drug therapy[MESH] |Protein Binding[MESH] |Protein Folding/*drug effects[MESH] |SARS-CoV-2[MESH]Interdiction of Protein Folding for Therapeutic Drug Development in SA(epmc).pdf DeepDyve Pubget Overpricing