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10.1063/5.0013029 http://scihub22266oqcxt.onion/10.1063/5.0013029 32611087!7286701!32611087     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32611087&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       Chaos 2020 ; 30 (6): 061102 Nephropedia Template TP {{tp|p=32611087|t=2020. Topological analysis of SARS CoV-2 main protease |pdf=|usr=}}{{32611087}} gab.com Text Topological analysis of SARS CoV-2 main protease JO: Chaos http://www.kidney.de/pget.php?&tw=1&pmid=32611087 #FOAvip There is an urgent necessity of effective medication against severe acute respiratory syndrome coronavirus 2 (SARS CoV-2), which is producing the COVID-19 pandemic across the world. Its main protease (M(pro)) represents an attractive pharmacological target due to its involvement in essential viral functions. The crystal structure of free M(pro) shows a large structural resemblance with the main protease of SARS CoV (nowadays known as SARS CoV-1). Here, we report that average SARS CoV-2 M(pro) is 1900% more sensitive than SARS CoV-1 M(pro) in transmitting tiny structural changes across the whole protein through long-range interactions. The largest sensitivity of M(pro) to structural perturbations is located exactly around the catalytic site Cys-145 and coincides with the binding site of strong inhibitors. These findings, based on a simplified representation of the protein as a residue network, may help in designing potent inhibitors of SARS CoV-2 M(pro). Twit Text FOAVip Topological analysis of SARS CoV-2 main protease ????Chaos http://www.kidney.de/pget.php?&tw=1&pmid=32611087 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32611087 #FOAvip English Wikipedia <ref>{{Cite pmid|32611087}}</ref> Topological analysis of SARS CoV-2 main protease #MMPMID32611087 Estrada E Chaos 2020[Jun]; 30 (6): 061102 PMID32611087show ga There is an urgent necessity of effective medication against severe acute respiratory syndrome coronavirus 2 (SARS CoV-2), which is producing the COVID-19 pandemic across the world. Its main protease (M(pro)) represents an attractive pharmacological target due to its involvement in essential viral functions. The crystal structure of free M(pro) shows a large structural resemblance with the main protease of SARS CoV (nowadays known as SARS CoV-1). Here, we report that average SARS CoV-2 M(pro) is 1900% more sensitive than SARS CoV-1 M(pro) in transmitting tiny structural changes across the whole protein through long-range interactions. The largest sensitivity of M(pro) to structural perturbations is located exactly around the catalytic site Cys-145 and coincides with the binding site of strong inhibitors. These findings, based on a simplified representation of the protein as a residue network, may help in designing potent inhibitors of SARS CoV-2 M(pro). |Amino Acid Sequence[MESH] |Betacoronavirus/*metabolism[MESH] |Binding Sites/drug effects[MESH] |COVID-19[MESH] |Catalytic Domain/*drug effects[MESH] |Coronavirus 3C Proteases[MESH] |Coronavirus Infections/*drug therapy[MESH] |Crystallography, X-Ray[MESH] |Cysteine Endopeptidases/drug effects/*metabolism[MESH] |Drug Design[MESH] |Humans[MESH] |Pandemics[MESH] |Pneumonia, Viral/*drug therapy[MESH] |Protease Inhibitors/*pharmacology[MESH] |SARS-CoV-2[MESH] |Severe acute respiratory syndrome-related coronavirus/metabolism[MESH]Topological analysis of SARS CoV-2 main protease (epmc).pdf DeepDyve Pubget Overpricing