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10.1016/j.jmgm.2020.107710 http://scihub22266oqcxt.onion/10.1016/j.jmgm.2020.107710 32829149!7417922!32829149     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Mol+Graph+Model 2020 ; 100 (ä): 107710 Nephropedia Template TP {{tp|p=32829149|t=2020. Structural analysis of experimental drugs binding to the SARS-CoV-2 target TMPRSS2 |pdf=|usr=}}{{32829149}} gab.com Text Structural analysis of experimental drugs binding to the SARS-CoV-2 target TMPRSS2 JO: J Mol Graph Model http://www.kidney.de/pget.php?&tw=1&pmid=32829149 #FOAvip The emergence of SARS-CoV-2 has prompted a worldwide health emergency. There is an urgent need for therapeutics, both through the repurposing of approved drugs and the development of new treatments. In addition to the viral drug targets, a number of human drug targets have been suggested. In theory, targeting human proteins should provide an advantage over targeting viral proteins in terms of drug resistance, which is commonly a problem in treating RNA viruses. This paper focuses on the human protein TMPRSS2, which supports coronavirus life cycles by cleaving viral spike proteins. The three-dimensional structure of TMPRSS2 is not known and so we have generated models of the TMPRSS2 in the apo state as well as in complex with a peptide substrate and putative inhibitors to aid future work. Importantly, many related human proteases have 80% or higher identity with TMPRSS2 in the S1-S1' subsites, with plasminogen and urokinase-type plasminogen activator (uPA) having 95% identity. We highlight 376 approved, investigational or experimental drugs targeting S1A serine proteases that may also inhibit TMPRSS2. Whilst the presence of a relatively uncommon lysine residue in the S2/S3 subsites means that some serine protease inhibitors will not inhibit TMPRSS2, this residue is likely to provide a handle for selective targeting in a focused drug discovery project. We discuss how experimental drugs targeting related serine proteases might be repurposed as TMPRSS2 inhibitors to treat coronaviruses. Twit Text FOAVip Structural analysis of experimental drugs binding to the SARS-CoV-2 target TMPRSS2 ????J Mol Graph Model http://www.kidney.de/pget.php?&tw=1&pmid=32829149 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32829149 #FOAvip English Wikipedia <ref>{{Cite pmid|32829149}}</ref> Structural analysis of experimental drugs binding to the SARS-CoV-2 target TMPRSS2 #MMPMID32829149 Huggins DJ J Mol Graph Model 2020[Nov]; 100 (ä): 107710 PMID32829149show ga The emergence of SARS-CoV-2 has prompted a worldwide health emergency. There is an urgent need for therapeutics, both through the repurposing of approved drugs and the development of new treatments. In addition to the viral drug targets, a number of human drug targets have been suggested. In theory, targeting human proteins should provide an advantage over targeting viral proteins in terms of drug resistance, which is commonly a problem in treating RNA viruses. This paper focuses on the human protein TMPRSS2, which supports coronavirus life cycles by cleaving viral spike proteins. The three-dimensional structure of TMPRSS2 is not known and so we have generated models of the TMPRSS2 in the apo state as well as in complex with a peptide substrate and putative inhibitors to aid future work. Importantly, many related human proteases have 80% or higher identity with TMPRSS2 in the S1-S1' subsites, with plasminogen and urokinase-type plasminogen activator (uPA) having 95% identity. We highlight 376 approved, investigational or experimental drugs targeting S1A serine proteases that may also inhibit TMPRSS2. Whilst the presence of a relatively uncommon lysine residue in the S2/S3 subsites means that some serine protease inhibitors will not inhibit TMPRSS2, this residue is likely to provide a handle for selective targeting in a focused drug discovery project. We discuss how experimental drugs targeting related serine proteases might be repurposed as TMPRSS2 inhibitors to treat coronaviruses. |Amino Acid Sequence[MESH] |Antiviral Agents/*chemistry[MESH] |Betacoronavirus/*chemistry/enzymology[MESH] |COVID-19[MESH] |Catalytic Domain[MESH] |Coronavirus Infections/drug therapy/virology[MESH] |Drug Repositioning[MESH] |Host-Pathogen Interactions[MESH] |Humans[MESH] |Ligands[MESH] |Molecular Dynamics Simulation[MESH] |Pandemics[MESH] |Plasminogen/antagonists & inhibitors/chemistry/metabolism[MESH] |Pneumonia, Viral/drug therapy/virology[MESH] |Protease Inhibitors/*chemistry[MESH] |Protein Binding[MESH] |Protein Interaction Domains and Motifs[MESH] |Protein Structure, Secondary[MESH] |SARS-CoV-2[MESH] |Sequence Alignment[MESH] |Serine Endopeptidases/*chemistry/metabolism[MESH] |Small Molecule Libraries/*chemistry[MESH] |Structural Homology, Protein[MESH] |Structure-Activity Relationship[MESH] |Thermodynamics[MESH]Structural analysis of experimental drugs binding to the SARS-CoV-2 ta(epmc).pdf DeepDyve Pubget Overpricing