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10.1021/acscombsci.0c00058 http://scihub22266oqcxt.onion/10.1021/acscombsci.0c00058 32402186!ä!32402186 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Comb+Sci 2020 ; 22 (6): 297-305 Nephropedia Template TP {{tp|p=32402186|t=2020. Targeting the Dimerization of the Main Protease of Coronaviruses: A Potential Broad-Spectrum Therapeutic Strategy |pdf=|usr=}}{{32402186}} gab.com Text Targeting the Dimerization of the Main Protease of Coronaviruses: A Potential Broad-Spectrum Therapeutic Strategy JO: ACS Comb Sci http://www.kidney.de/pget.php?&tw=1&pmid=32402186 #FOAvip A new coronavirus (CoV) caused a pandemic named COVID-19, which has become a global health care emergency in the present time. The virus is referred to as SARS-CoV-2 (severe acute respiratory syndrome-coronavirus-2) and has a genome similar ( approximately 82%) to that of the previously known SARS-CoV (SARS coronavirus). An attractive therapeutic target for CoVs is the main protease (M(pro)) or 3-chymotrypsin-like cysteine protease (3CL(pro)), as this enzyme plays a key role in polyprotein processing and is active in a dimeric form. Further, M(pro) is highly conserved among various CoVs, and a mutation in M(pro) is often lethal to the virus. Thus, drugs targeting the M(pro) enzyme significantly reduce the risk of mutation-mediated drug resistance and display broad-spectrum antiviral activity. The combinatorial design of peptide-based inhibitors targeting the dimerization of SARS-CoV M(pro) represents a potential therapeutic strategy. In this regard, we have compiled the literature reports highlighting the effect of mutations and N-terminal deletion of residues of SARS-CoV M(pro) on its dimerization and, thus, catalytic activity. We believe that the present review will stimulate research in this less explored yet quite significant area. The effect of the COVID-19 epidemic and the possibility of future CoV outbreaks strongly emphasize the urgent need for the design and development of potent antiviral agents against CoV infections. Twit Text FOAVip Targeting the Dimerization of the Main Protease of Coronaviruses: A Potential Broad-Spectrum Therapeutic Strategy ????ACS Comb Sci http://www.kidney.de/pget.php?&tw=1&pmid=32402186 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32402186 #FOAvip English Wikipedia <ref>{{Cite pmid|32402186}}</ref> Targeting the Dimerization of the Main Protease of Coronaviruses: A Potential Broad-Spectrum Therapeutic Strategy #MMPMID32402186 Goyal B; Goyal D ACS Comb Sci 2020[Jun]; 22 (6): 297-305 PMID32402186show ga A new coronavirus (CoV) caused a pandemic named COVID-19, which has become a global health care emergency in the present time. The virus is referred to as SARS-CoV-2 (severe acute respiratory syndrome-coronavirus-2) and has a genome similar ( approximately 82%) to that of the previously known SARS-CoV (SARS coronavirus). An attractive therapeutic target for CoVs is the main protease (M(pro)) or 3-chymotrypsin-like cysteine protease (3CL(pro)), as this enzyme plays a key role in polyprotein processing and is active in a dimeric form. Further, M(pro) is highly conserved among various CoVs, and a mutation in M(pro) is often lethal to the virus. Thus, drugs targeting the M(pro) enzyme significantly reduce the risk of mutation-mediated drug resistance and display broad-spectrum antiviral activity. The combinatorial design of peptide-based inhibitors targeting the dimerization of SARS-CoV M(pro) represents a potential therapeutic strategy. In this regard, we have compiled the literature reports highlighting the effect of mutations and N-terminal deletion of residues of SARS-CoV M(pro) on its dimerization and, thus, catalytic activity. We believe that the present review will stimulate research in this less explored yet quite significant area. The effect of the COVID-19 epidemic and the possibility of future CoV outbreaks strongly emphasize the urgent need for the design and development of potent antiviral agents against CoV infections. |Antiviral Agents/pharmacology[MESH] |Betacoronavirus/chemistry/drug effects/*enzymology/genetics[MESH] |COVID-19[MESH] |Coronavirus 3C Proteases[MESH] |Coronavirus Infections/*drug therapy/virology[MESH] |Cysteine Endopeptidases/chemistry/genetics/*metabolism[MESH] |Drug Discovery[MESH] |Humans[MESH] |Models, Molecular[MESH] |Molecular Targeted Therapy[MESH] |Mutation/drug effects[MESH] |Pandemics[MESH] |Peptides/pharmacology[MESH] |Pneumonia, Viral/*drug therapy/virology[MESH] |Protease Inhibitors/*pharmacology[MESH] |Protein Conformation/drug effects[MESH] |Protein Multimerization/*drug effects[MESH] |SARS-CoV-2[MESH]Targeting the Dimerization of the Main Protease of Coronaviruses: A Po(epmc).pdf DeepDyve Pubget Overpricing