Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1038/s41467-020-18233-x http://scihub22266oqcxt.onion/10.1038/s41467-020-18233-x 32887884!7474075!32887884     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2020 ; 11 (1): 4417 Nephropedia Template TP {{tp|p=32887884|t=2020. Both Boceprevir and GC376 efficaciously inhibit SARS-CoV-2 by targeting its main protease |pdf=|usr=}}{{32887884}} gab.com Text Both Boceprevir and GC376 efficaciously inhibit SARS-CoV-2 by targeting its main protease JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32887884 #FOAvip COVID-19 was declared a pandemic on March 11 by WHO, due to its great threat to global public health. The coronavirus main protease (M(pro), also called 3CLpro) is essential for processing and maturation of the viral polyprotein, therefore recognized as an attractive drug target. Here we show that a clinically approved anti-HCV drug, Boceprevir, and a pre-clinical inhibitor against feline infectious peritonitis (corona) virus (FIPV), GC376, both efficaciously inhibit SARS-CoV-2 in Vero cells by targeting M(pro). Moreover, combined application of GC376 with Remdesivir, a nucleotide analogue that inhibits viral RNA dependent RNA polymerase (RdRp), results in sterilizing additive effect. Further structural analysis reveals binding of both inhibitors to the catalytically active side of SARS-CoV-2 protease M(pro) as main mechanism of inhibition. Our findings may provide critical information for the optimization and design of more potent inhibitors against the emerging SARS-CoV-2 virus. Twit Text FOAVip Both Boceprevir and GC376 efficaciously inhibit SARS-CoV-2 by targeting its main protease ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32887884 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32887884 #FOAvip English Wikipedia <ref>{{Cite pmid|32887884}}</ref> Both Boceprevir and GC376 efficaciously inhibit SARS-CoV-2 by targeting its main protease #MMPMID32887884 Fu L; Ye F; Feng Y; Yu F; Wang Q; Wu Y; Zhao C; Sun H; Huang B; Niu P; Song H; Shi Y; Li X; Tan W; Qi J; Gao GF Nat Commun 2020[Sep]; 11 (1): 4417 PMID32887884show ga COVID-19 was declared a pandemic on March 11 by WHO, due to its great threat to global public health. The coronavirus main protease (M(pro), also called 3CLpro) is essential for processing and maturation of the viral polyprotein, therefore recognized as an attractive drug target. Here we show that a clinically approved anti-HCV drug, Boceprevir, and a pre-clinical inhibitor against feline infectious peritonitis (corona) virus (FIPV), GC376, both efficaciously inhibit SARS-CoV-2 in Vero cells by targeting M(pro). Moreover, combined application of GC376 with Remdesivir, a nucleotide analogue that inhibits viral RNA dependent RNA polymerase (RdRp), results in sterilizing additive effect. Further structural analysis reveals binding of both inhibitors to the catalytically active side of SARS-CoV-2 protease M(pro) as main mechanism of inhibition. Our findings may provide critical information for the optimization and design of more potent inhibitors against the emerging SARS-CoV-2 virus. |Animals[MESH] |Antiviral Agents/pharmacology[MESH] |Betacoronavirus/*drug effects/enzymology[MESH] |Binding Sites/drug effects[MESH] |COVID-19[MESH] |COVID-19 Drug Treatment[MESH] |Catalytic Domain[MESH] |Chlorocebus aethiops[MESH] |Coronavirus 3C Proteases[MESH] |Coronavirus Infections/*drug therapy/*virology[MESH] |Crystallography, X-Ray[MESH] |Cysteine Endopeptidases/chemistry/metabolism[MESH] |Disease Models, Animal[MESH] |High-Throughput Screening Assays[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Pneumonia, Viral/*drug therapy/*virology[MESH] |Proline/*analogs & derivatives/pharmacology[MESH] |Protease Inhibitors/*pharmacology[MESH] |Pyrrolidines/*pharmacology[MESH] |RNA-Dependent RNA Polymerase/antagonists & inhibitors/chemistry/metabolism[MESH] |SARS-CoV-2[MESH] |Sulfonic Acids[MESH] |Vero Cells[MESH] |Viral Nonstructural Proteins/*antagonists & inhibitors/chemistry/metabolism[MESH]Both Boceprevir and GC376 efficaciously inhibit SARS-CoV-2 by targetin(epmc).pdf DeepDyve Pubget Overpricing