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.

http://scihub22266oqcxt.onion/ 32905393!7471349!32905393     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Am+J+Cancer+Res 2020 ; 10 (8): 2535-2545 Nephropedia Template TP {{tp|p=32905393|t=2020. Structural basis of SARS-CoV-2 main protease inhibition by a broad-spectrum anti-coronaviral drug |pdf=|usr=}}{{32905393}} gab.com Text Structural basis of SARS-CoV-2 main protease inhibition by a broad-spectrum anti-coronaviral drug JO: Am J Cancer Res http://www.kidney.de/pget.php?&tw=1&pmid=32905393 #FOAvip The coronavirus disease 2019 (COVID-19) pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) or 2019 novel coronavirus (2019-nCoV), took tens of thousands of lives and caused tremendous economic losses. The main protease (M(pro)) of SARS-CoV-2 is a potential target for treatment of COVID-19 due to its critical role in maturation of viral proteins and subsequent viral replication. Conceptually and technically, targeting therapy against M(pro) is similar to target therapy to treat cancer. Previous studies show that GC376, a broad-spectrum dipeptidyl M(pro) inhibitor, efficiently blocks the proliferation of many animal and human coronaviruses including SARS-CoV, Middle East respiratory syndrome coronavirus (MERS-CoV), porcine epidemic diarrhea virus (PEDV), and feline infectious peritonitis virus (FIPV). Due to the conservation of structure and catalytic mechanism of coronavirus main protease, repurposition of GC376 against SARS-CoV-2 may be an effective way for the treatment of COVID-19 in humans. To validate this conjecture, the binding affinity and IC(50) value of M(pro) with GC376 was determined by isothermal titration calorimetry (ITC) and fluorescence resonance energy transfer (FRET) assay, respectively. The results showed that GC376 binds to SARS-CoV-2 M(pro) tightly (K(D) = 1.6 muM) and efficiently inhibit its proteolytic activity (IC(50) = 0.89 muM). We also elucidate the high-resolution structure of dimeric SARS-CoV-2 M(pro) in complex with GC376. The cocrystal structure showed that GC376 and the catalytic Cys145 of M(pro) covalently linked through forming a hemithioacetal group and releasing a sulfonic acid group. Because GC376 is already known as a broad-spectrum antiviral medication and successfully used in animal, it will be a suitable candidate for anti-COVID-19 treatment. Twit Text FOAVip Structural basis of SARS-CoV-2 main protease inhibition by a broad-spectrum anti-coronaviral drug ????Am J Cancer Res http://www.kidney.de/pget.php?&tw=1&pmid=32905393 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32905393 #FOAvip English Wikipedia <ref>{{Cite pmid|32905393}}</ref> Structural basis of SARS-CoV-2 main protease inhibition by a broad-spectrum anti-coronaviral drug #MMPMID32905393 Wang YC; Yang WH; Yang CS; Hou MH; Tsai CL; Chou YZ; Hung MC; Chen Y Am J Cancer Res 2020[]; 10 (8): 2535-2545 PMID32905393show ga The coronavirus disease 2019 (COVID-19) pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) or 2019 novel coronavirus (2019-nCoV), took tens of thousands of lives and caused tremendous economic losses. The main protease (M(pro)) of SARS-CoV-2 is a potential target for treatment of COVID-19 due to its critical role in maturation of viral proteins and subsequent viral replication. Conceptually and technically, targeting therapy against M(pro) is similar to target therapy to treat cancer. Previous studies show that GC376, a broad-spectrum dipeptidyl M(pro) inhibitor, efficiently blocks the proliferation of many animal and human coronaviruses including SARS-CoV, Middle East respiratory syndrome coronavirus (MERS-CoV), porcine epidemic diarrhea virus (PEDV), and feline infectious peritonitis virus (FIPV). Due to the conservation of structure and catalytic mechanism of coronavirus main protease, repurposition of GC376 against SARS-CoV-2 may be an effective way for the treatment of COVID-19 in humans. To validate this conjecture, the binding affinity and IC(50) value of M(pro) with GC376 was determined by isothermal titration calorimetry (ITC) and fluorescence resonance energy transfer (FRET) assay, respectively. The results showed that GC376 binds to SARS-CoV-2 M(pro) tightly (K(D) = 1.6 muM) and efficiently inhibit its proteolytic activity (IC(50) = 0.89 muM). We also elucidate the high-resolution structure of dimeric SARS-CoV-2 M(pro) in complex with GC376. The cocrystal structure showed that GC376 and the catalytic Cys145 of M(pro) covalently linked through forming a hemithioacetal group and releasing a sulfonic acid group. Because GC376 is already known as a broad-spectrum antiviral medication and successfully used in animal, it will be a suitable candidate for anti-COVID-19 treatment. äStructural basis of SARS-CoV-2 main protease inhibition by a broad-spe(epmc).pdf DeepDyve Pubget Overpricing