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.

10.1126/sciadv.abe0751 http://scihub22266oqcxt.onion/10.1126/sciadv.abe0751 33158912!7725459!33158912     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 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 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Adv 2020 ; 6 (50): ä Nephropedia Template TP {{tp|p=33158912|t=2020. Structure and inhibition of the SARS-CoV-2 main protease reveal strategy for developing dual inhibitors against M(pro) and cathepsin L |pdf=|usr=}}{{33158912}} gab.com Text Structure and inhibition of the SARS-CoV-2 main protease reveal strategy for developing dual inhibitors against M(pro) and cathepsin L JO: Sci Adv http://www.kidney.de/pget.php?&tw=1&pmid=33158912 #FOAvip The main protease (M(pro)) of SARS-CoV-2 is a key antiviral drug target. While most M(pro) inhibitors have a gamma-lactam glutamine surrogate at the P1 position, we recently found that several M(pro) inhibitors have hydrophobic moieties at the P1 site, including calpain inhibitors II and XII, which are also active against human cathepsin L, a host protease that is important for viral entry. In this study, we solved x-ray crystal structures of M(pro) in complex with calpain inhibitors II and XII and three analogs of GC-376 The structure of M(pro) with calpain inhibitor II confirmed that the S1 pocket can accommodate a hydrophobic methionine side chain, challenging the idea that a hydrophilic residue is necessary at this position. The structure of calpain inhibitor XII revealed an unexpected, inverted binding pose. Together, the biochemical, computational, structural, and cellular data presented herein provide new directions for the development of dual inhibitors as SARS-CoV-2 antivirals. Twit Text FOAVip Structure and inhibition of the SARS-CoV-2 main protease reveal strategy for developing dual inhibitors against M(pro) and cathepsin L ????Sci Adv http://www.kidney.de/pget.php?&tw=1&pmid=33158912 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33158912 #FOAvip English Wikipedia <ref>{{Cite pmid|33158912}}</ref> Structure and inhibition of the SARS-CoV-2 main protease reveal strategy for developing dual inhibitors against M(pro) and cathepsin L #MMPMID33158912 Sacco MD; Ma C; Lagarias P; Gao A; Townsend JA; Meng X; Dube P; Zhang X; Hu Y; Kitamura N; Hurst B; Tarbet B; Marty MT; Kolocouris A; Xiang Y; Chen Y; Wang J Sci Adv 2020[Dec]; 6 (50): ä PMID33158912show ga The main protease (M(pro)) of SARS-CoV-2 is a key antiviral drug target. While most M(pro) inhibitors have a gamma-lactam glutamine surrogate at the P1 position, we recently found that several M(pro) inhibitors have hydrophobic moieties at the P1 site, including calpain inhibitors II and XII, which are also active against human cathepsin L, a host protease that is important for viral entry. In this study, we solved x-ray crystal structures of M(pro) in complex with calpain inhibitors II and XII and three analogs of GC-376 The structure of M(pro) with calpain inhibitor II confirmed that the S1 pocket can accommodate a hydrophobic methionine side chain, challenging the idea that a hydrophilic residue is necessary at this position. The structure of calpain inhibitor XII revealed an unexpected, inverted binding pose. Together, the biochemical, computational, structural, and cellular data presented herein provide new directions for the development of dual inhibitors as SARS-CoV-2 antivirals. |*Drug Design[MESH] |*Molecular Dynamics Simulation[MESH] |Animals[MESH] |Caco-2 Cells[MESH] |Cathepsin L/antagonists & inhibitors/*chemistry/metabolism[MESH] |Cell Line[MESH] |Cell Line, Tumor[MESH] |Chlorocebus aethiops[MESH] |Coronavirus 3C Proteases/antagonists & inhibitors/*chemistry/metabolism[MESH] |Crystallography, X-Ray[MESH] |Dogs[MESH] |Humans[MESH] |Kinetics[MESH] |Madin Darby Canine Kidney Cells[MESH] |Models, Chemical[MESH] |Molecular Structure[MESH] |Protease Inhibitors/*chemistry/metabolism/pharmacology[MESH] |Protein Domains[MESH]Structure and inhibition of the SARS-CoV-2 main protease reveal strate(epmc).pdf DeepDyve Pubget Overpricing