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.

10.1016/j.antiviral.2021.105020 http://scihub22266oqcxt.onion/10.1016/j.antiviral.2021.105020 33515606!7839511!33515606     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Antiviral+Res 2021 ; 187 (ä): 105020 Nephropedia Template TP {{tp|p=33515606|t=2021. Dual inhibition of SARS-CoV-2 and human rhinovirus with protease inhibitors in clinical development |pdf=|usr=}}{{33515606}} gab.com Text Dual inhibition of SARS-CoV-2 and human rhinovirus with protease inhibitors in clinical development JO: Antiviral Res http://www.kidney.de/pget.php?&tw=1&pmid=33515606 #FOAvip The 3-chymotrypsin-like cysteine protease (3CLpro) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is considered a major target for the discovery of direct antiviral agents. We previously reported the evaluation of SARS-CoV-2 3CLpro inhibitors in a novel self-assembled monolayer desorption ionization mass spectrometry (SAMDI-MS) enzymatic assay (Gurard-Levin et al., 2020). The assay was further improved by adding the rhinovirus HRV3C protease to the same well as the SARS-CoV-2 3CLpro enzyme. High substrate specificity for each enzyme allowed the proteases to be combined in a single assay reaction without interfering with their individual activities. This novel duplex assay was used to profile a diverse set of reference protease inhibitors. The protease inhibitors were grouped into three categories based on their relative potency against 3CLpro and HRV3C including those that are: equipotent against 3CLpro and HRV3C (GC376 and calpain inhibitor II), selective for 3CLpro (PF-00835231, calpain inhibitor XII, boceprevir), and selective for HRV3C (rupintrivir). Structural analysis showed that the combination of minimal interactions, conformational flexibility, and limited bulk allows GC376 and calpain inhibitor II to potently inhibit both enzymes. In contrast, bulkier compounds interacting more tightly with pockets P2, P3, and P4 due to optimization for a specific target display a more selective inhibition profile. Consistently, the most selective viral protease inhibitors were relatively weak inhibitors of human cathepsin L. Taken together, these results can guide the design of cysteine protease inhibitors that are either virus-specific or retain a broad antiviral spectrum against coronaviruses and rhinoviruses. Twit Text FOAVip Dual inhibition of SARS-CoV-2 and human rhinovirus with protease inhibitors in clinical development ????Antiviral Res http://www.kidney.de/pget.php?&tw=1&pmid=33515606 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33515606 #FOAvip English Wikipedia <ref>{{Cite pmid|33515606}}</ref> Dual inhibition of SARS-CoV-2 and human rhinovirus with protease inhibitors in clinical development #MMPMID33515606 Liu C; Boland S; Scholle MD; Bardiot D; Marchand A; Chaltin P; Blatt LM; Beigelman L; Symons JA; Raboisson P; Gurard-Levin ZA; Vandyck K; Deval J Antiviral Res 2021[Mar]; 187 (ä): 105020 PMID33515606show ga The 3-chymotrypsin-like cysteine protease (3CLpro) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is considered a major target for the discovery of direct antiviral agents. We previously reported the evaluation of SARS-CoV-2 3CLpro inhibitors in a novel self-assembled monolayer desorption ionization mass spectrometry (SAMDI-MS) enzymatic assay (Gurard-Levin et al., 2020). The assay was further improved by adding the rhinovirus HRV3C protease to the same well as the SARS-CoV-2 3CLpro enzyme. High substrate specificity for each enzyme allowed the proteases to be combined in a single assay reaction without interfering with their individual activities. This novel duplex assay was used to profile a diverse set of reference protease inhibitors. The protease inhibitors were grouped into three categories based on their relative potency against 3CLpro and HRV3C including those that are: equipotent against 3CLpro and HRV3C (GC376 and calpain inhibitor II), selective for 3CLpro (PF-00835231, calpain inhibitor XII, boceprevir), and selective for HRV3C (rupintrivir). Structural analysis showed that the combination of minimal interactions, conformational flexibility, and limited bulk allows GC376 and calpain inhibitor II to potently inhibit both enzymes. In contrast, bulkier compounds interacting more tightly with pockets P2, P3, and P4 due to optimization for a specific target display a more selective inhibition profile. Consistently, the most selective viral protease inhibitors were relatively weak inhibitors of human cathepsin L. Taken together, these results can guide the design of cysteine protease inhibitors that are either virus-specific or retain a broad antiviral spectrum against coronaviruses and rhinoviruses. |Antiviral Agents/chemistry/*pharmacology[MESH] |Binding Sites[MESH] |Cathepsin L/metabolism[MESH] |Coronavirus 3C Proteases/*antagonists & inhibitors[MESH] |Drug Discovery[MESH] |Glycoproteins/pharmacology[MESH] |Humans[MESH] |Kinetics[MESH] |Models, Molecular[MESH] |Protease Inhibitors/chemistry/*pharmacology[MESH] |Pyrrolidines/pharmacology[MESH] |Rhinovirus/*drug effects[MESH] |SARS-CoV-2/*drug effects[MESH]Dual inhibition of SARS-CoV-2 and human rhinovirus with protease inhib(epmc).pdf DeepDyve Pubget Overpricing