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.biteb.2021.100756 http://scihub22266oqcxt.onion/10.1016/j.biteb.2021.100756 34226889!8245309!34226889     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Bioresour+Technol+Rep 2021 ; 15 (ä): 100756 Nephropedia Template TP {{tp|p=34226889|t=2021. Repurposing proteases: An in-silico analysis of the binding potential of extracellular fungal proteases with selected viral proteins |pdf=|usr=}}{{34226889}} gab.com Text Repurposing proteases: An in-silico analysis of the binding potential of extracellular fungal proteases with selected viral proteins JO: Bioresour Technol Rep http://www.kidney.de/pget.php?&tw=1&pmid=34226889 #FOAvip Proteases have long been the target of many drugs, but their potential as therapeutic agents is a well-known, but under-explored area. Due to the heightened threat from new and emerging infectious agents, it is worthwhile to tap into the vast microbial protease resource to identify potential therapeutics. By docking proteases of the fungus Penicillium janthinellum NCIM 1366 with the proteins encoded by the SARS-CoV-2 virus, the enzymes that have the potential to bind with, and thereby degrade viral proteins were identified. In-silico docking analysis revealed that both fungal and commercially available proteases belonging to the A1A, M20A, S10, S8A and T1A families were able to bind the viral spike, envelope, ORF-7a and Nsp2 proteins (binding energy < -50 kJ/mol), thereby opening up the possibility of developing additional therapeutic applications for these enzymes. Twit Text FOAVip Repurposing proteases: An in-silico analysis of the binding potential of extracellular fungal proteases with selected viral proteins ????Bioresour Technol Rep http://www.kidney.de/pget.php?&tw=1&pmid=34226889 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34226889 #FOAvip English Wikipedia <ref>{{Cite pmid|34226889}}</ref> Repurposing proteases: An in-silico analysis of the binding potential of extracellular fungal proteases with selected viral proteins #MMPMID34226889 Christopher M; Kooloth-Valappil P; Sreeja-Raju A; Sukumaran RK Bioresour Technol Rep 2021[Sep]; 15 (ä): 100756 PMID34226889show ga Proteases have long been the target of many drugs, but their potential as therapeutic agents is a well-known, but under-explored area. Due to the heightened threat from new and emerging infectious agents, it is worthwhile to tap into the vast microbial protease resource to identify potential therapeutics. By docking proteases of the fungus Penicillium janthinellum NCIM 1366 with the proteins encoded by the SARS-CoV-2 virus, the enzymes that have the potential to bind with, and thereby degrade viral proteins were identified. In-silico docking analysis revealed that both fungal and commercially available proteases belonging to the A1A, M20A, S10, S8A and T1A families were able to bind the viral spike, envelope, ORF-7a and Nsp2 proteins (binding energy < -50 kJ/mol), thereby opening up the possibility of developing additional therapeutic applications for these enzymes. äRepurposing proteases: An in-silico analysis of the binding potential (epmc).pdf DeepDyve Pubget Overpricing