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.ejphar.2020.173499 http://scihub22266oqcxt.onion/10.1016/j.ejphar.2020.173499 32841639!7443098!32841639     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32841639&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Eur+J+Pharmacol 2020 ; 885 (ä): 173499 Nephropedia Template TP {{tp|p=32841639|t=2020. Food proteins are a potential resource for mining cathepsin L inhibitory drugs to combat SARS-CoV-2 |pdf=|usr=}}{{32841639}} gab.com Text Food proteins are a potential resource for mining cathepsin L inhibitory drugs to combat SARS-CoV-2 JO: Eur J Pharmacol http://www.kidney.de/pget.php?&tw=1&pmid=32841639 #FOAvip The entry of SARS-CoV-2 into host cells proceeds by a proteolysis process, which involves the lysosomal peptidase cathepsin L. Inhibition of cathepsin L is therefore considered an effective method to decrease the virus internalization. Analysis from the perspective of structure-functionality elucidates that cathepsin L inhibitory proteins/peptides found in food share specific features: multiple disulfide crosslinks (buried in protein core), lack or low contents of (small) alpha-helices, and high surface hydrophobicity. Lactoferrin can inhibit cathepsin L, but not cathepsins B and H. This selective inhibition might be useful in fine targeting of cathepsin L. Molecular docking indicated that only the carboxyl-terminal lobe of lactoferrin interacts with cathepsin L and that the active site cleft of cathepsin L is heavily superposed by lactoferrin. A controlled proteolysis process might yield lactoferrin-derived peptides that strongly inhibit cathepsin L. Twit Text FOAVip Food proteins are a potential resource for mining cathepsin L inhibitory drugs to combat SARS-CoV-2 ????Eur J Pharmacol http://www.kidney.de/pget.php?&tw=1&pmid=32841639 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32841639 #FOAvip English Wikipedia <ref>{{Cite pmid|32841639}}</ref> Food proteins are a potential resource for mining cathepsin L inhibitory drugs to combat SARS-CoV-2 #MMPMID32841639 Madadlou A Eur J Pharmacol 2020[Oct]; 885 (ä): 173499 PMID32841639show ga The entry of SARS-CoV-2 into host cells proceeds by a proteolysis process, which involves the lysosomal peptidase cathepsin L. Inhibition of cathepsin L is therefore considered an effective method to decrease the virus internalization. Analysis from the perspective of structure-functionality elucidates that cathepsin L inhibitory proteins/peptides found in food share specific features: multiple disulfide crosslinks (buried in protein core), lack or low contents of (small) alpha-helices, and high surface hydrophobicity. Lactoferrin can inhibit cathepsin L, but not cathepsins B and H. This selective inhibition might be useful in fine targeting of cathepsin L. Molecular docking indicated that only the carboxyl-terminal lobe of lactoferrin interacts with cathepsin L and that the active site cleft of cathepsin L is heavily superposed by lactoferrin. A controlled proteolysis process might yield lactoferrin-derived peptides that strongly inhibit cathepsin L. |*Food[MESH] |Antiviral Agents/chemistry/*pharmacology[MESH] |Betacoronavirus/*drug effects/*physiology[MESH] |Cathepsin L/*antagonists & inhibitors[MESH] |Lactoferrin/chemistry/*pharmacology[MESH] |Protease Inhibitors/chemistry/*pharmacology[MESH] |SARS-CoV-2[MESH]Food proteins are a potential resource for mining cathepsin L inhibito(epmc).pdf DeepDyve Pubget Overpricing