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.

10.1021/ml2002373 http://scihub22266oqcxt.onion/10.1021/ml2002373 C4025764!4025764!24900449     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Med+Chem+Lett 2012 ; 3 (3): 193-7 Nephropedia Template TP {{tp|p=24900449|t=2012. BACE1 Inhibitor Peptides: Can an Infinitely Small kcat Value Turn the Substrate of an Enzyme into Its Inhibitor?|pdf=|usr=}}{{24900449}} gab.com Text BACE1 Inhibitor Peptides: Can an Infinitely Small kcat Value Turn the Substrate of an Enzyme into Its Inhibitor JO: ACS Med Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=24900449 #FOAvip Recently, we reported substrate-based pentapeptidic ?-secretase (BACE1) inhibitors with a hydroxymethylcarbonyl isostere as a substrate transition-state mimic. These inhibitors showed potent BACE1 inhibitory activity in enzyme and cell assays, with KMI-429 showing in vivo inhibition of A? production. We also designed and synthesized nonpeptidic and small-sized BACE1 inhibitors using ?in-silico conformational structure-based design?. By studying the structure?activity relationship of these inhibitors, we found that the ??? interaction of an inhibitor with the BACE1-Arg235 side chain played a key role in the inhibition of BACE1. We speculated that a peptide capable of binding to the BACE1-Arg235 side chain via the ??? interaction might exhibit BACE1 inhibitory activity. Hence, we designed and synthesized a series of peptides that were modified at the P2 position and found that some of these peptides exhibited a potent BACE1 inhibitory activity despite their structural similarity to the BACE1 substrate. Twit Text FOAVip BACE1 Inhibitor Peptides: Can an Infinitely Small kcat Value Turn the Substrate of an Enzyme into Its Inhibitor ????ACS Med Chem Lett http://www.kidney.de/pget.php?&tw=1&pmid=24900449 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24900449 #FOAvip English Wikipedia <ref>{{Cite pmid|24900449}}</ref> BACE1 Inhibitor Peptides: Can an Infinitely Small kcat Value Turn the Substrate of an Enzyme into Its Inhibitor? #MMPMID24900449 Hamada Y; Ishiura S; Kiso Y ACS Med Chem Lett 2012[Mar]; 3 (3): 193-7 PMID24900449show ga Recently, we reported substrate-based pentapeptidic ?-secretase (BACE1) inhibitors with a hydroxymethylcarbonyl isostere as a substrate transition-state mimic. These inhibitors showed potent BACE1 inhibitory activity in enzyme and cell assays, with KMI-429 showing in vivo inhibition of A? production. We also designed and synthesized nonpeptidic and small-sized BACE1 inhibitors using ?in-silico conformational structure-based design?. By studying the structure?activity relationship of these inhibitors, we found that the ??? interaction of an inhibitor with the BACE1-Arg235 side chain played a key role in the inhibition of BACE1. We speculated that a peptide capable of binding to the BACE1-Arg235 side chain via the ??? interaction might exhibit BACE1 inhibitory activity. Hence, we designed and synthesized a series of peptides that were modified at the P2 position and found that some of these peptides exhibited a potent BACE1 inhibitory activity despite their structural similarity to the BACE1 substrate. äBACE1 Inhibitor Peptides: Can an Infinitely Small kcat Value Turn the (epmc).pdf DeepDyve Pubget Overpricing