| pubmed-article:14695821 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C0006784 | lld:lifeskim |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C0733755 | lld:lifeskim |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C0600115 | lld:lifeskim |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C0813983 | lld:lifeskim |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
| pubmed-article:14695821 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:14695821 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:14695821 | pubmed:dateCreated | 2003-12-29 | lld:pubmed |
| pubmed-article:14695821 | pubmed:abstractText | A series of novel alpha-ketoamides incorporating stereoisomeric residues with different electronic properties at the P(1)'-position were synthesized to study the electronic requirements for inhibitor binding to the S(1)'-subsite of calpain I. The results of the study suggested the presence of an acidic amino acid residue at the S(1)'-subsite of calpain I. For example, ester 1a (Cbz-l-Leu-l-Phe-CO-d-Phe-OMe) was over 450-fold more potent than its carboxylic acid derivative 2a (Cbz-l-Leu-l-Phe-CO-d-Phe-OH). Additionally, amidino derivative 3a (Cbz-l-Leu-l-Phe-CONH-d-CH[C(NH)NH(2)]Bn) was about 6000-fold more potent than 2a. Furthermore, 4a (Cbz-l-Leu-l-Phe-CONHCH(2)Bn) was 12-fold less potent than its aza analogue 4b (Cbz-l-Leu-l-Phe-CONHNHBn). The results are consistent with the presence of an acidic amino acid residue at the S(1)'-subsite of calpain I. The acidic amino acid residue was found to be Glu261 via molecular modeling studies. | lld:pubmed |
| pubmed-article:14695821 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14695821 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14695821 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14695821 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14695821 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14695821 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14695821 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14695821 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14695821 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:14695821 | pubmed:issn | 0022-2623 | lld:pubmed |
| pubmed-article:14695821 | pubmed:author | pubmed-author:EckR LRL | lld:pubmed |
| pubmed-article:14695821 | pubmed:author | pubmed-author:DonkorIsaac... | lld:pubmed |
| pubmed-article:14695821 | pubmed:author | pubmed-author:ZhengXiaozhan... | lld:pubmed |
| pubmed-article:14695821 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14695821 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:14695821 | pubmed:volume | 47 | lld:pubmed |
| pubmed-article:14695821 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14695821 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14695821 | pubmed:pagination | 72-9 | lld:pubmed |
| pubmed-article:14695821 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:14695821 | pubmed:meshHeading | pubmed-meshheading:14695821... | lld:pubmed |
| pubmed-article:14695821 | pubmed:meshHeading | pubmed-meshheading:14695821... | lld:pubmed |
| pubmed-article:14695821 | pubmed:meshHeading | pubmed-meshheading:14695821... | lld:pubmed |
| pubmed-article:14695821 | pubmed:meshHeading | pubmed-meshheading:14695821... | lld:pubmed |
| pubmed-article:14695821 | pubmed:meshHeading | pubmed-meshheading:14695821... | lld:pubmed |
| pubmed-article:14695821 | pubmed:meshHeading | pubmed-meshheading:14695821... | lld:pubmed |
| pubmed-article:14695821 | pubmed:meshHeading | pubmed-meshheading:14695821... | lld:pubmed |
| pubmed-article:14695821 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14695821 | pubmed:articleTitle | Design, synthesis, molecular modeling studies, and calpain inhibitory activity of novel alpha-ketoamides incorporating polar residues at the P1'-position. | lld:pubmed |
| pubmed-article:14695821 | pubmed:affiliation | Department of Pharmaceutical Sciences, University of Tennessee Health Science Center, Memphis, Tennessee 38163, USA. idonkor@utmem.edu | lld:pubmed |
| pubmed-article:14695821 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14695821 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14695821 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:14695821 | lld:chembl |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14695821 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14695821 | lld:pubmed |
