| pubmed-article:18096385 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18096385 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:18096385 | lifeskim:mentions | umls-concept:C0870883 | lld:lifeskim |
| pubmed-article:18096385 | lifeskim:mentions | umls-concept:C0599740 | lld:lifeskim |
| pubmed-article:18096385 | lifeskim:mentions | umls-concept:C1958507 | lld:lifeskim |
| pubmed-article:18096385 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:18096385 | pubmed:dateCreated | 2008-5-21 | lld:pubmed |
| pubmed-article:18096385 | pubmed:abstractText | The naturally occurring phosphonotripeptide K-26 is a potent angiotensin converting enzyme (ACE) inhibitor containing an alpha-amino phosphonic acid analogue of tyrosine. Previous studies have demonstrated that canonical peptide analogues of K-26 are micromolar inhibitors of ACE. To ascertain the structure-activity relationships in this class of ACE inhibitory natural products, K-26 and eight analogues were chemically synthesized and evaluated. Phosphonyl substitution was found to be the critical determinant of activity, resulting in a 1500-fold increase in ACE inhibition versus carboxyl analogues. Secondarily, the absolute configuration of the terminal alpha-amino phosphonate and N-acetylation were found to significantly modulate ACE inhibitory activity. | lld:pubmed |
| pubmed-article:18096385 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18096385 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18096385 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18096385 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18096385 | pubmed:month | May | lld:pubmed |
| pubmed-article:18096385 | pubmed:issn | 1464-3405 | lld:pubmed |
| pubmed-article:18096385 | pubmed:author | pubmed-author:NtaiIoannaI | lld:pubmed |
| pubmed-article:18096385 | pubmed:author | pubmed-author:BachmannBrian... | lld:pubmed |
| pubmed-article:18096385 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18096385 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:18096385 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:18096385 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18096385 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18096385 | pubmed:pagination | 3068-71 | lld:pubmed |
| pubmed-article:18096385 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
| pubmed-article:18096385 | pubmed:meshHeading | pubmed-meshheading:18096385... | lld:pubmed |
| pubmed-article:18096385 | pubmed:meshHeading | pubmed-meshheading:18096385... | lld:pubmed |
| pubmed-article:18096385 | pubmed:meshHeading | pubmed-meshheading:18096385... | lld:pubmed |
| pubmed-article:18096385 | pubmed:meshHeading | pubmed-meshheading:18096385... | lld:pubmed |
| pubmed-article:18096385 | pubmed:meshHeading | pubmed-meshheading:18096385... | lld:pubmed |
| pubmed-article:18096385 | pubmed:meshHeading | pubmed-meshheading:18096385... | lld:pubmed |
| pubmed-article:18096385 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18096385 | pubmed:articleTitle | Identification of ACE pharmacophore in the phosphonopeptide metabolite K-26. | lld:pubmed |
| pubmed-article:18096385 | pubmed:affiliation | Department of Chemistry, Vanderbilt University, Nashville, TN 37235, USA. | lld:pubmed |
| pubmed-article:18096385 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18096385 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:18096385 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:18096385 | lld:chembl |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18096385 | lld:pubmed |
