| pubmed-article:1480035 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1480035 | lifeskim:mentions | umls-concept:C1123023 | lld:lifeskim |
| pubmed-article:1480035 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:1480035 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:1480035 | lifeskim:mentions | umls-concept:C0172956 | lld:lifeskim |
| pubmed-article:1480035 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:1480035 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:1480035 | pubmed:dateCreated | 1993-2-5 | lld:pubmed |
| pubmed-article:1480035 | pubmed:abstractText | Substitution of the phosphonamidate linkage (PO2-NH) for the peptide bond (CO-NH) in substrate-like sequences produces inhibitors of human skin fibroblast collagenase with Ki's far below Km for the native collagen substrate. Using a thiol ester substrate at pH 6.5, phthaloyl-GlyP-Ile-Trp-(S)NHCH-(Me)Ph, the phosphonamidate analog of phthaloyl-Gly-Ile-Trp-(S)NHCH(Me)Ph, has a Ki of 20 nM. Peptide phosphonamidates with amino acid sequences extended further to the right or the left of the Gly-Ile-Trp sequence had higher Ki's. Substitution of the phosphinate linkage (PO2-CH2) for the peptide bond also gives potent inhibitors such as napthoyl-GlyP-C-Leu-Trp-NHBzl, the phosphinate analog of naphtholyl-Gly-Leu-Trp-NHBzl, which has a Ki of 10 nM. Some of the phosphonamidates and phosphinates are also excellent inhibitors of the bacterial zinc metalloproteases thermolysin and Pseudomonas aeruginosa elastase. | lld:pubmed |
| pubmed-article:1480035 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1480035 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1480035 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1480035 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1480035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1480035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1480035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1480035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1480035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1480035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1480035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1480035 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1480035 | pubmed:issn | 0940-1199 | lld:pubmed |
| pubmed-article:1480035 | pubmed:author | pubmed-author:GalardyR ERE | lld:pubmed |
| pubmed-article:1480035 | pubmed:author | pubmed-author:PonczLL | lld:pubmed |
| pubmed-article:1480035 | pubmed:author | pubmed-author:GrobelnyDD | lld:pubmed |
| pubmed-article:1480035 | pubmed:author | pubmed-author:KortylewiczZ... | lld:pubmed |
| pubmed-article:1480035 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1480035 | pubmed:volume | 1 | lld:pubmed |
| pubmed-article:1480035 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1480035 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1480035 | pubmed:pagination | 259-62 | lld:pubmed |
| pubmed-article:1480035 | pubmed:dateRevised | 2008-2-26 | lld:pubmed |
| pubmed-article:1480035 | pubmed:meshHeading | pubmed-meshheading:1480035-... | lld:pubmed |
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| pubmed-article:1480035 | pubmed:meshHeading | pubmed-meshheading:1480035-... | lld:pubmed |
| pubmed-article:1480035 | pubmed:meshHeading | pubmed-meshheading:1480035-... | lld:pubmed |
| pubmed-article:1480035 | pubmed:meshHeading | pubmed-meshheading:1480035-... | lld:pubmed |
| pubmed-article:1480035 | pubmed:meshHeading | pubmed-meshheading:1480035-... | lld:pubmed |
| pubmed-article:1480035 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1480035 | pubmed:articleTitle | Inhibition of human skin fibroblast collagenase by phosphorus-containing peptides. | lld:pubmed |
| pubmed-article:1480035 | pubmed:affiliation | University of Kentucky, Lexington 40536. | lld:pubmed |
| pubmed-article:1480035 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1480035 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1480035 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1480035 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1480035 | lld:pubmed |
