| pubmed-article:2539108 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2539108 | lifeskim:mentions | umls-concept:C0022634 | lld:lifeskim |
| pubmed-article:2539108 | lifeskim:mentions | umls-concept:C0162745 | lld:lifeskim |
| pubmed-article:2539108 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:2539108 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
| pubmed-article:2539108 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:2539108 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:2539108 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
| pubmed-article:2539108 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2539108 | pubmed:dateCreated | 1989-4-25 | lld:pubmed |
| pubmed-article:2539108 | pubmed:abstractText | The ketone cinnamoyl-(1-13C-Phe)-CGly-Pro-Pro [(4-13C-5-cinnamido-4-oxo-6-phenylhexanoyl)-Pro-Pro 2] competitively inhibits a mixture of collagenases from Clostridium histolyticum with a Ki of 40 +/- 6 nM. 13C-nmr spectroscopy of the ketone in the presence of this collagenase shows a bound 13C resonance at 102.6 ppm and the resonance of the free ketone at 212 ppm. Ketone alone shows no trace (less than 0.5%) of a resonance in the region around 100 ppm. The bound resonance is displaceable by another competitive inhibitor. This ketone is thus a transition state analog which is rehybridized from trigonal planar to tetrahedral upon binding to collagenase. | lld:pubmed |
| pubmed-article:2539108 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2539108 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2539108 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2539108 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2539108 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2539108 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2539108 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2539108 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2539108 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:2539108 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:2539108 | pubmed:author | pubmed-author:GalardyR ERE | lld:pubmed |
| pubmed-article:2539108 | pubmed:author | pubmed-author:GrobelnyDD | lld:pubmed |
| pubmed-article:2539108 | pubmed:author | pubmed-author:TeaterCC | lld:pubmed |
| pubmed-article:2539108 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2539108 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2539108 | pubmed:volume | 159 | lld:pubmed |
| pubmed-article:2539108 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2539108 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2539108 | pubmed:pagination | 426-31 | lld:pubmed |
| pubmed-article:2539108 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2539108 | pubmed:meshHeading | pubmed-meshheading:2539108-... | lld:pubmed |
| pubmed-article:2539108 | pubmed:meshHeading | pubmed-meshheading:2539108-... | lld:pubmed |
| pubmed-article:2539108 | pubmed:meshHeading | pubmed-meshheading:2539108-... | lld:pubmed |
| pubmed-article:2539108 | pubmed:meshHeading | pubmed-meshheading:2539108-... | lld:pubmed |
| pubmed-article:2539108 | pubmed:meshHeading | pubmed-meshheading:2539108-... | lld:pubmed |
| pubmed-article:2539108 | pubmed:meshHeading | pubmed-meshheading:2539108-... | lld:pubmed |
| pubmed-article:2539108 | pubmed:meshHeading | pubmed-meshheading:2539108-... | lld:pubmed |
| pubmed-article:2539108 | pubmed:meshHeading | pubmed-meshheading:2539108-... | lld:pubmed |
| pubmed-article:2539108 | pubmed:meshHeading | pubmed-meshheading:2539108-... | lld:pubmed |
| pubmed-article:2539108 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2539108 | pubmed:articleTitle | The ketone cinnamoyl-(1-13C-Phe)-CGly-Pro-Pro is a tetrahedral transition state analog inhibitor of C. histolyticum collagenase. | lld:pubmed |
| pubmed-article:2539108 | pubmed:affiliation | Department of Biochemistry, University of Kentucky, Lexington 40536. | lld:pubmed |
| pubmed-article:2539108 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2539108 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2539108 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
