| pubmed-article:1317162 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C0145988 | lld:lifeskim |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C0172537 | lld:lifeskim |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C1611645 | lld:lifeskim |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:1317162 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:1317162 | pubmed:dateCreated | 1992-6-23 | lld:pubmed |
| pubmed-article:1317162 | pubmed:abstractText | Recombinant 72 kDa gelatinase A and a truncated form lacking the C-terminal domain were shown to be activated by organomercurials and to possess similar activities towards a number of substrates. The truncated proenzyme differed from the full-length gelatinase in that it could not be activated by a membrane activator and did not bind tissue inhibitor of metalloproteinase (TIMP)-2. Kinetic studies also showed that the inhibition of the activated truncated enzyme, by both TIMP-1 and TIMP-2, was considerably decreased compared with the full-length enzyme. We conclude that the C-terminal domain plays an important role in the regulation of gelatinase A by a potential physiological activator and inhibitors. | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1317162 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1317162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1317162 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1317162 | pubmed:month | May | lld:pubmed |
| pubmed-article:1317162 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:1317162 | pubmed:author | pubmed-author:MurphyGG | lld:pubmed |
| pubmed-article:1317162 | pubmed:author | pubmed-author:WardR VRV | lld:pubmed |
| pubmed-article:1317162 | pubmed:author | pubmed-author:WillenbrockFF | lld:pubmed |
| pubmed-article:1317162 | pubmed:author | pubmed-author:DochertyA JAJ | lld:pubmed |
| pubmed-article:1317162 | pubmed:author | pubmed-author:CockettM IMI | lld:pubmed |
| pubmed-article:1317162 | pubmed:author | pubmed-author:EatonDD | lld:pubmed |
| pubmed-article:1317162 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1317162 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1317162 | pubmed:volume | 283 ( Pt 3) | lld:pubmed |
| pubmed-article:1317162 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1317162 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1317162 | pubmed:pagination | 637-41 | lld:pubmed |
| pubmed-article:1317162 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:meshHeading | pubmed-meshheading:1317162-... | lld:pubmed |
| pubmed-article:1317162 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1317162 | pubmed:articleTitle | The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases. | lld:pubmed |
| pubmed-article:1317162 | pubmed:affiliation | Strangeways Research Laboratory, Worts Causeway, Cambridge, U.K. | lld:pubmed |
| pubmed-article:1317162 | pubmed:publicationType | Journal Article | lld:pubmed |
