| pubmed-article:9119036 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9119036 | lifeskim:mentions | umls-concept:C0145988 | lld:lifeskim |
| pubmed-article:9119036 | lifeskim:mentions | umls-concept:C0528100 | lld:lifeskim |
| pubmed-article:9119036 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:9119036 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:9119036 | lifeskim:mentions | umls-concept:C1548602 | lld:lifeskim |
| pubmed-article:9119036 | lifeskim:mentions | umls-concept:C0246551 | lld:lifeskim |
| pubmed-article:9119036 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9119036 | pubmed:dateCreated | 1997-4-22 | lld:pubmed |
| pubmed-article:9119036 | pubmed:abstractText | Membrane-type-1 matrix metalloproteinase has been identified as an activator of the matrix metalloproteinase progelatinase A at cell surfaces. We report here that a soluble active form of membrane-type-2 matrix metalloproteinase can also process progelatinase A in a comparable fashion to the type-1 at rates which are dependent on the concentration of the proenzyme. Activation is inhibited by tissue inhibitors of metalloproteinases TIMP-2 and TIMP-3, but only partially by TIMP-1. These results suggest that cellular activation of progelatinase A may be initiated by different members of the membrane-type matrix metalloproteinase family depending on tissue distribution. | lld:pubmed |
| pubmed-article:9119036 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9119036 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9119036 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9119036 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9119036 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9119036 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:9119036 | pubmed:author | pubmed-author:MurphyGG | lld:pubmed |
| pubmed-article:9119036 | pubmed:author | pubmed-author:WillHH | lld:pubmed |
| pubmed-article:9119036 | pubmed:author | pubmed-author:ButlerG SGS | lld:pubmed |
| pubmed-article:9119036 | pubmed:author | pubmed-author:AtkinsonS JSJ | lld:pubmed |
| pubmed-article:9119036 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9119036 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9119036 | pubmed:volume | 244 | lld:pubmed |
| pubmed-article:9119036 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9119036 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9119036 | pubmed:pagination | 653-7 | lld:pubmed |
| pubmed-article:9119036 | pubmed:dateRevised | 2009-9-29 | lld:pubmed |
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| pubmed-article:9119036 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9119036 | pubmed:articleTitle | Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases. | lld:pubmed |
| pubmed-article:9119036 | pubmed:affiliation | Strangeways Research Laboratory, Cambridge, UK. | lld:pubmed |
| pubmed-article:9119036 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9119036 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:9119036 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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