| pubmed-article:15137052 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15137052 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:15137052 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:15137052 | lifeskim:mentions | umls-concept:C0014139 | lld:lifeskim |
| pubmed-article:15137052 | lifeskim:mentions | umls-concept:C0025543 | lld:lifeskim |
| pubmed-article:15137052 | lifeskim:mentions | umls-concept:C1618608 | lld:lifeskim |
| pubmed-article:15137052 | lifeskim:mentions | umls-concept:C1417203 | lld:lifeskim |
| pubmed-article:15137052 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:15137052 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15137052 | pubmed:dateCreated | 2004-5-11 | lld:pubmed |
| pubmed-article:15137052 | pubmed:abstractText | Matrix metalloproteinases (MMPs) are multidomain zinc-dependent proteolytic enzymes that play pivotal roles in many normal and pathological processes. Some members of the MMP family are anchored to the plasma membrane via specialized domains and thus are perfectly suited for pericellular proteolysis. Membrane-anchoring also confers the membrane type-MMPs (MT-MMPs) a unique and complex array of regulatory processes that endow cells with the ability to control MT-MMP-dependent proteolytic activity independently of the levels of endogenous protease inhibitors. Emerging evidence indicates that mechanisms as diverse as autocatalytic processing, ectodomain shedding, homodimerization and internalization can all contribute to the modulation of MT-MMP activity on the cell surface. How these distinct processes interact to attain the optimal level of enzyme activity in a particular setting and the molecular signals that trigger them constitute a new paradigm in MMP regulation. This review will discuss the recent findings concerning these diverse regulatory mechanisms in the context of MT1-MMP (MMP-14). | lld:pubmed |
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| pubmed-article:15137052 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15137052 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15137052 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15137052 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15137052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15137052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15137052 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15137052 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:15137052 | pubmed:issn | 0021-9541 | lld:pubmed |
| pubmed-article:15137052 | pubmed:author | pubmed-author:FridmanRafael... | lld:pubmed |
| pubmed-article:15137052 | pubmed:author | pubmed-author:TothMartaM | lld:pubmed |
| pubmed-article:15137052 | pubmed:author | pubmed-author:OsenkowskiPam... | lld:pubmed |
| pubmed-article:15137052 | pubmed:copyrightInfo | Copyright 2004 Wiley-Liss, Inc. | lld:pubmed |
| pubmed-article:15137052 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15137052 | pubmed:volume | 200 | lld:pubmed |
| pubmed-article:15137052 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15137052 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15137052 | pubmed:pagination | 2-10 | lld:pubmed |
| pubmed-article:15137052 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:15137052 | pubmed:meshHeading | pubmed-meshheading:15137052... | lld:pubmed |
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| pubmed-article:15137052 | pubmed:meshHeading | pubmed-meshheading:15137052... | lld:pubmed |
| pubmed-article:15137052 | pubmed:meshHeading | pubmed-meshheading:15137052... | lld:pubmed |
| pubmed-article:15137052 | pubmed:meshHeading | pubmed-meshheading:15137052... | lld:pubmed |
| pubmed-article:15137052 | pubmed:meshHeading | pubmed-meshheading:15137052... | lld:pubmed |
| pubmed-article:15137052 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15137052 | pubmed:articleTitle | Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP). | lld:pubmed |
| pubmed-article:15137052 | pubmed:affiliation | Department of Pathology, Wayne State University School of Medicine, Detroit, Michigan 48201, USA. | lld:pubmed |
| pubmed-article:15137052 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15137052 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15137052 | pubmed:publicationType | Review | lld:pubmed |
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