| pubmed-article:8910479 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8910479 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8910479 | lifeskim:mentions | umls-concept:C0041455 | lld:lifeskim |
| pubmed-article:8910479 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8910479 | lifeskim:mentions | umls-concept:C0162745 | lld:lifeskim |
| pubmed-article:8910479 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:8910479 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:8910479 | lifeskim:mentions | umls-concept:C1704222 | lld:lifeskim |
| pubmed-article:8910479 | pubmed:issue | 45 | lld:pubmed |
| pubmed-article:8910479 | pubmed:dateCreated | 1996-12-30 | lld:pubmed |
| pubmed-article:8910479 | pubmed:abstractText | Vertebrate collagenases, matrix metalloproteinases (MMPs), cleave type I collagen at a single helical locus. We show here that rodent interstitial collagenases (MMP-13), but not human fibroblast collagenase (MMP-1), cleave type I collagen at an additional aminotelopeptide locus. Collagenase cDNAs and chimeric constructs in pET-3d, juxtaposing MMP-13 sequences amino-terminal to the active site in the catalytic domain and MMP-1 sequences carboxyl-terminal and vice versa, were expressed in Escherichia coli. Assays utilized collagen from wild type (+/+) mice or mice that carry a targeted mutation (r/r) that encodes substitutions in alpha1(I) chains that prevent collagenase cleavage at the helical locus. MMP-13 and chimeric molecules that contained the MMP-13 sequences amino-terminal to the active site cleaved (+/+) collagen at the helical locus and cleaved cross-linked (r/r) collagen in the aminotelopeptide (beta components converted to alpha chains). Human MMP-1 and chimeric MMP-1/MMP-13 with MMP-1 sequences amino-terminal to the active site cleaved collagen at the helical locus but not in the aminotelopeptide. All activities were inhibited by TIMP-1, 1,10-phenanthroline, and EDTA. Sequences in the distal two-thirds of the catalytic domain determine the aminotelopeptide-degrading capacity of MMP-13. | lld:pubmed |
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| pubmed-article:8910479 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8910479 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8910479 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8910479 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8910479 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8910479 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8910479 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8910479 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8910479 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:8910479 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8910479 | pubmed:author | pubmed-author:EeckhoutYY | lld:pubmed |
| pubmed-article:8910479 | pubmed:author | pubmed-author:JaenischRR | lld:pubmed |
| pubmed-article:8910479 | pubmed:author | pubmed-author:KraneS MSM | lld:pubmed |
| pubmed-article:8910479 | pubmed:author | pubmed-author:LimPP | lld:pubmed |
| pubmed-article:8910479 | pubmed:author | pubmed-author:JeffreyJ JJJ | lld:pubmed |
| pubmed-article:8910479 | pubmed:author | pubmed-author:WitterJ PJP | lld:pubmed |
| pubmed-article:8910479 | pubmed:author | pubmed-author:HenrietPP | lld:pubmed |
| pubmed-article:8910479 | pubmed:author | pubmed-author:WuHH | lld:pubmed |
| pubmed-article:8910479 | pubmed:author | pubmed-author:ByrneM HMH | lld:pubmed |
| pubmed-article:8910479 | pubmed:author | pubmed-author:LemaîtreVV | lld:pubmed |
| pubmed-article:8910479 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8910479 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:8910479 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8910479 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8910479 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8910479 | pubmed:pagination | 28509-15 | lld:pubmed |
| pubmed-article:8910479 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8910479 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8910479 | pubmed:articleTitle | Different collagenase gene products have different roles in degradation of type I collagen. | lld:pubmed |
| pubmed-article:8910479 | pubmed:affiliation | Department of Medicine, Harvard Medical School and the Arthritis Unit, Massachusetts General Hospital, Boston, Massachusetts 02114, USA. kranes@A1.mgh.harvard.edu | lld:pubmed |
| pubmed-article:8910479 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8910479 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8910479 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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