| pubmed-article:7811262 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7811262 | lifeskim:mentions | umls-concept:C0002395 | lld:lifeskim |
| pubmed-article:7811262 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
| pubmed-article:7811262 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:7811262 | lifeskim:mentions | umls-concept:C0172537 | lld:lifeskim |
| pubmed-article:7811262 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:7811262 | lifeskim:mentions | umls-concept:C0758515 | lld:lifeskim |
| pubmed-article:7811262 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:7811262 | pubmed:dateCreated | 1995-2-2 | lld:pubmed |
| pubmed-article:7811262 | pubmed:abstractText | It has been recently reported that the 72 kDa proteolytic enzyme gelatinase A/type IV collagenase/matrix metalloproteinase 2 (MMP2) hydrolyzed the Lys 16-Leu 17 peptide bond of a synthetic decapeptide (YEVHHQKLVFF) representing the soluble A beta sequence of amino acid residues 10-20. Our aim was to test if this enzyme could also degrade the insoluble 40-42 residues long A beta peptides purified from Alzheimer Disease brain. Our results indicate that MMP2 hydrolyzes A beta 1-40 and A beta 1-42 peptides at Lys 16-Leu 17, at Leu 34-Met 35, and Met 35-Val 36 peptide bonds. These results suggest that MMP2 has the ability of degrading A beta of AD in vitro. If this hydrolysis also occurs in the brain's extracellular matrix, the enzymatic action of gelatinase a could prevent the generation of amyloidogenic A beta 1-40(42). | lld:pubmed |
| pubmed-article:7811262 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7811262 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7811262 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7811262 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7811262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7811262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7811262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7811262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7811262 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7811262 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7811262 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:7811262 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:7811262 | pubmed:author | pubmed-author:BallM JMJ | lld:pubmed |
| pubmed-article:7811262 | pubmed:author | pubmed-author:FridmanRR | lld:pubmed |
| pubmed-article:7811262 | pubmed:author | pubmed-author:CotterR JRJ | lld:pubmed |
| pubmed-article:7811262 | pubmed:author | pubmed-author:WoodsA SAS | lld:pubmed |
| pubmed-article:7811262 | pubmed:author | pubmed-author:RoherA EAE | lld:pubmed |
| pubmed-article:7811262 | pubmed:author | pubmed-author:KasunicT CTC | lld:pubmed |
| pubmed-article:7811262 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7811262 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:7811262 | pubmed:volume | 205 | lld:pubmed |
| pubmed-article:7811262 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7811262 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7811262 | pubmed:pagination | 1755-61 | lld:pubmed |
| pubmed-article:7811262 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:7811262 | pubmed:meshHeading | pubmed-meshheading:7811262-... | lld:pubmed |
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| pubmed-article:7811262 | pubmed:meshHeading | pubmed-meshheading:7811262-... | lld:pubmed |
| pubmed-article:7811262 | pubmed:meshHeading | pubmed-meshheading:7811262-... | lld:pubmed |
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| pubmed-article:7811262 | pubmed:meshHeading | pubmed-meshheading:7811262-... | lld:pubmed |
| pubmed-article:7811262 | pubmed:meshHeading | pubmed-meshheading:7811262-... | lld:pubmed |
| pubmed-article:7811262 | pubmed:meshHeading | pubmed-meshheading:7811262-... | lld:pubmed |
| pubmed-article:7811262 | pubmed:meshHeading | pubmed-meshheading:7811262-... | lld:pubmed |
| pubmed-article:7811262 | pubmed:meshHeading | pubmed-meshheading:7811262-... | lld:pubmed |
| pubmed-article:7811262 | pubmed:meshHeading | pubmed-meshheading:7811262-... | lld:pubmed |
| pubmed-article:7811262 | pubmed:meshHeading | pubmed-meshheading:7811262-... | lld:pubmed |
| pubmed-article:7811262 | pubmed:meshHeading | pubmed-meshheading:7811262-... | lld:pubmed |
| pubmed-article:7811262 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7811262 | pubmed:articleTitle | Proteolysis of A beta peptide from Alzheimer disease brain by gelatinase A. | lld:pubmed |
| pubmed-article:7811262 | pubmed:affiliation | Department of Anatomy and Cell Biology, Wayne State University School of Medicine, Detroit, MI 48201. | lld:pubmed |
| pubmed-article:7811262 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7811262 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:7811262 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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