pubmed-article:17439641 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17439641 | lifeskim:mentions | umls-concept:C0042567 | lld:lifeskim |
pubmed-article:17439641 | lifeskim:mentions | umls-concept:C0043457 | lld:lifeskim |
pubmed-article:17439641 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
pubmed-article:17439641 | lifeskim:mentions | umls-concept:C0015219 | lld:lifeskim |
pubmed-article:17439641 | lifeskim:mentions | umls-concept:C0008807 | lld:lifeskim |
pubmed-article:17439641 | pubmed:dateCreated | 2007-5-11 | lld:pubmed |
pubmed-article:17439641 | pubmed:abstractText | The metzincins are a large gene superfamily of proteases characterized by the presence of a zinc protease domain, and include the ADAM, ADAMTS, BMP1/TLL, meprin and MMP genes. Metzincins are involved in the proteolysis of a wide variety of proteins, including those of the extracellular matrix. The metzincin gene superfamily comprises eighty proteins in the human genome and ninety-three in the mouse. When and how the level of complexity apparent in the vertebrate metzincin gene superfamily arose has not been determined in detail. Here we present a comprehensive analysis of vertebrate metzincins using genes from both Ciona intestinalis and Danio rerio to provide new insights into the complex evolution of this gene superfamily. | lld:pubmed |
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pubmed-article:17439641 | pubmed:language | eng | lld:pubmed |
pubmed-article:17439641 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17439641 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17439641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17439641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17439641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17439641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17439641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17439641 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17439641 | pubmed:issn | 1471-2148 | lld:pubmed |
pubmed-article:17439641 | pubmed:author | pubmed-author:BeckChristine... | lld:pubmed |
pubmed-article:17439641 | pubmed:author | pubmed-author:RobertsonDavi... | lld:pubmed |
pubmed-article:17439641 | pubmed:author | pubmed-author:Boot-Handford... | lld:pubmed |
pubmed-article:17439641 | pubmed:author | pubmed-author:Huxley-JonesJ... | lld:pubmed |
pubmed-article:17439641 | pubmed:author | pubmed-author:ClarkeToni-Ki... | lld:pubmed |
pubmed-article:17439641 | pubmed:author | pubmed-author:ToubarisGeorg... | lld:pubmed |
pubmed-article:17439641 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:17439641 | pubmed:volume | 7 | lld:pubmed |
pubmed-article:17439641 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17439641 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17439641 | pubmed:pagination | 63 | lld:pubmed |
pubmed-article:17439641 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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