| pubmed-article:19657145 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19657145 | lifeskim:mentions | umls-concept:C0009325 | lld:lifeskim |
| pubmed-article:19657145 | lifeskim:mentions | umls-concept:C0019143 | lld:lifeskim |
| pubmed-article:19657145 | lifeskim:mentions | umls-concept:C0668727 | lld:lifeskim |
| pubmed-article:19657145 | lifeskim:mentions | umls-concept:C0009647 | lld:lifeskim |
| pubmed-article:19657145 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:19657145 | lifeskim:mentions | umls-concept:C1539327 | lld:lifeskim |
| pubmed-article:19657145 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:19657145 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:19657145 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:19657145 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
| pubmed-article:19657145 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:19657145 | pubmed:issue | 40 | lld:pubmed |
| pubmed-article:19657145 | pubmed:dateCreated | 2009-10-5 | lld:pubmed |
| pubmed-article:19657145 | pubmed:abstractText | Mutations in the TNF family ligand EDA1 cause X-linked hypohidrotic ectodermal dysplasia (XLHED), a condition characterized by defective development of skin appendages. The EDA1 protein displays a proteolytic processing site responsible for its conversion to a soluble form, a collagen domain, and a trimeric TNF homology domain (THD) that binds the receptor EDAR. In-frame deletions in the collagen domain reduced the thermal stability of EDA1. Removal of the collagen domain decreased its activity about 100-fold, as measured with natural and engineered EDA1-responsive cell lines. The collagen domain could be functionally replaced by multimerization domains or by cross-linking antibodies, suggesting that it functions as an oligomerization unit. Surprisingly, mature soluble EDA1 containing the collagen domain was poorly active when administered in newborn, EDA-deficient (Tabby) mice. This was due to a short stretch of basic amino acids located at the N terminus of the collagen domain that confers EDA1 with proteoglycan binding ability. In contrast to wild-type EDA1, EDA1 with mutations in this basic sequence was a potent inducer of tail hair development in vivo. Thus, the collagen domain activates EDA1 by multimerization, whereas the proteoglycan-binding domain may restrict the distribution of endogeneous EDA1 in vivo. | lld:pubmed |
| pubmed-article:19657145 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19657145 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19657145 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19657145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19657145 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19657145 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19657145 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:19657145 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:19657145 | pubmed:author | pubmed-author:SchneiderPasc... | lld:pubmed |
| pubmed-article:19657145 | pubmed:author | pubmed-author:MikkolaMarjaM | lld:pubmed |
| pubmed-article:19657145 | pubmed:author | pubmed-author:DemotzStéphan... | lld:pubmed |
| pubmed-article:19657145 | pubmed:author | pubmed-author:GaideOlivierO | lld:pubmed |
| pubmed-article:19657145 | pubmed:author | pubmed-author:TardivelAubry... | lld:pubmed |
| pubmed-article:19657145 | pubmed:author | pubmed-author:FavreManuelM | lld:pubmed |
| pubmed-article:19657145 | pubmed:author | pubmed-author:SweeLee KimLK | lld:pubmed |
| pubmed-article:19657145 | pubmed:author | pubmed-author:WillenLaureL | lld:pubmed |
| pubmed-article:19657145 | pubmed:author | pubmed-author:Ingold-Salami... | lld:pubmed |
| pubmed-article:19657145 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19657145 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:19657145 | pubmed:volume | 284 | lld:pubmed |
| pubmed-article:19657145 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19657145 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19657145 | pubmed:pagination | 27567-76 | lld:pubmed |
| pubmed-article:19657145 | pubmed:dateRevised | 2010-10-5 | lld:pubmed |
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| pubmed-article:19657145 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19657145 | pubmed:articleTitle | Biological activity of ectodysplasin A is conditioned by its collagen and heparan sulfate proteoglycan-binding domains. | lld:pubmed |
| pubmed-article:19657145 | pubmed:affiliation | Department of Biochemistry, University of Lausanne, CH-1066 Epalinges, Switzerland. | lld:pubmed |
| pubmed-article:19657145 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19657145 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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