| pubmed-article:16762833 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16762833 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:16762833 | lifeskim:mentions | umls-concept:C1333530 | lld:lifeskim |
| pubmed-article:16762833 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16762833 | lifeskim:mentions | umls-concept:C1513371 | lld:lifeskim |
| pubmed-article:16762833 | lifeskim:mentions | umls-concept:C0913626 | lld:lifeskim |
| pubmed-article:16762833 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:16762833 | pubmed:dateCreated | 2006-6-9 | lld:pubmed |
| pubmed-article:16762833 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16762833 | pubmed:abstractText | The structure of FADD has been solved in solution, revealing that the death effector domain (DED) and death domain (DD) are aligned with one another in an orthogonal, tail-to-tail fashion. Mutagenesis of FADD and functional reconstitution with its binding partners define the interaction with the intracellular domain of CD95 and the prodomain of procaspase-8 and reveal a self-association surface necessary to form a productive complex with an activated "death receptor." The identification of a procaspase-specific binding surface on the FADD DED suggests a preferential interaction with one, but not both, of the DEDs of procaspase-8 in a perpendicular arrangement. FADD self-association is mediated by a "hydrophobic patch" in the vicinity of F25 in the DED. The structure of FADD and its functional characterization, therefore, illustrate the architecture of key components in the death-inducing signaling complex. | lld:pubmed |
| pubmed-article:16762833 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16762833 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16762833 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16762833 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16762833 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:16762833 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:16762833 | pubmed:author | pubmed-author:QiY FYF | lld:pubmed |
| pubmed-article:16762833 | pubmed:author | pubmed-author:SanduCristine... | lld:pubmed |
| pubmed-article:16762833 | pubmed:author | pubmed-author:HillJustine... | lld:pubmed |
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| pubmed-article:16762833 | pubmed:author | pubmed-author:WeiYufengY | lld:pubmed |
| pubmed-article:16762833 | pubmed:author | pubmed-author:WernerMilton... | lld:pubmed |
| pubmed-article:16762833 | pubmed:author | pubmed-author:MorisawaGakuG | lld:pubmed |
| pubmed-article:16762833 | pubmed:author | pubmed-author:HuangTedT | lld:pubmed |
| pubmed-article:16762833 | pubmed:author | pubmed-author:GavathiotisEv... | lld:pubmed |
| pubmed-article:16762833 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16762833 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:16762833 | pubmed:volume | 22 | lld:pubmed |
| pubmed-article:16762833 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16762833 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16762833 | pubmed:pagination | 599-610 | lld:pubmed |
| pubmed-article:16762833 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:16762833 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16762833 | pubmed:articleTitle | The structure of FADD and its mode of interaction with procaspase-8. | lld:pubmed |
| pubmed-article:16762833 | pubmed:affiliation | Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, Box 42, New York, New York 10021, USA. | lld:pubmed |
| pubmed-article:16762833 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16762833 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16762833 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16762833 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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