| pubmed-article:9582077 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9582077 | lifeskim:mentions | umls-concept:C0079866 | lld:lifeskim |
| pubmed-article:9582077 | lifeskim:mentions | umls-concept:C1333530 | lld:lifeskim |
| pubmed-article:9582077 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9582077 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:9582077 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:9582077 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9582077 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:9582077 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:9582077 | pubmed:issue | 6679 | lld:pubmed |
| pubmed-article:9582077 | pubmed:dateCreated | 1998-5-18 | lld:pubmed |
| pubmed-article:9582077 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582077 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582077 | pubmed:abstractText | When activated, membrane-bound receptors for Fas and tumour-necrosis factor initiate programmed cell death by recruiting the death domain of the adaptor protein FADD to the membrane. FADD then activates caspase 8 (also known as FLICE or MACH) through an interaction between the death-effector domains of FADD and caspase 8. This ultimately leads to the apoptotic response. Death-effector domains and homologous protein modules known as caspase-recruitment domains have been found in several proteins and are important regulators of caspase (FLICE) activity and of apoptosis. Here we describe the solution structure of a soluble, biologically active mutant of the FADD death-effector domain. The structure consists of six antiparallel, amphipathic alpha-helices and resembles the overall fold of the death domains of Fas and p75. Despite this structural similarity, mutations that inhibit protein-protein interactions involving the Fas death domain have no effect when introduced into the FADD death-effector domain. Instead, a hydrophobic region of the FADD death-effector domain that is not present in the death domains is vital for binding to FLICE and for apoptotic activity. | lld:pubmed |
| pubmed-article:9582077 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9582077 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582077 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9582077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9582077 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9582077 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9582077 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:9582077 | pubmed:author | pubmed-author:ChefRR | lld:pubmed |
| pubmed-article:9582077 | pubmed:author | pubmed-author:HuangBB | lld:pubmed |
| pubmed-article:9582077 | pubmed:author | pubmed-author:NgS CSC | lld:pubmed |
| pubmed-article:9582077 | pubmed:author | pubmed-author:FesikS WSW | lld:pubmed |
| pubmed-article:9582077 | pubmed:author | pubmed-author:ZhengLL | lld:pubmed |
| pubmed-article:9582077 | pubmed:author | pubmed-author:LenardoM JMJ | lld:pubmed |
| pubmed-article:9582077 | pubmed:author | pubmed-author:MeadowsR PRP | lld:pubmed |
| pubmed-article:9582077 | pubmed:author | pubmed-author:EberstadtMM | lld:pubmed |
| pubmed-article:9582077 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9582077 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:9582077 | pubmed:volume | 392 | lld:pubmed |
| pubmed-article:9582077 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9582077 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9582077 | pubmed:pagination | 941-5 | lld:pubmed |
| pubmed-article:9582077 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:meshHeading | pubmed-meshheading:9582077-... | lld:pubmed |
| pubmed-article:9582077 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9582077 | pubmed:articleTitle | NMR structure and mutagenesis of the FADD (Mort1) death-effector domain. | lld:pubmed |
| pubmed-article:9582077 | pubmed:affiliation | Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Illinois 60064, USA. | lld:pubmed |
| pubmed-article:9582077 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9582077 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9582077 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:9582077 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:8772 | entrezgene:pubmed | pubmed-article:9582077 | lld:entrezgene |
| family:PF01335.16 | family:pubmed | pubmed-article:9582077 | lld:pfam |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9582077 | lld:pubmed |
