Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2006-7-17
pubmed:databankReference
pubmed:abstractText
Death receptors (DRs) induce intracellular signalling upon engagement of their cognate ligands, leading to apoptosis, cell survival or pro-inflammatory responses. In mammals, DR signalling is mediated by the recruitment of several DD (death domain)-containing molecules, such as FADD (Fas-associated DD) and RIP1 (receptor-interacting protein 1).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/CASP8 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Caspase 8, http://linkedlifedata.com/resource/pubmed/chemical/Caspases, http://linkedlifedata.com/resource/pubmed/chemical/FADD protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Fas-Associated Death Domain Protein, http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase Kinases, http://linkedlifedata.com/resource/pubmed/chemical/MAP kinase kinase kinase 7, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 8, http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B, http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/RIPK1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Receptor-Interacting Protein..., http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/TNF Receptor-Associated Factor 2, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor AP-1, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor..., http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins, http://linkedlifedata.com/resource/pubmed/chemical/death receptor M1, Xenopus, http://linkedlifedata.com/resource/pubmed/chemical/death receptor M2, Xenopus
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0248-4900
pubmed:author
pubmed:issnType
Print
pubmed:volume
98
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
465-78
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed-meshheading:16597320-Adaptor Proteins, Signal Transducing, pubmed-meshheading:16597320-Animals, pubmed-meshheading:16597320-Binding Sites, pubmed-meshheading:16597320-Caspase 8, pubmed-meshheading:16597320-Caspases, pubmed-meshheading:16597320-Cell Line, pubmed-meshheading:16597320-Fas-Associated Death Domain Protein, pubmed-meshheading:16597320-Gene Expression, pubmed-meshheading:16597320-Humans, pubmed-meshheading:16597320-MAP Kinase Kinase Kinases, pubmed-meshheading:16597320-Mitogen-Activated Protein Kinase 8, pubmed-meshheading:16597320-Molecular Sequence Data, pubmed-meshheading:16597320-NF-kappa B, pubmed-meshheading:16597320-Protein Binding, pubmed-meshheading:16597320-Protein Isoforms, pubmed-meshheading:16597320-Protein-Serine-Threonine Kinases, pubmed-meshheading:16597320-Receptor-Interacting Protein Serine-Threonine Kinases, pubmed-meshheading:16597320-Receptors, Cell Surface, pubmed-meshheading:16597320-Sequence Homology, Amino Acid, pubmed-meshheading:16597320-TNF Receptor-Associated Factor 2, pubmed-meshheading:16597320-Transcription Factor AP-1, pubmed-meshheading:16597320-Transfection, pubmed-meshheading:16597320-Tumor Necrosis Factor Receptor-Associated Peptides and..., pubmed-meshheading:16597320-Xenopus Proteins, pubmed-meshheading:16597320-Xenopus laevis
pubmed:year
2006
pubmed:articleTitle
Xenopus death-domain-containing proteins FADD and RIP1 synergistically activate JNK and NF-kappaB.
pubmed:affiliation
Department of Bioscience, School of Science, Kitasato University, 1-15-1 Kitasato, Sagamihara 228-8555, Japan.
pubmed:publicationType
Journal Article