Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-3-31
pubmed:databankReference
pubmed:abstractText
A novel member of the tumor necrosis factor (TNF) receptor family, designated TRAMP, has been identified. The structural organization of the 393 amino acid long human TRAMP is most homologous to TNF receptor 1. TRAMP is abundantly expressed on thymocytes and lymphocytes. Its extracellular domain is composed of four cysteine-rich domains, and the cytoplasmic region contains a death domain known to signal apoptosis. Overexpression of TRAMP leads to two major responses, NF-kappaB activation and apoptosis. TRAMP-induced cell death is inhibited by an inhibitor of ICE-like proteases, but not by Bcl-2. In addition, TRAMP does not appear to interact with any of the known apoptosis-inducing ligands of the TNF family.
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/Apoptosis Regulatory Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/FADD protein, human, http://linkedlifedata.com/resource/pubmed/chemical/FASLG protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Fas Ligand Protein, http://linkedlifedata.com/resource/pubmed/chemical/Fas-Associated Death Domain Protein, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor..., http://linkedlifedata.com/resource/pubmed/chemical/TNF-Related Apoptosis-Inducing..., http://linkedlifedata.com/resource/pubmed/chemical/TNFRSF25 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/TNFSF10 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1074-7613
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
79-88
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9052839-Adaptor Proteins, Signal Transducing, pubmed-meshheading:9052839-Amino Acid Sequence, pubmed-meshheading:9052839-Apoptosis, pubmed-meshheading:9052839-Apoptosis Regulatory Proteins, pubmed-meshheading:9052839-Carrier Proteins, pubmed-meshheading:9052839-Chromosomes, Human, Pair 1, pubmed-meshheading:9052839-Cytoplasm, pubmed-meshheading:9052839-Fas Ligand Protein, pubmed-meshheading:9052839-Fas-Associated Death Domain Protein, pubmed-meshheading:9052839-Gene Expression, pubmed-meshheading:9052839-Humans, pubmed-meshheading:9052839-Ligands, pubmed-meshheading:9052839-Lymphocytes, pubmed-meshheading:9052839-Membrane Glycoproteins, pubmed-meshheading:9052839-Molecular Sequence Data, pubmed-meshheading:9052839-Multigene Family, pubmed-meshheading:9052839-NF-kappa B, pubmed-meshheading:9052839-RNA, Messenger, pubmed-meshheading:9052839-Receptors, Cell Surface, pubmed-meshheading:9052839-Receptors, Tumor Necrosis Factor, pubmed-meshheading:9052839-Receptors, Tumor Necrosis Factor, Member 25, pubmed-meshheading:9052839-Sequence Alignment, pubmed-meshheading:9052839-Sequence Homology, Amino Acid, pubmed-meshheading:9052839-Signal Transduction, pubmed-meshheading:9052839-TNF-Related Apoptosis-Inducing Ligand, pubmed-meshheading:9052839-Tumor Necrosis Factor-alpha
pubmed:year
1997
pubmed:articleTitle
TRAMP, a novel apoptosis-mediating receptor with sequence homology to tumor necrosis factor receptor 1 and Fas(Apo-1/CD95).
pubmed:affiliation
Institute of Biochemistry, University of Lausanne, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't