About: Self-association of the Death Domains of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects

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About: Self-association of the Death Domains of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects Goto Sponge NotDistinct Permalink

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scientific article published in Journal of Biological Chemistry

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1995 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Januar 1995 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q59707705-257569A6-8678-49E8-9659-D6F80F185A8B
publication date	1995-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59707705-F075B1C6-1A44-4B20-A90E-85730203D39B
language of work or name	English
cites work	wds:Q59707705-74F8AE6F-D687-419A-B373-73B896A67903
cites work	Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
author name string	wds:Q59707705-13214E8B-4E2B-4C82-88C0-1177E1AEBF59 wds:Q59707705-4B6D74F1-C352-4589-BFE4-21764253CE99 wds:Q59707705-575FC7F2-1167-49DC-BBD6-7C9087A3EE78 wds:Q59707705-5DF6001B-9A9E-4EE3-B28F-9E5D07B6D6D8 wds:Q59707705-9E0FDC96-C74D-45BD-BCAE-B4546EBCDFD3 wds:Q59707705-F22A101B-867B-4A3D-8D1B-42685D3308C1
author name string	D Wallach E E Varfolomeev I L Mett J H Camonis I Chumakov Y Shemer-Avni
rdfs:label	Self-association of the Death Domains of the p55 Tumor Necrosis Factor (nl) Self-association of the Death Domains of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects (en)
skos:prefLabel	Self-association of the Death Domains of the p55 Tumor Necrosis Factor (nl) Self-association of the Death Domains of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects (en)
name	Self-association of the Death Domains of the p55 Tumor Necrosis Factor (nl) Self-association of the Death Domains of the p55 Tumor Necrosis Factor (TNF) Receptor and Fas/APO1 Prompts Signaling for TNF and Fas/APO1 Effects (en)
author	wds:Q59707705-C812DEF4-EC03-407B-8312-38D2893658B7
author	Mark P. Boldin
title	wds:Q59707705-D5A810A1-8838-4605-A2EF-BE4941238AD7
title	Self-association of the "death domains" of the p55 tumor necrosis factor (TNF) receptor and Fas/APO1 prompts signaling for TNF and Fas/APO1 effects (en)
page(s)	wds:Q59707705-BF1CD367-210A-44BD-B894-FDBE8AC442EC
page(s)	387-391
instance of	wds:Q59707705-EE641720-7F47-488C-907F-34E1A232AF53
instance of	scholarly article
main subject	wds:Q59707705-9983094D-B81C-44D3-8117-6B8D28A6FBBB
main subject	wd:Q18032037
PubMed ID	wds:Q59707705-3F822141-4D0A-457B-9735-37AD58A0E59C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7529234
PubMed ID	7529234
published in	wds:Q59707705-15BCB5D4-275B-40AB-97A2-8C86BEA89A59
published in	Journal of Biological Chemistry
issue	wds:Q59707705-6BECB019-62CB-4E9F-86E1-D6361CBA076B
volume	wds:Q59707705-8679B408-80DB-463D-9CC6-39FA8315D768
issue	1
volume	270
DOI	wds:Q59707705-F865F3F0-CCC9-43F0-9454-AAB8D71E593D
DOI	http://dx.doi.org/10.1074/JBC.270.1.387
DOI	10.1074/JBC.270.1.387
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59707705
is cites work of	TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways The cell-death machine Involvement of two NF-kappa B binding elements in tumor necrosis factor alpha -, CD40-, and epstein-barr virus latent membrane protein 1-mediated induction of the cellular inhibitor of apoptosis protein 2 gene Deletion of tumor necrosis factor death receptor inhibits amyloid beta generation and prevents learning and memory deficits in Alzheimer's mice Characterization of reaper- and FADD-induced apoptosis in a lepidopteran cell line PLAIDD, a type II death domain protein that interacts with p75 neurotrophin receptor An MMP-2/MMP-9 inhibitor, 5a, enhances apoptosis induced by ligands of the TNF receptor superfamily in cancer cells Lentiviral expression of HIV-1 Vpr induces apoptosis in human neurons Daxx, a novel Fas-binding protein that activates JNK and apoptosis Cell death induction by receptors of the TNF family: towards a molecular understanding. Human immunodeficiency virus type 1 Vpr induces apoptosis in human neuronal cells Involvement of FAN in TNF-induced apoptosis Apo-3, a new member of the tumor necrosis factor receptor family, contains a death domain and activates apoptosis and NF-kappa B TRAMP, a novel apoptosis-mediating receptor with sequence homology to tumor necrosis factor receptor 1 and Fas(Apo-1/CD95) Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation TRAF-interacting protein (TRIP): a novel component of the tumor necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits TRAF2-mediated NF-kappaB activation Lymphotoxin-beta receptor signaling complex: role of tumor necrosis factor receptor-associated factor 3 recruitment in cell death and activation of nuclear factor kappaB The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-kappaB activation The cytoplasmic domain of the lymphotoxin-beta receptor mediates cell death in HeLa cells A death-domain-containing receptor that mediates apoptosis Induction of cell death by tumour necrosis factor (TNF) receptor 2, CD40 and CD30: a role for TNF-R1 activation by endogenous membrane-anchored TNF. Lipopolysaccharide induces disseminated endothelial apoptosis requiring ceramide generation A Fas-associated protein factor, FAF1, potentiates Fas-mediated apoptosis The molecular biology of apoptosis A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor Targeting death and decoy receptors of the tumour-necrosis factor superfamily Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012 Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor. Structures of the extracellular domain of the type I tumor necrosis factor receptor Dissecting Fas signaling with an altered-specificity death-domain mutant: requirement of FADD binding for apoptosis but not Jun N-terminal kinase activation FLICE-inhibitory protein is a key regulator of germinal center B cell apoptosis MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase A critical role of the p75 tumor necrosis factor receptor (p75TNF-R) in organ inflammation independent of TNF, lymphotoxin alpha, or the p55TNF-R. HIV-1 kills renal tubular epithelial cells in vitro by triggering an apoptotic pathway involving caspase activation and Fas upregulation Apoptosis and molecular targeting therapy in cancer Intracellular mediators of erucylphosphocholine-induced apoptosis Altered death receptor signaling promotes epithelial-to-mesenchymal transition and acquired chemoresistance. Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis Casper is a FADD- and caspase-related inducer of apoptosis Transgenic mice expressing the intracellular domain of the p75 neurotrophin receptor undergo neuronal apoptosis. Serum concentrations of markers of TNFalpha and Fas-mediated pathways and renal function in nonproteinuric patients with type 1 diabetes. A potential mechanism of "cross-talk" between the p55 tumor necrosis factor receptor and Fas/APO1: proteins binding to the death domains of the two receptors also bind to each other Two tumour necrosis factor receptors: structure and function.

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