The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Prevention of Constitutive TNF Receptor 1 Signaling by Silencer of Death Domains
Abstract
Tumor necrosis factor receptor type 1 (TNF-R1) contains a cytoplasmic death domain that is required for the signaling of TNF activities such as apoptosis and nuclear factor kappa B (NF-κB) activation. Normally, these signals are generated only after TNF-induced receptor aggregation. However, TNF-R1 self-associates and signals independently of ligand when overexpressed. This apparent paradox may be explained by silencer of death domains (SODD), a widely expressed ∼60-kilodalton protein that was found to be associated with the death domain of TNF-R1. TNF treatment released SODD from TNF-R1, permitting the recruitment of proteins such as TRADD and TRAF2 to the active TNF-R1 signaling complex. SODD also interacted with death receptor–3 (DR3), another member of the TNF receptor superfamily. Thus, SODD association may be representative of a general mechanism for preventing spontaneous signaling by death domain–containing receptors.
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Cited by
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IAP proteins: blocking the road to death's door
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Metadata
- Authors
- Jiang, Y., Woronicz, J. D., Liu, W., & Goeddel, D. V.
- Venue
- Science
- Published
- 1999-01-22
- Volume
- 283
- Issue
- 5401
- Pages
- 543-546
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2071055800
- Cited by
- 417
- References
- 16
- FWCI
- 17.71
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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