Topic
TRAF2
About: TRAF2 is a research topic. Over the lifetime, 372 publications have been published within this topic receiving 47468 citations. The topic is also known as: MGC:45012 & TRAP.
Papers published on a yearly basis
Papers
TL;DR: Tumor necrosis factor alpha binding to the TNF receptor (TNFR) potentially initiates apoptosis and activates the transcription factor nuclear factor kappa B (NF-kappaB), which suppresses apoptosis by an unknown mechanism.
Abstract: Tumor necrosis factor alpha (TNF-alpha) binding to the TNF receptor (TNFR) potentially initiates apoptosis and activates the transcription factor nuclear factor kappa B (NF-kappaB), which suppresses apoptosis by an unknown mechanism. The activation of NF-kappaB was found to block the activation of caspase-8. TRAF1 (TNFR-associated factor 1), TRAF2, and the inhibitor-of-apoptosis (IAP) proteins c-IAP1 and c-IAP2 were identified as gene targets of NF-kappaB transcriptional activity. In cells in which NF-kappaB was inactive, all of these proteins were required to fully suppress TNF-induced apoptosis, whereas c-IAP1 and c-IAP2 were sufficient to suppress etoposide-induced apoptosis. Thus, NF-kappaB activates a group of gene products that function cooperatively at the earliest checkpoint to suppress TNF-alpha-mediated apoptosis and that function more distally to suppress genotoxic agent-mediated apoptosis.
2,846 citations
TL;DR: This work investigated how TNFR1 activates different effector functions; the protein kinase JNK, transcription factor NF-kappaB, and apoptosis, finding that the three responses are mediated through separate pathways.
2,040 citations
TL;DR: The discovery of a novel 34 kDa protein, designated TRADD, that specifically interacts with an intracellular domain of TNFR1 known to be essential for mediating programmed cell death shows that the signaling pathways for TNF-induced cell death and NF-κB activation are distinct.
2,031 citations
TL;DR: The biochemical purification and subsequent molecular cloning of two novel TNFR2-associated proteins, designated c-IAP1 and c- IAP2, that are closely related mammalian members of the inhibitor of apoptosis protein (IAP) family originally identified in baculoviruses are reported.
1,375 citations
TL;DR: It is shown that TRADD interacts strongly with RIP, another death domain protein that was shown previously to associate with Fas antigen, and is a serine-threonine kinase that is recruited by TRADD to TNFR1 in a TNF-dependent process.
1,233 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2025 | 6 |
| 2024 | 15 |
| 2023 | 24 |
| 2022 | 28 |
| 2021 | 11 |
| 2020 | 4 |