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ProteomicsProteomic analysis of TRAIL-induced endogenous RIPK3-dependent necrosome complex
Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) is a well-known inducer of apoptosis via formation of the primary death-inducing signaling complex (TRAIL-DISC) at the level of membrane death receptors (DR4 and DR5) which recruit successively FADD and caspase-8. TRAIL can also induce ...
ORGANISM(S): Colon Homo sapiens (Human) 
2021-03-18 | PXD003383 | Pride
Ripk3-dependent necrosome  disc  mass spectrometry  trail  trim21 
ProteomicsStoichiometric organisation of necrosome
The necrosome is a key macromolecular platform that initiates the RIPK1/RIPK3-dependent programme of cell death, termed necroptosis. Necroptosis plays an important role in controlling inflammation and cell death in multicellular organisms. Here, we used quantitative mass spectrometry to decipher the...
ORGANISM(S): Homo sapiens (Human) 
2025-03-06 | PXD059873 | Pride
Stoichiometry Necrosome Aqua 
UnknownTriad3a induces the degradation of early necrosome to limit RipK1-dependent cytokine production and necroptosis.
Not available
S-EPMC5964080 | biostudies-literature
UnknownOligomerised RIPK1 is the main core component of the CD95 necrosome.
Not available
S-EPMC12130296 | biostudies-literature
UnknownDepletion of RIPK3 or MLKL blocks TNF-driven necroptosis and switches towards a delayed RIPK1 kinase-dependent apoptosis.
Not available
S-EPMC4040672 | biostudies-literature
UnknownCombination simvastatin and metformin induces G1-phase cell cycle arrest and Ripk1- and Ripk3-dependent necrosis in C4-2B osseous metastatic castration-resistant prostate cancer cells.
Not available
S-EPMC4260755 | biostudies-literature
UnknownOligomerised RIPK1 is the main core component of the CD95 necrosome
Not available
S-SCDT-10_1038-S44318-025-00433-0 | biostudies-other
UnknownTRAF2 is a biologically important necroptosis suppressor.
Not available
S-EPMC4648330 | biostudies-literature
ProteomicsUSP22 controls necroptosis by regulating receptor interacting protein kinase 3 ubiquitination
Dynamic control of ubiquitination by deubiquitinating enzymes is essential for almost all biological processes. Ubiquitin-specific peptidase 22 (USP22) is part of the SAGA complex and catalyzes the removal of monoubiquitination from histone H2B, thereby regulating gene transcription. However, novel ...
ORGANISM(S): Homo sapiens (Human) 
2021-05-03 | PXD020909 | Pride
Cancer/mlkl/posttranslational modifications/ripk1/ubiquitin hydrolase 
UnknownPRMT5-mediated regulatory arginine methylation of RIPK3.
Not available
S-EPMC9852244 | biostudies-literature
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