ArticleCell death discovery2025
RIPK1 S213E mutant suppresses RIPK1-dependent cell death by preventing interactions with RIPK3 and CASP8.
Article in Cell death discovery, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed.
- Solution NMR reveals micelle-stabilized α-helical segments flanking the RIPK1 RHIM amyloid core.Biochemical and biophysical research communications · 2026Article
- Precision tumor targeting: gamma-irradiated ellagic acid therapy for ferroptosis and necroptosis modulation via GPX4/ALOX/RIPK/MLKL pathway inhibition.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Activation of RIPK3 drives PANoptosis in human cells and inflammatory apoptosis in canine cells dependent on RIPK1, FADD and caspases.Apoptosis : an international journal on programmed cell death · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
RIPK1 (Receptor-interacting serine/threonine-protein kinase 1) is fundamental in regulating cell proliferation, programmed cell death, and inflammation. Within the TNF (tumor necrosis factor) signaling pathway, the kinase activity of RIPK1 is essential for determining cellular fate, promoting either apoptosis or necroptosis. Mutations disrupting RIPK1 kinase activity significantly impact cellular fate decisions, highlighting its importance in the TNF signaling cascade. This study generated and characterized a novel mutation of human RIPK1, S213E that exhibits unique inhibitory properties. Although located in the kinase domain, the S213E mutation disrupts RIPK1 homodimerization and its interactions with downstream effectors, such as RIPK3, without directly suppressing RIPK1 kinase activity. These findings indicate that the S213E mutation converts RIPK1 into a super-autoinhibitory state, effectively isolating it from downstream effectors involved in both apoptosis and necroptosis.
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.