ReviewCell death & disease2015
DED or alive: assembly and regulation of the death effector domain complexes.
Review in Cell death & disease, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed, 57 citations in OpenAlex.
- Synthetic Toll-Like Receptors for Control of Innate Immunity With Far-Red Light.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Mechanism and role of regulated cell death in tumor immunity and immunotherapy.Cancer communications (London, England) · 2025Review
- Caspases: structural and molecular mechanisms and functions in cell death, innate immunity, and disease.Cell discovery · 2025Review
- Cell death in glioblastoma and the central nervous system.Cellular oncology (Dordrecht, Netherlands) · 2025Review
- Fungal Als proteins hijack host death effector domains to promote inflammasome signaling.Nature communications · 2025Article
- cFLIP - An interacting partner and a novel substrate for pro-apoptotic serine protease HtrA2.Biochemistry and biophysics reports · 2024Article
- Apoptosis dysfunction: unravelling the interplay between ZBP1 activation and viral invasion in innate immune responses.Cell communication and signaling : CCS · 2024Review
- The Identification of New c-FLIP Inhibitors for Restoring Apoptosis in TRAIL-Resistant Cancer Cells.Current issues in molecular biology · 2024Article
- Sequential Unfolding Mechanisms of Monomeric Caspases.Biochemistry · 2023Article
- When cell death goes wrong: inflammatory outcomes of failed apoptosis and mitotic cell death.Cell death and differentiation · 2023Review
- Sequential unfolding mechanisms of monomeric caspases.bioRxiv : the preprint server for biology · 2023Article
- TIAMMAt: Leveraging Biodiversity to Revise Protein Domain Models, Evidence from Innate Immunity.Molecular biology and evolution · 2021Article
- The stressosome, a caspase-8-activating signalling complex assembled in response to cell stress in an ATG5-mediated manner.Journal of cellular and molecular medicine · 2021Article
- Caspase-8 mutations associated with head and neck cancer differentially retain functional properties related to TRAIL-induced apoptosis and cytokine induction.Cell death & disease · 2021Article
- Reconstruction of the Fas-Based Death-Inducing Signaling Complex (DISC) Using a Protein-Protein Docking Meta-Approach.Journal of chemical information and modeling · 2021Article
- Dying to Survive-The p53 Paradox.Cancers · 2021Review
- Cryo-EM structural analysis of FADD:Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate.Nature communications · 2021Article
- Article
- The pseudo-caspase FLIP(L) regulates cell fate following p53 activation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Molecular basis of dimerization of initiator caspase was revealed by crystal structure of caspase-8 pro-domain.Cell death and differentiation · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Death effector domains (DEDs) are protein-protein interaction domains initially identified in proteins such as FADD, FLIP and caspase-8 involved in regulating apoptosis. Subsequently, these proteins have been shown to have important roles in regulating other forms of cell death, including necroptosis, and in regulating other important cellular processes, including autophagy and inflammation. Moreover, these proteins also have prominent roles in innate and adaptive immunity and during embryonic development. In this article, we review the various roles of DED-containing proteins and discuss recent developments in our understanding of DED complex formation and regulation. We also briefly discuss opportunities to therapeutically target DED complex formation in diseases such as cancer.
Indexed as
Identifiers
What Socratic holds
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 Socratic graph.