ReviewAdvances in experimental medicine and biology2024
Regulation of the Inflammasome Activation by Ubiquitination Machinery.
Review in Advances in experimental medicine and biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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Who cites it
5 citing papers in PubMed.
- TRIM21 facilitates inflammasome assembly and contributes to autoinflammatory disease.Nature communications · 2026Article
- The Crohn's disease-related RNF123 prevents NLRP3 inflammasome assembly by catalyzing unanchored K63-linked ubiquitination on NEK7.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Gut microbiota and NLRP3 inflammasome activation in hemodialysis patients: exploring the link with systemic inflammation.Molecular biology reports · 2025Article
- Macrophage pyroptosis and its crucial role in ALI/ARDS.Frontiers in immunology · 2025Review
- Targeting inflammasome pathway towards therapeutics of neurodegenerative diseases.Organelle (Tucson, Ariz.) · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Inflammasomes are multiprotein complexes that assemble in response to the detection of stress- or infection-associated stimuli and lead to the activation of caspase-1 and consequent maturation of caspase-1 target molecules such as interleukin (IL)-1β and IL-18. Although inflammasome is the essential component of the innate immunity system to defense against insults, inappropriate or prolonged activation of inflammasome may be harmful and is associated with various diseases, e.g., gout, atherosclerosis, diabetes, and Alzheimer's disease. Therefore, regulating inflammasome activation is crucial for maintaining immune homeostasis. Studies have found that post-translational modifications (PTMs), e.g., ubiquitination and phosphorylation, are critical for inflammasome activation. Ubiquitination is an important form of post-translational modification of proteins that plays a pivotal role in various cellular functions. In recent years, its function in regulating inflammasome assembly has been a hot topic of interest. This study discussed the function and mechanism of the ubiquitin system controlling inflammasome activation and highlighted the challenges of this research area.
Indexed as
Identifiers
39546140What OpenQuestion 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 OpenQuestion graph.