Evidence map›Paper›PMID 38763335›Full record

ReviewThe Journal of biological chemistry2024

Post-translational control of NLRP3 inflammasome signaling.

Meghan E O'Keefe, George R Dubyak, Derek W Abbott

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Trial
  3. Mitochondria-associated programmed cell death in pancreatic β cell of T2DM.Apoptosis : an international journal on programmed cell death · 2026
    Review
  4. Molecular mechanisms of NLRP3 inflammasome activation.Experimental & molecular medicine · 2026
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Meghan E O'KeefeDepartment of Pathology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
George R DubyakDepartment of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Derek W AbbottDepartment of Pathology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA. Electronic address: dwa4@case.edu.

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007250 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI HUANG, ALEX YEE-CHEN · 1985 to 2023
$33.4M
The Cleveland Digestive Diseases Research Core Center (DDRCC)P30DK097948 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI Fabio Cominelli · 2015 to 2026
$15.6M
Molecular mechanisms of gasdermin recognition by proteases and autophagy proteins in cytokine releaseP01AI141350 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI ABBOTT, DEREK W · 2020 to 2024
$9.4M
Medical Scientist Training Program at Case Western Reserve UniversityT32GM152319 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI Heather Broihier, Alex Yee-Chen Huang · 2024 to 2026
$5.1M
Innate Immune Signal Transduction Specificity in Inflammatory DiseaseR35GM141603 · NIGMS · NATIONAL JEWISH HEALTH · PI Derek W Abbott · 2021 to 2026
$1.9M
NIAID NIH HHS P01 AI141350NIDDK NIH HHS P30 DK097948NIGMS NIH HHS R35 GM141603NIGMS NIH HHS T32 GM007250NIGMS NIH HHS T32 GM152319
6 · The paper itself

Abstract

Inflammasomes serve as critical sensors for disruptions to cellular homeostasis, with inflammasome assembly leading to inflammatory caspase activation, gasdermin cleavage, and cytokine release. While the canonical pathways leading to priming, assembly, and pyroptosis are well characterized, recent work has begun to focus on the role of post-translational modifications (PTMs) in regulating inflammasome activity. A diverse array of PTMs, including phosphorylation, ubiquitination, SUMOylation, acetylation, and glycosylation, exert both activating and inhibitory influences on members of the inflammasome cascade through effects on protein-protein interactions, stability, and localization. Dysregulation of inflammasome activation is associated with a number of inflammatory diseases, and evidence is emerging that aberrant modification of inflammasome components contributes to this dysregulation. This review provides insight into PTMs within the NLRP3 inflammasome pathway and their functional consequences on the signaling cascade and highlights outstanding questions that remain regarding the complex web of signals at play.

Indexed as

InflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinProtein Processing, Post-TranslationalSignal TransductionAcetylationAnimalsHumansInflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinNLRP3 protein, humancell deathinflammasomeNLRP3post-translational modification (PTM)signaling

Identifiers

PMID38763335
PMCPMC11245928

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.