Evidence map›Paper›PMID 31121538›Full record

ReviewCurrent opinion in immunology2019

The NLRP1 inflammasome: new mechanistic insights and unresolved mysteries.

Patrick S Mitchell, Andrew Sandstrom, Russell E Vance

Abstract readReview
In one paragraph

Review in Current opinion in immunology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
128citing 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

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

  1. Pooled it
  2. Article
  3. Review
  4. Microbiology spectrum · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Mast Cells Are a Reservoir of NLRP1 in Human Skin.International journal of molecular sciences · 2026
    Article
  9. NLRP1B is an integrated decoy that subvertsProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Deficiency in platelet 12-lipoxygenase exacerbates inflammation and disease severity during SARS-CoV-2 infection.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Article

68 more citing papers are in PubMed but not listed here.

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.

Patrick S MitchellDivision of Immunology & Pathogenesis, Department of Molecular & Cell Biology, and Cancer Research Laboratory, University of California, Berkeley, CA, USA.
Andrew SandstromDivision of Immunology & Pathogenesis, Department of Molecular & Cell Biology, and Cancer Research Laboratory, University of California, Berkeley, CA, USA; Howard Hughes Medical Institute, University of California, Berkeley, CA, USA.
Russell E VanceDivision of Immunology & Pathogenesis, Department of Molecular & Cell Biology, and Cancer Research Laboratory, University of California, Berkeley, CA, USA; Howard Hughes Medical Institute, University of California, Berkeley, CA, USA. Electronic address: rvance@berkeley.edu.

Funding

The role of Listeria cyclic-di-AMP during infection and immunityP01AI063302 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI STANLEY, SARAH A · 2004 to 2025
$45.5M
Functional and Structural Dissection of Inflammasome ActivationR37AI075039 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI RUSSELL E VANCE · 2018 to 2026
$3.8M
Specificity and in vivo function of the Naip/Nlrc4 inflammasomesR01AI075039 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI VANCE, RUSSELL E · 2008 to 2017
$3.6M
Howard Hughes Medical InstituteNIAID NIH HHS P01 AI063302NIAID NIH HHS R01 AI075039NIAID NIH HHS R37 AI075039
6 · The paper itself

Abstract

Nucleotide-binding domain, leucine-rich repeat (NLR) proteins constitute a diverse class of innate immune sensors that detect pathogens or stress-associated stimuli in plants and animals. Some NLRs are activated upon direct binding to pathogen-derived ligands. In contrast, we focus here on a vertebrate NLR called NLRP1 that responds to the enzymatic activities of pathogen effectors. We discuss a newly proposed 'functional degradation' mechanism that explains activation and assembly of NLRP1 into an oligomeric complex called an inflammasome. We also discuss how NLRP1 is activated by non-pathogen-associated triggers such as the anti-cancer drug Val-boroPro, or by human disease-associated mutations. Finally, we discuss how research on NLRP1 has led to additional biological insights, including the unexpected discovery of a new CARD8 inflammasome.

Indexed as

Adaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsCARD Signaling Adaptor ProteinsHumansImmunity, InnateInflammasomesNeoplasm ProteinsNLR ProteinsAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsCARD8 protein, humanCARD Signaling Adaptor ProteinsInflammasomesNeoplasm ProteinsNLRP1 protein, humanNLR Proteins

Identifiers

PMID31121538
PMCPMC6800612

What OpenQuestion holds

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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.