Evidence map›Paper›PMID 21976665›Full record

ArticleThe Journal of biological chemistry2011

Uncoupling of Pyrin-only protein 2 (POP2)-mediated dual regulation of NF-κB and the inflammasome.

Maninjay K Atianand, Jonathan A Harton

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.9field-weighted citation impact, top 27% of its field
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

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. An overview of human inflammasomes: Activation and regulation.Journal of immunology (Baltimore, Md. : 1950) · 2026
    Review
  2. Polydatin: A natural compound with multifaceted anticancer properties.Journal of traditional and complementary medicine · 2025
    Review
  3. New Insights on NLRP3 Inflammasome: Mechanisms of Activation, Inhibition, and Epigenetic Regulation.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2024
    Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. COPs and POPs Patrol Inflammasome Activation.Journal of molecular biology · 2018
    Review
  11. Article
  12. Article
  13. Assembly and regulation of ASC specks.Cellular and molecular life sciences : CMLS · 2017
    Review
  14. Review
  15. Review
  16. Review
  17. An updated view on the structure and function of PYRIN domains.Apoptosis : an international journal on programmed cell death · 2015
    Article
  18. Activation and assembly of the inflammasomes through conserved protein domain families.Apoptosis : an international journal on programmed cell death · 2015
    Review
  19. Article
  20. Review
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

2 authors at 1 institution in 1 country.

Maninjay K AtianandCenter for Immunology and Microbial Disease, Albany Medical College, Albany, New York 12208, USA.
Jonathan A Harton
Albany Medical Center Hospital · US

Funding

Regulation of Innate Immunity by Pyrin ProteinsR01AI072259 · NIAID · ALBANY MEDICAL COLLEGE · PI HARTON, JONATHAN A · 2009 to 2012
$1.4M
NIAID NIH HHS R01 AI072259NIAID NIH HHS R01AI072259
6 · The paper itself

Abstract

Activation of transcription factor NF-κB and inflammasome-directed caspase-1 cleavage of IL-1β are key processes in the inflammatory response to pathogen or host-derived signals. Pyrin-only proteins (POPs) are restricted to Old World monkeys, apes, and humans and have previously been shown to impair inflammasome assembly and/or NF-κB p65 transcriptional activity in transfected epithelial cells. However, the biological role of POP2 and the molecular basis for its observed functions are not well understood. In this report we demonstrate that POP2 regulates TNFα and IL-1β responses in human monocytic THP-1 cells and in stable transfectants of mouse J774A.1 macrophages. Deletion analysis of POP2 revealed that the first α-helix (residues 1-19) is necessary and sufficient for both inflammasome and NF-κB inhibitory functions. Further, key acidic residues Glu(6), Asp(8), and Glu(16), believed critical for Pyrin/Pyrin domain interaction, are important for inflammasome inhibition. Moreover, these mutations did not reduce the effect of POP2 upon NF-κB, indicating that the inflammasome and NF-κB inhibitory properties of POP2 can be uncoupled mechanistically. Collectively, these data demonstrate that POP2 acts as a regulator of inflammatory signals and exerts its two known functions through distinct modalities employed by its first α-helix.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsApoptosis Regulatory ProteinsCARD Signaling Adaptor ProteinsCarrier ProteinsCytoskeletal ProteinsFrancisellaHEK293 CellsHumansInflammasomesInterleukin-1betaLipopolysaccharidesMacrophagesMiceMolecular Sequence DataAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsCARD Signaling Adaptor ProteinsCarrier ProteinsCytoskeletal ProteinsInflammasomesInterleukin-1betaLipopolysaccharidesNLR Family, Pyrin Domain-Containing 3 ProteinNLRP2 protein, humanNLRP3 protein, humanPYCARD protein, humanTranscription Factor RelATumor Necrosis Factor-alpha

Identifiers

PMID21976665
PMCPMC3220484
OpenAlexW2014461782

What OpenQuestion holds

Textmetadata
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.