Evidence map›Paper›PMID 32542665›Full record

ArticleFEBS letters2020

Crystal structure of the human NLRP9 pyrin domain suggests a distinct mode of inflammasome assembly.

Michael Marleaux, Kanchan Anand, Eicke Latz, Matthias Geyer

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in FEBS letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

24 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Review
  3. An overview of human inflammasomes: Activation and regulation.Journal of immunology (Baltimore, Md. : 1950) · 2026
    Review
  4. Article
  5. Review
  6. Review
  7. Pattern Recognition by NOD-Like Receptors.Advances in experimental medicine and biology · 2025
    Review
  8. Review
  9. Review
  10. Review
  11. Review
  12. The NLR gene family: from discovery to present day.Nature reviews. Immunology · 2023
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. An Assay for the Seeding of Homotypic Pyrin Domain Filament Transitions.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Michael MarleauxInstitute of Structural Biology, University of Bonn, Bonn, Germany.
Kanchan AnandInstitute of Structural Biology, University of Bonn, Bonn, Germany.
Eicke LatzInstitute of Innate Immunity, University of Bonn, Bonn, Germany.
Matthias GeyerInstitute of Structural Biology, University of Bonn, Bonn, Germany.ORCID 0000-0002-7718-5002
University of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inflammasomes are cytosolic multimeric signaling complexes of the innate immune system that induce activation of caspases. The NOD-like receptor NLRP9 recruits the adaptor protein ASC to form an ASC-dependent inflammasome to limit rotaviral replication in intestinal epithelial cells, but only little is known about the molecular mechanisms regulating and driving its assembly. Here, we present the crystal structure of the human NLRP9 pyrin domain (PYD). We show that NLRP9

Indexed as

Crystallography, X-RayHEK293 CellsHumansInflammasomesNLR ProteinsInflammasomesNLR ProteinsASC specksfilamentinflammasomesNLRP9PYDstructure

Identifiers

PMID32542665
OpenAlexW3034597200

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.