Evidence map›Paper›PMID 35382945›Full record

ArticleTrends in biochemical sciences2022

NLRP3 is its own gatekeeper: a group hug of NLRP3 monomers controls inflammation.

Iva Hafner-Bratkovič

Open access · greenAbstract readComment
PubMed Publisher
In one paragraph

Article in Trends in biochemical sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 42% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Iva Hafner-BratkovičDepartment of Synthetic Biology and Immunology, National Institute of Chemistry, Hajdrihova 19, Ljubljana, 1000, Slovenia; EN-FIST Centre of Excellence, Trg Osvobodilne Fronte 13, Ljubljana, Slovenia. Electronic address: iva.hafner@ki.si.
EN-FIST Centre of Excellence (Slovenia) · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A recent study by Hochheiser et al. describes the cryo-electron microscopy (cryoEM) structure of an autoinhibited nucleotide-binding domain-, leucine-rich repeat (LRR)- and pyrin domain-containing protein 3 (NLRP3) decamer that assembles via LRR interactions and is further stabilized by the small-molecule NLRP3-specific inhibitor CRID3 binding into a cleft within the NACHT domain. The study provides a springboard for the development of novel NLRP3-based therapies.

Indexed as

InflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinCryoelectron MicroscopyHumansInflammationInflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinCRID3InflammasomeinhibitorMCC950NLRP3oligomer

Identifiers

PMID35382945
OpenAlexW4224026697

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.