Evidence map›Paper›PMID 35759199›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

An Assay for the Seeding of Homotypic Pyrin Domain Filament Transitions.

Inga V Hochheiser, Matthias Geyer

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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 2 institutions in 1 country.

Inga V HochheiserInstitute of Structural Biology, University Hospital Bonn, University of Bonn, Bonn, Germany.
Matthias GeyerInstitute of Structural Biology, University Hospital Bonn, University of Bonn, Bonn, Germany. matthias.geyer@uni-bonn.de.
University Hospital Bonn · DEUniversity of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pattern recognition receptors of innate immune cells allow the recognition of invariant microbial structures. The nucleotide-binding oligomerization domain-like receptors (NLRs) comprise 22 members, divided into 3 subfamilies. Homotypic pyrin domain (PYD) interactions were shown to mediate the interaction of inflammasome forming NLRPs with the adaptor protein ASC, bridging the interaction to caspase-1 and resulting in caspase-1-induced cytokine maturation and pyroptotic cell death. Here we describe a NLRP3

Indexed as

NLR Family, Pyrin Domain-Containing 3 ProteinPyrin DomainCaspase 1Cytoskeletal ProteinsProtein BindingCaspase 1Cytoskeletal ProteinsNLR Family, Pyrin Domain-Containing 3 ProteinASCElectron microscopyFilament elongationFilament nucleationInflammasomeInnate immunityNLRP3PYDPyrin domain

Identifiers

PMID35759199
OpenAlexW4285163866

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.