Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Pyrin variant E148Q potentiates inflammasome activation and the effect of pathogenic mutations in cis.

Rheumatology (Oxford, England) - 1 Mar 2024

Reygaerts Thomas, Laohamonthonkul Pawat, Hrovat-Schaale Katja, Moghaddas Fiona, Baker Paul J, Gray Paul E, Masters Seth L

Abstract excerpt

OBJECTIVE: The p.E148Q variant in pyrin is present in different populations at a frequency of up to 29%, and has been associated with diseases, including vasculitis and FMF. The pathogenicity of p.E148Q in FMF is unclear, even when observed in cis or in trans to a single, typically recessive, pathogenic mutation. We performed functional validation to determine whether p.E148Q increases the ability of pyrin to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Australia
Share to Bacterial Toxins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HEK293 Cells

Share to Inflammasomes

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 37481715
DOI: 10.1093/rheumatology/kead376
PMCID: PMC10907813

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Pyrin variant E148Q potentiates inflammasome activation and the effect of pathogenic mutations in cis.PMID 37481715Read ↗

Mutations in the B30.2 and the Central Helical scaffold domains of pyrin differentially affect inflammasome activationSemantic proximity Read ↗

Familial Mediterranean fever mutations are hypermorphic mutations that specifically decrease the activation threshold of the Pyrin inflammasome.Semantic proximity Read ↗

A novel Pyrin-Associated Autoinflammation with Neutrophilic Dermatosis mutation further defines 14-3-3 binding of pyrin and distinction to Familial Mediterranean Fever.Semantic proximity Read ↗

Familial autoinflammation with neutrophilic dermatosis reveals a regulatory mechanism of pyrin activation.Semantic proximity Read ↗

Mutations in the B30.2 and the central helical scaffold domains of pyrin differentially affect inflammasome activation.Semantic proximity Read ↗

Familial Mediterranean fever mutations lift the obligatory requirement for microtubules in Pyrin inflammasome activation.Semantic proximity Read ↗

The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1beta production.Semantic proximity Read ↗

Apoptosis-associated speck-like protein containing a CARD (ASC) expression profiles in familial Mediterranean fever (FMF) patients with different MEFV mutation patterns.Semantic proximity Read ↗

Functional Assessment of Disease-Associated Pyrin Variants.Semantic proximity Read ↗

A genotype-first approach reveals the molecular basis of pyrin inflammasome activation.Semantic proximity Read ↗

SpeckSeq enables high-throughput functional stratification of MEFV variants in autoinflammatory diseasesSemantic proximity Read ↗

The immunological function of familial Mediterranean fever disease protein PyrinSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.