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

NLRP3 cages revealed by full-length mouse NLRP3 structure control pathway activation.

Cell - 22 Dec 2021

Andreeva Liudmila, David Liron, Rawson Shaun, Shen Chen, Pasricha Teerithveen, Pelegrin Pablo, Wu Hao

Abstract excerpt

The NACHT-, leucine-rich-repeat- (LRR), and pyrin domain-containing protein 3 (NLRP3) is emerging to be a critical intracellular inflammasome sensor of membrane integrity and a highly important clinical target against chronic inflammation. Here, we report that an endogenous, stimulus-responsive form of full-length mouse NLRP3 is a 12- to 16-mer double-ring cage held together by LRR-LRR interactions with the pyrin...

Read the complete abstract on PubMed

Topics

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

Share to Cryoelectron Microscopy
Share to HEK293 Cells
Share to Inflammasomes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to NIMA-Related Kinases

Share to NLR Family, Pyrin Domain-Containing 3 Protein

Share to Protein Domains

Share to Protein Multimerization

Share to trans-Golgi Network

Source

Open in PubMed Open full text

Identifiers

PMID: 34861190
DOI: 10.1016/j.cell.2021.11.011
PMCID: PMC8763037

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

NLRP3 cages revealed by full-length mouse NLRP3 structure control pathway activation.PMID 34861190Read ↗

<i>In vivo</i> cellular localisation and nanoscale organisation of NLRP3 inflammasomesSemantic proximity Read ↗

Spatiotemporal proteomic profiling of cellular responses to NLRP3 agonistsSemantic proximity Read ↗

Revealing the dance of NLRP3: spatiotemporal patterns in inflammasome activationSemantic proximity Read ↗

A detailed Molecular Network Map and Model of the NLRP3 InflammasomeSemantic proximity Read ↗

Defective endosome-TGN retrograde transport promotes NLRP3 inflammasome activationSemantic proximity Read ↗

Structural basis for the oligomerization-mediated regulation of NLRP3 inflammasome activation.Semantic proximity Read ↗

NLRP3 acts as a direct sensor of intracellular potassium ionsSemantic proximity Read ↗

Defective endosome-TGN retrograde transport promotes NLRP3 inflammasome activationSemantic proximity Read ↗

Intrinsic flexibility of NLRP pyrin domains is a key factor in their conformational dynamics, fold stability, and dimerization.Semantic proximity Read ↗

NLRP3 Cys126 palmitoylation by ZDHHC7 Promotes Inflammasome ActivationSemantic proximity Read ↗

C-terminal lysine residues localise NLRP10 at lipid compartments and govern NLRP10 oligomer formationSemantic proximity Read ↗

Cryo-EM structure of the gasdermin A3 membrane pore.Semantic proximity Read ↗

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