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

S5D mutation of NLRP3 revealed its role in NLRP3 inflammasome complex using split-luciferase complementation assay.

Biochimica et biophysica acta. Molecular cell research - 1 Jun 2026

Amandadi Mojdeh, Ravan Hadi, Hashemabadi Mohammad, Hosseinkhani Saman

Abstract excerpt

The NOD-like receptor (NLR) family pyrin domain-containing protein 3 (NLRP3) is a critical cytosolic inflammasome sensor of exogenous and endogenous danger signals and is a highly attractive medicinal target against inflammatory diseases. The molecular mechanism leading to NLRP3 inflammasome activation through conformational changes of NLRP3 and apoptosis-associated speck-like protein containing a CARD (ASC)...

Read the complete abstract on PubMed

Topics

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

Share to NLR Family, Pyrin Domain-Containing 3 Protein
Share to CARD Signaling Adaptor Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to NLRP3 gene

Share to HEK293 Cells

Share to Inflammasomes

Share to Luciferases

Share to Mutation

Source

Identifiers

PMID: 41819454
DOI: 10.1016/j.bbamcr.2026.120133

Genes

NLRP3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

S5D mutation of NLRP3 revealed its role in NLRP3 inflammasome complex using split-luciferase complementation assay.PMID 41819454Read ↗

A phenotypic high-content, high-throughput screen identifies inhibitors of NLRP3 inflammasome activation.Semantic proximity Read ↗

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

Distinct interaction modes orchestrate the polymerization of ASC PYD and CARD domains into filamentous structures.Semantic proximity Read ↗

Biochemical and structural aspects of the ATP‐binding domain in inflammasome‐forming human NLRP proteinsSemantic proximity Read ↗

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

Identification of Multifaceted Binding Modes for Pyrin and ASC Pyrin Domains Gives Insights into Pyrin Inflammasome AssemblySemantic 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 ↗

Cold-induced loss of interaction with HSC70 triggers inflammasome activity of familial cold autoinflammatory syndrome-causing mutants of NLRP3Semantic proximity Read ↗

NLRP3 cages revealed by full-length mouse NLRP3 structure control pathway activation.Semantic proximity Read ↗

Evaluation of protein kinase D auto-phosphorylation as biomarker for NLRP3 inflammasome activationSemantic proximity Read ↗

ASC filament formation serves as a signal amplification mechanism for inflammasomes.Semantic proximity Read ↗

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