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

Autolytic proteolysis within the function to find domain (FIIND) is required for NLRP1 inflammasome activity.

The Journal of biological chemistry - 20 Jul 2012

Finger Joshua N, Lich John D, Dare Lauren C, Cook Michael N, Brown Kristin K, Duraiswami Chaya, Bertin John, Bertin John J, Gough Peter J

Abstract excerpt

Nucleotide-binding domain leucine-rich repeat proteins (NLRs) play a key role in immunity and disease through their ability to modulate inflammation in response to pathogen-derived and endogenous danger signals. Here, we identify the requirements for activation of NLRP1, an NLR protein associated with a number of human pathologies, including vitiligo, rheumatoid arthritis, and Crohn disease. We demonstrate that...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Apoptosis Regulatory Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HEK293 Cells

Share to Immunity, Innate

Share to Inflammasomes

Share to NLR Proteins

Share to Protein Processing, Post-Translational

Share to Proteolysis

Source

Open in PubMed Open full text

Identifiers

PMID: 22665479
DOI: 10.1074/jbc.M112.378323
PMCID: PMC3408201

Genes

NLRP1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Autolytic proteolysis within the function to find domain (FIIND) is required for NLRP1 inflammasome activity.PMID 22665479Read ↗

NLRP3, NLRP6, and NLRP12 are inflammasomes with distinct expression patternsSemantic proximity Read ↗

Mechanisms of NLRP1-Mediated Autoinflammatory Disease in Humans and Mice.Semantic proximity Read ↗

Human DPP9 represses NLRP1 inflammasome and protects against autoinflammatory diseases via both peptidase activity and FIIND domain bindingSemantic proximity Read ↗

Human caspase-1 autoproteolysis is required for ASC-dependent and -independent inflammasome activationSemantic proximity Read ↗

DPP9 is an endogenous and direct inhibitor of the NLRP1 inflammasome that guards against human auto-inflammatory diseasesSemantic proximity Read ↗

The NLRP1 Inflammasome in Human Skin and BeyondSemantic proximity Read ↗

The tetrapeptide sequence of IL-1β regulates its recruitment and activation by inflammatory caspasesSemantic proximity Read ↗

Regulation of inflammasome activation.Semantic proximity Read ↗

Structure-based alignment of human caspase recruitment domains provides a framework for understanding their functionSemantic proximity Read ↗

To protect or adversely affect? The dichotomous role of the NLRP1 inflammasome in human diseaseSemantic proximity Read ↗

Peptidyl Arginine Deiminases in Chronic Diseases: A Focus on Rheumatoid Arthritis and Interstitial Lung DiseaseSemantic proximity Read ↗

Autoinflammatory mutation in NLRC4 reveals a leucine-rich repeat (LRR)–LRR oligomerization interfaceSemantic proximity Read ↗

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