ArticleCommunications biology2022
ATP-binding and hydrolysis of human NLRP3.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 64 citations in OpenAlex.
- Structural mechanisms for ATP-mediated inhibition of human NLRP6 inflammasome.Nature structural & molecular biology · 2026Article
- The Role of Skeletal Muscle Mitochondria in NLRP3 Inflammasome Signaling.Biomolecules · 2026Review
- A Review on Structural Insights into NLRP3 and NEK7: Domain Architecture, Subcellular Localization, and Their Interaction in Inflammasome Assembly and Signaling.Molecular neurobiology · 2026Review
- C-terminal lysine residues localise NLRP10 at lipid droplets and govern NLRP10 oligomer formation.EMBO reports · 2026Article
- Stage-dependent role of NEK7 in the inactive-to-active conformational transition of NLRP3 monomer.PLoS computational biology · 2026Article
- Cofilin-1 is a redox-sensitive guard of the NLRP3 inflammasome.Nature immunology · 2026Article
- Human NLRP3 inflammasome activation leads to formation of condensate at the microtubule organizing center.Science advances · 2026Article
- Mice humanized by syntenic replacement with full-length NLRP3 disease-associated variants model the clinical cryopyrinopathy continuum.JCI insight · 2026Article
- The NLRP6 inflammasome is activated by sterile or pathogen-induced endolysosomal damage.The EMBO journal · 2026Article
- Article
- Discovery of potent and selective inhibitors of human NLRP3 with a novel mechanism of action.The Journal of experimental medicine · 2025Article
- High Glucose Aggravates Cerebral Ischemia/Reperfusion via Truncated NLRP3-Mediated Hexokinase-2 Translocation.CNS neuroscience & therapeutics · 2025Article
- Molecular mechanisms and regulation of inflammasome activation and signaling: sensing of pathogens and damage molecular patterns.Cellular & molecular immunology · 2025Review
- How interactions between oxidized DNA and the NLRP3 inflammasome fuel inflammatory disease.Trends in biochemical sciences · 2025Review
- The expanding role of the NLRP3 inflammasome from periodic fevers to therapeutic targets.Nature immunology · 2025Review
- Nitroxoline is a novel inhibitor of NLRP3-dependent pyroptosis.Cell death discovery · 2025Article
- Identifying therapeutic targets for erectile dysfunction in the European population using genome-wide Mendelian randomization.Sexual medicine · 2025Article
- NLRP3 inflammasome: structure, mechanism, drug-induced organ toxicity, therapeutic strategies, and future perspectives.RSC medicinal chemistry · 2025Review
- Clustering of NLRP3 induced by membrane or protein scaffolds promotes inflammasome assembly.Nature communications · 2025Article
- ATP functions as a pathogen-associated molecular pattern to activate the E3 ubiquitin ligase RNF213.Nature communications · 2025Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The innate immune system uses inflammasomal proteins to recognize danger signals and fight invading pathogens. NLRP3, a multidomain protein belonging to the family of STAND ATPases, is characterized by its central nucleotide-binding NACHT domain. The incorporation of ATP is thought to correlate with large conformational changes in NLRP3, leading to an active state of the sensory protein. Here we analyze the intrinsic ATP hydrolysis activity of recombinant NLRP3 by reverse phase HPLC. Wild-type NLRP3 appears in two different conformational states that exhibit an approximately fourteen-fold different hydrolysis activity in accordance with an inactive, autoinhibited state and an open, active state. The impact of canonical residues in the nucleotide binding site as the Walker A and B motifs and sensor 1 and 2 is analyzed by site directed mutagenesis. Cellular experiments show that reduced NLRP3 hydrolysis activity correlates with higher ASC specking after inflammation stimulation. Addition of the kinase NEK7 does not change the hydrolysis activity of NLRP3. Our data provide a comprehensive view on the function of conserved residues in the nucleotide-binding site of NLRP3 and the correlation of ATP hydrolysis with inflammasome activity.
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Registered trials
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.