ReviewMolecules (Basel, Switzerland)2020
ATP-Binding and Hydrolysis in Inflammasome Activation.
Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 72 citations in OpenAlex.
- Structural mechanisms for ATP-mediated inhibition of human NLRP6 inflammasome.Nature structural & molecular biology · 2026Article
- Construction of an ATP hydrolysis-related 11-gene signature for predicting prognosis and immune response in hepatocellular carcinoma.Medicine · 2026Article
- Structural mechanisms of SAMD9 autoinhibition and pathogenic dysregulation.Science advances · 2026Article
- Comprehensive pan-cancer analysis of MEX3C in human tumors.Discover oncology · 2026Article
- Unravelling the role of PANoptosis in diseases: from emerging molecular mechanisms-to-therapeutic implications.Cancer biology & medicine · 2026Review
- Precision Editing of NLRS Improves Effector Recognition for Enhanced Disease Resistance.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- PANoptosis nexus in ischemia-reperfusion injury: from integrated cell death mechanisms to novel therapeutic opportunities.Frontiers in immunology · 2026Review
- The NLRP6 inflammasome is activated by sterile or pathogen-induced endolysosomal damage.The EMBO journal · 2026Article
- Role of macrophage ATP metabolism disorder in SiOPurinergic signalling · 2025Review
- NLRP3 inflammasome: structure, mechanism, drug-induced organ toxicity, therapeutic strategies, and future perspectives.RSC medicinal chemistry · 2025Review
- Targeting the NLRP3 inflammasome as a novel therapeutic target for osteoarthritis.Inflammopharmacology · 2025Review
- Structural Insight into the Binding Pattern and Interaction Mechanism of Antagonist MCC950 and Agonist BMS986299 with NLRP3 by Molecular Dynamics Simulation.Current computer-aided drug design · 2025Article
- Potential Mechanisms of COVID-19 Related Nervous System Damage and Effects on Female Fertility.Current medicinal chemistry · 2025Review
- The human disease-associated gene ZNFX1 controls inflammation through inhibition of the NLRP3 inflammasome.The EMBO journal · 2024Article
- Outcomes of female reproductive performance with assisted reproductive techniques after recent mild to moderate COVID-19 infections: An observational study.Clinical and experimental reproductive medicine · 2024Article
- Comparative analysis on natural variants of fire blight resistance protein FB_MR5 indicates distinct effector recognition mechanisms.Molecules and cells · 2024Article
- High-Throughput Molecular Modeling and Evaluation of the Anti-Inflammatory Potential of Açaí Constituents against NLRP3 Inflammasome.International journal of molecular sciences · 2024Article
- Conservation and similarity of bacterial and eukaryotic innate immunity.Nature reviews. Microbiology · 2024Review
- NFκB and NLRP3/NLRC4 inflammasomes regulate differentiation, activation and functional properties of monocytes in response to distinct SARS-CoV-2 proteins.Nature communications · 2024Article
- New Insights on NLRP3 Inflammasome: Mechanisms of Activation, Inhibition, and Epigenetic Regulation.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2024Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The prototypical model for NOD-like receptor (NLR) inflammasome assembly includes nucleotide-dependent activation of the NLR downstream of pathogen- or danger-associated molecular pattern (PAMP or DAMP) recognition, followed by nucleation of hetero-oligomeric platforms that lie upstream of inflammatory responses associated with innate immunity. As members of the STAND ATPases, the NLRs are generally thought to share a similar model of ATP-dependent activation and effect. However, recent observations have challenged this paradigm to reveal novel and complex biochemical processes to discern NLRs from other STAND proteins. In this review, we highlight past findings that identify the regulatory importance of conserved ATP-binding and hydrolysis motifs within the nucleotide-binding NACHT domain of NLRs and explore recent breakthroughs that generate connections between NLR protein structure and function. Indeed, newly deposited NLR structures for NLRC4 and NLRP3 have provided unique perspectives on the ATP-dependency of inflammasome activation. Novel molecular dynamic simulations of NLRP3 examined the active site of ADP- and ATP-bound models. The findings support distinctions in nucleotide-binding domain topology with occupancy of ATP or ADP that are in turn disseminated on to the global protein structure. Ultimately, studies continue to reveal how the ATP-binding and hydrolysis properties of NACHT domains in different NLRs integrate with signaling modules and binding partners to control innate immune responses at the molecular level.
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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.