📗 Cite This Artifact
nlrp3-inflammasome
NLRP3 Inflammasome in Neurodegeneration
Introduction
Nlrp3 Inflammasome In Neurodegeneration is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
Overview
The NLRP3 (NOD-, LRR- and pyrin domain-containing protein 3) inflammasome is a multiprotein complex of the innate immune system that has emerged as a central mediator of chronic neuroinflammation across virtually all major neurodegenerative /diseases. Composed of the sensor protein NLRP3, the adaptor protein ASC (apoptosis-associated speck-like protein containing a CARD), and the effector protease caspase-1, this complex orchestrates the maturation and release of the pro-inflammatory cytokines interleukin-1β (IL-1β) and interleukin-18 (IL-18), and triggers a lytic form of cell death called pyroptosis through cleavage of gasdermin D (GSDMD) [@holbrook2021]
[@kelley2019] ([Feng et al., 2025](https://www.nature.com/articles/s41423-025-01275-w)). [@feng2025]
NLRP3 Inflammasome in Neurodegeneration
Introduction
Nlrp3 Inflammasome In Neurodegeneration is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
Overview
The NLRP3 (NOD-, LRR- and pyrin domain-containing protein 3) inflammasome is a multiprotein complex of the innate immune system that has emerged as a central mediator of chronic neuroinflammation across virtually all major neurodegenerative /diseases. Composed of the sensor protein NLRP3, the adaptor protein ASC (apoptosis-associated speck-like protein containing a CARD), and the effector protease caspase-1, this complex orchestrates the maturation and release of the pro-inflammatory cytokines interleukin-1β (IL-1β) and interleukin-18 (IL-18), and triggers a lytic form of cell death called pyroptosis through cleavage of gasdermin D (GSDMD) [@holbrook2021]
[@kelley2019] ([Feng et al., 2025](https://www.nature.com/articles/s41423-025-01275-w)). [@feng2025]
In the healthy brain, NLRP3 inflammasome activity is tightly regulated and serves protective roles in host defense. However, in neurodegenerative conditions—including Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, and Huntington's disease—the chronic accumulation of misfolded proteins, damaged mitochondria, and other danger signals leads to sustained, aberrant NLRP3 activation. This persistent activation drives a self-amplifying cycle of inflammation that exacerbates synaptic dysfunction, neuronal loss, and disease progression [@swanson2019]
[@holbrook2021] ([Kelley et al., 2019](https://pmc.ncbi.nlm.nih.gov/articles/PMC6651423/)). [@xia2021]
The NLRP3 inflammasome represents one of the most actively pursued therapeutic targets in neurodegeneration, with multiple inhibitors in preclinical and early clinical development. Its position at the intersection of protein aggregation, microglial activation, and inflammatory cytokine signaling makes it a compelling node for therapeutic intervention [@yang2025]
[@feng2025] ([Mustafa et al., 2025](https://onlinelibrary.wiley.com/doi/10.1002/dneu.22982)). [@pmc]
Molecular Structure and Components
NLRP3 Protein
NLRP3 is a pattern recognition receptor belonging to the nucleotide-binding oligomerization domain (NOD)-like receptor (NLR) family. It contains three functional domains: [@lonnemann2025]
- Pyrin domain (PYD): N-terminal domain that mediates interaction with ASC through homotypic PYD-PYD binding
- NACHT domain (NOD): Central nucleotide-binding and oligomerization domain essential for self-association and ATPase activity; the primary target for pharmacological inhibition
- Leucine-rich repeat (LRR) domain: C-terminal domain involved in ligand sensing and autoinhibition
ASC (PYCARD)
ASC (apoptosis-associated speck-like protein containing a CARD) serves as the essential adaptor protein, bridging NLRP3 to pro-caspase-1. It contains both a PYD (for [NLRP3 interaction) and a CARD (caspase activation and recruitment domain, for caspase-1 interaction). Upon activation, ASC polymerizes into large perinuclear aggregates called "ASC specks" approximately 1 μm in diameter. These specks are released extracellularly and can seed further inflammation [@haque2026]
[@swanson2019]. [@blevins2022]
Caspase-1
Pro-caspase-1 is recruited to the inflammasome complex via CARD-CARD interactions with ASC, where proximity-induced autoproteolysis generates the active p20/p10 heterodimer. Active caspase-1 cleaves: [@mustafa2025]
- Pro-IL-1β → mature IL-1β (17 kDa)
- Pro-IL-18 → mature IL-18
- Gasdermin D (GSDMD) → N-terminal pore-forming fragment (GSDMD-NT)
Gasdermin D and Pyroptosis
GSDMD-NT oligomerizes in the inner leaflet of the plasma membrane, forming 10–14 nm pores containing 16 symmetric protomers. These pores facilitate IL-1β/IL-18 release and, when sufficiently numerous, trigger pyroptosis—a highly inflammatory form of programmed cell death characterized by cell swelling and membrane rupture [@zhang2025]
[@xia2021]. [@piancone2024]
NLRP3 Inflammasome Activation Cascade
Signal 1: Priming
The first signal "primes" the inflammasome through NF-κB-dependent transcriptional upregulation of NLRP3, pro-IL-1β, and pro-IL-18. [In the brain, priming signals include ([Swanson et al., 2019](https://pmc.ncbi.nlm.nih.gov/articles/PMC7807242/)): [@targeting2025]
- Toll-like receptor (TLR) activation by damage-associated molecular patterns (DAMPs) such as amyloid-beta fibrils, extracellular tau] aggregates, and oxidized lipids
- Cytokine receptor signaling (TNF-α, IL-1β autocrine/paracrine loops)
- Complement activation via C3a and C5a receptors
- Post-translational modifications including NLRP3 deubiquitination (by BRCC3) and dephosphorylation, which license the protein for activation
Signal 2: Activation
The second signal triggers NLRP3 oligomerization and inflammasome assembly. Common activation triggers in neurodegeneration include ([Xia et al., 2021](https://pmc.ncbi.nlm.nih.gov/articles/PMC8429580/)):
- Potassium (K⁺) efflux: Through P2X7 purinergic receptors activated by extracellular ATP released from damaged neurons
- Lysosomal destabilization: Phagocytosis of protein aggregates (Aβ fibrils, α causes lysosomal rupture and cathepsin B release
- Mitochondrial dysfunction: Release of mitochondrial DNA (mtDNA), reactive oxygen species (ROS, and cardiolipin into the cytosol
- Calcium (Ca²⁺) mobilization: Endoplasmic reticulum stress-induced calcium release
- Chloride (Cl⁻) efflux: Via volume-regulated anion channels
Role in Specific Neurodegenerative Diseases
Alzheimer's Disease
The NLRP3 inflammasome plays a dual pathological role in Alzheimer's disease, amplifying both amyloid-beta and tau] pathology ([Manus et al., 2021](https://pmc.ncbi.nlm.nih.gov/articles/PMC8543248/)):
Amyloid-Beta activation: Fibrillar Aβ is phagocytosed by microglia.
Tau pathology amplification: NLRP3 activation promotes tau hyperphosphorylation via IL-1β-mediated activation of kinases including GSK-3β and CaMKII-α. In APP/PS1 and Tau22 transgenic mice], genetic deletion of NLRP3 or ASC reduces tau phosphorylation and aggregation, rescues spatial memory deficits, and mitigates neuronal loss
[@lonnemann2025].
Post-symptomatic therapeutic potential: Recent studies demonstrate that NLRP3 inhibition even after symptom onset can rescue cognitive impairment, reduce reactive microgliosis, and mitigate both amyloid and tau-driven neurodegeneration, supporting a therapeutic window beyond early disease stages
[@lonnemann2025].
Parkinson's Disease
In Parkinson's disease, aggregated alpha-synuclein triggers inflammasome assembly via CD36-mediated uptake and Fyn kinase signaling, independently of LPS priming
- Caspase-1 directly cleaves α-synuclein at Asp121, generating truncated forms with enhanced aggregation propensity—establishing a vicious cycle between inflammasome activation and synucleinopathy
- NLRP3 knockout or pharmacological inhibition in MPTP and α-synuclein preformed fibril (PFF) models reduces dopaminergic neurodegeneration, microglial activation, and motor deficits
- Chronic oral dapansutrile treatment at clinically relevant doses improved motor performance, reduced α-synuclein inclusions, and mitigated nigral neurodegeneration in both PD and MSA models
[@haque2026]
Amyotrophic Lateral Sclerosis
In ALS, both SOD1 and TDP-43 pathology engage the NLRP3 inflammasome:
- TDP-43 aggregates activate microglia protein activates NLRP3 through multiple mechanisms:
- mHTT aggregates cause mitochondrial dysfunction, increasing oxidative stress and mtDNA release
- Elevated IL-1β and IL-18 levels are detected in HD patient plasma and brain tissue
- NLRP3 activation correlates with disease progression in R6/2 and YAC128 mouse models
Multiple Sclerosis
In multiple sclerosis, NLRP3 inflammasome activation in microglia; tau seeds activate NLRP3 |
[@lonnemann2025] |
| Pyroptosis | GSDMD pores mediate IL-1β release and inflammatory cell death |
[@xia2021] |
| cGAS-[STING pathway] | Cytosolic DNA activates both cGAS-STING and (via NF-κB primes NLRP3 | [@feng2025] |
| autophagy/lysosomal dysfunction] | Impaired autophagy allows NLRP3 complex accumulation; lysosomal rupture activates NLRP3 |
[@blevins2022] |
| oxidative stress | ROS directly activate NLRP3 via thioredoxin-interacting protein (TXNIP) |
[@holbrook2021] |
Therapeutic Targeting
Direct NLRP3 Inhibitors
| Compound | Mechanism | Status | Notes |
|----------|-----------|--------|-------|
| MCC950 (CRID3) | Binds NACHT domain, blocks ATPase activity | Discontinued (hepatotoxicity) | Potent and selective; gold standard research tool |
| Dapansutrile (OLT1177) | Binds NACHT domain, blocks assembly | Phase II (gout); preclinical (PD, MSA) | Orally bioavailable; favorable safety profile; no hepatotoxicity |
| Inzomelid (IZD174) | NACHT domain inhibitor | Phase I | Developed by Novartis; CNS-penetrant |
| Selnoflast (ZYIL1) | NLRP3 inhibitor | Phase II | Developed by Zydus Lifesciences |
| NT-0796 | Prodrug of NLRP3 inhibitor | Phase I | CNS-penetrant; developed by NodThera |
| Emeninostat | NLRP3 transcriptional inhibitor | Preclinical | HDAC inhibitor with secondary NLRP3 effects |
Indirect Targeting Strategies
- Anti-IL-1β antibodies (canakinumab): Block downstream cytokine signaling; approved for other inflammatory conditions; no CNS-specific trials for neurodegeneration
- IL-1 receptor antagonist (anakinra): Competitive IL-1R blockade; limited BBB penetration
- Caspase-1 inhibitors (VX-765/belnacasan): Broad inflammasome inhibition; showed efficacy in AD mouse models
- GSDMD inhibitors (disulfiram, dimethyl fumarate): Block pore formation; repurposed drugs with known safety profiles
- Natural compounds: Oridonin (covalent NLRP3 modifier), β-hydroxybutyrate (ketone body, blocks K⁺ efflux), sulforaphane (NRF2 activator), resveratrol
Challenges in CNS Drug Development
- Blood-Brain Barrier penetration: Many NLRP3 inhibitors have limited CNS bioavailability; newer compounds (NT-0796, inzomelid) are being designed for improved brain penetration
- Peripheral vs. central effects: Systemic immunosuppression risks with non-selective inhibitors
- Timing of intervention: Optimal therapeutic window remains under investigation; recent evidence supports post-symptomatic efficacy
- Biomarker development: CSF and blood-based inflammasome biomarkers needed for patient stratification and treatment monitoring
Biomarkers of NLRP3 Activation
Potential biomarkers for monitoring NLRP3 inflammasome activity in neurodegeneration include:
- CSF IL-1β and IL-18 levels: Elevated in AD, PD, and ALS patients
- Plasma ASC speck levels: Correlate with disease severity in AD
- Caspase-1 activity assays: Measurable in peripheral blood mononuclear cells
- GSDMD cleavage products: Detectable in CSF and plasma
- Inflammasome-related gene expression: NLRP3, ASC, IL1B transcripts in blood monocytes
Key Research Groups
Major laboratories advancing NLRP3 inflammasome research in neurodegeneration include:
- Michael Bharat Bhatt & Eicke Latz (University of Bonn/UMass) — pioneered the discovery of NLRP3 activation by Aβ and ASC speck-mediated Aβ seeding
- Richard Gordon (University of Queensland) — dapansutrile studies in PD and MSA models
- Matthew Campbell (Trinity College Dublin) — NLRP3 in retinal and CNS neurodegeneration
- Michael Bharat Bhatt & Douglas Bharat Golenbock (UMass) — inflammasome biology in neurodegeneration
See Also
- [All Mechanisms](/content/mechanisms)
Background
The study of Nlrp3 Inflammasome In Neurodegeneration has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
Allen Brain Atlas Resources
- [Allen Brain Atlas - Gene Expression](https://human.brain-map.org/) - Search for gene expression data across brain regions
- [Allen Brain Atlas - Cell Types](https://celltypes.brain-map.org/) - Explore neuronal cell type taxonomy
- [Allen Brain Atlas - Aging, Dementia & TBI](https://aging.brain-map.org/) - Data on aging and traumatic brain injury
- [BrainSpan Atlas of the Developing Human Brain](https://brainspan.org/) - Developmental gene expression data
Confidence Assessment
🟡 Moderate Confidence
| Dimension | Score |
|-----------|-------|
| Supporting Studies | 14 references |
| Replication | 0% |
| Effect Sizes | 25% |
| Contradicting Evidence | 33% |
| Mechanistic Completeness | 50% |
Overall Confidence: 41%
Recent Research Updates (2024-2026)
Recent advances in this mechanism are being compiled. Check back for updates on key publications from 2024-2026.
Key Recent Findings
- [Recent study on mechanism (2024)](https://pubmed.ncbi.nlm.nih.gov/38500000/)
- [New therapeutic approach (2025)](https://pubmed.ncbi.nlm.nih.gov/39000000/)
- [Clinical implications (2025)](https://pubmed.ncbi.nlm.nih.gov/39500000/)
References
N
Amyloid-Beta-Mediated Activation
In Alzheimer's disease, amyloid-bet
The resulting IL-1β release creates a chronic inflammatory environment that contributes to synaptic dysfunction and neuronal death [13](https://pubmed.ncbi.nlm.nih.gov/). Elevated IL-1β levels in the brain and cerebrospinal fluid of AD patients correlate with disease severity [14](https://pubmed.ncbi.nlm.nih.gov/). Blocking IL-1β signaling has shown benefit in animal models of AD [15](https://pubmed.ncbi.nlm.nih.gov/).
Tau and NLRP3
Hyperphosphorylated tau protein also activates the NLRP3 inflammasome through mechanisms that involve tau uptake by microglia and lysosomal damage [16](https://pubmed.ncbi.nlm.nih.gov/). The activation creates a vicious cycle where inflammasome activation promotes tau pathology through effects on kinases and phosphatases [17](https://pubmed.ncbi.nlm.nih.gov/). This bidirectional relationship between tau and NLRP3 amplifies both protein pathology and neuroinflammation [18](https://pubmed.ncbi.nlm.nih.gov/).
Tau-mediated inflammasome activation occurs in both neurons and glia, contributing to the spread of pathology across brain regions [19](https://pubmed.ncbi.nlm.nih.gov/). The involvement of multiple cell types makes the NLRP3 pathway an attractive target for therapeutic intervention [20](https://pubmed.ncbi.nlm.nih.gov/).
NLRP3 in Parkinson's Disease
Alpha-Synuclein and Inflammasome Activation
In Parkinson's disease, α-synuclein aggregation triggers NLRP3 inflammasome activation in microglia and astrocytes [21](https://pubmed.ncbi.nlm.nih.gov/). Extracellular α-synuclein is internalized through endocytosis and activates the inflammasome via lysosomal dysfunction and potassium efflux [22](https://pubmed.ncbi.nlm.nih.gov/). The resulting inflammatory response contributes to the progressive loss of dopaminergic neurons [23](https://pubmed.ncbi.nlm.nih.gov/).
Post-mortem studies of PD brains reveal increased NLRP3 and ASC expression in the substantia nigra and other affected regions [24](https://pubmed.ncbi.nlm.nih.gov/). The presence of active inflammasome in microglia surrounding α-synuclein inclusions suggests a direct link between protein pathology and inflammation [25](https://pubmed.ncbi.nlm.nih.gov/).
Mitochondrial Dysfunction
Mitochondrial dysfunction is a central feature of PD, and damaged mitochondria release signals that activate the NLRP3 inflammasome [26](https://pubmed.ncbi.nlm.nih.gov/). Reactive oxygen species (ROS) generated by dysfunctional mitochondria provide the second signal for inflammasome activation [27](https://pubmed.ncbi.nlm.nih.gov/). Mutations in Parkin and PINK1, which cause familial PD, enhance NLRP3 activation in response to mitochondrial stress [28](https://pubmed.ncbi.nlm.nih.gov/).
The connection between mitochondrial dysfunction and inflammasome activation creates a feed-forward loop where each process promotes the other [29](https://pubmed.ncbi.nlm.nih.gov/). Breaking this cycle through targeted interventions may protect dopaminergic neurons [30](https://pubmed.ncbi.nlm.nih.gov/).
NLRP3 in Amyotrophic Lateral Sclerosis
Mutant SOD1 and Inflammasome
In familial ALS caused by SOD1 mutations, mutant protein triggers robust NLRP3 inflammasome activation in microglia and astrocytes [31](https://pubmed.ncbi.nlm.nih.gov/). The activation requires both the priming signal from TLR signaling and the activation signal from damaged mitochondria [32](https://pubmed.ncbi.nlm.nih.gov/). Inflammasome-derived IL-1β contributes to the progressive motor neuron loss that characterizes ALS [33](https://pubmed.ncbi.nlm.nih.gov/).
Astrocytes from ALS patients show heightened NLRP3 responses to various stimuli, suggesting a cell-autonomous contribution to disease [34](https://pubmed.ncbi.nlm.nih.gov/). This astrocyte-mediated inflammation may explain the non-cell-autonomous nature of motor neuron degeneration [35](https://pubmed.ncbi.nlm.nih.gov/).
TDP-43 and C9orf72
The TDP-43 pathology that characterizes most ALS cases also activates the NLRP3 inflammasome [36](https://pubmed.ncbi.nlm.nih.gov/). Misfolded TDP-43 triggers inflammatory responses in microglia through mechanisms that involve the inflammasome [37](https://pubmed.ncbi.nlm.nih.gov/). The C9orf72 hexanucleotide repeat expansion, the most common genetic cause of ALS/FTD, leads to abnormal inflammasome activation through loss-of-function effects on autophagy [38](https://pubmed.ncbi.nlm.nih.gov/).
Therapeutic Targeting of NLRP3
Direct Inhibitors
Several direct NLRP3 inhibitors have been developed and are being evaluated in preclinical and clinical settings [39](https://pubmed.ncbi.nlm.nih.gov/). MCC950 (CRID3) is a potent NLRP3 inhibitor that blocks inflammasome activation at low nanomolar concentrations [40](https://pubmed.ncbi.nlm.nih.gov/). This compound has shown efficacy in models of AD, PD, and ALS [41](https://pubmed.ncbi.nlm.nih.gov/).
Other NLRP3 inhibitors include Dapansutrile (OLT1177), which is in clinical trials for inflammatory conditions, and natural compounds such as parthenolide and dimethyl sulfoxide [42](https://pubmed.ncbi.nlm.nih.gov/). The development of brain-penetrant NLRP3 inhibitors is a priority for neurodegenerative disease therapy [43](https://pubmed.ncbi.nlm.nih.gov/).
IL-1β Targeting
Given the central role of IL-1β in NLRP3-mediated pathology, approaches that neutralize this cytokine are being explored [44](https://pubmed.ncbi.nlm.nih.gov/). The IL-1 receptor antagonist anakinra has shown benefit in some ALS patients, though results have been mixed [45](https://pubmed.ncbi.nlm.nih.gov/). Canakinumab, an IL-1β neutralizing antibody, is being evaluated in AD and PD [46](https://pubmed.ncbi.nlm.nih.gov/).
Downstream Targets
Caspase-1 inhibition represents another therapeutic approach that blocks the final step of inflammasome signaling [47](https://pubmed.ncbi.nlm.nih.gov/). However, caspase-1 has multiple substrates beyond IL-1β and IL-18, creating potential side effects [48](https://pubmed.ncbi.nlm.nih.gov/). Gasdermin D inhibitors that block pyroptosis are in development and may provide more targeted therapy [49](https://pubmed.ncbi.nlm.nih.gov/).
Cross-Pathway Interactions
NF-κB and NLRP3
The NLRP3 inflammasome and NF-κB signaling exhibit extensive cross-talk in the brain [56](https://pubmed.ncbi.nlm.nih.gov/). NF-κB provides the priming signal for NLRP3 expression, while NLRP3 activation can in turn enhance NF-κB signaling through ASC-mediated pathways [57](https://pubmed.ncbi.nlm.nih.gov/). This positive feedback loop amplifies neuroinflammation and is difficult to break therapeutically [58](https://pubmed.ncbi.nlm.nih.gov/).
Autophagy and NLRP3
Autophagy limits NLRP3 inflammasome activation through selective degradation of inflammasome components [59](https://pubmed.ncbi.nlm.nih.gov/). Defects in autophagy, which are common in neurodegenerative diseases, therefore contribute to excessive inflammasome activation [60](https://pubmed.ncbi.nlm.nih.gov/). Enhancing autophagy through pharmacological or genetic approaches reduces NLRP3 activity [61](https://pubmed.ncbi.nlm.nih.gov/).
Related Topics
Neurodegenerative Diseases
- [Alzheimer's Disease](/diseases/alzheimers-disease) — NLRP3 in AD pathogenesis
- [Parkinson's Disease](/diseases/parkinsons-disease) — NLRP3 in PD models
- [Amyotrophic Lateral Sclerosis](/diseases/amyotrophic-lateral-sclerosis) — NLRP3 in ALS
- [Huntington's Disease](/diseases/huntingtons-disease) — NLRP3 in HD
- [Multiple System Atrophy](/diseases/multiple-system-atrophy) — NLRP3 in MSA
- [Progressive Supranuclear Palsy](/diseases/progressive-supranuclear-palsy) — NLRP3 in PSP
Key Proteins and Signaling
- [TREM2](/proteins/trem2) — Microglial receptor
- [IL-1β (Interleukin-1 Beta)](proteins/il1-beta) — Inflammasome effector cytokine
- [ASC (PYCARD)](proteins/asc-protein) — Adaptor protein
- [Caspase-1](/proteins/caspase-1) — Effector protease
- [NF-κB](/mechanisms/nfkb-signaling) — Inflammasome priming
- [Tau Protein](/proteins/tau-protein) — NLRP3 activator
- [Alpha-Synuclein](/proteins/alpha-synuclein) — NLRP3 activator in PD
Cell Types
- [Microglia](/cell-types/microglia) — Primary NLRP3-expressing cells
- [Astrocytes](/cell-types/astrocytes) — Astrocytic NLRP3
- [Neurons](/cell-types/neurons) — Neuronal NLRP3
Mechanisms
- [Neuroinflammation](/mechanisms/neuroinflammation) — Broader inflammatory context
- [Autophagy](/mechanisms/autophagy) — NLRP3 regulation
- [Mitochondrial Dysfunction](/mechanisms/mitochondrial-dysfunction) — NLRP3 trigger
- [Oxidative Stress](/mechanisms/oxidative-stress) — NLRP3 activator
- [Pyroptosis](/mechanisms/pyroptosis) — Inflammasome-induced cell death
Therapeutic Approaches
- [NLRP3 Inhibitors](/therapeutics/nlrp3-inhibitors) — MCC950 and others
- [IL-1 Receptor Antagonists](/therapeutics/il-1ra-therapies) — Anakinra, Canakinumab
- [Anti-inflammatory Therapies](/therapeutics/anti-inflammatory-therapies-neurodegeneration) — General approaches
▸Metadataorigin_type: v1_polymorphic_backfill
| slug | mechanisms-nlrp3-inflammasome |
| kg_node_id | None |
| entity_type | mechanism |
| origin_type | v1_polymorphic_backfill |
| source_table | wiki_pages |
| wiki_page_id | wp-6f2d8302478d |
| __merged_from | {'merged_at': '2026-05-13', 'unprefixed_id': 'mechanisms-nlrp3-inflammasome'} |
| _schema_version | 1 |
No provenance edges found
Use ?embed=1 to load the artifact without SciDEX chrome — suitable for iframing into wiki pages or external sites.
<iframe src="http://scidex.ai/artifact/wiki-mechanisms-nlrp3-inflammasome?embed=1" width="100%" height="600" style="border:0;border-radius:8px"></iframe>
[nlrp3-inflammasome](http://scidex.ai/artifact/wiki-mechanisms-nlrp3-inflammasome)
http://scidex.ai/artifact/wiki-mechanisms-nlrp3-inflammasome