The NLRP3 inflammasome is released as a particulate danger signal that amplifies the inflammatory response
Open accessAbstract
Assembly of the NLRP3 inflammasome activates caspase-1 and mediates the processing and release of the leaderless cytokine IL-1β and thereby serves a central role in the inflammatory response and in diverse human diseases. Here we found that upon activation of caspase-1, oligomeric NLRP3 inflammasome particles were released from macrophages. Recombinant oligomeric protein particles composed of the adaptor ASC or the p.D303N mutant form of NLRP3 associated with cryopyrin-associated periodic syndromes (CAPS) stimulated further activation of caspase-1 extracellularly, as well as intracellularly after phagocytosis by surrounding macrophages. We found oligomeric ASC particles in the serum of patients with active CAPS but not in that of patients with other inherited autoinflammatory diseases. Our findings support a model whereby the NLRP3 inflammasome, acting as an extracellular oligomeric complex, amplifies the inflammatory response.
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ASC specks can be recognized by neighboring microglia as a danger signal and induce inflammatory responses including activation of the NLRP3 inflammasome, thereby propagating inflammation.
“They can also be recognized by neighboring microglia as a danger signal and induce inflammatory responses including activation of the NLRP3 inflammasome, thereby propagating inflammation [70–72].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [71]
NLRP3 inflammasome activity leads to extracellular release of ASC particles that may function as danger signals.
“In turn, NLRP3 inflammasome activity leads to the extracellular release of ASC particles that may function as danger signals (246).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [246]
Increased expression and activity of NLRP3 inflammasome machinery in circulating immune cells have been reported in patients with depression, bipolar disorder, and ASD.
“Increased expression and activity of the NLRP3 inflammasome machinery in circulating immune cells of patients affected by depression (245), bipolar disorder (246), and ASD (226), have been reported.”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [246]
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“Interestingly, the release of cellular content following pyroptosis includes the preformed prion-like ASC speck that can propagate inflammation by acting as a stable signalling platform for continued caspase-1 activation within the extracellular space [86,87].”
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Giorgi, C., Marchi, S., Simões, I. C. M., Ren, Z., Morciano, G., Perrone, M., Patalas‐Krawczyk, P., Borchard, S., Jędrak, P., Pierzynowska, K., et al. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.05.006 · Cited by 467 · see citing works
Dying cells actively regulate adaptive immune responses
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Immune mechanisms linked to depression via oxidative stress and neuroprogression
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Interleukin-1 Beta—A Friend or Foe in Malignancies?
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“Interestingly, in CAPS patients with mutated NLRP3, catalytically active extracellular NLRP3 inflammasomes were detected [79].”
BackgroundASC filament formation serves as a signal amplification mechanism for inflammasomes
Dick, M. S., Sborgi, L., Rühl, S., Hiller, S., & Brož, P. (2016) · Nature Communications · doi:10.1038/ncomms11929 · Cited by 405 · see citing works
Cryo-EM structure of the activated NAIP2-NLRC4 inflammasome reveals nucleated polymerization
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“Our data extend previous studies showing the detrimental inflammatory effects of inflammasome activation already during the earliest phases of ischemic stroke (Baroja-Mazo et al., 2014; Ismael et al., 2018).”
Mitochondria-associated membranes (MAMs) and inflammation
Missiroli, S., Patergnani, S., Caroccia, N., Pedriali, G., Perrone, M., Previati, M., Wieckowski, M. R., & Giorgi, C. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0027-2 · Cited by 389 · see citing works
Drugging the NLRP3 inflammasome: from signalling mechanisms to therapeutic targets
Walle, L. V., & Lamkanfi, M. (2023) · Nature Reviews Drug Discovery · doi:10.1038/s41573-023-00822-2 · Cited by 376 · see citing works
The Pyrin Inflammasome in Health and Disease
Schnappauf, O., Chae, J. J., Kastner, D. L., & Aksentijevich, I. A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01745 · Cited by 365 · see citing works
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“cytokines, extracellular ATP, extracellular oligomeric complex of NLRP3 inflammasome [112], circulating mitochondrial DNA [113], circulating microRNAs [114] and shuttles (e.”
BackgroundThe Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules
Wu, H., & Fuxreiter, M. (2016) · Cell · doi:10.1016/j.cell.2016.05.004 · Cited by 352 · see citing works
The NLRP3 inflammasome functions as a driver of the myelodysplastic syndrome phenotype
Basiorka, A. A., McGraw, K. L., Eksioglu, E. A., Chen, X., Johnson, J., Zhang, L., Zhang, Q., Irvine, B. A., Cluzeau, T., Sallman, D. A., et al. (2016) · Blood · doi:10.1182/blood-2016-07-730556 · Cited by 356 · see citing works
Programmed Necrosis in the Cross Talk of Cell Death and Inflammation
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“Interestingly, although the filamentous inflammasome complex is not amyloid in nature, it can apparently seed further polymerization reactions in neighboring cells as it is released from cells undergoing pyroptosis (126, 127).”
BackgroundSendler, M., van den Brandt, C., Glaubitz, J., Wilden, A., Golchert, J., Weiß, F. U., Homuth, G., Chama, L. L. D. F., Mishra, N., Mahajan, U. M., et al. (2019) · Gastroenterology · doi:10.1053/j.gastro.2019.09.040 · Cited by 352 · see citing works
Systemic inflammation impairs microglial Aβ clearance through NLRP3 inflammasome
Tejera, D., Mercan, D., Sanchez‐Caro, J. M., Hanan, M., Greenberg, D., Soreq, H., Latz, E., Golenbock, D., & Heneka, M. T. (2019) · The EMBO Journal · doi:10.15252/embj.2018101064 · Cited by 351 · see citing works
“The activation of the inflammasome and subsequent release of IL-1 b requires the adaptor protein ASC, which in turn leads to the recruitment of the effector caspase-1 (Baroja-Mazo et al , 2014).”
NLRP3 inflammasome activation triggers gasdermin D–independent inflammation
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SMOCs: supramolecular organizing centres that control innate immunity
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Neuroinflammation in Alzheimer’s Disease
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Inflammasomes in the gastrointestinal tract: infection, cancer and gut microbiota homeostasis
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“Cryoelectron microscopy analysis revealed that ASC and caspase 1 act in a prionoid-like fashion to form filamentous structures and catalyse formation of the inflammasome speck [59] [60] [61] [62] .”
BackgroundThe Inflammasomes and Autoinflammatory Syndromes
Broderick, L., Nardo, D. D., Franklin, B. S., Hoffman, H. M., & Latz, E. (2014) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012414-040431 · Cited by 296 · see citing works
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Streptococcus pneumoniae’s Virulence and Host Immunity: Aging, Diagnostics, and Prevention
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“ASC, the adapter protein for the NLRP3 inflammasome, forms spec-like structures and propagates in a “prionoid” fashion to propagate the inflammasome.(33,49) As expected, both rotenone and tebufenpyrad treatments led to the formation of ASC specs (Fig.”
BackgroundProtein kinase D at the Golgi controls NLRP3 inflammasome activation
Zhang, Z., Mészáros, G., He, W., Xu, Y., Magliarelli, H. D. F., Mailly, L., Mihlan, M., Liu, Y., Gámez, M. P., Goginashvili, A., et al. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20162040 · Cited by 279 · see citing works
“These mutations result in spontaneous self-oligomerization of the NLRP3 protein (Baroja-Mazo et al., 2014).”
BackgroundInflammasome-dependent IL-1β release depends upon membrane permeabilisation
Martín‐Sánchez, F., Diamond, C. E., Zeitler, M., Gomez, A. I., Baroja‐Mazo, A., Bagnall, J., Spiller, D. G., White, M. H., Daniels, M. J. D., Mortellaro, A., et al. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2015.176 · Cited by 279 · see citing works
“Caspase-1 activity is suggested as the main driver of a specific programme of cell death termed pyroptosis that is associated with the leakage of intracellular proteins, including the release of large inflammasome complexes.(33,34) Our data show that both mechanisms, membrane permeability and caspase-1 activity, are i…”
Backgroundde Jesus, A. A., Canna, S., Liu, Y., & Goldbach‐Mansky, R. T. (2015) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112227 · Cited by 277 · see citing works
“In stimulated macrophages or in macrophages carrying a NOMIDassociated NLRP3 mutation, inflammasome particles can be released into the serum, retain enzymatic activity in the extracellular environment, and, upon being phagocytosed by neighboring macrophages, transfer inflammasome activity to unstimulated/wild-type cel…”
BackgroundWhich cell death modality wins the contest for photodynamic therapy of cancer?
Mishchenko, T. A., Balalaeva, I. V., Gorokhova, A. A., Vedunova, M. V., & Krysko, D. V. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04851-4 · Cited by 290 · see citing works
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NLRP3: A promising therapeutic target for autoimmune diseases
Shen, H., Yang, Y., Meng, X. L., Luo, X., Li, X., Shuai, Z., Ye, D., & Pan, H. (2018) · Autoimmunity Reviews · doi:10.1016/j.autrev.2018.01.020 · Cited by 272 · see citing works
Spotlight on the NLRP3 inflammasome pathway
Groslambert, M., & Py, B. F. (2018) · Journal of Inflammation Research · doi:10.2147/jir.s141220 · Cited by 267 · see citing works
Urate‐induced immune programming: Consequences for gouty arthritis and hyperuricemia
Cabău, G., Crișan, T. O., Klück, V., Popp, R. A., & Joosten, L. A. B. (2019) · Immunological Reviews · doi:10.1111/imr.12833 · Cited by 262 · see citing works
Innate Immune Cell Death in Neuroinflammation and Alzheimer’s Disease
Rajesh, Y., & Kanneganti, T. (2022) · Cells · doi:10.3390/cells11121885 · Cited by 261 · see citing works
Fyn kinase regulates misfolded α-synuclein uptake and NLRP3 inflammasome activation in microglia
Panicker, N., Sarkar, S., Harischandra, D. S., Neal, M. P., Kam, T., Jin, H., Saminathan, H., Langley, M. R., Charli, A., Samidurai, M., et al. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20182191 · Cited by 255 · see citing works
Inflammasomes in Tissue Damages and Immune Disorders After Trauma
Bortolotti, P., Faure, E., & Kipnis, É. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01900 · Cited by 259 · see citing works
“inflammation After Trauma Both inflammasome-mediated pro-inflammatory mediator release and pyroptotic cell death contribute to initiating, enhancing, and propagating inflammation after trauma (30, 71).”
BackgroundOf Inflammasomes and Alarmins: IL-1β and IL-1α in Kidney Disease
Anders, H. (2016) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016020177 · Cited by 251 · see citing works
Mechanisms governing inflammasome activation, assembly and pyroptosis induction
Kesavardhana, S., & Kanneganti, T. (2017) · International Immunology · doi:10.1093/intimm/dxx018 · Cited by 254 · see citing works
Epicardial adipose tissue and cardiovascular diseases
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P2X7 receptor and the NLRP3 inflammasome: Partners in crime
Pelegrı́n, P. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114385 · Cited by 241 · see citing works
An Update on Inflammation in the Acute Phase of Intracerebral Hemorrhage
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“For the upstream of those inflammatory molecules, inflammasomes are intracellular protein complexes that play an important role in regulating inflammation [16].”
Inflammasome‐associated cell death: Pyroptosis, apoptosis, and physiological implications
Tsuchiya, K. (2020) · Microbiology and Immunology · doi:10.1111/1348-0421.12771 · Cited by 238 · see citing works
“Extracellular ASC specks may be taken up by phagocytes, in which the aggregates may activate caspase‐1 to sustain and spread inflammation, indicating a role for calpains in the propagation of inflammasome responses.(45) By contrast, the influx of Ca due to plasma membrane damage also activates membrane repair programs…”
BackgroundThe NLRP3 and Pyrin Inflammasomes: Implications in the Pathophysiology of Autoinflammatory Diseases
de Torre‐Minguela, C., Mesa-del-Castillo, P., & Pelegrı́n, P. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00043 · Cited by 239 · see citing works
“Mutant NLRP3 drives a constitutive hyperactivity of inflammasome, activation of caspase-1, and an excessive unregulated release of IL-1β, although systemic circulating levels of IL-1β during inflammatory flares are in most cases undetectable (11, 147).”
BackgroundTargeting Neuroinflammation to Treat Alzheimer’s Disease
Ardura-Fabregat, A., Boddeke, E., Boza‐Serrano, A., Brioschi, S., Castro‐Gomez, S., Ceyzériat, K., Dansokho, C., Dierkes, T., Gelders, G., Heneka, M. T., et al. (2017) · CNS Drugs · doi:10.1007/s40263-017-0483-3 · Cited by 236 · see citing works
Martínez-García, J. J., Martínez-Banaclocha, H., Angosto-Bazarra, D., de Torre-Minguela, C., Baroja-Mazo, A., Alarcón-Vila, C., Martínez-Alarcón, L., Amores-Iniesta, J., Martín-Sánchez, F., Ercole, G. A., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10626-x · Cited by 233 · see citing works
Targeting Microglial α-Synuclein/TLRs/NF-kappaB/NLRP3 Inflammasome Axis in Parkinson’s Disease
Li, Y., Xia, Y., Yin, S., Wan, F., Hu, J., Kou, L., Sun, Y., Wu, J., Zhou, Q., Huang, J., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.719807 · Cited by 230 · see citing works
Caspase-8 as an Effector and Regulator of NLRP3 Inflammasome Signaling
Antonopoulos, C. H., Russo, H. M., Sanadi, C. E. E., Martin, B. N., Li, X., Kaiser, W. J., Mocarski, E. S., & Dubyak, G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.652321 · Cited by 225 · see citing works
“An alternative mechanism for the delayed propidium2 uptake in Casp1/11 / DC AUGUST 14, 2015 • VOLUME 290 • NUMBER 33 JOURNAL OF BIOLOGICAL CHEMISTRY 20181 may involve a canonical caspase-8-driven apoptotic cascade that facilitates caspase-3-mediated proteolytic gating of pannexin-1 channels that are also expressed in…”
BackgroundInfluentialThe NLRP3 inflammasome is activated by nanoparticles through ATP, ADP and adenosine
Baron, L., Gombault, A., Fanny, M., Villeret, B., Savigny, F., Guillou, N., Panek, C., Bert, M. L., Lagente, V., Rassendren, F., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2014.576 · Cited by 221 · see citing works
Structural mechanisms of inflammasome assembly
Lu, A. Z., & Wu, H. (2014) · FEBS Journal · doi:10.1111/febs.13133 · Cited by 219 · see citing works
Beclin1‐driven autophagy modulates the inflammatory response of microglia via NLRP3
Houtman, J., Freitag, K., Gimber, N., Schmoranzer, J., Heppner, F. L., & Jendrach, M. (2019) · The EMBO Journal · doi:10.15252/embj.201899430 · Cited by 212 · see citing works
Microglial PGC-1α protects against ischemic brain injury by suppressing neuroinflammation
Han, B., Jiang, W., Cui, P., Zheng, K., Dang, C., Wang, J., Li, H., Chen, L., Zhang, R., Wang, Q. M., et al. (2021) · Genome Medicine · doi:10.1186/s13073-021-00863-5 · Cited by 208 · see citing works
“Previous studies have suggested that the NLRP3 inflammasome plays a crucial role in amplifying the inflammatory response [28].”
BackgroundCathepsin B Is Required for NLRP3 Inflammasome Activation in Macrophages, Through NLRP3 Interaction
Chevriaux, A., Pilot, T., Dérangère, V., Simonin, H., Martine, P., Chalmin, F., Ghiringhelli, F., & Rébé, C. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00167 · Cited by 202 · see citing works
“Once constituted, the NLRP3 inflammasome is then secreted in cell supernantant and can amplify the inflammatory response by activating inflammasomes and caspase-1 in neighboring cells (Baroja-Mazo et al., 2014; Franklin et al., 2014).”
BackgroundBiological and clinical roles of IL-18 in inflammatory diseases
Landy, E., Carol, H. A., Ring, A. M., & Canna, S. (2023) · Nature Reviews Rheumatology · doi:10.1038/s41584-023-01053-w · Cited by 206 · see citing works
“macrophages 38,39 .”
Systemic autoinflammatory diseases
Krainer, J., Siebenhandl, S., & Weinhaeusel, A. (2020) · Journal of Autoimmunity · doi:10.1016/j.jaut.2020.102421 · Cited by 177 · see citing works
The role of IL-1B in breast cancer bone metastasis
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Chloride regulates dynamic NLRP3-dependent ASC oligomerization and inflammasome priming
Green, J., Yu, S., Martín‐Sánchez, F., Pelegrı́n, P., López‐Castejón, G., Lawrence, C. B., & Brough, D. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1812744115 · Cited by 191 · see citing works
“The inflammasome specks released from pyroptotic cells can also further contribute to inflammatory responses (10, 11).”
BackgroundResponse of host inflammasomes to viral infection
Chen, I.-Y., & Ichinohe, T. (2014) · Trends in Microbiology · doi:10.1016/j.tim.2014.09.007 · Cited by 189 · see citing works
β-amyloid, microglia, and the inflammasome in Alzheimer’s disease
Gold, M., & El Khoury, J. (2015) · Seminars in Immunopathology · doi:10.1007/s00281-015-0518-0 · Cited by 187 · see citing works
Molecular mechanisms of inflammasome signaling
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Inflammatory outcomes of apoptosis, necrosis and necroptosis
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“5 / 21 addition to mature IL-1β, whole inflammasome particles are released in response to agents that promote maturation of this cytokine (Baroja-Mazo et al., 2014; Franklin et al., 2014), which is consistent with the interpretation that cell death is a primary driver of IL-1β release.”
BackgroundMünzer, P., Negro, R., Fukui, S., Meglio, L. D., Aymonnier, K., Chu, L., Cherpokova, D., Gutch, S., Sorvillo, N., Shi, L. S., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.683803 · Cited by 186 · see citing works
“Indeed, ASC has been described as a “prionoid”, that, when phagocytosed by macrophages, induce inflammasome assembly (27, 71, 72).”
BackgroundGomez‐Lopez, N., Galaz, J., Miller, D., Farías, M., Liu, Z., Arenas‐Hernandez, M., Garcia‐Flores, V., Shaffer, Z., Greenberg, J. M., Theis, K. R., et al. (2022) · Reproduction · doi:10.1530/rep-22-0046 · Cited by 186 · see citing works
Integrated NLRP3, AIM2, NLRC4, Pyrin inflammasome activation and assembly drive PANoptosis
Oh, S., Lee, J., Oh, J.-E., Yu, G., Ryu, H., Kim, D., & Lee, S. (2023) · Cellular and Molecular Immunology · doi:10.1038/s41423-023-01107-9 · Cited by 188 · see citing works
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“Recently, it has been shown that in mouse bone-marrowderived macrophages (BMDMs), the activation of inflammasomes resulted in the extracellular release of active inflammasome oligomers as particles that acted extracellularly as danger signals to amplify the inflammatory response by activating caspase-1 [45].”
BackgroundPost-ischemic inflammation regulates neural damage and protection
Shichita, T., Ito, M., & Yoshimura, A. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00319 · Cited by 184 · see citing works
Poh, L., Kang, S.-W., Baik, S., Ng, G. Y. Q., She, D. T., Balaganapathy, P., Dheen, S. T., Magnus, T. U., Gelderblom, M., Sobey, C. G., et al. (2018) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2018.09.001 · Cited by 184 · see citing works
Nanobodies that block gating of the P2X7 ion channel ameliorate inflammation
Danquah, W., Meyer‐Schwesinger, C., Rissiek, B., Pinto, C., Prat, A. S., Amadi, M., Iacenda, D., Knop, J., Hammel, A., Bergmann, P., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf8463 · Cited by 182 · see citing works
Ferulic acid inhibits neuro-inflammation in mice exposed to chronic unpredictable mild stress
Liu, Y., Shen, J.-D., Xu, L., Li, H., Li, Y., & Yi, L. (2017) · International Immunopharmacology · doi:10.1016/j.intimp.2017.02.007 · Cited by 184 · see citing works
“NLRP3 inflammasome, the best characterized inflammasome, mediates the processing and release of the leaderless cytokine IL-1β and thereby amplifies the inflammatory response [35].”
BackgroundAmores, J., Barberà-Cremades, M., Martínez, C. M., Pons, J. A., Revilla‐Nuin, B., Martínez-Alarcón, L., Virgilio, F. D., Parrilla, P., Baroja‐Mazo, A., & Pelegrı́n, P. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.11.079 · Cited by 181 · see citing works
“BMDM were obtained from wild-type or P2rx7-/- mice using 25% of L-cell conditioned media as previously described (Baroja-Mazo et al., 2014). pmeLuc cells were maintained in DMEM:F12 (1:1) supplemented with 10% foetal calf serum (FCS), 2mM glutamax 1% and G418 0.2 mg/ml (Acros Organic).”
MethodInfluential
- Authors
- Baroja-Mazo, A., Martín-Sánchez, F., Gomez, A. I., Martínez, C. M., Amores-Iniesta, J., Compan, V., Barberà-Cremades, M., Yagüe, J., Ruiz-Ortiz, E., Antón, J., Buján, S., Couillin, I., Brough, D., Arostegui, J. I., & Pelegrín, P.
- Affiliations
- Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas (ES)
- University of Manchester (GB)
- Hospital Clínic de Barcelona (ES)
- Hospital Sant Joan de Déu Barcelona (ES)
- Vall d'Hebron Hospital Universitari (ES)
- Université d'Orléans (FR)
- ORCID
- Venue
- Nature Immunology
- Published
- 2014-06-22
- Volume
- 15
- Issue
- 8
- Pages
- 738-748
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- OpenAlex
- W2143119237
- Cited by
- 790
- References
- 50
- Citations by year
- 2026: 28 · 2025: 39 · 2024: 41 · 2023: 63 · 2022: 81 · 2021: 84 · 2020: 86 · 2019: 68 · 2018: 74 · 2017: 88 · 2016: 60 · 2015: 57 · 2014: 20
- FWCI
- 30.77
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- cc-by-nc-nd
- www.springer.com/tdm (tdm)
- Locations
- Nature Immunology (publishedVersion)
- PubMed (publishedVersion)
- Hispana (publishedVersion, cc-by-nc-nd)
- Research Explorer (The University of Manchester) (submittedVersion)
- Funders
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Health Sciences › Medicine › Hematology › Autoimmune and Inflammatory Disorders Research
- Keywords
- NLRP3 inflammasome, caspase-1, IL-1β processing, cryopyrin-associated periodic syndromes, macrophages, autoinflammatory disease, phagocytosis
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Carrier Proteins, Cells, Cultured, Cytoskeletal Proteins, Humans, Inflammation, Macrophages, Mice, Inbred C57BL, Phagocytosis, Signal Transduction, Mice, Knockout, Caspases, Caspase 1, Apoptosis Regulatory Proteins, Mice, CARD Signaling Adaptor Proteins, Caspases, Initiator, Interleukin-1beta, Cryopyrin-Associated Periodic Syndromes, HEK293 Cells, Inflammasomes
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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