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The NALP3 inflammasome is involved in the innate immune response to amyloid-β
Open accessAbstract
The fibrillar peptide amyloid-beta (A beta) has a chief function in the pathogenesis of Alzheimer's disease. Interleukin 1 beta (IL-1 beta) is a key cytokine in the inflammatory response to A beta. Insoluble materials such as crystals activate the inflammasome formed by the cytoplasmic receptor NALP3, which results in the release of IL-1 beta. Here we identify the NALP3 inflammasome as a sensor of A beta in a process involving the phagocytosis of A beta and subsequent lysosomal damage and release of cathepsin B. Furthermore, the IL-1 beta pathway was essential for the microglial synthesis of proinflammatory and neurotoxic factors, and the inflammasome, caspase-1 and IL-1 beta were critical for the recruitment of microglia to exogenous A beta in the brain. Our findings suggest that activation of the NALP3 inflammasome is important for inflammation and tissue damage in Alzheimer's disease.
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“Based on the previous literature42,43,46, we reasoned that cathepsin B leaking from the destabilized lysosomes may mediate the NLRP3 inflammasome activation upon SHIP1 inhibition11.”
From INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia (2025) · cites this paper as [43]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Fibrillar Aβ (fAβ), following phagocytosis by microglia, activates the NLRP3 inflammasome and leads to increases in secretion of IL-1β and IL-18.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [78]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Sustained elevations of IL-1β have been postulated to play a key role in AD pathogenesis [6, 12–14].”
From 25-Hydroxycholesterol amplifies microglial IL-1β production in an apoE isoform-dependent manner (2020) · cites this paper as [13]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Halle et al. found that fibrillar Aβ can induce the secretion of IL-1β which depends on the presence of NLRP3.352,353”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [352]
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In the citing paper
“lysosomal cathepsins, such as cathepsin B, can induce NLRP3 inflammasome activation upon leaking into the cytosol following lysosomal membrane permeabilization (LMP)42,43”
From INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia (2025) · cites this paper as [43]
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“fAβ phagocytosis results in lysosomal dysfunction and release of lysosomal contents into the cytoplasm, including the lysosomal protease cathepsin B, which is a mediator of inflammasome activation induced by Aβ [78].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [78]
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In the citing paper
“In line with these findings, another study showed that aggregated tau seeds activated the NLRP3 inflammasome in primary mouse microglia by inducing lysosomal destabilization and release of the lysosomal protease cathepsin B, similar to fAβ [78, 82].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [78]
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“In parallel, reduction of SHIP1 activity is poised to disinhibit signaling pathways that are involved in the phagocytosis of Aβ, which is a required step for Aβ-induced activation of the NLRP3 inflammasome [78].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [78]
In the citing paper
“Notably, Aβ also can activate NF-κB signaling and the NLRP3-ASC inflammasome [426, 427], suggesting that Aβ and tau share common mechanisms in microglia activation.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [426]
In the citing paper
“Following phagocytosis by microglia, Aβ activates the NLRP3 inflammasome leading to caspase-1 activation and IL-1β maturation and release (Halle et al., 2008).”
From Alzheimer Disease: An Update on Pathobiology and Treatment Strategies (2019) · cites this paper as Halle et al., 2008
In the citing paper
“Fibrillar Aβ amyloids can induce the secretion of IL-1β from microglia, via the NLRP3 inflammasome (228, 249).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [228]
In the citing paper
“Importantly, researchers also found that ASC-, caspase-1-, IL-1 receptor-, and MyD88-deficient mice had less recruitment of microglia and mononuclear phagocytes to Aβ in the brain as compared to the wild type control after the injection of Aβ into the striatum (228).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [228]
In the citing paper
“NLRP3 has been shown to respond to sterile stimuli, including asbestos, silica, MSU and CPPD crystals55, cholesterol crystals and β-amyloid fibrils56.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [56]
In the citing paper
“Furthermore, there is only partial inhibition of the neutrophil infiltration and IL-1β production associated with sterile inflammation in response to cholesterol crystals44,56,59,67.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [56]
In the citing paper
“However, cathepsin b-deficient macrophages have no impairment in IL-1β production in response to certain NLRP3 agonists, including LPS plus ATP, or MSU crystals, despite the impairment in their response to silica44,56,59,67.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [56]
In the citing paper
“evidence to support this are the observations that artificial lysosomal rupture alone can activate NLRP3 and that pharmacological inhibition or genetic depletion of cathepsin b results in inhibition of caspase 1 activation, although this inhibition was only partial44,56,59.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [56]
In the citing paper
“In support of this, direct treatment of ATP on primed microglia is sufficient for maturation and release of IL-1β in vitro (Halle et al, 2008) and does so via the P2X 7 receptor (Colomar et al, 2003) expressed on microglia (Monif et al, 2009).”
From Repeated Social Defeat, Neuroinflammation, and Behavior: Monocytes Carry the Signal (2017) · cites this paper as Halle et al, 2008
In the citing paper
“In particular, microglial NLRP3 has been shown to be a major driver of amyloid beta and tau toxicity in AD, suggesting its activation has important implications for disease progression (Halle et al, 2008; Venegas et al, 2017; Ising et al, 2019).”
From Mechanisms of DNA damage-mediated neurotoxicity in neurodegenerative disease (2022) · cites this paper as Halle et al, 2008
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Gout-associated uric acid crystals activate the NALP3 inflammasome
Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., & Tschopp, J. (2006) · Nature · doi:10.1038/nature04516 · Cited by 5,326
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160
Cryopyrin activates the inflammasome in response to toxins and ATP
Mariathasan, S., Weiss, D. S., Newton, K., McBride, J., O'Rourke, K., Roose-Girma, M., Lee, W. P., Weinrauch, Y., Monack, D. M., & Dixit, V. M. (2006) · Nature · doi:10.1038/nature04515 · Cited by 3,080
Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica
Dostert, C., Pétrilli, V., Van Bruggen, R., Steele, C., Mossman, B. T., & Tschopp, J. (2008) · Science · doi:10.1126/science.1156995 · Cited by 2,658
Germline Transmission and Tissue-Specific Expression of Transgenes Delivered by Lentiviral Vectors
Lois, C., Hong, E. J., Pease, S., Brown, E. J., & Baltimore, D. (2002) · Science · doi:10.1126/science.1067081 · Cited by 1,992
Brain interleukin 1 and S-100 immunoreactivity are elevated in Down syndrome and Alzheimer disease.
Griffin, W. S., Stanley, L. C., Ling, C., White, L., MacLeod, V, Perrot, L. J., White, C. L., & Araoz, C. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.19.7611 · Cited by 1,777
Agostini, L., Martinon, F., Burns, K., McDermott, M. F., Hawkins, P. N., & Tschopp, J. (2004) · Immunity · doi:10.1016/s1074-7613(04)00046-9 · Cited by 1,768
Altered Cytokine Export and Apoptosis in Mice Deficient in Interleukin-1β Converting Enzyme
Kuida, K., Lippke, J. A., Ku, G., Harding, M. W., Livingston, D. J., Su, M. S. S., & Flavell, R. A. (1995) · Science · doi:10.1126/science.7535475 · Cited by 1,631
A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
Weggen, S., Eriksen, J. L., Das, P., Sagi, S. A., Wang, R., Pietrzik, C. U., Findlay, K. A., Smith, T. E., Murphy, M. P., Bulter, T., et al. (2001) · Nature · doi:10.1038/35102591 · Cited by 1,388
Simard, A. R., Soulet, D., Gowing, G., Julien, J.-P., & Rivest, S. (2006) · Neuron · doi:10.1016/j.neuron.2006.01.022 · Cited by 1,265
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ATP release and purinergic signaling in NLRP3 inflammasome activation
Gombault, A., Baron, L., & Couillin, I. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00414 · Cited by 326
Mechanisms of interleukin-1β release
Eder, C. (2009) · Immunobiology · doi:10.1016/j.imbio.2008.11.007 · Cited by 317
Neuroinflammation in Alzheimer’s Disease
Onyango, I. G., Jauregui, G. V., Čarná, M., Bennett, J. P., & Stokin, G. B. (2021) · Biomedicines · doi:10.3390/biomedicines9050524 · Cited by 330
The IL-1β phenomena in neuroinflammatory diseases
Mendiola, A. S., & Cardona, A. E. (2017) · Journal of Neural Transmission · doi:10.1007/s00702-017-1732-9 · Cited by 328
The effects of microglia-associated neuroinflammation on Alzheimer’s disease
Wang, C., Zong, S., Cui, X., Wang, X., Wu, S., Wang, L., Liu, Y., & Lu, Z. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1117172 · Cited by 331
The role of inflammasomes in kidney disease
Komada, T., & Muruve, D. A. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0158-z · Cited by 317
Trimethylamine-N-Oxide Instigates NLRP3 Inflammasome Activation and Endothelial Dysfunction
Boini, K. M., Hussain, T., Li, P.-L., & Koka, S. S. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000484623 · Cited by 302
Salminen, A., Ojala, J. O., Kaarniranta, K., & Kauppinen, A. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-0962-0 · Cited by 308
Microglia actions in Alzheimer's disease
Prokop, S., Miller, K. R., & Heppner, F. L. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1182-x · Cited by 291
The NLRP3 inflammasome in pathogenic particle and fibre-associated lung inflammation and diseases
Sayan, M., & Mossman, B. T. (2015) · Particle and Fibre Toxicology · doi:10.1186/s12989-016-0162-4 · Cited by 308
Nanoparticle-Based Vaccines Against Respiratory Viruses
Soultan, A. H., Gauthier, L., Arpin, D., Bourgault, S., & Archambault, D. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00022 · Cited by 304
Lonnemann, N., Hosseini, S., Marchetti, C., Skouras, D. B., Stefanoni, D., D’Alessandro, A., Dinarello, C. A., & Korte, M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009680117 · Cited by 298
Critical functions of priming and lysosomal damage for NLRP3 activation
Hornung, V., & Latz, E. (2010) · European Journal of Immunology · doi:10.1002/eji.200940185 · Cited by 297
Self-citationEmerging roles of innate and adaptive immunity in Alzheimer’s disease
Chen, X., & Holtzman, D. M. (2022) · Immunity · doi:10.1016/j.immuni.2022.10.016 · Cited by 297
Alzheimer’s disease: pathological mechanisms and the beneficial role of melatonin
Rosales‐Corral, S., Acuña-Castroviejo, D., Coto‐Montes, A. M., Boga, J. A., Manchester, L. C., Fuentes‐Broto, L., Korkmaz, A., Ma, S., Tan, D. X., & Reiter, R. J. (2011) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2011.00937.x · Cited by 299
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Haneklaus, M., & O'Neill, L. A. J. (2015) · Immunological Reviews · doi:10.1111/imr.12285 · Cited by 296
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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 304
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Fusco, R., Siracusa, R., Genovese, T., Cuzzocrea, S., & Paola, R. D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124223 · Cited by 301
Lopez‐Rodriguez, A. B., Hennessy, E., Murray, C. L., Nazmi, A., Delaney, H. J., Healy, D., Fagan, S. G., Rooney, M., Stewart, E., Lewis, A., et al. (2021) · Alzheimer's & Dementia · doi:10.1002/alz.12341 · Cited by 293
Tseng, W. A., Thein, T., Kinnunen, K., Lashkari, K., Gregory, M. S., D'Amore, P. A., & Ksander, B. R. (2012) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.12-10655 · Cited by 295
The amyloid cascade hypothesis: an updated critical review
Kepp, K. P., Robakis, N. K. R. K., Høilund‐Carlsen, P. F., Sensi, S. L., & Vissel, B. (2023) · Brain · doi:10.1093/brain/awad159 · Cited by 315
The dual roles of cytokines in Alzheimer’s disease: update on interleukins, TNF-α, TGF-β and IFN-γ
Zheng, C., Zhou, X.-W., & Wang, J.-Z. (2016) · Translational Neurodegeneration · doi:10.1186/s40035-016-0054-4 · Cited by 292
Freeman, D., Cedillos, R., Choyke, S., Lukic, Z., McGuire, K., Marvin, S., Burrage, A. M., Sudholt, S., Rana, A., O'Connor, C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062143 · Cited by 289
Lam, S. M., Zhang, C., Wang, Z., Zhen, N., Zhang, S., Yang, S., Huang, X., Mo, L., Li, J., Lee, B. T. K., et al. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00425-4 · Cited by 285
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Schartz, N. D., & Tenner, A. J. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-02024-8 · Cited by 298
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Feldman, N., Rotter-Maskowitz, A., & Okun, E. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.01.003 · Cited by 283
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Kufer, T. A., & Sansonetti, P. J. (2011) · Nature Immunology · doi:10.1038/ni.1985 · Cited by 297
Rosin, D. L., & Okusa, M. D. (2011) · Journal of the American Society of Nephrology · doi:10.1681/asn.2010040430 · Cited by 292
Sarkar, S., Malovic, E., Harischandra, D. S., Ghaisas, S., Panicker, N., Charli, A., Palanisamy, B. N., Rokad, D., Jin, H., Anantharam, V., et al. (2017) · npj Parkinson s Disease · doi:10.1038/s41531-017-0032-2 · Cited by 288
Lee, H. J., Lee, J. K., Lee, H.-W., Carter, J., Chang, J. W., Oh, W., Yang, Y. S., Suh, J., Lee, B., Jin, H. K., et al. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.03.024 · Cited by 291
Krishnan, S. M., Ling, Y. H., Huuskes, B. M., Ferens, D. M., Saini, N., Chan, C. T., Diep, H., Kett, M. M., Samuel, C. S., Kemp‐Harper, B. K., et al. (2018) · Cardiovascular Research · doi:10.1093/cvr/cvy252 · Cited by 287
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Weber, M. D., Godbout, J. P., & Sheridan, J. F. (2017) · Neuropsychopharmacology · doi:10.1038/npp.2016.102 · Cited by 283
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Leemans, J. C., Cassel, S. L., & Sutterwala, F. S. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01043.x · Cited by 281
Drivers of age‐related inflammation and strategies for healthspan extension
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Liu, H., Li, W., Chen, Z.-R., Hu, Y.-C., Zhang, D.-D., Shen, W., Zhou, M., Zhu, L., & Hang, C. (2013) · Neurochemical Research · doi:10.1007/s11064-013-1115-z · Cited by 276
Shimada, T., Park, B. G., Wolf, A. J., Brikos, C., Goodridge, H. S., Becker, C. A., Reyes, C. N., Miao, E. A., Aderem, A., Götz, F., et al. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2009.12.008 · Cited by 274
Microglia in Alzheimer Disease: Well-Known Targets and New Opportunities
Hemonnot, A.-L., Hua, J., Ulmann, L., & Hirbec, H. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00233 · Cited by 298
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Saxena, M., & Yeretssian, G. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00327 · Cited by 282
He, Y., Varadarajan, S., Muñoz-Planillo, R., Burberry, A., Nakamura, Y., & Núñez, G. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.515080 · Cited by 275
AIM2 and NLRC4 inflammasomes contribute with ASC to acute brain injury independently of NLRP3
Dénes, Á., Coutts, G., Lénárt, N., Cruickshank, S. M., Pelegrín, P., Skinner, J., Rothwell, N. J., Allan, S. M., & Brough, D. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419090112 · Cited by 277
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Orlowski, G. M., Colbert, J. D., Sharma, S., Bogyo, M., Robertson, S. A., & Rock, K. L. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1500509 · Cited by 268
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Dénes, Á., López‐Castejón, G., & Brough, D. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.86 · Cited by 274
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Busillo, J. M., Azzam, K. M., & Cidlowski, J. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.275370 · Cited by 264
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Self-citationBuck, M. D., Gouwy, M., Wang, J., Snick, J. V., Opdenakker, G., Struyf, S., & Damme, J. V. (2016) · Current Medicinal Chemistry · doi:10.2174/0929867323666160418114600 · Cited by 248
Ma, Q. (2023) · Pharmacological Reviews · doi:10.1124/pharmrev.122.000629 · Cited by 260
Niemi, K., Teirilä, L., Lappalainen, J., Rajamäki, K., Baumann, M. H., Öörni, K., Wolff, H., Kovanen, P. T., Matikainen, S., & Eklund, K. K. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002843 · Cited by 298
Ritter, M., Gross, O., Kays, S., Ruland, J., Nimmerjahn, F., Saijo, S., Tschopp, J., Layland, L. E., & Prazeres da Costa, C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010337107 · Cited by 243
Retinal microglia – A key player in healthy and diseased retina
Rathnasamy, G., Foulds, W. S., Ling, E., & Kaur, C. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.05.006 · Cited by 250
Zamyatina, A., & Heine, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.585146 · Cited by 254
Wu, Z., Ni, J., Liu, Y., Teeling, J. L., Takayama, F., Collcutt, A. W., Ibbett, P., & Nakanishi, H. (2017) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2017.06.002 · Cited by 246
Regulation of NLRP3 Inflammasome by Phosphorylation
Song, N., & Li, T. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02305 · Cited by 239
Serum Amyloid A Activates the NLRP3 Inflammasome and Promotes Th17 Allergic Asthma in Mice
Ather, J. L., Ckless, K., Martin, R., Foley, K. L., Suratt, B. T., Boyson, J. E., Fitzgerald, K. A., Flavell, R. A., Eisenbarth, S. C., & Poynter, M. E. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100500 · Cited by 245
Self-citationNLRP3 Inflammasome Inhibitor Ameliorates Amyloid Pathology in a Mouse Model of Alzheimer’s Disease
Yin, J., Zhao, F., Chojnacki, J. E., Fulp, J., Klein, W. L., Zhang, S., & Zhu, X. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0467-9 · Cited by 244
Orchestration of NLRP3 Inflammasome Activation by Ion Fluxes
Gong, T., Yang, Y., Jin, T., Jiang, W., & Zhou, R. (2018) · Trends in Immunology · doi:10.1016/j.it.2018.01.009 · Cited by 249
Wang, W., Hu, D., Feng, Y., Wu, J., Li, A., Wang, Y., Cheng, K., Tian, M., Xiao, F., Zhang, Q., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008335 · Cited by 240
Danger-associated molecular patterns in Alzheimer’s disease
Venegas, C., & Heneka, M. T. (2017) · Journal of Leukocyte Biology · doi:10.1189/jlb.3mr0416-204r · Cited by 236
Caspase-1 Inflammasome Activation Mediates Homocysteine-Induced Pyrop-Apoptosis in Endothelial Cells
Xi, H., Zhang, Y., Xu, Y., Yang, W. Y., Jiang, X., Sha, X., Cheng, X., Wang, J., Qin, X., Yu, J., et al. (2016) · Circulation Research · doi:10.1161/circresaha.116.308501 · Cited by 234
Wang, D., Zhang, J., Jiang, W., Cao, Z., Zhao, F., Cai, T., Aschner, M., & Luo, W. (2017) · Autophagy · doi:10.1080/15548627.2017.1293766 · Cited by 236
The Role of Microglia and the Nlrp3 Inflammasome in Alzheimer's Disease
Hanslik, K. L., & Ulland, T. K. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.570711 · Cited by 236
Detection and Clearance of Damaged Lysosomes by the Endo-Lysosomal Damage Response and Lysophagy
Papadopoulos, C., & Meyer, H. (2017) · Current Biology · doi:10.1016/j.cub.2017.11.012 · Cited by 230
Sensing pathogens and danger signals by the inflammasome
Pedra, J. H., Cassel, S. L., & Sutterwala, F. S. (2009) · Current Opinion in Immunology · doi:10.1016/j.coi.2009.01.006 · Cited by 233
Unleashing the therapeutic potential of NOD-like receptors
Geddes, K., Magalhaes, J. G., & Girardin, S. E. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2783 · Cited by 242
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Shaw, P. J., McDermott, M., & Kanneganti, T. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.11.001 · Cited by 240
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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 241
The roles of TNF in brain dysfunction and disease
Clark, I. A., Alleva, L. M., & Vissel, B. (2010) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2010.08.007 · Cited by 239
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Thériault, P., ElAli, A., & Rivest, S. (2015) · Alzheimer s Research & Therapy · doi:10.1186/s13195-015-0125-2 · Cited by 237
Parajuli, B., Sonobe, Y., Horiuchi, H., Takeuchi, H., Mizuno, T., & Suzumura, A. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.503 · Cited by 232
Rapid inflammasome activation in microglia contributes to brain disease in HIV/AIDS
Walsh, J. G., Reinke, S. N., Mamik, M. K., McKenzie, B., Maingat, F. G., Branton, W. G., Broadhurst, D., & Power, C. (2014) · Retrovirology · doi:10.1186/1742-4690-11-35 · Cited by 236
Exosome-inflammasome crosstalk and their roles in inflammatory responses
Noonin, C., & Thongboonkerd, V. (2021) · Theranostics · doi:10.7150/thno.54004 · Cited by 234
Inflammasomes as therapeutic targets in human diseases
Li, Y., Huang, H., Liu, B., Zhang, Y. L., Pan, X., Yu, X., Shen, Z., & Song, Y. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00650-z · Cited by 238
Insulin Resistance and Diabetes Mellitus in Alzheimer’s Disease
Burillo, J., Marqués, P., Jiménez, B., González-Blanco, C., Benito, M., & Guillén, C. (2021) · Cells · doi:10.3390/cells10051236 · Cited by 246
Marchesi, V. T. (2011) · The FASEB Journal · doi:10.1096/fj.11-0102ufm · Cited by 232
The NLRP3 inflammasome in traumatic brain injury: potential as a biomarker and therapeutic target
O’Brien, W. T., Pham, L., Symons, G. F., Monif, M., Shultz, S. R., & McDonald, S. J. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01778-5 · Cited by 233
The Caspase-1 Inflammasome: A Pilot of Innate Immune Responses
Yu, H. B., & Finlay, B. B. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.08.007 · Cited by 229
An Overview of in vitro Methods to Study Microglia
Timmerman, R., Burm, S. M., & Bajramovic, J. J. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00242 · Cited by 243
Innate and adaptive immune responses to cell death
Rock, K. L., Lai, J., & Kono, H. (2011) · Immunological Reviews · doi:10.1111/j.1600-065x.2011.01040.x · Cited by 226
Liu, W., Yin, Y., Zhou, Z., He, M. Y., & Dai, Y. (2013) · Inflammation Research · doi:10.1007/s00011-013-0667-3 · Cited by 223
Bonham, K. S., Orzalli, M. H., Hayashi, K., Wolf, A. I., Glanemann, C., Weninger, W., Iwasaki, A., Knipe, D. M., & Kagan, J. C. (2014) · Cell · doi:10.1016/j.cell.2014.01.019 · Cited by 232
Sibley, C. H., Plass, N., Snow, J., Wiggs, E. A., Brewer, C. C., King, K. A., Zalewski, C. K., Kim, H. J., Bishop, R. J., Hill, S. C., et al. (2012) · Arthritis & Rheumatism · doi:10.1002/art.34409 · Cited by 221
The role of the NLRP3 inflammasome in gout
McDermott, M., Kingsbury, S. R., & Conaghan, P. G. (2011) · Journal of Inflammation Research · doi:10.2147/jir.s11330 · Cited by 225
Crystal nephropathies: mechanisms of crystal-induced kidney injury
Mulay, S. R., & Anders, H. (2017) · Nature Reviews Nephrology · doi:10.1038/nrneph.2017.10 · Cited by 227
Metadata
- Authors
- Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., & Golenbock, D. T.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- Harvard University (US)
- University of Freiburg (DE)
- Corresponding author
- Golenbock, Douglas T
- ORCID
- Venue
- Nature Immunology
- Published
- 2008-07-11
- Volume
- 9
- Issue
- 8
- Pages
- 857-865
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- PMC
- PMC3101478
- OpenAlex
- W2119098586
- Cited by
- 2,441
- References
- 50
- Citations by year
- 2026: 92 · 2025: 124 · 2024: 143 · 2023: 165 · 2022: 191 · 2021: 188 · 2020: 169 · 2019: 151 · 2018: 136 · 2017: 139 · 2016: 138 · 2015: 146 · 2014: 149 · 2013: 153 · 2012: 98
- FWCI
- 35.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Immunology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship@UMassChan (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- National Institute on Aging (R01AG020255, AG20255)
- National Institute of General Medical Sciences (R37GM054060, R01GM054060, GM 54060)
- National Institute of Allergy and Infectious Diseases (AI065483, R01AI065483)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- NLRP3 inflammasome, amyloid-beta, Alzheimer's disease, innate immunity, IL-1β, caspase-1, microglia, phagocytosis, lysosomal damage, cathepsin B, neuroinflammation, neurotoxicity
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Alzheimer Disease, Carrier Proteins, Immunity, Innate, Inflammation, Amyloid beta-Peptides, Inflammation Mediators
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