The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
NLRP3 inflammasome activation drives tau pathology
Open accessAbstract
Alzheimer’s disease is characterized by the accumulation of amyloid-beta in plaques, aggregation of hyperphosphorylated tau in neurofibrillary tangles and neuroinflammation, together resulting in neurodegeneration and cognitive decline1. The NLRP3 inflammasome assembles inside of microglia on activation, leading to increased cleavage and activity of caspase-1 and downstream interleukin-1β release2. Although the NLRP3 inflammasome has been shown to be essential for the development and progression of amyloid-beta pathology in mice3, the precise effect on tau pathology remains unknown. Here we show that loss of NLRP3 inflammasome function reduced tau hyperphosphorylation and aggregation by regulating tau kinases and phosphatases. Tau activated the NLRP3 inflammasome and intracerebral injection of fibrillar amyloid-beta-containing brain homogenates induced tau pathology in an NLRP3-dependent manner. These data identify an important role of microglia and NLRP3 inflammasome activation in the pathogenesis of tauopathies and support the amyloid-cascade hypothesis in Alzheimer’s disease, demonstrating that neurofibrillary tangles develop downstream of amyloid-beta-induced microglial activation. The authors show that NLRP3 inflammasome is activated in microglia of patients with fronto-temporal dementia and in a mouse model of tau pathology, and that the loss of NLRP3 inflammasome function decreases tau pathology and improves cognition in mice.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The NLRP3-ASC inflammasome mechanisms contributing to increased beta-amyloids and tau are thought to be a combination of kinases and phosphatases involved in tau phosphorylation [96] through the production of IL-1 beta.”
From The Role of Cortisol in Chronic Stress, Neurodegenerative Diseases, and Psychological Disorders (2023) · cites this paper as [96]
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
“The activation of hippocampal NLRP3 inflammasome-mediated pyroptosis is associated with neuronal damage, cognitive decline, and neuronal death (Hanslik & Ulland, 2020; Heneka et al., 2013; Ising et al., 2019; Venegas et al., 2017).”
From Picroside II Alleviates the Progression of Alzheimer’s Disease via the NLRP3/Caspase-1/GSDMD Pathway (2025) · cites this paper as Ising et al., 2019
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
“On the other hand, treatment of mouse primary hippocampal neurons with conditioned media from wild-type, but not Nlrp3−/− and Asc−/−, microglia primed with LPS resulted in elevated total and phosphorylated tau levels, suggesting that NLRP3 inflammasome activation in microglia can induce tau pathology in neurons.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
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
“Additionally, several cytokines, including IL-1β and IL-6, can directly induce tau phosphorylation in vitro, thus potentially contributing to the development of tau pathology.54”
From Amelioration of Tau and ApoE4-linked glial lipid accumulation and neurodegeneration with an LXR agonist (2024) · cites this paper as [56]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Research by Ising et al. suggests that tau proteins can activate the NLRP3 inflammasome, which then promotes excessive tau phosphorylation and aggregation by affecting specific tau kinases and phosphatases.252”
From Recent advances in Alzheimer's disease: Mechanisms, clinical trials and new drug development strategies. (2024) · cites this paper as [252]
The cited source says what the claim attributes to it.
In the citing paper
“In turn, the NLRP3 inflammasome is essential for the development and progression of Aβ pathology in mice29 and may drive tau pathology through Aβ-induced microglial activation30.”
From New insights into the genetic etiology of Alzheimer’s disease and related dementias (2022) · cites this paper as [30]
The cited source says what the claim attributes to it.
In the citing paper
“On the other hand, microglia could also drive tau spreading and toxicity by promoting neuroinflammation, such as activating NACHT-, LRR- and pyrin (PYD)-domain-containing protein 3 (NLRP3) inflammasome155 or inducing NF-kB signaling.”
From Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets (2023) · cites this paper as [155]
The cited source says what the claim attributes to it.
In the citing paper
“Tau oligomers and monomers can also activate NLRP3 inflammasomes, further perpetuating microglial activation [162] and potential progression of tau pathology.”
From Microglia and monocytes in inflammatory CNS disease: integrating phenotype and function (2022) · cites this paper as [162]
The cited source says what the claim attributes to it.
In the citing paper
“Treatment of wild-type primary microglia with recombinant wild-type tau and recombinant tau with a P301S mutation increased IL-1β secretion, an effect that was attenuated in Nlrp3−/− and Asc−/− microglia, suggesting that tau induces IL-1β secretion in a NLRP3-dependent manner [81].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“Inhibiting or downregulating the NLRP3 inflammasome ameliorates AD neuropathology in animal models, which opens up a therapeutic avenue for modulators of NLRP3 activation in AD.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“On the other hand, treatment of mouse primary hippocampal neurons with conditioned media from wild-type, but not Nlrp3−/− and Asc−/−, microglia primed with LPS resulted in elevated total and phosphorylated tau levels, suggesting that NLRP3 inflammasome activation in microglia can induce tau pathology in neurons.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“Treatment of wild-type primary microglia with recombinant wild-type tau and recombinant tau with a P301S mutation increased IL-1β secretion, an effect that was attenuated in Nlrp3−/− and Asc−/− microglia, suggesting that tau induces IL-1β secretion in a NLRP3-dependent manner [81].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“The NLRP3 inflammasome has a bidirectional relationship with AD-related tau pathology as well.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“Evidence suggests that while some forms of tau can activate the NLRP3 inflammasome, inflammasome activation can exacerbate tau pathology by promoting elevated phosphorylation of tau [81, 82].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“Moreover, treatment with brain homogenates from APP/PS1 mice induced tau hyperphosphorylation in a mouse model of tau aggregation pathology (Tau22) but not in Tau22/Nlrp3−/− and Tau22/Asc−/− mice, indicating the NLRP3 inflammasome as a mediator of Aβ-induced tau pathology [81].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“Moreover, treatment with brain homogenates from APP/PS1 mice induced tau hyperphosphorylation in a mouse model of tau aggregation pathology (Tau22) but not in Tau22/Nlrp3−/− and Tau22/Asc−/− mice, indicating the NLRP3 inflammasome as a mediator of Aβ-induced tau pathology [81].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“Evidence suggests that while some forms of tau can activate the NLRP3 inflammasome, inflammasome activation can exacerbate tau pathology by promoting elevated phosphorylation of tau [81, 82].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
The cited source says what the claim attributes to it.
In the citing paper
“In Tau22 mice, ablation of Nlrp3 or Asc reduced levels of hyperphosphorylated tau and tau aggregates and rescued tau-induced spatial memory deficits [81].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [81]
In the citing paper
“Studies have demonstrated important roles of the NLRP3 inflammasome in aging and age-related diseases, such as atherosclerosis metabolic syndrome, type 2 diabetes, and Alzheimer’s disease (81–83).”
From Connecting aging biology and inflammation in the omics era (2022) · cites this paper as [83]
In the citing paper
“For example, in AD and frontotemporal dementia, neuroinflammation and microglia activation potentiate the spreading of pathological tau neurofibrillary tangles (83, 175).”
From Connecting aging biology and inflammation in the omics era (2022) · cites this paper as [83]
In the citing paper
“In AD, this relationship may be mediated by NLRP3 inflammasome activation in microglia, a process that activates tau kinases (e.g., GSK-3β and CaMKII-α) and results in tau hyperphosphorylation (83).”
From Connecting aging biology and inflammation in the omics era (2022) · cites this paper as [83]
In the citing paper
“The knockout of ASC or NLRP3 ameliorates AD‐like brain pathology in animal models. 68”
From Senescence, brain inflammation, and oligomeric tau drive cognitive decline in Alzheimer's disease: Evidence from clinical and preclinical studies (2024) · cites this paper as [68]
In the citing paper
“The activation of the NLRP3 inflammasome drives tau pathology. 68”
From Senescence, brain inflammation, and oligomeric tau drive cognitive decline in Alzheimer's disease: Evidence from clinical and preclinical studies (2024) · cites this paper as [68]
In the citing paper
“Inflammaging can drive tau pathology and neurodegeneration in AD by impairing the clearance of Aβ peptides, altering BBB integrity, and affecting the synaptic functions. 68”
From Senescence, brain inflammation, and oligomeric tau drive cognitive decline in Alzheimer's disease: Evidence from clinical and preclinical studies (2024) · cites this paper as [68]
In the citing paper
“A recent study shows that NLR family pyrin domain-containing protein 3 (NLRP3) inflammasome activation induces tau hyperphosphorylation and aggregation through modulating tau kinases and phosphatases [159].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [159]
In the citing paper
“In the CNS, inflammasome activation has been mainly linked to neuroinflammatory conditions. As example, it has an essential role in the progression of several neurological disorders like MS, AD, PPD, and NPS (132, 193–197).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [197]
In the citing paper
“In general, patients affected by tauopathies showed elevated levels of cleaved caspase-1 and ASC and mature IL-1β in the cortex (197).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [197]
In the citing paper
“Injecting brain homogenates from APP/PS1 or wild-type mice into the hippocampus of Tau22 mice, induced tau hyperphosphorylation in the hippocampus of Tau22 wild-type but not Tau22/Pycard−/− or Tau22/Nlrp3−/− deficient mice”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [197]
In the citing paper
“suggesting that NLRP3 activation is upstream the Aβ-tau cascade and tau pathology (197).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [197]
In the citing paper
“Consistent with this, Tau22 mice lacking ASC or NLRP3 expression had lower levels of aggregated and hyperphosphorylated tau in the hippocampus, and their typical spatial memory deficits were rescued (197).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [197]
In the citing paper
“Also, Tau22 mice, another model of AD and other tauopathies, had increased levels of cleaved caspase-1 and ASC in their brain at the age of 11 months compared to their 3-month-old counterparts.”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [197]
In the citing paper
“Further, activated microglia promote tau phosphorylation and aggregation by activation of the NLRP3 (nucleotide binding oligomerisation domain (NOD)-, leucine-rich repeat (LRR)- and pyrin domain-containing protein 3) inflammasome in response to amyloid-β [22,23].”
From ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease (2020) · cites this paper as [23]
In the citing paper
“Further, there is evidence tauopathy is driven by NLRP3 inflammasome activation in microglia in response to amyloid-β [23].”
From ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease (2020) · cites this paper as [23]
In the citing paper
“ROS from NOX4 also contribute to activation of the NLRP3 inflammasome, a driver of both amyloid-β [156] and tau [23] pathology.”
From ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease (2020) · cites this paper as [23]
In the citing paper
“Growing evidence indicates that Aβ accumulation stimulates tau phosphorylation and fibrillary tangle formation, leading to the process of neurodegeneration.112–114”
From Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future (2023) · cites this paper as [112]
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 Ising et al, 2019
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Szklarczyk, D., Morris, J. H., Cook, H., Kuhn, M., Wyder, S., Simonovic, M., Santos, A., Doncheva, N. T., Roth, A., Bork, P., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkw937 · Cited by 6,980
NLRP3 is activated in Alzheimer’s disease and contributes to pathology in APP/PS1 mice
Heneka, M. T., Kummer, M. P., Stutz, A., Delekate, A., Schwartz, S., Vieira-Saecker, A., Griep, A., Axt, D., Remus, A., Tzeng, T.-C., et al. (2013) · Nature · doi:10.1038/nature11729 · Cited by 2,898
Self-citationThe NALP3 inflammasome is involved in the innate immune response to amyloid-β
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. (2008) · Nature Immunology · doi:10.1038/ni.1636 · Cited by 2,441
Self-citationDepletion of microglia and inhibition of exosome synthesis halt tau propagation
Asai, H., Ikezu, S., Tsunoda, S., Medalla, M., Luebke, J., Haydar, T., Wolozin, B., Butovsky, O., Kügler, S., & Ikezu, T. (2015) · Nature Neuroscience · doi:10.1038/nn.4132 · Cited by 1,591
Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils
Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526
Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3
Kanneganti, T., Özören, N., Body–Malapel, M., Amer, A. O., Park, J., Franchi, L., Whitfield, J. R., Barchet, W., Colonna, M., Vandenabeele, P., et al. (2006) · Nature · doi:10.1038/nature04517 · Cited by 1,149
Tau pathology in Alzheimer disease and other tauopathies
Iqbal, K., del C. Alonso, A., Chen, S., Chohan, M. O., El-Akkad, E., Gong, C.-X., Khatoon, S., Li, B., Liu, F., Rahman, A., et al. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.008 · Cited by 1,037
Microglia-derived ASC specks cross-seed amyloid-β in Alzheimer’s disease
Venegas, C., Kumar, S., Franklin, B. S., Dierkes, T., Brinkschulte, R., Tejera, D., Vieira-Saecker, A., Schwartz, S., Santarelli, F., Kummer, M. P., et al. (2017) · Nature · doi:10.1038/nature25158 · Cited by 983
Self-citationInflammasome signalling in brain function and neurodegenerative disease
Heneka, M. T., McManus, R. M., & Latz, E. (2018) · Nature Reviews Neuroscience · doi:10.1038/s41583-018-0055-7 · Cited by 836
Self-citationCanonical Nlrp3 Inflammasome Links Systemic Low-Grade Inflammation to Functional Decline in Aging
Youm, Y.-H., Grant, R. W., McCabe, L. R., Albarado, D. C., Nguyen, K. Y., Ravussin, A., Pistell, P., Newman, S., Carter, R., Laque, A., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.09.010 · Cited by 674
Cited by
Sorted by citations
Items 501–600 of 1,003
Proteomic Approaches to Study Cysteine Oxidation: Applications in Neurodegenerative Diseases
Pham, T. K., Buczek, W. A., Mead, R. J., Shaw, P. J., & Collins, M. O. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.678837 · Cited by 31
Tang, H., & Harte, M. (2021) · Genes · doi:10.3390/genes12111753 · Cited by 28
Yang, Y., Seok, M., Kim, Y. E., Choi, Y., Song, J., Sulistio, Y. A., Kim, S., Chang, M., Oh, S., Nam, M., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01693-6 · Cited by 30
Innate immune activation: Parallels in alcohol use disorder and Alzheimer’s disease
Ramos, A., Joshi, R., & Szabó, G. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.910298 · Cited by 29
Kattan, D., Barsa, C., Mekhijian, S., Shakkour, Z., Jammoul, M., Doumit, M., Zabala, M. C. P., Darwiche, N., Eid, A. H., Mechref, Y. S., et al. (2022) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2022.104969 · Cited by 28
Manet, C., Mansuroglu, Z., Conquet, L., Bortolin, V., Comptdaer, T., Segrt, H., Bourdon, M., Menidjel, R., Stadler, N., Tian, G., et al. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02668-8 · Cited by 30
Self-citationThe role of adenosine A2A receptors in Alzheimer's disease and tauopathies
Launay, A., Nebie, O., Shankara, J. V., Lebouvier, T., Buée, L., Faivre, É., & Blum, D. L. (2022) · Neuropharmacology · doi:10.1016/j.neuropharm.2022.109379 · Cited by 29
Self-citationFriend or foe: role of pathological tau in neuronal death
Wu, M., Chen, Z., Jiang, M. H., Bao, B., Li, D., Yin, X., Wang, X., Liu, D., & Zhu, L. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02024-z · Cited by 28
Fernández Zapata, C., Giacomello, G., Spruth, E. J., Middeldorp, J., Gallaccio, G., Dehlinger, A., Dames, C., Leman, J. K. H., van Dijk, R. E., Meisel, A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34719-2 · Cited by 27
Tang, L., Xu, Y., Wang, L., & Pan, J. (2023) · Neuroreport · doi:10.1097/wnr.0000000000001941 · Cited by 28
Hong, Y., Wei, C., Fu, M., Li, X., Zhang, H., & Yao, B. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.111236 · Cited by 28
Biechele, G., Rauchmann, B., Janowitz, D., Büerger, K., Franzmeier, N., Weidinger, E., Guersel, S., Schuster, S., Finze, A., Harris, S., et al. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03020-y · Cited by 30
Inflammatory Markers Associated with Physical Frailty and Cognitive Impairment
Pan, Y., & Ma, L. (2024) · Aging and Disease · doi:10.14336/ad.2024.0258 · Cited by 29
Psilocybin for the treatment of Alzheimer’s disease
Zheng, S., Ma, R., Yang, Y., & Li, G. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1420601 · Cited by 27
Ketone body metabolism and the NLRP3 inflammasome in Alzheimer's disease
Shippy, D. C., Evered, A. H., & Ulland, T. K. (2024) · Immunological Reviews · doi:10.1111/imr.13365 · Cited by 33
A novel tri‐culture model for neuroinflammation
Zheng, Y., Zhou, X., Chang, D., Bhuyan, D. J., Zhang, J., Yu, W., Jiang, X., Seto, S. W., Yeon, S. Y., Li, J., et al. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15171 · Cited by 27
Cellular Biology of Tau Diversity and Pathogenic Conformers
Kang, S., Eskandari‐Sedighi, G., Hromádková, L., Safar, J., & Westaway, D. A. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590199 · Cited by 29
Microglial activation in Alzheimer's disease: The role of flavonoids and microRNAs
Medrano-Jiménez, E., Meza‐Sosa, K. F., Aragon, J. A. U., Secundino, I., Pedraza-Alva, G., & Pérez-Martínez, L. (2022) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mr1021-531r · Cited by 28
Advances in the Functions of Thioredoxin System in Central Nervous System Diseases
Jia, J., Xu, G., Zhu, D., Liu, H., Zeng, X., & Li, L. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0079 · Cited by 28
Sonn, I., Honda‐Ozaki, F., Yoshimatsu, S., Morimoto, S., Watanabe, H., & Okano, H. (2022) · Inflammation and Regeneration · doi:10.1186/s41232-022-00201-1 · Cited by 30
Beyond the amyloid cascade: An update of Alzheimer's disease pathophysiology
Gouilly, D., Rafiq, M., Nogueira, L., Salabert, A., Payoux, P., Péran, P., & Pariente, J. (2023) · Revue Neurologique · doi:10.1016/j.neurol.2022.12.006 · Cited by 31
Ye, X., Zhang, H., Li, Q., Ren, H., Xu, X., & Li, X.-R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108625 · Cited by 26
Progressive Supranuclear Palsy Syndrome: An Overview
Ichikawa-Escamilla, E., Velasco-Martínez, R. A., & Adalid-Peralta, L. V. (2024) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2024.04.008 · Cited by 31
Ge, T.-Q., Guan, P.-P., & Wang, P. (2024) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2024.105868 · Cited by 28
Ramos, E. L. P., Neto, I. V. D. S., Pinto, A. P., Cintra, D. E., Ropelle, E. R., Pauli, J., de Freitas, E. C., Mineo, T. W. P., & da Silva, A. S. R. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102821 · Cited by 30
Alemán-Villa, K. M., Armienta-Rojas, D. A., Camberos-Barraza, J., Rábago-Monzón, Á. R., Camacho-Zamora, A., Osuna‐Ramos, J. F., Magaña‐Gómez, J. A., Guadrón‐Llanos, A. M., Calderón-Zamora, L., Norzagaray-Valenzuela, C. D., et al. (2025) · NeuroImmunoModulation · doi:10.1159/000548021 · Cited by 34
McCarty, M. F., DiNicolantonio, J. J., & Lerner, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042140 · Cited by 27
de Oliveira, P., Cella, C. V., Locker, N., Ravindran, K. K. G., Mendis, A., Wafford, K. A., Gilmour, G., Dijk, D., & Winsky‐Sommerer, R. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.2162-21.2022 · Cited by 25
Bajracharya, R., Cruz, E., Götz, J., & Nisbet, R. M. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.07.026 · Cited by 27
Microglia as a cellular target of diclofenac therapy in Alzheimer’s disease
Stopschinski, B. E., Weideman, R. A., McMahan, D., Jacob, D. A., Little, B. B., Chiang, H.-S., Saez Calveras, N., & Stuve, O. (2023) · Therapeutic Advances in Neurological Disorders · doi:10.1177/17562864231156674 · Cited by 26
Yang, Z., Liu, F., Li, Z., Liu, N., Yao, X., Zhou, Y., Zhang, L., Pan, J., Liu, H., Kong, L., et al. (2023) · Clinical Epigenetics · doi:10.1186/s13148-023-01506-9 · Cited by 27
Ye, Y., Gao, M., Shi, W., Gao, Y., Li, Y., Yang, W., Zheng, X., & Lu, X. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1325530 · Cited by 29
CNS Resident Innate Immune Cells: Guardians of CNS Homeostasis
Muzio, L., & Perego, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094865 · Cited by 27
Zhao, N., 东南大学医学院神经内科, 江. 南. 2., Xiu, C., Chen, Q.-G., Liu, X.-T., Geng, F., Zhu, M., Yan, F., Zhang, Z., Ren, Q., et al. (2024) · 动物学研究 · doi:10.24272/j.issn.2095-8137.2024.085 · Cited by 27
Auger, A., Faidi, R., Rickman, A. D., Peña-Martinez, C., Fajfer, A., Carling, J., Hilyard, A., Ali, M., Ono, R., Cleveland, C., et al. (2025) · npj Dementia · doi:10.1038/s44400-025-00011-5 · Cited by 31
Diverse functions of NLRP3 inflammasome in PANoptosis and diseases
Jiang, Y., Qiang, Z., Liu, Y., Zhu, L., Xiao, L., Du, Z., Cai, R., & Qiang, S. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02689-1 · Cited by 25
Ren, J., Wang, Q., Hong, H., & Tang, C. (2025) · Microorganisms · doi:10.3390/microorganisms13081956 · Cited by 28
Immune-Related Hub Genes and the Competitive Endogenous RNA Network in Alzheimer’s Disease
Xu, H., & Jia, J. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200081 · Cited by 26
Reece, A. S., & Hulse, G. K. (2020) · BMC Public Health · doi:10.1186/s12889-020-09748-5 · Cited by 25
Manifestations and mechanisms of central nervous system damage caused by SARS-CoV-2
Yang, F., Zhao, H., Liu, H., Wu, X., & Li, Y. (2021) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2021.09.015 · Cited by 24
Wu, L., Kalish, B. T., Finander, B., Cao, T., Jin, G., Yahya, T., Levy, E. S., Kukreja, B., LaRovere, E. S., Chung, J. Y., et al. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.0682-21.2021 · Cited by 28
Microglial Endocannabinoid Signalling in AD
Scipioni, L., Ciaramellano, F., Carnicelli, V., Leuti, A., Lizzi, A. R., Dominicis, N. D., Oddi, S., & Maccarrone, M. (2022) · Cells · doi:10.3390/cells11071237 · Cited by 26
Pini, L., Salvalaggio, A., Wennberg, A. M. V., Dimakou, A., Matteoli, M., & Corbetta, M. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101867 · Cited by 26
FAM69C functions as a kinase for eIF2α and promotes stress granule assembly
Wu, Z., Mei, F., Gan, Y., Liu, A., Hu, J., Jin, Y., & Yin, Y. (2023) · EMBO Reports · doi:10.15252/embr.202255641 · Cited by 28
Complexity of Sex Differences and Their Impact on Alzheimer’s Disease
Kadlecová, M., Freude, K., & Haukedal, H. (2023) · Biomedicines · doi:10.3390/biomedicines11051261 · Cited by 27
Jiang, K., Zhang, F., Chen, Y., Li, X., Zhao, X., Jiang, P., & Li, Y. (2024) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.65.6.2 · Cited by 24
Daniilidou, M., Holleman, J., Hagman, G., Kåreholt, I., Aspö, M., Brinkmalm, A., Zetterberg, H., Blennow, K., Solomon, A., Kivipelto, M., et al. (2024) · Translational Psychiatry · doi:10.1038/s41398-024-03072-x · Cited by 27
Magagnoli, J., Ambati, M., Cummings, T. H., Nguyen, J. D. K., Thomas, C. C., Ambati, V. L., Sutton, S. S., Gelfand, B. D., & Ambati, J. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70180 · Cited by 22
The Multifaceted Role of P2X7R in Microglia and Astrocytes
Bedetta, M., Pizzo, P., & Lia, A. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04502-y · Cited by 28
Hassan, H., Rawlinson, C., Lan, Y., Jenkins, S. I., & Chen, R. (2025) · Biomolecules · doi:10.3390/biom15111629 · Cited by 30
Md, S., Alhakamy, N. A., Alfaleh, M. A., Afzal, O., Altamimi, A. S. A., Iqubal, A., & Shaik, R. A. (2021) · Journal of Personalized Medicine · doi:10.3390/jpm11111116 · Cited by 24
Yu, H., Tang, M.-H., Zeng, Z., Huang, S.-J., Zheng, X., & Liu, Z. (2022) · Brain Sciences · doi:10.3390/brainsci12020191 · Cited by 25
The emerging role of LRRK2 in tauopathies
Herbst, S., Lewis, P. A., & Morris, H. R. (2022) · Clinical Science · doi:10.1042/cs20220067 · Cited by 23
Perner, C., & Krüger, E. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.859703 · Cited by 27
Lv, L., Maimaitiming, M., Huang, Y., Yang, J., Chen, S., Sun, Y., Zhang, X., Li, X., Xue, C., Wang, P., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115346 · Cited by 26
Duan, L., Hu, M., Tamm, J. A., Grinberg, Y. Y., Shen, F., Chai, Y., Xi, H. S., Gibilisco, L., Ravikumar, B., Gautam, V., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-82658-7 · Cited by 26
Yi, X., Song, Y., Xu, J., Wang, L., Liu, L., Huang, D., & Zhang, L. (2023) · Odontology · doi:10.1007/s10266-023-00813-0 · Cited by 23
Zhong, H., Liu, T., Shang, Y., Huang, C., & Pan, S. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117042 · Cited by 24
Ayyubova, G., & Madhu, L. N. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04758-z · Cited by 23
Faridar, A., Gamez, N., Li, D., Wang, Y., Boradia, R., Thome, A. D., Zhao, W., Beers, D. R., Thonhoff, J. R., Nakawah, M. O., et al. (2025) · Alzheimer s Research & Therapy · doi:10.1186/s13195-025-01791-x · Cited by 27
p38 Inhibition Decreases Tau Toxicity in Microglia and Improves Their Phagocytic Function
Perea, J. R., Bolós, M., Cuadros, R., García, E., García‐Escudero, V., Hernández, F., McManus, R. M., Heneka, M. T., & Ávila, J. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02715-0 · Cited by 24
Self-citationXia, Y., Prokop, S., Bell, B. M., Gorion, K.-M. M., Croft, C. L., Nasif, L. H., Xu, G. M., Riffe, C. J., Manaois, A. N., Strang, K. H., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03373-1 · Cited by 24
TRIM50 promotes NLRP3 inflammasome activation by directly inducing NLRP3 oligomerization
Lin, Y., Lv, X., Sun, C., Sun, Y., Yang, M., Ma, D., Jing, W., Zhao, Y., Cheng, Y., Xuan, H., et al. (2022) · EMBO Reports · doi:10.15252/embr.202154569 · Cited by 23
Is Drp1 a link between mitochondrial dysfunction and inflammation in Alzheimer’s disease?
Sbai, O., Bazzani, V., Tapaswi, S., McHale, J., Vascotto, C., & Perrone, L. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1166879 · Cited by 24
Pati, S., Gautam, A. S., Dey, M., Tiwari, A., & Singh, R. K. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103750 · Cited by 23
Mészáros, Á., Molnár, K., Fazakas, C., Nógrádi, B., Lüvi, A., Dudás, T., Tiszlavicz, L., Farkas, A. E., Krizbai, I. A., & Wilhelm, I. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01646-2 · Cited by 23
Li, C., Zhao, Z., Jin, J., Zhao, C., Zhao, B., & Liu, Y. (2023) · Neuroscience · doi:10.1016/j.neuroscience.2023.12.006 · Cited by 24
Moghaddam, S. A., Pourabdolhossein, F., Najafzadehvarzi, H., Sarbishegi, M., Saleki, K., & Nouri, H. R. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e25523 · Cited by 25
Jacobs, T., Jacobson, S. R., Fortea, J., Berger, J. S., Vedvyas, A., Marsh, K., He, T., Gutiérrez‐Jiménez, E., Fillmore, N. R., Gonzalez, M., et al. (2024) · Immunity & Ageing · doi:10.1186/s12979-024-00435-2 · Cited by 27
Yin, X., Zhou, H., Cao, T., Yang, X., Meng, F., Dai, X., Wang, Y., Li, S., Zhai, W., Yang, Z., et al. (2024) · ACS Nano · doi:10.1021/acsnano.3c08823 · Cited by 26
Microglia in Alzheimer’s Disease
Süß, P., & Schlachetzki, J. C. M. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666200212155234 · Cited by 26
Masuoka, N., Lei, C., Li, H., Inamura, N., Shiotani, S., Yanai, N., Sato, K., Sakurai, K., & Hisatsune, T. (2021) · Aging · doi:10.18632/aging.202535 · Cited by 23
Investigating interleukin-8 in Alzheimer's disease: A comprehensive review
Righi, D., Manco, C., Pardini, M., Stufano, A., Schino, V., Pelagotti, V., Massa, F., Stefano, N. D., & Plantone, D. (2024) · Journal of Alzheimer s Disease · doi:10.1177/13872877241298973 · Cited by 21
Zinc homeostasis regulates caspase activity and inflammasome activation
Gong, X., Gu, W., Fu, S., Zou, G., & Jiang, Z. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012805 · Cited by 21
Church, T. R., & Margolis, S. S. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1531797 · Cited by 25
Li, B., Wang, L., Xiao, Y. C., Wang, Y., Wang, Y., Peng, Y., Zhang, A., Tang, Z., & Qi, X. (2025) · Phytotherapy Research · doi:10.1002/ptr.8461 · Cited by 23
Macrocyclic Immunoproteasome Inhibitors as a Potential Therapy for Alzheimer’s Disease
Lee, M. J., Bhattarai, D., Jang, H., Baek, A., Yeo, I. J., Lee, S., Miller, Z. C., Lee, S., Hong, J. T., Kim, D., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00291 · Cited by 22
A novel mechanism for NLRP3 inflammasome activation
Zhang, T., Zhao, J., Liu, T., Cheng, W., Wang, Y., Ding, S., & Wang, R. (2022) · Metabolism Open · doi:10.1016/j.metop.2022.100166 · Cited by 22
Diverse pathways to neuronal necroptosis in Alzheimer's disease
Jayaraman, A., & Reynolds, R. (2022) · European Journal of Neuroscience · doi:10.1111/ejn.15662 · Cited by 21
Jayashankar, S. S., Arifin, K. T., & Nasaruddin, M. L. (2023) · Nutrients · doi:10.3390/nu15030524 · Cited by 24
Ni, H., Ren, J., Wang, Q., Li, X., Wu, Y. H., Liu, D., & Wang, J. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e16755 · Cited by 22
Emerging Roles of Cells and Molecules of Innate Immunity in Alzheimer’s Disease
Tamburini, B., Badami, G. D., Manna, M. P. L., Azgomi, M. S., Caccamo, N., & Dieli, F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241511922 · Cited by 22
Zhang, N., Nao, J., & Dong, X. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c06672 · Cited by 23
Zhang, S., Chen, Y., Wang, Y., Wang, H., Yao, D., & Chen, G. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-023-01152-4 · Cited by 23
Self-citationTLR4/Rac1/NLRP3 Pathway Mediates Amyloid-β-Induced Neuroinflammation in Alzheimer’s Disease
Zhu, M., Liu, Y., Chen, C., Chen, H., Ni, W., Song, Y., Lv, B., Hua, F., Cui, G., & Zhang, Z. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240012 · Cited by 23
Li, K., Shi, G., Zhao, Y., Chen, Y., Gao, J., Yao, L., Zhao, J., Li, H., Xu, Y., & Chen, Y. (2021) · Neural Plasticity · doi:10.1155/2021/8814616 · Cited by 23
Wang, J., Wang, D., Zhou, Z., Zhang, X., Zhang, C., He, Y., Liu, C., Yuan, C., Yuan, D., & Wang, T. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105098 · Cited by 22
Zhao, M., Ma, G., Yan, X., Li, X., Wang, E., Xu, X.-X., Zhao, J.-B., Ma, X., & Zeng, J. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02428-5 · Cited by 21
Guzman‐Hernandez, R. A., & Fossati, S. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70077 · Cited by 23
How interactions between oxidized DNA and the NLRP3 inflammasome fuel inflammatory disease
Lackner, A., Leonidas, L., Macapagal, A., Lee, H. J., & McNulty, R. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2025.07.007 · Cited by 23
Pathways linking Alzheimer’s disease risk genes expressed highly in microglia
Hodges, A. K., Piers, T. M., Collier, D., Cousins, O., & Pocock, J. M. (2021) · Neuroimmunology and Neuroinflammation · doi:10.20517/2347-8659.2020.60 · Cited by 21
Nizami, S., Millar, V., Arunasalam, K., Zarganes‐Tzitzikas, T., Brough, D., Tresadern, G., Brennan, P. E., Davis, J. B., Ebner, D. V., & Daniel, E. D. (2021) · Scientific Reports · doi:10.1038/s41598-021-94850-w · Cited by 21
Zhao, Y., Tan, S.-W., Huang, Z., Shan, F., Li, P., Ning, Y.-L., Ye, S., Zhao, Z.-A., Du, H., Xiong, R.-P., et al. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.721474 · Cited by 17
The NLRP3 Inflammasome in the Pathogenesis and Treatment of Alzheimer’s Disease
Golzari-Sorkheh, M., Brown, C. E., Weaver, D. F., & Reed, M. A. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210660 · Cited by 21
Chang, H., Chen, C., & Huang, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147951 · Cited by 21
The role of regulatory necrosis in traumatic brain injury
Nie, Z., Tan, L., Niu, J., & Wang, B. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1005422 · Cited by 21
Vascular endothelial cells: a fundamental approach for brain waste clearance
Wei, H., Jiang, H., Zhou, Y., Xiao, X., Zhou, C., & Ji, X. (2022) · Brain · doi:10.1093/brain/awac495 · Cited by 20
Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective
Ferrer, I. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-3806 · Cited by 25
Beltran-Lobo, P., Hughes, M. M., Troakes, C., Croft, C. L., Rupawala, H., Jutzi, D., Ruepp, M., Jiménez-Sánchez, M., Perkinton, M. S., Kassiou, M., et al. (2023) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2023.09.011 · Cited by 21
Immunity impacts cognitive deficits across neurological disorders
Shaw, B. C., Anders, V., Tinkey, R. A., Habean, M. L., Brock, O. D., Frostino, B. J., & Williams, J. L. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15999 · Cited by 27
Metadata
- Authors
- Ising, C., Venegas, C., Zhang, S., Scheiblich, H., Schmidt, S. V., Vieira-Saecker, A., Schwartz, S., Albasset, S., McManus, R. M., Tejera, D., Griep, A., Santarelli, F., Brosseron, F., Opitz, S., Stunden, J., Merten, M., Kayed, R., Golenbock, D. T., Blum, D., Latz, E., Buée, L., & Heneka, M. T.
- Affiliations
- University Hospital Bonn (DE)
- German Center for Neurodegenerative Diseases (DE)
- The University of Texas Medical Branch at Galveston (US)
- University of Massachusetts Chan Medical School (US)
- Inserm (FR)
- Corresponding author
- Heneka, Michael T.
- ORCID
- Venue
- Nature
- Published
- 2019-11-20
- Volume
- 575
- Issue
- 7784
- Pages
- 669-673
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC7324015
- OpenAlex
- W2990312754
- Semantic Scholar
- 6a9d745a33a2d013c621f57586d9d719671530a7
- Cited by
- 1,487
- References
- 28
- Citations by year
- 2026: 189 · 2025: 226 · 2024: 255 · 2023: 226 · 2022: 248 · 2021: 193 · 2020: 143 · 2019: 3
- FWCI
- 101.29
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Open Repository and Bibliography (University of Luxembourg) (submittedVersion, other-oa)
- HAL (submittedVersion, other-oa)
- RePEc: Research Papers in Economics (submittedVersion)
- Institutional Repository of the University of Granada (University of Granada) (submittedVersion, cc-by-nc-nd)
- DZNE Pub (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (R01 AG059752-02)
- Agence Nationale de la Recherche (ANR-11-LABX-0009)
- Deutsches Zentrum für Neurodegenerative Erkrankungen
- National Institutes of Health
- National Institute on Aging (R01AG059752, R01AG054025)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- NLRP3 inflammasome, tau hyperphosphorylation, tau aggregation, neurofibrillary tangles, Alzheimer's disease, amyloid-beta, microglia, amyloid hypothesis, frontotemporal dementia, neuroinflammation, caspase-1, IL-1β
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Gene Expression Regulation, Humans, Mice, Inbred C57BL, Phosphorylation, tau Proteins, Microglia, Cyclin-Dependent Kinase 5, Mice, Inflammasomes, Protein Aggregation, Pathological
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 ›
Are you an author, or do you see a problem with this page? Request a review
