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
“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]
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 measured
The 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
“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]
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
“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 801–900 of 1,003
Rubinski, A., Dewenter, A., Zheng, L., Franzmeier, N., Stephenson, H. G., Deming, Y. K., Duering, M., Gesierich, B. G., Denecke, J., Pham, A.-V., et al. (2023) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-023-06530-8 · Cited by 11
Usui‐Kawanishi, F., Kani, K., Karasawa, T., Honda, H., Takayama, N., Takahashi, M., Takatsu, K., & Nagai, Y. (2024) · Genes to Cells · doi:10.1111/gtc.13108 · Cited by 11
Neuronal Cell Cycle Re-Entry Enhances Neuropathological Features in App NLF Knock-In Mice
Barrett, T., Stangis, K. A., Saito, T., Saido, T. C., & Park, K. H. J. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210091 · Cited by 12
Immune modulations and immunotherapies for Alzheimer’s disease: a comprehensive review
Mahdiabadi, S., Momtazmanesh, S., Perry, G. L., & Rezaei, N. (2021) · Reviews in the Neurosciences · doi:10.1515/revneuro-2021-0092 · Cited by 13
NLRP3 inflammasome and Alzheimer’s disease: bridging inflammation and neurodegeneration
Wasim, R., Azmi, S., Ahmad, A., & Srivastava, A. (2026) · Inflammopharmacology · doi:10.1007/s10787-025-02092-3 · Cited by 11
Basic Microglial Functions and How They Go Awry in Neurodegenerative Disease
McKinney, J. E., Bennett, M. L., & Bennett, F. C. (2026) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-042624-114332 · Cited by 13
Chronic inflammation: a potential target in tauopathies
Ising, C., & Heneka, M. T. (2023) · The Lancet Neurology · doi:10.1016/s1474-4422(23)00116-3 · Cited by 10
Self-citationLi, P., He, Y., Yang, Q., Guo, H., Li, N., & Zhang, D. (2023) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.22-105 · Cited by 10
FUBP3 mediates the amyloid-β-induced neuronal NLRP3 expression
Yao, J., Li, Y., Liu, X., Liang, W., Li, Y., Wu, L., Wang, Z., & Song, W. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01799 · Cited by 13
A Natural Metabolite and Inhibitor of the NLRP3 Inflammasome: 4-hydroxynonenal
Zhang, J., Berk, B. C., & Hsu, C. G. (2024) · Journal of Cellular Immunology · doi:10.33696/immunology.6.192 · Cited by 9
The putative contribution of cellular senescence to driving tauopathies
Karabag, D., Heneka, M. T., & Ising, C. (2024) · Trends in Immunology · doi:10.1016/j.it.2024.08.006 · Cited by 11
Self-citationComparison of Methods of Detecting IL-1β in the Blood of Alzheimer’s Disease Subjects
Remnitz, A. D., Hadad, R., Keane, R. W., Dietrich, W. D., & Vaccari, J. P. D. R. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26020831 · Cited by 13
Li, X., Jin, S., Wang, D., Wu, Y., Tang, X., Liu, Y., Yao, T., Han, S., Sun, L., Wang, Y., et al. (2025) · Advanced Science · doi:10.1002/advs.202414260 · Cited by 11
Eid, F., Boushehri, M., Boucher, C., Rajkanth, N., Sa, A. F., Alhoutan, T., Vavetsi, K., Dibart, S., & Ma, Y. (2025) · The FASEB Journal · doi:10.1096/fj.202403117rr · Cited by 10
Villacampa, N., Sarlus, H., Martorell, P., Bhalla, K., Castro‐Gomez, S., Vieira-Saecker, A. M. M., Slutzkin, I., Händler, K., Venegas, C., McManus, R. M., et al. (2025) · ASN NEURO · doi:10.1080/17590914.2025.2506406 · Cited by 11
Self-citationBrezáni, V., Joshi, R., Ortega‐Ribera, M., Nagesh, P. T., Brezáni, V., Zivny, A., Kurt‐Jones, E. A., Golenbock, D. T., & Szabó, G. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03501-8 · Cited by 12
Self-citationFreyssin, A., Bilan, A. R., Fauconneau, B., Galineau, L., Sérrière, S., Tauber, C., Perrin, F., Guillard, J., Chalon, S., & Page, G. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.803927 · Cited by 10
“Other Than NLRP3” Inflammasomes: Multiple Roles in Brain Disease
Chiarini, A., Armato, U., Gui, L., & Prà, I. D. (2022) · The Neuroscientist · doi:10.1177/10738584221106114 · Cited by 10
Babaei, F., Mirzababaei, M., Dargahi, L., Shahsavari, Z., Nassiri‐Asl, M., & Karima, S. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00500 · Cited by 10
Mu, G., Ren, C., Zhang, Y., Lu, B., Feng, J., Wu, D., Xu, X., & Ou, C. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109544 · Cited by 10
EuHD1 protects against inflammatory injury driven by NLRP3 inflammasome
Qiu, H., Wang, W., Hu, K., Liu, W., Pan, S., Lv, Q., Xu, G., & Yu, Q. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.109712 · Cited by 10
Roles of Microglia in AD Pathology
Gao, R., Wu, H., Li, Q., & Zhao, J. (2023) · Current Alzheimer Research · doi:10.2174/1567205020666230203112351 · Cited by 10
The Role of Pyroptosis in Alzheimer's Disease
Ju, Y., Zhao, L., Li, S., & Zhao, Q. (2023) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2205129 · Cited by 11
Li, F., Zhu, H., Chang, Z., & Li, Y. (2023) · Experimental Biology and Medicine · doi:10.1177/15353702231199076 · Cited by 10
Wu, Y., Sun, J., Chen, M., Lin, Q. D., Jin, K.-Y., Su, S., & Hai, J. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.111108 · Cited by 10
The Gut-Brain Axis in Autoimmune Diseases: Emerging Insights and Therapeutic Implications
Khawar, M. M., Ijaz, S., Goyal, P., Kandambige, D., Sharifa, M., Maslamani, A. N. J., Kutabi, S. A., Saleh, I., Albshir, M. M., Almadhoun, M. K. I. K., et al. (2023) · Cureus · doi:10.7759/cureus.48655 · Cited by 11
Phenotypic Insights Into Anti-IgLON5 Disease in IgLON5-Deficient Mice
Lee, S. Y., Shoji, H., Shimozawa, A., Aoyagi, H., Sato, Y., Tsumagari, K., Terumitsu, ○., Motegi, H., Okada, K., Sekiguchi, K., et al. (2024) · Neurology Neuroimmunology & Neuroinflammation · doi:10.1212/nxi.0000000000200234 · Cited by 10
Morimoto, S., Ishikawa, M., Watanabe, H., Isoda, M., Takao, M., Nakamura, S., Ozawa, F., HIROKAWA, Y. S., Kuzuhara, S., Okano, H., et al. (2020) · Antioxidants · doi:10.3390/antiox9050423 · Cited by 9
Heller, A., Coffman, S. S., & Jarvis, K. A. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200535 · Cited by 10
Tissue-specific features of microglial innate immune responses
Timmerman, R., Burm, S. M., & Bajramovic, J. J. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104924 · Cited by 10
Wickstead, E. S., Irving, M. A., Getting, S. J., & McArthur, S. (2021) · FEBS Journal · doi:10.1111/febs.15861 · Cited by 10
Inhibition of caspase-1 ameliorates tauopathy and rescues cognitive impairment in SAMP8 mice
Tan, M.-S., Liu, Y., Hu, H., Tan, C.-C., & Tan, L. (2022) · Metabolic Brain Disease · doi:10.1007/s11011-022-00914-9 · Cited by 10
Supramolecular organizing centers at the interface of inflammation and neurodegeneration
Sušjan, P., Ramuta, T. Ž., Boršić, E., Orehek, S., & Hafner‐Bratkovič, I. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.940969 · Cited by 11
Inflammasome elements in epilepsy and seizures
Saleki, K., Mohamadi, M., Alijanizadeh, P., & Rezaei, N. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-85841-0.00005-5 · Cited by 10
Jin, M., Xu, R., Alam, M. M., Ma, Z., Zhu, S., Wang, L., Martini, A. C., Bernabucci, M., Xie, P., Kwan, K. Y., et al. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3985173 · Cited by 10
Tijms, B. M., Vromen, E. M., Mjaavatten, O., Holstege, H., Reus, L. M., van der Lee, S., Wesenhagen, K. E., Lorenzini, L., Vermunt, L., Venkatraghavan, V., et al. (2023) · doi:10.1101/2023.05.10.23289793 · Cited by 10
Attenuation of HECT-E3 ligase expression rescued memory deficits in 3xTg-AD mice
Suresh, P., Jasmin, S., Yen, Y., Hsu, H., Varinthra, P., Pairojana, T., Chen, C., & Liu, I. Y. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.916904 · Cited by 9
Wang, K., Zan, S., Xu, J., Sun, W., Li, C., Zhang, W., Ni, D., Cheng, R., Li, L., Yu, Z., et al. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e35800 · Cited by 9
Almalki, W. H., & Almujri, S. S. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2024.155614 · Cited by 9
Rahimpour, S., Clary, B. L., Nasoohi, S., Berhanu, Y. S., & Brown, C. M. (2024) · Aging and Disease · doi:10.14336/ad.2024.1293 · Cited by 13
Wang, F., Wang, J., Luo, N., Luo, Y., Gao, Z., Ye, C., Jiang, M., Shen, Z., Xiao, J., Xue, P., et al. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.117736 · Cited by 13
Multifunctional Carbon Quantum Dots for Monitoring and Therapy of Bacterial Infected Wounds
Qi, W., Liu, Y., Dong, N., Li, M., Zhou, J., Xie, Y., Chang, Q., Luo, B., Celia, C., Wang, J., et al. (2025) · Advanced Healthcare Materials · doi:10.1002/adhm.202403670 · Cited by 11
Xu, J., Ma, L., Xiang, Y., Dai, M.-Q., Li, Q.-H., Jin, X., Ruan, Y., Li, Y., Wang, J., & Shen, X. (2025) · Acta Pharmacologica Sinica · doi:10.1038/s41401-025-01526-6 · Cited by 10
Exploring the Role of NLRP3 in Neurodegeneration: Cutting‐Edge Therapeutic Strategies and Inhibitors
Mustafa, M. A., Bansal, P., Pallavi, M., Panigrahi, R., Nathiya, D., Kumar, S., Al-Hasnaawei, S., Chauhan, A. S., & Singla, S. (2025) · Developmental Neurobiology · doi:10.1002/dneu.22982 · Cited by 12
Wu, W., Meng, T., Han, L., Jin, F., Han, P., & Zhou, Y. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1630205 · Cited by 9
Yu, M., Ma, H., Lai, X., Wu, J., Shen, M., & Yan, J. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1592578 · Cited by 10
Hok‐A‐Hin, Y. S., Vermunt, L., Peeters, C. F. W., van der Ende, E. L., de Boer, S. C. M., Meeter, L. H. H., Houwer, J. F. H. D., Seelaar, H., Swieten, J. C. V., Hu, W. T., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00882-5 · Cited by 19
Shafiee, L., Pishva, M. S., Hosseinzadegsn, R., Bahadori, Z., Baziyar, P., Mehboodi, M., Khademee, S., Akbari, M., Motamed, M., & Nadimi, E. (2025) · Scientific Reports · doi:10.1038/s41598-025-25777-9 · Cited by 9
Alzheimer's disease: from molecular pathways to therapies
Feng, J.-Q., Yang, L.-L., Ya-xi, L., & Yao, X. (2026) · Molecular Biomedicine · doi:10.1186/s43556-026-00443-2 · Cited by 10
A network medicine-based approach to explore the relationship between depression and inflammation
Hu, X., Pang, H., Liu, J., Wang, Y., Lou, Y., & Zhao, Y. (2023) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2023.1184188 · Cited by 11
Alí‐Ruiz, D., Vitureira, N., & Peluffo, H. (2023) · Scientific Reports · doi:10.1038/s41598-023-43840-1 · Cited by 8
Lu, M., Hao, C., Xu, L., Feng, Y., Jiang, J., Wang, Y., Xu, J., Kuang, H., Xu, C., & Sun, M. (2024) · Science China Chemistry · doi:10.1007/s11426-023-1859-4 · Cited by 9
Argentati, C., Tortorella, I., Bazzucchi, M., Emiliani, C., Morena, F., & Martino, S. (2020) · Journal of Personalized Medicine · doi:10.3390/jpm10030115 · Cited by 10
Aging and Microglial Response following Systemic Stimulation with Escherichia coli in Mice
Hoogland, I. C. M., Westhoff, D., Engelen-Lee, J.-Y., Serón, M. V., Houben-Weerts, J. H. P. M., van Westerloo, D. J., van der Poll, T., van Gool, W. A., & van de Beek, D. (2021) · Cells · doi:10.3390/cells10020279 · Cited by 9
Platelet Behavior Contributes to Neuropathologies: A Focus on Alzheimer's and Parkinson's Disease
Page, M. J., & Pretorius, E. (2021) · Seminars in Thrombosis and Hemostasis · doi:10.1055/s-0041-1733960 · Cited by 11
Curcumin suppresses neuroinflammation to protect neurons by preventing NLRP3 inflammasome activation
Shi, Q., Zheng, Y., Wang, L., Xue, Y., & Yang, Y. (2021) · European Journal of Inflammation · doi:10.1177/20587392211058615 · Cited by 10
Savonenko, A. V., Wong, P. C., & Li, T. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85654-6.00022-8 · Cited by 8
Lubec, J., Hussein, A. M., Kalaba, P., Feyissa, D. D., Arias‐Sandoval, E., Cybulska-Kłosowicz, A., Bezu, M., Stojanovic, T., Korz, V., Maliković, J., et al. (2023) · Biomolecules · doi:10.3390/biom13030467 · Cited by 9
Zhang, M., Shan, K., Song, S., Bai, J., Jiang, P., Zhao, D., Ke, W., Zhou, G., & Li, C. (2023) · Food Frontiers · doi:10.1002/fft2.239 · Cited by 9
In vivo Assessment of Neuroinflammation in 4-Repeat TauopathiesPreprint
Palleis, C., Sauerbeck, J., Beyer, L., Harris, S., Schmitt, J., Morenas‐Rodríguez, E., Finze, A., Nitschmann, A., Ruch, F., Eckenweber, F., et al. (2020) · medRxiv · doi:10.1101/2020.07.14.20150243 · Cited by 10
Magagnoli, J., Yerramothu, P., Ambati, K., Cummings, T. H., Nguyen, J. D. K., Thomas, C. C., Wang, S.-B., Cheng, K., Juraev, M., Dholkawala, R., et al. (2023) · medRxiv · doi:10.1101/2023.03.17.23287375 · Cited by 9
Spatiotemporal proteomic profiling of cellular responses to NLRP3 agonistsPreprint
Hollingsworth, L. R., Veeraraghavan, P., Paulo, J. A., & Harper, J. W. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.19.590338 · Cited by 10
Diverse influences on tau aggregation and implications for disease progressionPreprint
Alstyne, M. V., Pratt, J., & Parker, R. (2025) · Genes & Development · doi:10.1101/gad.352551.124 · Cited by 11
INPP5D/SHIP1 regulates inflammasome activation in human microglia
Chou, V., Fancher, S. B., Pearse, R. V., Lee, H., Lam, M., Seyfried, N. T., Bennett, D. A., De Jager, P. L., Menon, V., & Young-Pearse, T. L. (2023) · doi:10.1101/2023.02.25.530025 · Cited by 8
Španić, E., Vogrinc, D., Fuller, H. R., Horvat, L. L., Mayer, D., Kopić, J., Pintarić, K., Leko, M. B., Pravica, M., Krsnik, Ž., et al. (2024) · Biomolecules · doi:10.3390/biom14030302 · Cited by 8
Review on pathogenesis and treatment of Alzheimer's disease
Cai, J., Liu, Y., & Fan, H. (2024) · Developmental Dynamics · doi:10.1002/dvdy.762 · Cited by 10
Walkiewicz, G., Ronisz, A., Ospitalieri, S., Tsaka, G., Tomé, S. O., Vandenberghe, R. R., Arnim, C. A. F. V., Rousseau, F., Schymkowitz, J. W. H., Groef, L. D., et al. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01907-8 · Cited by 8
Inflammasomes in Alzheimer’s Progression: Nrf2 as a Preventive Target
López-Hernández, R., de la Torre-Álamo, M. M., García-Bueno, B., Baroja‐Mazo, A., Fenoy, F. J., & Cuevas, S. (2025) · Antioxidants · doi:10.3390/antiox14020121 · Cited by 9
Silva-Llanes, I., Rodríguez-López, S., González-Naranjo, P., del Sastre, E., López, M. G., Paez, J. A., Campillo, N. E., & Lastres‐Becker, I. (2025) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2025.03.008 · Cited by 8
Bartra, C., Vuraić, K., Yuan, Y., Codony, S., Valdés-Quiroz, H., Casal, C., SLEVIN, M. A., Márquez‐Kisinousky, L., Planas, A. M., Griñán‐Ferré, C., et al. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.114644 · Cited by 8
IC100 blocks inflammasome activation induced by α-synuclein aggregates and ASC specks
Cyr, B. S., Vontell, R., Hadad, R., Vaccari, J. P. D. R., & Keane, R. W. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-00963-8 · Cited by 11
pS396/pS404 (PHF1) tau vaccine outperforms pS199/pS202 (AT8) in rTg4510 tauopathy model
Hulse, J. P., Maphis, N. M., Peabody, J., Bondu, V., Chackerian, B., & Bhaskar, K. (2025) · npj Vaccines · doi:10.1038/s41541-025-01147-4 · Cited by 9
Prabha, S., Choudhury, A., Jawaid, T., Saeed, M. U., Thakur, S. C., & Hassan, M. I. (2025) · 3 Biotech · doi:10.1007/s13205-025-04413-3 · Cited by 8
Guo, Z., Ni, H., Yu, L., Cui, Z., Wang, Y., Zhu, Z., Wei, X., Xia, C., Xu, M., Du, L., et al. (2025) · Advanced Science · doi:10.1002/advs.202510885 · Cited by 8
Environmental Stressors and Neuroinflammation: Linking Climate Change to Alzheimer’s Disease
Caldarelli, M., Rio, P., Gasbarrini, A., Gambassi, G., & Cianci, R. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47110959 · Cited by 8
Sterile innate immune mechanisms in neurodegenerative diseases
Ealy, A., Serapiglia, A. M., & Panicker, N. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.111039 · Cited by 8
Neuroimmune Dysregulation and AI-Driven Therapeutic Strategies in Alzheimer’s Disease
Ghosh, S., Bhaskar, R., Singh, D. K. K., Sharma, S., Yarlagadda, B., Sinha, J. K., & Han, S. S. (2025) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-025-01651-0 · Cited by 11
Recent advances in Alzheimer’s disease: From molecular mechanisms to therapeutic strategies
Rudman, M. D., Ulrich, J. D., & Holtzman, D. M. (2026) · Cell · doi:10.1016/j.cell.2026.06.006 · Cited by 12
Activation of NLRP3 Inflammasome by Virus-Like Particles of Human Polyomaviruses in Macrophages
Lučiūnaitė, A., Dalgėdienė, I., Žilionis, R., Mašalaitė, K., Norkienė, M., Šinkūnas, A., Gedvilaitė, A., Kučinskaitė-Kodzė, I., & Žvirblienė, A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.831815 · Cited by 8
Mechanism of NLRP3 inflammasome activation and its role in Alzheimer’s disease
Gao, X., Zhang, X., Sun, Y., & Dai, X. (2022) · Exploration of Immunology · doi:10.37349/ei.2022.00048 · Cited by 8
Potential drugs for the treatment of Alzheimer’s disease
Montero-Cosme, T. G., Pascual-Mathey, L. I., Hernández‐Aguilar, M. E., Herrera‐Covarrubias, D., Rojas-Durán, F., & Aranda-Abreu, G. E. (2023) · Pharmacological Reports · doi:10.1007/s43440-023-00481-5 · Cited by 8
Liu, M., Liu, R., Yang, M., Ba, Y., Deng, Q., Zhang, Y., Han, L. G., Gao, L., & Huang, H. (2023) · Food and Chemical Toxicology · doi:10.1016/j.fct.2023.113857 · Cited by 8
Can statin preventative treatment inform geroscience‐guided therapeutics?
Guaraldi, G., Erlandson, K. M., Milić, J., LANDAY, A. L., & Montano, M. A. (2023) · Aging Cell · doi:10.1111/acel.13998 · Cited by 8
Lee, Y., Yoon, B., Son, S., Cho, E., Kim, K. B., Choi, E. Y., & Kim, D. (2024) · Cells · doi:10.3390/cells13080675 · Cited by 8
Mouse serum albumin induces neuronal apoptosis and tauopathies
Hou, S., Huang, Y., Zhu, J., Jia, Y., Niu, X.-Y., Yang, J.-J., Yu, X., Du, X.-Y., Liang, S., Cui, F., et al. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01771-6 · Cited by 9
A Mutant Variant of E2F4 Triggers Multifactorial Therapeutic Effects in 5xFAD Mice
López‐Sánchez, N., Ramón‐Landreau, M., Trujillo, C., Garrido‐García, A., & Frade, J. M. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02764-z · Cited by 7
Casaril, A. M., Katsalifis, A., Schmidt, R. M., & Orth, C. B. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.03.120 · Cited by 8
Shi, N., Zheng, Q., & Zhang, H. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00866 · Cited by 8
Reece, A. S., & Hulse, G. K. (2022) · European Archives of Psychiatry and Clinical Neuroscience · doi:10.1007/s00406-022-01446-0 · Cited by 8
Zhang, Y., Liu, D., Yao, X., Wen, J., Wang, Y., & Zhang, Y. (2022) · Neuroscience Letters · doi:10.1016/j.neulet.2022.136770 · Cited by 9
Zhang, L., Song, H., Ding, J., Wang, D., Zhu, S.-P., Liu, C., Jin, X., & Chen, J. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/8661200 · Cited by 8
Huo, C., Chen, M., Hour, T., Huang, L., Fong, Y.-O., Kuo, Y., Yang, Y., & Chuu, C. (2022) · Brain Sciences · doi:10.3390/brainsci12091134 · Cited by 8
Disease mechanisms as subtypes: Inflammation in Parkinson disease and related disorders
Standaert, D. G., Harms, A. S., Childers, G. M., & Webster, J. M. (2023) · Handbook of clinical neurology · doi:10.1016/b978-0-323-85555-6.00011-4 · Cited by 8
Wang, L., Wei, Y., Sun, Z., Jiang, L., Yin, Y., Zheng, P., Fu, Y., Wang, H., Li, C., & Wang, J. (2023) · Neuroscience · doi:10.1016/j.neuroscience.2023.07.004 · Cited by 8
Komorowska, J., Wątroba, M., Bednarzak, M., Grabowska, A. D., & Szukiewicz, D. (2023) · Medical Science Monitor · doi:10.12659/msm.941044 · Cited by 8
Glycogen Synthase Kinase-3β, NLRP3 Inflammasome, and Alzheimer’s Disease
Jia, Y.-R., Guo, Z.-Q., Guo, Q., & Wang, X. (2023) · Current Medical Science · doi:10.1007/s11596-023-2788-4 · Cited by 10
Distinct responses of human peripheral blood cells to different misfolded protein oligomers
Leal‐Lasarte, M., Mannini, B., Chiti, F., Vendruscolo, M., Dobson, C. M., Roodveldt, C., & Pozo, D. (2021) · Immunology · doi:10.1111/imm.13377 · Cited by 8
Circular RNA aptamers ameliorate AD-relevant phenotypes by targeting PKRPreprint
Feng, X., Jiang, B., Zhai, S.-N., Liu, C., Wu, H., Zhu, B.-Q., Wei, M.-Y., Wei, J., Yang, L. C., & Chen, L. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.27.583257 · Cited by 8
Zhang, J., Xie, D., Jiao, D., Zhou, S. Y., Liu, S., Ju, Z., Hu, L., Li, Q., Yao, C., & Chen, Z. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e32688 · Cited by 9
Quan, W., Decker, Y., Luo, Q., Chemla, A., Chang, H., Li, D., Fassbender, K. C., & Liu, Y. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1471005 · Cited by 7
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
