INPP5D/SHIP1 regulates inflammasome activation in human microglia
Open accessAbstract
Microglia and neuroinflammation are implicated in the development and progression of Alzheimer’s disease (AD). To better understand microglia-mediated processes in AD, we studied the function of INPP5D/SHIP1, a gene linked to AD through GWAS. Immunostaining and single nucleus RNA sequencing confirmed that INPP5D expression in the adult human brain is largely restricted to microglia. Examination of prefrontal cortex across a large cohort revealed reduced full length INPP5D protein levels in AD patient brains compared to cognitively normal controls. The functional consequences of reduced INPP5D activity were evaluated in human induced pluripotent stem cell derived microglia (iMGLs), using both pharmacological inhibition of the phosphatase activity of INPP5D and genetic reduction in copy number. Unbiased transcriptional and proteomic profiling of iMGLs suggested an upregulation of innate immune signaling pathways, lower levels of scavenger receptors, and altered inflammasome signaling with INPP5D reduction. INPP5D inhibition induced the secretion of IL-1ß and IL-18, further implicating inflammasome activation. Inflammasome activation was confirmed through visualization of inflammasome formation through ASC immunostaining in INPP5D-inhibited iMGLs, increased cleaved caspase-1 and through rescue of elevated IL-1ß and IL-18 with caspase-1 and NLRP3 inhibitors. This work implicates INPP5D as a regulator of inflammasome signaling in human microglia.
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iMGs with biallelic INPP5D loss-of-function alleles and microglia from AD brain tissue both show a reduction in RNA levels of NF-kB pathway genes.
“For example, iMGs with biallelic INPP5D LOF alleles and microglia from AD brain tissue both show a reduction in RNA levels of NF-kB pathway genes.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
The section on chronic genetic reduction reports loss-of-function mutations in a single INPP5D allele, not biallelic loss. The section on acute inhibition reports upregulated NF-κB signaling in treated iMGLs, while the AD brain analysis reports reduced INPP5D protein rather than reduced NF-κB-pathway RNA in microglia. (LLM, conf=0.89)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredOverexpression of INPP5D in iMGs showed an elevation in RNA levels of NF-kB pathway genes.
“In accord, overexpression of INPP5D in iMGs showed an elevation in RNA levels of NF-kB pathway genes, suggesting that microglia from AD brains may display changes relevant to reduced SHIP1 activity [161].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
The section on acute INPP5D inhibition (page unavailable) reports increased NF-κB pathway activity after treating iMGLs with 3AC, an INPP5D inhibitor. It does not report this elevation after INPP5D overexpression; the claimed direction of manipulation is opposite to the one studied. (LLM, conf=0.88)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredSHIP1 may be aggregated and perhaps aqueous-insoluble in the AD brain.
“suggesting that SHIP1 may be aggregated (and perhaps aqueous-insoluble) in the AD brain [161].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
In “INPP5D expression is restricted to human microglia and reduced in Alzheimer’s disease” (page unavailable), the authors suggest that TBS-soluble extracts may not capture all full-length INPP5D/SHIP1. They note that many proteins form insoluble aggregates in high-pathology brains, but do not show that SHIP1 itself aggregates; their urea-extract analysis instead finds lower SHIP1 levels in AD brain. (LLM, conf=0.84)
Experimental — accuracy not yet measuredAD brains displayed increased immunostaining for SHIP1 compared to age and sex-matched brain tissue from non-cognitively impaired individuals when a C-terminally directed antibody to SHIP1 was used.
“However, we found that AD brains displayed increased immunostaining for SHIP1 compared to age and sex-matched brain tissue from non-cognitively impaired individuals when a C-terminally directed antibody to SHIP1 was used.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
The section on INPP5D expression reports an age- and sex-matched comparison of AD and non-cognitively impaired brain tissue, and the Figure 1 legend documents INPP5D immunostaining of human brain sections. But the paper does not report increased staining in AD with a C-terminally directed antibody; its quantified Western blots instead show reduced full-length INPP5D protein in AD. Those blots are a different assay, so they do not directly contradict the claimed staining result. (LLM, conf=0.83)
Experimental — accuracy not yet measuredPeptide-level mass spectrometry analyses of TBS- and urea-solubilized postmortem brain lysates revealed a reduction of peptides encoding the phosphatase domain of SHIP1 in the AD brain.
“Peptide-level mass spectrometry analyses of TBS- and urea-solubilized postmortem brain lysates revealed a reduction of peptides encoding the phosphatase domain of SHIP1 in the AD brain [161].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
The section “INPP5D expression is restricted to human microglia and reduced in Alzheimer's disease” (page unavailable) reports reduced full-length SHIP1/INPP5D protein in AD brain using TBS- and urea-solubilized postmortem tissue. It identifies Western blotting, not peptide-level mass spectrometry, as the method; it does not report a reduction specifically in peptides encoding the phosphatase domain. (LLM, conf=0.89)
Experimental — accuracy not yet measured
Acute pharmacological inhibition of SHIP1's phosphatase activity as well as genetic ablation of a single copy of INPP5D in iMGs induced the secretion of IL-18 and IL-1β that was blocked by NLRP3 inhibition with MCC950 and also with caspase-1 inhibitors.
“Acute pharmacological inhibition of SHIP1’s phosphatase activity as well as genetic ablation of a single copy of INPP5D in iMGs induced the secretion of IL-18 and IL-1β that was blocked by NLRP3 inhibition with MCC950 and also with caspase-1 inhibitors [161].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
Split into 2 atoms — 1 confirmed, 1 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measuredLower SHIP1 levels were significantly associated with elevated IL-18 protein levels in brain lysates, with the correlation driven by data from AD brain tissue.
“When levels of secreted IL-1β and IL-18 were compared to aqueous-soluble SHIP1 levels in brain lysates, lower SHIP1 levels were signficantly associated with elevated IL-18 protein levels, with the correlation driven by data from AD brain tissue.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
The section on INPP5D expression in human microglia reports significantly lower INPP5D/SHIP1 protein in AD brain tissue, and the paper reports increased IL-18 secretion when INPP5D is reduced in cultured microglia. However, our copy does not report a significant correlation between SHIP1 and IL-18 levels in brain lysates, or show that such a correlation was driven by AD tissue. No page numbers were available in the indexed passages. (LLM, conf=0.82)
Experimental — accuracy not yet measuredLower SHIP1 levels were significantly correlated with a higher percentage of microglia with ASC specks in the AD brain.
“Further, comparison of immunoreactivity for SHIP1 and ASC specks in brain tissue from aged individuals revealed that lower SHIP1 levels were significantly correlated with a higher percentage of microglia with ASC specks in the AD brain [161].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
The section ‘INPP5D expression is restricted to human microglia and reduced in Alzheimer's disease’ (page unavailable) reports lower INPP5D/SHIP1 protein levels in AD brain tissue. The section ‘INPP5D inhibition results in inflammasome activation’ (page unavailable) reports ASC specks after SHIP1 inhibition in iPSC-derived microglia. Neither section reports a significant correlation between SHIP1 levels and the percentage of microglia with ASC specks in AD brain tissue. (LLM, conf=0.88)
Experimental — accuracy not yet measuredReduction of INPP5D increased the secretion of IL-18 and IL-1β but lowered their mRNA expression.
“Though reduction of INPP5D increased the secretion of IL-18 and IL-1β, it lowered their mRNA expression, suggesting that reduction of SHIP1 activity positively regulates the activation step but may act through a feedback mechanism to inhibit the priming step for the NLRP3 inflammasome [161] (Fig. 3D).”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
In “INPP5D inhibition results in inflammasome activation” (page unavailable), the paper reports that 3AC treatment increased secretion of both IL-1β and IL-18 while reducing IL1B mRNA. It does not report a corresponding reduction in IL18 mRNA, so the claim that both had lowered mRNA expression is unsupported. (LLM, conf=0.88)
Experimental — accuracy not yet measuredLevels of full-length SHIP1 protein that include its phosphatase domain are reduced in brain tissue of individuals with AD.
“levels of full-length SHIP1 protein that include its phosphatase domain are reduced65.”
From INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia (2025) · cites this paper as [65]
The mRNA expression of INPP5D is increased in brain tissue of individuals with AD.
“while the mRNA expression of INPP5D is increased in brain tissue of individuals with AD”
From INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia (2025) · cites this paper as [65]
Aqueous-soluble SHIP1 protein levels are reduced in brain tissue from individuals diagnosed with AD compared with non-AD individuals.
“we also found that aqueous-soluble SHIP1 protein levels are reduced in brain tissue from individuals diagnosed with AD compared with non-AD individuals [161].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
Data from the authors' group agrees with the elevation of INPP5D mRNA levels in human AD post-mortem brains.
“While data from our group agrees with the elevation of INPP5D mRNA levels in human AD post-mortem brains, we also found that aqueous-soluble SHIP1 protein levels are reduced in brain tissue from individuals diagnosed with AD compared with non-AD individuals [161].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
Acute pharmacological inhibition of SHIP1 with 3α-aminocholestane (3AC) in human iPSC-derived microglial cells upregulated the mRNA and protein expression of Axl.
“Acute pharmacological inhibition of SHIP1 with 3α-aminocholestane (3AC) in human iPSC-derived microglial cells (iMGs) upregulated the mRNA and protein expression of Axl [161].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
The authors recently discovered a direct connection between SHIP1 and the NLRP3 inflammasome in iMGs.
“Corroborating SHIP1’s role in modulating microglial activation and inflammation, we recently discovered a direct connection between SHIP1 and the NLRP3 inflammasome in iMGs.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
Microglia from AD brains may display changes relevant to reduced SHIP1 activity.
“suggesting that microglia from AD brains may display changes relevant to reduced SHIP1 activity [161].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
Reduction of SHIP1 activity positively regulates the activation step but may act through a feedback mechanism to inhibit the priming step for the NLRP3 inflammasome.
“suggesting that reduction of SHIP1 activity positively regulates the activation step but may act through a feedback mechanism to inhibit the priming step for the NLRP3 inflammasome [161] (Fig. 3D).”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
There are multiple pools of SHIP1 in the brain, and in the AD brain, enzymatically active SHIP1 is reduced.
“Together, these findings support the hypothesis that there are multiple pools of SHIP1 in the brain, and that in the AD brain, enzymatically active SHIP1 is reduced.”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
Plaque-associated microglia displayed higher SHIP1 immunostaining than microglia distal to plaques.
“Plaque-associated microglia clearly displayed higher SHIP1 immunostaining than microglia distal to plaques, SHIP1 levels significantly correlated with microglial ramification, where less ramified and putatively more activated plaque-associated microglia had lower levels of SHIP1 immunostaining [161].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
The Introduction discusses amyloid plaques, and the Immunocytochemistry of iMGLs and human-brain immunostaining methods describe SHIP1 staining, but none reports a staining comparison between microglia near and distal to plaques. Searches for plaque proximity, SHIP1 staining, and ramification found no passage establishing the claimed difference; no page numbers were available in our copy. (LLM, conf=0.72)
Experimental — accuracy not yet measuredSHIP1 levels significantly correlated with microglial ramification, where less ramified and putatively more activated plaque-associated microglia had lower levels of SHIP1 immunostaining.
“SHIP1 levels significantly correlated with microglial ramification, where less ramified and putatively more activated plaque-associated microglia had lower levels of SHIP1 immunostaining [161].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
The Immunocytochemistry of iMGLs section describes SHIP1 staining, but does not report a correlation with microglial ramification. Searches for ramification, plaque-associated microglia, and SHIP1 immunostaining found no passage reporting lower SHIP1 staining in less-ramified plaque-associated cells; page numbers were unavailable. (LLM, conf=0.72)
Experimental — accuracy not yet measuredIn AD brain tissue, SHIP1 localization shifted from diffuse to punctate patterns in microglia.
“In AD brain tissue, SHIP1 localization was shifted from diffuse to punctate patterns in microglia, suggesting that SHIP1 may be aggregated (and perhaps aqueous-insoluble) in the AD brain [161].”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [161]
The section on INPP5D expression in human microglia (page unavailable) reports that INPP5D/SHIP1 and IBA1 co-localize in brain tissue and that INPP5D protein levels are lower in AD tissue. It does not describe a shift from diffuse to punctate localization. Searches for “punctate,” “diffuse,” and SHIP1 aggregation found no passage establishing that pattern change. (LLM, conf=0.73)
Experimental — accuracy not yet measured
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Self-citationRecent progress in phospholipase A2 research: From cells to animals to humans
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CD36 Mediates the Innate Host Response to β-Amyloid
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O’Donoghue, M. L., Braunwald, E., White, H. D., Steen, D. P., Lukas, M. A., Tarka, E., Steg, P. G., Hochman, J. S., Bode, C., Maggioni, A. P., et al. (2014) · JAMA · doi:10.1001/jama.2014.11061 · Cited by 456 · see citing works
McQuade, A., Coburn, M., Tu, C. H., Hasselmann, J., Davtyan, H., & Blurton-Jones, M. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0297-x · Cited by 449 · see citing works
TREM2- and DAP12-dependent activation of PI3K requires DAP10 and is inhibited by SHIP1
Peng, Q., Malhotra, S., Torchia, J. A., Kerr, W. G., Coggeshall, K. M., & Humphrey, M. B. (2010) · Science Signaling · doi:10.1126/scisignal.2000500 · Cited by 413 · see citing works
Bekker‐Jensen, D. B., Martínez‐Val, A., Steigerwald, S., Rüther, P. L., Fort, K. L., Arrey, T. N., Harder, A., Makarov, A., & Olsen, J. V. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir119.001906 · Cited by 409 · see citing works
ASC filament formation serves as a signal amplification mechanism for inflammasomes
Dick, M. S., Sborgi, L., Rühl, S., Hiller, S., & Brož, P. (2016) · Nature Communications · doi:10.1038/ncomms11929 · Cited by 405 · see citing works
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Self-citationStructure, function, and biology of SHIP proteins
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The P2X7 receptor directly interacts with the NLRP3 inflammasome scaffold protein
Franceschini, A., Capece, M., Chiozzi, P., Falzoni, S., Sanz, J. M., Sarti, A. C., Bonora, M., Pinton, P., & Di Virgilio, F. (2015) · The FASEB Journal · doi:10.1096/fj.14-268714 · Cited by 225 · see citing works
Global quantitative analysis of the human brain proteome in Alzheimer’s and Parkinson’s Disease
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Rapid and efficient induction of functional astrocytes from human pluripotent stem cells
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Self-citationSignalling thresholds and negative B-cell selection in acute lymphoblastic leukaemia
Chen, Z., Shojaee, S., Buchner, M., Geng, H., Lee, J. W., Klemm, L., Titz, B., Graeber, T. G., Park, E., Tan, Y. X., et al. (2015) · Nature · doi:10.1038/nature14231 · Cited by 149 · see citing works
Multi-cellular communities are perturbed in the aging human brain and Alzheimer’s disease
Cain, A., Taga, M., McCabe, C., Green, G., Hekselman, I., White, C. C., Lee, D. I., Gaur, P., Rozenblatt-Rosen, O., Zhang, F., et al. (2020) · doi:10.1101/2020.12.22.424084 · Cited by 143 · see citing works
Self-citationMulticellular communities are perturbed in the aging human brain and Alzheimer’s disease
Cain, A., Taga, M., McCabe, C., Green, G. S., Hekselman, I., White, C. C., Lee, D. I., Gaur, P., Rozenblatt-Rosen, O., Zhang, F., et al. (2023) · Nature Neuroscience · doi:10.1038/s41593-023-01356-x · Cited by 142 · see citing works
Self-citationBrooks, R., Fuhler, G. M., Iyer, S., Smith, M. J., Park, M.-Y., Paraiso, K. H. T., Engelman, R. W., & Kerr, W. G. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902844 · Cited by 140 · see citing works
Global quantitative analysis of the human brain proteome and phosphoproteome in Alzheimer’s disease
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Self-citationInhibitor and activator: dual functions for SHIP in immunity and cancer
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Deletion of Alzheimer's disease‐associated CD33 results in an inflammatory human microglia phenotype
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Pan-SHIP1/2 inhibitors promote microglia effector functions essential for CNS homeostasis
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Possible role of scavenger receptor SRCL in the clearance of amyloid‐βin Alzheimer's disease
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Coordinate Expansion of Murine Hematopoietic and Mesenchymal Stem Cell Compartments by SHIPi
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Triazole derivatives: A series of Darapladib analogues as orally active Lp-PLA2 inhibitors
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Moving beyond amyloid and tau to capture the biological heterogeneity of Alzheimer’s disease
Young‐Pearse, T. L., Lee, H., Hsieh, Y., Chou, V., & Selkoe, D. J. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.03.005 · Cited by 99 · see citing works
Self-citationTerzioglu, G., & Young-Pearse, T. L. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00674-9 · Cited by 95 · see citing works
Self-citationMatera, A., Compagnion, A.-C., Pedicone, C., Kotah, J. M., Ivanov, A., Monsorno, K., Labouèbe, G., Leggio, L., Pereira-Iglesias, M., Beule, D., et al. (2025) · Immunity · doi:10.1016/j.immuni.2024.11.003 · Cited by 34 · see citing works
Cardona, C. L., Wei, L., Kim, J., Angeles, E., Singh, G., Chen, S., Patel, R., Ifediora, N., Canoll, P., Teich, A. F., et al. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03562-9 · Cited by 8 · see citing works
Regulation of Microglial Signaling by Lyn and SHIP-1 in the Steady-State Adult Mouse Brain
Chu, E., Mychasiuk, R., Tsantikos, E., Raftery, A. L., L’Estrange-Stranieri, E., Dill, L. K., Semple, B. D., & Hibbs, M. L. (2023) · Cells · doi:10.3390/cells12192378 · Cited by 8 · see citing works
INPP5D/SHIP1 regulates endo-lysosomal function and cargo-selective phagocytosis in human microglia
Terzioglu, G., Karp, E. S., Heuer, S. E., Chadarevian, J. P., Ahsan, F. M., Haage, V. C., Davtyan, H., Fogo, G. M., Curle, A. J., Ashour, N., et al. (2025) · doi:10.1101/2025.10.27.684632 · Cited by 3 · see citing works
Self-citationDavtyan, H., Naguib, S. A., Voskobiynyk, Y., Chadarevian, J. P., Capocchi, J. K., Giacchino, J. L., Eskandari‐Sedighi, G., DeNittis, V. R., Ford, J. B., Agababian, A., et al. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00978-6 · Cited by 2 · see citing works
Li, Y.-J., Zhang, X. F., Fu, J.-N., & Zhang, T. (2026) · Inflammation · doi:10.1007/s10753-025-02413-2 · Cited by 1 · see citing works
Xi, R., Zheng, X., Zhao, J., & Fu, Y. (2026) · Journal of Neuroinflammation · doi:10.1186/s12974-026-03819-x · Cited by 1 · see citing works
- Authors
- 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.
- Affiliations
- Brigham and Women's Hospital (US)
- Columbia University Irving Medical Center (US)
- Emory University (US)
- Rush University Medical Center (US)
- ORCID
- Venue
- bioRxiv (Cold Spring Harbor Laboratory)
- Publisher
- openRxiv
- Published
- 2023-02-26
- PMC
- PMC9980181
- OpenAlex
- W4322207826
- Cited by
- 8
- References
- 79
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 1 · 2023: 3
- Type
- posted content
- Language
- en
- Open access
- green
- doi.org
- Locations
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion)
- Funders
- Brigham and Women's Hospital
- Emory University
- National Institutes of Health
- Harvard Stem Cell Institute
- National Institute on Aging (R01AG017917, F31AG063398, U01AG046152, R01AG015819, P30AG010161, U01AG061356, P30AG072975)
- Topics
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Keywords
- INPP5D, SHIP1, microglia, inflammasome activation, Alzheimer's disease, neuroinflammation, IL-1β, IL-18, caspase-1, NLRP3 inflammasome, ASC, induced pluripotent stem cell-derived microglia, phosphatase activity, prefrontal cortex, innate immune signaling, scavenger receptors
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.
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