The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo
Open accessAbstract
Emerging studies suggest a role for tau in regulating the biology of RNA binding proteins (RBPs). We now show that reducing the RBP T-cell intracellular antigen 1 (TIA1) in vivo protects against neurodegeneration and prolongs survival in transgenic P301S Tau mice. Biochemical fractionation shows co-enrichment and co-localization of tau oligomers and RBPs in transgenic P301S Tau mice. Reducing TIA1 decreased the number and size of granules co-localizing with stress granule markers. Decreasing TIA1 also inhibited the accumulation of tau oligomers at the expense of increasing neurofibrillary tangles. Despite the increase in neurofibrillary tangles, TIA1 reduction increased neuronal survival and rescued behavioral deficits and lifespan. These data provide in vivo evidence that TIA1 plays a key role in mediating toxicity and further suggest that RBPs direct the pathway of tau aggregation and the resulting neurodegeneration. We propose a model in which dysfunction of the translational stress response leads to tau-mediated pathology.
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 cell body MAPT pathology is particularly important because this pathology colocalizes with markers of the translational stress response, such as stress granule proteins HNRNPA2B1, TIA1, EIF3n and PABP, and also neuronal death (as shown by cleaved caspase 3 and loss of NeuN positive cells) (Ash et al., 2014; Apicco et al., 2018; Maziuk et al., 2018; Apicco et al., 2019; Jiang et al., 2019, 2021”
From β-amyloid accumulation enhances microtubule associated protein tau pathology in an APPNL-G-F/MAPTP301S mouse model of Alzheimer’s disease (2024) · cites this paper as Apicco et al., 2018
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
“Tau-RBP interactions disrupt RNA splicing resulting in gene dysregulation and neurotoxicity (Apicco et al., 2018; Bai et al., 2013; Hsieh et al., 2019).”
From Selective removal of astrocytic APOE4 strongly protects against tau-mediated neurodegeneration and decreases synaptic phagocytosis by microglia (2021) · cites this paper as Apicco et al., 2018
Experimental — accuracy not yet measured
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
Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Biomolecular condensates: organizers of cellular biochemistry
Banani, S. F., Lee, H. O., Hyman, A. A., & Rosen, M. K. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.7 · Cited by 6,058
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791 · cited 1×
“The classic model for protein aggregation in neurodegenerative diseases posits that proteins with disordered or hydrophobic regions inappropriately aggregate through a process of random association that has little or no biological function 34 .”
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927
Molliex, A., Temirov, J. P., Lee, J., Coughlin, M., Kanagaraj, A., Kim, H. J., Mittag, T., & Taylor, J. P. (2015) · Cell · doi:10.1016/j.cell.2015.09.015 · Cited by 2,690
Phase transitions in the assembly of multivalent signalling proteins
Li, P., Banjade, S., Cheng, H., Kim, S., Chen, B., Guo, L., Llaguno, M. C., Hollingsworth, J. V., King, D., Banani, S. F., et al. (2012) · Nature · doi:10.1038/nature10879 · Cited by 2,565 · cited 1×
“These proteins all contain low complexity domains whose biophysical properties promote aggregation under normal physiological conditions 9–12 , 35 .”
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251 · cited 1×
“Tau is normally located in axons where it functions to bind and stabilize microtubules, but in tauopathies, pathological tau accumulates in the somatodendritic compartment, where it form oligomers and fibrils 15 .”
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · cited 11×
“PS19 (B6;C3-Tg(Prnp-MAPT*P301S)PS19Vle/J, stock #008169) and C57BL/6J (stock #000664) mice were purchased from Jackson Laboratory 16 .”
InfluentialDecoding ALS: from genes to mechanism
Taylor, J. P., Brown, R. H., & Cleveland, D. W. (2016) · Nature · doi:10.1038/nature20413 · Cited by 2,120 · cited 5×
“This work suggests that the pathophysiology of tauopathy is dependent on the interaction of tau with RBPs, and add tauopathies such as AD and FTD to the growing list of diseases linked to the dysfunction of RNA metabolism.”
InfluentialTau Suppression in a Neurodegenerative Mouse Model Improves Memory Function
SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014
Coexisting Liquid Phases Underlie Nucleolar Subcompartments
Feric, M., Vaidya, N., Harmon, T. S., Mitrea, D. M., Zhu, L., Richardson, T. M., Kriwacki, R. W., Pappu, R. V., & Brangwynne, C. P. (2016) · Cell · doi:10.1016/j.cell.2016.04.047 · Cited by 1,934
Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811 · cited 1×
“RBPs such as TIA1 have multiple roles in the cell, regulating RNA localization and utilization in the soma and dendritic arbor, and processes such as splicing and RNA polymerase procession in the nucleus 43, 44 .”
Nott, T. J., Petsalaki, E., Farber, P., Jervis, D., Fussner, E., Plochowietz, A., Craggs, T. D., Bazett-Jones, D. P., Pawson, T., Forman-Kay, J. D., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.013 · Cited by 1,803
Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins
Lin, Y., Protter, D. S. W., Rosen, M. K., & Parker, R. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.018 · Cited by 1,593 · cited 1×
“These proteins all contain low complexity domains whose biophysical properties promote aggregation under normal physiological conditions 9–12 , 35 .”
Object recognition test in mice
Leger, M., Quiedeville, A., Bouet, V., Haelewyn, B., Boulouard, M., Schumann-Bard, P., & Freret, T. (2013) · Nature Protocols · doi:10.1038/nprot.2013.155 · Cited by 1,357
Compositional Control of Phase-Separated Cellular Bodies
Banani, S. F., Rice, A. M., Peeples, W. B., Lin, Y., Jain, S., Parker, R., & Rosen, M. K. (2016) · Cell · doi:10.1016/j.cell.2016.06.010 · Cited by 1,257
Stress granules: the Tao of RNA triage
Anderson, P., & Kedersha, N. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.12.003 · Cited by 1,161
Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies
Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986
Stress granules as crucibles of ALS pathogenesis
Li, Y. R., King, O. D., Shorter, J., & Gitler, A. D. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201302044 · Cited by 948 · cited 1×
“Dysfunction of RBPs is implicated in multiple neurodegenerative diseases 32, 33 .”
RNA phase transitions in repeat expansion disorders
(2017) · doi:10.1038/nature22386 · Cited by 911
The neurobiological basis of spontaneous alternation
Lalonde, R. (2002) · Neuroscience & Biobehavioral Reviews · doi:10.1016/s0149-7634(01)00041-0 · Cited by 857 · cited 1×
“While both SAT and NOR tasks depend in part on hippocampal function, the SAT depends on additional circuitry, including the prefrontal cortex, basal forebrain, and dorsal striatum 19 whereas the NOR more selectively depends on the hippocampus and perirhinal cortex 20 .”
The genetics of myelodysplastic syndrome: from clonal haematopoiesis to secondary leukaemia
Sperling, A. S., Gibson, C. J., & Ebert, B. L. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.112 · Cited by 706
Assessing rodent hippocampal involvement in the novel object recognition task. A review
Cohen, S. J., & Stackman, R. W. (2014) · Behavioural Brain Research · doi:10.1016/j.bbr.2014.08.002 · Cited by 592 · cited 1×
“While both SAT and NOR tasks depend in part on hippocampal function, the SAT depends on additional circuitry, including the prefrontal cortex, basal forebrain, and dorsal striatum 19 whereas the NOR more selectively depends on the hippocampus and perirhinal cortex 20 .”
Caspase activation precedes and leads to tangles
de Calignon, A., Fox, L. M., Pitstick, R., Carlson, G. A., Bacskai, B. J., Spires-Jones, T. L., & Hyman, B. T. (2010) · Nature · doi:10.1038/nature08890 · Cited by 517
Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy
Berger, Z., Roder, H. M., Hanna, A., Carlson, A. M., Rangachari, V., Yue, M., Wszołek, Z. K., Ashe, K. H., Knight, J. A., Dickson, D. W., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0587-07.2007 · Cited by 503 · cited 1×
“The insoluble material (S1p) from the TBS-extractable fraction contains oligomeric tau species that correlate with neurodegeneration in rTg4510 mice, while the P3 fraction contains mostly fibrillar, hyper-phosphorylated (CP13-/PHF1-positive) tau 29 .”
Mechanistic insights into mammalian stress granule dynamics
Panas, M. D., Ivanov, P. V., & Anderson, P. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201609081 · Cited by 374 · cited 1×
“Mice were aged to 3, 6, and 9 months for analysis by the behavioral, biochemical, and histological approaches described below.”
Regulated protein aggregation: stress granules and neurodegeneration
Wolozin, B. L. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-56 · Cited by 350 · cited 1×
“Dysfunction of RBPs is implicated in multiple neurodegenerative diseases 32, 33 .”
Self-citationInteraction of tau with the RNA-Binding Protein TIA1 Regulates tau Pathophysiology and Toxicity
Vanderweyde, T. E., Apicco, D. J., Youmans-Kidder, K., Ash, P. E. A., Cook, C. N., da Rocha, E. L., Jansen‐West, K. R., Frame, A. A., Citro, A., Leszyk, J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.045 · Cited by 346 · cited 5×
“We also observed that the association of tau with SGs promotes its aggregation 13 .”
InfluentialSelf-citationC-terminal inhibition of tau assembly in vitro and in Alzheimer’s disease
Abraha, A., Ghoshal, N., Gamblin, T. C., Cryns, V. L., Berry, R. W., Kuret, J., & Binder, L. I. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.21.3737 · Cited by 326
RNA stores tau reversibly in complex coacervates
Zhang, X., Lin, Y., Eschmann, N. A., Zhou, H., Rauch, J. N., Hernández, I., Guzman, E., Kosik, K. S., & Han, S. (2017) · PLoS Biology · doi:10.1371/journal.pbio.2002183 · Cited by 312 · cited 2×
“The putative importance of tau oligomers in the interactions with TIA1 and RNA is supported by a recent study demonstrating that tau phase separates in the presence of RNA 41 .”
Lost after translation: missorting of Tau protein and consequences for Alzheimer disease
Zempel, H., & Mandelkow�, E. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.08.004 · Cited by 284 · cited 1×
“The process of tau aggregation is known to proceed through multiple steps, including misfolding, oligomerization and fibrillization, but how RBPs might interact with these intermediates is unknown 42 .”
Frontotemporal lobar degeneration: defining phenotypic diversity through personalized medicine
Irwin, D. J., Cairns, N. J., Grossman, M., McMillan, C. T., Lee, E. B., Deerlin, V. M. V., Lee, V. M. ‐., & Trojanowski, J. Q. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1380-1 · Cited by 278
Takeuchi, H., Iba, M., Inoue, H., Higuchi, M., Takao, K., Tsukita, K., Karatsu, Y., Iwamoto, Y., Miyakawa, T., Suhara, T., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021050 · Cited by 247 · cited 1×
“Previous studies found that PS19 mice exhibit cognitive impairment 18 .”
Contrasting Pathology of the Stress Granule Proteins TIA-1 and G3BP in Tauopathies
Vanderweyde, T. E., Yu, W. H., Varnum, M. M., Liu‐Yesucevitz, L., Citro, A., Ikezu, T., Duff, K., & Wolozin, B. L. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1592-12.2012 · Cited by 235
Self-citationPhillips, K., Kedersha, N., Shen, L., Blackshear, P. J., & Anderson, P. J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400148101 · Cited by 199
Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo
Kuchibhotla, K. V., Wegmann, S., Kopeikina, K. J., Hawkes, J., Rudinskiy, N., Andermann, M. L., Spires-Jones, T. L., Bacskai, B. J., & Hyman, B. T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318807111 · Cited by 193 · cited 1×
“This possibility seemed particularly plausible given the recent findings that neurons containing NFT-like inclusions remain functional and that different strains of tau aggregates exhibit distinct patterns of propagation and pathophysiology when injected into tauopathy mice 23–27 .”
Meier, S., Bell, M., Lyons, D. N., Rodriguez-Rivera, J., Ingram, A., Fontaine, S. N., Mechas, E., Chen, J., Wolozin, B., LeVine, H., et al. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.3029-15.2016 · Cited by 190 · cited 1×
“Somatodendritic mislocalization would allow tau to interact with RBPs, RNA, and ribosomes, which provides a mechanism through which tau can inhibit protein synthesis 40 .”
Self-citationStructural and functional changes in tau mutant mice neurons are not linked to the presence of NFTs
Rocher, A. B., Crimins, J. L., Amatrudo, J. M., Kinson, M. S., Todd-Brown, M. A., Lewis, J., & Luebke, J. I. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.07.029 · Cited by 187 · cited 2×
“This possibility seemed particularly plausible given the recent findings that neurons containing NFT-like inclusions remain functional and that different strains of tau aggregates exhibit distinct patterns of propagation and pathophysiology when injected into tauopathy mice 23–27 .”
Self-citationRNA Protein Interaction in Neurons
Darnell, R. B. (2013) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-062912-114322 · Cited by 181 · cited 1×
“RBPs such as TIA1 have multiple roles in the cell, regulating RNA localization and utilization in the soma and dendritic arbor, and processes such as splicing and RNA polymerase procession in the nucleus 43, 44 .”
RNA-binding proteins with prion-like domains in ALS and FTLD-U
Gitler, A. D., & Shorter, J. (2011) · Prion · doi:10.4161/pri.5.3.17230 · Cited by 167
Dysregulation of RNA Binding Protein Aggregation in Neurodegenerative Disorders
Maziuk, B. F., Ballance, H. I., & Wolozin, B. L. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00089 · Cited by 147
Self-citationPathological stress granules in Alzheimer’s disease
Ash, P. E. A., Vanderweyde, T. E., Youmans, K. L., Apicco, D. J., & Wolozin, B. (2014) · Brain Research · doi:10.1016/j.brainres.2014.05.052 · Cited by 129
Self-citationDing, H., Matthews, T. A., & Johnson, G. V. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511697200 · Cited by 112 · cited 1×
“Tau phosphorylation leads to aggregation of tau proteins 21, 22 .”
Sahara, N., Deture, M. A., Ren, Y., Ebrahim, A.-S., Kang, D., Knight, J. A., Volbracht, C., Pedersen, J. T., Dickson, D. W., Yen, S.-H. C., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121093 · Cited by 108 · cited 1×
“Biochemical fractionation studies identify tau species with distinct structural properties that are apparent upon separation of TBS-extractable (S1), sarkosyl-soluble (S3), and sarkosyl-insoluble (P3) fractions 28 .”
Combs, B., Hamel, C., & Kanaan, N. M. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.05.016 · Cited by 93 · cited 1×
“S10) 30 .”
Self-citationInternalized Tau sensitizes cells to stress by promoting formation and stability of stress granules
Brunello, C. A., Yan, X., & Huttunen, H. J. (2016) · Scientific Reports · doi:10.1038/srep30498 · Cited by 89 · cited 15×
“These results now allow us to extend the model of tau aggregation to propose that tau oligomers selectively associate with RBPs, raising the possibility that tau oligomers might be an active species in promoting pSGs and the translational stress response.”
Influential
Cited by
Sorted by citations
Protein Phase Separation: A New Phase in Cell Biology
Boeynaems, S., Alberti, S., Fawzi, N. L., Mittag, T., Polymenidou, M., Rousseau, F., Schymkowitz, J. W. H., Shorter, J., Wolozin, B. L., Bosch, L. V. D., et al. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.004 · Cited by 2,001
Self-citationBiomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing
Alberti, S., & Hyman, A. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00326-6 · Cited by 1,165
Stress granules and neurodegeneration
Wolozin, B., & Ivanov, P. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0222-5 · Cited by 810
Self-citationConverging pathways in neurodegeneration, from genetics to mechanisms
Gan, L., Cookson, M. R., Petrucelli, L., & Spada, A. R. L. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0237-7 · Cited by 500
Stress Granule Assembly Disrupts Nucleocytoplasmic Transport
Zhang, K., Daigle, J. G., Cunningham, K. M., Coyne, A. N., Ruan, K., Grima, J. C., Bowen, K., Wadhwa, H., Yang, P., Rigo, F., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.025 · Cited by 420
“Indeed, loss of SG proteins Ataxin-2 or TIA-1 has been shown to suppress toxicity in yeast and animal models of ALS or tauopathies (Apicco et al., 2018; Elden et al., 2010; Kim et al., 2014).”
Metadata
- Authors
- Apicco, D. J., Ash, P. E. A., Maziuk, B., LeBlang, C., Medalla, M., Al Abdullatif, A., Ferragud, A., Botelho, E., Ballance, H. I., Dhawan, U., Boudeau, S., Cruz, A. L., Kashy, D., Wong, A., Goldberg, L. R., Yazdani, N., Zhang, C., Ung, C. Y., Tripodis, Y., Kanaan, N. M., Ikezu, T., Cottone, P., Leszyk, J., Li, H., Luebke, J., Bryant, C. D., & Wolozin, B.
- Affiliations
- Boston University (US)
- Mayo Clinic (US)
- Michigan State University (US)
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- Wolozin, Benjamin
- ORCID
- Apicco, Daniel J.
- Ash, Peter E. A.
- LeBlang, Chelsey
- Medalla, Maria
- Ferragud, Antonio
- Ballance, Heather I.
- Dhawan, Uma
- Cruz, Anna Lourdes
- Kashy, Daniel
- Goldberg, Lisa R.
- Zhang, Cheng
- Ung, Choong Y.
- Tripodis, Yorghos
- Kanaan, Nicholas M.
- Ikezu, Tsuneya
- Cottone, Pietro
- Li, Hu
- Luebke, Jennifer
- Bryant, Camron D.
- Wolozin, Benjamin
- Venue
- Nature Neuroscience
- Published
- 2017-11-20
- Volume
- 21
- Issue
- 1
- Pages
- 72-80
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- PMC
- PMC5745051
- OpenAlex
- W2768176302
- Cited by
- 281
- References
- 47
- Citations by year
- 2026: 28 · 2025: 35 · 2024: 26 · 2023: 24 · 2022: 42 · 2021: 32 · 2020: 33 · 2019: 34 · 2018: 25 · 2017: 1
- FWCI
- 18.82
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Glenn Foundation for Medical Research
- National Institutes of Health (1s10od023663-01)
- National Institute on Aging (RF1AG056318, R01AG050471, RF1AG054199, P30AG013846, R01AG054199)
- National Institute of General Medical Sciences (T32GM008541)
- National Institute of Neurological Disorders and Stroke (R01NS089544)
- National Institute of Environmental Health Sciences (R01ES020395)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- TIA-1, RNA-binding proteins, tau protein, tauopathy, neurodegeneration, stress granules, tau oligomers, neurofibrillary tangles, tau aggregation, lifespan, behavioral deficits
- MeSH terms
- Animals, Animals, Newborn, Cognition Disorders, Cytoplasm, Disease Models, Animal, Endoribonucleases, Female, Gene Expression Regulation, Locomotion, Male, Mice, Inbred C57BL, Mice, Transgenic, Mutation, Neurons, Synapses, Trans-Activators, RNA-Binding Proteins, Neurofibrillary Tangles, tau Proteins, Maze Learning, Tauopathies, Mice
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
