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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.
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“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
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“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
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“The RBP TIA1 was also shown to interact with tau to promote tau misfolding, leading to protein aggregation and formation of stress granules both in vitro (Vanderweyde et al., 2016) and in vivo (Apicco et al., 2018).”
BackgroundTau: Enabler of diverse brain disorders and target of rapidly evolving therapeutic strategies
Chang, C.-W., Shao, E., & Mucke, L. (2021) · Science · doi:10.1126/science.abb8255 · Cited by 263
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BackgroundLysine/RNA-interactions drive and regulate biomolecular condensation
Ukmar, T., Hutten, S., Grieshop, M. P., Rezaei‐Ghaleh, N., Cima‐Omori, M., Biernat, J., Mandelkow�, E., Söding, J., Dormann, D., & Zweckstetter, M. (2019) · Nature Communications · doi:10.1038/s41467-019-10792-y · Cited by 257
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Selective Neuronal Vulnerability in Alzheimer’s Disease: A Network-Based Analysis
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Self-citationThe RNA-Binding Protein PUM2 Impairs Mitochondrial Dynamics and Mitophagy During Aging
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BackgroundSelf-citationTIA1 potentiates tau phase separation and promotes generation of toxic oligomeric tau
Ash, P. E. A., Lei, S., Shattuck, J., Boudeau, S., Carlomagno, Y., Medalla, M., Mashimo, B. L., Socorro, G., Al-Mohanna, L. F. A., Jiang, L., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2014188118 · Cited by 159
“Interaction of tau with TIA1, a stress granule (SG) nucleating RBP (27), is necessary for tau-dependent neurodegeneration in PS19 transgenic mice (8).”
InfluentialSelf-citationStress granule mediated protein aggregation and underlying gene defects in the FTD-ALS spectrum
Baradaran‐Heravi, Y., Broeckhoven, C. V., & van der Zee, J. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104639 · Cited by 165
“In turn, phospho-tau regulates the interaction of TIA1 with other RBPS (Apicco et al., 2018; Vanderweyde et al., 2016; Vanderweyde et al., 2012).”
RNA binding proteins co-localize with small tau inclusions in tauopathy
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“The association of phosphorylated tau with the stress granule protein TIA1 raises the possibility that other RBPs and ribosomal proteins might also interact with tau [1, 25, 26, 37].”
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BackgroundDysregulation of autophagy and stress granule-related proteins in stress-driven Tau pathology
Silva, J. M., Rodrigues, S., Sampaio‐Marques, B., Gomes, P., Neves‐Carvalho, A., Dioli, C., Soares‐Cunha, C., Mazuik, B. F., Takashima, A., Ludovico, P., et al. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0217-1 · Cited by 123
Self-citationTau drives translational selectivity by interacting with ribosomal proteins
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BackgroundZinc promotes liquid–liquid phase separation of tau protein
Singh, V. P., Xu, L., Boyko, S., Surewicz, K. A., & Surewicz, W. K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ac120.013166 · Cited by 122
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Tau Isoforms: Gaining Insight into MAPT Alternative Splicing
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Tau interactome and RNA binding proteins in neurodegenerative diseases
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“Reduction of TIA1 inhibits the spread and prevents toxicity of seeded tau aggregates, but interestingly, increased neurofibrillary tangle burden and neuroinflammation [8, 56, 65].”
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Self-citationTIA1 regulates the generation and response to toxic tau oligomers
Jiang, L., Ash, P. E. A., Maziuk, B. F., Ballance, H. I., Boudeau, S., Abdullatif, A. A., Orlando, M., Petrucelli, L., Ikezu, T., & Wolozin, B. L. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1937-5 · Cited by 100
Self-citationChronic Sleep Disruption Advances the Temporal Progression of Tauopathy in P301S Mutant Mice
Zhu, Y., Zhan, G., Fenik, P., Brandes, M., Bell, P., François, N., Shulman, K., & Veasey, S. C. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.0275-18.2018 · Cited by 110
“In the LC in P301S mice, CSS neuron loss does not appear to require NFT as the LC in CSS-exposed mice exhibited rare tangles.”
BackgroundInfluentialAbskharon, R. N. N., Sawaya, M. R., Boyer, D. R., Cao, Q., Nguyen, B. A., Cascio, D., & Eisenberg, D. S. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2119952119 · Cited by 97
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MethodQuality Control of Membraneless Organelles
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Dysregulation of RNA Splicing in Tauopathies
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Self-citationFyn Kinase Controls Tau Aggregation In Vivo
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“Currently, the physiological role of BAD domains in U1-70K and other RNA-binding proteins is unclear, and understanding their role in protein–protein interactions may shed light on the mech-anismsunderlyingRBPaggregationandtheirassociationwithTau in AD (7, 28).”
BackgroundFriend or foe: The role of stress granule in neurodegenerative disease
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Zika Virus Subverts Stress Granules To Promote and Restrict Viral Gene Expression
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“A549 cells (39), the impact of TIA-1 and TIAR might be better elucidated in neuronal cells where 665 a link between TIA-1, the microtubule protein Tau and the neurodegenerative tauopathies has 666 been described (61, 62).”
BackgroundOrdered Assembly of Tau Protein and Neurodegeneration
Goedert, M., & Spillantini, M. G. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_1 · Cited by 74
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“As previous studies have shown that pathological Tau induces neuroinflammation leading to synapse loss in PS19 mice [1, 11, 35], we also examined the effect of AZD0530 treatment on neuroinflammation in PS19 mice using anti-Iba1 and GFAP antibodies, general makers for microgliosis and astrocytosis, respectively.”
MethodResultAltered ribosomal function and protein synthesis caused by tau
Evans, H. T., Taylor, D. W., Kneynsberg, A., Bodea, L., & Götz, J. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01208-4 · Cited by 73
“D‑lysine; Proj-dom hTau: N‑terminal projection domain human tau construct; RIPA: Radioimmunoprecipitation assay; RP: Ribosomal protein; RPL: Ribosomal protein large subunit; RPS: Ribosomal protein small subunit; SFPQ: Splicing factor proline and glutamine rich; qRT‑PCR: Semi‑quantitative real‑time polymerase chain rea…”
BackgroundInfluentialIntracellular energy controls dynamics of stress-induced ribonucleoprotein granules
Wang, T., Tian, X., Kim, H. B., Jang, Y., Huang, Z., Na, C. H., & Wang, J. (2022) · Nature Communications · doi:10.1038/s41467-022-33079-1 · Cited by 71
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“The importance of the TIA1–Tau interaction for tauopathies was further explored using the PS19 transgenic Tau mice [445].”
BackgroundFRET-based Tau seeding assay does not represent prion-like templated assembly of Tau filaments
Kaniyappan, S., Tepper, K., Biernat, J., Chandupatla, R., Hübschmann, S., Irsen, S. H., Bicher, S., Klatt, C., Mandelkow, E., & Mandelkow�, E. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00389-1 · Cited by 65
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“Indeed, TIA1 knockdown prevents pathological tau aggregation (Apicco et al., 2018; Vanderweyde et al., 2016).”
BackgroundIdentification of circRNAs linked to Alzheimer's disease and related dementias
Puri, S., Hu, J., Sun, Z., Lin, M., Stein, T. D., Farrer, L. A., Wolozin, B. L., & Zhang, X. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.12960 · Cited by 54
Self-citationBond-selective intensity diffraction tomography
Zhao, J., Matlock, A. C., Zhu, H., Song, Z., Zhu, J., Wang, B., Chen, F., Zhan, Y., Chen, Z., Xu, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-35329-8 · Cited by 50
USP10 is a critical factor for Tau-positive stress granule formation in neuronal cells
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Gao, Y., Zhong, T., Wang, L., Zhang, N., Zeng, Y., Hu, J.-Y., Dang, H.-B., Chen, J., & Liang, Y. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.04.034 · Cited by 48
Zhou, Y., Zhao, Q., Zhang, Y., Di, L., Feng, X., Xu, W., Gao, W.-P., Guo, Y., He, Y., Kou, J., et al. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.155298 · Cited by 48
Montalbano, M., McAllen, S., Sengupta, U., Puangmalai, N., Bhatt, N. N., Ellsworth, A., & Kayed, R. (2019) · Aging Cell · doi:10.1111/acel.13035 · Cited by 46
Cannabinoid receptor CB2 ablation protects against TAU induced neurodegeneration
Galán-Ganga, M., Rodríguez‐Cueto, C., Merchán‐Rubira, J., Hernández, F., Ávila, J., Posada-Ayala, M., Lanciego, J. L., Luengo, E., López, M. G., Rábano, A., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01196-5 · Cited by 46
“Immunofluorescence on mouse tissues Mouse tissue was sectioned at 30 μm on a cryostat and stained as free floating sections using Netwell baskets [3].”
MethodRNA induces unique tau strains and stabilizes Alzheimer’s disease seeds
Zwierzchowski-Zarate, A. N., Mendoza‐Oliva, A., Kashmer, O. M., Collazo-Lopez, J. E., White, C. L., & Diamond, M. I. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102132 · Cited by 48
Pathophysiology of stress granules: An emerging link to diseases (Review)
Wang, J., Gan, Y., Cao, J. P., Dong, X.-F., & Ouyang, W. (2022) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2022.5099 · Cited by 47
“In addition, TIA‑1 or TIAR may also promote the formation of SGs alone (23,25).”
BackgroundInfluentialFormation of Toxic Oligomeric Assemblies of RNA-binding Protein: Musashi in Alzheimer’s disease
Sengupta, U., Montalbano, M., McAllen, S., Minuesa, G., Kharas, M. G., & Kayed, R. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0615-0 · Cited by 43
Koren, S. A., Galvis-Escobar, S., & Abisambra, J. F. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104939 · Cited by 49
Tau–RNA complexes inhibit microtubule polymerization and drive disease-relevant conformation change
McMillan, P. J., Benbow, S. J., Uhrich, R. L., Saxton, A. D., Baum, M., Strovas, T. J., Wheeler, J. M., Baker, J. D., Liachko, N. F., Keene, C. D., et al. (2023) · Brain · doi:10.1093/brain/awad032 · Cited by 43
Stress and the Etiopathogenesis of Alzheimer’s Disease and Depression
Sotiropoulos, I., Silva, J. M., Gomes, P., Sousa, N., & Almeida, O. F. X. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_20 · Cited by 42
Exosomal and vesicle‐free tau seeds—propagation and convergence in endolysosomal permeabilization
Polanco, J. C., & Götz, J. (2021) · FEBS Journal · doi:10.1111/febs.16055 · Cited by 43
The Pathophysiology of Tau and Stress Granules in Disease
Cruz, A. L., Verma, M., & Wolozin, B. L. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_26 · Cited by 42
“Molecular pathology studies show colocalization of pathological tau (hyperphosphorylated or misfolded) with multiple RBPs [2, 3, 55, 82, 87, 88].”
BackgroundInfluentialSelf-citationWebber, C. J., Lei, S. (., & Wolozin, B. L. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.04.021 · Cited by 41
Self-citationAnnadurai, N., Sanctis, J. B. D., Hajdúch, M., & Das, V. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113756 · Cited by 41
Emerging Roles of RNA-Binding Proteins in Neurodevelopment
Parra, A. S., & Johnston, C. A. (2022) · Journal of Developmental Biology · doi:10.3390/jdb10020023 · Cited by 40
RNA: The Unsuspected Conductor in the Orchestra of Macromolecular Crowding
Zacco, E., Broglia, L., Kurihara, M., Monti, M. M., Gustincich, S., Pastore, A., Plath, K., Nagakawa, S., Cerase, A., de Groot, N. S., et al. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00575 · Cited by 41
Single cell transcriptomic profiling of a neuron-astrocyte assembloid tauopathy model
Rickner, H., Jiang, L., Hong, R., O’Neill, N. K., Mojica, C. A., Snyder, B. J., Zhang, L., Shaw, D., Medalla, M., Wolozin, B. L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34005-1 · Cited by 43
“Human oligomeric tau (oTau) was isolated from 9-month-old PS19 P301S tau mice by centrifugation using a well-validated method 55,66,67 .”
Self-citationCytosolic condensates rich in polyserine define subcellular sites of tau aggregation
Lester, E., Alstyne, M. V., McCann, K. L., Reddy, S., Cheng, L. Y., Kuo, J., Pratt, J., & Parker, R. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2217759120 · Cited by 37
“PNN_FL (1-718) Frag_1 (571-637) Halo Ser* Halo Halo D”
InfluentialDisrupting pathologic phase transitions in neurodegeneration
Hurtle, B. T., Xie, L., & Donnelly, C. J. (2023) · Journal of Clinical Investigation · doi:10.1172/jci168549 · Cited by 40
Reduction of the RNA Binding Protein TIA1 Exacerbates Neuroinflammation in Tauopathy
LeBlang, C. J., Medalla, M., Nicoletti, N. W., Hays, E. C., Zhao, J., Shattuck, J. E., Cruz, A. L., Wolozin, B. L., & Luebke, J. I. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00285 · Cited by 38
“While we have previously demonstrated that TIA1 plays a key role in regulating phospho-tau aggregation dynamics (Vanderweyde et al., 2016; Apicco et al., 2017; Maziuk et al., 2018; Jiang et al., 2019), our observation of increased synapse loss with TIA1 reduction in advanced disease indicates that reducing TIA1 system…”
InfluentialSelf-citationBiomolecular condensation of the microtubule-associated protein tau
Ukmar, T., Wegmann, S., & Zweckstetter, M. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.06.007 · Cited by 41
Mechanisms and regulation underlying membraneless organelle plasticity control
Ismail, H., Liu, X., Yang, F., Li, J., Zahid, A., Dou, Z., Liu, X., & Yao, X. (2021) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjab028 · Cited by 40
“TIA-1 knockdown prevented Tau pathology in neuronal culture and rodent models (Apicco et al., 2018).”
BackgroundPapanikolopoulou, K., Roussou, I. G., Gouzi, J. Y., Samiotaki, M. K., Panayotou, G., Turin, L., & Skoulakis, E. M. C. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.0391-19.2019 · Cited by 37
“Congruently, vertebrate tau is a negative regulator of translation (Apicco et al., 2018) and was also recently reported to act as a negative regulator of ribosomal protein levels in mouse brains (Koren et al.”
BackgroundAge‐related neurodegenerative diseases
Duggan, M. R., Torkzaban, B., Ahooyi, T. M., Khalili, K., & Gordon, J. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29248 · Cited by 40
Zhou, Y., Luo, D., Shi, J.-Z., Yang, X., Xu, W., Gao, W.-P., Guo, Y., Zhao, Q., Xie, X., He, Y., et al. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.116455 · Cited by 37
Amalric, M., Pattij, T., Sotiropoulos, I., Silva, J. M., Sousa, N., Ztaou, S., Chiamulera, C., Wahlberg, L. U., Emerich, D. F., & Paolone, G. (2021) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2021.661973 · Cited by 35
Stress granules: emerging players in neurodegenerative diseases
Yuan, L., Mao, L.-H., Huang, Y.-Y., Outeiro, T. F., Li, W., Vieira, T. C. R. G., & Li, J. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00482-9 · Cited by 48
“Interestingly, a decrease in SG assembly is associated with alleviation of tau pathology, suggesting that reducing SG assembly could inhibit AD progression [128].”
Saturated fatty acids entrap PDX1 in stress granules and impede islet beta cell function
Zhang, M., Yang, C., Zhu, M., Li, Q., Luo, Y., Cheng, H., Geng, R., Xu, X., Cheng, Q., & Liu, Y. (2021) · Diabetologia · doi:10.1007/s00125-021-05389-4 · Cited by 34
Liquid-liquid phase separation in Alzheimer’s disease
Fu, Q., Zhang, B., Chen, X., & Chu, L. (2024) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02407-3 · Cited by 33
“This interaction has also been reported in the PS19 AD mouse model [86].”
Neuronal biomolecular condensates and their implications in neurodegenerative diseases
Nam, J., & Gwon, Y. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1145420 · Cited by 34
Increased G3BP2-Tau interaction in tauopathies is a natural defense against Tau aggregation
Wang, C., Terrigno, M., Li, J., Distler, T., Pandya, N. J., Ebeling, M., Tyanova, S., Hoozemans, J. J. M., Dijkstra, A. A., Fuchs, L., et al. (2023) · Neuron · doi:10.1016/j.neuron.2023.05.033 · Cited by 35
“10 Neuron 111, 1–15, September 6, 2023 eration.(8) Until now, research has focused onmodels in which Tau is overexpressed or on transgenic tauopathy rodent models, whereas our work investigates the roles of RBPs in modulating Tau under physiological and pathological conditions.”
BackgroundRNA G-quadruplexes and calcium ions synergistically induce Tau phase transition in vitro
Yabuki, Y., Matsuo, K., Komiya, G., Kudo, K., Hori, K., Ikenoshita, S., Kawata, Y., Mizobata, T., & Shioda, N. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107971 · Cited by 33
“T-cell intracytoplasmic antigen 1 knockdown attenuates Tau aggregation, neuronal death, and memory de fi cits in mouse models expressing human mutated Tau (P301L or P301S) (50, 51), suggesting that the recruitment of Tau into SGs may trigger aggregation.”
Verde, E. M., Secco, V., Ghezzi, A., Mandrioli, J., & Carra, S. (2025) · Cells · doi:10.3390/cells14100680 · Cited by 35
“Tofersen, as an example, is an FDA-approved treatment for ALS cases associated with SOD1 mutations; this ASO was indeed designed to target SOD1 mRNA, limiting the expression of the mutant protein without affecting the host DNA [353].”
Takahashi, H., Bhagwagar, S. Z., Nies, S. H., Ye, H., Han, X., Chiasseu, M., Wang, G., Mackenzie, I. R., & Strittmatter, S. M. (2024) · Nature Communications · doi:10.1038/s41467-024-45692-3 · Cited by 32
“Strikingly, we detected high GlcCer positivity in NFTs of the anterior hippocampus in all of fi ve AD brains and four AH2 brains we tested (Fig.”
InfluentialTranslational control in brain pathologies: biological significance and therapeutic opportunities
Delaidelli, A., Jan, A., Herms, J. W., & Sorensen, P. H. B. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01971-8 · Cited by 31
Selective neuronal vulnerability in Alzheimer’s disease: a network-based analysisPreprint
Roussarie, J.-P., Yao, V., Plautz, Z., Kasturia, S. E., Albornoz, C. A., Schmidt, E. F., Brichta, L., Barnea-Cramer, A. O., Heintz, N., Hof, P. R., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/499897 · Cited by 31
Liquid − liquid phase separation of tau: Driving forces, regulation, and biological implications
Li, P., Chen, J., Wang, X., Su, Z., Gao, M., & Huang, Y. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106167 · Cited by 30
Connecting the dots: Neuronal senescence, stress granules, and neurodegeneration
Ma, Y., & Farny, N. G. (2023) · Gene · doi:10.1016/j.gene.2023.147437 · Cited by 30
New roles for the de-ubiquitylating enzyme OTUD4 in an RNA-protein network and RNA granules
Das, R., Schwintzer, L., Vinopal, S., Roca, E. A., Sylvester, M., Oprişoreanu, A., Schoch, S., Bradke, F., & Broemer, M. (2019) · Journal of Cell Science · doi:10.1242/jcs.229252 · Cited by 32
“Impressive recent work has shown that reducing levels of TIA1 or ataxin-2 delays disease progression in models for Alzheimer’s disease (AD) or ALS, respectively (Apicco et al., 2018; Becker et al., 2017), further supporting the importance of RBPs in neurodegenerative diseases.”
BackgroundJiang, L., Zhao, J., Cheng, J., & Wolozin, B. L. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.579434 · Cited by 31
“Small oTau Inclusions Co-Localize to Stress Granules in the Recipient Neurons Our previous studies found that RNA binding protein TIA1 appeared to stabilize oligomeric tau and reduce conversion into larger fibrillar tau tangles (20).”
BackgroundResultInfluentialSelf-citationEarly alterations of neurovascular unit in the retina in mouse models of tauopathy
Xia, F., Ha, Y., Shi, S., Li, Y., Li, S., Luisi, J. D., Kayed, R., Motamedi, M., Liu, H., & Zhang, W. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01149-y · Cited by 30
“Therefore, these mouse strains have been widely used as models to study mechanisms and treatments of tauopathy including AD [4, 10, 37, 60, 65].”
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
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