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.”
Influential
Cited by
Sorted by citations
Items 101–200 of 281
Genetic Perturbation of TIA1 Reveals a Physiological Role in Fear Memory
Rayman, J. B., Hijazi, J., Li, X., Kedersha, N., Anderson, P., & Kandel, E. R. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.048 · Cited by 29
Frydrýšková, K., Mašek, T., & Pospíšek, M. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1596 · Cited by 29
“In line with this, reducing the number of SGs was proposed as a new way to fight Alzheimer disease (Apicco et al., 2018; Vanderweyde et al., 2012).”
BackgroundCoiled-Coil Motifs of RNA-Binding Proteins: Dynamicity in RNA Regulation
Ford, L. K., & Fioriti, L. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.607947 · Cited by 29
Tau liquid–liquid phase separation: At the crossroads of tau physiology and tauopathy
Islam, M., Shen, F., Regmi, D., Petersen, K., Karim, M. R. U., & Du, D. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.30853 · Cited by 28
“Interestingly, the binding of TIA1 to tau was reported to induce toxic tau oligomers in PS19 mice (expressing P301S tau) (Apicco et al., 2017) and aggregation in rTg4510 mice (Vanderweyde et al., 2016).”
BackgroundCellular Biology of Tau Diversity and Pathogenic Conformers
Kang, S., Eskandari‐Sedighi, G., Hromádková, L., Safar, J., & Westaway, D. A. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590199 · Cited by 29
“, oxidative and mild heat stresses) (45, 46) and participates in RNA metabolism through direct association with RNA-binding proteins (47, 48).”
BackgroundStress granules and organelles: coordinating cellular responses in health and disease
Liu, Y., Li, Y., & Zhang, P. (2024) · Protein & Cell · doi:10.1093/procel/pwae057 · Cited by 26
Liquid-Liquid Phase Separation of Tau Protein in Neurobiology and Pathology
Wegmann, S. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_25 · Cited by 28
Molecular interaction of stress granules with Tau and autophagy in Alzheimer's disease
Yu, Q.-Y., Ye, L., & Li, H. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105342 · Cited by 27
Self-citationNuclear Tau, p53 and Pin1 Regulate PARN-Mediated Deadenylation and Gene Expression
Baquero, J., Varriano, S., Ordonez, M., Kuczaj, P., Murphy, M. R., Aruggoda, G., Lundine, D., Morozova, V., Makki, A. E.-H., Alonso, A. D. C., et al. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00242 · Cited by 26
“These cytoplasmic functional interactions are affected in AD (Meier et al., 2016; Vanderweyde et al., 2016; Apicco et al., 2018).”
BackgroundInfluentialBiomolecular condensates and disease pathogenesis
Ruan, K., Bai, G., Fang, Y., Li, D., Li, T., Liu, X., Lu, B., Lü, Q., Songyang, Z., Sun, S., et al. (2024) · Science China Life Sciences · doi:10.1007/s11427-024-2661-3 · Cited by 28
“…hyperphosphorylated Tau has been observed to gather in neuronal inclusions alongside various RNA-binding proteins, including TIA1 (indicative of stress granules) and HNRNPA2B1 (linked with N6-methylade-nosine [m 6 A] RNA) (Apicco et al., 2018; Jiang et al., 2021; Vanderweyde et al., 2016).”
Choudhary, B. C., Mandelkow�, E., Mandelkow, E.-M., & Pir, G. J. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.06.005 · Cited by 26
Guo, Q., Dammer, E. B., Zhou, M., Kundinger, S. R., Gearing, M., Lah, J. J., Levey, A. I., Shulman, J. M., & Seyfried, N. T. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.623659 · Cited by 27
The Multifunctional Faces of T-Cell Intracellular Antigen 1 in Health and Disease
Fernández-Gómez, A., & Izquierdo, J. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031400 · Cited by 25
“Although TIA1 depletion increases tau fibrillation, it generally leads to decreased neurodegeneration, increased life expectancy and improved memory in animals [107].”
BackgroundZhao, J., Jiang, L., Matlock, A. C., Xu, Y., Zhu, J., Zhu, H., Tian, L., Wolozin, B. L., & Cheng, J. (2023) · Light Science & Applications · doi:10.1038/s41377-023-01191-6 · Cited by 26
“Then it was homogenized with TBS buffer (50 mM Tris, pH 8.0, 274 mM NaCl, 5 mM KCl) supplemented with protease and phosphatase inhibitor cocktails (Roche, cat#05892791001 and cat#04906837001) 34 .”
BackgroundMethodInfluentialSelf-citationTau/DDX6 interaction increases microRNA activity
Chauderlier, A., Gilles, M., Špolcová, A., Caillierez, R., Chwastyniak, M., Kress, M., Drobecq, H., Bonnefoy, E., Pinet, F., Barbieri-Weill, D., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2018.06.006 · Cited by 26
Poly(ADP-ribose) promotes toxicity of C9ORF72 arginine-rich dipeptide repeat proteins
Gao, J., Mewborne, Q. T., Girdhar, A., Sheth, U., Coyne, A. N., Punathil, R., Kang, B. G., Dasovich, M., Veire, A. M., Hernandez, M. D., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abq3215 · Cited by 26
“As SGs were also implicated in neurodegeneration observed in mouse models of other diseases, including tauopathies, a prion disease, and a vanishing white matter disease (74, 77, 78), PAR likely also contributes to their pathogenesis.”
BackgroundAntisense oligonucleotide therapies for Amyotrophic Lateral Sclerosis: Existing and emerging targets
Klim, J. R., Vance, C. A., & Scotter, E. L. (2019) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2019.03.009 · Cited by 27
Modulation of biomolecular phase behavior by metal ions
Sołtys, K., Tarczewska, A., & Bystranowska, D. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119567 · Cited by 23
Liquid–liquid phase separation in diseases
Zhang, X., Lin, Y., Zhang, W., Zhang, Y., Wu, Q. J., Li, C., Wu, M., & Huang, Y. (2024) · MedComm · doi:10.1002/mco2.640 · Cited by 24
“511 In addition, targeting the neural pathways involved in SGs, including the mTOR pathway and the eIF2 α pathway, is also considered as a potential therapeutic means.”
BackgroundExperimental Models of Tauopathy – From Mechanisms to Therapies
Götz, J. J., & Götz, J. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_28 · Cited by 24
Protein Interaction Network Biology in Neuroscience
Basu, A., Ash, P. E. A., Wolozin, B. L., & Emili, A. (2020) · PROTEOMICS · doi:10.1002/pmic.201900311 · Cited by 23
Self-citationDecoding phase separation of prion-like domains through data-driven scaling lawsPreprint
Maristany, M. J., Gonzalez, A. A., Espinosa, J. R., Huertas, J., Collepardo‐Guevara, R., & Joseph, J. A. (2024) · eLife · doi:10.7554/elife.99068 · Cited by 21
Platelet miRNA Biosignature Discriminates between Dementia with Lewy Bodies and Alzheimer’s Disease
Gámez‐Valero, A., Campdelacreu, J., Vilas, D., Ispierto, L., Gascón‐Bayarri, J., Reñé, R., Álvarez, R., Armengol, M. P., Borràs, F. E., & Beyer, K. (2021) · Biomedicines · doi:10.3390/biomedicines9091272 · Cited by 20
“TIA1 is involved in RNA splicing and post-transcriptional gene regulation, has been found in stress granules [45], and has been related to tau oligomerization and neurofibrillary tangle deposition in AD [43].”
BackgroundRispe, C., Hervet, C., de la Cotte, N., Daveu, R., Labadie, K., Noël, B., Aury, J., Thany, S. H., Taillebois, E., Cartereau, A., et al. (2022) · BMC Genomics · doi:10.1186/s12864-022-08669-4 · Cited by 20
“For example, we found that several of the genes with the highest log-fold variation in expression in the synganglion have vertebrates homologues which have been extensively studied for their association with Alzheimer’s Disease: this is the case for the APPlike peptide (APPL) and of tau protein [28], as well as a homo…”
BackgroundSuppressing Tau Aggregation and Toxicity by an Anti-Aggregant Tau Fragment
Pir, G. J., Choudhary, B. C., Kaniyappan, S., Chandupatla, R., Mandelkow�, E., Mandelkow, E., & Wang, Y. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1326-z · Cited by 20
Targeting tau in Alzheimer’s and beyond: Insights into pathology and therapeutic strategies
Singh, S., Khan, S., Shahid, M., Sardar, M., Hassan, M. I., & Islam, A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102639 · Cited by 19
Neuroprotective effects of hawthorn leaf flavonoids in Aβ25–35‐induced Alzheimer's disease model
Xu, Y. X., Deng, T., Xie, L., Qin, T., & Sun, T. (2022) · Phytotherapy Research · doi:10.1002/ptr.7690 · Cited by 20
“…by the accumulation of β-amyloid (Aβ), neurofibrillary tangles caused by the aberrant hyperphosphorylation and aggregation of tau, as well as the loss of neuronal cells and oxida- tive stress in the brain are the main pathological hallmarks of AD (Apicco et al., 2018; Querfurth & LaFerla, 2010).”
BackgroundDecoding phase separation of prion-like domains through data-driven scaling laws
Maristany, M. J., Gonzalez, A. A., Espinosa, J. R., Huertas, J., Collepardo‐Guevara, R., & Joseph, J. A. (2025) · eLife · doi:10.7554/elife.99068.3 · Cited by 19
YAP maintains the dynamics of TDP-43 condensates and antagonizes TDP-43 pathological aggregates
Zhang, J., Hu, J., Liu, R., Zhou, T., Luo, X., Liang, P., Xie, Z., Zhao, Q., Chen, Y., Du, D., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01685-y · Cited by 24
“We prepared [ 15 N]-labelled TDP-43 NTD and titrated it with YAP WT or YAP S94A.”
Tau13 Antibody Preferentially Immunoprecipitates High Molecular Weight Tau Proteins
Umstead, A., & Vega, I. E. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181187 · Cited by 18
“In contrast, previous studies showed that deletion of the RNA-binding proteins (RBPs) T-cell intracellular antigen 1 (TIA1) gene increased survival of mice expressing human P301S tau mutant, decreasing the accumulation of tau oligomers, but increased neurofibrillary tangles [10].”
Dementia Therapy Targeting Tau
Buée, L. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_30 · Cited by 18
Wan, M., Sun, S., Di, X., Zhao, M., Lu, F., Zhang, Z., & Li, Y. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.117029 · Cited by 18
Takahashi, F., Zhang, C., Hohjoh, H., Raveney, B. J. E., Yamamura, T., Hayashi, N., & Oki, S. (2022) · iScience · doi:10.1016/j.isci.2022.104278 · Cited by 22
“Some L1s are still retrotranspositioncompetent and L1 mobilization is one of the major causes of neurodevelopmental and neurodegenerative disorders (Apicco et al., 2018; Frost et al., 2014; Prudencio et al., 2017).”
BackgroundSelf-citationSu, W.-C., & Harrison, P. M. (2020) · PeerJ · doi:10.7717/peerj.9023 · Cited by 17
“Reduction of Tia1 levels protects against tau-mediated neurodegeneration in the brain, rescues behavioural deficits and improves survival (Apicco et al., 2018).”
BackgroundThe Tau of Nuclear-Cytoplasmic Transport
Lester, E., & Parker, R. (2018) · Neuron · doi:10.1016/j.neuron.2018.08.026 · Cited by 17
Loss of aly/ALYREF suppresses toxicity in both tau and TDP-43 models of neurodegeneration
Kow, R. L., Black, A. H., Saxton, A. D., Liachko, N. F., & Kraemer, B. C. (2022) · GeroScience · doi:10.1007/s11357-022-00526-2 · Cited by 18
Tau, RNA, and RNA-Binding Proteins: Complex Interactions in Health and Neurodegenerative Diseases
Lester, E., & Parker, R. (2023) · The Neuroscientist · doi:10.1177/10738584231154551 · Cited by 16
Reversible protein assemblies in the proteostasis network in health and disease
Kohler, V., & Andréasson, C. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1155521 · Cited by 17
“Consistently, Ubc9, SOD1 and other misfolding-prone proteins were shown to accumulate in stress granules, changing their properties and dynamics (Ganassi et al., 2016; Lee et al., 2016; Boeynaems et al., 2017; Mateju et al., 2017; Apicco et al., 2018).”
BackgroundCarrascoso, I., Sánchez-Jiménez, C., Silion, E., Alcalde, J., & Izquierdo, J. M. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00299-18 · Cited by 16
Jiang, L., Roberts, R., Wong, M., Zhang, L., Webber, C. J., Libera, J., Wang, Z., Kilci, A., Jenkins, M., Ortiz, A. R., et al. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1372297 · Cited by 15
Self-citationPhenotypic Suppression of ALS/FTD-Associated Neurodegeneration Highlights Mechanisms of Dysfunction
Bartoletti, M., Bosco, D. A., Cruz, S. D., Lagier‐Tourenne, C., Liachko, N. F., Markmiller, S., Webster, K. M., & Wharton, K. A. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1159-19.2019 · Cited by 15
“Importantly, therapeutic reduction of the SG-associated proteins Ataxin-2 and TIA1 components was recently shown to provide neuroprotective effects in animal models of ALS (Becker et al., 2017; Apicco et al., 2018).”
BackgroundWang, H., Ma, Z., Shen, H., Wu, Z., Liu, L., Ren, B., Wong, P., Sethi, G., & Tang, F.-R. (2021) · Cells · doi:10.3390/cells10092476 · Cited by 16
“It aggregates to form SG following cellular damage, which is strongly linked to the pathophysiology of neurodegeneration [37,38].”
BackgroundInfluentialAPEX Proximity Labeling of Stress Granule Proteins
Elmsaouri, S., Markmiller, S., & Yeo, G. W.-M. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1975-9_23 · Cited by 16
Ma, D., Luo, Y., Huang, R., Zhao, Z., Zhang, L., Li, Y., Wang, Q., Li, L., & Zhang, L. (2020) · Current Medical Science · doi:10.1007/s11596-020-2284-z · Cited by 15
Tau mRNA Metabolism in Neurodegenerative Diseases: A Tangle Journey
da Costa, P. J., Hamdane, M., Buée, L., & Martin, F. (2022) · Biomedicines · doi:10.3390/biomedicines10020241 · Cited by 16
“More recently, it was shown that reducing TIA1 in vivo rescued the tau-associated phenotype in P301S tau mice [162,179].”
BackgroundInfluentialLiquid-liquid phase separation of tau and α-synuclein: A new pathway of overlapping neuropathologies
Rodríguez, L. C., Foressi, N. N., & Celej, M. S. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.151053 · Cited by 15
Emerging Connections Between Tau and Nucleic Acids
Galas, M., Bonnefoy, E., Buée, L., & Lefebvre, B. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_12 · Cited by 17
Phase separation of the microtubule-associated protein tau
Chakraborty, P., & Zweckstetter, M. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220066 · Cited by 15
“Phosphorylation of tau also plays an important role in this pathway by promoting the formation of larger stress-granules [67].”
BackgroundHeat resilience in embryonic zebrafish revealed using an in vivo stress granule reporter
Wang, R., Zhang, H., Du, J., & Xu, J. (2019) · Journal of Cell Science · doi:10.1242/jcs.234807 · Cited by 13
“Mounting evidence indicates that stress granule dysregulation could contribute to the development of some neurodegenerative diseases (Apicco et al., 2018; Ash et al., 2014; Li et al., 2013; Maziuk et al., 2017; Xu et al., 2019) and chemoresistance in cancer cells (Anderson et al.”
BackgroundAlves, R. L., Gonçalves, A., Voytyuk, I., & Harrison, D. C. (2025) · Experimental Neurology · doi:10.1016/j.expneurol.2025.115234 · Cited by 11
Hu, L., Mao, S., Li, L., Bai, G., Liu, B., & Mao, J. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105749 · Cited by 13
hnRNP A1 dysfunction in oligodendrocytes contributes to the pathogenesis of multiple sclerosis
Jahan-Abad, A. J., Salapa, H. E., Libner, C. D., Thibault, P., & Levin, M. (2022) · Glia · doi:10.1002/glia.24300 · Cited by 12
The enigma of ultraviolet radiation stress granules: Research challenges and new perspectives
Cabral, A. J., Costello, D. C., & Farny, N. G. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1066650 · Cited by 14
“pSGs have been most closely associated to date with ALS and Alzheimer’s Disease (Vanderweyde et al., 2012; Vanderweyde et al., 2016; Ash et al., 2014; Aulas and vande Velde, 2015; Apicco et al., 2018; Zhang et al., 2019; Marmor-Kollet et al., 2020; An et al., 2022).”
BackgroundPeng, Y., Liou, B., Inskeep, V., Blackwood, R., Mayhew, C. N., Grabowski, G. A., & Sun, Y. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz184 · Cited by 11
“ing lysosomes, axons and terminals, which become particularly argyrophilic (30).”
BackgroundLi, S., Lv, H., Zhang, R., Li, J., Chen, Z., Yang, N., & Dai, S. (2025) · Frontiers in Aging · doi:10.3389/fragi.2025.1575862 · Cited by 12
RNA-Binding Proteins: A Role in Neurotoxicity?
Ocharán-Mercado, A., Loaeza-Loaeza, J., Castro-Coronel, Y., Acosta-Saavedra, L. C., Hernández-Kelly, L. C., Hernández-Sotelo, D., & Ortega, A. (2023) · Neurotoxicity research · doi:10.1007/s12640-023-00669-w · Cited by 9
“Recent studies show that few nuclear RBPs are expressed under neuropathological conditions, and a higher fraction is present in SG (Apicco et al. 2018; Armstrong et al. 2012; Janssens et al. 2013).”
BackgroundCarrascoso, I., Alcalde, J., Tabas‐Madrid, D., Oliveros, J. C., & Izquierdo, J. M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0208526 · Cited by 10
The Effects of a Blood–Brain Barrier Penetrating Erythropoietin in a Mouse Model of Tauopathy
Yang, J., Ou, W., Jagadeesan, N., Simanauskaite, J., Sun, J., Castellanos, D. M., Cribbs, D. H., & Sumbria, R. K. (2023) · Pharmaceuticals · doi:10.3390/ph16040558 · Cited by 9
“PS19 mice exhibit behavioral abnormalities such as hyperactive locomotor activity and reduced anxiety caused by mutant tau overexpression [31,32].”
BackgroundEarly Chronic Stress Induced Changes within the Locus Coeruleus in Sporadic Alzheimer’s Disease
Minné, D., Marnewick, J. L., & Engel-Hills, P. C. (2023) · Current Alzheimer Research · doi:10.2174/1567205020666230811092956 · Cited by 10
Shen, Y., Zhang, T., Zhang, Y., Wang, Y., & Yao, J. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.718701 · Cited by 9
“In addition, recent studies reported that TIA1 could interact with tau protein to induce AD-related neurotoxicity (Apicco et al., 2018).”
BackgroundNelson, R. S., Dammer, E. B., Santiago, J. V., Seyfried, N. T., & Rangaraju, S. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.902146 · Cited by 10
Focusing on oligomeric tau as a therapeutic target in Alzheimer’s disease and other tauopathies
Rayman, J. B. (2023) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2023.2206561 · Cited by 11
“cellular pathology and memory deficits [113,116].”
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
“TIA1-con-taining stress granules are proposed to facilitate tau aggregation, and the reduction of TIA1 levels reduces tau pathology in a mouse model (Apicco et al. 2018).”
Puangmalai, N., Aday, A. E., Samples, M., Bhatt, N. N., Cascio, F. L., Marcatti, M., Park, S. J., Fung, L., Jerez, C., Penalva, L. O. F., et al. (2025) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2025.102742 · Cited by 8
“…has been observed for other RNA-binding proteins such as TDP-43 (Takeda, 2018; Davis et al., 2017; De Conti et al., 2017; Conlon and Manley, 2017; Apicco 2018; Deng et al., 2014; Ederle and Dormann 2017; Ratti and Buratti 2016), TIA-1 and Parkinson ’ s, Spinocerebellar ataxia, Huntington ’ s,…”
Anschuetz, A., Schwab, K., Harrington, C. R., Wischik, C. M., & Riedel, G. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251362212 · Cited by 7
Tian, S., Liu, Y., Hong, H., & Li, S. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05280-y · Cited by 8
“Additionally, research has shown that core protein components of SGs, such as the RNA-binding protein TIA1, interact with tau to induce its aggregation and drive neurotoxicity [78, 79].”
Bakheet, T. M., Al‐Ahmadi, W., Al-Mutairi, N., Doubi, M., Alhosaini, K. A., & Al-Zoghaibi, F. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031017 · Cited by 8
“TIA1 reduces the number and size of SGs, protects against neurodegeneration, and prolongs the survival of transgenic O301S tau mice and tau oligomer aggregation [33].”
Interactions and interplay of MLOs with classical membrane-bound organelles
Sasidharan, S., Nag, N., Tripathi, T., & Saudagar, P. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-823967-4.00024-5 · Cited by 9
Dissolution of ribonucleoprotein condensates by the embryonic stem cell protein L1TD1
Jin, S. W., Seong, Y., Yoon, D., Kwon, Y., & Song, H. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkad1244 · Cited by 9
“The impacts of RNP granules on neurological disorders are further supported by animal models with reduced expression of RBPs of SGs ( 66 ,67 ).”
BackgroundShapley, S. M., Shantaraman, A., Gadhavi, J. D., Kearney, M. A., Dammer, E. B., Duong, D. M., Bowen, C. A., Watson, C. M., Bagchi, P., Guo, Q., et al. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.101458 · Cited by 9
“…TauRD interacting proteins within disease-related protein modules were enriched in nuclear pathways consistent with prior studies highlighting the relevance of splicing factors and RBPs in AD pathogenesis (16, 126) and loss of function with downstream splicing defects (16, 17, 22, 28, 31, 63, 108).”
Liquid–liquid phase separation in neurodegenerative diseases
Haider, R., Boyko, S., & Surewicz, W. K. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-823967-4.00018-x · Cited by 7
Pathophysiological implications of RNP granules in frontotemporal dementia and ALS
Desai, P., & Bandopadhyay, R. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104819 · Cited by 9
“Under conditions of stress, NEAT1_2 expression is upregulated, leading to an increased number and size of paraspeckles (Sunwoo et al., 2009; Hirose et al., 2014).”
BackgroundInfluentialRayman, J. B., Melas, P. A., Schalling, M., Forsell, Y., Kandel, E. R., & Lavebratt, C. (2019) · Journal of Affective Disorders · doi:10.1016/j.jad.2019.09.018 · Cited by 8
Mark4 ablation attenuates pathological phenotypes in a mouse model of tauopathy
Sultanakhmetov, G., Limlingan, S. J. M., Fukuchi, A., Tsuda, K., Suzuki, H., Kato, I., Saito, T., Weitemier, A. Z., & Ando, K. (2024) · Brain Communications · doi:10.1093/braincomms/fcae136 · Cited by 5
“To assay recognition memory in our transgenic mice, 33 we performed the novel object recognition test and observed that PS19 mice performed more poorly than WT in agreement with previous studies 32,45 (Fig.”
BackgroundMethodLee, S., Jung, D., Kim, E.-M., & Kim, K. K. (2024) · Chemosphere · doi:10.1016/j.chemosphere.2024.142485 · Cited by 6
TIA1 Mediates Divergent Inflammatory Responses to Tauopathy in Microglia and MacrophagesPreprint
Webber, C. J., van der Spek, S. J. F., Cruz, A. L., Puri, S., Zhang, C., Aw, J. T. M., Papadimitriou, G.-Z., Roberts, R., Jiang, K., Tran, T., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.06.622325 · Cited by 6
“We have shown that reducing TIA1 in neurons strongly protects against tau-mediated toxicity 14 .”
Self-citationRational Modulation of Liquid–Liquid Phase Separation Offers Novel Ways to Combat Tauopathies
Zhang, X., Wang, L., Lin, N., Gao, M. Y., & Huang, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146709 · Cited by 7
“Importantly, TIA1 accelerates the liquid-to-solid transition of tau droplets and promotes the formation of tau oligomers [102,141,142].”
Younas, N., & Zerr, I. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1686571 · Cited by 6
Carrascoso, I., Velasco, B., & Izquierdo, J. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312775 · Cited by 5
“This phenotype is observed predominantly in female mice [29], and TIA1 haploinsufficiency exacerbates neuroinflammation in tauopathy [31,48].”
BackgroundDisruption of RNA-binding proteins in neurological disorders
Huang, L., Zhao, B., & Wan, Y. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.115119 · Cited by 5
Stress granule‐mediated RNA regulatory mechanism in Alzheimer's disease
Sato, K., Takayama, K., & Inoue, S. (2023) · Geriatrics and gerontology international/Geriatrics & gerontology international · doi:10.1111/ggi.14663 · Cited by 5
“79 Thus, these results suggest that SGs contribute to the misfolding of tau, leading to the formation of NFTs (Fig.”
BackgroundActive protein neddylation or ubiquitylation is dispensable for stress granule dynamicsPreprint
Markmiller, S., Fulzele, A., Higgins, R., Yeo, G. W.-M., & Bennett, E. J. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/418848 · Cited by 5
Identification of circRNAs linked to Alzheimer’s disease and related dementiasPreprint
Puri, S., Hu, J., Sun, Z., Lin, M., Stein, T. D., Farrer, L. A., Wolozin, B. L., & Zhang, X. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.13.499937 · Cited by 5
Self-citationSUMO2 Protects Against Tau-induced Synaptic and Cognitive DysfunctionPreprint
Orsini, F., Argyrousi, E. K., Restelli, E., Ford, L. K., Takamura, H., Matsuzaki, S., Zentilin, L., Pascente, R., Kanaan, N. M., Soni, R. K., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.11.516192 · Cited by 5
Self-citationJiang, L., Roberts, R., Wong, M., Zhang, L., Webber, C. J., Kilci, A., Jenkins, M., Sun, G., Rashad, S., Sun, J., et al. (2023) · Research Square · doi:10.1101/2023.03.28.534515 · Cited by 5
“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) [23, 25, 36, 51-53].”
BackgroundSelf-citationLibera, J., Hu, J., Hu, J., Nguyen, T.-A., Wang, Z., van der Spek, S. J. F., Schult, K., Dorrian, L., Majka, J., Tobunluepop, K., et al. (2025) · SSRN Electronic Journal · doi:10.1101/2025.05.02.651974 · Cited by 7
Self-citationDeciphering the RNA Landscape of RNA Granules.
Ren, Z.-Q., Zhao, S.-R., & Zou, P. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00265 · Cited by 6
Role of Tau Protein Hyperphosphorylation in Diabetic Retinal Neurodegeneration
Mu, J., Zhang, Z., Jiang, C., Geng, H., & Duan, J. (2025) · Journal of Ophthalmology · doi:10.1155/joph/3278794 · Cited by 5
Jhanji, M., Bhan, A., Arrowood, C. A., Yakout, D. W., Shroff, A., McManus, D., Gifford, H., Vacharasin, J. M., Lizarraga, S. B., Nazarko, T. Y., et al. (2025) · IUBMB Life · doi:10.1002/iub.70030 · Cited by 4
Differences in the soluble and insoluble proteome between primary tauopathies
Kavanagh, T., Balcomb, K., Trgovcevic, S., Nementzik, L. R., Kanshin, E., Halliday, G. M., Ueberheide, B. M., & Drummond, E. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70401 · Cited by 5
Aviolat, H., Nominé, Y., Gioria, S., Bonhoure, A., Hoffmann, D., Ruhlmann, C., Nierengarten, H., Ruffenach, F., Villa, P., Trottier, Y., et al. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.09.009 · Cited by 4
Shapeshifting tau: from intrinsically disordered to paired-helical filaments
Mengham, K., Al‐Hilaly, Y. K., Oakley, S. S., Kasbi, K., Maina, M. B., & Serpell, L. C. (2022) · Essays in Biochemistry · doi:10.1042/ebc20220150 · Cited by 4
Kizhakkeduth, S. T., Vahid, A. A., Hassan, M. S. O., Parambil, A. K., Jain, P., & Vijayan, V. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00456 · Cited by 3
Decoding stress granules dynamics: Implications for neurodegenerative disease
Wang, Z., Yang, C., Wang, X., Liu, X., Liu, H., Liu, X., Liu, H., Zhang, L., Shen, H., Zhang, L., et al. (2025) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2025.102758 · Cited by 4
Translated retained intron 11 sequence confers pathological properties to Tau in Alzheimer’s disease
Tan, Y.-Y., Leow, C., Choo, C., Tan, J., & Ong, C. (2025) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2025.102872 · Cited by 3
Heterotypic phase separation in aggregation: Driver or deterrent?
Jacob, T., & Hoyer, W. (2026) · Biophysical Chemistry · doi:10.1016/j.bpc.2026.107577 · Cited by 3
Post-translational modifications as a regulatory code for tau function in health and disease
Nordbeck, A. J., Sharma, B., Garcia, C. A., & Tseng, J. (2026) · Frontiers in Dementia · doi:10.3389/frdem.2026.1834737 · Cited by 3
Rickner, H., Jiang, L., Hong, R., O’Neill, N. K., Wolozin, B. L., & Cheng, C. S. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.058551 · Cited by 4
Self-citationYates, D. M. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.163 · Cited by 3
Decoding Phase Separation of Prion-Like Domains through Data-Driven Scaling LawsPreprint
Maristany, M. J., Gonzalez, A. A., Espinosa, J. R., Huertas, J., Collepardo‐Guevara, R., & Joseph, J. A. (2025) · eLife · doi:10.7554/elife.99068.2 · Cited by 3
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
