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A tau homeostasis signature is linked with the cellular and regional vulnerability of excitatory neurons to tau pathology
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Excitatory neurons are vulnerable cell populations in FTLD-tau, AD, and other tauopathies.
“Excitatory neurons (EX) are vulnerable cell populations in FTLD-tau, AD, and other tauopathies31–33.”
From GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau (2025) · cites this paper as [31]
Neurons are preferentially vulnerable to tau pathology in tauopathies, including FTLD and AD.
“Neurons are preferentially vulnerable to tau pathology in a group of diseases known as tauopathies, including FTLD and AD, a secondary tauopathy31,55.”
From GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau (2025) · cites this paper as [31]
The lower level of PHF1 in homozygous HNOs may be due to increased inhibitory neuronal populations, which are less vulnerable to phosphorylated tau accumulation.
“The lower level of PHF1 in homozygous HNOs may be due to increased inhibitory neuronal populations (Fig. 1e and f), which are less vulnerable to phosphorylated tau accumulation31,50.”
From GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau (2025) · cites this paper as [31]
Excitatory neuronal populations are a vulnerable cell type in human FTLD and AD cases.
“Excitatory neuronal populations are a vulnerable cell type in human FTLD and AD cases31,55.”
From GRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau (2025) · cites this paper as [31]
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Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
A General Framework for Weighted Gene Co-Expression Network Analysis
Zhang, B., & Horvath, S. (2005) · Statistical Applications in Genetics and Molecular Biology · doi:10.2202/1544-6115.1128 · Cited by 5,684
Alzheimer's disease: cell-specific pathology isolates the hippocampal formation.
Hyman, B. T., Van Hoesen, G. W., Damasio, A. R., & Barnes, C. L. (1984) · Science · doi:10.1126/science.6474172 · Cited by 2,268
Adult mouse cortical cell taxonomy revealed by single cell transcriptomics
Tasic, B., Menon, V., Nguyen, T. N., Kim, T. K., Jarsky, T., Yao, Z., Levi, B., Gray, L. T., Sorensen, S. A., Dolbeare, T., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4216 · Cited by 1,714
Pathology of Neurodegenerative Diseases
Dugger, B. N., & Dickson, D. W. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028035 · Cited by 1,665
The Biology of Proteostasis in Aging and Disease
Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472
Propagation of Tau Pathology in a Model of Early Alzheimer's Disease
de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427
Massively parallel single-nucleus RNA-seq with DroNc-seq
Habib, N., Avraham-Davidi, I., Basu, A., Burks, T., Shekhar, K., Hofree, M., Choudhury, S. R., Aguet, F., Gelfand, E., Ardlie, K., et al. (2017) · Nature Methods · doi:10.1038/nmeth.4407 · Cited by 1,069
Neuronal subtypes and diversity revealed by single-nucleus RNA sequencing of the human brain
Lake, B. B., Ai, R., Kaeser, G. E., Salathia, N. S., Yung, Y. C., Liu, R., Wildberg, A., Gao, D., Fung, H.-L., Chen, S., et al. (2016) · Science · doi:10.1126/science.aaf1204 · Cited by 957
Self-citationSelective vulnerability in neurodegenerative diseases
Fu, H., Hardy, J., & Duff, K. E. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0221-2 · Cited by 585
Self-citationAging as an event of proteostasis collapse
Taylor, R. C., & Dillin, A. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004440 · Cited by 538
Flagged first, then by citations
Research works printed but not linked: 31
- Šimić, G. et al. Tau protein hyperphosphorylation and aggregation in Alzheimer’s disease and other tauopathies, and possible neuroprotective strategies. Biomolecules 6, 6 (2016). · DOI
- Spina, S. et al. The tauopathy associated with mutation+3 in intron 10 of Tau: characterization of the MSTD family. Brain 131, 72–89 (2008). · DOI
- Davies, P. & Maloney, A. J. Selective loss of central cholinergic neurons in Alzheimer’s disease. Lancet 2, 1403 (1976). · DOI · Paper page
- Morrison, B. M., Hof, P. R. & Morrison, J. H. Determinants of neuronal vulnerability in neurodegenerative diseases. Ann. Neurol. 44(Suppl 1), S32–S44 (1998). · DOI
- Götz, J., Schonrock, N., Vissel, B. & Ittner, L. M. Alzheimer’s disease selective vulnerability and modeling in transgenic mice. J. Alzheimers Dis. 18, 243–251 (2009). · DOI
- Riascos, D. et al. Age-related loss of calcium buffering and selective neuronal vulnerability in Alzheimer’s disease. Acta Neuropathol. 122, 565–576 (2011). · DOI
- Ahmadian, S. S. et al. Loss of calbindin-D28K is associated with the full range of tangle pathology within basal forebrain cholinergic neurons in Alzheimer’s disease. Neurobiol. Aging 36, 3163–3170 (2015). · DOI
- Hof, P. R. et al. Age-related distribution of neuropathologic changes in the cerebral cortex of patients with Down’s syndrome. Quantitative regional analysis and comparison with Alzheimer’s disease. Arch. Neurol. 52, 379–391 (1995). · DOI
- Seeley, W. W. Selective functional, regional, and neuronal vulnerability in frontotemporal dementia. Curr. Opin. Neurol. 21, 701–707 (2008). · DOI
- Mattson, M. P. & Magnus, T. Ageing and neuronal vulnerability. Nat. Rev. Neurosci. 7, 278–294 (2006). · DOI · Paper page
- Saxena, S. & Caroni, P. Selective neuronal vulnerability in neurodegenerative diseases: from stressor thresholds to degeneration. Neuron 71, 35–48 (2011). · DOI
- Roselli, F. & Caroni, P. From intrinsic firing properties to selective neuronal vulnerability in neurodegenerative diseases. Neuron 85, 901–910 (2015). · DOI
- Kaushik, S. & Cuervo, A. M. Proteostasis and aging. Nat. Med. 21, 1406–1415 (2015). · DOI · Paper page
- Freer, R. et al. A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimer’s disease. Sci. Adv. 2, e1600947 (2016). · DOI
- Liu, L. et al. Trans-synaptic spread of tau pathology in vivo. PLoS One 7, e31302 (2012). · DOI
- Lei, Z., Brizzee, C. & Johnson, G. V. BAG3 facilitates the clearance of endogenous tau in primary neurons. Neurobiol. Aging 36, 241–248 (2015). · DOI
- Seidel, K. et al. The HSPB8-BAG3 chaperone complex is upregulated in astrocytes in the human brain affected by protein aggregation diseases. Neuropathol. Appl. Neurobiol. 38, 39–53 (2012). · DOI
- Wegmann, S. et al. Removing endogenous tau does not prevent tau propagation yet reduces its neurotoxicity. EMBO J. 34, 3028–3041 (2015). · DOI · Paper page
- Ciryam, P. et al. A transcriptional signature of Alzheimer’s disease is associated with a metastable subproteome at risk for aggregation. Proc. Natl Acad. Sci. USA 113, 4753–4758 (2016). · DOI
- Fu, H. et al. 3D visualization of the temporal and spatial spread of tau pathology reveals extensive sites of tau accumulation associated with neuronal loss and recognition memory deficit in aged tau transgenic mice. PLoS One 11, e0159463 (2016). · DOI
- Ferrer, I. et al. Glial and neuronal tau pathology in tauopathies: characterization of disease-specific phenotypes and tau pathology progression. J. Neuropathol. Exp. Neurol. 73, 81–97 (2014). · DOI · Paper page
- Kahlson, M. A. & Colodner, K. J. Glial tau pathology in tauopathies: functional consequences. J. Exp. Neurosci. 9(Suppl 2), 43–50 (2016).
- Leyns, C. E. G. & Holtzman, D. M. Glial contributions to neurodegeneration in tauopathies. Mol. Neurodegener. 12, 50 (2017). · DOI · Paper page
- Baranczak, A. & Kelly, J. W. A current pharmacologic agent versus the promise of next generation therapeutics to ameliorate protein misfolding and/or aggregation diseases. Curr. Opin. Chem. Biol. 32, 10–21 (2016). · DOI
- Balch, W. E., Morimoto, R. I., Dillin, A. & Kelly, J. W. Adapting proteostasis for disease intervention. Science 319, 916–919 (2008). · DOI · Paper page
- Seubert, P. et al. Detection of phosphorylated Ser262 in fetal tau, adult tau, and paired helical filament tau. J. Biol. Chem. 270, 18917–18922 (1995). · DOI · Paper page
- Sanders, D. W. et al. Distinct tau prion strains propagate in cells and mice and define different tauopathies. Neuron 82, 1271–1288 (2014). · DOI · Paper page
- Fu, H. et al. Tau pathology induces excitatory neuron loss, grid cell dysfunction, and spatial memory deficits reminiscent of early Alzheimer’s disease. Neuron 93, 533–541.e5 (2017). · DOI · Paper page
- Ji, C., Steimle, B. L., Bailey, D. K. & Kosman, D. J. The ferroxidase hephaestin but not amyloid precursor protein is required for ferroportin-supported iron efflux in primary hippocampal neurons. Cell. Mol. Neurobiol. 38, 941–954 (2018). · DOI
- Tosto, G. et al. F-box/LRR-repeat protein 7 is genetically associated with Alzheimer’s disease. Ann. Clin. Transl. Neurol 2, 810–820 (2015). · DOI
- Wu, J. W. et al. Small misfolded Tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons. J. Biol. Chem. 288, 1856–1870 (2013). · DOI · Paper page
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Aman, Y., Schmauck-Medina, T., Hansen, M., Morimoto, R. I., Simon, A. K., Bjedov, I., Palikaras, K., Simonsen, A., Johansen, T., Tavernarakis, N., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00098-4 · Cited by 1,313
Synergy between amyloid-β and tau in Alzheimer’s disease
Busche, M. A., & Hyman, B. T. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0687-6 · Cited by 1,242
Molecular characterization of selectively vulnerable neurons in Alzheimer’s disease
Leng, K., Li, E., Eser, R., Piergies, A., Sit, R., Tan, M., Neff, N., Li, S. H., Rodriguez, R. D., Suemoto, C. K., et al. (2021) · Nature Neuroscience · doi:10.1038/s41593-020-00764-7 · Cited by 485
The clinical promise of biomarkers of synapse damage or loss in Alzheimer’s disease
the Synaptic Health Endpoints Working Group, Colom-Cadena, M., Spires-Jones, T., Zetterberg, H., Blennow, K., Caggiano, A., DeKosky, S. T., Fillit, H., Harrison, J. E., Schneider, L. S., et al. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00588-4 · Cited by 328
Chaperone-mediated autophagy prevents collapse of the neuronal metastable proteome
Bourdenx, M., Martín-Segura, A., Scrivo, A., Rodriguez-Navarro, J. A., Kaushik, S., Tasset, I., Diaz, A., Storm, N. J., Xin, Q., Juste, Y. R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.048 · Cited by 337
Tau: 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
Molecular signatures underlying neurofibrillary tangle susceptibility in Alzheimer’s disease
Otero-Garcia, M., Mahajani, S. U., Wakhloo, D., Tang, W., Xue, Y.-Q., Morabito, S., Pan, J., Oberhauser, J., Madira, A. E., Shakouri, T., et al. (2022) · Neuron · doi:10.1016/j.neuron.2022.06.021 · Cited by 262
Somatic genomic changes in single Alzheimer’s disease neurons
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Profiling senescent cells in human brains reveals neurons with CDKN2D/p19 and tau neuropathology
Dehkordi, S. K., Walker, J., Sah, E., Bennett, E., Atrian, F., Frost, B., Woost, B., Bennett, R. E., Orr, T. C., Zhou, Y., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00142-3 · Cited by 169
Compilation of reported protein changes in the brain in Alzheimer's disease
Askenazi, M., Kavanagh, T., Pires, G., Ueberheide, B., Wisniewski, T., & Drummond, E. (2023) · Nature Communications · doi:10.1038/s41467-023-40208-x · Cited by 174
Harris, S. S., Wolf, F., De Strooper, B., & Busche, M. A. (2020) · Neuron · doi:10.1016/j.neuron.2020.06.005 · Cited by 161
The informed road map to prevention of Alzheimer Disease: a call to arms
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Pharmacological modulation of autophagy for Alzheimer's disease therapy: Opportunities and obstacles
Deng, Z., Dong, Y., Zhou, X., Lu, J.-H., & Yue, Z. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.12.009 · Cited by 58
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D’Oliveira Albanus, R., Finan, G. M., Brase, L., Sweeney, N., Kim, T. Y., Chen, S., Ryoo, Y., Park, J., Guo, Q., Iyer, A. K., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adx0027 · Cited by 19
Self-citationGRAMD1B is a regulator of lipid homeostasis, autophagic flux and phosphorylated tau
Acosta Ingram, D., Turkes, E., Kim, T. Y., Vo, S., Sweeney, N., Bonte, M.-A., Rutherford, R., Julian, D. L., Pan, M., Marsh, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58585-w · Cited by 12
Self-citation
Metadata
- Authors
- Fu, H., Possenti, A., Freer, R., Nakano, Y., Hernandez Villegas, N. C., Tang, M., Cauhy, P. V. M., Lassus, B. A., Chen, S., Fowler, S. L., Figueroa, H. Y., Huey, E. D., Johnson, G. V. W., Vendruscolo, M., & Duff, K. E.
- Venue
- Nature Neuroscience
- Published
- 2018-12-17
- Volume
- 22
- Issue
- 1
- Pages
- 47-56
- ISSN
- 1097-6256
- 1546-1726
- PMC
- PMC6330709
- Cited by
- 258
- References
- 11
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
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