Acetylated Tau Neuropathology in Sporadic and Hereditary Tauopathies

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works

The Consortium to Establish a Registry for Alzheimer's Disease (CERAD): Part II. Standardization of the neuropathologic assessment of Alzheimer's disease

Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961 · see citing works

Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17

Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498 · see citing works

National Institute on Aging–Alzheimer's Association guidelines for the neuropathologic assessment of Alzheimer's disease

Hyman, B. T., Phelps, C. H., Beach, T. G., Bigio, E. H., Cairns, N. J., Carrillo, M. C., Dickson, D. W., Duyckaerts, C., Frosch, M. P., Masliah, E., et al. (2012) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2011.10.007 · Cited by 3,092 · see citing works

National Institute on Aging–Alzheimer’s Association guidelines for the neuropathologic assessment of Alzheimer’s disease: a practical approach

Montine, T. J., Phelps, C. H., Beach, T. G., Bigio, E. H., Cairns, N. J., Dickson, D. W., Duyckaerts, C., Frosch, M. P., Masliah, E., Mirra, S. S., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-011-0910-3 · Cited by 2,992 · see citing works

Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480 · see citing works

Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update

Mackenzie, I. R. A., Neumann, M., Bigio, E. H., Cairns, N. J., Alafuzoff, I., Kril, J., Kovacs, G. G., Ghetti, B., Halliday, G., Holm, I. E., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-009-0612-2 · Cited by 1,012 · see citing works

Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949 · see citing works

The acetylation of tau inhibits its function and promotes pathological tau aggregation

Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., Trojanowski, J. Q., & Lee, V. M. Y. (2011) · Nature Communications · doi:10.1038/ncomms1255 · Cited by 724 · see citing works

Mutations of Tau Protein in Frontotemporal Dementia Promote Aggregation of Paired Helical Filaments by Enhancing Local β-Structure

von Bergen�, M., Barghorn, S., Li, L., Marx, A., Biernat, J., Mandelkow, E., & Mandelkow�, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105196200 · Cited by 590 · see citing works

Monoclonal antibody PHF‐1 recognizes tau protein phosphorylated at serine residues 396 and 404

Otvos, L., Feiner, L., Lang, E., Szendrei, G. I., Goedert, M., & Lee, V. M. (1994) · Journal of Neuroscience Research · doi:10.1002/jnr.490390607 · Cited by 488 · see citing works

Frontotemporal dementia: Clinicopathological correlations

Forman, M. S., Farmer, J., Johnson, J. K., Clark, C. M., Arnold, S. E., Coslett, H. B., Chatterjee, A., Hurtig, H. I., Karlawish, J. H., Rosen, H. J., et al. (2006) · Annals of Neurology · doi:10.1002/ana.20873 · Cited by 478 · see citing works

Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies

Irwin, D. J., Cohen, T. J., Grossman, M., Arnold, S. E., Xie, S. X., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Brain · doi:10.1093/brain/aws013 · Cited by 281 · see citing works

Argyrophilic Grain Disease Is a Sporadic 4-Repeat Tauopathy

Togo, T., Sahara, N., Yen, S.-H., Cookson, N., Ishizawa, T., Hutton, M., de Silva, R., Lees, A., & Dickson, D. W. (2002) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/61.6.547 · Cited by 273 · see citing works

Decreased interleukin-10 and increased interleukin-12p40 mRNA are associated with disease activity and characterize different disease stages in multiple sclerosis

van Boxel-Dezaire, A. H. H., Hoff, S. C. J., van Oosten, B. W., Verweij, C. L., Dräger, A. M., Adèr, H. J., van Houwelingen, H. C., Barkhof, F., Polman, C. H., & Nagelkerken, L. M. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199906)45:6 · Cited by 266 · see citing works

Argyrophilic grain disease

Ferrer, I., Santpere, G., & van Leeuwen, F. W. (2008) · Brain · doi:10.1093/brain/awm305 · Cited by 256 · see citing works

Pathological inclusion bodies in tauopathies contain distinct complements of tau with three or four microtubule‐binding repeat domains as demonstrated by new specific monoclonal antibodies

de Silva, R., Lashley, T., Gibb, G., Hanger, D. P., Hope, A., Reid, A. R., Bandopadhyay, R., Utton, M. A., Strand, C., Jowett, T. P., et al. (2003) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2003.00463.x · Cited by 220 · see citing works

Distinct isoforms of tau aggregated in neurons and glial cells in brains of patients with Pick's disease, corticobasal degeneration and progressive supranuclear palsy

Arai, T., Ikeda, K., Akiyama, H., Shikamoto, Y., Tsuchiya, K., Yagishita, S., Beach, T. G., Rogers, J., Schwab, C., & McGeer, P. L. (2001) · Acta Neuropathologica · doi:10.1007/s004010000283 · Cited by 197 · see citing works

Sporadic Pick's disease: A tauopathy characterized by a spectrum of pathological τ isoforms in gray and white matter

Zhukareva, V., Mann, D., Pickering-Brown, S., Uryu, K., Shuck, T., Shah, K., Grossman, M., Miller, B. L., Hulette, C., Feinstein, S., et al. (2002) · Annals of Neurology · doi:10.1002/ana.10222 · Cited by 157 · see citing works

Neurofibrillary tangle-predominant dementia: comparison with classical Alzheimer disease

Jellinger, K. A., & Attems, J. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0156-7 · Cited by 157 · see citing works

The microtubule-associated tau protein has intrinsic acetyltransferase activity

Cohen, T. J., Friedmann, D., Hwang, A. W., Marmorstein, R., & Lee, V. M. Y. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2555 · Cited by 149 · see citing works

Senile Dementia with Tangles (Tangle Predominant Form of Senile Dementia)

Jellinger, K. A., & Bancher, C. (1998) · Brain Pathology · doi:10.1111/j.1750-3639.1998.tb00160.x · Cited by 148 · see citing works

Novel Presenilin 1 Mutation (S170F) Causing Alzheimer Disease With Lewy Bodies in the Third Decade of Life

Snider, B. J., Norton, J. B., Coats, M. A., Chakraverty, S., Hou, C. E., Jervis, R., Lendon, C. L., Goate, A., McKeel, D. W., & Morris, J. C. (2005) · Archives of Neurology · doi:10.1001/archneur.62.12.1821 · Cited by 129 · see citing works

Molecular analysis of neurofibrillary degeneration in Alzheimer's disease. An immunohistochemical study.

Bondareff, W., Wischik, C. M., Novák, M., Amos, W. B., Klug, A., & Roth, M. (1990) · Europe PMC (PubMed Central) · Cited by 121 · see citing works

Argyrophilic grain disease: widespread hyperphosphorylation of tau protein in limbic neurons

Tolnay, M., Spillantini, M. G., Goedert, M., ULRICH, J., Langui, D., & Probst, A. (1997) · Acta Neuropathologica · doi:10.1007/s004010050642 · Cited by 115 · see citing works

Cellular tau pathology and immunohistochemical study of tau isoforms in sporadic tauopathies

Yoshida, M. (2006) · Neuropathology · doi:10.1111/j.1440-1789.2006.00743.x · Cited by 108 · see citing works

Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation

Grinberg, L. T., Wang, X., Wang, C., Sohn, P., Theofilas, P., Sidhu, M., Arevalo, J. B., Heinsen, H., Huang, E. J., Rosen, H. J., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1080-2 · Cited by 107 · see citing works

Building an integrated neurodegenerative disease database at an academic health center

Xie, S. X., Baek, Y., Grossman, M., Arnold, S. E., Karlawish, J. H., Siderowf, A. D., Hurtig, H. I., Elman, L. B., McCluskey, L. F., Deerlin, V. M. V., et al. (2011) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.08.233 · Cited by 83 · see citing works

A study of dementia with argyrophilic grains Possible cytoskeletal abnormality in dendrospinal portion of neurons and oligodendroglia

Ikeda, K., Akiyama, H., Kondo, H., & Haga, C. (1995) · Acta Neuropathologica · doi:10.1007/bf00307644 · Cited by 80 · see citing works

The impact of argyrophilic grain disease on the development of dementia and its relationship to concurrent Alzheimer's disease‐related pathology

Thal, D. R., Schultz, C., Botez, G., Del Tredici, K., Mrak, R. E., Griffin, W. S. T., Wiestler, O. D., Braak, H., & Ghebremedhin, E. (2005) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2005.00635.x · Cited by 69 · see citing works

Biochemical Analysis of τ Proteins in Argyrophilic Grain Disease, Alzheimer's Disease, and Pick's Disease: A Comparative Study

Zhukareva, V., Shah, K., Uryu, K., Braak, H., Tredici, K. D., Sundarraj, S., Clark, C., Trojanowski, J., & Lee, V. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64390-8 · Cited by 64 · see citing works

Increased Frequency of Argyrophilic Grain Disease in Alzheimer Disease with 4R Tau-Specific Immunohistochemistry

Fujino, Y., Wang, D.-S., Thomas, N., Espinoza, M., Davies, P., & Dickson, D. W. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.3.209 · Cited by 63 · see citing works

Argyrophilic Grain Disease in Demented Subjects Presenting Initially With Amnestic Mild Cognitive Impairment

Jicha, G. A., Petersen, R. C., Knopman, D. S., Boeve, B. F., Smith, G. E., Geda, Y. E., Johnson, K., Cha, R. H., DeLucia, M. W., Braak, H., et al. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000225312.11858.57 · Cited by 52 · see citing works

Neuropathologic variation in frontotemporal dementia due to the intronic tau 10 +16 mutation

Lantos, P. L., Cairns, N. J., Khan, M. N., King, A., Révész, T., Janssen, J. C., Morris, H. R., & Rossor, M. N. (2002) · Neurology · doi:10.1212/wnl.58.8.1169 · Cited by 51 · see citing works

Argyrophilic grain disease: frequency and neuropathology in centenarians

Ding, Z., Wang, Y., Jiang, Y., Yoshida, M., Mimuro, M., Inagaki, T., Iwase, T., & Hashizume, Y. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0043-2 · Cited by 50 · see citing works

Tau-positive grains are constant in centenarians’ hippocampus

Pham, C.-T., de Silva, R., Haı̈k, S., Verny, M., Sachet, A., Forette, B., Lees, A. J., Hauw, J., & Duyckaerts, C. J. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.07.009 · Cited by 29 · see citing works

Frequency and Clinicopathological Characteristics of Presenilin 1 Gly206Ala Mutation in Puerto Rican Hispanics with Dementia

Arnold, S. E., Vega, I. E., Karlawish, J. H., Wolk, D. A., Nuñez, J., Negrón, M., Xie, S. X., Wang, L.-S., Dubroff, J. G., McCarty-Wood, E., et al. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121570 · Cited by 27 · see citing works

Familial Frontotemporal Dementia: From Gene Discovery to Clinical Molecular Diagnostics

Deerlin, V. M. V., Gill, L. H., Farmer, J. M., Trojanowski, J. Q., & Lee, V. M. ‐. (2003) · Clinical Chemistry · doi:10.1373/49.10.1717 · Cited by 21 · see citing works

Tau in physiology and pathology

Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251 · see citing works

Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders

Falkenberg, K. J., & Johnstone, R. W. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4360 · Cited by 1,564 · see citing works

Roles of tau protein in health and disease

Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003 · see citing works

Role of Tau as a Microtubule-Associated Protein: Structural and Functional Aspects

Barbier, P., Zejneli, O., Martinho, M., Lasorsa, A., Belle, V., Smet‐Nocca, C., Tsvetkov, P. O., Devred, F., & Landrieu, I. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00204 · Cited by 623 · see citing works

Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits

Min, S.-W., Chen, X., Tracy, T. E., Li, Y., Zhou, Y., Wang, C., Shirakawa, K., Minami, S. S., Defensor, E., Mok, S. A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3951 · Cited by 516 · see citing works

Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation

Chen, Y., & Yu, Y. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02853-3 · Cited by 516 · see citing works

MAPT mutations, tauopathy, and mechanisms of neurodegeneration

Strang, K. H., Golde, T. E., & Giasson, B. I. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0197-x · Cited by 424 · see citing works

What is the evidence that tau pathology spreads through prion-like propagation?

Mudher, A., Colin, M., Dujardin, S., Medina, M., Dewachter, I., Alavi Naini, S. M., Mandelkow, E.-M., Mandelkow, E., Buée, L., Goedert, M., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0488-7 · Cited by 384 · see citing works

Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation

Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367 · see citing works

An acetylation switch controls TDP-43 function and aggregation propensity

Cohen, T. J., Hwang, A. W., Restrepo, C. R., Yuan, C., Trojanowski, J. Q., & Lee, V. M. ‐. (2015) · Nature Communications · doi:10.1038/ncomms6845 · Cited by 357 · see citing works

Acetylated Tau Obstructs KIBRA-Mediated Signaling in Synaptic Plasticity and Promotes Tauopathy-Related Memory Loss

Tracy, T. E., Sohn, P. D., Minami, S. S., Wang, C., Min, S.-W., Li, Y., Zhou, Y., Le, D., Lo, I., Ponnusamy, R., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.005 · Cited by 277 · see citing works

Alzheimer's disease and type 2 diabetes: a critical assessment of the shared pathological traits

Chatterjee, S., & Mudher, A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00383 · Cited by 270 · see citing works

Differential induction and spread of tau pathology in young PS19 tau transgenic mice following intracerebral injections of pathological tau from Alzheimer’s disease or corticobasal degeneration brains

Boluda, S., Iba, M., Zhang, B., Raible, K. M., Lee, V. M. ‐., & Trojanowski, J. Q. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1373-0 · Cited by 259 · see citing works

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 262 · see citing works

Cellular and pathological functions of tau

Bravo, C. P., Naguib, S. A., & Gan, L. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00753-9 · Cited by 245 · see citing works

Protein phosphorylation in neurodegeneration: friend or foe?

Tenreiro, S., Eckermann, K., & Outeiro, T. F. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00042 · Cited by 252 · see citing works

Alpha-Synuclein Function and Dysfunction on Cellular Membranes

Snead, D., & Eliezer, D. (2014) · Experimental Neurobiology · doi:10.5607/en.2014.23.4.292 · Cited by 222 · see citing works

Acetylated tau inhibits chaperone-mediated autophagy and promotes tau pathology propagation in mice

Caballero, B., Bourdenx, M., Luengo, E., Diaz, A., Sohn, P. D., Chen, X., Wang, C., Juste, Y. R., Wegmann, S., Patel, B., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22501-9 · Cited by 223 · see citing works

Deep clinical and neuropathological phenotyping of P ick disease

Irwin, D. J., Brettschneider, J., McMillan, C. T., Cooper, F. I., Olm, C. A., Arnold, S. E., Deerlin, V. M. V., Seeley, W. W., Miller, B. L., Lee, E. B., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24559 · Cited by 204 · see citing works

Tauopathies as clinicopathological entities

Irwin, D. J. (2015) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2015.09.020 · Cited by 199 · see citing works

An inhibitor of the proteasomal deubiquitinating enzyme USP14 induces tau elimination in cultured neurons

Boselli, M. G., Lee, B., Robert, J., Prado, M. A., Min, S., Cheng, C., Silva, M. C., Seong, C., Elsasser, S., Hatle, K. M., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.815126 · Cited by 152 · see citing works

SIRT1 Deacetylates Tau and Reduces Pathogenic Tau Spread in a Mouse Model of Tauopathy

Min, S., Sohn, P., Li, Y., Devidze, N., Johnson, J. R., Krogan, N. J., Masliah, E., Mok, S., Gestwicki, J. E., & Gan, L. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.2369-17.2018 · Cited by 148 · see citing works

Lysine-Directed Post-translational Modifications of Tau Protein in Alzheimer's Disease and Related Tauopathies

Kontaxi, C., Piccardo, P., & Gill, A. C. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00056 · Cited by 138 · see citing works

New Insights Into Drug Discovery Targeting Tau Protein

Soeda, Y., & Takashima, A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.590896 · Cited by 133 · see citing works

Diversity of astroglial responses across human neurodegenerative disorders and brain aging

Ferrer, I. (2017) · Brain Pathology · doi:10.1111/bpa.12538 · Cited by 123 · see citing works

Genetics, Functions, and Clinical Impact of Presenilin-1 (PSEN1) Gene

Bagaria, J., Bagyinszky, E., & An, S. S. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810970 · Cited by 114 · see citing works

Glial Tau Pathology in Tauopathies: Functional Consequences

Kahlson, M. A., & Colodner, K. J. (2015) · Journal of Experimental Neuroscience · doi:10.4137/jen.s25515 · Cited by 110 · see citing works

A Dual Pathogenic Mechanism Links Tau Acetylation to Sporadic Tauopathy

Trzeciakiewicz, H., Tseng, J., Wander, C. M., Madden, V. J., Tripathy, A., Yuan, C., & Cohen, T. J. (2017) · Scientific Reports · doi:10.1038/srep44102 · Cited by 111 · see citing works

Acetylation as a major determinant to microtubule-dependent autophagy: Relevance to Alzheimer's and Parkinson disease pathology

Esteves, A. R., Palma, A. M., Gomes, R., Santos, D., Silva, D. F., & Cardoso, S. M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.11.014 · Cited by 103 · see citing works

Pathological Changes of Tau Related to Alzheimer’s Disease

Chu, D., & Liu, F. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00457 · Cited by 103 · see citing works

Detection of Alzheimer Disease (AD)-Specific Tau Pathology in AD and NonAD Tauopathies by Immunohistochemistry With Novel Conformation-Selective Tau Antibodies

Gibbons, G. S., Banks, R. A., Kim, B., Changolkar, L., Riddle, D. M., Leight, S. N., Irwin, D. J., Trojanowski, J. Q., & Lee, V. M. Y. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nly010 · Cited by 94 · see citing works

Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies

Silva, M. C., & Haggarty, S. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238948 · Cited by 87 · see citing works

Tau and MAPT genetics in tauopathies and synucleinopathies

Léveillé, E., Ross, O. A., & Gan‐Or, Z. (2021) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2021.09.008 · Cited by 83 · see citing works

Incipient progressive supranuclear palsy is more common than expected and may comprise clinicopathological subtypes: a forensic autopsy series

Yoshida, K., Hata, Y., Kinoshita, K., Takashima, S., Tanaka, K., & Nishida, N. (2017) · Acta Neuropathologica · doi:10.1007/s00401-016-1665-7 · Cited by 78 · see citing works

Regulation of neuronal microtubule dynamics by tau: Implications for tauopathies

Venkatramani, A., & Panda, D. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.04.120 · Cited by 79 · see citing works

Asymmetry of post-mortem neuropathology in behavioural-variant frontotemporal dementia

Irwin, D. J., McMillan, C. T., Xie, S. X., Rascovsky, K., Deerlin, V. M. V., Coslett, H. B., Hamilton, R. H., Aguirre, G. K., Lee, E. B., Lee, V. M. ‐., et al. (2017) · Brain · doi:10.1093/brain/awx319 · Cited by 74 · see citing works

The Role of Post-Translational Modifications on the Structure and Function of Tau Protein

Ye, H., Han, Y., Li, P., Su, Z., & Huang, Y. (2022) · Journal of Molecular Neuroscience · doi:10.1007/s12031-022-02002-0 · Cited by 74 · see citing works

Nuclear Magnetic Resonance Analysis of the Acetylation Pattern of the Neuronal Tau Protein

Kamah, A., Huvent, I., Cantrelle, F., Qi, H., Lippens, G. M., Landrieu, I., & Smet‐Nocca, C. (2014) · Biochemistry · doi:10.1021/bi500006v · Cited by 73 · see citing works

Degradation or aggregation: the ramifications of post-translational modifications on tau

Park, S., Lee, J. H., Jeon, J. H., & Lee, M. J. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.6.077 · Cited by 68 · see citing works

Semi-Automated Digital Image Analysis of Pick’s Disease and TDP-43 Proteinopathy

Irwin, D. J., Byrne, M. D., McMillan, C. T., Cooper, F. I., Arnold, S. E., Lee, E. B., Deerlin, V. M. V., Xie, S. X., Lee, V. M. ‐., Grossman, M., et al. (2015) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155415614303 · Cited by 64 · see citing works

Oligodendrogliopathy in neurodegenerative diseases with abnormal protein aggregates: The forgotten partner

Ferrer, I. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.07.004 · Cited by 62 · see citing works

SIRT1 as a therapeutic target for Alzheimer’s disease

Wong, S. Y., & Tang, B. L. (2016) · Reviews in the Neurosciences · doi:10.1515/revneuro-2016-0023 · Cited by 59 · see citing works

Quantification of Tau Protein Lysine Methylation in Aging and Alzheimer’s Disease

Huseby, C. J., Hoffman, C. N., Cooper, G. L., Cocuron, J.-C., Alonso, A. P., Thomas, S. N., Yang, A. J., & Kuret, J. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-190604 · Cited by 54 · see citing works

Distinct populations of highly potent TAU seed conformers in rapidly progressing Alzheimer’s disease

Kim, C., Haldiman, T., Kang, S.-G., Hromadkova, L., Han, Z. Z., Chen, W., Lissemore, F., Lerner, A., de Silva, R., Cohen, M. L., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abg0253 · Cited by 55 · see citing works

SIRT6-CBP-dependent nuclear Tau accumulation and its role in protein synthesis

Portillo, M., Eremenko, E., Kaluski, S., García-Venzor, A., Onn, L., Stein, D., Slobodnik, Z., Zaretsky, A., Ueberham, U., Einav, M., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109035 · Cited by 55 · see citing works

Oxidative Stress in Tauopathies: From Cause to Therapy

Bartolomé, F. B., Carro, E., & Alquézar, C. (2022) · Antioxidants · doi:10.3390/antiox11081421 · Cited by 57 · see citing works

Neuropathology and pathogenesis of extrapyramidal movement disorders: a critical update—I. Hypokinetic-rigid movement disorders

Jellinger, K. A. (2019) · Journal of Neural Transmission · doi:10.1007/s00702-019-02028-6 · Cited by 55 · see citing works

Evaluation of the brain-penetrant microtubule-stabilizing agent, dictyostatin, in the PS19 tau transgenic mouse model of tauopathy

Makani, V. S., Zhang, B., Han, H., Yao, Y., Lassalas, P., Lou, K., Paterson, I., Lee, V. M. ‐., Trojanowski, J. Q., Ballatore, C., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0378-4 · Cited by 51 · see citing works

Lysine acetylation regulates the RNA binding, subcellular localization and inclusion formation of FUS

Arenas, A., Chen, J., Kuang, L., Barnett, K. R., Kasarskis, E. J., Gál, J., & Zhu, H. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa159 · Cited by 51 · see citing works

An acetylation mimicking mutation, K274Q, in tau imparts neurotoxicity by enhancing tau aggregation and inhibiting tubulin polymerization

Rane, J. S., Kumari, A. R., & Panda, D. (2019) · Biochemical Journal · doi:10.1042/bcj20190042 · Cited by 47 · see citing works

Acetylation discriminates disease-specific tau deposition

Chakraborty, P., Rivière, G., Hebestreit, A., de Opakua, A. I., Vorberg, I. M., Andreas, L. B., & Zweckstetter, M. (2023) · Nature Communications · doi:10.1038/s41467-023-41672-1 · Cited by 47 · see citing works

Neurodegeneration and sport

Davis, G. A., Castellani, R. J., & McCrory, P. (2015) · Neurosurgery · doi:10.1227/neu.0000000000000722 · Cited by 47 · see citing works

Tau Propagation, Different Tau Phenotypes, and Prion-like Properties of Tau

Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.06.004 · Cited by 44 · see citing works

A brain-penetrant triazolopyrimidine enhances microtubule-stability, reduces axonal dysfunction and decreases tau pathology in a mouse tauopathy model

Zhang, B., Yao, Y., Cornec, A., Oukoloff, K., James, M. J., Koivula, P. P., Trojanowski, J. Q., Smith, A. B., Lee, V. M. ‐., Ballatore, C., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0291-3 · Cited by 44 · see citing works

Detection of Alzheimer’s disease (AD) specific tau pathology with conformation-selective anti-tau monoclonal antibody in co-morbid frontotemporal lobar degeneration-tau (FTLD-tau)

Gibbons, G. S., Kim, S., Robinson, J. L., Changolkar, L. N., Irwin, D. J., Shaw, L. M. J., Lee, V. M. ‐., & Trojanowski, J. Q. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0687-5 · Cited by 43 · see citing works

Invited review: Drug development for tauopathies

Grüninger, F. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12192 · Cited by 40 · see citing works

Characteristic asymmetric limbic and anterior temporal atrophy in demented patients with pathologically confirmed argyrophilic grain disease

Sakurai, K., Tokumaru, A. M., Ikeda, T., Morimoto, S., Inui, S., Sumida, K., Oba, H., Nakagawa, M., Matsukawa, N., & Hashizume, Y. (2019) · Neuroradiology · doi:10.1007/s00234-019-02247-4 · Cited by 40 · see citing works

Post-translational modifications within tau paired helical filament nucleating motifs perturb microtubule interactions and oligomer formation

Acosta, D. M., Mancinelli, C. D., Bracken, C., & Eliezer, D. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101442 · Cited by 35 · see citing works

Isoform-specific patterns of tau burden and neuronal degeneration in MAPT-associated frontotemporal lobar degeneration

Giannini, L., Ohm, D. T., Rozemüller, A. J. M., Dratch, L., Suh, E. R., Deerlin, V. M. V., Trojanowski, J. Q., Lee, E. B., Swieten, J. C. V., Grossman, M., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02487-4 · Cited by 34 · see citing works

Tau Seeding Mouse Models with Patient Brain-Derived Aggregates

Robert, A., Schöll, M., & Vogels, T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116132 · Cited by 35 · see citing works

Tau K321/K353 pseudoacetylation within KXGS motifs regulates tau–microtubule interactions and inhibits aggregation

Xia, Y., Bell, B. M., & Giasson, B. I. (2021) · Scientific Reports · doi:10.1038/s41598-021-96627-7 · Cited by 33 · see citing works

AMPK Ameliorates Tau Acetylation and Memory Impairment Through Sirt1

Wang, L., Shi, F.-X., Li, N., Cao, Y., Lei, Y., Wang, J., Tian, Q., & Zhou, X. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02079-x · Cited by 33 · see citing works

A unique tau conformation generated by an acetylation-mimic substitution modulates P301S-dependent tau pathology and hyperphosphorylation

Ajit, D., Trzeciakiewicz, H., Tseng, J., Wander, C. M., Chen, Y., Ajit, A., King, D. P., & Cohen, T. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009674 · Cited by 31 · see citing works

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 · see citing works

Brain microRNAs dysregulation: Implication for missplicing and abnormal post-translational modifications of tau protein in Alzheimer’s disease and related tauopathies

Bazrgar, M., Khodabakhsh, P., Mohagheghi, F., Prudencio, M., & Ahmadiani, A. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104729 · Cited by 28 · see citing works

The diagnosis of progressive supranuclear palsy: current opinions and challenges

Ali, F., & Josephs, K. A. (2018) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2018.1489241 · Cited by 27 · see citing works

Astrogliopathy in Tauopathies

Ferrer, I. (2018) · Neuroglia · doi:10.3390/neuroglia1010010 · Cited by 25 · see citing works

The Acetyl Mimicking Mutation, K274Q in Tau, Enhances the Metal Binding Affinity of Tau and Reduces the Ability of Tau to Protect DNA

Rane, J. S., Kumari, A. R., & Panda, D. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00455 · Cited by 27 · see citing works

Acetylation of Aβ42 at Lysine 16 Disrupts Amyloid Formation

Adhikari, R., Yang, M., Saikia, N., Dutta, C., Alharbi, W. F. A., Shan, Z. J., Pandey, R., & Tiwari, A. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00069 · Cited by 29 · see citing works

A Distinct Tau Code Controlled by HDAC6 is Linked to Tau Pathogenesis and the Neuronal Stress Response

Tseng, J., Ajit, A., Tabassum, Z., Patel, N., Tian, X., Chen, Y., Prevatte, A. W., Ling, K., Rigo, F., Meeker, R. B., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2021.109037 · Cited by 26 · see citing works

Identification of high-performing antibodies for the reliable detection of Tau proteoforms by Western blotting and immunohistochemistry

Ellis, M. J., Lekka, C., Holden, K. L., Tulmin, H., Seedat, F., O'Brien, D. P., Dhayal, S., Zeissler, M., Knudsen, J. G., Kessler, B. M., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02729-7 · Cited by 26 · see citing works

The Structure Biology of Tau and Clue for Aggregation Inhibitor Design

Wang, D., Huang, X., Yan, L., Zhou, L., Chang, Y., Wu, J., Su, Z., & Huang, Y. (2021) · The Protein Journal · doi:10.1007/s10930-021-10017-6 · Cited by 26 · see citing works

Sirtuins as Modifiers of Huntington's Disease (HD) Pathology

Neo, S. H., & Tang, B. L. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.11.013 · Cited by 24 · see citing works

Modulation of Tau Pathology in Alzheimer’s Disease by Dietary Bioactive Compounds

Shi, H., & Zhao, Y. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020831 · Cited by 24 · see citing works

Pan-HDAC Inhibitors Promote Tau Aggregation by Increasing the Level of Acetylated Tau

Jeong, H., Shin, S., Lee, J., Lee, S. H., Baik, J., Lim, S., & Kim, Y. K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20174283 · Cited by 22 · see citing works

Directed evolution of a picomolar-affinity, high-specificity antibody targeting phosphorylated tau

Li, D., Wang, L., Maziuk, B. F., Yao, X., Wolozin, B. L., & Cho, Y. K. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003557 · Cited by 21 · see citing works

Rhythms in barriers and fluids: Circadian clock regulation in the aging neurovascular unit

Skapetze, L., Owino, S., Lo, E. H., Arai, K., Merrow, M. W., & Harrington, M. E. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106120 · Cited by 20 · see citing works

Unraveling the Influence of K280 Acetylation on the Conformational Features of Tau Core Fragment: A Molecular Dynamics Simulation Study

Zou, Y. F., & Guan, L. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.801577 · Cited by 19 · see citing works

Conserved Lysine Acetylation within the Microtubule-Binding Domain Regulates MAP2/Tau Family Members

Hwang, A. W., Trzeciakiewicz, H., Friedmann, D., Yuan, C., Marmorstein, R., Lee, V. M. ‐., & Cohen, T. J. (2016) · PLoS ONE · doi:10.1371/journal.pone.0168913 · Cited by 18 · see citing works

Acetylation and phosphorylation processes modulate Tau’s binding to microtubules: A molecular dynamics study

Castro, T. G., Ferreira, T., Matamá, T., Munteanu, F., & Cavaco-Paulo, A. M. (2022) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2022.130276 · Cited by 18 · see citing works

Untangling Tau: Molecular Insights into Neuroinflammation, Pathophysiology, and Emerging Immunotherapies

Davidson, R., Krider, R. I., Borsellino, P., Noorda, K., Alhwayek, G., & Vida, T. A. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45110553 · Cited by 17 · see citing works

Molecular Insights into the Differential Effects of Acetylation on the Aggregation of Tau Microtubule-Binding Repeats

Zou, Y. F., Guan, L., Tan, J., Qi, B., Sun, Y., Huang, F., & Zhang, Q. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c01929 · Cited by 16 · see citing works

Intrinsic Origin of Tau Protein Aggregation: Effects of Histidine Tautomerism on Tau267–312 Monomer

Chatterjee, S., Salimi, A., & Lee, J. Y. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00587 · Cited by 16 · see citing works

Palmitic Acid Induces Posttranslational Modifications of Tau Protein in Alzheimer’s Disease–Related Epitopes and Increases Intraneuronal Tau Levels

García-Cruz, V. M., & Arias, C. (2024) · Molecular Neurobiology · doi:10.1007/s12035-023-03886-8 · Cited by 14 · see citing works

Experimental Disease-Modifying Agents for Frontotemporal Lobar Degeneration

Giunta, M., Solje, E., Gardoni, F., Borroni, B., & Benussi, A. (2021) · Journal of Experimental Pharmacology · doi:10.2147/jep.s262352 · Cited by 14 · see citing works

Aging-Related Tau Astrogliopathy in Aging and Neurodegeneration

McCann, H., Durand, B., & Shepherd, C. E. (2021) · Brain Sciences · doi:10.3390/brainsci11070927 · Cited by 14 · see citing works

Therapeutic strategies for tauopathies and drug repurposing as a potential approach

Islam, M., Shen, F., Regmi, D., & Du, D. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.114979 · Cited by 14 · see citing works

Proteomic Profiling of Cranial (Superior) Cervical Ganglia Reveals Beta-Amyloid and Ubiquitin Proteasome System Perturbations in an Equine Multiple System Neuropathy

McGorum, B. C., Pirie, R. S., Eaton, S. L., Keen, J., Cumyn, E. M., Arnott, D. M., Chen, W., Lamont, D. J., Graham, L. C., Hurtado, M. L., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.054635 · Cited by 14 · see citing works

The unique neuropathological vulnerability of the human brain to aging

Ferrer, I. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101916 · Cited by 14 · see citing works

The hidden players: Shedding light on the significance of post-translational modifications and miRNAs in Alzheimer's disease development

Singh, R. J., Hussain, J., Kaur, A., Jamdare, B. G., Pathak, D., Garg, K., Kaur, R., Shankar, S., & Sunkaria, A. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102002 · Cited by 13 · see citing works

A small‐molecule microtubule‐stabilizing agent safely reduces Aβ plaque and tau pathology in transgenic mouse models of Alzheimer's disease

Yao, Y., Muench, M., Alle, T., Zhang, B., Lucero, B., Perez‐Tremble, R., McGrosso, D., Newman, M., Gonzalez, D. J., Lee, V. M. ‐., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13875 · Cited by 12 · see citing works

Oligodendrocyte Dysfunction in Tauopathy: A Less Explored Area in Tau-Mediated Neurodegeneration

Majumder, M., & Dutta, D. (2024) · Cells · doi:10.3390/cells13131112 · Cited by 13 · see citing works

Acetylation of Aβ 40 Alters Aggregation in the Presence and Absence of Lipid Membranes

Pilkington, A. W., Schupp, J. E., Nyman, M., Valentine, S. J., Smith, D. M., & Legleiter, J. A. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00483 · Cited by 12 · see citing works

Histological assessment of β‐amyloid precursor protein immunolabelled rectal biopsies aids diagnosis of equine grass sickness

Jago, R. C., Scholes, S. F. E., Mair, T. S., Pearson, G. R., Pirie, R. S., Handel, I. G., Milne, E., Coyle, F., & McGorum, B. C. (2017) · Equine Veterinary Journal · doi:10.1111/evj.12710 · Cited by 11 · see citing works

Identification of Aggregation Mechanism of Acetylated PHF6* and PHF6 Tau Peptides Based on Molecular Dynamics Simulations and Markov State Modeling

Shah, S. J. A., Zhang, Q., Guo, J., Liu, H., Liu, H., & Villà­-Freixa, J. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00578 · Cited by 10 · see citing works

Re-Arranging the Puzzle between the Amyloid-Beta and Tau Pathology: An APP-Centric Approach

Haut, F., Argyrousi, E. K., & Arancio, O. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010259 · Cited by 11 · see citing works

Targeting tau in Alzheimer’s Disease: rationale, approach and challenges

Aslanyan, A., Foiani, M. S., Giovannucci, T. A., McDade, E., Duff, K., Mummery, C. J., Schöll, M., Wildsmith, K. R., & Paterson, R. W. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00925-5 · Cited by 10 · see citing works

Decoding tau acetylation in Alzheimer’s disease and tauopathies: from site-specific mechanisms to therapeutic horizons

Oh, Y. R., & Shin, M. (2025) · BMB Reports · doi:10.5483/bmbrep.2025-0077 · Cited by 9 · see citing works

Histone Deacetylation in Alzheimer’s Diseases (AD); Hope or Hype

Ateya, N. H., Al-Taie, S., Jasim, S., Uthirapathy, S., Chaudhary, K., Rani, P., Kundlas, M., Naidu, K., Amer, N. A. A., & Ahmed, J. K. (2025) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-025-01670-0 · Cited by 5 · see citing works

Role of tau in non-familial dementia

Wilhelmsen, K. C., Geschwind, D. H., Clark, L. N., Sobrido, M. J., Heyn, S. N., Kloeckener‐Gruissem, B., Feiger, J., & Miller, B. L. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)83231-5

Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies

Irwin, D. J., Cohen, T. J., Grossman, M., Arnold, S. E., Xie, S. X., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Brain · doi:10.1093/brain/aws013 · Cited by 281 · see citing works

Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation

Grinberg, L. T., Wang, X., Wang, C., Sohn, P., Theofilas, P., Sidhu, M., Arevalo, J. B., Heinsen, H., Huang, E. J., Rosen, H. J., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1080-2 · Cited by 107 · see citing works

The acetylation of tau inhibits its function and promotes pathological tau aggregation

Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., Trojanowski, J. Q., & Lee, V. M. Y. (2011) · Nature Communications · doi:10.1038/ncomms1255 · Cited by 724 · see citing works

Role of Tau Acetylation in Alzheimer’s Disease and Chronic Traumatic Encephalopathy: The Way Forward for Successful Treatment

Lucke-Wold, B., Seidel, K., Udo, R., Omalu, B., Ornstein, M., Nolan, R. L., Rosen, C., & Ross, J. (2017) · Journal of Neurology and Neurosurgery · doi:10.19104/jnn.2017.40 · Cited by 49 · see citing works