An HDAC6-dependent surveillance mechanism suppresses tau-mediated neurodegeneration and cognitive decline

Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation

Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530 · see citing works

HDAC6 is a microtubule-associated deacetylase

Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403 · see citing works

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 · see citing works

The Deacetylase HDAC6 Regulates Aggresome Formation and Cell Viability in Response to Misfolded Protein Stress

Kawaguchi, Y., Kovacs, J. J., McLaurin, A. C., Vance, J. M., Ito, A., & Yao, T. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,529 · see citing works

HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS.

Pandey, U. B., Nie, Z., Batlevi, Y., McCray, B. A., Ritson, G. P., Nedelsky, N. B., Schwartz, S. L., DiProspero, N. A., Knight, M. A., Schuldiner, O., et al. (2007) · Nature · doi:10.1038/nature05853 · Cited by 1,234 · see citing works

HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor

Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153 · see citing works

Assembly of τ protein into Alzheimer paired helical filaments depends on a local sequence motif ( ³⁰⁶ VQIVYK ³¹¹ ) forming β structure

von Bergen, M., Friedhoff, P., Biernat, J., Heberle, J., Mandelkow, E.-M., & Mandelkow, E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.10.5129 · Cited by 1,021 · 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

HDAC6 Modulates Cell Motility by Altering the Acetylation Level of Cortactin

Zhang, X. M., Yuan, Z., Zhang, Y., Yong, S., Salas-Burgos, A., Koomen, J. M., Olashaw, N., Parsons, J. T., Yang, X., Dent, S., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.033 · Cited by 731 · 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

Mice Lacking Histone Deacetylase 6 Have Hyperacetylated Tubulin but Are Viable and Develop Normally

Zhang, Y., Kwon, S., Yamaguchi, T., Cubizolles, F., Rousseaux, S., Kneissel, M., Cao, C., Li, N., Cheng, H.-L., Chua, K., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01154-06 · Cited by 559 · see citing works

Disease-causing mutations in Parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy

Lee, J., Nagano, Y., Taylor, J. P., Lim, K. L., & Yao, T. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201001039 · Cited by 517 · 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 post-translational modifications in wild-type and human amyloid precursor protein transgenic mice

Morris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472 · see citing works

HDAC and HDAC Inhibitor: From Cancer to Cardiovascular Diseases

Yoon, S., & Eom, G. H. (2016) · Chonnam Medical Journal · doi:10.4068/cmj.2016.52.1.1 · Cited by 469 · see citing works

Tau prion strains dictate patterns of cell pathology, progression rate, and regional vulnerability in vivo

Kaufman, S. K., Sanders, D. W., Thomas, T. L., Ruchinskas, A. J., Vaquer-Alicea, J., Sharma, A. M., Miller, T. M., & Diamond, M. I. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.055 · Cited by 450 · see citing works

HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1–induced Charcot-Marie-Tooth disease

d’Ydewalle, C. V. O., Krishnan, J., Chiheb, D., Damme, P. V., Irobi, J., Kozikowski, A. P., Berghe, P. V., Timmerman, V., Robberecht, W., & Bosch, L. V. D. (2011) · Nature Medicine · doi:10.1038/nm.2396 · Cited by 448 · see citing works

Unique pathological tau conformers from Alzheimer’s brains transmit tau pathology in nontransgenic mice

Guo, J. L., Narasimhan, S., Changolkar, L., He, Z., Stieber, A., Zhang, B., Gathagan, R. J., Iba, M., McBride, J. D., Trojanowski, J. Q., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20160833 · Cited by 440 · see citing works

An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function

Scroggins, B. T., Robzyk, K., Wang, D., Marcu, M. G., Tsutsumi, S., Beebe, K., Cotter, R. J., Felts, S., Toft, D., Karnitz, L., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.008 · Cited by 413 · see citing works

Pathological Tau Strains from Human Brains Recapitulate the Diversity of Tauopathies in Nontransgenic Mouse Brain

Narasimhan, S., Guo, J. L., Changolkar, L., Stieber, A., McBride, J. D., Silva, L. V., He, Z., Zhang, B., Gathagan, R. J., Trojanowski, J. Q., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.1230-17.2017 · Cited by 374 · see citing works

HDAC6 inhibition reverses axonal transport defects in motor neurons derived from FUS-ALS patients

Guo, W., Naujock, M., Fumagalli, L., Vandoorne, T., Baatsen, P., Boon, R., Ordovás, L., Patel, A., Welters, M., Vanwelden, T., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00911-y · Cited by 373 · see citing works

HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregatesPreprint

Boyault, C., Zhang, Y., Fritah, S., Caron, C., Gilquin, B., Kwon, S. H., Garrido, C., Yao, T., Vourc’h, C., Matthias, P., et al. (2007) · Genes & Development · doi:10.1101/gad.436407 · Cited by 370 · see citing works

Reducing HDAC6 ameliorates cognitive deficits in a mouse model for Alzheimer's disease

Govindarajan, N., Rao, P., Burkhardt, S., Sananbenesi, F., Schlüter, O. M., Bradke, F., Lu, J., & Fischer, A. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201201923 · Cited by 346 · see citing works

Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance

Cook, C. N., Carlomagno, Y., Gendron, T. F., Dunmore, J. H., Scheffel, K., Stetler, C. T., Davis, M., Dickson, D. W., Jarpe, M. B., Deture, M. A., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt402 · Cited by 309 · see citing works

Acetylation of intrinsically disordered regions regulates phase separation

Saito, M., Heß, D., Eglinger, J., Fritsch, A. W., Kreysing, M., Weinert, B. T., Choudhary, C., & Matthias, P. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0180-7 · Cited by 300 · 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

Histone Deacetylase 6 Regulates Growth Factor-Induced Actin Remodeling and Endocytosis

Gao, Y., Hubbert, C. C., Lu, J., Lee, Y.-S., Lee, J., & Yao, T. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00393-07 · Cited by 209 · see citing works

Recognition of the minimal epitope of monoclonal antibody Tau‐1 depends upon the presence of a phosphate group but not its location

Szendrei, G., Lee, V. M. Y., & Otvos, L. (1993) · Journal of Neuroscience Research · doi:10.1002/jnr.490340212 · Cited by 204 · see citing works

Tubastatin A/ACY-1215 Improves Cognition in Alzheimer's Disease Transgenic Mice

Zhang, L., Liu, C., Wu, J., Tao, J.-J., Sui, X., Yao, Z., Xu, Y., Huang, L., Zhu, H., Sheng, S., et al. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140066 · Cited by 193 · see citing works

Acetylated tau destabilizes the cytoskeleton in the axon initial segment and is mislocalized to the somatodendritic compartment

Sohn, P. D., Tracy, T. E., Son, H.-I., Zhou, Y., Leite, R. E. P., Miller, B. L., Seeley, W. W., Grinberg, L. T., & Gan, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0109-0 · Cited by 160 · see citing works

Recent advances in the discovery of potent and selective HDAC6 inhibitors

Wang, X.-X., Wan, R.-Z., & Liu, Z.-P. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.10.040 · Cited by 152 · 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

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

Distinct differences in prion-like seeding and aggregation between Tau protein variants provide mechanistic insights into tauopathies

Strang, K. H., Croft, C. L., Sorrentino, Z. A., Chakrabarty, P., Golde, T. E., & Giasson, B. I. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.815357 · Cited by 144 · see citing works

An acetylation–phosphorylation switch that regulates tau aggregation propensity and function

Carlomagno, Y., Chung, D.-E. C., Yue, M., Castanedes-Casey, M., Madden, B. J., Dunmore, J., Tong, J., DeTure, M., Dickson, D. W., Petrucelli, L., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.794602 · Cited by 143 · see citing works

Histone deacetylase 6 inhibition improves memory and reduces total tau levels in a mouse model of tau deposition

Selenica, M. B., Benner, L., Housley, S. B., Manchec, B., Lee, D. C., Nash, K. R., Kalin, J. H., Bergman, J. A., Kozikowski, A. P., Gordon, M. N., et al. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt241 · Cited by 142 · see citing works

Nucleation-dependent Tau Filament Formation

Congdon, E. E., Kim, S., Bonchak, J., Songrug, T., Anastasios Matzavinos, A., & Kuret, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800247200 · Cited by 126 · see citing works

Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease

Jicha, G. A., Berenfeld, B., & Davies, P. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19990315)55:6 · Cited by 123 · see citing works

Defective axonal transport: A common pathological mechanism in inherited and acquired peripheral neuropathies

Prior, R. C., Helleputte, L. V., Benoy, V., & Bosch, L. V. D. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.02.009 · Cited by 118 · see citing works

Imbalance of Hsp70 family variants fosters tau accumulation

Jinwal, U. K., Akoury, E., Abisambra, J. F., O’Leary, J. C., Thompson, A. D., Blair, L. J., Jin, Y., Bacon, J. A., Nordhues, B. A., Cockman, M. E., et al. (2012) · The FASEB Journal · doi:10.1096/fj.12-220889 · Cited by 117 · see citing works

HDAC6 is a therapeutic target in mutant GARS-induced Charcot-Marie-Tooth disease

Benoy, V., Helleputte, L. V., Prior, R. C., d’Ydewalle, C. V. O., Haeck, W., Geens, N., Scheveneels, W., Schevenels, B., Cader, M. Z., Talbot, K., et al. (2017) · Brain · doi:10.1093/brain/awx375 · Cited by 116 · see citing works

HDAC6 Inhibitor Blocks Amyloid Beta-Induced Impairment of Mitochondrial Transport in Hippocampal Neurons

Kim, C., Choi, H., Jung, E. S., Lee, W., Oh, S., Jeon, N. L., & Mook‐Jung, I. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042983 · Cited by 115 · 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 110 · 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

HDAC inhibitors: A new promising drug class in anti-aging research

Pasyukova, E. G., & Vaiserman, A. M. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.08.008 · Cited by 99 · see citing works

Two motifs within the tau microtubule‐binding domain mediate its association with the hsc70 molecular chaperone

Sarkar, M., Kuret, J., & Lee, G. S. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21721 · Cited by 96 · 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

The Deacetylase HDAC6 Mediates Endogenous Neuritic Tau Pathology

Tseng, J.-H., Xie, L., Song, S., Xie, Y., Allen, L., Ajit, D., Hong, J.-S., Chen, X., Meeker, R. B., & Cohen, T. J. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.082 · Cited by 93 · see citing works

Impaired Function of HDAC6 Slows Down Axonal Growth and Interferes with Axon Initial Segment Development

Tapia, M., Wandosell, F. G., & Garrido, J. J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012908 · Cited by 92 · see citing works

Histone Deacetylase Inhibitors: New Promise in the Treatment of Immune and Inflammatory Diseases

Shuttleworth, S. J., Bailey, S. G., & Townsend, P. A. (2010) · Current Drug Targets · doi:10.2174/1389450111009011430 · Cited by 88 · see citing works

TOC1: Characterization of a Selective Oligomeric Tau Antibody

Ward, S., Himmelstein, D. S., Lancia, J. K., Fu, Y., Patterson, K. R., & Binder, L. I. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-131235 · Cited by 77 · see citing works

HDAC6 inhibition results in tau acetylation and modulates tau phosphorylation and degradation in oligodendrocytes

Noack, M., Leyk, J., & Richter‐Landsberg, C. (2014) · Glia · doi:10.1002/glia.22624 · Cited by 77 · see citing works

HDAC6 and RhoA are novel players in Abeta-driven disruption of neuronal polarity

Tsushima, H., Emanuele, M., Polenghi, A., Esposito, A., Vassalli, M., Barberis, A., Difato, F., & Chieregatti, E. (2015) · Nature Communications · doi:10.1038/ncomms8781 · Cited by 71 · see citing works

Proteomic identification and functional characterization of MYH9, Hsc70, and DNAJA1 as novel substrates of HDAC6 deacetylase activity

Zhang, L., Liu, S., Liu, N., Zhang, Y., Liu, M., Li, D., Seto, E., Yao, T., Shui, W., & Zhou, J. (2014) · Protein & Cell · doi:10.1007/s13238-014-0102-8 · Cited by 66 · see citing works

rAAV-based brain slice culture models of Alzheimer’s and Parkinson’s disease inclusion pathologies

Croft, C. L., Cruz, P. E., Ryu, D. H., Ceballos‐Diaz, C., Strang, K. H., Woody, B. M., Lin, W.-L., Deture, M. A., Rodríguez-Lebrón, E., Dickson, D. W., et al. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20182184 · Cited by 64 · see citing works

Combining P301L and S320F tau variants produces a novel accelerated model of tauopathy

Koller, E. J., Gonzalez De La Cruz, E., Machula, T., Ibanez, K. R., Lin, W.-L., Williams, T., Riffe, C. J., Ryu, D., Strang, K. H., Liu, X., et al. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz151 · Cited by 63 · see citing works

iPSC-derived neurons profiling reveals GABAergic circuit disruption and acetylated α-tubulin defect which improves after iHDAC6 treatment in Rett syndrome

Landucci, E., Brindisi, M., Bianciardi, L., Catania, L. M., Daga, S., Croci, S., Frullanti, E., Fallerini, C., Butini, S., Brogi, S., et al. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.05.001 · Cited by 56 · see citing works

Different immunoreactivities of the microtubule-binding region of tau and its molecular basis in brains from patients with Alzheimer's disease, Pick's disease, progressive supranuclear palsy and corticobasal degeneration

Arai, T., Ikeda, K., Akiyama, H., Tsuchiya, K., Iritani, S., Ishiguro, K., Yagishita, S., Oda, T., Odawara, T., & Iseki, E. (2003) · Acta Neuropathologica · doi:10.1007/s00401-003-0671-8 · Cited by 54 · see citing works

Inhibition of HDAC6 Modifies Tau Inclusion Body Formation and Impairs Autophagic Clearance

Leyk, J., Goldbaum, O., Noack, M., & Richter‐Landsberg, C. (2014) · Journal of Molecular Neuroscience · doi:10.1007/s12031-014-0460-y · Cited by 49 · see citing works

The role of histone deacetylase 6 in synaptic plasticity and memory

Perry, S., Kiragasi, B., Dickman, D., & Ray, A. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.01.028 · Cited by 49 · 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

Dopaminergic abnormalities in Hdac6-deficient mice

Fukada, M., Nakayama, A., Mamiya, T., Yao, T., & Kawaguchi, Y. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.08.018 · Cited by 17 · see citing works

Untitled work

(1997) · doi:10.1002/(sici)1097-4547(19970415)48:2

Brain-Derived Neurotrophic Factor in Alzheimer’s Disease and Its Pharmaceutical Potential

Gao, L., Zhang, Y., Sterling, K., & Song, W. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00279-0 · Cited by 606 · see citing works

Neuroinflammation in Alzheimer disease

Heneka, M. T., van der Flier, W. M., Jessen, F., Hoozemanns, J., Thal, D. R., Boche, D., Brosseron, F., Teunissen, C., Zetterberg, H., Jacobs, A. H., et al. (2025) · Nature Reviews Immunology · doi:10.1038/s41577-024-01104-7 · Cited by 638 · 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

Protein acylation: mechanisms, biological functions and therapeutic targets

Shang, S., Liu, J., & Hua, F. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01245-y · Cited by 247 · see citing works

Updates in Alzheimer's disease: from basic research to diagnosis and therapies

Liu, E., Zhang, Y., & Wang, J. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00432-x · Cited by 220 · see citing works

X-linked ubiquitin-specific peptidase 11 increases tauopathy vulnerability in women

Yan, Y., Wang, X., Chaput, D., Shin, M.-K., Koh, Y., Gan, L., Pieper, A. A., Woo, J.-A. A., & Kang, D. E. (2022) · Cell · doi:10.1016/j.cell.2022.09.002 · Cited by 144 · see citing works

Neurodegenerative Disease Tauopathies

Creekmore, B. C., Watanabe, R., & Lee, E. B. (2023) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-051222-120750 · Cited by 144 · see citing works

Disruption of axonal transport in neurodegeneration

Berth, S. H., & Lloyd, T. E. (2023) · Journal of Clinical Investigation · doi:10.1172/jci168554 · Cited by 126 · see citing works

Role of Histone Post-Translational Modifications in Inflammatory Diseases

Lin, Y., Qiu, T., Wei, G., Que, Y., Wang, W., Kong, Y., Xie, T., & Chen, X. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.852272 · Cited by 95 · see citing works

Protein interaction networks in neurodegenerative diseases: From physiological function to aggregation

Calabrese, G., Molzahn, C. M., & Mayor, T. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102062 · Cited by 90 · see citing works

Combining histone deacetylase inhibitors (HDACis) with other therapies for cancer therapy

Zhou, M., Yuan, M., Zhang, M., Lei, C., Aras, O., Zhang, X., & An, F. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113825 · Cited by 92 · see citing works

Inhibition of Histone Deacetylase 6 (HDAC6) as a therapeutic strategy for Alzheimer's disease: A review (2010–2020)

Li, Y., Sang, S., Ren, W., Pei, Y., Bian, Y., Chen, Y., & Sun, H. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113874 · Cited by 77 · see citing works

Targeting tau in Alzheimer's disease: from mechanisms to clinical therapy

Ye, J., Wan, H., Chen, S., & Liu, G. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.385847 · Cited by 69 · see citing works

Microtubule acetylation dyshomeostasis in Parkinson’s disease

Naren, P., Khan, S. S., Tryphena, K. P., Vora, L. K., Srivastava, S., Singh, S. B., & Khatri, D. K. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00354-0 · Cited by 63 · see citing works

Multiancestry analysis of the HLA locus in Alzheimer’s and Parkinson’s diseases uncovers a shared adaptive immune response mediated by HLA-DRB1*04 subtypes

Guen, Y. L., Luo, G., Ambati, A., Damotte, V., Jansen, I. E., Yu, E., Nicolas, A., de Rojas, I., Leal, T. P., Miyashita, A., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2302720120 · Cited by 56 · see citing works

Protopine promotes the proteasomal degradation of pathological tau in Alzheimer's disease models via HDAC6 inhibition

Sreenivasmurthy, S. G., Iyaswamy, A., Krishnamoorthi, S., Senapati, S., Malampati, S., Zhu, Z., Su, C.-F., Liu, J., Guan, X.-J., Tong, B. C., et al. (2021) · Phytomedicine · doi:10.1016/j.phymed.2021.153887 · Cited by 57 · see citing works

New insights into the non-enzymatic function of HDAC6

Zhu, Y.-Z., Feng, M., Wang, B., Zheng, Y., Jiang, D., Zhao, L., Mamun, M., Kang, H., Nie, H., Zhang, X., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114438 · Cited by 55 · see citing works

Development of a potential PET probe for HDAC6 imaging in Alzheimer's disease

Bai, P., Mondal, P., Bagdasarian, F. A., Rani, N., Liu, Y., Gomm, A., Tocci, D. R., Choi, S. H., Wey, H., Tanzi, R. E., et al. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.05.017 · Cited by 50 · see citing works

Histone deacetylase-6 modulates Tau function in Alzheimer's disease

Qureshi, T., & Chinnathambi, S. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119275 · Cited by 49 · 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

Small molecules targeting HDAC6 for cancer treatment: Current progress and novel strategies

Huang, Z., Li, L., Cheng, B., & Li, D. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117218 · Cited by 45 · see citing works

Structure‐Based Discovery of A Small Molecule Inhibitor of Histone Deacetylase 6 (HDAC6) that Significantly Reduces Alzheimer's Disease Neuropathology

Mondal, P., Bai, P., Gomm, A., Bakiasi, G., Lin, C., Wang, Y., Choi, S. H., Tanzi, R. E., Wang, C., & Zhang, C. M. (2023) · Advanced Science · doi:10.1002/advs.202304545 · Cited by 42 · see citing works

Histone deacetylase inhibitors VPA and WT161 ameliorate the pathological features and cognitive impairments of the APP/PS1 Alzheimer’s disease mouse model by regulating the expression of APP secretases

Zhang, M., Wang, W., Ye, Q., Fu, Y., Li, X., Yang, K., Gao, F., Zhou, A., Wei, Y., Tian, S., et al. (2024) · Alzheimer s Research & Therapy · doi:10.1186/s13195-024-01384-0 · Cited by 41 · see citing works

Recent development of selective inhibitors targeting the HDAC6 as anti-cancer drugs: Structure, function and design

Peng, J., Xie, F., Qin, P., Liu, Y., Niu, H., Sun, J., Xue, H., Zhao, Q., Liu, J., & Wu, J. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.106622 · Cited by 36 · see citing works

HDAC6 Inhibition Alleviates Ischemia- and Cisplatin-Induced Acute Kidney Injury by Promoting Autophagy

Shi, L., Song, Z., Li, C., Deng, F., Xia, Y., Huang, J., Wu, X., & Zhu, J. (2022) · Cells · doi:10.3390/cells11243951 · Cited by 35 · see citing works

DUBs in Alzheimer’s disease: mechanisms and therapeutic implications

Qin, B., Chen, X., Wang, F., & Wang, Y. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-02237-3 · Cited by 33 · see citing works

Dual Targeting Strategies on Histone Deacetylase 6 (HDAC6) and Heat Shock Protein 90 (Hsp90)

Bonanni, D., Citarella, A., Moi, D., Pinzi, L., Bergamini, E., & Rastelli, G. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867328666210902145102 · Cited by 33 · see citing works

Zinc-dependent deacetylases (HDACs) as potential targets for treating Alzheimer’s disease

Li, Y., Lin, S., Gu, Z., Chen, L., & He, B. (2022) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2022.129015 · Cited by 33 · see citing works

Tubulin Cytoskeleton in Neurodegenerative Diseases–not Only Primary Tubulinopathies

Cyske, Z., Gaffke, L., Pierzynowska, K., & Węgrzyn, G. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01304-6 · Cited by 32 · see citing works

Similarities and Differences in the Pattern of Tau Hyperphosphorylation in Physiological and Pathological Conditions: Impacts on the Elaboration of Therapies to Prevent Tau Pathology

Duquette, A., Pernègre, C., Carpentier, A. V., & Leclerc, N. M. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.607680 · 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

Unlocking the Epigenetic Symphony: Histone Acetylation’s Impact on Neurobehavioral Change in Neurodegenerative Disorders

Basavarajappa, B. S., & Subbanna, S. (2024) · Epigenomics · doi:10.2217/epi-2023-0428 · Cited by 24 · see citing works

The Peptide PROTAC Modality: A New Strategy for Drug Discovery

Zhu, Y., Dai, Y., & Tian, Y. (2025) · MedComm · doi:10.1002/mco2.70133 · Cited by 23 · see citing works

Upregulation of ISG15 induced by MAPT/tau accumulation represses autophagic flux by inhibiting HDAC6 activity: a vicious cycle in Alzheimer disease

Liu, Q. R., Wang, X., Fang, Z., Zhao, J.-N., RUI, X., Zhang, B., He, Y., Liu, R., Chen, J., Chai, G., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2431472 · Cited by 20 · see citing works

Cytoplasmic HDAC4 recovers synaptic function in the 3×Tg mouse model of Alzheimer's disease

Colussi, C., Aceto, G., Ripoli, C., Bertozzi, A., Puma, D. D. L., Paccosi, E., D’Ascenzo, M., & Grassi, C. (2022) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12861 · Cited by 19 · see citing works

Activity-dependent tau cleavage by caspase-3 promotes neuronal dysfunction and synaptotoxicity

Opland, C. K., Bryan, M. R., Harris, B., McGillion-Moore, J., Tian, X., Chen, Y., Itano, M. S., Diering, G. H., Meeker, R. B., & Cohen, T. J. (2023) · iScience · doi:10.1016/j.isci.2023.106905 · Cited by 21 · see citing works

A hybrid approach unveils drug repurposing candidates targeting an Alzheimer pathophysiology mechanism

Lage‐Rupprecht, V., Schultz, B. T., Dick, J., Namysł, M., Zaliani, A., Gebel, S., Pleß, O., Reinshagen, J., Ellinger, B., Ebeling, C., et al. (2022) · Patterns · doi:10.1016/j.patter.2021.100433 · Cited by 20 · see citing works

Medicinal chemistry insights into non-hydroxamate HDAC6 selective inhibitors

Faridoon, Zha, Y. L., Zhang, G., & Li, J. J. (2022) · Medicinal Chemistry Research · doi:10.1007/s00044-022-02987-8 · Cited by 19 · see citing works

Design, Synthesis, and Proof of Concept of Balanced Dual Inhibitors of Butyrylcholinesterase (BChE) and Histone Deacetylase 6 (HDAC6) for the Treatment of Alzheimer’s Disease

Wang, L., Sun, T., Wang, Z., Liu, H., Qiu, W., Tang, X., Guo, H., Yang, P., Yao, C., & Sun, H. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00358 · Cited by 19 · see citing works

Comprehensive Analysis of the Differential Expression and Prognostic Value of Histone Deacetylases in Glioma

Li, J., Yan, X., Liang, C., Chen, H., Liu, M., Wu, Z., Zheng, J., Dang, J., La, X., & Liu, Q. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.840759 · Cited by 20 · see citing works

Transactive Response DNA-Binding Protein (TARDBP/TDP-43) Regulates Cell Permissivity to HIV-1 Infection by Acting on HDAC6

Cabrera-Rodríguez, R., Pérez-Yanes, S., González‐Montelongo, R., Lorenzo-Salazar, J. M., Estévez‐Herrera, J., García-Luis, J., Íñigo-Campos, A., Rubio‐Rodríguez, L. A., Muñoz‐Barrera, A., Trujillo‐González, R., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116180 · Cited by 18 · see citing works

HDAC6-specific inhibitor alleviates hashimoto's thyroiditis through inhibition of Th17 cell differentiation

Chang, Q., Yin, D., Li, H., Du, X., Wang, Z., Liu, Y., & Zhang, J. (2022) · Molecular Immunology · doi:10.1016/j.molimm.2022.05.004 · Cited by 17 · see citing works

HDAC6 Inhibition Alleviates Anesthesia and Surgery-Induced Less Medial Prefrontal-Dorsal Hippocampus Connectivity and Cognitive Impairment in Aged Rats

Chen, J., Liu, S., Wang, X., Huang, J., Phillips, J., Ma, D., Ouyang, W., & Tong, J. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02959-4 · Cited by 17 · see citing works

Aromatic Ring Fluorination Patterns Modulate Inhibitory Potency of Fluorophenylhydroxamates Complexed with Histone Deacetylase 6

Watson, P. R., Bai, P., Wang, C., Cragin, A. D., Hooker, J. M., & Christianson, D. W. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00332 · Cited by 15 · see citing works

High levels of HDAC expression correlate with microglial aging

Auzmendi-Iriarte, J., Moreno‐Cugnon, L., Saenz‐Antoñanzas, A., Grassi, D., de Pancorbo, M. M., Arévalo, M., Wood, I. C., & Matheu, A. (2022) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2022.2158081 · Cited by 12 · see citing works

Elaboration of the Effective Multi-Target Therapeutic Platform for the Treatment of Alzheimer’s Disease Based on Novel Monoterpene-Derived Hydroxamic Acids

Aleksandrova, Y. R., Munkuev, A. A., Mozhaitsev, E. S., Суслов, Е. В., Tsypyshev, D. O., Chaprov, K., Бегунов, Р. С., Volcho, K. P., Salakhutdinov, N. F., & Неганова, М. Е. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119743 · Cited by 13 · see citing works

HDAC6-selective inhibitor CAY10603 ameliorates cigarette smoke-induced small airway remodeling by regulating epithelial barrier dysfunction and reversing

Zhang, Q., Yan, L., Ye, L., Liu, X., Yin, Y., Wang, Q., Gu, X., & Zhou, X. (2024) · Respiratory Research · doi:10.1186/s12931-024-02688-3 · Cited by 13 · see citing works

A novel insight into neurological disorders through HDAC6 protein–protein interactions

Sangani, N. B., Koetsier, J., Mélius, J., Kutmon, M., Ehrhart, F., Evelo, C. T., Curfs, L., Reutelingsperger, C. P. M., & Eijssen, L. (2024) · Scientific Reports · doi:10.1038/s41598-024-65094-1 · Cited by 13 · see citing works

LRRK2 kinase-mediated accumulation of lysosome-associated phospho-Rabs in tauopathies and synucleinopathies

Buck, S. A., Malankhanova, T. B., Strader, S., Eileen, B., Yim, S., Pratt, H. W., Ervin, J. F., Lee, E. B., Wang, S. J., Cohen, T. J., et al. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02951-x · Cited by 11 · see citing works

Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons

Saleem, K., Xiao, Z., Zhu, B., Ren, Y., Yan, Z., & Feng, J. (2026) · Molecular Psychiatry · doi:10.1038/s41380-025-03225-4 · Cited by 10 · see citing works

The regulatory mechanisms and treatment of HDAC6 in immune dysregulation diseases

Liang, Y., Wang, Y., Xing, J., Li, J., & Zhang, K. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1653588 · Cited by 10 · see citing works

First in Class Dual Non-ATP-Competitive Glycogen Synthase Kinase 3β/Histone Deacetylase Inhibitors as a Potential Therapeutic to Treat Alzheimer’s Disease

Santini, A., Tassinari, E., Poeta, E., Loi, M., Ciani, E., Trazzi, S., Piccarducci, R., Daniele, S., Martini, C., Pagliarani, B., et al. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00061 · Cited by 10 · see citing works

Pathogenic variants of TUBB8 cause oocyte spindle defects by disrupting with EB1/CAKP5 interactions and potential treatment targeting microtubule acetylation through HDAC6 inhibition

Luo, H., Chen, J., Cao, L., Wu, T., Yin, S., Yang, G., Wang, Y., Guo, Z., Hu, S., He, Y., et al. (2025) · Clinical and Translational Medicine · doi:10.1002/ctm2.70193 · Cited by 10 · see citing works

Effects of chronic kidney disease on cognitive function and α-klotho expression in hippocampus

Huang, M., Li, G., Tan, J., Huang, M., Huang, F., Ma, R., Xiao, Y., & Wang, J. (2022) · Translational Andrology and Urology · doi:10.21037/tau-22-465 · Cited by 10 · see citing works

Emerging Roles of Ubiquitination in Biomolecular Condensates

Liang, P., Zhang, J., & Wang, B. (2023) · Cells · doi:10.3390/cells12182329 · Cited by 11 · see citing works

Biochemical approaches to assess the impact of post-translational modifications on pathogenic tau conformations using recombinant protein

Alhadidy, M. M., & Kanaan, N. M. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230596 · Cited by 9 · see citing works

Histone deacetylase’s regulates Tau function in Alzheimer’s disease

Chinnathambi, S. (2024) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.09.008 · Cited by 9 · see citing works

Epigenome-wide DNA methylation analysis of late-stage mild cognitive impairment

Zhang, Y., & Shen, S. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1276288 · Cited by 9 · see citing works

Development and characterization of novel anti-acetylated tau monoclonal antibodies to probe pathogenic tau species in Alzheimer’s disease

Bryan, M. R., Tian, X., Tseng, J., Evangelista, B., Ragusa, J. V., Bryan, A. F., Trotman, W., Irwin, D. J., & Cohen, T. J. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01865-1 · Cited by 8 · see citing works

Dual inhibitors of butyrylcholinesterase and histone deacetylase 6 for the treatment of Alzheimer’s disease: design, synthesis, and biological evaluation

Lv, B., Wang, Z., Wang, Q., Xu, Z., Tang, J., Pei, Y., Bian, Y., Sun, H., & Chen, Y. (2025) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2025.118219 · Cited by 7 · see citing works

Therapeutic potential of dual HDAC6/SIRT2 inhibition in Alzheimer's disease

Wang, X., Li, C., Chen, L., He, B., & Li, Y. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117733 · Cited by 8 · see citing works

The double‐edged sword effect of HDAC6 in Aβ toxicities

Cheng, K., Hwang, Y., & Chiang, H. (2021) · The FASEB Journal · doi:10.1096/fj.202101061r · Cited by 7 · see citing works

Bombesin receptor-activated protein exacerbates cisplatin-induced AKI by regulating the degradation of SIRT2

Peng, L., Liu, D., Liu, H., Xia, M., Wan, L., Li, M., Zhao, J., Tang, C., Chen, G., Qu, X., et al. (2022) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfac164 · Cited by 7 · see citing works

Histone Deacetylase 6: At the Interface of Cancer and Neurodegeneration

Pu, J., Sharma, A., Hou, J., & Schmidt‐Wolf, I. G. H. (2023) · Epigenomics · doi:10.2217/epi-2023-0373 · Cited by 7 · see citing works

Therapeutic indications for HDAC6 inhibitors in the peripheral and central nervous disorders

van Eyll, J. M., Prior, R. C., Célanire, S., Bosch, L. V. D., & Rombouts, F. J. R. (2024) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2024.2404571 · Cited by 6 · see citing works

Histone Deacetylase Inhibition in Alzheimer’s Disease: Molecular Mechanisms, Therapeutic Potential, and Future Perspectives

Joshi, N., Khadse, P., Jadhav, S., & Alavala, R. R. (2025) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266360664250606110220 · Cited by 6 · see citing works

Acetylation Mimetic and Null Mutations Within the Filament Core of P301L Tau Have Varied Effects on Susceptibility to Seeding and Aggregation

Smith, E. D., Torrellas, J., McKenna, R., Vo, Q., Mietzsch, M., Borchelt, D., Prokop, S., & Chakrabarty, P. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70221 · Cited by 6 · see citing works

Nanozymes - A new opportunity for the treatment of neurodegenerative diseases

Zhou, Y., Zhou, X., Song, Y., Tian, Q., Li, S., Li, T., & Lu, X. F. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.169965 · Cited by 6 · see citing works

An acetylated Tau-174 CSF biomarker discriminates between TDP-43 and tau pathology in patients with frontotemporal lobar degeneration

Honey, M. I. J., Hok‐A‐Hin, Y. S., Thijssen, E. H., Cousins, K. A. Q., van der Weijden, B., Veld, L. I. ‘., Stoops, E., de Boer, S. C. M., Duits, F. H., Houwer, J. F. H. D., et al. (2026) · Nature Medicine · doi:10.1038/s41591-026-04341-6 · Cited by 6 · see citing works

Chemobrain: An accelerated aging process linking adenosine A2A receptor signaling in cancer survivors

Oliveros, A., Poleschuk, M., Cole, P. D., Boison, D., & Jang, M. (2023) · International review of neurobiology · doi:10.1016/bs.irn.2023.08.003 · Cited by 5 · see citing works

From Better Diagnostics to Earlier Treatment: The Rapidly Evolving Alzheimer’s Disease Landscape

Bougea, A. M., Debasa‐Mouce, M., Gulkarov, S., Castro‐Mosquera, M., Reiss, A. B., & Ouro, A. (2025) · Medicina · doi:10.3390/medicina61081462 · Cited by 5 · see citing works

Hippocampal SIRT1 improves cognitive impairment by deacetylating tau protein in diabetic models

Shi, N., Lin, Y., Yan, B., Jiao, X., Ding, X., Wu, Y., & Zhou, C. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174666 · Cited by 5 · see citing works

Evaluating Fatty Acid Amide Hydrolase as a Suitable Target for Sleep Promotion in a Transgenic TauP301S Mouse Model of Neurodegeneration

Martin, S. C., Joyce, K. K., Harper, K. M., Harp, S. J., Cohen, T. J., Moy, S. S., & Diering, G. H. (2024) · Pharmaceuticals · doi:10.3390/ph17030319 · Cited by 5 · see citing works

HDAC6 mediates tumorigenesis during mitosis and the development of targeted deactivating agents

Peng, J., Liu, H., Liu, Y., Liu, J., Zhao, Q., Liu, W., Niu, H., Xue, H., Sun, J., & Wu, J. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107818 · Cited by 5 · see citing works

Zinc exacerbates tau-induced Alzheimer-like pathology in C57BL/6J mice

Li, X., Le, L., Shi, Q., Xu, H., Wang, C., Xiong, Y., Wang, X., Wu, G., Liu, Q., & Du, X. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.124652 · Cited by 5 · see citing works

The degradation of α--synuclein is limited by dynein to drive the AALP pathway through HDAC6 upon paraquat exposure

Ai, Q., Wang, K., Li, Y., Hu, R., Hu, G., Li, Y., Shi, G., & Huang, M. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.116841 · Cited by 4 · see citing works

Advancing histone deacetylase 6 (HDAC6) as a promising therapeutic target for Alzheimer’s disease: from molecular insights to clinical prospects

Zhang, W., Zhang, Y., Wang, Y., Wang, C., & Zhang, C. M. (2025) · Frontiers in Drug Discovery · doi:10.3389/fddsv.2025.1662691 · Cited by 3 · see citing works

Modeling spastic paraplegia 4 with corticospinal motor neuron-enriched cortical organoids reveals genotype-phenotype and HDAC6-targetable pathology

Mohan, N., Ramakrishnan, S., Sun, X., Sun, Y., Connors, T., Chai, V. Z., Piermarini, E., Baas, P. W., Cai, J. J., Liu, M., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117036 · Cited by 3 · see citing works

Bridging protein quality control and epigenetic dysregulation: The HDAC6 paradox in neurological disorders and therapeutic targeting

Chen, Y., Wu, Y., Liu, X., Wan, J., Shen, M., & Zhang, Q. (2026) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2026.178721 · Cited by 3 · see citing works

HDAC6 regulates BACE1 stability and NLRP3 inflammasome activation in Alzheimer's disease

Lee, J., Cho, Y., Choi, B. Y., Kim, H. K., Lee, Y., Kim, E., Han, J., Sul, J. H., Kim, J. S., Baek, S. H., et al. (2026) · Brain · doi:10.1093/brain/awag089 · Cited by 4 · see citing works

Protective association of HLA-DRB1*04 subtypes in neurodegenerative diseases implicates acetylated tau PHF6 sequencesPreprint

Mignot, E. J.-M., Guen, Y. L., Luo, G., Ambati, A., Damotte, V., Jansen, I. E., Yu, E., Nicolas, A., de Rojas, I., Leal, T. P., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1285855/v1 · Cited by 3 · see citing works

Tau protein aggregation: A therapeutic target for neurodegenerative diseases

Duggal, A., Mahindru, D., Baghel, K., Mehrotra, S., & Prajapati, V. K. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2024.11.012 · Cited by 2 · see citing works

AR-A014418-based dual Glycogen Synthase Kinase 3β/Histone Deacetylase inhibitors as potential therapeutics for Alzheimer's disease

Santini, A., Tassinari, E., Altomare, A., Loi, M., Ciani, E., Trazzi, S., Piccarducci, R., Daniele, S., Martini, C., Pagliarani, B., et al. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117838 · Cited by 2 · see citing works

The emerging nontraditional roles for tau in the brain

Tseng, J., & Cohen, T. J. (2023) · Cytoskeleton · doi:10.1002/cm.21811 · Cited by 2 · see citing works

Histone Deacetylase 6 Brain PET in Amyotrophic Lateral Sclerosis‐Frontotemporal Spectrum Disorder

Vanderlinden, G., Carron, C. P., Weehaeghe, D. V., Vocht, J. D., Ombelet, F., Masrori, P., Weerdt, C. D., James, R. E., Evans, L. J., Schroeder, F. A., et al. (2025) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.70067 · Cited by 2 · see citing works

Extracellular HDAC6 ZnF UBP domain enhances podosome-mediated neuronal migrationPreprint

Qureshi, T., Desale, S. E., Sonawane, S. K., Balmik, A. A., Chidambaram, H., & Chinnathambi, S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.04.626746 · Cited by 2 · see citing works

Impact of Lysine Acetylation Mutations on the Structure of Full-Length Tau Fibrils

Dregni, A. J., & Hong, M. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00149 · Cited by 1 · see citing works

Integrative Bioinformatic Characterization of the HDAC6-Driven Cytoskeleton–Wnt Signaling Interface in Hepatocellular Carcinoma: Implications for Immune Modulation and Therapeutic Targeting

Bayram, E., Broggi, G., & Ayan, D. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27125201 · Cited by 1 · see citing works

Transactive response DNA-binding Protein (TDP-43) regulates early HIV-1 entry and infectionPreprint

Cabrera-Rodríguez, R., Pérez-Yanes, S., González‐Montelongo, R., Lorenzo-Salazar, J. M., Estévez‐Herrera, J., García-Luis, J., Íñigo-Campos, A., Rubio‐Rodríguez, L. A., Muñoz‐Barrera, A., Trujillo‐González, R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.06.471424

Additional file 1 of Histone deacetylase inhibitors VPA and WT161 ameliorate the pathological features and cognitive impairments of the APP/PS1 Alzheimer’s disease mouse model by regulating the expression of APP secretases

Zhang, M., Wang, W., Ye, Q., Fu, Y., Li, X., Yang, K., Gao, F., Zhou, A., Wei, Y., Tian, S., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25036293

Ar-A014418-Based Dual Glycogen Synthase Kinase 3β / Histone Deacetylases Inhibitors as Potential Therapeutics for Alzheimer's DiseasePreprint

Santini, A., Tassinari, E., Altomare, A., Loi, M., Ciani, E., Trazzi, S., Piccarducci, R., Daniele, S., Martini, C., Pagliarani, B., et al. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5212874

Genotype–Phenotype Distinctions in Spastic Paraplegia 4 Reveal HDAC6 as a Therapeutic TargetPreprint

Mohan, N., Ramakrishnan, S., Sun, X., Sun, Y., Connors, T. M., Chai, V. Z., Piermarini, E., Baas, P. W., Cai, J. J., Liu, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.15.664947

Dual mechanism of autophagy gene repression by PHF23 and therapeutic potential of its inhibition in protein aggregation disorders

Choi, S. A., Kim, J., Yu, Y. S., Kim, J., Kim, S. I., Bae, H., Kwon, J., Kim, K. I., & Baek, S. H. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1317

Additional file 1 of HDAC6-selective inhibitor CAY10603 ameliorates cigarette smoke-induced small airway remodeling by regulating epithelial barrier dysfunction and reversing

Zhang, Q., Yan, L., Lu, Y., Liu, X., Yin, Y., Wang, Q., Gu, X., & Zhou, X. (2024) · Figshare · doi:10.6084/m9.figshare.25150620

Synergistic MAPT mutations as a platform to uncover modifiers of tau pathogenesisPreprint

Bryan, M. R., Almeida, M. F., Pellegrino, K., Opland, C. K., Paulakonis, J. E., McGillion-Moore, J., Trzeciakiewicz, H., King, D. P., Tian, X., Tseng, J., et al. (2025) · eLife · doi:10.7554/elife.109145

Synergistic MAPT mutations as a platform to uncover modifiers of tau pathogenesisPreprint

Bryan, M. R., Almeida, M. F., Pellegrino, K., Opland, C. K., Paulakonis, J. E., McGillion-Moore, J., Trzeciakiewicz, H., King, D. P., Tian, X., Tseng, J., et al. (2025) · eLife · doi:10.7554/elife.109145.1

Serotonergic psychedelics as epigenetic modulators: A paradigm shift in Alzheimer's disease therapeutics

Gojani, E. G., Farzin, H., Sutherland, R. J., & Mohajerani, M. H. (2026) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2026.106619

TARDBP as a regulator of HIV-1 assembly and infection: a review of targeting the viral capsid precursor Pr55Gag and limiting viral core entry

Cabrera-Rodríguez, R., Pons-Grífols, A., Pernas, M., Casado, C., Trujillo‐González, R., Lorenzo-Sánchez, I., Reyes-Castañeda, I., Trinité, B., Blanco, J., & Valenzuela-Fernández, A. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02762-x

Early proteomic signatures of Alzheimer’s disease in the retina and brain of 3xTg-AD mice

Puja, A., McNeel, R., Xu, R., Zhu, S., Hansman, D., & Du, J. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1827348

THE REGULATION OF TAU PATHOGENESIS IN NEURODEGENERATION

Trzeciakiewicz, H. (2020) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/xwcc-h138

Acetylation: a new key to unlock tau’s role in neurodegeneration

Cook, C. N., Stankowski, J. N., Carlomagno, Y., Stetler, C. T., & Petrucelli, L. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt259 · Cited by 133 · see citing works

Histone deacetylase 6 interacts with the microtubule‐associated protein tau

Ding, H., Dolan, P. J., & Johnson, G. V. W. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05564.x · Cited by 387 · see citing works

Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation

Cook, C. N., Gendron, T. F., Scheffel, K., Carlomagno, Y., Dunmore, J. H., Deture, M. A., & Petrucelli, L. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds125 · Cited by 129 · see citing works

Histone deacetylase-6 modulates Tau function in Alzheimer's disease

Qureshi, T., & Chinnathambi, S. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119275 · Cited by 49 · see citing works