Cited by 75Histone Deacetylase Inhibitors ResearchAlzheimer's disease research and treatmentsGenetic Neurodegenerative Diseases

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The role of altered protein acetylation in neurodegenerative disease

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Kabir, Fariha, Atkinson, Rachel, Cook, Anthony L., Phipps, Andrew James, King, Anna Elizabeth·2023·Frontiers in Aging Neuroscience

DOI 10.3389/fnagi.2022.1025473PMC PMC9845957

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Abstract

Acetylation is a key post-translational modification (PTM) involved in the regulation of both histone and non-histone proteins. It controls cellular processes such as DNA transcription, RNA modifications, proteostasis, aging, autophagy, regulation of cytoskeletal structures, and metabolism. Acetylation is essential to maintain neuronal plasticity and therefore essential for memory and learning. Homeostasis of acetylation is maintained through the activities of histone acetyltransferases (HAT) and histone deacetylase (HDAC) enzymes, with alterations to these tightly regulated processes reported in several neurodegenerative diseases including Alzheimer’s disease (AD), Parkinson’s disease (PD), Huntington’s disease (HD), and amyotrophic lateral sclerosis (ALS). Both hyperacetylation and hypoacetylation can impair neuronal physiological homeostasis and increase the accumulation of pathophysiological proteins such as tau, α-synuclein, and Huntingtin protein implicated in AD, PD, and HD, respectively. Additionally, dysregulation of acetylation is linked to impaired axonal transport, a key pathological mechanism in ALS. This review article will discuss the physiological roles of protein acetylation and examine the current literature that describes altered protein acetylation in neurodegenerative disorders.

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Items 201–324 of 324

Microtubule destabilization and nuclear entry are sequential steps leading to toxicity in Huntington's disease
Trushina, E. V., Heldebrant, M. P., Pérez-Terzic, C. M., Bortolon, R., Kovtun, I. V., Badger, J. D., Terzic, A., Estévez, Á. G., Windebank, A. J., Dyer, R. B., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2034961100 · Cited by 88
MOZ-Mediated Repression of p16INK4a Is Critical for the Self-Renewal of Neural and Hematopoietic Stem Cells
Pérez-Campo, F. M., Costa, G., Lie‐A‐Ling, M., Stifani, S., Kouskoff, V., & Lacaud, G. (2013) · Stem Cells · doi:10.1002/stem.1606 · Cited by 88
The phosphorylation of α‐synuclein: development and implication for the mechanism and therapy of the Parkinson's disease
Xu, Y., Deng, Y., & Qing, H. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13234 · Cited by 87
SIRTUIN 1: Regulating the regulator
Zschoernig, B., & Mahlknecht, U. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.08.137 · Cited by 87
Microtubule: A Common Target for Parkin and Parkinson’s Disease Toxins
Feng, J. (2006) · The Neuroscientist · doi:10.1177/1073858406293853 · Cited by 85
Gcn5 regulates the dissociation of SWI/SNF from chromatin by acetylation of Swi2/Snf2Preprint
Kim, J., Saraf, A., Florens, L. A., Washburn, M. P., & Workman, J. L. (2010) · Genes & Development · doi:10.1101/gad.1979710 · Cited by 85
HDAC11: a multifaceted histone deacetylase with proficient fatty deacylase activity and its roles in physiological processes
Núñez‐Álvarez, Y., & Suelves, M. (2021) · FEBS Journal · doi:10.1111/febs.15895 · Cited by 85
Histone modification patterns correlate with patient outcome in oral squamous cell carcinoma
Chen, Y., Kao, S., Wang, H., & Yang, M. (2013) · Cancer · doi:10.1002/cncr.28356 · Cited by 85
Small Molecules Targeting HATs, HDACs, and BRDs in Cancer Therapy
Wu, D., Qiu, Y., Jiao, Y., Qiu, Z., & Liu, D. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.560487 · Cited by 84
Neuroprotection by Histone Deacetylase-7 (HDAC7) Occurs by Inhibition of c-jun Expression through a Deacetylase-independent Mechanism
Ma, C., & D’Mello, S. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.146860 · Cited by 83
Nucleocytoplasmic translocation of HDAC9 regulates gene expression and dendritic growth in developing cortical neurons
Sugo, N., Oshiro, H., Takemura, M., Kobayashi, T., Kohno, Y., Uesaka, N., Song, W., & Yamamoto, N. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07218.x · Cited by 83
Development of Improved HDAC6 Inhibitors as Pharmacological Therapy for Axonal Charcot–Marie–Tooth Disease
Benoy, V., Berghe, P. V., Jarpe, M. B., Damme, P. V., Robberecht, W., & Bosch, L. V. D. (2016) · Neurotherapeutics · doi:10.1007/s13311-016-0501-z · Cited by 83
A work in progress: The clinical development of histone deacetylase inhibitor
Marsoni, S., Damia, G. L. M., & Camboni, G. (2008) · Epigenetics · doi:10.4161/epi.3.3.6253 · Cited by 80
The Logic Linking Protein Acetylation and Metabolism
Guarente, L. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.07.007 · Cited by 79
Histone Deacetylase 3 Is Necessary for Proper Brain Development
Norwood, J. N., Franklin, J. M., Sharma, D., & D’Mello, S. R. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.576397 · Cited by 79
p180 Is Involved in the Interaction between the Endoplasmic Reticulum and Microtubules through a Novel Microtubule-binding and Bundling Domain
Ogawa‐Goto, K., Tanaka, K., Ueno, T., Tanaka, K., Kurata, T., Sata, T., & Irie, S. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-12-1125 · Cited by 79
Unique functional roles for class I and class II histone deacetylases in central nervous system development and function
Morris, M. J., & Monteggia, L. M. (2013) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2013.02.005 · Cited by 78
Chemical and functional aspects of posttranslational modification of proteins.
Knorre, D. G., Kudryashova, N. V., & Godovikova, T. S. (2009) · PubMed Central · Cited by 77
Epigenetic events, remodelling enzymes and their relationship to chromatin organization in prostatic intraepithelial neoplasia and prostatic adenocarcinoma
Mohamed, M. A., Greif, P. A., Diamond, J., Sharaf, O. F., Maxwell, P., Montironi, R., Young, R. A. M., & Hamilton, P. W. (2007) · British Journal of Urology · doi:10.1111/j.1464-410x.2006.06704.x · Cited by 74
Pathologies of axonal transport in neurodegenerative diseases
Liu, X.-A., Rizzo, V., & Puthanveettil, S. V. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0044-7 · Cited by 73
Histone deacetylases as targets for the treatment of neurodegenerative disorders: Challenges and future opportunities
Rodrigues, D. A., Pinheiro, P. D. S. M., Sagrillo, F. S., Bolognesi, M. L., & Fraga, C. A. M. (2020) · Medicinal Research Reviews · doi:10.1002/med.21701 · Cited by 73
Common Protective Strategies in Neurodegenerative Disease: Focusing on Risk Factors to Target the Cellular Redox System
Hrelia, P., Sita, G., Ziche, M., Ristori, E., Marino, A., Cordaro, M., Molteni, R., Spero, V., Malaguti, M., Morroni, F., et al. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8363245 · Cited by 73
HDAC6 Regulates Mutant SOD1 Aggregation through Two SMIR Motifs and Tubulin Acetylation
Gál, J., Chen, J., Barnett, K. R., Yang, L., Brumley, E., & Zhu, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.431957 · Cited by 70
A Structural Ensemble of a Tau-Microtubule Complex Reveals Regulatory Tau Phosphorylation and Acetylation Mechanisms
Brotzakis, Z. F., Lindstedt, P. R., Taylor, R. J., Rinauro, D. J., Gallagher, N. C. T., Bernardes, G. J. L., & Vendruscolo, M. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00585 · Cited by 70
Sirtuin modulators control reactive gliosis in an in vitro model of Alzheimer’s disease
Scuderi, C., Stecca, C., Bronzuoli, M. R., Rotili, D., Valente, S., Mai, A., & Steardo, L. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00089 · Cited by 69
Lysine Acetylation and Deacetylation in Brain Development and Neuropathies
Tapias, A., & Wang, Z. (2017) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2016.09.002 · Cited by 69
Histone acetylation in astrocytes suppresses GFAP and stimulates a re-organization of the intermediate filament network
Kanski, R., Sneeboer, M. A. M., van Bodegraven, E. J., Sluijs, J. A., Kropff, W., Vermunt, M. W., Creyghton, M. P., Filippis, L. D., Vescovi, A. L., Aronica, E., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.145912 · Cited by 68
Histone Hyperacetylation Up-regulates Protein Kinase Cδ in Dopaminergic Neurons to Induce Cell Death
Jin, H., Kanthasamy, A., Harischandra, D. S., Kondru, N. C., Ghosh, A., Panicker, N., Anantharam, V., Rana, A., & Kanthasamy, A. G. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.576702 · Cited by 67
Panobinostat (Farydak): A Novel Option for the Treatment of Relapsed Or Relapsed and Refractory Multiple Myeloma.
Moore, D. C. (2016) · PubMed Central · Cited by 67
Nuclear Accumulation of Histone Deacetylase 4 (HDAC4) Exerts Neurotoxicity in Models of Parkinson’s Disease
Wu, Q., Yang, X., Zhang, L., Zhang, Y., & Feng, L. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0199-2 · Cited by 66
The Role of SIRT3 in the Brain Under Physiological and Pathological Conditions
Sidorova‐Darmos, E., Sommer, R., & Eubanks, J. H. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00196 · Cited by 66
Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation‐Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6
Chiki, A., DeGuire, S. M., Ruggeri, F. S., Sanfelice, D., Ansaloni, A., Wang, Z., Cendrowska, U., Burai, R., Vieweg, S., Pastore, A., et al. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201611750 · Cited by 65
HDAC6 inhibition promotes α-tubulin acetylation and ameliorates CMT2A peripheral neuropathy in mice
Picci, C., Wong, V. S. C., Costa, C. J., McKinnon, M. C., Goldberg, D. C., Swift, M. L., Alam, N. M., Prusky, G. T., Shen, S., Kozikowski, A. P., et al. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113281 · Cited by 64
Differential sirtuin expression patterns in amyotrophic lateral sclerosis (ALS) postmortem tissue: neuroprotective or neurotoxic properties of sirtuins in ALS?
Körner, S., Böselt, S., Thau, N., Rath, K. J., Dengler, R., & Petri, S. (2013) · Neurodegenerative Diseases · doi:10.1159/000338048 · Cited by 64
Image-Guided Synthesis Reveals Potent Blood-Brain Barrier Permeable Histone Deacetylase Inhibitors
Seo, Y. J., Kang, Y., Muench, L., Reid, A. E., Caesar, S., Jean, L., Wagner, F. F., Holson, E. B., Haggarty, S. J., Weiss, P., et al. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500021p · Cited by 63
N-Myc and GCN5 Regulate Significantly Overlapping Transcriptional Programs in Neural Stem Cells
Martínez‐Cerdeño, V., Lemen, J. M., Chan, V., Wey, A., Lin, W., Dent, S., & Knoepfler, P. S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039456 · Cited by 63
A selective histone deacetylase-6 inhibitor improves BDNF trafficking in hippocampal neurons from Mecp2 knockout mice: implications for Rett syndrome
Xu, X., Kozikowski, A. P., & Pozzo‐Miller, L. D. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00068 · Cited by 63
Partial loss of Tip60 slows mid-stage neurodegeneration in a spinocerebellar ataxia type 1 (SCA1) mouse model
Gehrking, K. M., Andresen, J. M., Duvick, L. A., Lough, J., Zoghbi, H. Y., & Orr, H. T. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr108 · Cited by 62
Pharmocologic treatment with histone deacetylase 6 inhibitor (ACY‐738) recovers Alzheimer's disease phenotype in amyloid precursor protein/presenilin 1 (APP/PS1) mice
Majid, T., Griffin, D. M., Criss, Z. K., Jarpe, M. B., & Pautler, R. G. (2015) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2015.08.001 · Cited by 60
Gcn5 loss-of-function accelerates cerebellar and retinal degeneration in a SCA7 mouse model
Chen, Y., Gatchel, J. R., Lewis, R. W., Mao, C., Grant, P. A., Zoghbi, H. Y., & Dent, S. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr474 · Cited by 59
Autophagy regulation by acetylation—implications for neurodegenerative diseases
Son, S. M., Park, S. J., Fernandez-Estévez, M., & Rubinsztein, D. C. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00556-4 · Cited by 59
Function of Sirtuins in Biological Tissues
Shoba, B., Lwin, Z. M., Ling, L. S., Bay, B., Yip, G. W. C., & Srinivasan, D. K. (2009) · The Anatomical Record · doi:10.1002/ar.20875 · Cited by 58
First-in-Class Selective HDAC6 Inhibitor (ACY-1215) Has a Highly Favorable Safety Profile in Patients with Relapsed and Refractory Lymphoma
Amengual, J. E., Lue, J. K., Ma, H., Lichtenstein, R., Shah, B. D., Cremers, S., Jones, S. S., & Sawas, A. (2021) · The Oncologist · doi:10.1002/onco.13673 · Cited by 57
Class II HDACs mediate CaMK-dependent signaling to NRSF in ventricular myocytes
Nakagawa, Y., Kuwahara, K., Harada, M., Takahashi, N., Yasuno, S., Adachi, Y., Kawakami, R., Nakanishi, M., Tanimoto, K., Usami, S., et al. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2006.08.010 · Cited by 57
The epigenetic regulator Histone Deacetylase 1 promotes transcription of a core neurogenic programme in zebrafish embryos
Harrison, M. R., Georgiou, A. S., Spaink, H. P., & Cunliffe, V. T. (2011) · BMC Genomics · doi:10.1186/1471-2164-12-24 · Cited by 56
Lysine acetylation in the lumen of the ER: A novel and essential function under the control of the UPR
Pehar, M., & Puglielli, L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.12.004 · Cited by 56
Impairment of human terminal erythroid differentiation by histone deacetylase 5 deficiency
Wang, Y., Li, W., Schulz, V., Zhao, H., Qu, X., Qi, Q., Cheng, Y., Guo, X., Zhang, S., Wei, X., et al. (2021) · Blood · doi:10.1182/blood.2020007401 · Cited by 56
Traffic signaling: new functions of huntingtin and axonal transport in neurological disease
Vitet, H., Brandt, V. L., & Saudou, F. (2020) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2020.04.001 · Cited by 55
HDAC6 regulates microtubule stability and clustering of AChRs at neuromuscular junctions
Osseni, A., Ravel‐Chapuis, A., Thomas, J.-L., Gache, V., Schaeffer, L., & Jasmin, B. J. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201901099 · Cited by 55
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Athira, K. V., Sadanandan, P., & Chakravarty, S. (2021) · NeuroMolecular Medicine · doi:10.1007/s12017-021-08660-4 · Cited by 55
Histone Deacetylase 10 Relieves Repression on the Melanogenic Program by Maintaining the Deacetylation Status of Repressors
Lai, I., Lin, T.-P., Yao, Y., Lin, C., Hsieh, M.-J., & Yang, W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.061861 · Cited by 54
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Sambataro, F., & Pennuto, M. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00082 · Cited by 54
N‐terminal acetylation modestly enhances phase separation and reduces aggregation of the low‐complexity domain of RNA‐binding protein fused in sarcoma
Bock, A. S., Murthy, A. C., Tang, W. S., Jovic, N., Shewmaker, F. P., Mittal, J., & Fawzi, N. L. (2021) · Protein Science · doi:10.1002/pro.4029 · Cited by 54
Histone deacetylases and their inhibitors: molecular mechanisms and therapeutic implications in diabetes mellitus
Wang, X., Wei, X., Pang, Q., & Yi, F. (2012) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2012.06.005 · Cited by 53
The Lysine Acetyltransferase Activator Brpf1 Governs Dentate Gyrus Development through Neural Stem Cells and Progenitors
You, L., Yan, K., Zhou, J., Hong, Z., Bertos, N., Park, M., Wang, E., & Yang, X. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005034 · Cited by 53
Histone Acetyltransferase Activities of cAMP-Regulated Enhancer-Binding Protein and p300 in Tissues of Fetal, Young, and Old Mice
Li, Q., Xiao, H., & Isobe, K. (2002) · The Journals of Gerontology Series A · doi:10.1093/gerona/57.3.b93 · Cited by 52
Mass Spectrometric Identification of Novel Lysine Acetylation Sites in Huntingtin
Cong, X., Held, J. M., DeGiacomo, F., Bonner, A., Chen, J. M., Schilling, B., Czerwieniec, G. A., Gibson, B. W., & Ellerby, L. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.009829 · Cited by 52
Autophagy induced by SAHA affects mutant P53 degradation and cancer cell survival
Foggetti, G., Ottaggio, L., Russo, D., Mazzitelli, C., Monti, P., Degan, P., Miele, M., Fronza, G., & Menichini, P. (2019) · Bioscience Reports · doi:10.1042/bsr20181345 · Cited by 51
Imbalance of Lysine Acetylation Contributes to the Pathogenesis of Parkinson’s Disease
Wang, R., Sun, H., Wang, G., & Ren, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197182 · Cited by 51
Acetylated α-tubulin K394 regulates microtubule stability to shape the growth of axon terminals
Saunders, H. A. J., Johnson-Schlitz, D. M., Jenkins, B., Volkert, P. J., Yang, S. Z., & Wildonger, J. (2022) · Current Biology · doi:10.1016/j.cub.2021.12.012 · Cited by 51
Enhanced SIRT6 activity abrogates the neurotoxic phenotype of astrocytes expressing ALS-linked mutant SOD1
Harlan, B. A., Pehar, M., Killoy, K. M., & Vargas, M. R. (2019) · The FASEB Journal · doi:10.1096/fj.201802752r · Cited by 50
Histone deacetylase class II and acetylated core histone immunohistochemistry in human brains with Huntington’s disease
Yeh, H. H., Young, D. P., Gelovani, J. G., Robinson, A., Davidson, Y. S., Herholz, K., & Mann, D. M. A. (2013) · Brain Research · doi:10.1016/j.brainres.2013.02.012 · Cited by 46
Post-Translational Modifications Modulate Proteinopathies of TDP-43, FUS and hnRNP-A/B in Amyotrophic Lateral Sclerosis
Farina, S., Esposito, F., Battistoni, M., Biamonti, G., & Francia, S. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.693325 · Cited by 46
The Role of Phosphorylation in Synucleinopathies: Focus on Parkinsons Disease
Cavallarin, N., Vicario, M., & Negro, A. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710791556140 · Cited by 46
MECP2 mutations affect ciliogenesis: a novel perspective for Rett syndrome and related disorders
Frasca, A., Spiombi, E., Palmieri, M., Albizzati, E., Valente, M. M., Bergo, A., Leva, B., Kilstrup‐Nielsen, C., Bianchi, F., Di Carlo, V., et al. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.201910270 · Cited by 46
Rotenone Induces the Formation of 4-Hydroxynonenal Aggresomes. Role of ROS-Mediated Tubulin Hyperacetylation and Autophagic Flux Disruption
Bonet‐Ponce, L., Sáez-Atiénzar, S., da Casa, C., Sancho-Pellúz, J., Barcia, J. M., Martínez‐Gil, N., Nava, E., Jordán, J., Romero, F. J., & Galindo, M. F. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9509-3 · Cited by 45
Lysine acetylation of cytoskeletal proteins: Emergence of an actin code
Mu, A., Latario, C. J., Pickrell, L. E., & Higgs, H. N. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202006151 · Cited by 45
N-terminal acetylation mutants affect alpha-synuclein stability, protein levels and neuronal toxicity
Vinueza‐Gavilanes, R., Íñigo-Marco, I., Larrea, L., Lasa, M., Carte, B., Santamaría, E., Fernández‐Irigoyen, J., Bugallo, R., Aragón, T., Aldabe, R., et al. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104781 · Cited by 44
LRRK2 at the Crossroad Between Autophagy and Microtubule Trafficking
Esteves, A. R., & Cardoso, S. M. (2016) · The Neuroscientist · doi:10.1177/1073858415616558 · Cited by 43
Regulation of Neuronal Cytoskeletal Protein Phosphorylation in Neurodegenerative Diseases
Rudrabhatla, P. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-130794 · Cited by 40
Acetylation and phosphorylation of STAT3 are involved in the responsiveness of microglia to beta amyloid
Eufemi, M., Cocchiola, R., Romaniello, D., Correani, V., Di Francesco, L., Fabrizi, C., Maras, B., & Schininà, M. E. (2015) · Neurochemistry International · doi:10.1016/j.neuint.2015.01.007 · Cited by 39
Molecular basis for N-terminal alpha-synuclein acetylation by human NatB
Deng, S., Pan, B., Gottlieb, L., Petersson, E. J., & Marmorstein, R. (2020) · eLife · doi:10.7554/elife.57491 · Cited by 38
Post-translational modifications in neurodegeneration
Didonna, A., & Benetti, F. (2015) · AIMS Biophysics · doi:10.3934/biophy.2016.1.27 · Cited by 36
Functions of Myst Family Histone Acetyltransferases and Their Link to Disease
Avvakumov, N., & Côté, J. (2007) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/1-4020-5466-1_13 · Cited by 35
Selective PCAF inhibitor ameliorates cognitive and behavioral deficits by suppressing NF-κB-mediated neuroinflammation induced by Aβ in a model of Alzheimer’s disease
Park, S., Kim, M., Kim, Y. J., Lee, Y., Bae, D., Kim, S., Na, Y., & Yoon, H. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2099 · Cited by 35
Design, synthesis and biological evaluation of a series of CNS penetrant HDAC inhibitors structurally derived from amyloid-β probes
Choi, M. A., Park, S. Y., Chae, H. Y., Song, Y., Sharma, C., & Seo, Y. H. (2019) · Scientific Reports · doi:10.1038/s41598-019-49784-9 · Cited by 35
Histone Deacetylase Rpd3 Regulates Olfactory Projection Neuron Dendrite Targeting via the Transcription Factor Prospero
Tea, J. S., Chihara, T., & Luo, L. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1643-10.2010 · Cited by 34
Proteomic analyses of intermediate filaments reveals cytokeratin8 is highly acetylated – implications for colorectal epithelial homeostasis
Leech, S. H., Evans, C. A., Shaw, L., Wong, C. H., Connolly, J., Griffiths, J. R., Whetton, A. D., & Corfe, B. M. (2008) · PROTEOMICS · doi:10.1002/pmic.200700404 · Cited by 34
Lysine Acetylation: The Tale of a Modification from Transcription Regulation to Metabolism
Arif, M., Selvi, B. R., & Kundu, T. K. (2010) · ChemBioChem · doi:10.1002/cbic.201000292 · Cited by 34
MicroRNAs and HDAC4 protein expression in the skeletal muscle of ALS patients
Pegoraro, V., Marozzo, R., & Angelini, C. I. (2020) · Clinical Neuropathology · doi:10.5414/np301233 · Cited by 34
Cortactin deacetylation by HDAC6 and SIRT2 regulates neuronal migration and dendrite morphogenesis during cerebral cortex development
Kim, J.-Y., Hwang, H.-G., Lee, J., Kim, J., & Kim, J. (2020) · Molecular Brain · doi:10.1186/s13041-020-00644-y · Cited by 34
HDAC10 Is Positively Associated With PD-L1 Expression and Poor Prognosis in Patients With NSCLC
Liu, X., Wang, D., Zhang, R., Jin, T., Qu, L., Jin, Q., Zheng, J., Sun, J., Wu, Z., Wang, L., et al. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00485 · Cited by 33
Role of Protein Aggregation in Neurodegenerative Diseases
Tutar, Y., zgur, A., & Tutar, L. (2013) · InTech eBooks · doi:10.5772/54487 · Cited by 31
Protein Aggregation
Merlini, G., Bellotti, V., Andreola, A., Palladini, G. O., Obici, L. P., Casarini, S., & Perfetti, V. (2001) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2001.172 · Cited by 31
Increased acetylation of microtubules rescues human tau-induced microtubule defects and neuromuscular junction abnormalities in Drosophila
Mao, C., Wen, X., Jin, S., & Zhang, Y. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.028316 · Cited by 30
Chemical Control of a CRISPR-Cas9 Acetyltransferase
Shrimp, J. H., Grose, C., Widmeyer, S. R. T., Thorpe, A. L., Jadhav, A., & Meier, J. L. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.7b00883 · Cited by 30
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LoPresti, P. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00519 · Cited by 30
Gene variants and expression changes of SIRT1 and SIRT6 in peripheral blood are associated with Parkinson’s disease
Maszlag-Török, R., Boros, F. A., Vécsei, L., & Klivènyi, P. (2021) · Scientific Reports · doi:10.1038/s41598-021-90059-z · Cited by 30
HDAC expression and activity is upregulated in diseased lupus-prone mice
Regna, N. L., Vieson, M. D., Gojmerac, A. M., Luo, X., Caudell, D. L., & Reilly, C. M. (2015) · International Immunopharmacology · doi:10.1016/j.intimp.2015.10.006 · Cited by 30
The role of histone deacetylase 6 (HDAC6) in neurodegeneration
Helleputte, L. V., Benoy, V., & Bosch, L. V. D. (2014) · Research and Reports in Biology · doi:10.2147/rrb.s35470 · Cited by 29
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
N-alpha-acetylation of Huntingtin protein increases its propensity to aggregate
Gottlieb, L., Guo, L. E., Shorter, J., & Marmorstein, R. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101363 · Cited by 29
Conditional deletion of histone deacetylase‐4 in the central nervous system has no major effect on brain architecture or neuronal viability
Price, V. J., Wang, L., & D’Mello, S. R. (2012) · Journal of Neuroscience Research · doi:10.1002/jnr.23170 · Cited by 28
SIRT6 Through the Brain Evolution, Development, and Aging
García-Venzor, A., & Toiber, D. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.747989 · Cited by 28
Lysine post-translational modifications and the cytoskeleton
Zencheck, W. D., Xiao, H., & Weiss, L. M. (2012) · Essays in Biochemistry · doi:10.1042/bse0520135 · Cited by 28
Application of High-Content Analysis to the Study of Post-Translational Modifications of the Cytoskeleton
Drake, P. J. M., Griffiths, G. J., Shaw, L., Benson, R., & Corfe, B. M. (2008) · Journal of Proteome Research · doi:10.1021/pr8006396 · Cited by 27
HDAC8 regulates neural differentiation through embryoid body formation in P19 cells
Katayama, S., Morii, A., Makanga, J. O., Suzuki, T., Miyata, N., & Inazu, T. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.02.195 · Cited by 27
Depletion of histone deacetylase 3 antagonizes PI3K-mediated overgrowth through the acetylation of histone H4 at lysine 16
Lv, W., Wei, H.-M., Wang, D.-L., Ni, J., & Sun, F.-L. (2012) · Journal of Cell Science · doi:10.1242/jcs.106336 · Cited by 23
HDAC6 Inhibition Corrects Electrophysiological and Axonal Transport Deficits in a Human Stem Cell‐Based Model of Charcot‐Marie‐Tooth Disease (Type 2D)
Smith, A. S. T., Kim, J. H., Chun, C., Gharai, A., Moon, H. W., Kim, E. Y., Nam, S. H., Ha, N., Song, J. Y., Chung, K. W., et al. (2021) · Advanced Biology · doi:10.1002/adbi.202101308 · Cited by 23
Identification of retinoblastoma binding protein 7 (Rbbp7) as a mediator against tau acetylation and subsequent neuronal loss in Alzheimer’s disease and related tauopathies
Dave, N., Vural, A. S., Piras, I. S., Winslow, W., Surendra, L., Winstone, J. K., Beach, T. G., Huentelman, M. J., & Velázquez, R. (2021) · Acta Neuropathologica · doi:10.1007/s00401-021-02323-1 · Cited by 22
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Bodai, L., Pallos, J., Thompson, L. M., & Marsh, J. (2011) · Neurodegenerative Diseases · doi:10.1159/000330505 · Cited by 21
Regulation of PGC-1α mediated by acetylation and phosphorylation in MPP+ induced cell model of Parkinson’s disease
Fan, F., Li, S., Wen, Z., Ye, Q., Chen, X., & Ye, Q. (2020) · Aging · doi:10.18632/aging.103219 · Cited by 21
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Li, Y., Huang, H., Zhu, M. L., Bai, H., & Huang, X. (2021) · Aging and Disease · doi:10.14336/ad.2020.0329 · Cited by 21
Role of the microtubule-associated TPPP/p25 in Parkinson’s and related diseases and its therapeutic potential
Oláh, J., Bertrand, P., & Ovádi, J. (2017) · Expert Review of Proteomics · doi:10.1080/14789450.2017.1304216 · Cited by 20
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Shirmast, P., Ghafoori, S. M., Irwin, R. M., Abendroth, J. A., Mayclin, S. J., Lorimer, D. D., Edwards, T. E., & Forwood, J. K. (2021) · Scientific Reports · doi:10.1038/s41598-020-79649-5 · Cited by 19
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Quan, P., Wang, K., Shi, Y., Wen, S., Wei, C., Zhang, X., Cao, J., & Yao, L. (2021) · Scientific Reports · doi:10.1038/s41598-021-92701-2 · Cited by 18
Therapeutic potential of HDAC6 in amyotrophic lateral sclerosis
Guo, W., & Bosch, L. V. D. (2018) · Cell Stress · doi:10.15698/cst2018.01.120 · Cited by 15
Expression of Acetylated and Dimethylated Histone H3 in Colorectal Cancer
Hashimoto, T., Yamakawa, M., Kimura, S., Usuba, O., & TOYONO, M. (2013) · Digestive Surgery · doi:10.1159/000351444 · Cited by 15
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Soriano, F. X., & Hardingham, G. E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021056 · Cited by 14
HDAC inhibitor ameliorates behavioral deficits in Mecp2308/y mouse model of Rett syndrome
Lebrun, N., Delépine, C., Selloum, M., Méziane, H., Nectoux, J., Hérault, Y., & Bienvenu, T. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147670 · Cited by 14
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Kim, C.-H., Kim, J.-W., Jang, S., An, J., Song, K., & Choi, K. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.06.126 · Cited by 13
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Ras-ERK1/2 Signaling Promotes The Development Of Osteosarcoma By Regulating H2BK12ac Through CBP
Xu, X., Yu, H., & Xu, Y. (2019) · Cancer Management and Research · doi:10.2147/cmar.s219535 · Cited by 10
Analysis of Expression and Functions of Histone Deacetylase 6 (HDAC6)
Li, M., Zhuang, Y., & Shan, B. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3667-0_6 · Cited by 8
Molecular Components of the Neuronal Cytoskeleton
Kirkpatrick, L., & Brady, S. T. (1999) · Cited by 7
Acetylation
Portaleone, P. (2004) · Elsevier eBooks · doi:10.1016/b0-12-475570-4/00003-2 · Cited by 7
HDAC11: A novel inflammatory biomarker in Huntington’s disease
Kumar, V., Kaur, S., Kapil, L., Singh, C., & Singh, A. (2022) · EXCLI journal · doi:10.17179/excli2022-4741 · Cited by 5
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Garth, F. (2011) · InTech eBooks · doi:10.5772/27973 · Cited by 3
Amyloid beta peptides, tau protein acetylation and therapeutic strategies for treating Alzheimer’s disease: a review
Guha, S. K., & Rajalakshmi, S. (2021) · Life Research · doi:10.53388/life2021-0121-305 · Cited by 3
Dementia: Unwelcome change has arrived and we are not ready!
Ashby, M. A. (2019) · Journal of Bioethical Inquiry · doi:10.1007/s11673-019-09921-5 · Cited by 3
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Wang, M., Cheng, F., Chen, J., Li, Y., Villagra, A., Smith, M. R., Seto, E., & Sotomayor, E. M. (2017) · Blood · doi:10.1182/blood.v130.suppl_1.3561.3561 · Cited by 2
Abstract CT107: Phase IB trial of ACY-1215 (ricolinostat) combined with nab-paclitaxel in metastatic breast cancer (MBC)
Silva, J., Kalinsky, K. M., Chiuzan, C. C., Zeleke, T. Z., Pan, Q., & Yu, J. (2020) · Cancer Research · doi:10.1158/1538-7445.am2020-ct107 · Cited by 1

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Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review
Yang, J., Zhi, W., & Wang, L. (2024) · Molecules · doi:10.3390/molecules29122812 · Cited by 63
“Speciﬁc acetylation sites regulate the formation of tau aggregates, synaptic signalling, and long-term potentiation [74,75].”
Background
Orthogonal Translation for Site-Specific Installation of Post-translational Modifications
Gan, Q., & Fan, C. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00850 · Cited by 55
Proteostasis disruption and senescence in Alzheimer’s disease pathways to neurodegeneration
Thapa, R., Bhat, A. A., Shahwan, M. J., Ali, H., Padmapriya, G., Bansal, P., Rajotiya, S., Barwal, A., Prasad, G. V. S., Pramanik, A., et al. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149202 · Cited by 48
The pathogenic mechanism of TAR DNA-binding protein 43 (TDP-43) in amyotrophic lateral sclerosis
Wang, X., Hu, Y., & Xu, R. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.382233 · Cited by 37
Post‐translational modifications of proteins in cardiovascular diseases examined by proteomic approaches
Št́astná, M. (2024) · FEBS Journal · doi:10.1111/febs.17108 · Cited by 32

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Authors: Kabir, F., Atkinson, R., Cook, A. L., Phipps, A. J., & King, A. E.
Affiliations: University of Tasmania (AU)
Corresponding author: Phipps, Andrew James
ORCID: Kabir, Fariha
Atkinson, Rachel
Cook, Anthony L.
King, Anna Elizabeth
Venue: Frontiers in Aging Neuroscience
Publisher: Frontiers Media SA
Published: 2023-01-04
Volume: 14
Pages: 1025473-1025473
ISSN: 1663-4365 (ISSN-L)
DOI: 10.3389/fnagi.2022.1025473
PMC: PMC9845957
OpenAlex: W4313477105
Cited by: 75
References: 325
Citations by year: 2026: 20 · 2025: 22 · 2024: 25 · 2023: 8
FWCI: 1.98
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Frontiers in Aging Neuroscience (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Figshare (submittedVersion, cc-by)
Funders: National Health and Medical Research Council (APP1136913)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Keywords: protein acetylation, post-translational modification, neurodegenerative diseases, histone acetyltransferase, histone deacetylase, Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis, tau protein, alpha-synuclein, huntingtin, axonal transport, neuroplasticity

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The role of altered protein acetylation in neurodegenerative disease

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