The physiological roles of histone deacetylase (HDAC) 1 and 2: complex co-stars with multiple leading parts

Lysine acetylation targets protein complexes and co-regulates major cellular functions

Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040

ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS

Allfrey, V. G., Faulkner, R. D., & Mirsky, A. E. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.5.786 · Cited by 2,788

The many roles of histone deacetylases in development and physiology: implications for disease and therapy

Haberland, M., Montgomery, R. L., & Olson, E. N. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2485 · Cited by 2,600

A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p

Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829

Structure and ligand of a histone acetyltransferase bromodomain

Dhalluin, C., Carlson, J. E., Zeng, L., He, C., Aggarwal, A. K., Zhou, M.-M., & Zhou, M.-M. (1999) · Nature · doi:10.1038/20974 · Cited by 1,732

HDAC2 negatively regulates memory formation and synaptic plasticity

Guan, J.-S., Haggarty, S. J., Giacometti, E., Dannenberg, J.-H., Joseph, N., Gao, J., Nieland, T. J. F., Zhou, Y., Wang, X., Mazitschek, R., et al. (2009) · Nature · doi:10.1038/nature07925 · Cited by 1,644

Recent progress in the biology and physiology of sirtuins

Finkel, T., Deng, C., & Mostoslavsky, R. (2009) · Nature · doi:10.1038/nature08197 · Cited by 1,506

Estrogen Receptor-α Directs Ordered, Cyclical, and Combinatorial Recruitment of Cofactors on a Natural Target Promoter

Métivier, R., Penot, G., Hübner, M. R., Reid, G., Brand, H., Koš, M., & Gannon, F. (2003) · Cell · doi:10.1016/s0092-8674(03)00934-6 · Cited by 1,431

Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes

Wang, Z., Zang, C., Cui, K., Schones, D. E., Barski, A., Peng, W., & Zhao, K. (2009) · Cell · doi:10.1016/j.cell.2009.06.049 · Cited by 1,344

Histone H3 Methylation by Set2 Directs Deacetylation of Coding Regions by Rpd3S to Suppress Spurious Intragenic Transcription

Carrozza, M. J., Li, B., Florens, L. A., Suganuma, T., Swanson, S. K., Lee, K. K., Shia, W.-J., Anderson, S., Yates, J. R., Washburn, M. P., et al. (2005) · Cell · doi:10.1016/j.cell.2005.10.023 · Cited by 1,338

Rescuing lung development through embryonic inhibition of histone acetylation

Stokes, G., Li, Z., Talaba, N., Genthe, W., Brix, M. B., Pham, B., Wienhold, M. D., Sandok, G., Hernan, R., Wynn, J., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adc8930 · Cited by 12

The ZFP541-KCTD19 complex is essential for pachytene progression by activating meiotic genes during mouse spermatogenesis

Li, Y., Meng, R., Li, S., Gu, B., Xu, X., Zhang, H., Tan, X., Shao, T., Wang, J., Xu, D., et al. (2022) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2022.03.005 · Cited by 12

The Nucleosome Remodeling and Deacetylase Complex in Development and Disease

Basta, J. M., & Rauchman, M. I. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-800802-7.00003-4 · Cited by 14

Overcome the tumor immunotherapy resistance by combination of the HDAC6 inhibitors with antitumor immunomodulatory agents

Khamis, M. Y., Wu, H.-P., Ma, Q., Li, Y., Ma, L., Zhang, X., & Liu, H. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104754 · Cited by 12

RNF168 promotes RHOC degradation by ubiquitination to restrain gastric cancer progression via decreasing HDAC1 expression

Xu, Y., Feng, Y., Sun, Z., & Li, Q. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.03.123 · Cited by 11

Involvement of HDAC2-mediated kcnq2/kcnq3 genes transcription repression activated by EREG/EGFR-ERK-Runx1 signaling in bone cancer pain

Zhang, Z.-X., Tian, Y., Li, S., Jing, H., Cai, J., Li, M., & Xing, G. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01797-2 · Cited by 11

Loss of TACC2 impairs chemokine CCL3 and CCL4 expression and reduces response to anti-PD-1 therapy in soft tissue sarcoma

Yang, J., Lu, X., Cai, Q., Liu, M., Xia, T., Hong, D., Le, L., Zhang, X., & Zhang, X. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02354-2 · Cited by 11

Loss of histone deacetylase HDAC1 induces cell death in Drosophila epithelial cells through JNK and Hippo signaling

Zhang, T., Sheng, Z., & Du, W. (2016) · Mechanisms of Development · doi:10.1016/j.mod.2016.07.001 · Cited by 12

Proteomic analysis of Plasmodium falciparum histone deacetylase 1 complex proteins

Engel, J. A., Norris, E. L., Gilson, P. R., Przyborski, J. M., Shonhai, A., Blatch, G. L., Skinner‐Adams, T. S., Gorman, J. J., Headlam, M. J., & Andrews, K. T. (2019) · Experimental Parasitology · doi:10.1016/j.exppara.2019.01.008 · Cited by 14

PROTACs targeting epigenetic proteins

Zhang, C., He, Y., Sun, X., Wei, W., Liu, Y., & Rao, Y. (2023) · Acta Materia Medica · doi:10.15212/amm-2023-0039 · Cited by 13

The role of epigenetic mechanisms in the long‐term effects of early‐life adversity and mother–infant relationship on physiology and behavior of offspring in laboratory rats and mice

Burenkova, O. V., & Grigorenko, E. L. (2024) · Developmental Psychobiology · doi:10.1002/dev.22479 · Cited by 11

Regulation of calpain 2 expression by miR-223 and miR-145

Siuda, D., Randriamboavonjy, V., & Fleming, I. (2019) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2019.194438 · Cited by 11

Cell-based multi-substrate assay coupled to UHPLC-ESI-MS/MS for a quick identification of class-specific HDAC inhibitors

Zwick, V., Simões‐Pires, C. A., & Cuendet, M. (2016) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2016.1180595 · Cited by 11

Transcription suppression is mediated by the HDAC1–Sin3 complex in Xenopus nucleoplasmic extract

Quaas, C. E., Lin, B., & Long, D. T. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102578 · Cited by 10

HDAC2 links ubiquitination to tumor suppression in synovial sarcoma

Cooley, C., & Su, L. (2021) · Molecular & Cellular Oncology · doi:10.1080/23723556.2021.1914291 · Cited by 10

Tubulin/HDAC dual-target inhibitors: Insights from design strategies, SARs, and therapeutic potential

Zhang, Z., Su, R. J., Liu, J., Chen, K., Wu, C., Sun, P., & Sun, T. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117022 · Cited by 10

Evaluating Chromatographic Approaches for the Quantitative Analysis of a Human Proteome on Orbitrap-Based Mass Spectrometry Systems

Zhang, Y., Wen, Z., Washburn, M. P., & Florens, L. A. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00036 · Cited by 9

Inhibition of Histone Deacetylases 1, 2, and 3 Enhances Clearance of Cholesterol Accumulation in Niemann-Pick C1 Fibroblasts

Cruz, D. L., Pipalia, N. H., Mao, S., Gadi, D., Liu, G., Grigalunas, M., O’Neill, M. J., Quinn, T. R., Kipper, A., Ekebergh, A., et al. (2021) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.1c00033 · Cited by 9

Selective Targeting of Class I Histone Deacetylases in a Model of Human Osteosarcoma

Torres, H. M., VanCleave, A. M., Vollmer, M. L., Callahan, D., Smithback, A., Conn, J. M., Rodezno, T. G., Gao, Z., Cao, Y. X., Tecleab, Y. A., et al. (2021) · Cancers · doi:10.3390/cancers13164199 · Cited by 10

Quantitative Acetylomics Uncover Acetylation-Mediated Pathway Changes Following Histone Deacetylase Inhibition in Anaplastic Large Cell Lymphoma

Zrimšek, M., Kuchaříková, H., Draganić, K., Dobrovolná, P., Spornberger, V. H., Winkelmayer, L., Hassler, M. R., Lochmanová, G., Zdráhal, Z., & Egger, G. (2022) · Cells · doi:10.3390/cells11152380 · Cited by 9

Oligodendroglial Development

Huang, N., Niu, J., Feng, Y., & Xiao, L. (2015) · The Neuroscientist · doi:10.1177/1073858414565467 · Cited by 9

Identification of candidate biomarkers that involved in the epigenetic transcriptional regulation for detection gastric cancer by iTRAQ based quantitative proteomic analysis

Jiang, Z., Sun, X., Zhang, Q., Ji, X., Yu, Q., Huang, T., Chen, D., Chen, H., Mei, X., Wang, L., et al. (2017) · Clinica Chimica Acta · doi:10.1016/j.cca.2017.05.015 · Cited by 9

HDAC1 acts as a tumor suppressor in ALK-positive anaplastic large cell lymphoma: implications for HDAC inhibitor therapy

Zrimšek, M., Draganić, K., Malzer, A., Doblmayr, V., Mišura, K., Silva, R. D. F. E., Matthews, J. D., Iannelli, F., Wohlhaupter, S., Malla, C. U. P., et al. (2025) · Leukemia · doi:10.1038/s41375-025-02584-9 · Cited by 8

Arid4b physically interacts with Tfap2c in mouse embryonic stem cells

Keskin, E. G., Huang, J., & Çizmecioğlu, N. T. (2021) · TURKISH JOURNAL OF BIOLOGY · doi:10.3906/biy-2010-67 · Cited by 8

OTUD5 limits replication fork instability by organizing chromatin remodelers

de Vivo, A., Song, H., Lee, Y., Tirado-Class, N., Sanchez, A. R., Westerheide, S. D., Dungrawala, H., & Kee, Y. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad732 · Cited by 8

A synergistic multitargeted of BET and HDAC: an intra-molecular mechanism of communication in treatment of Waldenström macroglobulinemia

Elamin, G., Aljoundi, A., & Soliman, M. E. S. (2021) · Molecular Simulation · doi:10.1080/08927022.2021.2005248 · Cited by 8

Improved Pharmacokinetic Profiles of HDAC6 Inhibitors via Cap Group Modifications

Olaoye, O. O., Erdogan, F., Gracia-Hernandez, M., Garcha, H. K., Sedighi, A., Ashraf, Q. F., Nawar, N., Geletu, M., Seo, H., Abdallah, D. I., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00479 · Cited by 8

HDAC3 inhibition improves urinary‐concentrating defect in hypokalaemia by promoting AQP2 transcription

Xu, L., Xie, H., Hu, S., Zhao, X., Han, M., Liu, Q., Feng, P., Wang, W., & Li, C. (2022) · Acta Physiologica · doi:10.1111/apha.13802 · Cited by 7

Hippo pathway and Bonus control developmental cell fate decisions in the Drosophila eye

Zhao, H., Moberg, K. H., & Veraksa, A. N. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.02.005 · Cited by 7

Untersuchung der Substratselektivität und Zusammensetzung endogener Histondeacetylase‐Komplexe durch chemische Sonden

Dose, A., Sindlinger, J., Bierlmeier, J., Bakirbas, A., Schulze‐Osthoff, K., Einsele‐Scholz, S., Hartl, M., Eßmann, F., Finkemeier, I., & Schwarzer, D. (2015) · Angewandte Chemie · doi:10.1002/ange.201508174 · Cited by 7

Network of phosphatases and HDAC complexes at repressed chromatin

de Castro, I. J., Amin, H. A., Vinciotti, V., & Vagnarelli, P. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1371883 · Cited by 7

Histone deacetylases 1 and 2 target gene regulatory networks of nephron progenitors to control nephrogenesis

Liu, H., Ngo, N. Y. N., Herzberger, K. F., Gummaraju, M., Hilliard, S. A., & Chen, C. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115341 · Cited by 6

SIN-3 acts in distinct complexes to regulate the germline transcriptional program in Caenorhabditis elegans

Robert, V. J. P., Caron, M. J., Gely, L., Adrait, A., Pakulska, V., Couté, Y., Chevalier, M., Riedel, C. G., Bedet, C., & Palladino, F. (2023) · Development · doi:10.1242/dev.201755 · Cited by 6

HDAC1 and HDAC2 orchestrate Wnt signaling to regulate neural progenitor transition during brain development

Zhu, Y., Huang, Y., Tang, T., & Xie, Y. (2024) · iScience · doi:10.1016/j.isci.2024.110600 · Cited by 6

Epigenetic Priming and Development of New Combination Therapy Approaches

Meneceur, S., Grunewald, C. M., Niegisch, G., & Hoffmann, M. J. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3291-8_16 · Cited by 6

Comparative interactome analysis of α-arrestin families in human and Drosophila

Lee, K.-T., Pranoto, I. K. A., Kim, S., Choi, H., To, N. B., Chae, H., Lee, J., Kim, J., Kwon, Y. V., & Nam, J. (2023) · eLife · doi:10.7554/elife.88328 · Cited by 6

Quantitative measurement of intracellular HDAC1/2 drug occupancy using a trans -cyclooctene largazole thiol probe

Xu, H., Roberts, L. R., Chou, S., Pierce, B. S., Narayanan, A., & Jones, L. H. (2017) · MedChemComm · doi:10.1039/c6md00633g · Cited by 6

A positive role of Sin3A in regulating Notch signaling during Drosophila wing development

Zhang, X., Chen, M., Nan, Z., Lyu, J., Xi, Y., Yang, X., & Ge, W. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.10.008 · Cited by 6

Epigenetic Mechanisms of Ischemic Stroke

Uzdensky, A. B., & Demyanenko, S. V. (2019) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s1990747819040093 · Cited by 6

HDAC1 was involved in placental breast cancer resistance protein regulation in vitro: A preliminary study

Duan, H., Zhou, K., Zhang, Y., Yue, P., Wang, T., Li, Y., Qiu, D., Hua, Y., & Wang, C. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14414 · Cited by 6

Bilateral histone deacetylase 1 and 2 activity and enrichment at unique genes following induction of long‐term potentiation in vivo

Kyrke‐Smith, M., Logan, B. J., Abraham, W. C., & Williams, J. M. (2020) · Hippocampus · doi:10.1002/hipo.23297 · Cited by 6

Histone-Binding Protein RBBP4 Is Necessary to Promote Neurogenesis in the Developing Mouse Neocortical Progenitors

Dhanya, S. K., Kalia, K., Mohanty, S., Azam, T., Channakkar, A. S., D’Souza, L., S., S. K., Reddy, P. C., & Muralidharan, B. (2024) · eNeuro · doi:10.1523/eneuro.0391-23.2024 · Cited by 6

Mutations on the surface of HDAC1 reveal molecular determinants of specific complex assembly and their requirement for gene regulation

Alshehri, A., Baker, I.-M., English, D. M., Fairall, L., Collins, M. O., Schwabe, J. W. R., & Cowley, S. M. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf918 · Cited by 5

ELM2‐SANT Domain‐Containing Scaffolding Protein 1 Regulates Differentiation and Maturation of Cardiomyocytes Derived From Human‐Induced Pluripotent Stem Cells

Lu, Y., Sun, J., Wang, L., Wang, M., Wu, Y., Getachew, A., Matthews, R. C., Li, H., Peng, W. G., Zhang, J. J., et al. (2024) · Journal of the American Heart Association · doi:10.1161/jaha.124.034816 · Cited by 5

Effect of Histone Deacetylase Inhibition on the Expression of Multidrug Resistance-associated Protein 2 in a Human Placental Trophoblast Cell Line

Duan, H., Ma, D., Zhou, K., Wang, T., Zhang, Y., Li, Y., Wu, J., Hua, Y., & Wang, C. (2017) · Chinese Medical Journal · doi:10.4103/0366-6999.206352 · Cited by 5

Histone Deacetylases in the Control of Epidermal Homeostasis: From Chromatin Biology toward Therapy

Botchkarev, V. A., & Sharov, A. A. (2021) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2021.06.021 · Cited by 4

HDACs in Diabetes

Schütz, L. F., Park, M. H., & Choudhury, M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-812019-4.00035-0 · Cited by 4

Proteomics-based trapping with single or multiple inactive mutants reproducibly profiles histone deacetylase 1 substrates

Herath, K. E., Kodikara, I. K. M., & Pflum, M. K. H. (2022) · Journal of Proteomics · doi:10.1016/j.jprot.2022.104807 · Cited by 4

Epigenetic Treatment Options in Urothelial Carcinoma

Pinkerneil, M., Hoffmann, M. J., & Niegisch, G. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7234-0_21 · Cited by 4

Amyloids in bladder cancer hijack cancer-related proteins and are positive correlated to tumor stage

Alem, D., García-Laviña, C. X., Garagorry, F., Centurión, D., Farías, J., Pazos-Espinosa, H., Cuitiño-Mendiberry, M. N., Villadóniga, C., Castro‐Sowinski, S., Fló, M., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-88307-7 · Cited by 3

In‐solution structure and oligomerization of human histone deacetylase 6 – an integrative approach

Shukla, S., Komárek, J., Nováková, Z., Nedvědová, J., Ustinova, K., Vaňková, P., Kádek, A., Uetrecht, C., Mertens, H. D. T., & Bařinka, C. (2022) · FEBS Journal · doi:10.1111/febs.16616 · Cited by 3

Embedded in bone, but looking beyond: osteocalcin, epigenetics and ectopic bone formation (ASBMR 2014)

Johnson, R. W., & Sims, N. A. (2014) · IBMS BoneKEy · doi:10.1038/bonekey.2014.108 · Cited by 3

ITGB4 deficiency induces DNA damage by downregulating HDAC1 in airway epithelial cells under stress stimulation

Xu, K., Yao, Y., Liu, H., Yang, M., Yuan, L., Du, X., Yang, Y., Qin, L., Wang, W., Zhou, K., et al. (2022) · Pediatric Allergy and Immunology · doi:10.1111/pai.13871 · Cited by 3

Structures and dynamics of Rpd3S complex bound to nucleosome

Wang, C., Chen, C., Guo, Z., & Zhan, X. (2024) · Science Advances · doi:10.1126/sciadv.adk7678 · Cited by 2

HDAC1 is involved in the destabilization of the HSF2 protein under nonstress and stress conditions

Daupin, K., Dubreuil, V., Ahlskog, J. K., Verrico, A., Sistonen, L., Mezger, V., & de Thonel, A. (2025) · Cell Stress and Chaperones · doi:10.1016/j.cstres.2025.100079 · Cited by 3

Therapeutic Potential of HDAC Inhibitors in Neurodegenerative Diseases

Singh, A. K., Sudhan, Y. G., Chandana, S. L., Iyaswamy, A., & Durairajan, S. S. K. (2026) · Springer eBooks · doi:10.1007/978-981-95-6099-8_14 · Cited by 2

Unlocking Macrophage Secrets: Histone Deacetylases in Chronic Transplant Rejection

Hałasa, M., & Wawruszak, A. (2024) · Results and problems in cell differentiation · doi:10.1007/978-3-031-65944-7_12 · Cited by 2

Papillomavirus binding factor (PBF) is an intrinsically disordered protein with potential participation in osteosarcoma genesis, in silico evidence

Castillo-Juárez, P., Cetina-Corona, A., Méndez-Tenorio, A., Espinoza-Fonseca, L. M., & Barrón, B. L. (2014) · Theoretical Biology and Medical Modelling · doi:10.1186/1742-4682-11-51 · Cited by 2

HDAC inhibitors: A novel approach to hyperglycaemia management and treatment

Suchitra, M., Kusuma, P. K., Katagi, M. S., Venkateswarlu, G., & Mahalakshmi, P. (2023) · Health Sciences Review · doi:10.1016/j.hsr.2023.100137 · Cited by 3

Targeting the catalytic activity of HDAC1 in T cells protects against experimental autoimmune encephalomyelitisPreprint

Zhu, C., Stolz, V., Simonovic, N., Al-Rubaye, O., Vcelkova, T., Moos, V., Hess, L., Hagelkrüys, A., Madern, M., Reiter, W., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.14.536700 · Cited by 2

The ZNF512B-NuRD complex co-ordinates a neural-specific gene expression programPreprint

Francis, H., Tabar, M. S., Parsania, C., Feng, Y., Giardina, C., Ibrahim, O., Singh, K. P., Gupta, S. K., Schmitz, U., Rasko, J. E. J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.23.660971 · Cited by 2

Valproic Acid Accelerates Neural Outgrowth during Dorsal Root Ganglia Neurogenesis In Vitro

Wiens, D. J., Bergan, H. M., Walter, O. S., McGinley, A., & Ahlrichs, B. (2019) · Annals of Behavioral Neuroscience · doi:10.18314/abne.v2i1.1607 · Cited by 1

Peritoneal fluid stimulates neoplastic transformation of normal HEK 293 cells by high expression of pluripotent genes

Szabłowska‐Gadomska, I., Ducher, M., Orzechowska, M., Bogusławska-Duch, J., Kowalska, M., Poławska, H., & Małecki, M. (2018) · Polish Journal of Pathology · doi:10.5114/pjp.2018.79550 · Cited by 1

Histone Deacetylase Functions in Epidermal Development, Homeostasis and Cancer

Brennan-Crispi, D. M., & Millar, S. E. (2018) · Contributions to management science · doi:10.1007/978-3-319-16769-5_5 · Cited by 1

Histone Deacetylases (HDACs) maintain expression of the pluripotent gene network via recruitment of RNA polymerase II to coding and non-coding lociPreprint

Kelly, R., Stengel, K. R., Chandru, A., Johnson, L., Hiebert, S. W., & Cowley, S. M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.06.535398 · Cited by 1

PTSD: rewriting fearful memories

Haas, M. J. (2014) · Science-Business eXchange · doi:10.1038/scibx.2014.107

Mechanisms underlying the neuroprotective effects of histone deacetylase inhibitors

Durham, B. S. (2015) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York)

Elucidating the Biochemical and Structural Features Required for SMYD5 Mediated Methylation of Histone H4 and Other Potential Substrates

Mongeon, V. (2014) · uO Research (University of Ottawa) · doi:10.20381/ruor-3825

Enzyme and Protein Families that Regulate Histone Modifications and Crosstalk

Rutledge, C. E., & Turner, B. M. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782628484-00020

Generation of Tissue-Specific Mouse Models to Analyze HDAC Functions

Hagelkrüys, A., Moser, M. A., & Seiser, C. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6527-4_13

Transcription factor specificity protein 1 (Sp1) regulates the centrochromatin landscape and centromeric transcription during mitosis

Sowash, A., & Clifford, J. (2016) · iDEA - Drexel University Institutional Repository · doi:10.17918/etd-7146

Epigenetic and Nongenomic Roles for Histone Deacetylases in Heart Failure

Blakeslee, W. W., Tatman, P. D., & McKinsey, T. A. (2016) · Cardiac and vascular biology · doi:10.1007/978-3-319-41457-7_9

Analysis of transcriptional targets of SOX9 during embryonic heart valve development reveals a critical network of transcription factors

Garside, V. C. (2015) · cIRcle (University of British Columbia) · doi:10.14288/1.0220645

Studies Towards Broadening The Substrate Profile And Regulation Of Histone Deacetylase 1

Nalawansha, D. A. (2016) · Human Biology

Histone Deacetylase 3 Coordinates Heart Development Through Stage-Specific Roles in Cardiac Progenitor Cells

Lewandowski, S. L. (2016) · eScholarship@UMassChan · doi:10.13028/m26p4d

Novel Tripartite Motif Containing 22 Interactions in the Context of Very Early Onset Inflammatory Bowel Disease

Hossain, K. (2018) · TSpace (University of Toronto)

Targeting histone modifications in psychotic disorders

Peedicayil, J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-816422-8.00012-x

The clinical landscape of HDAC inhibitors

Ganesan, A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-823928-5.00036-0

Genetic and functional analysis of rat mammary cancer susceptibility.

Duderstadt, E. L. (2021) · ThinkIR: The University of Louisville's Institutional Repository (University of Louisville) · doi:10.18297/etd/3628

Faculty Opinions recommendation of Systematic chemical and molecular profiling of MLL-rearranged infant acute lymphoblastic leukemia reveals efficacy of romidepsin.

Hunger, S. P., & Green, A. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.726574059.793537563

Reviewer #3 (Public Review): Comparative Interactome Analysis of α-arrestin Families in Human and Drosophila

(2023) · eLife · doi:10.7554/elife.88328.2.sa0

Comparative Interactome Analysis of α-arrestin Families in Human and DrosophilaPreprint

‍Lee, K.-T., Pranoto, I. K. A., Kim, S., Choi, H., To, N. B., Chae, H., Lee, J., Kim, J., Kwon, Y. V., & Nam, J. (2023) · eLife · doi:10.7554/elife.88328.2

Author Response: Comparative Interactome Analysis of α-arrestin Families in Human and Drosophila

‍Lee, K.-T., Pranoto, I. K. A., Kim, S., Choi, H., To, N. B., Chae, H., Lee, J., Kim, J., Kwon, Y. V., & Nam, J. (2023) · eLife · doi:10.7554/elife.88328.3.sa4

Reviewer #1 (Public Review): Comparative Interactome Analysis of α-arrestin Families in Human and Drosophila

(2023) · eLife · doi:10.7554/elife.88328.3.sa2

eLife Assessment: Comparative Interactome Analysis of α-arrestin Families in Human and Drosophila

Choi, M. (2023) · eLife · doi:10.7554/elife.88328.3.sa3

Reviewer #2 (Public Review): Comparative Interactome Analysis of α-arrestin Families in Human and Drosophila

(2023) · eLife · doi:10.7554/elife.88328.3.sa1

Glioblastoma

Paul, D., & Barhoi, D. (2023) · Advances in bioinformatics and biomedical engineering book series · doi:10.4018/978-1-6684-9675-6.ch014

Chemoproteomics Sheds Light on Epigenetic Targets of [11C]Martinostat in the Human Brain

Catanese, M. C., Klingl, Y. E., Gilbert, T. M., Strebl, M. G., Hartigan, C. R., Schenone, M., & Hooker, J. M. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00781

Targeted Protein Degradation of Metalloenzymes

O’Herin, C., & Cohen, S. M. (2025) · Wiley eBooks · doi:10.1002/0471266949.bmc303

Hispidulin: a potential alternative to vorinostat against HDAC1 for acute myeloid leukemia

Balaji, S., Anbarasu, S., Ramaiah, S., & Anbarasu, A. (2025) · Discover Oncology · doi:10.1007/s12672-025-03182-y

HDAC2 inhibition restores H4K16ac and delays senescence in HGPS VSMCsPreprint

Karimpour, R., Ngubo, M., Stanford, W. L., & Hendzel, M. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.07.687234

Kinetic Analysis of HDAC‐ and Sirtuin‐Mediated Deacylation on Chemically Defined Histones and Nucleosomes

Niu, Z. L., Zhang, L., Zhou, Y., & Wang, Z. A. (2025) · Current Protocols · doi:10.1002/cpz1.70251

Pervasive binding of the stem cell transcription factor SALL4 shapes the chromatin landscapePreprint

Chhatbar, K., Giuliani, S., Quante, T., Alexander-Howden, B., Selfridge, J., Guy, J., Auchynnikava, T., Spanos, C., Mathieson, T., Sanguinetti, G., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.14.688441

Étude de l’interaction physique et fonctionnelle entre le complexe histone méthyltransférase SET-2/SET1 et le complexe histone déacétylase SIN-3S dans l’embryon de C. elegans

Beurton, F. (2018) · theses.fr (ABES) · doi:10.70675/7b849740z180fz4592za622zc7e30bc46cf1

Caractérisation de protéines nucléaires ciblées par la bactérie pathogène Listeria monocytogenes

Pourpre, R. (2019) · theses.fr (ABES) · doi:10.70675/3e0b933ez114cz48e2zae8dzabf6fa8d37b1

Etude structurale du complexe de remodelage de la chromatine NuRD et sa sous-unité MBD3 liée à l'ADN

Tabaroni, R. (2018) · theses.fr (ABES) · doi:10.70675/7ad702abz74c7z45a9z9ecdz6aff4ba871ad

The role of histone deacetylase 3 (HDAC3) during megakaryopoiesis

Ishaq, R. (2020) · theses.fr (ABES) · doi:10.70675/08096a2ez3ccaz4219za256zfb0a9d758e0e

Homeobox transcription factor MSX2 down-regulates ERα action to facilitate anti-estrogensensitivity in ERα+ breast cancerPreprint

Feng, J., Zeng, K., Wang, A., Sun, H., Jin, Z., Jin, Z., Feng, S., Sun, X., Bai, Y., He, M., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.12.731842

BindingDB Entry 50016954: Glioblastoma: Current Status, Emerging Targets, and Recent Advances.

BindingDB (2023) · UC San Diego · doi:10.7270/q2d79gfs

BindingDB Entry 50013364: Thirty Years of HDAC Inhibitors: 2020 Insight and Hindsight.

BindingDB (2022) · UC San Diego · doi:10.7270/q2f76h9k

Analysis of the Developmental and Physiological Roles of Histone Deacetylases 1 and 2

Dovey, O. M. (2012) · Figshare

Investigating the physiological role of HDAC1 and HDAC2 in embryonic stem cells

Jamaladdin, S. (2016) · Figshare

Effects of catalytic inactivation of HDAC1 on skin homeostasis and immunity

Wagner, S. P. K. (2022) · University of Vienna · doi:10.25365/thesis.72494

Histone deacetylase (HDAC) 1 and 2 are essential for normal T cell development and genomic stability in mice

Dovey, O. M., Vasilliou, G. S., Bradley, A., & Cowley, S. M. (2013) · Clinical Epigenetics · doi:10.1186/1868-7083-5-s1-s11 · Cited by 7

Trans-regulation of Histone Deacetylase Activities through Acetylation

Luo, Y., Jian, W., Stavreva, D. A., Fu, X., Hager, G. L., Bungert, J., Huang, S., & Qiu, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.038356 · Cited by 80