Enzymatic Activity Associated with Class II HDACs Is Dependent on a Multiprotein Complex Containing HDAC3 and SMRT/N-CoR

Crystal structure of the nucleosome core particle at 2.8 Å resolution

Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466

Current protocols in molecular biology

Sargent, T. (1988) · Analytical Biochemistry · doi:10.1016/0003-2697(88)90147-9 · Cited by 7,281

Histone acetylation in chromatin structure and transcription

Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884

The coregulator exchange in transcriptional functions of nuclear receptors

Glass, C. K., & Rosenfeld, M. G. (2000) · Genes & Development · doi:10.1101/gad.14.2.121 · Cited by 2,233

Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor

Hörlein, A., Näär, A. M., Heinzel, T., Torchia, J., Gloss, B. R., Kurokawa, R., Ryan, A. K., Kamei, Y., Söderström, M., Glass, C. K., et al. (1995) · Nature · doi:10.1038/377397a0 · Cited by 2,072

Twenty-Five Years of the Nucleosome, Fundamental Particle of the Eukaryote Chromosome

Kornberg, R. D., & Lorch, Y. (1999) · Cell · doi:10.1016/s0092-8674(00)81958-3 · Cited by 1,833

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

Histone acetylation and transcriptional regulatory mechanisms

Struhl, K. (1998) · Genes & Development · doi:10.1101/gad.12.5.599 · Cited by 1,815

Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors

Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714

Tumor necrosis factor alpha and interleukin 1 stimulate the human immunodeficiency virus enhancer by activation of the nuclear factor kappa B.

Osborn, L., Kunkel, S. L., & Nabel, G. J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.7.2336 · Cited by 1,583

A critical analysis of the (near) legendary status of vitamin D

McMillan, A. N., Hicks, J., Isabella, C., & Higa, G. M. (2011) · Expert Review of Endocrinology & Metabolism · doi:10.1586/eem.11.81 · Cited by 5

Synthesis of thiazolyl-based hydroxamic acids as histone deacetylase inhibitors

Asfaha, Y., Skerhut, A. J., Avelar, L. A. A., Horstick‐Muche, N., Lungerich, B., Klinken, S., Kassack, M. U., & Kurz, T. (2020) · ARKIVOC · doi:10.24820/ark.5550190.p011.279 · Cited by 5

Structure-Based Identification of Novel Histone Deacetylase 4 (HDAC4) Inhibitors

Agarwal, R., Pattarawat, P., Duff, M. R., Wang, H. R., Baudry, J. Y., & Smith, J. C. (2024) · Pharmaceuticals · doi:10.3390/ph17070867 · Cited by 5

Editorial: Epigenetics in Systemic Sclerosis

Lafyatis, R. (2016) · Arthritis & Rheumatology · doi:10.1002/art.39830 · Cited by 5

Salt-inducible Kinase Regulation of Adipose Tissue Metabolism

Shi, F., Agrawal, V., McKinsey, T. A., & Collins, S. (2025) · Endocrinology · doi:10.1210/endocr/bqaf092 · Cited by 4

Neuronal HDAC9: A key regulator of cognitive and synaptic aging, rescuing Alzheimer’s disease-related phenotypes

Lei, Y., Chen, Y., Guo, M., Patel, F., Bai, Y., Goo, B. M. S. S., Du, Q., Weintraub, N. L., & Lu, X. (2026) · Molecular Psychiatry · doi:10.1038/s41380-026-03556-w · Cited by 5

Role of human Myocyte Enhancer Factor 2 (MEF2) proteins in cancer: structural insights, functional diversity, and regulatory mechanisms

Khandelwal, A., Fathi, A. H., Shetty, S., Mukhopadhyay, A., Devi, V., & Kabekkodu, S. P. (2025) · Cancer Cell International · doi:10.1186/s12935-025-03995-5 · Cited by 5

Molecular Structure and Function of Zinc-Dependent Histone Deacetylases

Christianson, D. W. (2026) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051424-053005 · Cited by 4

Deciphering the roles of subcellular distribution and interactions involving the MEF2 binding region, the ankyrin repeat binding motif and the catalytic site of HDAC4 in Drosophila neuronal morphogenesis

Tan, W. J., Hawley, H. R., Wilson, S. J., & Fitzsimons, H. L. (2024) · BMC Biology · doi:10.1186/s12915-023-01800-1 · Cited by 4

Upregulation of HDAC3 mediates behavioral impairment in the bile duct ligation model of hepatic encephalopathy

Gupta, S., Rishi, V., Elipilla, P., & Aggarwal, A. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.141596 · Cited by 4

Approaches for Studying the Subcellular Localization, Interactions, and Regulation of Histone Deacetylase 5 (HDAC5)

Guise, A. J., & Cristea, I. M. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3667-0_5 · Cited by 4

Present and future perspectives for targeting histone modifications in therapy

Camilo, V., & Jerónimo, C. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-816422-8.00018-0 · Cited by 4

Design, synthesis and biological evaluation of selective histone deacetylase 6 (HDAC6) inhibitors bearing benzoindazole or pyrazoloindazole scaffold as surface recognition motif

Xu, Q., Mou, Y., Wang, S., Gao, X., Zhang, Y., Wang, Z., Xu, X., Han, Y. K., Jia, W., Zhang, M., et al. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104910 · Cited by 4

Epigenetic regulation of T cell lineages in skin and blood following hematopoietic stem cell transplantation

Pandey, R. V., Strobl, J., Redl, A., Unterluggauer, L., Gail, L. M., Kleißl, L., Müller, S., Atzmüller, D., Fife, V. E. R., Krausgruber, T., et al. (2023) · Clinical Immunology · doi:10.1016/j.clim.2023.109245 · Cited by 4

The Biology of HDAC3

Seto, E. (2006) · Humana Press eBooks · doi:10.1385/1-59745-024-3:61 · Cited by 4

Cloning, expression, and biochemical characterization of a new histone deacetylase-like protein from Thermus caldophilus GK24

Song, Y., Kim, Y. S., Kim, D., Lee, D., & Kwon, H. J. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.147 · Cited by 4

Protein Acetylation as an Integral Part of Metabolism in Cancer Development and Progression

Čuperlović‐Culf, M., & Culf, A. S. (2014) · 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

Not Just for Muscle Anymore: Activity and Calcium Regulation of MEF2-Dependent Transcription in Neuronal Survival and Differentiation

Shalizi, A., & Bonni, A. (2007) · Springer eBooks · doi:10.1007/978-0-387-73609-9_12 · Cited by 4

Structural Biology of Epigenetic Targets

Romier, C., Wurtz, J., Renaud, J., & Cavarelli, J. (2009) · Methods and principles in medicinal chemistry · doi:10.1002/9783527627073.ch2 · Cited by 4

HDAC7 influences ER-⍺ transcription via NCoR-HDAC3 dissociation

Kodikara, I. K. M., Nwanelo, V. O., Belanger, A. K., & Pflum, M. K. H. (2025) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2025.141083 · Cited by 3

N-terminal oligomerization drives HDAC4 nuclear condensation and neurodevelopmental dysfunction in Drosophila

Hawley, H. R., Sutherland‐Smith, A. J., Savoian, M. S., & Fitzsimons, H. L. (2025) · Open Biology · doi:10.1098/rsob.250095 · Cited by 2

The transposon-driven evolutionary origin and basis of histone deacetylase functions and limitations in disease prevention

Peek, G. W., & Tollefsbol, T. O. (2011) · Clinical Epigenetics · doi:10.1007/s13148-011-0020-z · Cited by 3

Current Status of Healthy Human Skin Models: Can Histone Deacetylase Inhibitors Potentially Improve the Present Replacement Models?

Lemper, M., Snykers, S., Vanhaecke, T., Paépe, K. D., & Rogiers, V. (2013) · Skin Pharmacology and Physiology · doi:10.1159/000351363 · Cited by 3

The Class IIa Histone Deacetylases

Kasler, H. G., & Verdin, E. M. (2006) · Humana Press eBooks · doi:10.1385/1-59745-024-3:129 · Cited by 4

DNA Methylation and Histone Deacetylation: Interplay and Combined Therapy in Cancer

Qiu, Y., Shabashvili, D., Li, X., Kumari, P., Chen, M., & Zajac‐Kaye, M. (2012) · InTech eBooks · doi:10.5772/35977 · Cited by 3

Transcriptional repression by the thyroid hormone receptor: function of corepressor complexes

Stewart, M. D., & Wong, J. (2004) · Current Opinion in Endocrinology & Diabetes · doi:10.1097/01.med.0000137761.03533.19 · Cited by 3

HATs and HDACs

Bolger, T. A., Cohen, T., & Yao, T. (2007) · Springer eBooks · doi:10.1007/978-0-387-40049-5_6 · Cited by 4

Resolving the Deceptive Isoform and Complex Selectivity of HDAC1/2 InhibitorsPreprint

Mazitschek, R., & Payne, N. C. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3960267 · Cited by 3

Recommended Tool Compounds: Isoform- and Class-Specific Histone Deacetylase Inhibitors

Schäker‐Hübner, L., & Hansen, F. K. (2026) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00619 · Cited by 3

Histone deacetylase enzyme activity is not the universal anticancer target of HDAC inhibitors

Rai, C., Ruan, H., Li, X., Li, W., Jeong, H.-H., Song, C., Liu, P., Chang, Y., Fang, H., Udhaya Kumar., S., et al. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02698-1 · Cited by 2

Passport control for foreign integrated DNAs

Palmisano, I., Chiara, G. D., Schiaffino, M. V., & Poli, G. (2012) · Mobile Genetic Elements · doi:10.4161/mge.22610 · Cited by 2

The Role of Histone Deacetylase Inhibition in the Accumulation and Stability of Disease-Related Proteins

Thomas, E. A. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805420-8.00007-x · Cited by 2

Design and synthesis of peptides as stabilizers of histone deacetylase 4

Lill, A., Schweipert, M., Nehls, T., Wurster, E., Lermyte, F., Meyer‐Almes, F., & Schmitz, K. (2024) · Journal of Peptide Science · doi:10.1002/psc.3603 · Cited by 2

Histone/protein deacetylase 3 dictates critical aspects of regulatory T cell development and function

Singer, B. D., & D’Alessio, F. R. (2015) · Cellular and Molecular Immunology · doi:10.1038/cmi.2015.51 · Cited by 2

The Role of Histone Deacetylases in Neurodegenerative Diseases and Small-Molecule Inhibitors as a Potential Therapeutic Approach

Bürli, R. W., Thomas, E. A., & Beaumont, V. (2010) · Topics in medicinal chemistry · doi:10.1007/7355_2010_10 · Cited by 2

Promotion of Anchorage-independent Growth by Cytoplasmic and Nuclear Histone Deacetylase 9

Yura, T., Hashizume, H., Suzuki, E., Imagawa, M., & Osada, S. (2010) · Eisei kagaku · doi:10.1248/jhs.56.581 · Cited by 2

Epigenomic adaptations of exercise in the control of metabolic disease and cancer

Dimauro, I., Paronetto, M. P., & Caporossi, D. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816843-1.00018-7 · Cited by 2

Acetylation and Methylation in Asthma, COPD, and Lung Cancer

Zwinderman, M. R. H., Cao, F., & Dekker, F. J. (2019) · Topics in medicinal chemistry · doi:10.1007/7355_2019_81 · Cited by 2

The Role of Epigenetics in Cardiovascular Disease

Zhou, B., Margariti, A., & Xu, Q. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-388415-2.00020-2 · Cited by 2

Epigenetics in exercise science and sports medicine

Schenk, A., Proschinger, S., & Zimmer, P. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-823928-5.00005-0 · Cited by 2

Histone Deacetylase Inhibitors: A Novel Therapeutic Approach for Cognitive Disorders

Labrie, V. (2011) · Springer eBooks · doi:10.1007/978-3-642-17426-1_12 · Cited by 2

Epigeneticmechanisms in drug addiction and depression

Renthal, W. R., & Nestler, E. J. (2012) · Cambridge University Press eBooks · doi:10.1017/cbo9781139025997.009 · Cited by 2

Epigenetic Targets in Drug Discovery: Cell‐Based Assays for HDAC Inhibitor Hit Validation

Jung, M., Yong, K., Velena, A., & Lee, S. (2009) · Methods and principles in medicinal chemistry · doi:10.1002/9783527627073.ch6 · Cited by 2

Temporal and Spatial Regulation of Histone Deacetylase-7 and β-Catenin in Endothelial Cells

Hui, S., Brunt, K. R., & Husain, M. (2010) · Circulation Research · doi:10.1161/circresaha.110.219345 · Cited by 2

Epigenetic regulation of general anesthesia-induced neonatal neurodegeneration

Jia, M., Ji, M., & Yang, J. (2017) · Oncotarget · doi:10.18632/oncotarget.14568 · Cited by 2

Class IIa HDACs in myelination

Velasco-Avilés, S., Gomez-Sanchez, J. A., & Cabedo, H. (2018) · Aging · doi:10.18632/aging.101443 · Cited by 2

Investigating the role of the mesoderm induction early response (MIER) family members as transcriptional co-repressors

Derwish, R. (2019) · Memorial University Research Repository (Memorial University) · Cited by 2

Turtle anoxia : biochemistry and gene regulation in an anaerobic extremist

Krivoruchko, A. (2010) · doi:10.22215/etd/2010-09691 · Cited by 2

1,3,5-Triazine Based Hydroxamic Acid Analogues as HDAC Inhibitors: Integrated Modelling by 3D QSAR, Hypogen Pharmacophore Based Virtual Screening and Molecular Dynamic Simulation StudiesPreprint

Patel, P., Navneesh, N., Kurmi, B. D., Rangra, N. K., Gupta, G. D., Rawat, R., Pagano, M. A., Brunati, A. M., & Rajak, H. (2023) · Research Square · doi:10.21203/rs.3.rs-2892636/v1 · Cited by 2

HDAC4 suppresses porcine epidemic diarrhea virus infection through negatively regulating MEF2A-GLUT1/3 axis- mediated glucose uptake

Wang, X., Wang, L., Li, D., Liu, Y., Shang, Q., Liu, Y., Zhang, L., Xu, Z., Huang, C., & Song, C. (2025) · Veterinary Microbiology · doi:10.1016/j.vetmic.2025.110520 · Cited by 1

Impact of Histone Acetyltransferases and Histone Deacetylases on Adult Brain Myelin Plasticity

Dominicis, A., Fabiano, T., Peria, S., Jaf, A. I. A. A., & Ragnini‐Wilson, A. (2025) · Results and problems in cell differentiation · doi:10.1007/978-3-031-91459-1_8 · Cited by 1

The multifactorial role of HDAC9 at the maternal–fetal interface in the pathogenesis of preeclampsia

Opichka, M. A., McIntosh, J. J., & Grobe, J. L. (2025) · Clinical Science · doi:10.1042/cs20242385 · Cited by 1

In vitro characterization of the catalytic domain of human histone deacetylase 5

Mammen, C., Hornung, F. M., Anzenhofer, C., Schumacher, J., Reiners, J., Li, J., Mazzone, F., Bilsing, F. L., Kassack, M. U., Kurz, T., et al. (2026) · Scientific Reports · doi:10.1038/s41598-026-37633-5 · Cited by 1

HDAC inhibition via suberoylanilide hydroxamic acid ameliorates doxorubicin-induced cardiotoxicity

Eksi, B., Finke, D., Michel, S., Brauer, J., Heckmann, M. B., Valadan, M., Schanze, L. M., Sunder, V., Steimel, K., Burhenne, J., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-77428-w · Cited by 1

A Tale of Two Epiphenomena: The Complex Interplay of Epigenetics and Epilepsy

Beth, S. T., & Jane, A. V. A. (2011) · InTech eBooks · doi:10.5772/24529 · Cited by 1

Inhibition of proliferation induced by anti-sense RNA of HDAC1 in MCF-7 cells

Cao (2009) · Molecular Medicine Reports · doi:10.3892/mmr_00000166 · Cited by 1

HDAC3-dependent Reversible Lysine Acetylation of Cardiac Myosin Heavy Chain Isoforms Modulates Their Enzymatic and

Samant, S. A., Courson, D. S., Sundaresan, N. R., Pillai, V. B., Tan, M., Zhao, Y., Shroff, S. G., Rock, R. S., Gupta, M. P., & DepartmentofSurgery, F. ‡. (2011) · Cited by 1

Assembly and Regulation of Nuclear Receptor Corepressor Complexes

Millard, C. J., & Schwabe, J. W. R. (2015) · Springer eBooks · doi:10.1007/978-3-319-18729-7_9 · Cited by 1

Histone Deacetylases in Cardiovascular Development and Disease

Young, B. D., & Olson, E. N. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-381332-9.00032-3 · 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

Class I histone deacetylase inhibition by aryl butenoic acid derivatives: In silico and in vitro studies

Bora, G., Sarı, S., Önel, G. T., Dalkara, S., & Erdem‐Yurter, H. (2019) · Journal of Research in Pharmacy · doi:10.35333/jrp.2019.42 · Cited by 1

Gene Regulation by Nuclear Calcium and Its Antagonism by NMDAR/TRPM4 Signaling

Pruunsild, P., Bengtson, C. P., Yan, J., Bading, H., & Hagenston, A. M. (2024) · Springer eBooks · doi:10.1007/978-3-031-68550-7_4 · Cited by 1

Metabolic Regulation of Liver Regeneration

Rudnick, D. A., & Huang, J. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-420128-6.00015-4 · Cited by 1

SREBP2 AND REVERB-ALPHA REGULATION OF HUMAN CYP8B1

Feng, H. (2009) · OhioLink ETD Center (Ohio Library and Information Network) · Cited by 1

Function of the CHD4/Mi-2ß chromatin remodelling ATPase during neural development of Xenopus laevis

Nieberler, M. (2012) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.13954 · Cited by 1

The Role of Histone Deacetylases in Cytokine Regulation in Human Gestational Tissues

Munro, S. K. (2013) · ResearchSpace (University of Auckland) · Cited by 1

Uncovering the interplay between epigenome editing efficiency and sequence context using a novel inducible targeting systemPreprint

Yang, B., Borgeaud, A. C., Aeschbach, L., & Dion, V. (2018) · ORCA Online Research @Cardiff (Cardiff University) · doi:10.1101/368480 · Cited by 1

HDAC class IIa expression and regulation in human endometrial tissues and stromal cells during the menstrual cyclePreprint

Gujral, P., Mahajan, V., & Ponnampalam, A. P. (2022) · Research Square · doi:10.21203/rs.3.rs-1355984/v1 · Cited by 1

Expanding the HDAC druggable landscape beyond enzymatic activityPreprint

Olivet, J., Choi, S. G., Sierra, S., O’Grady, T. M., Revenga, M. D. L. F., Laval, F., Botchkarev, V. V., Gorgulla, C., Coote, P. W., Blavier, J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.07.519454 · Cited by 1

Regulation of Muscle Gene Expression by Histone Deacetylases

McKinsey, T. A., & Olson, E. N. (2006) · Humana Press eBooks · doi:10.1385/1-59745-024-3:107 · Cited by 1

The role of class I histone deacetylases in cardiac development of chicken embryos

Engelmaier, C. (2011) · University of Vienna · doi:10.25365/thesis.15429

Nuclear receptor co-repressor functions in prostate cancer; in vitro, in vivo and in silico approaches

Battaglia, S. (2010) · University of Birmingham Institutional Research Archive (University of Birmingham)

Characterization of HDAC4's role in brain

Darcy, M. (2010)

Histone deacetylase 3 and histone deacetylase 7 Have opposite effects on osteoclast differentiation.

Romsa, A. M. (2010) · University of Minnesota Digital Conservancy (University of Minnesota)

The regulation of osteoclastogenesis by bone morphogenetic proteins, twisted gastrulation, and histone deacetylases.

Pham, L. (2012) · University of Minnesota Digital Conservancy (University of Minnesota)

Human histone deacetylase 1: Mutagenesis and small molecule studies

Wambua, M. K. (2013)

Cellular Adaptation of Macrophages to Anthrax Lethal Toxin-Induced Pyroptosis via Epigenetic Mechanisms

Han, C. Y. (2013) · Scholarship@Western (Western University)

Aktueller Stand der Modelle gesunder menschlicher Haut: Können Histon-Deacetylase-Inhibitoren die derzeitigen Ersatzmodelle verbessern?

Lemper, M., Snykers, S., Vanhaecke, T., Paépe, K. D., & Rogiers, V. (2014) · Kompass Dermatologie · doi:10.1159/000356994

Anti-histone acetyltransferase activity from aloe inhibits androgen receptor-dependent prostate cancer cell growth

Jeong, M.-G., Lee, Y., Kim, M., Jeong, S.-I., Choi, K., & Yoon, H. (2008) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2008.07.1742

Smooth Muscle Cell Differentiation from Embryonic Stem Cells: Role of HDAC7 and PDGF-BB

Sims, D., & Xiao, Q. (2011) · Springer eBooks · doi:10.1007/978-94-007-2828-8_7

An Overview of Epigenetic Mechanisms in Health and Disease

Westerland, C., & Karagiannis, T. C. (2014) · Springer eBooks · doi:10.1007/978-1-4939-0706-9_3

CaMKII : do not work too hard in the failing heart

Liu, M., Li, Y., & Chen, R. (2015) · The Journal of Pathology · doi:10.1002/path.4507

Functions of the coregulator protein SNURF (RNF4) in transcription and cell growth

Häkli, M. (2005) · Työväentutkimus Vuosikirja

Regulation of Nox4 expression by histone deacetylases in human endothelial cells: involvement of epigenetic mechanisms

der Naturwissenschaften, D. (2013)

MOLECULAR DETERMINANTS OF ANDROGEN ACTION

Santti, H. (2004) · Työväentutkimus Vuosikirja

KUOPION YLIOPISTON JULKAISUJA C. LUONNONTIETEET JA YMPÄRISTÖTIETEET 246 KUOPIO UNIVERSITY PUBLICATIONS C. NATURAL AND ENVIRONMENTAL SCIENCES 246

Saramäki, A. (2008)

Role of Signal-responsive Class IIa Histone Deacetylases in Regulating Neuronal Activity-dependent Gene Expression

Lam, B., & Chawla, S. (2007) · Springer eBooks · doi:10.1007/978-0-387-73609-9_9

Histone deacetylase inhibition-mediated cytotoxicity of oligodendrocytes.

Dincman, T. A. (2011) · ThinkIR: The University of Louisville's Institutional Repository (University of Louisville) · doi:10.18297/etd/351

Elucidation of the Histone Deacetylase 6 Pharmacophore

Kalin, J. H. (2012) · Figshare

Mechanisms underlying the regulation and functions of HDAC7.

Gao, C. (2008) · OhioLink ETD Center (Ohio Library and Information Network)

Part 1 Synthesis of a potent histone deacetylase inhibitor; Part 2 Studies towards a stabilized helix-turn-helix peptide

Liu, T. (2007) · VTechWorks (Virginia Tech)

Rôle de l’acétylation/déacétylation des histones dans la régulation de l’expression des gènes de la COX-2, iNOS et mPGES-1 dans les tissus articulaires

Chabane, N. (2012) · doi:10.71781/29709

The Actions of the Vitamin D Receptor in Health and Malignancy; Polymorphic Associations and Gene Regulatory Actions

Campbell, M. J., & Colston, K. W. (2006) · CRC Press eBooks · doi:10.1201/9781420004847-8

Epigenetics and Cardiovascular Disease

Marı́n-Garcı́a, J. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-404599-6.00022-6

The molecular pathogenesis of skeletal muscle atrophy

Bongers, K. S., Shibata, E. F., Snyder, P. M., Zabner, J., Moye-Rowley, S., Adams, C. M., & Henry, M. D. (2016) · doi:10.17077/etd.n2myp7k9

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

Heterochromatin effects in Friedreich's ataxia and sexual dimorphism

Yandım, C. (2012) · Spiral (Imperial College London) · doi:10.25560/9644

HDAC Signaling Networks in Heart Failure

Kronlage, M., Katus, H. A., & Backs, J. (2016) · Cardiac and vascular biology · doi:10.1007/978-3-319-41457-7_8

Epigenetic repression of the NFATc1 transcription factor in human lymphomas

Akimzhanov, A. M. (2005) · Online Publication Service of Würzburg University (Würzburg University)

The SMRT and N-CoR Corepressors Are Activating Cofactors for Histone Deacetylase 3

Guenther, M. G., Barak, O., & Lazar, M. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.18.6091-6101.2001 · Cited by 611

Human HDAC7 Histone Deacetylase Activity Is Associated with HDAC3in Vivo

Fischle, W., Dequiedt, F., Fillion, M., Hendzel, M. J., Voelter, W., & Verdin, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104935200 · Cited by 232

Insights into the Recruitment of Class IIa Histone Deacetylases (HDACs) to the SMRT/NCoR Transcriptional Repression Complex

Hudson, G. M., Watson, P. J., Fairall, L., Jamieson, A. G., & Schwabe, J. W. R. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.661058 · Cited by 58

Mutagenesis Study Reveals the Rim of Catalytic Entry Site of HDAC4 and -5 as the Major Binding Surface of SMRT Corepressor

Kim, G. S., Jung, H.-E., Kim, J., & Lee, Y. C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0132680 · Cited by 8

Structural basis of the specific interaction of SMRT corepressor with histone deacetylase 4

Park, S., Kim, G. S., Hwang, H.-J., Nam, T.-H., Park, H.-S., Song, J., Jang, T.-H., Lee, Y. C., & Kim, J. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky926 · Cited by 36