Cited by 697Histone Deacetylase Inhibitors ResearchGenomics and Chromatin DynamicsEpigenetics and DNA Methylation

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HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics

Gallinari, Paola, Marco, Stefania Di, Jones, Phillip, Pallaoro, Michele, Steinkühler, Christian·2007·Cell Research

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Abstract

Histone deacetylases (HDACs) and histone acetyl transferases (HATs) are two counteracting enzyme families whose enzymatic activity controls the acetylation state of protein lysine residues, notably those contained in the N-terminal extensions of the core histones. Acetylation of histones affects gene expression through its influence on chromatin conformation. In addition, several non-histone proteins are regulated in their stability or biological function by the acetylation state of specific lysine residues. HDACs intervene in a multitude of biological processes and are part of a multiprotein family in which each member has its specialized functions. In addition, HDAC activity is tightly controlled through targeted recruitment, protein-protein interactions and post-translational modifications. Control of cell cycle progression, cell survival and differentiation are among the most important roles of these enzymes. Since these processes are affected by malignant transformation, HDAC inhibitors were developed as antineoplastic drugs and are showing encouraging efficacy in cancer patients.

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BindingDB Entry 50039943: Synthesis and biological evaluation of 1-arylsulfonyl-5-(N-hydroxyacrylamide)indoles as potent histone deacetylase inhibitors with antitumor activity in vivo.
BindingDB (2013) · UC San Diego · doi:10.7270/q2cr5vd7
BindingDB Entry 50031707: Synthesis and biological activity of cyclotetrapeptide analogues of the natural HDAC inhibitor FR235222.
BindingDB (2010) · UC San Diego · doi:10.7270/q2bc3zp6
BindingDB Entry 50010003: Development of a Potent and Selective HDAC8 Inhibitor.
BindingDB (2021) · UC San Diego · doi:10.7270/q2qc0718
BindingDB Entry 50038154: Histone deacetylase inhibitors: from bench to clinic.
BindingDB (2012) · UC San Diego · doi:10.7270/q2m32wmt
BindingDB Entry 50040763: Rapid discovery of highly potent and selective inhibitors of histone deacetylase 8 using click chemistry to generate candidate libraries.
BindingDB (2013) · UC San Diego · doi:10.7270/q25x2b3q
BindingDB Entry 50046743: New macrocyclic analogs of the natural histone deacetylase inhibitor FK228; design, synthesis and preliminary biological evaluation.
BindingDB (2016) · UC San Diego · doi:10.7270/q21n82xf
BindingDB Entry 50008254: Systematically Mitigating the p38α Activity of Triazole-based BET Inhibitors.
BindingDB (2021) · UC San Diego · doi:10.7270/q2h998kq
BindingDB Entry 50023137: Design, Synthesis, and Biological Evaluation of Novel Fms-Like Tyrosine Kinase 3/VEGFR2/Histone Deacetylase Inhibitors for the Treatment of Acute Myeloid Leukemia.
BindingDB (2026) · UC San Diego · doi:10.7270/q21c22r5
BindingDB Entry 50027491: Studies of the metabolic stability in cells of 5-(trifluoroacetyl)thiophene-2-carboxamides and identification of more stable class II histone deacetylase (HDAC) inhibitors.
BindingDB (2010) · UC San Diego · doi:10.7270/q2v987xh
BindingDB Entry 50045746: Macrocyclic compounds as anti-cancer agents: design and synthesis of multi-acting inhibitors against HDAC, FLT3 and JAK2.
BindingDB (2016) · UC San Diego · doi:10.7270/q2cz38ws
BindingDB Entry 50020302: Selective HDAC3 Inhibitors with Potent In Vivo Antitumor Efficacy against Triple-Negative Breast Cancer.
BindingDB (2024) · UC San Diego · doi:10.7270/q2s46xfd
BindingDB Entry 50017485: Development of Alkylated Hydrazides as Highly Potent and Selective Class I Histone Deacetylase Inhibitors with T cell Modulatory Properties.
BindingDB (2023) · UC San Diego · doi:10.7270/q2959nmg
BindingDB Entry 50002419: Indole in the target-based design of anticancer agents: A versatile scaffold with diverse mechanisms.
BindingDB (2020) · UC San Diego · doi:10.7270/q2x92dxx
BindingDB Entry 50021808: Leveraging a rationally designed veliparib-based anilide eliciting anti-leukemic effects for the design of pH-responsive polymer nanoformulation.
BindingDB (2025) · UC San Diego · doi:10.7270/q2mk6jj4
BindingDB Entry 7762: The antiparasitic clioquinol induces apoptosis in leukemia and myeloma cells by inhibiting histone deacetylase activity.
BindingDB (2017) · UC San Diego · doi:10.7270/q2668c1k
BindingDB Entry 50046204: Design, synthesis and biological evaluation of 4-anilinothieno[2,3-d]pyrimidine-based hydroxamic acid derivatives as novel histone deacetylase inhibitors.
BindingDB (2016) · UC San Diego · doi:10.7270/q2vq34f7
BindingDB Entry 50032896: Structure and property based design, synthesis and biological evaluation of¿-lactam based HDAC inhibitors.
BindingDB (2011) · UC San Diego · doi:10.7270/q28k79c8
BindingDB Entry 50005744: Design, synthesis and biological evaluation of di-substituted cinnamic hydroxamic acids bearing urea/thiourea unit as potent histone deacetylase inhibitors.
BindingDB (2020) · UC San Diego · doi:10.7270/q24f1tpm
BindingDB Entry 50007155: Identification of novel quinazoline derivatives as potent antiplasmodial agents.
BindingDB (2021) · UC San Diego · doi:10.7270/q21v5j76
BindingDB Entry 50027517: Identification of KD5170: a novel mercaptoketone-based histone deacetylase inhibitor.
BindingDB (2010) · UC San Diego · doi:10.7270/q2f18zjs
Discriminating malignancy of pulmonary nodules using a peripheral blood leukocyte DNA methylation-based SEMO network model
Huang, B., Shen, L., Hu, F., Zhou, J., Song, X., Dong, Z., Wu, J., Fu, H., Feng, J., Yang, Z., et al. (2026) · Frontiers in Oncology · doi:10.3389/fonc.2026.1968970
Epigenetic immune memory in chronic inflammatory dermatoses: tissue-resident programming, barrier dysfunction and disease recurrence
Tajanlangit, P. S., Tajanlangit, S. M., & Khoury, K. S. (2026) · Skin Health and Disease · doi:10.1093/skinhd/vzag170
The Role of Two Homeodomain Genes PENNYWISE(PNY) and POUNDFOOLISH(PNF) in Regulating Meristem Maintenance of Shoot Apical Meristem
Wu, S. (2012) · eScholarship (California Digital Library)

Authors: Gallinari, P., Marco, S. D., Jones, P., Pallaoro, M., & Steinkühler, C.
Affiliations: Institute of Molecular Biology and Pathology (IT)
Corresponding author: Steinkühler, Christian
ORCID: Gallinari, Paola
Steinkühler, Christian
Venue: Cell Research
Publisher: Springer Science and Business Media LLC
Published: 2007-02-27
Volume: 17
Issue: 3
Pages: 195-211
ISSN: 1001-0602 (ISSN-L)
1748-7838
DOI: 10.1038/sj.cr.7310149
OpenAlex: W2031954417
Semantic Scholar: 755cb3e836171a20f267d47b6677a035efcf7c22
Cited by: 678
References: 165
Citations by year: 2026: 47 · 2025: 87 · 2024: 38 · 2023: 37 · 2022: 52 · 2021: 58 · 2020: 30 · 2019: 29 · 2018: 28 · 2017: 20 · 2016: 29 · 2015: 22 · 2014: 27 · 2013: 38 · 2012: 20
FWCI: 2.44
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Cell Research (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
Keywords: histone deacetylase, histone acetyltransferase, histone acetylation, gene transcription, chromatin conformation, histone deacetylase inhibitors, cancer therapeutics, non-histone protein acetylation, post-translational modification, cell cycle regulation, cell differentiation, malignant transformation
MeSH terms: Acetylation, Animals, Histone Deacetylases, Histones, Humans, Models, Biological, Models, Molecular, Molecular Biology, Neoplasms, Transcription, Genetic, Histone Deacetylase Inhibitors

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HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics

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