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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“A uthor M anuscript A uthor M anuscript A uthor M anuscript A uthor M anuscript HDAC are potentially able to target not only histones but also non-histone proteins (Gallinari et al., 2007; Choudhary et al., 2009; Iyer et al., 2012).”
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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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