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HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics
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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“The mammalian HDAC family consists of 18 isoforms categorized into four major classes (Classes I–IV) (Zhang et al., 2024; Glozak et al., 2005; Gallinari et al., 2007; Yang and Grégoire, 2005), as summarized in Table 1 (Vanaja et al., 2018; Johnstone, 2002; Gao et al., 2002; Tong et al., 2002; Hubbert et al., 2002).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Gallinari et al., 2007
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Targeting Class I Histone Deacetylases in Human Uterine Leiomyosarcoma
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Nucleotide Metabolism Behind Epigenetics
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“dinucleotide, NAD, as a co-substrate and transfer the acetyl group onto adenosine diphosphate ribose (ADPR) to form a 2’-Oacetyl-ADPR (8, 9).”
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Metadata
- Authors
- Gallinari, P., Marco, S. D., Jones, P., Pallaoro, M., & Steinkühler, C.
- Affiliations
- Institute of Molecular Biology and Pathology (IT)
- Corresponding author
- Steinkühler, Christian
- Venue
- Cell Research
- Published
- 2007-02-27
- Volume
- 17
- Issue
- 3
- Pages
- 195-211
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- 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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