The DOI matches its Crossref record; 165 of the 165 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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
Citations
Cites
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756
Histone deacetylases (HDACs): characterization of the classical HDAC family
RUIJTER, A. J. M. D., GENNIP, A. H. V., CARON, H. N., KEMP, S., & KUILENBURG, A. B. P. V. (2003) · Biochemical Journal · doi:10.1042/bj20021321 · Cited by 3,114
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
Bannister, A. J., Zegerman, P., Partridge, J. F., Miska, E. A., Thomas, J. O., Allshire, R. C., & Kouzarides, T. (2001) · Nature · doi:10.1038/35065138 · Cited by 2,903
Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868
DNA methylation and human disease
Robertson, K. D. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1655 · Cited by 2,864
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
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403
Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,233
The diverse functions of histone lysine methylation
Martin, C., & Zhang, Y. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1761 · Cited by 2,157
Dent, S., Denu, J. M., & Allis, C. D. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.81 · Cited by 1,906
Research works printed but not linked: 1
- Vaisburg A . Discovery and development of MGCD0103 – an orally active HDAC inhibitor in human clinical trials. XIXth International Symposium on Medical Chemistry, Istanbul, Aug 29-Sep 2, 2006.
Cited by
Sorted by citations
The world of protein acetylation
Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 847
SCFAs strongly stimulate PYY production in human enteroendocrine cells
Larraufie, P., Martin‐Gallausiaux, C., Lapaque, N., Dore, J. M., Gribble, F. M., Reimann, F. M., & Blottière, H. M. (2018) · Scientific Reports · doi:10.1038/s41598-017-18259-0 · Cited by 484
The emerging role of epigenetic therapeutics in immuno-oncology
Topper, M. J., Vaz, M., Marrone, K. A., Brahmer, J. R., & Baylin, S. B. (2020) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-019-0266-5 · Cited by 433
Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents
Tan, J., Cang, S., Ma, Y., Petrillo, R. L., & Liu, D. (2010) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-3-5 · Cited by 431
Jares, P., Colomer, D., & Campo, E. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2230 · Cited by 466
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
