The DOI matches its Crossref record; 128 of the 130 references it cites were found in a registry or an index.
Regulation of chromatin by histone modifications
Open accessAbstract
Chromatin is not an inert structure, but rather an instructive DNA scaffold that can respond to external cues to regulate the many uses of DNA. A principle component of chromatin that plays a key role in this regulation is the modification of histones. There is an ever-growing list of these modifications and the complexity of their action is only just beginning to be understood. However, it is clear that histone modifications play fundamental roles in most biological processes that are involved in the manipulation and expression of DNA. Here, we describe the known histone modifications, define where they are found genomically and discuss some of their functional consequences, concentrating mostly on transcription where the majority of characterisation has taken place.
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“The acetylation state of histones is regulated by the following two classes of enzymes: histone acetyltransferases (HATs), which add acetyl groups to histone tails at lysine residues, and histone deacetylases (HDACs), which removes these acetyl groups.”
From The Epigenetics of Anxiety Pathophysiology: A DNA Methylation and Histone Modification Focused Review (2023) · cites this paper as Bannister and Kouzarides, 2011
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“D-2-hydroxyglutarate (D2HG) is one such oncometabolite, which inhibits numerous demethylases, leading to changes in genomic and transcriptomic methylation profiles as well as gene expression and genome topology 32,90-92 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [32]
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Cites
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
Self-citationCrystal structure of the nucleosome core particle at 2.8 Å resolution
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High-Resolution Profiling of Histone Methylations in the Human Genome
Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Schones, D. E., Wang, Z., Wei, G., Chepelev, I., & Zhao, K. (2007) · Cell · doi:10.1016/j.cell.2007.05.009 · Cited by 6,845
Functional Demarcation of Active and Silent Chromatin Domains in Human HOX Loci by Noncoding RNAs
Rinn, J. L., Kertesz, M., Wang, J. K., Squazzo, S. L., Xu, X. H., Brugmann, S. A., Goodnough, L. H., Helms, J. A., Farnham, P., Segal, E., et al. (2007) · Cell · doi:10.1016/j.cell.2007.05.022 · Cited by 4,246
Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
Shi, Y., Lan, F., Matson, C., Mulligan, P., Whetstine, J. R., Cole, P. A., Casero, R. A., & Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.12.012 · Cited by 4,051
Long Noncoding RNA as Modular Scaffold of Histone Modification Complexes
Tsai, M.-C., Manor, O., Wan, Y., Mosammaparast, N., Wang, J. K., Lan, F., Shi, Y., Segal, E., & Chang, H. Y. (2010) · Science · doi:10.1126/science.1192002 · Cited by 3,290
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
Self-citationMethylation 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
Regulation of chromatin structure by site-specific histone H3 methyltransferases
Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845
Flagged first, then by citations
2 of the 130 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Kouzarides T, Berger SL . Chromatin modifications and their mechanism of action. In: Allis CD, Jenuwein T, Reinberg D, eds. Epigenetics, New York: Cold Spring Harbor Laboratory Press, 2007:191–210.
Cited by
Sorted by citations
Histone methylation: a dynamic mark in health, disease and inheritance
Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241
Transcriptional Regulation and Its Misregulation in Disease
Lee, T. I., & Young, R. A. (2013) · Cell · doi:10.1016/j.cell.2013.02.014 · Cited by 1,676
The many faces and functions of β‐catenin
Valenta, T., Hausmann, G., & Basler, K. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.150 · Cited by 1,598
Epigenetic protein families: a new frontier for drug discovery
Arrowsmith, C. H., Bountra, C., Fish, P. V., Lee, K., & Schapira, M. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3674 · Cited by 1,327
Obesity: Epidemiology, Pathophysiology, and Therapeutics
Lin, X., & Li, H. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.706978 · Cited by 1,530
Metadata
- Authors
- Bannister, A. J., & Kouzarides, T.
- Affiliations
- University of Cambridge (GB)
- Corresponding author
- Kouzarides, Tony
- Venue
- Cell Research
- Published
- 2011-02-15
- Volume
- 21
- Issue
- 3
- Pages
- 381-395
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- PMC
- PMC3193420
- OpenAlex
- W2147524392
- Cited by
- 6,012
- References
- 130
- Citations by year
- 2026: 322 · 2025: 536 · 2024: 558 · 2023: 510 · 2022: 523 · 2021: 490 · 2020: 502 · 2019: 427 · 2018: 404 · 2017: 383 · 2016: 348 · 2015: 283 · 2014: 253 · 2013: 219 · 2012: 176
- FWCI
- 20.90
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cell Research (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- chromatin regulation, histone modifications, transcriptional regulation, epigenetics
- MeSH terms
- Chromatin, Heterochromatin, Histones, Protein Processing, Post-Translational, Histone Demethylases
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