The DOI matches its Crossref record; 90 of the 91 references it cites were found in a registry or an index.
Chromatin Modifications and Their Function
Open accessAbstract
The surface of nucleosomes is studded with a multiplicity of modifications. At least eight different classes have been characterized to date and many different sites have been identified for each class. Operationally, modifications function either by disrupting chromatin contacts or by affecting the recruitment of nonhistone proteins to chromatin. Their presence on histones can dictate the higher-order chromatin structure in which DNA is packaged and can orchestrate the ordered recruitment of enzyme complexes to manipulate DNA. In this way, histone modifications have the potential to influence many fundamental biological processes, some of which may be epigenetically inherited.
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“Combinatorial PTM patterns—the so-called “histone code”—are interpreted by reader proteins that recruit effector complexes to regulate chromatin accessibility (Kouzarides, 2007; Campos and Reinberg, 2009).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Kouzarides, 2007
In the citing paper
“This is in agreement with previous studies investigating the role of HDACiongeneexpression changes in HL60 cells (2, 29, 30, 35, 43).”
From Histone Deacetylase (HDAC) Inhibitor Kinetic Rate Constants Correlate with Cellular Histone Acetylation but Not Transcription and Cell Viability (2013) · cites this paper as [2]
Citations
Cites
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 · cited 5×
“LSD1 acts to demethylate H3K4 and repress transcription (Shi et al., 2004).”
InfluentialHistone demethylation by a family of JmjC domain-containing proteins
Tsukada, Y.-I., Fang, J., Erdjument‐Bromage, H., Warren, M., Borchers, C. H., Tempst, P., & Zhang, Y. (2005) · Nature · doi:10.1038/nature04433 · Cited by 2,244 · cited 4×
“H3K9 can also be demethylated by JHDM2A (Yamane et al., 2006), JMJD2A/JHDM3A (Tsukada et al., 2006; Whetstine et al., 2006), JMJD2B (Fodor et al., 2006), JMJD2C/GASC1 (Cloos et al., 2006), and JMJD2D (Shin and Janknecht, 2006).”
InfluentialHistone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions
Shogren‐Knaak, M. A., Ishii, H., Sun, J.-M., Pazin, M. J., Davie, J., & Peterson, C. L. (2006) · Science · doi:10.1126/science.1124000 · Cited by 1,959 · cited 2×
“In vitro experiments provide a role for H4K16Ac in chromatin decondensation (Shogren-Knaak et al., 2006).”
Role of histone H2A ubiquitination in Polycomb silencing
Wang, H., Wang, L., Erdjument‐Bromage, H., Vidal, M., Tempst, P., Jones, R. S., & Zhang, Y. (2004) · Nature · doi:10.1038/nature02985 · Cited by 1,856 · cited 3×
“In addition, in vivo data demonstrate that mono- (but not di-) methylated arginines can be deiminated (Wang et al., 2004a).”
Acetylation of Histones and Transcription-Related Factors
Sterner, D. E., & Berger, S. L. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.2.435-459.2000 · Cited by 1,824 · cited 3×
“Acetyltransferases are divided into three main families, GNAT, MYST, and CBP/p300 (Sterner and Berger, 2000).”
LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
Metzger, E., Wissmann, M., Yin, N., Müller, J. M., Schneider, R., Peters, A. H. F. M., Günther, T., Buettner, R., & Schüle, R. (2005) · Nature · doi:10.1038/nature04020 · Cited by 1,780 · cited 3×
“…are found may specify a preference for nucleosomal verses free histones (Lee et al., 2005a); proteins that associate with the enzyme may affect its selection of residue to modify (Metzger et al., 2005) or the degree of methylation (mono-, di-, or tri-) at a specific site (Steward et al., 2006).”
Zhang, Y., & Reinberg, D. (2001) · Genes & Development · doi:10.1101/gad.927301 · Cited by 1,639 · cited 3×
“Enzymes have been identified for acetylation (Sterner and Berger, 2000), methylation (Zhang and Reinberg, 2006), phosphorylation (Nowak and Corces, 2004), ubiquitination (Shilatifard, 2006), sumoylation (Nathan et al.”
Genomic Maps and Comparative Analysis of Histone Modifications in Human and Mouse
Bernstein, B., Kamal, M., Lindblad‐Toh, K., Bekiranov, S., Bailey, D. K., Huebert, D. J., McMahon, S., Karlsson, E. K., Kulbokas, E. J., Gingeras, T., et al. (2005) · Cell · doi:10.1016/j.cell.2005.01.001 · Cited by 1,567 · cited 3×
“Limited evidence from mouse and human tissues indicates that this is a conserved characteristic (Bernstein et al., 2005; see Review by B.E. Bernstein et al., page 669 of this issue).”
Genome-wide Map of Nucleosome Acetylation and Methylation in Yeast
Pokholok, D., Harbison, C. T., Levine, S. S., Cole, M. F., Hannett, N. M., Lee, T. I., Bell, G. W., Walker, K., Rolfe, A., Herbolsheimer, E., et al. (2005) · Cell · doi:10.1016/j.cell.2005.06.026 · Cited by 1,477 · cited 1×
“Most of the information we have has come from global analyses in budding yeast (Liu et al., 2005; Pokholok et al., 2005).”
Métivier, R., Penot, G., Hübner, M. R., Reid, G., Brand, H., Koš, M., & Gannon, F. (2003) · Cell · doi:10.1016/s0092-8674(03)00934-6 · Cited by 1,431
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1 of the 91 references couldn’t be matched to a known paper.
Cited by
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An integrated encyclopedia of DNA elements in the human genome
The ENCODE Project Consortium (2012) · Nature · doi:10.1038/nature11247 · Cited by 18,072
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
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
Self-citationGenome-wide maps of chromatin state in pluripotent and lineage-committed cells
Mikkelsen, T. S., Ku, M., Jaffe, D. B., Issac, B., Lieberman, E., Giannoukos, G., Alvarez, P., Brockman, W., Kim, T.-K., Koche, R. P., et al. (2007) · Nature · doi:10.1038/nature06008 · Cited by 4,129
Esteller, M. (2008) · New England Journal of Medicine · doi:10.1056/nejmra072067 · Cited by 3,767
Metadata
- Authors
- Kouzarides, T.
- Affiliations
- University of Cambridge (GB)
- Corresponding author
- Kouzarides, Tony
- ORCID
- Kouzarides, Tony
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2007-02
- Volume
- 128
- Issue
- 4
- Pages
- 693-705
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2096083625
- Cited by
- 10,883
- References
- 91
- Citations by year
- 2026: 260 · 2025: 374 · 2024: 387 · 2023: 414 · 2022: 472 · 2021: 616 · 2020: 561 · 2019: 578 · 2018: 530 · 2017: 624 · 2016: 679 · 2015: 664 · 2014: 733 · 2013: 686 · 2012: 796
- FWCI
- 45.57
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (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
- histone modifications, chromatin modification, nucleosome, chromatin structure, epigenetic inheritance, chromatin remodeling
- MeSH terms
- Animals, DNA, Enzymes, Histones, Humans, Nucleosomes, Protein Processing, Post-Translational, Chromatin Assembly and Disassembly, Epigenesis, Genetic
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