The DOI matches its Crossref record; 95 of the 95 references it cites were found in a registry or an index.
A brief review of nucleosome structure
Open accessAbstract
The nucleosomal subunit organization of chromatin provides a multitude of functions. Nucleosomes elicit an initial ∼7‐fold linear compaction of genomic DNA. They provide a critical mechanism for stable repression of genes and other DNA‐dependent activities by restricting binding of trans‐acting factors to cognate DNA sequences. Conversely they are engineered to be nearly meta‐stable and disassembled (and reassembled) in a facile manner to allow rapid access to the underlying DNA during processes such as transcription, replication and DNA repair. Nucleosomes protect the genome from DNA damaging agents and provide a lattice onto which a myriad of epigenetic signals are deposited. Moreover, vast strings of nucleosomes provide a framework for assembly of the chromatin fiber and higher‐order chromatin structures. Thus, in order to provide a foundation for understanding these functions, we present a review of the basic elements of nucleosome structure and stability, including the association of linker histones.
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Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
Chen, X., Xiu, M., Xing, J., Yu, S., Min, D., & Guo, F. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479439 · Cited by 5,742
Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions
Shogren-Knaak, M., Ishii, H., Sun, J.-M., Pazin, M. J., Davie, J. R., & Peterson, C. L. (2006) · Science · doi:10.1126/science.1124000 · Cited by 1,873
Thoma, F., Koller, T., & Klug, A. (1979) · The Journal of cell biology · doi:10.1083/jcb.83.2.403 · Cited by 1,558
Solvent Mediated Interactions in the Structure of the Nucleosome Core Particle at 1.9Å Resolution
Davey, C. A., Sargent, D. F., Luger, K., Maeder, A. W., & Richmond, T. J. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00386-8 · Cited by 1,489
The structure of DNA in the nucleosome core
Richmond, T. J., & Davey, C. A. (2003) · Nature · doi:10.1038/nature01595 · Cited by 1,286
A positive role for histone acetylation in transcription factor access to nucleosomal DNA
Lee, D. Y., Hayes, J. J., Pruss, D., & Wolffe, A. P. (1993) · Cell · doi:10.1016/0092-8674(93)90051-q · Cited by 1,122
Self-citationStructure of the nucleosome core particle at 7 Å resolution
Richmond, T. J., Finch, J. T., Rushton, B., Rhodes, D., & Klug, A. (1984) · Nature · doi:10.1038/311532a0 · Cited by 1,060
Arents, G., Burlingame, R. W., Wang, B. C., Love, W. E., & Moudrianakis, E. N. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.10148 · Cited by 759
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Succinylation of H3K122 destabilizes nucleosomes and enhances transcription
Zorro Shahidian, L., Haas, M., Le Gras, S., Nitsch, S., Mourão, A., Geerlof, A., Margueron, R., Michaelis, J., Daujat, S., & Schneider, R. (2021) · The EMBO Reports · doi:10.15252/embr.202051009 · Cited by 92
Acetylation of histone H3 in cancer progression and prognosis
Miziak, P., Baran, M., Borkiewicz, L., Trombik, T., & Stepulak, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252010982 · Cited by 49
Unveiling the Conformational Dynamics of the Histone Tails Using Markov State Modeling
Patel, R., & Loverde, S. M. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5c00196 · Cited by 13
Image-based 3D genomics through chromatin tracing
Yang, T., & Wang, S. (2024) · Nature Reviews Methods Primers · doi:10.1038/s43586-024-00354-y · Cited by 10
Metadata
- Authors
- Cutter, A. R., & Hayes, J. J.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2015-05-14
- Volume
- 589
- Issue
- 20PartA
- Pages
- 2914-2922
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1744656122
- Cited by
- 433
- References
- 95
- FWCI
- 11.45
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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