The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The tale beyond the tail: histone core domain modifications and the regulation of chromatin structure
Open accessAbstract
Histone post-translational modifications occur, not only in the N-terminal tail domains, but also in the core domains. While modifications in the N-terminal tail function largely through the regulation of the binding of non-histone proteins to chromatin, based on their location in the nucleosome, core domain modifications may also function through distinct mechanisms involving structural alterations to the nucleosome. This article reviews the recent developments in regards to these novel histone modifications and discusses their important role in the regulation of chromatin structure.
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Citations
Cites
Heterochromatin and Epigenetic Control of Gene Expression
Grewal, S. I. S., & Moazed, D. (2003) · Science · doi:10.1126/science.1086887 · Cited by 1,065
Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
Huyen, Y., Zgheib, O., DiTullio Jr, R. A., Gorgoulis, V. G., Zacharatos, P., Petty, T. J., Sheston, E. A., Mellert, H. S., Stavridi, E. S., & Halazonetis, T. D. (2004) · Nature · doi:10.1038/nature03114 · Cited by 884 · cited 2×
“Curiously, unlike many histone modifications involved in the DNA repair process, H3 lysine 79 methylation is not induced by the presence of DNA damage suggesting that some aspect of chromatin structure is altered by the presence of DNA damage such that this modification can be accessed by 53BP1 (69).”
BackgroundThe Occurrence of iε-N-Methyl Lysine in Histones
Murray, K. (1964) · Biochemistry · doi:10.1021/bi00889a003 · Cited by 521
Cited by
Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902
Nucleosome structure and function
McGinty, R. K., & Tan, S. (2015) · Chemical Reviews · doi:10.1021/cr500373h · Cited by 530
Xie, H., Vucetic, S., Iakoucheva, L. M., Oldfield, C. J., Dunker, A. K., Obradovic, Z., & Uversky, V. N. (2007) · Journal of Proteome Research · doi:10.1021/pr060394e · Cited by 382
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
Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure
North, J. A., Šimon, M., Ferdinand, M. B., Shoffner, M. A., Picking, J. W., Howard, C. J., Mooney, A. M., van Noort, J., Poirier, M. G., & Ottesen, J. J. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku150 · Cited by 46
Metadata
- Authors
- Mersfelder, E. L., & Parthun, M. R.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2006-05-19
- Volume
- 34
- Issue
- 9
- Pages
- 2653-2662
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2156222068
- Cited by
- 221
- References
- 3
- FWCI
- 4.30
- Type
- journal article
- Language
- en
- Open access
- gold
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