The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
The epigenetic magic of histone lysine methylation: Delivered on 6 July 2005 at the 30th FEBS Congress in Budapest, Hungary
Open accessAbstract
Epigenetic mechanisms control eukaryotic development beyond DNA‐stored information. There are several pathways, including histone tail modifications, histone variant incorporation, nucleosome remodelling, DNA methylation and noncoding RNAs that together all contribute to the dynamic ‘make‐up’ of chromatin under distinct developmental options. The histone tail modifications are most variable and over 50 marks have by now been mapped. While the majority of these modifications are transient, histone lysine methylation and, in particular, a histone lysine tri‐methyl state has been regarded as a more robust signal, consistent with proposed roles to impart long‐term epigenetic memory. Based on the paradigm of SET‐domain histone lysine methyltransferases (HMTases) and chromo‐domain adaptor proteins, and in conjunction with the Sir Hans Krebs Medal 2005, I describe here my personal view on the discovery of the first HMTase in 2000, and the subsequent advances on the biology of histone lysine methylation. This discovery has changed my scientific career and significantly contributed to a better understanding of epigenetic control, with important implications for heterochromatin formation, X inactivation, Polycomb group silencing and novel insights into stem cell research, nuclear reprogramming and cancer.
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Cites
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Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
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Self-citationRegulation of chromatin structure by site-specific histone H3 methyltransferases
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Active Genes Are Tri-Methylated at K4 of Histone H3
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Cited by
Jones, P. A., & Baylin, S. B. (2007) · Cell · doi:10.1016/j.cell.2007.01.029 · Cited by 4,515
Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact
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Reversal of H3K9me2 by a Small-Molecule Inhibitor for the G9a Histone Methyltransferase
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Self-citationDynamic Regulation of Histone Lysine Methylation by Demethylases
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Synthetic lethality by targeting EZH2 methyltransferase activity in ARID1A-mutated cancers
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Metadata
- Authors
- Jenuwein, T.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2006-06-29
- Volume
- 273
- Issue
- 14
- Pages
- 3121-3135
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W1757349669
- Cited by
- 235
- References
- 16
- FWCI
- 7.00
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Jenuwein, T. (2006). The epigenetic magic of histone lysine methylation: Delivered on 6 July 2005 at the 30th FEBS Congress in Budapest, Hungary. The FEBS Journal. https://doi.org/10.1111/j.1742-4658.2006.05343.x
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