The DOI matches its Crossref record; 114 of the 114 references it cites were found in a registry or an index.
Understanding the language of Lys36 methylation at histone H3
Open accessAbstract
Histone side chains are post-translationally modified at multiple sites, including at Lys36 on histone H3 (H3K36). Several enzymes from yeast and humans, including the methyltransferases SET domain-containing 2 (Set2) and nuclear receptor SET domain-containing 1 (NSD1), respectively, alter the methylation status of H3K36, and significant progress has been made in understanding how they affect chromatin structure and function. Although H3K36 methylation is most commonly associated with the transcription of active euchromatin, it has also been implicated in diverse processes, including alternative splicing, dosage compensation and transcriptional repression, as well as DNA repair and recombination. Disrupted placement of methylated H3K36 within the chromatin landscape can lead to a range of human diseases, underscoring the importance of this modification.
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Cited by
Comprehensive molecular characterization of clear cell renal cell carcinoma
The Cancer Genome Atlas Research Network (2013) · Nature · doi:10.1038/nature12222 · Cited by 3,485
Writing, erasing and reading histone lysine methylations
Hyun, K., Jeon, J., Park, K., & Kim, J. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.11 · Cited by 1,250
Gene Body Methylation Can Alter Gene Expression and Is a Therapeutic Target in Cancer
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Regulation of nucleosome dynamics by histone modifications
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Intragenic DNA methylation prevents spurious transcription initiation
Neri, F., Rapelli, S., Krepelova, A., Incarnato, D., Parlato, C., Basile, G., Maldotti, M., Anselmi, F., & Oliviero, S. (2017) · Nature · doi:10.1038/nature21373 · Cited by 739
Metadata
- Authors
- Wagner, E. J., & Carpenter, P. B.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2012-01-23
- Volume
- 13
- Issue
- 2
- Pages
- 115-126
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W1969451832
- Cited by
- 936
- References
- 114
- FWCI
- 3.95
- Type
- journal article
- Language
- en
- Open access
- green
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