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Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association
The amino-terminal histone tails are subject to covalent post-translational modifications such as acetylation, methylation, and phosphorylation. In the histone code hypothesis, these exposed and unstructured histone tails are accessible to a repertoire of regulatory factors that specifically recogni...
Tallennettuna:
| Päätekijät: | , , , , , , |
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| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Cold Spring Harbor Laboratory Press
2002
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC186335/ https://ncbi.nlm.nih.gov/pubmed/12080090 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1101/gad.1001502 |
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