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...

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Dades bibliogràfiques

Publicat a:	Genes Dev
Autors principals:	Ng, Huck Hui, Feng, Qin, Wang, Hengbin, Erdjument-Bromage, Hediye, Tempst, Paul, Zhang, Yi, Struhl, Kevin
Format:	Artigo
Idioma:	Inglês
Publicat:	Cold Spring Harbor Laboratory Press 2002
Matèries:	Research Paper
Accés en línia:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC186335/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12080090/ https://ncbi.nlm.nih.govhttps://doi.org/10.1101/gad.1001502
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