The language of covalent histone modifications View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-01

AUTHORS

Brian D. Strahl, C. David Allis

ABSTRACT

Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of these highly conserved modifications has remained elusive, converging biochemical and genetic evidence suggests functions in several chromatin-based processes. We propose that distinct histone modifications, on one or more tails, act sequentially or in combination to form a ‘histone code’ that is, read by other proteins to bring about distinct downstream events. More... »

PAGES

41-45

Journal

TITLE

Nature

ISSUE

6765

VOLUME

403

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/47412

    DOI

    http://dx.doi.org/10.1038/47412

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1025852070

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/10638745


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