Accessibility of the histone H3 tail in the nucleosome for binding of paired readers
Accessibility of the histone H3 tail in the nucleosome for binding of paired readers
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Publisher
London: Nature Publishing Group UK
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Language
English
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London: Nature Publishing Group UK
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Combinatorial polyvalent contacts of histone-binding domains or readers commonly mediate localization and activities of chromatin-associated proteins. A pair of readers, the PHD fingers of the protein CHD4, has been shown to bivalently recognize histone H3 tails. Here we describe a mechanism by which these linked but independent readers bind to the...
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Full title
Accessibility of the histone H3 tail in the nucleosome for binding of paired readers
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TN_cdi_doaj_primary_oai_doaj_org_article_80503b36d74a4bc3b72aa20bc28f7b84
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_80503b36d74a4bc3b72aa20bc28f7b84
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-017-01598-x
