Spindlin‐1 recognizes methylations of K20 and R23 of histone H4 tail

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A combinatorial H4 tail library for exploring the histone code.

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Structure and binding of the H4 histone tail and the effects of lysine 16 acetylationw

The H4 histone tail plays a critical role in chromatin folding and regulation—it mediates strong interactions with the acidic patch of proximal nucleosomes and its acetylation at lysine 16 (K16) leads to partial unfolding of chromatin. The molecular mechanism associated with the H4 tail/acidic patch interactions and its modulation via K16 acetylation remains unknown. Here we employ a combinatio...

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Structure and binding of the H4 histone tail and the effects of lysine 16 acetylation.

The H4 histone tail plays a critical role in chromatin folding and regulation--it mediates strong interactions with the acidic patch of proximal nucleosomes and its acetylation at lysine 16 (K16) leads to partial unfolding of chromatin. The molecular mechanism associated with the H4 tail/acidic patch interactions and its modulation via K16 acetylation remains unknown. Here we employ a combinati...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 2018

ISSN: 0014-5793,1873-3468

DOI: 10.1002/1873-3468.13281