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Article

Molecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain.

Molecular cell - 21 Apr 2016

Li Yuanyuan, Sabari Benjamin R, Panchenko Tatyana, Wen Hong, Zhao Dan, Guan Haipeng, Wan Liling, Huang He, Tang Zhanyun, Zhao Yingming, Roeder Robert G, Shi Xiaobing, Allis C David, Li Haitao

Abstract excerpt

Recognition of histone covalent modifications by chromatin-binding protein modules ("readers") constitutes a major mechanism for epigenetic regulation, typified by bromodomains that bind acetyllysine. Non-acetyl histone lysine acylations (e.g., crotonylation, butyrylation, propionylation) have been recently identified, but readers that prefer these acylations have not been characterized. Here we report that the...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 27105114
DOI: 10.1016/j.molcel.2016.03.028
PMCID: PMC4841940

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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