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Article

Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A.

Science (New York, N.Y.) - 5 May 2006

Huang Ying, Fang Jia, Bedford Mark T, Zhang Yi, Xu Rui-Ming

Abstract excerpt

Biological responses to histone methylation critically depend on the faithful readout and transduction of the methyl-lysine signal by "effector" proteins, yet our understanding of methyl-lysine recognition has so far been limited to the study of histone binding by chromodomain and WD40-repeat pro...

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Identifiers

PMID: 16601153
DOI: 10.1126/science.1125162

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-16601153-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A.PMID 16601153Read ↗

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