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Article

A molecular threading mechanism underlies Jumonji lysine demethylase KDM2A regulation of methylated H3K36.

Genes & development - 15 Aug 2014

Cheng Zhongjun, Cheung Peggie, Kuo Alex J, Yukl Erik T, Wilmot Carrie M, Gozani Or, Patel Dinshaw J

Abstract excerpt

The dynamic reversible methylation of lysine residues on histone proteins is central to chromatin biology. Key components are demethylase enzymes, which remove methyl moieties from lysine residues. KDM2A, a member of the Jumonji C domain-containing histone lysine demethylase family, specifically targets lower methylation states of H3K36. Here, structural studies reveal that H3K36 specificity for KDM2A is mediated...

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Identifiers

PMID: 25128496
DOI: 10.1101/gad.246561.114
PMCID: PMC4197961

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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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