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Article

Quantitative proteomics reveals histone modifications in crosstalk with H3 lysine 27 methylation.

Molecular & cellular proteomics : MCP - 1 Mar 2014

Zhang Chunchao, Gao Shan, Molascon Anthony J, Liu Yifan, Andrews Philip C

Abstract excerpt

Methylation at histone H3 lysine 27 (H3K27me) is an evolutionarily conserved epigenetic mark associated with transcriptional repression and replication elongation. We have previously shown that in Tetrahymena thermophila, a unicellular eukaryote, the histone methyltransferases (HMTs) TXR1 and EZL2 are primarily responsible for H3K27 mono-methylation (H3K27me1) and di-/tri-methylation (H3K27me2/3), respectively....

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

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Identifiers

PMID: 24382802
DOI: 10.1074/mcp.M113.029025
PMCID: PMC3945906

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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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