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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 EZL...

Topics

Acetylation
DNA Damage
DNA, Ribosomal
Electrophoresis, Polyacrylamide Gel
Epigenesis, Genetic
Histones
Lysine
Methylation
Mutation
Protein Processing, Post-Translational
Protein Structure, Tertiary

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Proteomics

Protozoan Proteins

Reproducibility of Results

Stress, Physiological

Tetrahymena

Source

Open in PubMed Open full text

Identifiers

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

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-24382802-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Quantitative proteomics reveals histone modifications in crosstalk with H3 lysine 27 methylation.PMID 24382802Read ↗

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