Quantitative proteomics reveals that the specific methyltransferases Txr1p and Ezl2p differentially affect the mono-, di- and trimethylation states of histone H3 lysine 27 (H3K27)

Molecular and Cellular Proteomics

Volumn 12, Issue 6, 2013, Pages 1678-1688

  Zhang, Chunchao ^a   Molascon, Anthony J ^a   Gao, Shan ^a   Liu, Yifan ^a   Andrews, Philip C ^a,b,c  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

^c NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EZL2P PROTEIN; HISTONE H3; HISTONE METHYLTRANSFERASE; LYSINE; NITROGEN 15; TXR1P PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; FUNCTIONAL PROTEOMICS; GENE SILENCING; HISTONE METHYLATION; IN VIVO STUDY; ISOTOPE LABELING; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; TETRAHYMENA THERMOPHILA;

CILIOPHORA; EUKARYOTA; TETRAHYMENA; TETRAHYMENA THERMOPHILA;

EID: 84878697014     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.021733     Document Type: Article

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