Arginine/lysine-methyl/methyl switches: Biochemical role of histone arginine methylation in transcriptional regulation

Epigenomics

Volumn 2, Issue 1, 2010, Pages 119-137

  Migliori, Valentina ^a   Phalke, Sameer ^a   Bezzi, Marco ^a   Guccione, Ernesto ^a  

^a INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

Author keywords

arginine methylation; chromatin; DNA methylation; histone binding domain; histone code; histones; post translational modification; PRMT; protein arginine methyltransferase; PTM; transcription regulation

Indexed keywords

ARGININE; CITRULLINE; HISTONE; LYSINE; PROTEIN ARGININE METHYLTRANSFERASE;

COMPUTER MODEL; CRYSTAL STRUCTURE; DEMETHYLATION; DNA METHYLATION; DOWNSTREAM PROCESSING; GENE REPRESSION; GENE SWITCHING; HIGH THROUGHPUT SCREENING; HISTONE CODE; HUMAN; MOLECULAR DOCKING; MOLECULAR INTERACTION; POST TRANSLATIONAL MODIFICATION; PRIORITY JOURNAL; PROTEIN MICROARRAY; PROTEIN MODIFICATION; PROTEIN PROTEIN INTERACTION; PROTEOMICS; REVIEW; SIGNAL TRANSDUCTION; TRANSCRIPTION INITIATION; TRANSCRIPTION REGULATION;

ARGININE; DNA METHYLATION; HISTONES; HUMANS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PROTEIN PROCESSING, POST-TRANSLATIONAL; TRANSCRIPTIONAL ACTIVATION;

EID: 77954103911     PISSN: 17501911     EISSN: 1750192X     Source Type: Journal    
DOI: 10.2217/epi.09.39     Document Type: Review

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