One, two, three: How histone methylation is read

Epigenomics

Volumn 4, Issue 6, 2012, Pages 641-653

  Fischle, Wolfgang ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

arginine; binding; chromatin; domains; epigenetic; histone; lysine; methylation; modules

Indexed keywords

AMINO ACID; ARGININE; BINDING PROTEIN; DNA; DNA METHYLTRANSFERASE; HISTONE; LYSINE; RETINOIC ACID;

CHROMATIN; EMBRYONIC STEM CELL; EPIGENETICS; GENOME; HISTONE METHYLATION; MOLECULAR INTERACTION; MUSCLE DEVELOPMENT; NERVE CELL DIFFERENTIATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; ARGININE; CHROMATIN; EPIGENESIS, GENETIC; HISTONES; HUMANS; LYSINE; METHYLATION; PROTEIN PROCESSING, POST-TRANSLATIONAL;

EID: 84871432519     PISSN: 17501911     EISSN: 1750192X     Source Type: Journal    
DOI: 10.2217/epi.12.56     Document Type: Review

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