Molecular Basis for the Regulation of the H3K4 Methyltransferase Activity of PRDM9

Cell Reports

Volumn 5, Issue 1, 2013, Pages 13-20

  Wu, Hong ^a   Mathioudakis, Nikolas ^b   Diagouraga, Boubou ^c   Dong, Aiping ^a   Dombrovski, Ludmila ^a   Baudat, Frédéric ^c   Cusack, Stephen ^b   DeMassy, Bernard ^c   Kadlec, Jan ^b  

^a UNIVERSITY OF TORONTO   (Canada)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

^c INSTITUTE OF HUMAN GENETICS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H3; HISTONE H3 LYSINE 4; HISTONE H3 PEPTIDE DIMETHYLATED ON LYSINE 4; HISTONE LYSINE METHYLTRANSFERASE; PRDM9 PROTEIN; S ADENOSYLHOMOCYSTEINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CATALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN METHYLATION; REGULATORY MECHANISM;

MUS; VERTEBRATA;

AMINO ACID SEQUENCE; HISTONE-LYSINE N-METHYLTRANSFERASE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

EID: 84885867381     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2013.08.035     Document Type: Article

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