Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 44, 2012, Pages 17954-17959

  Yang, Na ^a   Wang, Weixiang ^b,e   Wang, Yan ^a,c   Wang, Mingzhu ^a   Zhao, Qiang ^d   Rao, Zihe ^a   Zhu, Bing ^b   Xu, Rui Ming ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b NATIONAL INSTITUTE OF BIOLOGICAL SCIENCES   (China)

^c UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^d SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

^e INSTITUTE OF ZOOLOGY   (China)

Author keywords

Methylation; RRNA expression

Indexed keywords

ARGININE; HISTONE H3; LYSINE; PROTEIN; PROTEIN SPINDLIN1; RNA PRECURSOR; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; EPIGENETICS; GENE EXPRESSION; HISTONE METHYLATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; CELL CYCLE PROTEINS; CRYSTALLOGRAPHY, X-RAY; HISTONES; LYSINE; METHYLATION; MICROTUBULE-ASSOCIATED PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHOPROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84868104227     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1208517109     Document Type: Article

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