The H3 tail domain participates in multiple interactions during folding and self-association of nucleosome arrays

Molecular and Cellular Biology

Volumn 27, Issue 6, 2007, Pages 2084-2091

  Kan, Pu Yeh ^a   Lu, Xu ^b   Hansen, Jeffrey C ^b   Hayes, Jeffrey J ^a,c  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

^b Department of Environmental and Radiological Health Sciences   (United States)

^c UNIVERSITY OF ROCHESTER SCHOOL OF MEDICINE AND DENTISTRY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMINE; HISTONE H3; LYSINE; MAGNESIUM CHLORIDE; MUTANT PROTEIN; PROTEIN SUBUNIT; SODIUM CHLORIDE;

ACETYLATION; AMINO ACID SUBSTITUTION; ARTICLE; CHROMATIN ASSEMBLY AND DISASSEMBLY; CHROMATIN CONDENSATION; CHROMATIN STRUCTURE; CONTROLLED STUDY; CROSS LINKING; DNA MICROARRAY; GENE EXPRESSION REGULATION; NONHUMAN; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MODIFICATION;

ACETYLATION; ANIMALS; DNA; HISTONES; MUTATION; NUCLEOSOMES; OLIGONUCLEOTIDE ARRAY SEQUENCE ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; XENOPUS LAEVIS;

EID: 33947201778     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.02181-06     Document Type: Article

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