DAXX co-folds with H3.3/H4 using high local stability conferred by the H3.3 variant recognition residues

Nucleic Acids Research

Volumn 42, Issue 7, 2014, Pages 4318-4331

  Denizio, Jamie E ^a   Elsässer, Simon J ^b   Black, Ben E ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

DAXX PROTEIN; HISTONE H3; HISTONE H3.3; HISTONE H4; MUTANT PROTEIN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CHROMATIN ASSEMBLY AND DISASSEMBLY; DEUTERIUM HYDROGEN EXCHANGE; MASS SPECTROMETRY; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN UNFOLDING; STRUCTURE ANALYSIS;

HISTONE CHAPERONES; HISTONES; MODELS, MOLECULAR; MUTATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING;

EID: 84898946550     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku090     Document Type: Article

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