Androgen Receptor Acetylation Site Mutations Cause Trafficking Defects, Misfolding, and Aggregation Similar to Expanded Glutamine Tracts

Journal of Biological Chemistry

Volumn 279, Issue 9, 2004, Pages 8389-8395

  Thomas, Monzy ^a   Dadgar, Nahid ^a   Aphale, Abhishek ^a   Harrell, Jennifer M ^a   Kunkel, Robin ^a   Pratt, William B ^a   Lieberman, Andrew P ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLATION; DISEASES; PROTEINS; TOXICITY;

AMINO TERMINUS; ANDROGEN RECEPTORS (AR);

BIOCHEMISTRY;

ANDROGEN RECEPTOR; GLUTAMINE; HEAT SHOCK PROTEIN 90; PROTEASOME; UBIQUITIN PROTEIN LIGASE;

ACETYLATION; AMINO TERMINAL SEQUENCE; ARTICLE; CELLULAR DISTRIBUTION; DEGENERATIVE DISEASE; GENE EXPRESSION REGULATION; GENE MUTATION; HUMAN; HUMAN CELL; LIGAND BINDING; NERVE DEGENERATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN MODIFICATION; PROTEIN PROCESSING; PROTEIN TERTIARY STRUCTURE;

ACETYLATION; BINDING SITES; BIOLOGICAL TRANSPORT; CELL NUCLEUS; FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT; GENE EXPRESSION; GLUTAMINE; GREEN FLUORESCENT PROTEINS; HELA CELLS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; LACTONES; LUMINESCENT PROTEINS; LYSINE; MACROLIDES; MUTATION; POINT MUTATION; PROTEIN FOLDING; RECEPTORS, ANDROGEN; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFECTION;

EID: 1542319221     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M311761200     Document Type: Article

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