The hsp90 co-chaperone XAP2 alters importin β recognition of the bipartite nuclear localization signal of the Ah receptor and represses transcriptional activity

Journal of Biological Chemistry

Volumn 278, Issue 4, 2003, Pages 2677-2685

  Petrulis, John R ^a   Kusnadi, Ann ^a   Ramadoss, Preeti ^a   Hollingshead, Brett ^a   Perdew, Gary H ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; CELLS; CLONING; DIMERS; VIRUSES;

POLYCLONAL ANTIBODY;

PROTEINS;

2,3,7,8 TETRACHLORODIBENZO PARA DIOXIN; AROMATIC HYDROCARBON RECEPTOR; CHAPERONE; COMPLEMENTARY DNA; GLUCOCORTICOID RECEPTOR; GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN 90; HEPATITIS B VIRUS X ASSOCIATED PROTEIN 2; KARYOPHERIN BETA; LEPTOMYCIN B; POLYCLONAL ANTIBODY; PROTEIN XAP2; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN; ACTIN; ARYL HYDROCARBON RECEPTOR INTERACTING PROTEIN; ARYL HYDROCARBON RECEPTOR-INTERACTING PROTEIN; LIGAND; PROTEIN; TUBULIN;

ANIMAL CELL; ARTICLE; CELL CULTURE; CELL NUCLEUS; CELLULAR DISTRIBUTION; CYTOPLASM; CYTOSKELETON; CYTOSOL; GENE EXPRESSION; GENE REPRESSION; GENETIC TRANSCRIPTION; GENETIC TRANSFECTION; IMMUNOPRECIPITATION; NONHUMAN; NUCLEAR LOCALIZATION SEQUENCE; NUCLEOCYTOPLASMIC TRANSPORT; PRIORITY JOURNAL; RABBIT; REPORTER GENE; TRANSCRIPTION REGULATION; ACTIVE TRANSPORT; ANIMAL; CELL STRAIN COS1; CHEMISTRY; FLUORESCENCE MICROSCOPY; GENE DELETION; GENE VECTOR; METABOLISM; MOUSE; NUCLEAR LOCALIZATION SIGNAL; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SERODIAGNOSIS;

ANIMALIA; HEPATITIS B VIRUS; ORYCTOLAGUS CUNICULUS;

ACTINS; ACTIVE TRANSPORT, CELL NUCLEUS; ANIMALS; BETA KARYOPHERINS; CELL NUCLEUS; COS CELLS; CYTOPLASM; CYTOSOL; GENE DELETION; GENETIC VECTORS; HSP90 HEAT-SHOCK PROTEINS; LIGANDS; MICE; MICROSCOPY, FLUORESCENCE; NUCLEAR LOCALIZATION SIGNALS; PRECIPITIN TESTS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; TRANSCRIPTION, GENETIC; TRANSFECTION; TUBULIN;

EID: 0037462747     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M209331200     Document Type: Article

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