Tryptophan 621 and serine 667 residues of Daxx regulate its nuclear export during glucose deprivation

Journal of Biological Chemistry

Volumn 279, Issue 29, 2004, Pages 30573-30578

  Song, Jae J ^a   Lee, Yong J ^a,b  

^a UNIVERSITY OF PITTSBURGH MEDICAL CENTER   (United States)

^b UNIVERSITY OF PITTSBURGH CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; CHROMOSOMES; PROTEINS;

NUCLEAR EXPORT SIGNAL (NES); PHOSPHORYLATION;

GLUCOSE;

ALANINE; AMINO ACID; CARRIER PROTEIN; DAXX PROTEIN; EXPORTIN 1; GLUCOSE; LEPTOMYCIN B; PROTEIN; SERINE; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CELL NUCLEUS; CONTROLLED STUDY; GLUCOSE METABOLISM; HUMAN; HUMAN CELL; NUCLEAR EXPORT SIGNAL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION; TRANSCRIPTION REGULATION; TRANSLATION REGULATION;

ACTIVE TRANSPORT, CELL NUCLEUS; ALANINE; ANTIBIOTICS, ANTINEOPLASTIC; BINDING SITES; CELL LINE, TUMOR; FATTY ACIDS, UNSATURATED; GENETIC VECTORS; GLUCOSE; HUMANS; IMMUNOBLOTTING; KARYOPHERINS; MALE; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; PROSTATIC NEOPLASMS; PROTEIN BINDING; RECEPTORS, CYTOPLASMIC AND NUCLEAR; SERINE; TIME FACTORS; TRYPTOPHAN;

NES;

EID: 3142742400     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M404512200     Document Type: Article

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