Nuclear retention of STAT3 through the coiled-coil domain regulates its activity

Biochemical and Biophysical Research Communications

Volumn 336, Issue 2, 2005, Pages 617-624

  Sato, Noriko ^a   Tsuruma, Rieko ^a   Imoto, Seiyu ^a   Sekine, Yuichi ^a   Muromoto, Ryuta ^a   Sugiyama, Kenji ^b   Matsuda, Tadashi ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b NIPPON BOEHRINGER INGELHEIM CO LTD   (Japan)

Author keywords

IL 6; LIF; Nuclear translocation; Phosphorylation; STAT3; Transcription

Indexed keywords

ALANINE; ARGININE; EXPORTIN 1; LEPTOMYCIN B; LEUKEMIA INHIBITORY FACTOR RECEPTOR; PROTEIN INHIBITOR; STAT3 PROTEIN; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CELL NUCLEUS MEMBRANE; CHROMOSOME TRANSLOCATION; COMPARATIVE STUDY; CONTROLLED STUDY; HUMAN; HUMAN CELL; INDUCED MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN SYNTHESIS REGULATION; SIGNAL TRANSDUCTION; TRANSCRIPTION INITIATION; TRANSCRIPTION REGULATION; WILD TYPE;

ACTIVE TRANSPORT, CELL NUCLEUS; AMINO ACID SUBSTITUTION; CARCINOMA, HEPATOCELLULAR; CELL LINE; CELL NUCLEUS; DNA-BINDING PROTEINS; HUMANS; KARYOPHERINS; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, CYTOPLASMIC AND NUCLEAR; STAT3 TRANSCRIPTION FACTOR; STRUCTURE-ACTIVITY RELATIONSHIP; TRANS-ACTIVATORS;

EID: 24644512928     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.145     Document Type: Article

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