Consequences of the disease-related l78R mutation for dimerization and activity of STAT3

Journal of Cell Science

Volumn 127, Issue 9, 2014, Pages 1899-1910

  Domoszlai, Tamás ^a   Martincuks, Antons ^a   Fahrenkamp, Dirk ^a   de Leur, Hildegard Schmitz Van ^a   Küster, Andrea ^a   Müller Newen, Gerhard ^a  

^a RWTH AACHEN UNIVERSITY   (Germany)

Author keywords

Dimerization; Fluorescence microscopy; Fret; Hyper ige syndrome; Inflammatory hepatocellular adenoma; JAK STAT signalling; Stat3

Indexed keywords

DIMER; PROTEIN SH2; STAT1 PROTEIN; STAT3 PROTEIN; STAT5 PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; DIMERIZATION; DNA SEQUENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; GENE EXPRESSION; HUMAN; HUMAN CELL; INFLAMMATORY HEPATOCELLULAR ADENOMA; LIVER ADENOMA; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PHOSPHORYLATION; SOMATIC MUTATION; CHEMISTRY; CONFOCAL MICROSCOPY; GENETICS; HELA CELL LINE; METABOLISM; MUTATION; PHOSPHORYLATION; WESTERN BLOTTING;

BLOTTING, WESTERN; DIMERIZATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; HELA CELLS; HUMANS; MICROSCOPY, CONFOCAL; MUTATION; PHOSPHORYLATION; STAT3 TRANSCRIPTION FACTOR; STAT5 TRANSCRIPTION FACTOR;

EID: 84899724903     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.137422     Document Type: Article

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