Multiple tyrosine residues in the cytosolic domain of the erythropoietin receptor promote activation of STAT5

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 16, 1996, Pages 8324-8328

  Klingmüller, Ursula ^a   Bergelson, Svetlana ^a   Hsiao, Jonathan G ^b   Lodish, Harvey F ^a,b  

^a WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

cytokine receptors; erythropoiesis; JAK kinases; transcription factors

Indexed keywords

ERYTHROPOIETIN; ERYTHROPOIETIN RECEPTOR; PROTEIN TYROSINE KINASE; TYROSINE;

ANIMAL CELL; ARTICLE; CELL NUCLEUS; CELL PROLIFERATION; CONTROLLED STUDY; CYTOSOL; ELECTROPHORETIC MOBILITY; ENZYME ACTIVATION; ERYTHROID PRECURSOR CELL; GENE ACTIVATION; IMMUNOBLOTTING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION;

AMINO ACID SEQUENCE; BASE SEQUENCE; CELL DIVISION; CELL NUCLEUS; CELLS, CULTURED; DNA-BINDING PROTEINS; MILK PROTEINS; MOLECULAR SEQUENCE DATA; OLIGONUCLEOTIDE PROBES; PHOSPHOTYROSINE; POINT MUTATION; PROTEIN BINDING; RECEPTORS, ERYTHROPOIETIN; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAINS; STAT5 TRANSCRIPTION FACTOR; STRUCTURE-ACTIVITY RELATIONSHIP; TRANS-ACTIVATORS; TYROSINE;

ANIMALIA;

EID: 0029738317     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.16.8324     Document Type: Article

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