μ-Opioid Receptor-mediated ERK Activation Involves Calmodulin-dependent Epidermal Growth Factor Receptor Transactivation

Journal of Biological Chemistry

Volumn 276, Issue 36, 2001, Pages 33847-33853

  Belcheva, Mariana M ^a   Szùcs, Maria ^a,b   Wang, Danxin ^c   Sadee, Wolfgang ^c   Coscia, Carmine J ^a  

^a SAINT LOUIS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CHEMICAL ACTIVATION; PROTEINS;

PROTEIN-COUPLED RECEPTORS;

BIOCHEMISTRY;

CALCIUM BINDING PROTEIN; CALMODULIN; ENKEPHALIN; ENKEPHALIN[2 DEXTRO ALANINE 4 METHYLPHENYLALANINE 5 GLYCINE]; EPIDERMAL GROWTH FACTOR RECEPTOR; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; MU OPIATE RECEPTOR; 1,10 PHENANTHROLINE; 1,10-PHENANTHROLINE; CROSS LINKING REAGENT; FORSKOLIN; ISOPROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHENANTHROLINE DERIVATIVE; PROTEIN KINASE C; PROTEINASE INHIBITOR;

ANIMAL CELL; ARTICLE; CALCIUM CELL LEVEL; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVATION; ENZYME PHOSPHORYLATION; GENE EXPRESSION REGULATION; MEMBRANE BINDING; MITOGENESIS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION; TRANSACTIVATION; ANIMAL; BIOLOGICAL MODEL; CELL LINE; DOSE RESPONSE; GENETIC TRANSFECTION; HUMAN; METABOLISM; MUTATION; PHOSPHORYLATION; PROTEIN BINDING; RAT; SERODIAGNOSIS; TIME;

ANIMALIA;

ANIMALS; CALMODULIN; CELL LINE; CROSS-LINKING REAGENTS; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME ACTIVATION; FORSKOLIN; HUMANS; MAP KINASE SIGNALING SYSTEM; MITOGEN-ACTIVATED PROTEIN KINASES; MODELS, BIOLOGICAL; MUTATION; PHENANTHROLINES; PHOSPHORYLATION; PRECIPITIN TESTS; PROTEASE INHIBITORS; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN KINASE C; RATS; RECEPTOR, EPIDERMAL GROWTH FACTOR; RECEPTORS, OPIOID, MU; SIGNAL TRANSDUCTION; TIME FACTORS; TRANS-ACTIVATION (GENETICS); TRANSFECTION;

EID: 0035823506     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M101535200     Document Type: Article

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