Retinoid-binding proteins are phosphorylated in vitro by soluble Ca+2- and phosphatidylserine-dependent protein kinase from mouse brain

Biochemical and Biophysical Research Communications

Volumn 120, Issue 2, 1984, Pages 593-601

  Cope, Frederick O ^a   Staller, Jon M ^a   Mahsem, Richard A ^a   Boutwell, R K ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AROTINOID; PROTEIN KINASE; RETINOID BINDING PROTEIN;

ANIMAL CELL; BRAIN; CALF; CARCINOGENESIS; CATTLE; CENTRAL NERVOUS SYSTEM; FEMALE GENITAL SYSTEM; IN VITRO STUDY; LIVER; MOUSE; NONHUMAN; PROTEIN PHOSPHORYLATION; UTERUS;

ANIMAL; BRAIN; CALCIUM; CARRIER PROTEINS; CATTLE; FEMALE; LIVER; MICE; NEOPLASM PROTEINS; PHOSPHATIDYLSERINES; PHOSPHORYLATION; PROTEIN KINASES; RECEPTORS, RETINOIC ACID; RETINOL-BINDING PROTEINS; SUBSTRATE SPECIFICITY; SUPPORT, U.S. GOV'T, P.H.S.; UTERUS;

EID: 0021153940     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/0006-291X(84)91296-8     Document Type: Article

References (23)

1. Vitamin A acid (retinoic acid), a potent inhibitor of 12-O-tetradecanoyl-phorbol-13-acetate-induced ornithine decarboxylase activity in mouse epidermis.