GDE1/MIR16 is a glycerophosphoinositol phosphodiesterase regulated by stimulation of G protein-coupled receptors

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

Volumn 100, Issue 4, 2003, Pages 1745-1750

  Zheng, Bin ^a   Berrie, Christopher P ^b   Corda, Daniela ^b   Farquhar, Marilyn G ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b Consorzio Mario Negri Sud ^*  (Italy)

Author keywords

GDE domain; Phosphoinositide; Phospholipid metabolism; RGS proteins

Indexed keywords

ALPHA ADRENERGIC RECEPTOR; BETA ADRENERGIC RECEPTOR; G PROTEIN COUPLED RECEPTOR; GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE; GLYCEROPHOSPHOINOSITOL PHOSPHODIESTERASE; GLYCOPROTEIN; LYSOPHOSPHOLIPID; PHOSPHATIDYLINOSITIDE; PHOSPHODIESTERASE; PROTEIN MIR16; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME SPECIFICITY; EXTRACELLULAR SPACE; GENE IDENTIFICATION; HUMAN; HUMAN CELL; HYDROLYSIS; MEMBRANE STRUCTURE; MOUSE; NONHUMAN; PHOSPHOLIPID METABOLISM; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN METABOLISM; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; RECEPTOR BINDING; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CELL LINE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; GTP-BINDING PROTEINS; HUMANS; MICE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHOSPHORIC DIESTER HYDROLASES; RECEPTORS, CELL SURFACE; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

ANIMALIA; BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 0037452765     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0337605100     Document Type: Article

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