N-glycosylation controls functional activity of Oatp1, an organic anion transporter

American Journal of Physiology - Gastrointestinal and Liver Physiology

Volumn 285, Issue 2 48-2, 2003, Pages

  Lee, Thomas K ^a   Koh, Albert S ^a   Cui, Zhifeng ^a   Pierce, Robert H ^a   Ballatori, Nazzareno ^a  

^a UNIVERSITY OF ROCHESTER SCHOOL OF MEDICINE AND DENTISTRY   (United States)

Author keywords

Membrane transport; Posttranslational modifications; Protein trafficking; Xenopus oocytes; Yeast

Indexed keywords

ASPARAGINE; ASPARTIC ACID; MUTANT PROTEIN; OATP1 PROTEIN; ORGANIC ANION TRANSPORTER; POLYPEPTIDE; TAUROCHOLIC ACID; TUNICAMYCIN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ANIMAL TISSUE; ANION EXCHANGE; ARTICLE; CELL LEVEL; CELL MEMBRANE TRANSPORT; CELLULAR DISTRIBUTION; CONTROLLED STUDY; GENE CONTROL; GENE MUTATION; INTRACELLULAR TRANSPORT; LIVER CELL MEMBRANE; MOLECULAR WEIGHT; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN LOCALIZATION; PROTEIN PROCESSING; PROTEIN TARGETING; PROTEIN TRANSPORT; RAT; REGULATORY MECHANISM; SACCHAROMYCES CEREVISIAE; SECRETORY VESICLE; TRANSPORT KINETICS; XENOPUS LAEVIS;

EID: 0037765324     PISSN: 01931857     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpgi.00358.2002     Document Type: Article

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