Regulated phosphorylation of a major UDP-glucuronosyltransferase isozyme by tyrosine kinases dictates endogenous substrate selection for detoxification

Journal of Biological Chemistry

Volumn 286, Issue 2, 2011, Pages 1639-1648

  Mitra, Partha S ^a   Basu, Nikhil K ^a   Basu, Mousumi ^a   Chakraborty, Sunit ^a   Saha, Tapas ^b   Owens, Ida S ^a  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b GEORGETOWN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL LINES; DEPURINATION; GENOTOXIC; GLUCURONIDATION; IN-VITRO; SIMILAR ANALYSIS; SPECIFIC INHIBITORS; SUBSTRATE SELECTION; TYROSINE KINASE; TYROSINE PHOSPHORYLATION;

AMINO ACIDS; CELL CULTURE; DETOXIFICATION; METABOLISM;

PHOSPHORYLATION;

ESTRADIOL; GLUCURONOSYLTRANSFERASE 2B7; PROTEIN TYROSINE KINASE;

ARTICLE; CELL METABOLISM; CONTROLLED STUDY; CYTOTOXICITY; DETOXIFICATION; DOWN REGULATION; ENZYME PHOSPHORYLATION; GLUCURONIDATION; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ANIMALS; CERCOPITHECUS AETHIOPS; COS CELLS; CRICETINAE; ESTRADIOL; ESTRONE; GLUCURONOSYLTRANSFERASE; HUMANS; ISOENZYMES; METABOLIC DETOXICATION, DRUG; MUTAGENESIS; PHOSPHATES; PHOSPHORYLATION; SRC-FAMILY KINASES; SUBSTRATE SPECIFICITY; TRANSFECTION;

EID: 78651405350     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.165126     Document Type: Article

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