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Volumn 285, Issue 6, 2010, Pages 3600-3607
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Modulation of the human glucuronosyltransferase UGT1A pathway by splice isoform polypeptides is mediated through protein-protein interactions
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Author keywords
[No Author keywords available]
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Indexed keywords
CELLULAR RESPONSE;
CO-EXPRESSION;
CO-IMMUNOPRECIPITATION EXPERIMENTS;
CO-SUBSTRATE;
COMPETITIVE BINDING;
GLUCURONIDATION;
GLUCURONIDES;
HEK293 CELLS;
HETEROLOGOUS SYSTEMS;
HUMAN TISSUES;
IN-DEPTH INVESTIGATION;
INDUCIBLE SYSTEMS;
ISOFORMS;
MOLECULAR MECHANISM;
PROTEIN-PROTEIN INTERACTIONS;
REGULATORY EFFECTS;
REGULATORY MECHANISM;
RELATIVE ABUNDANCE;
UDP-GLUCURONIC ACID;
COMPLEXATION;
GLUCOSE;
PROTEINS;
SUBSTRATES;
GLUCURONIC ACID;
GLUCURONOSYLTRANSFERASE 1A;
GLUCURONOSYLTRANSFERASE 1A I1;
GLUCURONOSYLTRANSFERASE 1A I2;
GLUCURONOSYLTRANSFERASE 1A1;
GLUCURONOSYLTRANSFERASE 1A7;
GLUCURONOSYLTRANSFERASE 1A8;
GLYCOSYLTRANSFERASE;
POLYPEPTIDE;
UNCLASSIFIED DRUG;
URIDINE DIPHOSPHATE;
BILIRUBIN URIDINE DIPHOSPHOGLUCURONOSYL TRANSFERASE 1A1;
BILIRUBIN URIDINE-DIPHOSPHOGLUCURONOSYL TRANSFERASE 1A1;
ECDYSONE;
GLUCURONIDE;
GLUCURONOSYLTRANSFERASE;
ISOENZYME;
PEPTIDE;
UDP GLUCURONOSYLTRANSFERASE, UGT1A8;
UDP-GLUCURONOSYLTRANSFERASE, UGT1A8;
UGT1A7 PROTEIN, HUMAN;
ALTERNATIVE RNA SPLICING;
ARTICLE;
BINDING AFFINITY;
CELL STRAIN HEK293;
CELLULAR IMMUNITY;
COMPLEX FORMATION;
CONTROLLED STUDY;
ENZYME KINETICS;
ENZYME REGULATION;
GLUCURONIDATION;
HETEROLOGOUS EXPRESSION;
HUMAN;
HUMAN CELL;
IMMUNOMODULATION;
INHIBITION KINETICS;
MOLECULAR WEIGHT;
PRIORITY JOURNAL;
PROTEIN EXPRESSION;
PROTEIN PROCESSING;
PROTEIN PROTEIN INTERACTION;
SIGNAL TRANSDUCTION;
CELL LINE;
CHEMISTRY;
DRUG EFFECT;
ENZYME SPECIFICITY;
GENETIC TRANSFECTION;
GENETICS;
IMMUNOPRECIPITATION;
KINETICS;
METABOLISM;
PROTEIN BINDING;
PROTEIN MULTIMERIZATION;
WESTERN BLOTTING;
ALTERNATIVE SPLICING;
BLOTTING, WESTERN;
CELL LINE;
ECDYSONE;
GLUCURONIDES;
GLUCURONOSYLTRANSFERASE;
HUMANS;
IMMUNOPRECIPITATION;
ISOENZYMES;
KINETICS;
PEPTIDES;
PROTEIN BINDING;
PROTEIN MULTIMERIZATION;
SIGNAL TRANSDUCTION;
SUBSTRATE SPECIFICITY;
TRANSFECTION;
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EID: 77950501858
PISSN: 00219258
EISSN: 1083351X
Source Type: Journal
DOI: 10.1074/jbc.M109.083139 Document Type: Article |
Times cited : (37)
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References (25)
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