2010
Aryl hydrocarbon receptor and NF-E2-related factor 2 are key regulators of human MRP4 expression
Xu S, Weerachayaphorn J, Cai SY, Soroka CJ, Boyer JL. Aryl hydrocarbon receptor and NF-E2-related factor 2 are key regulators of human MRP4 expression. AJP Gastrointestinal And Liver Physiology 2010, 299: g126-g135. PMID: 20395535, PMCID: PMC2904108, DOI: 10.1152/ajpgi.00522.2010.Peer-Reviewed Original ResearchMeSH Keywords5' Flanking RegionAnimalsAryl Hydrocarbon Receptor Nuclear TranslocatorBase SequenceBasic Helix-Loop-Helix Transcription FactorsBinding SitesButylaminesChromatin ImmunoprecipitationDose-Response Relationship, DrugElectrophoretic Mobility Shift AssayGenes, ReporterHep G2 CellsHepatocytesHumansMethylcholanthreneMiceMolecular Sequence DataMultidrug Resistance-Associated ProteinsMutationNF-E2-Related Factor 2Polychlorinated DibenzodioxinsPromoter Regions, GeneticPyrazinesReceptors, Aryl HydrocarbonResponse ElementsRNA InterferenceRNA, MessengerThionesThiophenesTime FactorsTransfectionConceptsMRP4 expressionAryl hydrocarbon receptorNF-E2Renal proximal tubule epitheliumCholestatic liver injuryHydrocarbon receptorXenobiotic response elementProximal tubule epitheliumMultidrug resistance protein 4Factor 2Bile salt conjugatesNuclear receptor agonistsLiver injuryPromoter activityReceptor agonistTherapeutic benefitAnimal modelsNrf2 activatorsTubule epitheliumHuman MRP4Conjugated steroidsNuclear factorAdaptive upregulationOxidative stressLuciferase reporter
2009
Nuclear factor erythroid 2–related factor 2 is a positive regulator of human bile salt export pump expression
Weerachayaphorn J, Cai S, Soroka CJ, Boyer JL. Nuclear factor erythroid 2–related factor 2 is a positive regulator of human bile salt export pump expression. Hepatology 2009, 50: 1588-1596. PMID: 19821532, PMCID: PMC3013376, DOI: 10.1002/hep.23151.Peer-Reviewed Original ResearchMeSH KeywordsATP Binding Cassette Transporter, Subfamily B, Member 11ATP-Binding Cassette TransportersBase SequenceHep G2 CellsHepatocytesHumansMaf Transcription FactorsMolecular Sequence DataNF-E2-Related Factor 2PyrazinesReverse Transcriptase InhibitorsRNA, MessengerSignal TransductionThionesThiophenesConceptsBile salt export pumpCholestatic liver injuryPositive transcriptional regulatorElectrophoretic mobility shift assaysHepG2 cellsBSEP expressionChromatin immunoprecipitation assaysBSEP promoterMobility shift assaysAdditional transcriptional factorsProximal promoter regionBSEP promoter activitySmall interfering RNAsFactor 2Liver injuryNuclear factorAntioxidant responsive elementTranscriptional regulatorsNrf2 transcriptional activationTranscriptional activationPositive regulatorBile salt export pump expressionNuclear farnesoid X receptorImmunoprecipitation assaysShift assays
2007
Threonine-509 Is a Determinant of Apparent Affinity for Both Substrate and Cations in the Human Na+/Dicarboxylate Cotransporter †
Weerachayaphorn J, Pajor AM. Threonine-509 Is a Determinant of Apparent Affinity for Both Substrate and Cations in the Human Na+/Dicarboxylate Cotransporter †. Biochemistry 2007, 47: 1087-1093. PMID: 18161988, PMCID: PMC2570185, DOI: 10.1021/bi701417h.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAnimalsChlorocebus aethiopsCitric AcidCOS CellsDicarboxylic Acid TransportersGene ExpressionHumansKineticsMolecular Sequence DataMutationOrganic Anion Transporters, Sodium-DependentRabbitsRecombinant ProteinsSequence Homology, Amino AcidSodiumSubstrate SpecificitySuccinic AcidSymportersThreonineConceptsTransmembrane helix 7Functional differencesApparent affinityApparent sodium affinitySubstrate Binding SiteAmino acid differencesCitric acid cycleCitrate affinityHelix 7Substrate specificityPosition -509Rabbit sequenceIndividual residuesAcid cycleAcid differencesSimilar apparent affinitiesLoop regionIntermediate KmAmino acidsBinding sitesMutantsNaDC1SerineThreonineExhibit differences