2013
Mineralocorticoid Receptor Phosphorylation Regulates Ligand Binding and Renal Response to Volume Depletion and Hyperkalemia
Shibata S, Rinehart J, Zhang J, Moeckel G, Castañeda-Bueno M, Stiegler AL, Boggon TJ, Gamba G, Lifton RP. Mineralocorticoid Receptor Phosphorylation Regulates Ligand Binding and Renal Response to Volume Depletion and Hyperkalemia. Cell Metabolism 2013, 18: 660-671. PMID: 24206662, PMCID: PMC3909709, DOI: 10.1016/j.cmet.2013.10.005.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAngiotensin IIAnimalsChlorocebus aethiopsCOS CellsCytoplasmElectrolytesHumansHyperkalemiaKidneyLigandsMiceMolecular Sequence DataPhosphoprotein PhosphatasesPhosphorylationPhosphoserinePotassium, DietaryProtein Serine-Threonine KinasesProtein TransportRatsReceptors, MineralocorticoidSignal TransductionTranscriptional ActivationConceptsVolume depletionMineralocorticoid receptorAldosterone-dependent increaseHormone receptor activityNuclear hormone receptor activityMR activationRenal responseDistinct adaptive responsesAngiotensin IIDistal nephronCl reabsorptionHyperkalemiaMR ligand-binding domainReceptor activityApical proton pumpPlasma volumeReceptor bindingHomeostatic responseNuclear receptorsReceptor phosphorylation
2005
Polymorphisms in Human Organic Anion-transporting Polypeptide 1A2 (OATP1A2) IMPLICATIONS FOR ALTERED DRUG DISPOSITION AND CENTRAL NERVOUS SYSTEM DRUG ENTRY*
Lee W, Glaeser H, Smith LH, Roberts RL, Moeckel GW, Gervasini G, Leake BF, Kim RB. Polymorphisms in Human Organic Anion-transporting Polypeptide 1A2 (OATP1A2) IMPLICATIONS FOR ALTERED DRUG DISPOSITION AND CENTRAL NERVOUS SYSTEM DRUG ENTRY*. Journal Of Biological Chemistry 2005, 280: 9610-9617. PMID: 15632119, DOI: 10.1074/jbc.m411092200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionBrainEnkephalin, D-Penicillamine (2,5)-EstroneHumansKidneyKineticsLiverLiver-Specific Organic Anion Transporter 1Models, MolecularMolecular Sequence DataOligopeptidesOrgan SpecificityPolymorphism, GeneticPolymorphism, Single NucleotideProtein ConformationProtein Structure, SecondaryConceptsTransport activityPlasma membrane expressionCell surface biotinylationBroad substrate specificityGenomic DNA samplesReduced transport activityApparent molecular sizeSingle nucleotide polymorphismsGenetic variationSubstrate specificitySurface biotinylationGlycosylation statusOrganic anion-transporting polypeptide 1A2Substrate-dependent changesNonsynonymous polymorphismsRenal distal nephronMembrane expressionNucleotide polymorphismsG variantDrug uptake transportersSubstrate drugsConfocal microscopyDrug dispositionCentral nervous system entryT variant
2002
A Novel Gene Encoding a TIG Multiple Domain Protein Is a Positional Candidate for Autosomal Recessive Polycystic Kidney Disease
Xiong H, Chen Y, Yi Y, Tsuchiya K, Moeckel G, Cheung J, Liang D, Tham K, Xu X, Chen XZ, Pei Y, Zhao ZJ, Wu G. A Novel Gene Encoding a TIG Multiple Domain Protein Is a Positional Candidate for Autosomal Recessive Polycystic Kidney Disease. Genomics 2002, 80: 96-104. PMID: 12079288, DOI: 10.1006/geno.2002.6802.Peer-Reviewed Original ResearchConceptsNorthern blot analysisNovel genesGenetic intervalStrong positional candidate geneMultiple alternative transcriptsExpression of PKHD1Positional candidate genesAutosomal recessive polycystic kidney diseaseBlot analysisImmunoglobulin-like foldGenetic linkage analysisTIG domainMultiple-domain proteinsDomain proteinsSitu hybridization analysisGenomic regionsPolycystic kidney diseaseAlternative transcriptsPositional candidatesRecessive polycystic kidney diseaseCommon hereditary renal cystic diseasesHepatic disease 1Gene productsCloning strategyCandidate genes