2008
A novel missense mutation in SLC34A3 that causes hereditary hypophosphatemic rickets with hypercalciuria in humans identifies threonine 137 as an important determinant of sodium-phosphate cotransport in NaPi-IIc
Jaureguiberry G, Carpenter TO, Forman S, Jüppner H, Bergwitz C. A novel missense mutation in SLC34A3 that causes hereditary hypophosphatemic rickets with hypercalciuria in humans identifies threonine 137 as an important determinant of sodium-phosphate cotransport in NaPi-IIc. American Journal Of Physiology. Renal Physiology 2008, 295: f371-f379. PMID: 18480181, PMCID: PMC2519180, DOI: 10.1152/ajprenal.00090.2008.Peer-Reviewed Original ResearchMeSH KeywordsAdultAllelesAnimalsBase SequenceExocytosisFamilial Hypophosphatemic RicketsFemaleHaplotypesHumansHypercalciuriaKidneyMaleMolecular Sequence DataMutation, MissenseOocytesOpossumsPhosphatesPolymorphism, Single NucleotideSodiumSodium-Phosphate Cotransporter ProteinsSodium-Phosphate Cotransporter Proteins, Type IIcThreonineXenopus laevisConceptsEncoding enhanced green fluorescent proteinHereditary hypophosphatemic ricketsNaPi-IIcSodium-phosphate cotransporterLoss of expressionAmino acid residuesSodium-phosphate cotransportGreen fluorescence proteinImportant functional roleComplete lossOpossum kidneyHypophosphatemic ricketsXenopus laevis oocytesNovel missense mutationPaternal alleleWild-typeFunctional analysisFluorescence proteinNH2 terminusAcid residuesApical patchesCompound heterozygous mutationsExpression plasmidFunctional roleRecurrent kidney stones
1997
Cloning and characterization of the vitamin D receptor from Xenopus laevis.
Li Y, Bergwitz C, Jüppner H, Demay M. Cloning and characterization of the vitamin D receptor from Xenopus laevis. Endocrinology 1997, 138: 2347-53. PMID: 9165021, DOI: 10.1210/endo.138.6.5210.Peer-Reviewed Original ResearchMeSH KeywordsAgingAmino Acid SequenceAnimalsBase SequenceBone and BonesChickensCloning, MolecularDimerizationEmbryo, NonmammalianFemaleGene Expression Regulation, DevelopmentalHumansIntestine, SmallKidneyMiceMolecular Sequence DataOrgan SpecificityPolymerase Chain ReactionRatsReceptors, CalcitriolReceptors, Retinoic AcidRecombinant ProteinsRetinoic Acid Receptor alphaSequence Homology, Amino AcidSkinSpecies SpecificityXenopus laevisConceptsVitamin D response elementRat osteocalcin vitamin D response elementVitamin D receptorOsteocalcin vitamin D response elementLower vertebrate speciesMessenger RNA speciesHuman vitamin D receptorMouse retinoid X receptor alphaAmino acid residuesRetinoid X receptor alphaRat osteocalcin vitamin D responsive elementAmino acid levelsX receptor alphaVertebrate speciesRNA speciesMammalian cellsTransfected mammalian cellsXenopus developmentDependent transactivationD response elementNuclear receptor superfamilyXenopus tissuesDNA bindingIon homeostasisNorthern analysisCloning and Characterization of the Vitamin D Receptor from Xenopus laevis*
Li Y, Bergwitz C, Jüppner H, Demay M. Cloning and Characterization of the Vitamin D Receptor from Xenopus laevis*. Endocrinology 1997, 138: 2347-2353. DOI: 10.1210/en.138.6.2347.Peer-Reviewed Original ResearchVitamin D response elementRat osteocalcin vitamin D responsive elementAmino acid residuesTransfected mammalian cellsMessenger RNA speciesVitamin D receptorNuclear receptor superfamilyOsteocalcin vitamin D response elementAmino acid levelsHuman vitamin D receptorRNA speciesXenopus tissuesD response elementDNA bindingMammalian cellsVertebrate speciesXenopus developmentAcid residuesNorthern analysisReceptor superfamilyIon homeostasisHormone bindingXenopusD receptorMessenger RNA