Short‐term response to dietary therapy in molybdenum cofactor deficiency
Boles R, Ment L, Meyn M, Horwich A, Kratz L, Rinaldo P. Short‐term response to dietary therapy in molybdenum cofactor deficiency. Annals Of Neurology 1993, 34: 742-744. PMID: 7694543, DOI: 10.1002/ana.410340520.Peer-Reviewed Original ResearchConceptsMolybdenum cofactor deficiencyCofactor deficiencyShort-term clinical improvementDietary methionine restrictionUrinary sulphiteClinical relapseClinical improvementLaboratory featuresDietary therapySevere irritabilityLactic acidosisHead growthMethionine restrictionDevelopmental delayCysteine supplementationCommercial dipstickTherapyIrritabilityDeficiencyDevelopmental progressRelapseHypouricemiaAcidosisInfantsMicrocephalyFolding in vivo of bacterial cytoplasmic proteins: Role of GroEL
Horwich A, Low K, Fenton W, Hirshfield I, Furtak K. Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL. Cell 1993, 74: 909-917. PMID: 8104102, DOI: 10.1016/0092-8674(93)90470-b.Peer-Reviewed Original ResearchMeSH KeywordsATP-Binding Cassette TransportersBacterial ProteinsBacteriophage lambdaCarrier ProteinsChaperonin 60Citrate (si)-SynthaseEscherichia coliEscherichia coli ProteinsHeat-Shock ProteinsKetoglutarate Dehydrogenase ComplexMaltoseMaltose-Binding ProteinsMethionineMonosaccharide Transport ProteinsOperonOrnithine CarbamoyltransferasePlasmidsPolyribonucleotide NucleotidyltransferasePromoter Regions, GeneticProtein BiosynthesisProtein FoldingProtein Sorting SignalsSequence DeletionTemperatureTransduction, GeneticConceptsCytoplasmic proteinsTemperature-sensitive lethal mutationBacterial cytoplasmic proteinsE. coli chaperonin GroELMaltose-binding proteinRole of GroELNative tertiary structureEssential genesChaperonin GroELBacterial cytoplasmMutant cellsLethal mutationsNonpermissive temperatureGenetic informationPolynucleotide phosphorylaseGeneral translationTertiary structureCitrate synthasePathways of transferKetoglutarate dehydrogenaseGeneral roleGroELNative conformationProteinTest proteins