Search results for "Inositol-1"

showing 2 items of 2 documents

Inducing Cold-Sensitivity in the Frigophilic Fly Drosophila montana by RNAi.

2016

Cold acclimation is a critical physiological adaptation for coping with seasonal cold. By increasing their cold tolerance individuals can remain active for longer at the onset of winter and can recover more quickly from a cold shock. In insects, despite many physiological studies, little is known about the genetic basis of cold acclimation. Recently, transcriptomic analyses in Drosophila virilis and D. montana revealed candidate genes for cold acclimation by identifying genes upregulated during exposure to cold. Here, we test the role of myo-inositol-1-phosphate synthase (Inos), in cold tolerance in D. montana using an RNAi approach. D. montana has a circumpolar distribution and overwinters…

CartographyEvolutionary GeneticsArthropodaDeath RatesAcclimatizationGene ExpressionArtificial Gene Amplification and ExtensionInsect PhysiologyResearch and Analysis MethodsBiochemistryPolymerase Chain ReactionExtreme Cold WeatherRNA interferenceModel OrganismsPopulation MetricsGeneticsAnimalsAnimal PhysiologyMolecular Biology TechniquesMolecular BiologyDemographyInvertebrate PhysiologyEvolutionary BiologyLatitudePopulation BiologyGeographyGene Expression ProfilingDrosophila MelanogasterfungiOrganismsBiology and Life SciencesAnimal ModelsInvertebratesCold TemperatureNucleic acidsInsectsGene Expression RegulationGenetic interferencePeople and PlacesEarth SciencesRNADrosophilaFemaleMyo-Inositol-1-Phosphate SynthaseEpigeneticsZoologyEntomologyResearch ArticlePloS one
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A novel target of lithium therapy.

2000

Phosphatases converting 3'-phosphoadenosine 5'-phosphate (PAP) into adenosine 5'-phosphate are of fundamental importance in living cells as the accumulation of PAP is toxic to several cellular systems. These enzymes are lithium-sensitive and we have characterized a human PAP phosphatase as a potential target of lithium therapy. A cDNA encoding a human enzyme was identified by data base screening, expressed in Escherichia coli and the 33 kDa protein purified to homogeneity. The enzyme exhibits high affinity for PAP (K(m)1 microM) and is sensitive to subtherapeutic concentrations of lithium (IC(50)=0.3 mM). The human enzyme also hydrolyzes inositol-1, 4-bisphosphate with high affinity (K(m)=0…

Inositol-14-bisphosphateDNA ComplementaryBicinePhosphataseMolecular Sequence DataBiophysicschemistry.chemical_elementSaccharomyces cerevisiaeLithiummedicine.disease_causeBiochemistrychemistry.chemical_compoundStructural BiologyNucleotidasesComplementary DNAPhosphataseGeneticsmedicineEscherichia coliHumansAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliIC50Chromatography High Pressure Liquidchemistry.chemical_classificationExpressed Sequence TagsBase Sequence3′-Phosphoadenosine 5′-phosphateCell BiologyMolecular biologyAdenosineAdenosine MonophosphatePhosphoric Monoester HydrolasesAdenosine DiphosphateEnzymechemistryBiochemistryLithiummedicine.drugHumanFEBS letters
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