Search results for "Enzyme complex"

showing 5 items of 55 documents

α-Synuclein expression levels do not significantly affect proteasome function and expression in mice and stably transfected PC12 cell lines

2004

α-Synuclein (α-syn) is a small protein of unknown function that is found aggregated in Lewy bodies, the histopathological hallmark of sporadic Parkinson disease and other synucleinopathies. Mutations in the α-syn gene and a triplication of its gene locus have been identified in early onset familial Parkinson disease. α-Syn turnover can be mediated by the proteasome pathway. A survey of published data may lead to the suggestion that overexpression of α-syn wild type, and/or their variants (A53T and A30P), may produce a decrease in proteasome activity and function, contributing to α-syn aggregation. To investigate the relationship between synuclein expression and proteasome function we have s…

Time Factorsanimal diseasesmedicine.disease_causePC12 CellsBiochemistryMicechemistry.chemical_compoundTransgenesPromoter Regions GeneticMice KnockoutGeneticsMutationInnervationBrainParkinson DiseaseProteasome complexAmyloidosisCell biologyInnervacióalpha-SynucleinAdditions and CorrectionsPèptidsPlasmidsProteasome Endopeptidase ComplexPrionsProtein subunitBlotting WesternImmunoblottingSynucleinsMice TransgenicNerve Tissue ProteinsBiologyTransfectionBacterial ProteinsMultienzyme ComplexesmedicineAnimalsImmunoprecipitationMolecular BiologyAlpha-synucleinSynucleinopathiesEpilepsyWild typeGenetic VariationCell BiologyAxonsRatsnervous system diseasesMice Inbred C57BLEpilèpsiaDisease Models AnimalLuminescent ProteinschemistryProteasomenervous systemSinapsiMutationSynapsesSynucleinAmiloïdosiPeptides
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Novel inhibitors of mitochondrial respiratory chain: endoperoxides from the marine tunicate Stolonica socialis.

2001

The Mediterranean tunicate Stolonica socialis contains a new class of powerful cytotoxic acetogenins, generically named stolonoxides. In this paper, which also details the isolation and chemical characterization of a minor component (3a) of the tunicate extract, we report the potent inhibitory activity (IC(50) < 1 microM) of stolonoxides (1a and 3a) on mitochondrial electron transfer. The compounds affect specifically the functionality of complex II (succinate:ubiquinone oxidoreductase) and complex III (ubiquinol:cytochrome C oxidoreductase) in mammalian cells, thereby causing a rapid collapse of the whole energetic metabolism. This result, which differs from the properties of similar known…

UbiquinolMagnetic Resonance SpectroscopyStereochemistryIn Vitro TechniquesFunctional activityElectron Transportchemistry.chemical_compoundElectron Transport Complex IIIMarine Natural ProductOxidoreductaseMultienzyme ComplexesDrug DiscoveryMediterranean SeaAnimalsNADH NADPH OxidoreductasesUrochordataEnzyme InhibitorsFuranschemistry.chemical_classificationElectron Transport Complex IbiologyCytochrome cElectron Transport Complex IISuccinate dehydrogenaseElectron Transport Complex IIMyocardiumDioxolanesMitochondriaPeroxidesSuccinate DehydrogenaseMitochondrial respiratory chainchemistryBiochemistryElectron Transport Complex ICoenzyme Q – cytochrome c reductasebiology.proteinMolecular MedicineCattleStructure ElucidationOxidoreductasesJournal of medicinal chemistry
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New molecular aspects of regulation of mitochondrial activity by fenofibrate and fasting

2000

Abstract Fenofibrate and fasting are known to regulate several genes involved in lipid metabolism in a similar way. In this study measuring several mitochondrial enzyme activities, we demonstrate that, in contrast to citrate synthase and complex II, cytochrome c oxidase (COX) is a specific target of these two treatments. In mouse liver organelles, Western blot experiments indicated that mitochondrial levels of p43, a mitochondrial T3 receptor, and mitochondrial peroxisome proliferator activated receptor (mt-PPAR), previously described as a dimeric partner of p43 in the organelle, are increased by both fenofibrate and fasting. In addition, in PPARα-deficient mice, this influence was abolishe…

[SDV]Life Sciences [q-bio]Receptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorMitochondria LiverMitochondrionBiochemistryMice0302 clinical medicineFenofibrateStructural BiologyBIOLOGIE CELLULAIRECitrate synthaseFibrateReceptorComputingMilieux_MISCELLANEOUSMice Knockoutchemistry.chemical_classification0303 health sciencesFenofibratebiologyElectron Transport Complex IIFastingPeroxisomeDNA-Binding ProteinsSuccinate Dehydrogenase[SDV] Life Sciences [q-bio]OxidoreductasesDimerizationmedicine.drugPeroxisome proliferator activated receptormedicine.medical_specialtyBiophysicsCitrate (si)-Synthase[INFO] Computer Science [cs]Mitochondrial T3 receptorElectron Transport Complex IV03 medical and health sciencesMultienzyme ComplexesInternal medicineGeneticsmedicineAnimalsCytochrome c oxidase[INFO]Computer Science [cs]MitochondrionMolecular BiologyCrosses Genetic030304 developmental biologyOrganellesLipid metabolismCell BiologyMice Inbred C57BLEndocrinologychemistrybiology.protein030217 neurology & neurosurgeryTranscription Factors
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Engineering a Saccharomyces cerevisiae Wine Yeast That Exhibits Reduced Ethanol Production during Fermentation under Controlled Microoxygenation Cond…

2006

ABSTRACTWe recently showed that expressing an H2O-NADH oxidase inSaccharomyces cerevisiaedrastically reduces the intracellular NADH concentration and substantially alters the distribution of metabolic fluxes in the cell. Although the engineered strain produces a reduced amount of ethanol, a high level of acetaldehyde accumulates early in the process (1 g/liter), impairing growth and fermentation performance. To overcome these undesirable effects, we carried out a comprehensive analysis of the impact of oxygen on the metabolic network of the same NADH oxidase-expressing strain. While reducing the oxygen transfer rate led to a gradual recovery of the growth and fermentation performance, its i…

[SDV]Life Sciences [q-bio]Saccharomyces cerevisiaeWineMICROOXYGENATIONEthanol fermentationBiologyApplied Microbiology and Biotechnology03 medical and health scienceschemistry.chemical_compoundOxygen ConsumptionMultienzyme ComplexesETHANOLNADPHEthanol fuelNADH NADPH Oxidoreductases030304 developmental biologySACCHAROMYCES CEREVISIAE0303 health sciencesEcology030306 microbiologyAcetaldehydebiology.organism_classificationPhysiology and BiotechnologyMicrooxygenationYeastRecombinant ProteinsLactococcus lactisYeast in winemakingKineticsGlucosechemistryBiochemistryGenes BacterialFermentationWINE YEASTFermentationGenetic EngineeringFood ScienceBiotechnology
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Inhibition of the herpes simplex virus-coded thymidine kinase-complex by 9-?-D-arabinofuranosyladenine 5?-monophosphate (ara-AMP) and 9-(2-hydroxyeth…

1984

The thymidine kinase-complex isolated from herpes simplex virus type 1 and type 2 (HSV-1 and HSV-2) is associated with the following enzyme activities: ATP:dThd (dCyd) deoxypyrimidine kinase, ATP:dTMP thymidylate kinase, ADP:dThd- and AMP:dThd5′-phosphotransferase. In kinetic experiments it is shown that ara-AMP inhibits AMP:dThd- and ADP:dThd phosphotransferase activity, while acyclo-GMP impairs ADP:dThd phosphotransferase reaction only; the inhibition was found to be non-compertitive. The functional subunit ATP:dThd kinase was not affected by either compound.

chemistry.chemical_classificationArabinonucleotidesGuanineKinaseAcyclovirGeneral MedicineBiologyThymidine KinaseThymidylate kinaseVirologyMolecular biologyPhosphotransferaseKineticschemistry.chemical_compoundEnzymechemistryBiochemistryMultienzyme ComplexesThymidine kinaseVirologySimplexvirusNucleotideThymidineVidarabine PhosphateArchives of Virology
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