Search results for "Reductases"

showing 10 items of 276 documents

Enzyme-responsive silica mesoporous supports capped with azopyridinium salts for controlled delivery applications

2012

11 páginas, 7 figuras, 3 tablas y 2 esquemas

INGENIERIA DE LA CONSTRUCCIONCell SurvivalPyridinesmedia_common.quotation_subjectenzymesNanoparticleNanotechnologyPyridinium Compoundsmesoporous materialsCatalysisgated materialsHeLachemistry.chemical_compoundQUIMICA ORGANICAQUIMICA ANALITICAmedicineRhodamine BHumansGated materialsInternalizationAzopyridinium derivativemedia_commonbiologyChemistryRhodaminesOrganic ChemistryQUIMICA INORGANICAGeneral Chemistrybiology.organism_classificationSilicon DioxideCombinatorial chemistryMesoporous materialsEnzymesazopyridinium derivativeDrug deliveryDrug deliveryMCF-7 CellsNanoparticlesnanoparticlesMesoporous materialOxidoreductasesAzo CompoundsPorosityCamptothecinIntracellularmedicine.drugHeLa Cells
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Dual enzyme-responsive "turn-on" fluorescence sensing systems based on in situ formation of 7-hydroxy-2-iminocoumarin scaffolds.

2015

A new strategy for the simultaneous fluorogenic detection of two distinct enzyme activities namely hydrolase (amidase or esterase) and reductase is described. This innovative biosensing method is based on the powerful "covalent-assembly" principle that involves in situ synthesis of a fluorophore from a non-fluorescent caged precursor and through domino reactions triggered by the two analytes of interest. To establish this approach, penicillin G acylase (PGA) (or pig liver esterase (PLE)) and nitroreductase (NTR) were chosen as model enzymes, and original bis-O-protected 2,4-dihydroxycinnamonitrile derivatives acting as dual-reactive probes readily convertible to highly fluorescent 7-hydroxy…

In situFluorophoreMolecular StructureStereochemistryChemistryOrganic ChemistryEsterasesBiochemistryFluorescenceEsteraseFluorescenceAmidaseAmidohydrolasesNitroreductasechemistry.chemical_compoundCoumarinsHydrolasePhysical and Theoretical ChemistryOxidoreductasesBiosensorOrganicbiomolecular chemistry
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A nitroreductase and glutathione responsive nanoplatform for integration of gene delivery and near-infrared fluorescence imaging

2020

A novel platform rationally integrating indocyanine green analogues and an arginine-rich dendritic peptide with both nitroreductase (NTR) and glutathione (GSH) reduction responsive linkers was developed. This multifunctional platform can enable selective and efficient gene delivery and specific turn-on fluorescence imaging in tumors.

Indocyanine GreenGlutathione metabolismFluorescence-lifetime imaging microscopyNear-Infrared Fluorescence ImagingInfrared RaysPeptideGene deliveryCatalysischemistry.chemical_compoundNitroreductaseOptical imagingMaterials ChemistryHumansFluorescent Dyeschemistry.chemical_classificationOptical ImagingGene Transfer TechniquesMetals and Alloysfood and beveragesGeneral ChemistryGlutathioneNitroreductasesGlutathioneSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialschemistryCeramics and CompositesBiophysicsPeptidesHeLa CellsChemical Communications
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The elemental role of iron in DNA synthesis and repair

2017

Iron is an essential redox element that functions as a cofactor in many metabolic pathways. Critical enzymes in DNA metabolism, including multiple DNA repair enzymes (helicases, nucleases, glycosylases, demethylases) and ribonucleotide reductase, use iron as an indispensable cofactor to function. Recent striking results have revealed that the catalytic subunit of DNA polymerases also contains conserved cysteine-rich motifs that bind iron–sulfur (Fe/S) clusters that are essential for the formation of stable and active complexes. In line with this, mitochondrial and cytoplasmic defects in Fe/S cluster biogenesis and insertion into the nuclear iron-requiring enzymes involved in DNA synthesis a…

Iron-Sulfur Proteins0301 basic medicineDNA RepairDNA polymeraseDNA damageDNA repairIronBiophysicsDNA repairEukaryotic DNA replicationSaccharomyces cerevisiaeBiochemistryDNA GlycosylasesBiomaterials03 medical and health sciencesRibonucleotide ReductasesHumansProtein–DNA interactionRibonucleotide reductaseReplication protein Achemistry.chemical_classificationDNA ligaseDeoxyribonucleasesDNA synthesis030102 biochemistry & molecular biologybiologyIron deficiencyDNA HelicasesMetals and AlloysHelicaseDNAYeast030104 developmental biologyIron cofactorBiochemistrychemistryChemistry (miscellaneous)biology.proteinIron-sulfur clusterMetallomics
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Regulatory O 2 tensions for the synthesis of fermentation products in Escherichia coli and relation to aerobic respiration

1997

In an oxystat, the synthesis of the fermentation products formate, acetate, ethanol, lactate, and succinate of Escherichia coli was studied as a function of the O2 tension (pO2) in the medium. The pO2 values that gave rise to half-maximal synthesis of the products (pO0. 5) were 0.2-0.4 mbar for ethanol, acetate, and succinate, and 1 mbar for formate. The pO0.5 for the expression of the adhE gene encoding alcohol dehydrogenase was approximately 0.8 mbar. Thus, the pO2 for the onset of fermentation was distinctly lower than that for anaerobic respiration (pO0.5/= 5 mbar), which was determined earlier. An essential role for quinol oxidase bd in microaerobic growth was demonstrated. A mutant de…

Iron-Sulfur ProteinsAnaerobic respirationFormatesCellular respirationSuccinic AcidAcetatesBiologymedicine.disease_causeColiphagesBiochemistryMicrobiologyGene Expression Regulation Enzymologicchemistry.chemical_compoundBioreactorsBacterial ProteinsMultienzyme ComplexesEscherichia coliGeneticsmedicineFormateAnaerobiosisMolecular BiologyEscherichia coliMixed acid fermentationAlcohol dehydrogenaseNitratesEthanolEthanolEscherichia coli ProteinsAlcohol DehydrogenaseGene Expression Regulation BacterialGeneral MedicineAldehyde OxidoreductasesAerobiosisArtificial Gene FusionOxygenRepressor ProteinsLac OperonchemistryBiochemistryFermentationLactatesbiology.proteinFermentationOxidoreductasesBacterial Outer Membrane ProteinsArchives of Microbiology
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Yeast Dun1 Kinase Regulates Ribonucleotide Reductase Inhibitor Sml1 in Response to Iron Deficiency

2014

Iron is an essential micronutrient for all eukaryotic organisms because it participates as a redox-active cofactor in many biological processes, including DNA replication and repair. Eukaryotic ribonucleotide reductases (RNRs) are Fe-dependent enzymes that catalyze deoxyribonucleoside diphosphate (dNDP) synthesis. We show here that the levels of the Sml1 protein, a yeast RNR large-subunit inhibitor, specifically decrease in response to both nutritional and genetic Fe deficiencies in a Dun1-dependent but Mec1/Rad53- and Aft1-independent manner. The decline of Sml1 protein levels upon Fe starvation depends on Dun1 forkhead-associated and kinase domains, the 26S proteasome, and the vacuolar pr…

Iron-Sulfur ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleotideIronDeoxyribonucleotidesGenes FungalSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeRibonucleotide reductase inhibitorProtein Serine-Threonine KinasesBiologyProtein degradationchemistry.chemical_compoundTristetraprolinRibonucleotide ReductasesAspartic Acid EndopeptidasesPhosphorylationMolecular BiologyCheckpoint Kinase 2Binding SitesKinaseIntracellular Signaling Peptides and ProteinsArticlesCell Biologybiology.organism_classificationDNA-Binding ProteinsDeoxyribonucleosideCheckpoint Kinase 2chemistryBiochemistryProteolysisGene DeletionTranscription FactorsMolecular and Cellular Biology
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Stimulation of Fe-S cluster insertion into apoFNR by Escherichia coli glutaredoxins 1, 2 and 3 in vitro.

2004

Abstract The oxygen sensor fumarate nitrate reductase regu-lator (FNR) of Escherichia coli contains in the active (anaerobic)state a [4Fe–4S] 2þ cluster which is lost after exposure to O 2 .Inaerobically prepared apoFNR, or in FNR obtained by treatmentof [4Fe–4S] FNR with O 2 in vitro, intramolecular cysteinedisulfides are found, including the cysteine residues which serveas ligands for the Fe–S cluster. It is shown here that thereconstitution of [4Fe–4S] FNR from this form of aerobicapoFNR was preceded by a long lag phase when glutathione wasused as the reducing agent. Addition of E. coli glutaredoxins(Grx) 1, 2 or 3 decreased the lag phase greatly and stimulatedthe reconstitution rate slig…

Iron-Sulfur ProteinsTime FactorsReducing agentFNRGlutaredoxinBiophysicsBiologyReductaseSulfidesmedicine.disease_causeNitrate reductaseBiochemistryOxygen sensorchemistry.chemical_compoundStructural BiologyGlutaredoxinGeneticsmedicineEscherichia coliCysteineDisulfidesThioredoxinMolecular BiologyEscherichia coliGlutaredoxinsDisulfide reductaseEscherichia coli ProteinsProteinsCell BiologyGlutathioneGlutathioneOxygenBiochemistrychemistryMultigene FamilyThioredoxinOxidoreductasesCysteineTranscription FactorsFEBS letters
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Tigliane diterpenes from the latex of Euphorbia obtusifolia with inhibitory activity on the mammalian mitochondrial respiratory chain

2003

Abstract Six diterpenes isolated from the latex of Euphorbia obtusifolia Poir. (Euphorbiaceae) were evaluated for their inhibition of the NADH oxidase activity in submitochondrial particles from beef heart. 4,20-Dideoxyphorbol-12,13-bis(isobutyrate) was the most potent inhibitor and showed an inhibitory concentration with IC 50 value of 2.6±0.3 mM. In the present study, some structure–activity trends are suggested for the inhibitory activity of the mammalian mitochondrial respiratory chain of these natural product derivatives of 4-deoxyphorbol esters.

LatexStereochemistryRespiratory chainIn Vitro TechniquesMitochondria HeartElectron Transportchemistry.chemical_compoundEuphorbiaRotenoneDrug DiscoveryAnimalsNADH NADPH OxidoreductasesSubmitochondrial particlePharmacologyEuphorbiaOxidase testbiologyPlant ExtractsUncoupling AgentsEuphorbiaceaeBiological activitybiology.organism_classificationMitochondrial respiratory chainchemistryBiochemistryCattleDiterpenesDiterpeneJournal of Ethnopharmacology
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Supplementary Ultraviolet-B Radiation Induces a Rapid Reversal of the Diadinoxanthin Cycle in the Strong Light-Exposed DiatomPhaeodactylum tricornutu…

2002

AbstractA treatment of the diatom Phaeodactylum tricornutum with high light (HL) in the visible range led to the conversion of diadinoxanthin (Dd) to diatoxanthin (Dt). In a following treatment with HL plus supplementary ultraviolet (UV)-B, the Dt was rapidly epoxidized to Dd. Photosynthesis of the cells was inhibited under HL + UV-B. This is accounted for by direct damage by UV-B and damage because of the UV-B-induced reversal of the Dd cycle and the associated loss of photoprotection. The reversal of the Dd cycle by UV-B was faster in the presence of dithiothreitol, an inhibitor of the Dd de-epoxidase. Our results imply that the reversal of the Dd cycle by HL + UV-B was caused by an incre…

LightUltraviolet RaysPhysiologyPlant ScienceXanthophyllsBiologyPhotosynthesisThylakoidsDithiothreitolchemistry.chemical_compoundGeneticsPhaeodactylum tricornutumDiatomsDiadinoxanthinDiatoxanthinDarknessHydrogen-Ion ConcentrationAscorbic acidbiology.organism_classificationAdaptation PhysiologicalDithiothreitolBiochemistrychemistryThylakoidPhotoprotectionBiophysicsOxidoreductasesSignal TransductionResearch ArticlePlant Physiology
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Nitric oxide synthase activity is inducible in rat, but not rabbit alveolar macrophages, with a concomitant reduction in arginase activity

1995

Alveolar macrophages were obtained by broncho-alveolar lavage of isolated rat and rabbit lungs and cultured (2.5 × 106 cells/dish) for 18 h in the absence or presence of bacterial lipopolysaccharides (LPS) alone or in combination with cytokines. Thereafter, accumulation of 3H-citrulline (NO synthase activity) and 3H-ornithine (arginase activity) were determined. During incubation of rat alveolar macrophages with 3H-arginine clear amounts of 3H-citrulline and 3H-ornithine (3.8 and 4.6% of the added 3H-arginine, respectively) were formed and most of these metabolites appeared in the incubation medium (ratios extra-/intracellular of 17 and 70 for 3H-citrulline and 3H-ornithine, respectively). …

LipopolysaccharidesMaleOrnithinemedicine.medical_specialtyArginineIn Vitro TechniquesArginineNitric OxideDexamethasoneNitric oxideRats Sprague-Dawleychemistry.chemical_compoundInternal medicineMacrophages AlveolarmedicineCitrullineAnimalsNitritesPharmacologyomega-N-MethylarginineArginasebiologyGeneral MedicineRatsArginaseNitric oxide synthaseEndocrinologychemistryEnzyme InductionOrnithine transportbiology.proteinCitrullineCytokinesFemaleTumor necrosis factor alphaAmino Acid OxidoreductasesRabbitsNitric Oxide SynthaseIntracellularNaunyn-Schmiedeberg's Archives of Pharmacology
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