Search results for "binding proteins"

showing 10 items of 911 documents

Xanthine oxidase catalyzes the oxidation of retinol.

2007

In mammals, xanthine oxidase (E.C. 1.17.3.2) catalyzes the hydroxylation of a wide variety of heterocyclic substrates such as purines, pyrimidines, and pterins, in addition to aldehydes [1] as all-trans-retinaldehyde [2-5]. Here, we show that buttermilk xanthine oxidase was capable to oxidizing all-trans-retinol (t-ROL) to all-trans-retinaldehyde (t-RAL) that was successively oxidized to all-trans-retinoic acid (t-RA). A rise in the enzyme activity, when t-ROL-CRBP complex was assayed, with respect to the free t-ROL, was observed. Furthermore, treatment of the enzyme with Na2S and glutathione resulted in a significant increment in catalytic activity toward t-ROL and t-RAL, due to the recons…

Xanthine OxidaseReceptors Retinoic Acidchemistry.chemical_elementTretinoinHydroxylationLigandsCatalysisHydroxylationchemistry.chemical_compoundRetinoidsDrug DiscoveryHumansXanthine oxidasePurine metabolismVitamin APharmacologychemistry.chemical_classificationHypoxanthinebiologyEthanolRetinol-Binding Proteins CellularGeneral MedicineGlutathioneEnzyme assayOxygenRetinol-Binding ProteinsKineticsEnzymechemistryBiochemistryXanthine dehydrogenaseMolybdenumbiology.proteinXanthine oxidase retinol oxidation retinaldehyde oxidation retinoic acid biosynthesis cellular retinoid binding protein (CRBP) Cellular retinoic acid binding protein (CRABP) retinol binding protein (RBP)Journal of enzyme inhibition and medicinal chemistry
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Expression of the human XPB/ERCC-3 excision repair gene-homolog in the sponge Geodia cydonium after exposure to ultraviolet radiation.

1998

Abstract The marine demosponge Geodia cydonium encodes a gene, termed GCXPB , which displays 62% identity to the human XPB/ERCC-3 gene that specifically corrects the repair defect in xeroderma pigmentosum and in Cockayne's syndrome. The cDNA was isolated and characterized the deduced aa sequence, XPB_GEOCY, with the calculated size of 91,541 Da comprises the characteristic domains found in the related helicases. Phylogenetic tree analysis revealed that the sponge sequence is grouped to the metazoan related XPB/ERCC-3 polypeptides. Northern Blot analyses have been performed with sponge samples collected at different depths, thus exposed to different intensities of UV sunlight in the field. T…

Xeroderma pigmentosumDNA ComplementaryDNA RepairUltraviolet RaysMolecular Sequence DataBiologyToxicologyRadiation ToleranceEvolution MolecularComplementary DNAGene expressionGeneticsmedicineAnimalsNorthern blotAmino Acid SequenceCloning MolecularMolecular BiologyGenePhylogenyGeneticsinduced dna-damage; xeroderma-pigmentosum; cockaynes-syndrome; alignment; biomarker; protein; stressSequence Homology Amino AcidNucleic acid sequenceDNA HelicasesHelicaseSequence Analysis DNAmedicine.diseaseMolecular biologyPoriferaUp-RegulationDNA-Binding Proteinsbiology.proteinNucleotide excision repairDNA DamageMutation research
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Polar Localization of a Tripartite Complex of the Two-Component System DcuS/DcuR and the Transporter DctA in Escherichia coli Depends on the Sensor K…

2014

The C4-dicarboxylate responsive sensor kinase DcuS of the DcuS/DcuR two-component system of E. coli is membrane-bound and reveals a polar localization. DcuS uses the C4-dicarboxylate transporter DctA as a co-regulator forming DctA/DcuS sensor units. Here it is shown by fluorescence microscopy with fusion proteins that DcuS has a dynamic and preferential polar localization, even at very low expression levels. Single assemblies of DcuS had high mobility in fast time lapse acquisitions, and fast recovery in FRAP experiments, excluding polar accumulation due to aggregation. DctA and DcuR fused to derivatives of the YFP protein are dispersed in the membrane or in the cytosol, respectively, when …

Yellow fluorescent proteinCardiolipinslcsh:MedicineMicrobiologyMreBMicrobial PhysiologyBacterial Physiologylcsh:ScienceCytoskeletonMicrobial MetabolismDicarboxylic Acid TransportersMultidisciplinaryEscherichia coli K12biologyBacterial GrowthEscherichia coli Proteinslcsh:RMicrobial Growth and DevelopmentBiology and Life SciencesFluorescence recovery after photobleachingBacteriologyFusion proteinTwo-component regulatory systemBacterial BiochemistryTransport proteinDNA-Binding ProteinsProtein TransportBiochemistryCytoplasmMultiprotein ComplexesBiophysicsbiology.proteinlcsh:QProtein KinasesResearch ArticleDevelopmental BiologyTranscription FactorsPLoS ONE
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Alternative splicing regulation by Muscleblind proteins: from development to disease.

2011

Regulated use of exons in pre-mRNAs, a process known as alternative splicing, strongly contributes to proteome diversity. Alternative splicing is finely regulated by factors that bind specific sequences within the precursor mRNAs. Members of the Muscleblind (Mbl) family of splicing factors control critical exon use changes during the development of specific tissues, particularly heart and skeletal muscle. Muscleblind homologs are only found in metazoans from Nematoda to mammals. Splicing targets and recognition mechanisms are also conserved through evolution. In this recognition, Muscleblind CCCH-type zinc finger domains bind to intronic motifs in pre-mRNA targets in which the protein can e…

Zinc fingerGeneticsAlternative splicingExonic splicing enhancerRNA-Binding ProteinsRNA-binding proteinBiologyGeneral Biochemistry Genetics and Molecular BiologyCell biologyExonchemistry.chemical_compoundAlternative SplicingchemistryGene Expression RegulationMultigene FamilyProteomeRNA splicingMBNL1AnimalsHumansMyotonic DystrophyRNAGeneral Agricultural and Biological SciencesProtein BindingBiological reviews of the Cambridge Philosophical Society
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Rapid odorant release in mammalian odour binding proteins facilitates their temporal coupling to odorant signals.

2010

 ; We have measured the effect of rat odorant-binding protein 1 on the rates of ligand uptake and liquid-to-air transfer rates with a set of defined odorous compounds. Comparison of observed rate constants (k(obs)) with data simulated over a wide range of different kinetic and thermodynamic regimes shows that the data do not agree with the previously held view of a slow off-rate regime (k(off) <0.0004 s(-1)). We propose that a rapid koff would be a necessary requirement for such a system, since slow odorant-release rates would result in significant decorrelation between the olfactory world and odour perception. (c) 2010 Elsevier Ltd. All rights reserved.

[SDV.BIO]Life Sciences [q-bio]/BiotechnologyKineticsAnalytical chemistryOlfactionAcetatesCalorimetryIn Vitro Techniques[ SDV.BA ] Life Sciences [q-bio]/Animal biologyLigandsReceptors OdorantDNA-binding proteinMass Spectrometry03 medical and health sciences0302 clinical medicineReaction rate constantStructural BiologyODORANT-BINDING PROTEINSAnimals[INFO.INFO-BT]Computer Science [cs]/BiotechnologyMolecular Biology030304 developmental biology0303 health sciencesChemistryTemporal couplingLigand[SDV.BA]Life Sciences [q-bio]/Animal biology[ SDV.BIO ] Life Sciences [q-bio]/BiotechnologyRecombinant ProteinsRatsSmellKineticsOdorantsBiophysicsOLFACTIONThermodynamics[ INFO.INFO-BT ] Computer Science [cs]/Biotechnology030217 neurology & neurosurgerypsychological phenomena and processesSignal TransductionJournal of molecular biology
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Characterization of variations responsible for neurodevelopmental disorders in the PTBP1 and PTBP2 genes

2022

Heterogeneous nuclear ribonucleoproteins (hnRNPs) polypyrimidine tract-binding protein 1 and 2 (PTBP1 and PTBP2) are splicing regulators, shuttling between nucleus and cytoplasm thanks to the action of partially overlapping nuclear localization and export signals (NLS and NES respectively). These two paralog proteins share similar RNA binding properties although they exhibit different expression levels and kinetics, post-translational modifications and cofactor interactions across tissues and cell types, thus regulating RNA metabolism in a cell- specific manner. Despite their fundamental role as alternative splicing factors implicated in cell growth, neuronal cell differentiation, and immun…

[SDV] Life Sciences [q-bio]corps-Pneurodéveloppement.navette nucléocytoplasmiquepolypyrimidine tract binding proteins
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Terminal tendon cell differentiation requires the glide/gcm complex.

2004

International audience; Locomotion relies on stable attachment of muscle fibres to their target sites, a process that allows for muscle contraction to generate movement. Here, we show that glide/gcm and glide2/gcm2, the fly glial cell determinants, are expressed in a subpopulation of embryonic tendon cells and required for their terminal differentiation. By using loss-of-function approaches, we show that in the absence of both genes, muscle attachment to tendon cells is altered, even though the molecular cascade induced by stripe, the tendon cell determinant, is normal. Moreover, we show that glide/gcm activates a new tendon cell gene independently of stripe. Finally, we show that segment p…

[SDV]Life Sciences [q-bio]Cellglide/gcmBiologyMotor ActivityTendonsglide2/gcm203 medical and health sciencesTendon cellMuscle attachmentmedicineMuscle attachmentAnimalsDrosophila ProteinsRNA MessengerMolecular BiologyIn Situ Hybridization030304 developmental biology0303 health sciencesMuscles030302 biochemistry & molecular biologyNeuropeptidesTendon cell differentiationGene Expression Regulation DevelopmentalCell DifferentiationEpistasis GeneticAnatomyTendon cell differentiationEmbryonic stem cellCell biologyTendonDNA-Binding ProteinsMicroscopy ElectronDrosophila melanogasterSegment polarity genemedicine.anatomical_structureEpidermal CellsOrgan SpecificityTrans-ActivatorsDrosophilamedicine.symptomEpidermisLocomotionDevelopmental BiologyMuscle contractionProtein BindingSignal TransductionTranscription FactorsDevelopment (Cambridge, England)
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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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Heat shock factor 2 is a stress-responsive mediator of neuronal migration defects in models of fetal alcohol syndrome

2014

Fetal alcohol spectrum disorder (FASD) is a frequent cause of mental retardation. However, the molecular mechanisms underlying brain development defects induced by maternal alcohol consumption during pregnancy are unclear. We used normal and Hsf2-deficient mice and cell systems to uncover a pivotal role for heat shock factor 2 (HSF2) in radial neuronal migration defects in the cortex, a hallmark of fetal alcohol exposure. Upon fetal alcohol exposure, HSF2 is essential for the triggering of HSF1 activation, which is accompanied by distinctive post-translational modifications, and HSF2 steers the formation of atypical alcohol-specific HSF1–HSF2 heterocomplexes. This perturbs the in vivo bindi…

[SDV]Life Sciences [q-bio][SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/NeurobiologyMice0302 clinical medicineradial neuronal migrationHeat Shock Transcription FactorsHSF1[SDV.BDD]Life Sciences [q-bio]/Development BiologyResearch ArticlesHeat-Shock ProteinsComputingMilieux_MISCELLANEOUSRegulation of gene expressionCerebral CortexMice Knockout0303 health sciences[SDV.BDD.EO] Life Sciences [q-bio]/Development Biology/Embryology and OrganogenesisCell biologyheat shock factorsDNA-Binding Proteins[SDV.TOX] Life Sciences [q-bio]/Toxicologymedicine.anatomical_structureCerebral cortexFetal Alcohol Spectrum Disorders[SDV.TOX]Life Sciences [q-bio]/Toxicology[ SDV.NEU.NB ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/NeurobiologyMolecular MedicinetranscriptionProtein BindingDoublecortin ProteinFetal alcohol syndromeBiology03 medical and health sciencesMediatorStress PhysiologicalHeat shock protein[SDV.BDD] Life Sciences [q-bio]/Development BiologymedicineAnimals[ SDV.BDD ] Life Sciences [q-bio]/Development Biologymicrotubule‐associated proteinsTranscription factor030304 developmental biologymicrotubule-associated proteins[SDV.NEU.NB] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiologymedicine.diseaseHeat shock factorDisease Models Animal[SDV.BDD.EO]Life Sciences [q-bio]/Development Biology/Embryology and OrganogenesisGene Expression RegulationImmunologyfetal alcohol syndrome030217 neurology & neurosurgeryMalformations of Cortical Development Group IITranscription FactorsNeuroscience
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Okadaic Acid, an Apoptogenic Toxin for Symbiotic/Parasitic Annelids in the Demosponge Suberites domuncula

2006

ABSTRACT The role of okadaic acid (OA) in the defense system of the marine demosponge Suberites domuncula against symbiotic/parasitic annelids was examined. Bacteria within the mesohyl produced okadaic acid at concentrations between 32 ng/g and 58 ng/g of tissue (wet weight). By immunocytochemical methods and by use of antibodies against OA, we showed that the toxin was intracellularly stored in vesicles. Western blotting experiments demonstrated that OA also existed bound to a protein with a molecular weight of 35,000 which was tentatively identified as a galectin (by application of antigalectin antibodies). Annelids that are found in S. domuncula undergo apoptotic cell death. OA is one ca…

animal structuresAnnelidaMolecular Sequence DataApoptosismedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologychemistry.chemical_compoundOkadaic AcidInvertebrate MicrobiologymedicineAnimalsHumansMesohylAmino Acid SequenceSymbiosisGalectinAnnelidBacteriaEcologybiologyToxinOkadaic acidbiology.organism_classificationDNA-Binding ProteinsSuberites domunculachemistryBiochemistrySuberitesBacteriaTranscription FactorsFood ScienceBiotechnologySuberitesApplied and Environmental Microbiology
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