Search results for "binding"

showing 10 items of 3896 documents

Recent advances in understanding vertebrate odorant-binding proteins

2011

[SDV.AEN] Life Sciences [q-bio]/Food and Nutrition[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutritionodorant-binding protein[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionolfaction
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Towards computational biomimetic nose

2016

International audience

[SDV.AEN] Life Sciences [q-bio]/Food and Nutritionodorant-binding protein[SDV.AEN]Life Sciences [q-bio]/Food and NutritionComputingMilieux_MISCELLANEOUSolfaction
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Structure-function analysis of peroxisomal ATP-binding cassette transporters using chimeric dimers

2014

Background: Peroxisomal ABC transporters are predicted to function as homodimers in mammals. [br/] Results: ABCD1 interacts with ABCD2. Chimeric proteins mimicking full-length dimers represent novel tools for functional study. Artificial homodimers and heterodimers are functional. [br/] Conclusion: Interchangeability between ABCD1 and ABCD2 is confirmed, but PUFA transport depends on ABCD2. [br/] Significance: For the first time, heterodimers in mammals are proven to be functional.[br/] ABCD1 and ABCD2 are two closely related ATP-binding cassette half-transporters predicted to homodimerize and form peroxisomal importers for fatty acyl-CoAs. Available evidence has shown that ABCD1 and ABCD2 …

[SDV.BA] Life Sciences [q-bio]/Animal biologyprotéine chimereanimal diseasesATP-binding cassette transporterProximity ligation assayProtein Chimerabiochimie structurale[ SDV.BA ] Life Sciences [q-bio]/Animal biologyPolymerase Chain ReactionBiochemistryGreen fluorescent proteininteraction moléculaireMice[ CHIM.OTHE ] Chemical Sciences/Otherhomodimèrereproductive and urinary physiologyAnimal biologyhétérodimèrechemistry.chemical_classification[SDV.BA]Life Sciences [q-bio]/Animal biologymammifèreTransfectionPeroxisomeprotéine de fusionBiochemistry[CHIM.OTHE] Chemical Sciences/OtherDimerizationPlasmidsABC Transporter;Fatty Acid;Peroxisome;Protein Chimera;Protein-Protein Interactiontransporteur abcBiologyPeroxisomeCell LineProtein–protein interactionStructure-Activity RelationshipMembrane BiologyBiologie animaleparasitic diseasesAutre (Chimie)PeroxisomesAnimalsHumansMolecular BiologyDNA PrimersBase SequenceABCD2fungiABCD1Fatty acidCell BiologyFusion proteinRatsProtein-Protein InteractionABC TransporterchemistryATP-Binding Cassette TransportersOther[CHIM.OTHE]Chemical Sciences/OtherFatty Acid
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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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Flavour retention and release from protein solutions

2006

International audience; This paper briefly presents the main results obtained up to now on protein–flavour binding and release in relation with flavour perception. Among the food proteins, β-lactoglobulin is the most extensively studied for its binding properties, which involve both hydrophobic and hydrogen binding. Recent developments using molecular modelling and Quantitative Structure–Activity Relationship confirmed the existence of two different binding sites for flavour compounds on β-lactoglobulin. During the aroma release process in the mouth, not only free aroma compounds are released but also those reversibly bound by the protein, pointing out the fact that flavour perception is on…

[SDV.BIO]Life Sciences [q-bio]/BiotechnologyPROTEINSFlavourBioengineeringLactoglobulins01 natural sciencesApplied Microbiology and Biotechnology0404 agricultural biotechnologyComputational chemistryCyclohexenesHumansBinding siteAromaStrong bindingFlavorBinding SitesbiologyFLAVOUR RELEASETerpenesChemistry010401 analytical chemistryBinding propertiesfood and beveragesSerum Albumin Bovine04 agricultural and veterinary sciencesHydrogen-Ion ConcentrationMilk Proteinsbiology.organism_classification040401 food science0104 chemical sciences[SDV.BIO] Life Sciences [q-bio]/BiotechnologyFlavoring AgentsBiochemistryBenzaldehydesTasteFLAVOUR BINDINGSoybean ProteinsFood TechnologyLimoneneProtein BindingBiotechnology
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Analysis of E2F1 by clAP1

2017

The cellular inhibitor of Apoptosis 1 (cIAP1) behaves as an E3 ubiquitin ligase and has oncogenic properties. Previously, our team has shown that cIAP1 can regulate the E2F1 transcription factor activity. My research project has been focused on deepening our current knowledge on this interaction. Firstly, we characterized the E2F1-cIAP1 interaction, then we analyzed the regulation of E2F1 by cIAP1 and finally assessed the importance of the cIAP1-E2F1 interaction for the oncogenic properties of cIAP1. I have demonstrated a interaction of E2F1 with the hydrophobic pocket of the BIR3 domain of cIAP1. Moreover, I highlighted that the alpha 1 helix of the BIR3 domain is mandatory for the stabili…

[SDV.SA] Life Sciences [q-bio]/Agricultural sciences[SDV.MHEP] Life Sciences [q-bio]/Human health and pathologyCIAP1E2F1UbiquitinylationIAP-Binding-MotifIBM
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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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Copper binding capacity of root exudates of cultivated plants and associated weeds

2001

International audience; Cu binding to root exudates of two cultivated plants, wheat (Triticum aestivum) and rape (Brassica napus), and two weeds associated with wheat, dog daisy (Matricaria inodora) and cornflower (Centaurea cyanus), was studied in vitro under hydroponic and sterile conditions. Nutrient solutions were prepared with or without P. A MetPLATE microbiological test was used to assess the metal complexing capacity of root exudates. In the P-deficient solutions, no exudation was observed for any of the four plants; consequently, no Cu binding occurred. When P was present in the nutrient solutions, the plant exudates displayed differing abilities to complex Cu. No difference was de…

[SDV]Life Sciences [q-bio]BrassicaSoil Science010501 environmental sciencesRELATION PLANTE SOL01 natural sciencesMicrobiologyMetalNutrientCopper bindingBotanyMatricaria0105 earth and related environmental sciencesCultivated plant taxonomybiologyfood and beverages04 agricultural and veterinary sciencesbiology.organism_classificationvisual_art[SDE]Environmental Sciences040103 agronomy & agriculturevisual_art.visual_art_medium0401 agriculture forestry and fisheriesHeavy metal bindingCentaurea cyanusAgronomy and Crop Science
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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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Interactions in the network of Usher syndrome type 1 proteins

2004

International audience; Defects in myosin VIIa, harmonin (a PDZ domain protein), cadherin 23, protocadherin 15 and sans (a putative scaffolding protein), underlie five forms of Usher syndrome type I (USH1). Mouse mutants for all these proteins exhibit disorganization of their hair bundle, which is the mechanotransduction receptive structure of the inner ear sensory cells, the cochlear and vestibular hair cells. We have previously demonstrated that harmonin interacts with cadherin 23 and myosin VIIa. Here we address the extent of interactions between the five known USH1 proteins. We establish the previously suggested sans-harmonin interaction and find that sans also binds to myosin VIIa. We …

[SDV]Life Sciences [q-bio]Hearing Loss SensorineuralStereocilia (inner ear)PDZ domainCadherin Related ProteinsProtocadherinCell Cycle ProteinsNerve Tissue ProteinsCuticular plateMyosinsBiologyMiceTwo-Hybrid System TechniquesHair Cells AuditoryBone plateMyosinotorhinolaryngologic diseasesGeneticsAnimalsHumansProtein PrecursorsMolecular BiologyGenetics (clinical)GeneticsStereociliumDyneinsSyndromeGeneral MedicineCadherinsCell biologyCytoskeletal ProteinsMyosin VIIaMutationsense organsCarrier ProteinsRetinitis PigmentosaPCDH15HeLa CellsProtein BindingHuman Molecular Genetics
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