Search results for "Protein Binding"

showing 10 items of 870 documents

Quantitative proteomics reveals a dynamic association of proteins to detergent-resistant membranes upon elicitor signaling in tobacco.

2009

International audience; A large body of evidence from the past decade supports the existence, in membrane from animal and yeast cells, of functional microdomains playing important roles in protein sorting, signal transduction, or infection by pathogens. In plants, as previously observed for animal microdomains, detergent-resistant fractions, enriched in sphingolipids and sterols, were isolated from plasma membrane. A characterization of their proteic content revealed their enrichment in proteins involved in signaling and response to biotic and abiotic stress and cell trafficking suggesting that these domains were likely to be involved in such physiological processes. In the present study, w…

0106 biological sciencesProteomicsGTPase-activating proteinQuantitative proteomicsDetergentsPlasma protein bindingBiologymedicine.disease_causeProteomics01 natural sciencesBiochemistryMass SpectrometryAnalytical ChemistryCell membraneFungal Proteins03 medical and health sciencesProtein targetingTobaccomedicine[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular Biology030304 developmental biologyPlant Proteins0303 health sciencesFungal proteinStaining and LabelingResearchAlgal ProteinsCell MembraneCell biologymedicine.anatomical_structureBiochemistryLuminescent MeasurementsSignal transductionPeptidesReactive Oxygen Species010606 plant biology & botanyProtein BindingSignal TransductionMolecularcellular proteomics : MCP
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Prefoldins contribute to maintaining the levels of the spliceosome LSM2–8 complex through Hsp90 in Arabidopsis

2020

14 p.-7 fig.-2 tab.

0106 biological sciencesSpliceosomeAcademicSubjects/SCI00010RNA SplicingMutantArabidopsis01 natural sciencesChaperonin//purl.org/becyt/ford/1 [https]03 medical and health sciencesGene Expression Regulation PlantArabidopsisRNA and RNA-protein complexesGeneticsHSP90 Heat-Shock Proteins//purl.org/becyt/ford/1.6 [https]030304 developmental biologyprefoldins0303 health sciencesbiologyArabidopsis ProteinsRNA-Binding Proteinsbiology.organism_classificationHsp903. Good healthCell biologyProteostasisMultiprotein ComplexesMutationRNA splicingSpliceosomesbiology.proteinLSM2-8 complexspliceosomeSmall nuclear RNAMolecular ChaperonesProtein Binding010606 plant biology & botany
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In vivoanalysis of the lumenal binding protein (BiP) reveals multiple functions of its ATPase domain

2007

International audience; The endoplasmic reticulum (ER) chaperone binding protein (BiP) binds exposed hydrophobic regions of misfolded proteins. Cycles of ATP hydrolysis and nucleotide exchange on the ATPase domain were shown to regulate the function of the ligand-binding domain in vitro. Here we show that ATPase mutants of BiP with defective ATP-hydrolysis (T46G) or ATP-binding (G235D) caused permanent association with a model ligand, but also interfered with the production of secretory, but not cytosolic, proteins in vivo. Furthermore, the negative effect of BiP(T46G) on secretory protein synthesis was rescued by increased levels of wild-type BiP, whereas the G235D mutation was dominant. U…

0106 biological sciencesgenetic structuresRecombinant Fusion ProteinsATPaseBlotting WesternGreen Fluorescent ProteinsPlant ScienceBINDING PROTEINEndoplasmic ReticulumModels Biological01 natural sciencesChromatography Affinity[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciencesAdenosine TriphosphateTobaccoPROTEIN FOLDINGGeneticsImmunoprecipitationEndoplasmic Reticulum Chaperone BiPHSP70Heat-Shock Proteins030304 developmental biologyCHAPERONEAdenosine Triphosphatases0303 health sciencesbiologyHydrolysisProtoplastsEndoplasmic reticulumBinding proteinCell BiologyPlants Genetically ModifiedLigand (biochemistry)Secretory proteinBiochemistryChaperone (protein)MutationChaperone bindingbiology.proteinATPASEElectrophoresis Polyacrylamide GelProtein foldingMolecular ChaperonesProtein BindingSignal Transduction010606 plant biology & botanyThe Plant Journal
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2018

ABC (ATP binding cassette) transporters, ubiquitous in all kingdoms of life, carry out essential substrate transport reactions across cell membranes. Their transmembrane domains bind and translocate substrates and are connected to a pair of nucleotide binding domains, which bind and hydrolyze ATP to energize import or export of substrates. Over four decades of investigations into ABC transporters have revealed numerous details from atomic-level structural insights to their functional and physiological roles. Despite all these advances, a comprehensive understanding of the mechanistic principles of ABC transporter function remains elusive. The human multidrug resistance transporter ABCB1, al…

0301 basic medicine030102 biochemistry & molecular biologyIn silicoBiophysicsATP-binding cassette transporterCell BiologyPlasma protein bindingBiologyBiochemistry03 medical and health sciencesTransmembrane domain030104 developmental biologyProtein structureBiochemistryATP hydrolysisFunction (biology)ATP-binding domain of ABC transportersBiochimica et Biophysica Acta (BBA) - Biomembranes
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Prox1 Is Required for Oligodendrocyte Cell Identity in Adult Neural Stem Cells of the Subventricular Zone

2016

Abstract Adult neural stem cells with the ability to generate neurons and glia cells are active throughout life in both the dentate gyrus (DG) and the subventricular zone (SVZ). Differentiation of adult neural stem cells is induced by cell fate determinants like the transcription factor Prox1. Evidence has been provided for a function of Prox1 as an inducer of neuronal differentiation within the DG. We now show that within the SVZ Prox1 induces differentiation into oligodendrocytes. Moreover, we find that loss of Prox1 expression in vivo reduces cell migration into the corpus callosum, where the few Prox1 deficient SVZ-derived remaining cells fail to differentiate into oligodendrocytes. Thu…

0301 basic medicineAdult neurogenesisMice0302 clinical medicineNeural Stem CellsCell MovementLateral VentriclesPromoter Regions GeneticCells CulturedMOUSE-BRAINReceptors NotchOligodendrocytesNeurogenesisCell DifferentiationLINEAGEAnatomyOlfactory BulbNeural stem cellCell biologyNeuroepithelial cellAdult Stem CellsOligodendrogliaDIFFERENTIATIONEnhancer Elements Geneticmedicine.anatomical_structureGene Knockdown TechniquesMolecular MedicineSPINAL-CORDStem cellSUBCELLULAR-LOCALIZATIONProtein BindingAdult stem cellOLIG2NeurogenesisSubventricular zoneBiology03 medical and health sciencesNeurosphereProx1medicineAnimalsCell LineageOLFACTORY-BULBBody PatterningHomeodomain ProteinsTumor Suppressor ProteinsCell BiologyMAMMALIAN BRAINOligodendrocyte Transcription Factor 2030104 developmental biologyNeuropoiesisPROGENITOR CELLSGene Expression Regulationnervous system030217 neurology & neurosurgeryDevelopmental BiologyStem Cells
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Severe pre-eclampsia is associated with alterations in cytotrophoblasts of the smooth chorion.

2016

Pre-eclampsia (PE), which affects ∼8% of first pregnancies, is associated with faulty placentation. Extravillous cytotrophoblasts (CTBs) fail to differentiate properly, contributing to shallow uterine invasion and deficient spiral artery remodeling. We studied the effects of severe PE (sPE) on the smooth chorion portion of the fetal membranes. The results showed a significant expansion of the CTB layer. The cells displayed enhanced expression of stage-specific antigens that extravillous CTBs normally upregulate as they exit the placenta. Transcriptomics revealed the dysregulated expression of many genes (e.g. placental proteins, markers of oxidative stress). We confirmed an sPE-related incr…

0301 basic medicineAdultSpiral arteryTranscription GeneticPlacentaHuman DevelopmentCTBSExtraembryonic MembranesBiology210Andrology03 medical and health sciences0302 clinical medicineDownregulation and upregulationPre-EclampsiaPregnancyPlacentamedicineHumansPregnancy-Associated Plasma Protein-AMolecular BiologyCytotrophoblastPAPPA1Cell ProliferationFetus030219 obstetrics & reproductive medicineCytotrophoblastPlacentationGene Expression Regulation DevelopmentalPreterm birthChorionPlacentationTrophoblastsOxidative Stress030104 developmental biologymedicine.anatomical_structureImmunologyembryonic structuresKeratinsFemaleCytotrophoblastsTranscriptomeDevelopmental BiologyProtein BindingHumanDevelopment (Cambridge, England)
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Sodium functions as a negative allosteric modulator of the oxytocin receptor

2017

Abstract The oxytocin receptor, a class A G protein coupled receptor (GPCR), is essentially involved in the physiology of reproduction. Two parameters are crucially important to support high-affinity agonist binding of the receptor: Mg2+ and cholesterol, both acting as positive modulators. Using displacement assays with a high-affinity fluorescent antagonist (OTAN-A647), we now show that sodium functions as a negative allosteric modulator of the oxytocin receptor. In membranes from HEK293 cells stably expressing the oxytocin receptor, oxytocin binding occurred with about 15-fold lower affinity when sodium chloride was increased from 0 to 300 mM, whereas antagonist binding remained largely u…

0301 basic medicineAgonistAllosteric modulatormedicine.drug_classSodiumBiophysicschemistry.chemical_elementBreast NeoplasmsSodium ChlorideOxytocinBiochemistryPotassium Chloride03 medical and health sciencesAllosteric RegulationCell Line TumormedicineHumansAmino Acid SequenceReceptorFluorescent DyesG protein-coupled receptorDose-Response Relationship DrugSequence Homology Amino AcidChemistryCell MembraneCell BiologyOxytocin receptorRecombinant ProteinsCell biologyCholesterolHEK293 Cells030104 developmental biologyOxytocinReceptors OxytocinMutagenesis Site-DirectedCalciumFemaleSequence Alignmenthormones hormone substitutes and hormone antagonistsIntracellularProtein Bindingmedicine.drugBiochimica et Biophysica Acta (BBA) - Biomembranes
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Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles.

2018

Abstract Background Virtually all cell types have the capacity to secrete nanometer-sized extracellular vesicles, which have emerged in recent years as potent signal transducers and cell-cell communicators. The multifunctional protein Alix is a bona fide exosomal regulator and skeletal muscle cells can release Alix-positive nano-sized extracellular vesicles, offering a new paradigm for understanding how myofibers communicate within skeletal muscle and with other organs. S-palmitoylation is a reversible lipid post-translational modification, involved in different biological processes, such as the trafficking of membrane proteins, achievement of stable protein conformations, and stabilization…

0301 basic medicineAlix (also known as PDCD6IP)Protein ConformationLipoylationLipid BilayersBiophysicsSkeletal muscle cellsCell Cycle ProteinsExosomesBiochemistryExosomeTetraspanin 29Cell Line03 medical and health sciencesExtracellular VesiclesPalmitoylationTetraspaninExtracellularHumansLipid bilayerMuscle SkeletalMolecular BiologyCells CulturedEndosomal Sorting Complexes Required for TransportChemistryVesicleCalcium-Binding ProteinsCell MembraneExtracellular vesicleTetraspaninSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Cell biologyExosomeProtein Transport030104 developmental biologyS-palmitoylationMembrane proteinextracellular vesicles (EVs)Skeletal muscle cellProtein Processing Post-TranslationalProtein BindingSignal TransductionBiochimica et biophysica acta. General subjects
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Hsp60, amateur chaperone in amyloid-beta fibrillogenesis

2016

BACKGROUND: Molecular chaperones are a very special class of proteins that play essential roles in many cellular processes like folding, targeting and transport of proteins. Moreover, recent evidence indicates that chaperones can act as potentially strong suppressor agents in Alzheimer's disease (AD). Indeed, in vitro experiments demonstrate that several chaperones are able to significantly slow down or suppress aggregation of Aβ peptide and in vivo studies reveal that treatment with specific chaperones or their overexpression can ameliorate some distinct pathological signs characterizing AD. METHODS: Here we investigate using a biophysical approach (fluorescence, circular dichroism (CD), t…

0301 basic medicineAmyloidMolecular chaperonesAmyloid betaBiophysicsPlasma protein bindingInhibition mechanismsBiochemistryChaperoninChaperonin03 medical and health sciences0302 clinical medicinemedicineHumansInhibition mechanismMolecular BiologyAmyloid aggregationAmyloid beta-PeptidesbiologyNeurodegenerationP3 peptideFibrillogenesisChaperonin 60medicine.diseaseAlzheimer's disease treatmentCell biology030104 developmental biologyChaperone (protein)biology.proteinHSP60030217 neurology & neurosurgeryProtein BindingBiochimica et Biophysica Acta (BBA) - General Subjects
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The Role of Osteoprotegerin and Its Ligands in Vascular Function

2019

International audience; The superfamily of tumor necrosis factor (TNF) receptors includes osteoprotegerin (OPG) and its ligands, which are receptor activators of nuclear factor kappa-B ligand (RANKL) and TNF-related apoptosis-inducing ligand (TRAIL). The OPG/RANKL/RANK system plays an active role in pathological angiogenesis and inflammation as well as cell survival. It has been demonstrated that there is crosstalk between endothelial cells and osteoblasts during osteogenesis, thus establishing a connection between angiogenesis and osteogenesis. This OPG/RANKL/RANK/TRAIL system acts on specific cell surface receptors, which are then able to transmit their signals to other intracellular comp…

0301 basic medicineAngiogenesismedicine.medical_treatmentReview030204 cardiovascular system & hematologyLigandslcsh:ChemistryTNF-Related Apoptosis-Inducing Ligand0302 clinical medicineReceptorlcsh:QH301-705.5Cellular SenescenceSpectroscopyReceptor Activator of Nuclear Factor-kappa BbiologyChemistryvascular diseaseGeneral MedicineComputer Science ApplicationsProtein Transportmedicine.anatomical_structureCytokineRANKLTumor necrosis factor alphaDisease Susceptibilitymedicine.symptomProtein BindingSignal Transductionmusculoskeletal diseasesProteasome Endopeptidase ComplexEndotheliumendotheliumNeovascularization PhysiologicInflammationCatalysisInorganic ChemistryStructure-Activity Relationship03 medical and health sciencesOsteoprotegerin[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemmedicineAnimalsHumansPhysical and Theoretical ChemistryMolecular BiologyMyocardiumRANK LigandOrganic ChemistryEndothelial Cells030104 developmental biologylcsh:Biology (General)lcsh:QD1-999osteoprotegerinOPG/RANKL/RANKCancer researchbiology.proteinBlood VesselsBiomarkers
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