Search results for "binding"

showing 10 items of 3896 documents

On dynamics of parvoviral replication protein NS1

2010

fluorescent fusion proteinshelicasesATPasescanine parvovirusfluoresenssifuusioproteiinitphotobleachingATP bindinghelikaasitkoiran parvovirusATP-molekyylitprotein dynamicsfluorescent recoveryparvovirukset
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Pellets based on polyuronates: Relationship between gelation and release properties

2017

International audience; Three polyuronates: amidated low methoxyl pectin (ALMP), low methoxyl pectin (LMP) and polygalacturonic acid (PGA) were used to encapsulate rutin in pellets, and they were characterized by different techniques (macroscopic properties, Calcium and rutin release). The ability of the three polyuronates to bind calcium ions and the viscoelastic properties of gels were performed to relate the properties of the pellets to the gel structures. The pellets size, the water content, the water uptake, the release of calcium and rutin varied depending on the polyuronate used. The pellets size of ALMP were smaller than LMP and PGA with a lower water content, but this matrix was mo…

food.ingredientPectinPelletsDiffusionEgg-box modelPelletschemistry.chemical_element02 engineering and technologyCalcium010402 general chemistry01 natural scienceslaw.inventionchemistry.chemical_compoundRutinFormulation parametersfoodMagazinelawAmideOrganic chemistryRheological propertiesIn-vitro releaseCa2+-pectin gelsWater contentChemistry[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringIn vitro releaseRheological behaviorBinding021001 nanoscience & nanotechnologyDrug-delivery0104 chemical sciencesChemical engineeringLow-methoxyl pectinCalciumPolyuronatesBeads0210 nano-technologyGelslonotropic gelationFood Science
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Impact of

2018

Drosophila melanogaster has been for over a century the model of choice of several neurobiologists to decipher the formation and development of the nervous system as well as to mirror the pathophysiological conditions of many human neurodegenerative diseases. The rare disease Friedreich’s ataxia (FRDA) is not an exception. Since the isolation of the responsible gene more than two decades ago, the analysis of the fly orthologue has proven to be an excellent avenue to understand the development and progression of the disease, to unravel pivotal mechanisms underpinning the pathology and to identify genes and molecules that might well be either disease biomarkers or promising targets for therap…

frataxinDrug Evaluation PreclinicalFriedreich’s ataxiaReviewLipid Metabolismdrug screensDisease Models AnimalOxidative Stressendoplasmic reticulumDrosophila melanogasterPhenotypeironFriedreich AtaxiaIron-Binding Proteinsmetal homeostasisAnimalsHumansGenetic Predisposition to DiseaseGene Silencinggenetic screensInternational journal of molecular sciences
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Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome

2022

Funding Information: This work was supported by Academy of Finland grants 285461 (H.T.), 330678 (H.T., J.R.), 277194 (H.L.), and 290677 (S.M.). We acknowledge the European Synchrotron Radiation Facility (ESRF) for providing synchrotron access for crystal data collection. We thank Prof. Janne Ihalainen (University of Jyväskylä) for all the help in all aspects of the paper, Prof. Gerrit Groenhof (University of Jyväskylä) for support, and Prof. Nikolai V. Tkachenko (Tampere University) for help and facilities for time-resolved absorption spectroscopy. We also thank M.Sc. Alli Liukkonen (University of Jyväskylä) and Dr. Heikki Häkkänen (University of Jyväskylä) for the assistance in laboratory …

fytokromitphytochrome structureProtein ConformationPhytochrome structureSpectral responsesspektroskopiafotobiologiabakteeritBacterial ProteinsHistidinePhysical and Theoretical ChemistryBinding Sites221 Nanotechnologyspectral responsesWaterBiliverdin protonationsäteilyWater networkkidetiedewater networkTyrosine1182 Biochemistry cell and molecular biologyPhytochromeDeinococcusproteiinitvalokemiabiliverdin protonationvalo
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The closure of Pak1-dependent macropinosomes requires the phosphorylation of CtBP1/BARS

2007

Membrane fission is an essential process in membrane trafficking and other cellular functions. While many fissioning and trafficking steps are mediated by the large GTPase dynamin, some fission events are dynamin independent and involve C-terminal-binding protein-1/brefeldinA-ADP ribosylated substrate (CtBP1/BARS). To gain an insight into the molecular mechanisms of CtBP1/BARS in fission, we have studied the role of this protein in macropinocytosis, a dynamin-independent endocytic pathway that can be synchronously activated by growth factors. Here, we show that upon activation of the epidermal growth factor receptor, CtBP1/BARS is (a) translocated to the macropinocytic cup and its surroundi…

genetic structuresEndocytic cycleGTPaseBiologyTRANSCRIPTIONAL COREPRESSOREPIDERMAL GROWTH-FACTORArticleGeneral Biochemistry Genetics and Molecular BiologySYNAPTIC VESICLE ENDOCYTOSISMembrane fissionCell Line TumorMacropinocytic cupHumansPhosphorylationMacropinosomeMolecular BiologyDynaminEpidermal Growth FactorGeneral Immunology and MicrobiologyMEMBRANE FISSIONGeneral NeuroscienceActinsEnterovirus B HumanProtein Structure TertiaryTransport proteinCell biologyDNA-Binding ProteinsAlcohol OxidoreductasesProtein Transportp21-Activated KinasesPLASMA-MEMBRANEPinocytosisPhosphorylationCell Surface ExtensionsIntegrin alpha2beta1The EMBO Journal
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Light-dependent CK2-mediated phosphorylation of centrins regulates complex formation with visual G-protein.

2008

AbstractCentrins are Ca2+-binding EF-hand proteins. All four known centrin isoforms are expressed in the ciliary apparatus of photoreceptor cells. Cen1p and Cen2p bind to the visual G-protein transducin in a strictly Ca2+-dependent way, which is thought to regulate light driven movements of transducin between photoreceptor cell compartments. These relatively slow motile processes represent a novel paradigm in light adaptation of photoreceptor cells.Here we validated specific phosphorylation as a novel regulator of centrins in photoreceptors. Centrins were differentially phosphorylated during photoreceptor dark adaptation. Inhibitor treatments revealed protein kinase CK2 as the major protein…

genetic structuresLightG proteinVisionChromosomal Proteins Non-HistoneBlotting WesternDark AdaptationBiologySignal transductionMicrotubulesPhotoreceptor cellMass SpectrometryCa2+-binding proteinsSubstrate SpecificityRats Sprague-DawleyMiceHeterotrimeric G proteinmedicineAnimalsCiliaTransducinPhosphorylationProtein kinase ACasein Kinase IIFluorescent Antibody Technique IndirectMicroscopy ImmunoelectronMolecular BiologyCytoskeletonCiliumCalcium-Binding ProteinsCell BiologyCell biologyRatsMice Inbred C57BLmedicine.anatomical_structureCentrinPhosphorylationHeterotrimeric G-proteinCalciumCattleTransducinsense organsMolecular translocationPhotoreceptor Cells VertebrateProtein BindingBiochimica et biophysica acta
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Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors.

1999

The assembly of signalling molecules into macromolecular complexes (transducisomes) provides specificity, sensitivity and speed in intracellular signalling pathways. Rod photoreceptors in the eye contain an unusual set of glutamic-acid-rich proteins (GARPs) of unknown function. GARPs exist as two soluble forms, GARP1 and GARP2, and as a large cytoplasmic domain (GARP' part) of the beta-subunit of the cyclic GMP-gated channel. Here we identify GARPs as multivalent proteins that interact with the key players of cGMP signalling, phosphodiesterase and guanylate cyclase, and with a retina-specific ATP-binding cassette transporter (ABCR), through four, short, repetitive sequences. In electron mic…

genetic structuresPhosphodiesterase InhibitorsMolecular Sequence DataCyclic Nucleotide-Gated Cation ChannelsGlutamic AcidNerve Tissue ProteinsPlasma protein bindingBiologyIn Vitro TechniquesRetinal Rod Photoreceptor CellsAnimalsAmino Acid SequenceTransducinEye ProteinsPeptide sequenceCyclic GMPMultidisciplinaryPhosphoric Diester HydrolasesPhosphodiesteraseProteinsTransporterGlutamic acidRod Cell Outer SegmentRecombinant ProteinsCell biologyBiochemistryCytoplasmGuanylate CyclaseATP-Binding Cassette TransportersCattleTransducinSignal transductionProtein BindingSignal TransductionNature
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Cooperativity of Protein Binding to Vesicles

2011

Electrostatics role is studied in protein adsorption to phosphatidylcholine (PC) and PC/phosphatidylglycerol (PG) small unilamellar vesicles (SUVs). Protein interaction is monitored vs. PG content at low ionic strength. Adsorption of lysozyme, myoglobin and bovine serum albumin (BSA) isoelectric point (pI) is investigated in SUVs, along with changes in protein fluorescence emission spectra. Partition coefficients and cooperativity parameters are calculated. At pI, binding is maximum while at lower/higher pHs binding drops. In Gouy–Chapman model activity coefficient goes with square charge number, which deviations indicate asymmetric location of anionic lipid in the bilayer inner leaflet, in…

genetic structuresbiologyBilayerVesicleBinding proteinCooperativitychemistry.chemical_compoundIsoelectric pointMyoglobinchemistrybiology.proteinBiophysicsBovine serum albuminProtein adsorption
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AMPA Receptor Auxiliary Proteins of the CKAMP Family

2019

α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors are assembled of four core subunits and several additional interacting proteins. Cystine-knot AMPA receptor-modulating proteins (CKAMPs) constitute a family of four proteins that influence the trafficking, subcellular localization and function of AMPA receptors. The four CKAMP family members CKAMP39/shisa8, CKAMP44/shisa9, CKAMP52/shisa6 and CKAMP59/shisa7 differ in their expression profile and their modulatory influence on AMPA receptor function. In this review, I report about recent findings on the differential roles of CKAMP family members.

glutamate receptorhippocampusGene ExpressionReviewAMPA receptorBiologySynaptic TransmissionCatalysisCell Linelcsh:ChemistryInorganic ChemistryLong term plasticitylateral geniculate nucleusAnimalsHumansAmino Acid SequenceReceptors AMPAAMPA receptorPhysical and Theoretical Chemistrysynaptic functionReceptorlcsh:QH301-705.5Molecular BiologySpectroscopyNeuronal Plasticitymusculoskeletal neural and ocular physiologyOrganic ChemistryGlutamate receptorGeniculate BodiesGeneral MedicineSubcellular localizationlong-term plasticityComputer Science ApplicationsCell biologyProtein TransportSynaptic functionlcsh:Biology (General)lcsh:QD1-999nervous systemauxiliary subunitMultigene FamilySynapsesCarrier ProteinsIon Channel Gatingshort-term plasticityFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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The shell matrix of the freshwater mussel Unio pictorum (Paleoheterodonta, Unionoida). Involvement of acidic polysaccharides from glycoproteins in na…

2007

13 pages; International audience; Among molluscs, the shell biomineralization process is controlled by a set of extracellular macromolecular components secreted by the calcifying mantle. In spite of several studies, these components are mainly known in bivalves from only few members of pteriomorph groups. In the present case, we investigated the biochemical properties of the aragonitic shell of the freshwater bivalve Unio pictorum (Paleoheterodonta, Unionoida). Analysis of the amino acid composition reveals a high amount of glycine, aspartate and alanine in the acid-soluble extract, whereas the acid-insoluble one is rich in alanine and glycine. Monosaccharidic analysis indicates that the in…

glycoproteinMESH: Amino AcidsMESH : PolysaccharidesMESH: BivalviaMESH : Calcification PhysiologicFresh WaterBiochemistryMESH : Spectroscopy Fourier Transform InfraredMESH : BivalviaSpectroscopy Fourier Transform InfraredMollusc shellMESH : Fresh Watercalcium-binding proteinElectrophoresis Gel Two-DimensionalMESH: AnimalsAmino Acidsmollusc shell nacreGel electrophoresisAlanine0303 health sciencesbiologyMESH : Carbohydrates030302 biochemistry & molecular biologyMESH : Extracellular Matrixmatrix macromoleculesExtracellular MatrixBiochemistryMESH: Fresh WaterElectrophoresis Polyacrylamide GelMESH: CarbohydratesFreshwater bivalveCarbohydratesMESH: GlycoproteinsMESH: Extracellular MatrixMESH : Electrophoresis Polyacrylamide GelMESH: Spectroscopy Fourier Transform InfraredMESH: Calcification Physiologic03 medical and health sciencesCalcification PhysiologicPolysaccharidesExtracellularAnimals[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyGlycoproteins030304 developmental biologyMolecular massUnio pictorumMESH : Electrophoresis Gel Two-DimensionalCell Biology[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/Biomaterialsbiology.organism_classificationbiomineralizationMESH: Electrophoresis Gel Two-DimensionalMESH : GlycoproteinsBivalviaIsoelectric pointMESH: PolysaccharidesMESH : Amino AcidsMESH : AnimalsMESH: Electrophoresis Polyacrylamide Gel
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