Search results for "Protein A"

showing 10 items of 364 documents

Artificial Oral Processing of Extruded Pea Flour Snacks

2021

International audience; The structure of extruded pea flour can affect chewing performances. Our objective was to relate the bolus properties (fragmentation, moisture content and viscosity) of chewed extruded pea snacks to their structure. In order to have control over oral physiological parameters, we opted for an in vitro approach using a chewing simulator, the variables of which were the flow rate of artificial salivary fluid and chewing time. The structure of the extruded pea snacks was characterized by its density and protein solubility in dithioerythritol (DTE), which reflected the amount of protein aggregates cross-linked by disulphide bonds. The particle size distribution and median…

0106 biological sciencesProtein aggregatesSalivaDithioerythritol[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringViscosity.[SPI.MECA.MSMECA]Engineering Sciences [physics]/Mechanics [physics.med-ph]/Materials and structures in mechanics [physics.class-ph]01 natural sciencesIndustrial and Manufacturing Engineeringchemistry.chemical_compound0404 agricultural biotechnology010608 biotechnology[SDV.IDA]Life Sciences [q-bio]/Food engineeringRelative density[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringFood scienceComputingMilieux_MISCELLANEOUS2. Zero hungerShear thinningRheometryViscositydigestive oral and skin physiologyPlasticizationPlasticizerfood and beveragesStarch04 agricultural and veterinary sciences040401 food scienceChewingstomatognathic diseaseschemistryParticle-size distributionGravimetric analysisDisulphide bonds
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Phosphorylation of CENP-A on serine 7 does not control centromere function.

2019

CENP-A is the histone H3 variant necessary to specify the location of all eukaryotic centromeres via its CENP-A targeting domain and either one of its terminal regions. In humans, several post-translational modifications occur on CENP-A, but their role in centromere function remains controversial. One of these modifications of CENP-A, phosphorylation on serine 7, has been proposed to control centromere assembly and function. Here, using gene targeting at both endogenous CENP-A alleles and gene replacement in human cells, we demonstrate that a CENP-A variant that cannot be phosphorylated at serine 7 maintains correct CENP-C recruitment, faithful chromosome segregation and long-term cell viab…

0301 basic medicine1.1 Normal biological development and functioningScience[SDV]Life Sciences [q-bio]CentromereGeneral Physics and Astronomy02 engineering and technology[SDV.BC]Life Sciences [q-bio]/Cellular Biologymacromolecular substancesBiologyGeneral Biochemistry Genetics and Molecular BiologyArticleSerineChromosome segregation03 medical and health sciencesHistone H3Underpinning researchCentromereGeneticsHumansViability assayPhosphorylationlcsh:ScienceComputingMilieux_MISCELLANEOUSCancerGene EditingMultidisciplinaryQGene targetingGeneral Chemistry021001 nanoscience & nanotechnologyCell biologySettore BIO/18 - Genetica030104 developmental biologyChromosome segragationHela CellsPhosphorylationEpigeneticslcsh:QGeneric health relevance0210 nano-technologyFunction (biology)Centromere Protein AHumanHeLa CellsNature communications
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Synergistic activation of AMPK prevents from polyglutamine-inducedtoxicity inCaenorhabditis elegans

2020

11 páginas, 4 figuras. Supplementary material related to this article can be found, in the online version, at doi: https://doi.org/10.1016/j.phrs.2020.105105.

0301 basic medicineAMPKProtein subunitMutantEnzyme ActivatorsAMP-Activated Protein KinasesProtein Serine-Threonine KinasesProtein Aggregation PathologicalpolyQ toxicityArticleAnimals Genetically ModifiedProtein Aggregates03 medical and health sciences0302 clinical medicineRNA interferenceAutophagymedicineAnimalsAMPK Caenorhabditis elegans Metformin Salycilate Synergy polyQ toxicityCaenorhabditis elegans ProteinsCaenorhabditis elegansLoss functionCaenorhabditis elegansNeuronsPharmacologybiologyChemistrySalycilateAutophagyAMPKDrug Synergismbiology.organism_classificationSalicylatesMetforminCell biologyMetforminEnzyme ActivationSynergy030104 developmental biology030220 oncology & carcinogenesisMutationProteostasisPeptidesmedicine.drug
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Trifluoroethanol modulates α-synuclein amyloid-like aggregate formation, stability and dissolution

2016

The conversion of proteins into amyloid fibrils and other amyloid-like aggregates is closely connected to the onset of a series of age-related pathologies. Upon changes in environmental conditions, amyloid-like aggregates may also undergo disassembly into oligomeric aggregates, the latter being recognized as key effectors in toxicity. This indicates new possible routes for in vivo accumulation of toxic species. In the light of the recognized implication of α-Synuclein (αSN) in Parkinson's disease, we present an experimental study on supramolecular assembly of αSN with a focus on stability and disassembly paths of such supramolecular aggregate species. Using spectroscopic techniques, two-pho…

0301 basic medicineAmyloidAmyloidBiophysicsSupramolecular chemistryProtein aggregationBiochemistrySupramolecular assembly03 medical and health scienceschemistry.chemical_compoundProtein AggregatesHumansDissolutionAlpha-synucleinProtein Stabilityproteins amyloid fibrils amyloid-like aggregates oligomeric aggregatesSpectrum AnalysisOrganic ChemistryAggregate (data warehouse)TemperatureTrifluoroethanolAmyloid fibrilCrystallography030104 developmental biologychemistryBiophysicsalpha-Synuclein
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Crosstalk between angiotensin and the nonamyloidogenic pathway of Alzheimer's amyloid precursor protein.

2017

The association between hypertension and an increased risk for Alzheimer's disease (AD) and dementia is well established. Many data suggest that modulation of the renin-angiotensin system may be meaningful for the prevention and therapy of neurodegenerative disorders, in particular AD. Proteolytic cleavage of the amyloid precursor protein (APP) by α-secretase precludes formation of neurotoxic Aβ peptides and is expected to counteract the development of AD. An established approach for the up-regulation of α-secretase cleavage is the activation of G protein-coupled receptors (GPCRs). Therefore, our study aimed to analyze whether stimulation of angiotensin AT1 or AT2 receptors stably expressed…

0301 basic medicineAngiotensin receptorAngiotensinsBiochemistryReceptor Angiotensin Type 2Receptor Angiotensin Type 103 medical and health sciencesAmyloid beta-Protein PrecursorAlzheimer DiseaseCyclohexanesGTP-Binding Protein gamma SubunitsAmyloid precursor proteinHumansMolecular Biologybeta-ArrestinsG protein-coupled receptorAngiotensin II receptor type 1biologyChemistryGTP-Binding Protein beta SubunitsP3 peptideCell BiologyAmyloidosisAngiotensin IIGTP-Binding Protein alpha SubunitsBiochemistry of Alzheimer's diseaseCell biology030104 developmental biologyHEK293 CellsPyrazinesProteolysisbiology.proteinAmyloid Precursor Protein SecretasesAmyloid precursor protein secretaseThe FEBS journal
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Improved display of synthetic IgG-binding domains on the baculovirus surface.

2004

Improved display of foreign protein moieties in combination with beneficial alteration of the viral surface properties should be of value for targeted and enhanced gene delivery. Here, we describe a vector based on Autographa californica multiple nucleopolyhedrovirus (AcMNPV) displaying synthetic IgG-binding domains (ZZ) of protein A fused to the transmembrane anchor of vesicular stomatitis virus (VSV) G protein. This display vector was equipped with a GFP/EGFP expression cassette enabling fluorescent detection in both insect and mammalian cells. The virus construct displayed the biologically active fusion protein efficiently and showed increased binding capacity to IgG. As the display is …

0301 basic medicineCancer ResearchvirusesRecombinant Fusion Proteins030106 microbiologyGenetic VectorsGene deliveryBiologySpodopteraVesicular stomatitis Indiana virusViral vectorCell Line03 medical and health sciencesViral Envelope ProteinsViral entryCricetinaeAnimalsMembrane GlycoproteinsImmune SerafungiGenetic Therapybiology.organism_classificationMolecular biologyFusion proteinNucleopolyhedroviruses030104 developmental biologyOncologyIgG bindingVesicular stomatitis virusImmunoglobulin Gbiology.proteinExpression cassetteBinding Sites AntibodyRabbitsProtein ABaculoviridaeTechnology in cancer researchtreatment
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Toxic Tau Oligomers Modulated by Novel Curcumin Derivatives

2019

AbstractThe pathological aggregation and accumulation of tau, a microtubule-associated protein, is a common feature amongst more than 18 different neurodegenerative diseases that are collectively known as tauopathies. Recently, it has been demonstrated that the soluble and hydrophobic tau oligomers are highly toxic in vitro due to their capacity towards seeding tau misfolding, thereby propagating the tau pathology seen across different neurodegenerative diseases. Modulating the aggregation state of tau oligomers through the use of small molecules could be a useful therapeutic strategy to target their toxicity, regardless of other factors involved in their formation. In this study, we screen…

0301 basic medicineCell biologyCurcuminCell SurvivalNeurotoxinsChemical biologyBiophysicsDrug Evaluation Preclinicallcsh:Medicinetau ProteinsProtein aggregationOligomerBiochemistryArticleBiophysical Phenomena03 medical and health scienceschemistry.chemical_compoundMiceProtein Aggregates0302 clinical medicineCell Line Tumormental disordersAnimalsHumanslcsh:ScienceNeuronsMultidisciplinaryCell DeathDrug discoveryDrug discoverySettore BIO/16 - Anatomia Umanalcsh:RSettore CHIM/06 - Chimica OrganicaSmall moleculeChemical biologyIn vitro3. Good healthTau protein Curcumin030104 developmental biologychemistryCell cultureBiophysicsCurcuminAlzheimerlcsh:QProtein Multimerization030217 neurology & neurosurgeryNeuroscience
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CENP-A Is Dispensable for Mitotic Centromere Function after Initial Centromere/Kinetochore Assembly

2016

SummaryHuman centromeres are defined by chromatin containing the histone H3 variant CENP-A assembled onto repetitive alphoid DNA sequences. By inducing rapid, complete degradation of endogenous CENP-A, we now demonstrate that once the first steps of centromere assembly have been completed in G1/S, continued CENP-A binding is not required for maintaining kinetochore attachment to centromeres or for centromere function in the next mitosis. Degradation of CENP-A prior to kinetochore assembly is found to block deposition of CENP-C and CENP-N, but not CENP-T, thereby producing defective kinetochores and failure of chromosome segregation. Without the continuing presence of CENP-A, CENP-B binding …

0301 basic medicineChromosomal Proteins Non-HistoneMedical PhysiologyEpigenesis GeneticChromosome segregationModelsChromosome SegregationKinetochoresGeneticsTumormitosiKinetochorekinetochoreCell biologyChromatinChromosomal Proteinsprotein degradationCENP-ACENP-BepigeneticCENP-C1.1 Normal biological development and functioningKinetochore assemblyCentromerechromosome segregationMitosismacromolecular substancesBiologyProtein degradationModels BiologicalGeneral Biochemistry Genetics and Molecular BiologyArticleCell Line03 medical and health sciencesGeneticUnderpinning researchCentromere Protein ACell Line TumorCentromereGeneticsHumansMitosisNon-HistoneBiologicalSettore BIO/18 - Genetica030104 developmental biologyGeneric health relevanceBiochemistry and Cell BiologyauxinCentromere Protein AEpigenesisCell Reports
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Loss of ISWI Function in Drosophila Nuclear Bodies Drives Cytoplasmic Redistribution of Drosophila TDP-43

2018

Over the past decade, evidence has identified a link between protein aggregation, RNA biology, and a subset of degenerative diseases. An important feature of these disorders is the cytoplasmic or nuclear aggregation of RNA-binding proteins (RBPs). Redistribution of RBPs, such as the human TAR DNA-binding 43 protein (TDP-43) from the nucleus to cytoplasmic inclusions is a pathological feature of several diseases. Indeed, sporadic and familial forms of amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration share as hallmarks ubiquitin-positive inclusions. Recently, the wide spectrum of neurodegenerative diseases characterized by RBPs functions’ alteration and loss was coll…

0301 basic medicineCytoplasmCytoplasmic inclusionFluorescent Antibody TechniqueProtein aggregationHeterogeneous ribonucleoprotein particleHeterogeneous-Nuclear Ribonucleoproteinslcsh:Chemistry0302 clinical medicineDrosophila Proteinsneurodegenerative diseasesnuclear bodylcsh:QH301-705.5SpectroscopyGeneral MedicinehnRNPsComputer Science ApplicationsCell biologyChromatinTransport proteinDNA-Binding ProteinsProtein Transportmedicine.anatomical_structureDrosophilaDrosophila ProteinProtein BindingImitation SWIBiologyCatalysisArticleInorganic Chemistryomega speckles03 medical and health sciencesmedicineAnimalsPhysical and Theoretical ChemistryMolecular BiologyGenetic Association StudiesCell NucleusOrganic Chemistryta1182Chromatin Assembly and DisassemblyCell nucleus030104 developmental biologylcsh:Biology (General)lcsh:QD1-999gene expression<i>Drosophila</i>; nuclear body; omega speckles; dTDP-43; hnRNPs; omega speckles; neurodegenerative diseases; gene expression; gene regulationdTDP-43gene regulation030217 neurology & neurosurgeryInternational Journal of Molecular Sciences
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Direct observation of alpha-lactalbumin, adsorption and incorporation into lipid membrane and formation of lipid/protein hybrid structures

2019

The interaction between proteins and membranes is of great interest in biomedical and biotechnological research for its implication in many functional and dysfunctional processes. We present an experimental study on the interaction between model membranes and alpha-lactalbumin (alpha-La). alpha-La is widely studied for both its biological function and its anti-tumoral properties. We use advanced fluorescence microscopy and spectroscopy techniques to characterize alpha-La-membrane mechanisms of interaction and alpha-La-induced modifications of membranes when insertion of partially disordered regions of protein chains in the lipid bilayer is favored. Moreover, using fluorescence lifetime imag…

0301 basic medicineFluorescence-lifetime imaging microscopyProtein ConformationLipid BilayersBiophysics02 engineering and technologyBiochemistryMembrane Lipids03 medical and health sciencesProtein structureMembrane fluidityFluorescence microscopeAnimalsHumansLipid bilayerMolecular BiologyFluorescent DyesChemistryMembrane structure021001 nanoscience & nanotechnologyLipids2-PHOTON FLUORESCENCE MICROSCOPY; MOLTEN GLOBULE STATE; PARTIALLY FOLDED CONFORMATIONS; PROTEIN INTERACTIONS; CIRCULAR-DICHROISM; AMPHITROPIC PROTEINS; AMYLOID AGGREGATION; PHASOR APPROACH; OLEIC-ACID; LAURDANSpectrometry Fluorescence030104 developmental biologyMembranefluorescence FLIM Protein membrane interaction IDPLactalbuminBiophysicsCattleAdsorption0210 nano-technologyProtein adsorptionBiochimica et Biophysica Acta (BBA) - General Subjects
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