Search results for "RESONANCE"

showing 10 items of 6625 documents

Characterization of a Novel Conformational GII.4 Norovirus Epitope: Implications for Norovirus-Host Interactions

2016

ABSTRACT Human noroviruses (NoVs) are the main etiological agents of acute gastroenteritis worldwide. While NoVs are highly diverse (more than 30 genotypes have been detected in humans), during the last 40 years most outbreaks and epidemics have been caused by GII.4 genotype strains, raising questions about their persistence in the population. Among other potential explanations, immune evasion is considered to be a main driver of their success. In order to study antibody recognition and evasion in detail, we analyzed a conformational epitope recognized by a monoclonal antibody (3C3G3) by phage display, site-directed mutagenesis, and surface plasmon resonance. Our results show that the predi…

0301 basic medicinePhage displayGenotypemedicine.drug_classviruses030106 microbiologyImmunologyPopulationBiologyAntibodies Viralmedicine.disease_causeMonoclonal antibodyMicrobiologyEpitope03 medical and health sciencesAntigenVirologymedicineHumanseducationeducation.field_of_studyNorovirusAntibodies Monoclonalvirus diseasesSurface Plasmon ResonanceVirologyVirus-Cell Interactions030104 developmental biologyInsect ScienceHost-Pathogen InteractionsMutagenesis Site-Directedbiology.proteinNorovirusEpitopes B-LymphocyteAntibodyCell Surface Display TechniquesProtein BindingConformational epitope
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Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”

2018

Editors at Science requested our input on the above discussion (comment by Best et al . and response by Riback et al .) because both sets of authors use our data from Fuertes et al . (2017) to support their arguments. The topic of discussion pertains to the discrepant inferences drawn from SAXS versus FRET measurements regarding the dimensions of intrinsically disordered proteins (IDPs) in aqueous solvents. Using SAXS measurements on labeled and unlabeled proteins, we ruled out the labels used for FRET measurements as the cause of discrepant inferences between the two methods. Instead, we propose that FRET and SAXS provide complementary readouts because of a decoupling of size and shape fl…

0301 basic medicinePhysicsMultidisciplinarySmall-angle X-ray scatteringScattering010402 general chemistryIntrinsically disordered proteins01 natural sciences0104 chemical sciences03 medical and health sciences030104 developmental biologyFörster resonance energy transferStatistical physicsDecoupling (electronics)Science
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Bistacrine derivatives as new potent antimalarials

2016

Linking two tacrine molecules results in a tremendous increase of activity against Plasmodia in comparison to the monomer. This finding prompted the synthesis of a library of monomeric and dimeric tacrine derivatives in order to derive structure-activity relationships. The most active compounds towards chloroquine sensitive Plasmodium strain 3D7 and chloroquine resistant strain Dd2 show IC50 values in the nanomolar range of concentration, low cytotoxicity and target the cysteine protease falcipain-2, which is essential for parasite growth.

0301 basic medicinePlasmodiumSpectrometry Mass Electrospray IonizationStereochemistryProton Magnetic Resonance SpectroscopyClinical BiochemistryPharmaceutical Science01 natural sciencesBiochemistryAntimalarialsInhibitory Concentration 50Structure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundChloroquineResistant strainDrug DiscoverymedicineAnimalsStructure–activity relationshipCarbon-13 Magnetic Resonance SpectroscopyCytotoxicityMolecular BiologyStrain (chemistry)010405 organic chemistryOrganic ChemistryCysteine protease0104 chemical sciences030104 developmental biologyMonomerchemistryBiochemistryTacrineTacrineMolecular MedicineDimerizationmedicine.drugBioorganic & Medicinal Chemistry
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Diagnostic Targeted Resequencing in 349 Patients with Drug-Resistant Pediatric Epilepsies Identifies Causative Mutations in 30 Different Genes

2017

Targeted resequencing gene panels are used in the diagnostic setting to identify gene defects in epilepsy. We performed targeted resequencing using a 30-genes panel and a 95-genes panel in 349 patients with drug-resistant epilepsies beginning in the first years of life. We identified 71 pathogenic variants, 42 of which novel, in 30 genes, corresponding to 20.3% of the probands. In 66% of mutation positive patients seizures onset occurred before age 6 months. The 95-genes panel allowed a genetic diagnosis in 22 (6.3%) patients that would have otherwise been missed using the 30-gene panel. About 50% of mutations were identified in genes coding for sodium and potassium channel components. SCN2…

0301 basic medicineProbandMaleCDKL5Drug Resistancemedicine.disease_causeBioinformaticsEpilepsyAnticonvulsantSTXBP1Age of OnsetChildGenetics (clinical)AlleleMutationepilepsy; next-generation sequencing; gene panel; mutationPhenotypeMagnetic Resonance ImagingSettore MED/39 - Neuropsichiatria Infantile3. Good healthPhenotypeChild PreschoolAnticonvulsantsFemaleSequence AnalysisHumanAdolescentGenotypeGenetic Association StudieBiologyMECP203 medical and health sciencesGeneticgene panelGeneticsmedicineHumansGenetic Predisposition to DiseasePreschoolGeneAllelesGenetic Association StudiesGene Expression ProfilingInfant NewbornComputational BiologyInfantMolecular Sequence AnnotationDNASequence Analysis DNANewbornmedicine.disease030104 developmental biologyepilepsynext-generation sequencingmutation
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Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions.

2016

Lunasin is a 43 amino acid peptide with anti-cancer, antioxidant, anti-inflammatory and cholesterol-lowering properties. Although the mechanism of action of lunasin has been characterized to some extent, its exact three-dimensional structure as well as the function of the N-terminal sequence remains unknown. We established a novel method for the production of recombinant lunasin that allows efficient isotope labeling for NMR studies. Initial studies showed that lunasin can exist in a reduced or oxidized state with an intramolecular disulfide bond depending on solution conditions. The structure of both forms of the peptide at pH 3.5 and 6.5 was characterized by CD spectroscopy and multidimen…

0301 basic medicineProtein Conformation alpha-HelicalCircular dichroismPhysiologyBeta sheetPeptideIntrinsically disordered proteinsBiochemistryLunasinAntioxidantsHistones03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineEndocrinologyNeoplasmsAnticarcinogenic AgentsHumansAmino Acid SequenceDisulfidesProtein secondary structureNuclear Magnetic Resonance BiomolecularPlant Proteinschemistry.chemical_classificationChemistryAcetylationNuclear magnetic resonance spectroscopyIntrinsically Disordered Proteins030104 developmental biologyBiochemistry030220 oncology & carcinogenesisBiophysicsSoybean ProteinsPeptidesOxidation-ReductionFunction (biology)Peptides
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Direct Visualization of the Conformational Dynamics of Single Influenza Hemagglutinin Trimers

2018

Influenza hemagglutinin (HA) is the canonical type I viral envelope glycoprotein and provides a template for the membrane-fusion mechanisms of numerous viruses. The current model of HA-mediated membrane fusion describes a static "spring-loaded" fusion domain (HA2) at neutral pH. Acidic pH triggers a singular irreversible conformational rearrangement in HA2 that fuses viral and cellular membranes. Here, using single-molecule Förster resonance energy transfer (smFRET)-imaging, we directly visualized pH-triggered conformational changes of HA trimers on the viral surface. Our analyses reveal reversible exchange between the pre-fusion and two intermediate conformations of HA2. Acidification of p…

0301 basic medicineProtein ConformationHemagglutinin (influenza)Hemagglutinin Glycoproteins Influenza VirusBiologyArticleGeneral Biochemistry Genetics and Molecular BiologyReaction coordinate03 medical and health sciencesViral envelopeInfluenza HumanFluorescence Resonance Energy TransferHumansDynamic equilibriumFusionCell MembraneLipid bilayer fusionHydrogen-Ion ConcentrationVirus InternalizationSingle Molecule ImagingHEK293 CellsHemagglutinins030104 developmental biologyMembraneFörster resonance energy transferA549 CellsInfluenza A virusBiophysicsbiology.proteinProtein BindingCell
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The Crystal Structure of Gurmarin, a Sweet Taste–Suppressing Protein: Identification of the Amino Acid Residues Essential for Inhibition

2018

International audience; Gurmarin is a highly specific sweet-taste suppressing protein in rodents that is isolated from the Indian plant Gymnemasylvestre. Gurmarin consists of 35 amino acid residues containing three intramolecular disulfide bridges that form a cystine knot. Here, we report the crystal structure of gurmarin at a 1.45 Å resolution and compare it with previously reported NMR solution structures. The atomic structure at this resolution allowed us to identify a very flexible region consisting of hydrophobic residues. Some of these amino acid residues had been identified as a putative binding site for the rat sweet taste receptor in a previous study. By combining alanine-scanning …

0301 basic medicineProtein ConformationPhysiologyCrystal structureCrystallography X-Ray03 medical and health sciencesBehavioral NeuroscienceGPCRsweet tastetaste receptorPhysiology (medical)goût sucréAnimalsHumansG protein-coupled receptorAmino AcidsBinding siteReceptorNuclear Magnetic Resonance BiomolecularPlant ProteinsGurmarininhibiteur030102 biochemistry & molecular biologybiologyChemistryMutagenesisCystine knotGymnema sylvestreSweet tastebiology.organism_classificationRecombinant ProteinsSensory SystemsRats3. Good healthinhibitorHEK293 Cells030104 developmental biologyBiochemistryGymnema sylvestreknottin[SDV.AEN]Life Sciences [q-bio]/Food and NutritionHydrophobic and Hydrophilic InteractionsChemical Senses
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Zero-field nuclear magnetic resonance of chemically exchanging systems.

2019

Zero- to ultralow-field (ZULF) nuclear magnetic resonance (NMR) is an emerging tool for precision chemical analysis. In this work, we study dynamic processes and investigate the influence of chemical exchange on ZULF NMR J-spectra. We develop a computational approach that allows quantitative calculation of J-spectra in the presence of chemical exchange and apply it to study aqueous solutions of [15N]ammonium (15N\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$${\mathrm{H}}_4^ +$$\end{document}H4+) as a model syst…

0301 basic medicineReaction kinetics and dynamicsSciencePhysics::Medical PhysicsGeneral Physics and AstronomyModel system02 engineering and technologyGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesNuclear magnetic resonanceZero fieldHyperpolarization (physics)lcsh:ScienceDissolutionQuantitative Biology::Biomolecules3403 Macromolecular and Materials ChemistryMultidisciplinaryAqueous solution34 Chemical SciencesChemical exchangeQ500Diagnostic markersGeneral ChemistryNuclear magnetic resonance spectroscopy021001 nanoscience & nanotechnologyequipment and supplies030104 developmental biologylcsh:Qddc:5000210 nano-technologyhuman activitiesSolution-state NMR51 Physical Sciences
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Peripherin-2 differentially interacts with cone opsins in outer segments of cone photoreceptors

2016

Peripherin-2 is a glycomembrane protein exclusively expressed in the light-sensing compartments of rod and cone photoreceptors designated as outer segments (OS). Mutations in peripherin-2 are associated with degenerative retinal diseases either affecting rod or cone photoreceptors. While peripherin-2 has been extensively studied in rods, there is only little information on its supramolecular organization and function in cones. Recently, we have demonstrated that peripherin-2 interacts with the light detector rhodopsin in OS of rods. It remains unclear, however, if peripherin-2 also binds to cone opsins. Here, using a combination of co-immunoprecipitation analyses, transmission electron micr…

0301 basic medicineRhodopsinOpsingenetic structuresmacromolecular substances030105 genetics & heredityBiologymedicine.disease_causeRetinaMice03 medical and health scienceschemistry.chemical_compoundImmunolabelingMicroscopy Electron TransmissionAntigens NeoplasmFluorescence Resonance Energy TransferGeneticsmedicineAnimalsHumansPeripherin 2Molecular BiologyGenetics (clinical)MutationRetinal DegenerationRetinalGeneral MedicineCone Opsinseye diseases030104 developmental biologyFörster resonance energy transfernervous systemchemistryRhodopsinMutationRetinal Cone Photoreceptor CellsBiophysicsbiology.proteinsense organsProtein BindingVisual phototransductionHuman Molecular Genetics
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Secondary Progression in Multiple Sclerosis: Neuronal Exhaustion or Distinct Pathology?

2016

Prevention of progression in neurological diseases, particularly in multiple sclerosis (MS) but also in neurodegenerative diseases, remains a significant challenge. MS patients switch from a relapsing-remitting to a progressive disease course, but it is not understood why and how this conversion occurs and why some patients never experience disease progression. Do aging and accumulation of neuronal damage induce progression, or do cognitive symptoms and accelerated grey matter (GM) atrophy point to distinct processes affecting networks? This review weighs accepted dogma against real data on the secondary progressive phase of the disease, highlighting current challenges in this important fie…

0301 basic medicineSenescencePathologymedicine.medical_specialtyMultiple SclerosisDiseaseGrey matter03 medical and health sciences0302 clinical medicineAtrophymedicineHumansSecondary progressiveNeuronsbusiness.industryGeneral NeuroscienceMultiple sclerosisNeurodegenerationBrainmedicine.diseaseMagnetic Resonance Imaging030104 developmental biologymedicine.anatomical_structureDisease ProgressionbusinessNeuroscience030217 neurology & neurosurgeryProgressive diseaseTrends in Neurosciences
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