Search results for "Mesh"

showing 10 items of 885 documents

Freezing and storage at -20 °C provides adequate preservation of Toxoplasma gondii DNA for retrospective molecular analysis.

2014

Equipe EA MERS; International audience; Nucleic acid-based testing has become crucial for toxoplasmosis diagnosis. For retrospective (forensic or scientific) studies, optimal methods must be employed for DNA long-term storage. We compared Toxoplasma gondii detection before and after DNA storage using real-time PCR. No significant differences were found depending on duration or storage conditions at -20 °C or -80 °C.

Microbiology (medical)Time Factors[SDV]Life Sciences [q-bio]educationBiologyReal-Time Polymerase Chain ReactionSpecimen HandlingToxoplasma gondii DNAchemistry.chemical_compoundparasitic diseasesFreezingmedicineRetrospective Studiestoxoplasma gondiiDNA storageToxoplasma gondiiamniotic fluidGeneral MedicineDNA Protozoanmedicine.diseasebiology.organism_classificationVirologyToxoplasmosisDna storageMolecular analysisInfectious DiseasesReal-time polymerase chain reaction[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologychemistryMolecular Diagnostic Techniquescongenital toxoplasmosisNucleic acidMESH: DNA Protozoan/isolation&purification; Freezing; Molecular Diagnostic Technics/methods; Specimen Handling/methods; Toxoplasmosis/diagnosisreal-Time PCRToxoplasmaDNAToxoplasmosisDiagnostic microbiology and infectious disease
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Broadening the phenotypic spectrum and physiological insights related toEIF2S3variants

2021

Mental deficiency, epilepsy, hypogonadism, microcephaly and obesity (MEHMO) syndrome is a severe X-linked syndrome caused by pathogenic variants in EIF2S3. The gene encodes the γ subunit of the eukaryotic translation initiation factor-2, eIF2, essential for protein translation. A recurrent frameshift variant is described in severely affected patients while missense variants usually cause a moderate phenotype. We identified a novel missense variant (c.433A>G, p.(Met145Val)) in EIF2S3 in a mildly affected patient. Studies on zebrafish confirm the pathogenicity of this novel variant and three previously published missense variants. CRISPR/Cas9 knockout of eif2s3 in zebrafish embryos recapitula…

MicrocephalyFrameshift mutation03 medical and health sciencesGeneticsmedicineAnimalsHumansMissense mutationGenitaliaCRISPR/Cas9GeneZebrafishZebrafishGenetics (clinical)030304 developmental biologyGenetics0303 health scienceseIF2EIF2S3biology030305 genetics & heredityapoptosisbiology.organism_classificationmedicine.diseasePhenotypePhenotypeMutationMental Retardation X-LinkedEIF2S3MEHMO syndromeHuman Mutation
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Interactions in dual species biofilms between Listeria monocytogenes EGD-e and several strains of Staphylococcus aureus.

2008

International audience; Six environmental isolates of Staphylococcus aureus and one collection strain were investigated for their ability to form monospecies biofilms and dual species biofilms with Listeria monocytogenes EGD-e on stainless steel coupons. All isolates were able to grow as biofilms but their ability to form monospecies biofilms differed. The population of L. monocytogenes EGD-e in dual species biofilms was not affected by the presence of S. aureus isolates except for strain CIP 53.156. The effect of L. monocytogenes EGD-e on the population of S. aureus was strain dependent: S. aureus population either increased or decreased or was not affected in the presence of L. monocytoge…

MicrococcaceaeColony Count Microbial[ SDV.MP.BAC ] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriologymedicine.disease_causeMESH: Listeria monocytogenesBacterial AdhesionMESH: Staphylococcus aureus0303 health scienceseducation.field_of_studybiologyStrain (chemistry)MESH : Staphylococcus aureusGeneral MedicineMESH: Stainless SteelMESH : BiofilmsStaphylococcus aureusScanning Electron MicroscopyMESH: Equipment ContaminationMESH : Microscopy Electron ScanningStaphylococcus aureusMESH: Microscopy Electron ScanningMESH : Bacterial AdhesionMESH : Stainless SteelMESH : Colony Count MicrobialPopulationFood ContaminationMESH: BiofilmsMicrobiologyMicrobiology03 medical and health sciencesSpecies SpecificityListeria monocytogenesMESH: Food-Processing IndustrymedicineMESH : Species SpecificityFood microbiologyMESH: Species SpecificityFood-Processing IndustryMESH: Bacterial AdhesioneducationMESH: Food MicrobiologyMESH: Colony Count Microbial030304 developmental biology030306 microbiologyBiofilmMESH : Food MicrobiologyMESH: Food Contaminationbiology.organism_classificationStainless SteelListeria monocytogenes[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyMESH : Food ContaminationMESH : Equipment ContaminationBiofilmsFood MicrobiologyMicroscopy Electron ScanningEquipment ContaminationMESH : Food-Processing IndustryMESH : Listeria monocytogenesBacteriaFood Science
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Effects of a high-fat diet on energy metabolism and ROS production in rat liver.

2011

International audience; BACKGROUND & AIMS: A high-fat diet affects liver metabolism, leading to steatosis, a complex disorder related to insulin resistance and mitochondrial alterations. Steatosis is still poorly understood since diverse effects have been reported, depending on the different experimental models used. METHODS: We hereby report the effects of an 8 week high-fat diet on liver energy metabolism in a rat model, investigated in both isolated mitochondria and hepatocytes. RESULTS: Liver mass was unchanged but lipid content and composition were markedly affected. State-3 mitochondrial oxidative phosphorylation was inhibited, contrasting with unaffected cytochrome content. Oxidative…

Mitochondrial ROSMaleTranscription GeneticMESH : Reactive Oxygen SpeciesMitochondria LiverMESH : HepatocytesMitochondrionOxidative PhosphorylationMESH: Hepatocytes0302 clinical medicineMESH: Membrane Potential MitochondrialCitrate synthaseMESH: AnimalsBeta oxidationMESH : Electron Transport2. Zero hungerMembrane Potential Mitochondrial0303 health sciencesMESH : RatsAdenine nucleotide translocatorMESH: Energy MetabolismMESH: Reactive Oxygen SpeciesLipidsBiochemistryLiverMESH: Dietary FatsMitochondrial matrix030220 oncology & carcinogenesisBody CompositionMESH : Oxidative PhosphorylationATP–ADP translocaseMESH: Mitochondria LiverMESH: RatsMESH : Body CompositionMESH : MaleOxidative phosphorylationBiologyMESH : Rats WistarElectron Transport03 medical and health sciencesMESH: Oxidative Phosphorylation[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyRats WistarMESH: Electron Transport[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular Biology030304 developmental biologyHepatologyMESH: Transcription GeneticMESH : Transcription GeneticMESH : LiverMESH : LipidsMESH: Body CompositionMESH: Rats WistarMESH: LipidsDietary FatsMESH: MaleRatsMESH : Energy MetabolismMESH : Membrane Potential MitochondrialMESH : Mitochondria Liverbiology.proteinHepatocytesMESH : AnimalsEnergy MetabolismReactive Oxygen SpeciesMESH : Dietary FatsMESH: Liver
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Correction to ‘Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy’

2021

The current pandemic situation caused by the Betacoronavirus SARS-CoV-2 (SCoV2) highlights the need for coordinated research to combat COVID-19. A particularly important aspect is the development of medication. In addition to viral proteins, structured RNA elements represent a potent alternative as drug targets. The search for drugs that target RNA requires their high-resolution structural characterization. Using nuclear magnetic resonance (NMR) spectroscopy, a worldwide consortium of NMR researchers aims to characterize potential RNA drug targets of SCoV2. Here, we report the characterization of 15 conserved RNA elements located at the 5' end, the ribosomal frameshift segment and the 3'-un…

Models Molecular2019-20 coronavirus outbreakMagnetic Resonance SpectroscopyCoronavirus disease 2019 (COVID-19)AcademicSubjects/SCI00010Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Genome ViralBiology03 medical and health sciencesGeneticsHumans3' Untranslated RegionsPandemicsProtein secondary structure030304 developmental biology0303 health sciencesBase SequenceSARS-CoV-2030302 biochemistry & molecular biologyCOVID-19Frameshifting RibosomalRNANuclear magnetic resonance spectroscopyVirologyNucleic Acid ConformationRNA ViralCorrigendumNucleic Acids Research
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Recurrent Mutations in the Basic Domain of TWIST2 Cause Ablepharon Macrostomia and Barber-Say Syndromes

2015

Contains fulltext : 153827.pdf (Publisher’s version ) (Open Access) Ablepharon macrostomia syndrome (AMS) and Barber-Say syndrome (BSS) are rare congenital ectodermal dysplasias characterized by similar clinical features. To establish the genetic basis of AMS and BSS, we performed extensive clinical phenotyping, whole exome and candidate gene sequencing, and functional validations. We identified a recurrent de novo mutation in TWIST2 in seven independent AMS-affected families, as well as another recurrent de novo mutation affecting the same amino acid in ten independent BSS-affected families. Moreover, a genotype-phenotype correlation was observed, because the two syndromes differed based s…

Models MolecularCandidate geneHirsutismProtein ConformationHeLa Cellmedicine.disease_causeTranscriptomeTwist transcription factorModelsGenetics(clinical)ExomeEye AbnormalitiesNon-U.S. Gov'tExomeGenetics (clinical)ZebrafishGeneticsMutationMicroscopyMacrostomiaSetleis syndromeHypertelorismResearch Support Non-U.S. Gov'tHypertrichosiEyelid DiseaseGENÉTICAPhenotypeEyelid DiseasesAbnormalitiesMultipleSequence AnalysisHumanChromatin ImmunoprecipitationMolecular Sequence DataMutation MissenseHypertrichosisAbnormalities; Multiple; Amino Acid Sequence; Animals; Base Sequence; Chromatin Immunoprecipitation; Exome; Eye Abnormalities; Eyelid Diseases; HeLa Cells; Hirsutism; Humans; Hypertelorism; Hypertrichosis; Macrostomia; Microscopy; Electron; Molecular Sequence Data; Mutation; Missense; Protein Conformation; Repressor Proteins; Sequence Analysis; DNA; Skin Abnormalities; Twist Transcription Factor; Zebrafish; Models; Molecular; Phenotype; Genetics; Genetics (clinical)Other Research Radboud Institute for Molecular Life Sciences [Radboudumc 0]BiologyResearch SupportElectronArticleFrameshift mutationGeneticAblepharon macrostomia syndromeSkin AbnormalitieGeneticsmedicineJournal ArticleAnimalsHumansAbnormalities MultipleAmino Acid SequenceNeurodevelopmental disorders Donders Center for Medical Neuroscience [Radboudumc 7]Base SequenceAnimalTwist-Related Protein 1MolecularSequence Analysis DNADNARepressor Proteinmedicine.diseaseRepressor ProteinsTwist Transcription FactorEye AbnormalitieMicroscopy ElectronMutationSkin Abnormalitiessense organsMissenseNanomedicine Radboud Institute for Molecular Life Sciences [Radboudumc 19]HeLa CellsAmerican journal of human genetics
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A Structural Model of the Human α7 Nicotinic Receptor in an Open Conformation

2015

International audience; Nicotinic acetylcholine receptors (nAchRs) are ligand-gated ion channels that regulate chemical transmission at the neuromuscular junction. Structural information is available at low resolution from open and closed forms of an eukaryotic receptor, and at high resolution from other members of the same structural family, two prokaryotic orthologs and an eukary- otic GluCl channel. Structures of human channels however are still lacking. Homology modeling and Molecular Dynamics simulations are valuable tools to predict structures of unknown proteins, however, for the case of human nAchRs, they have been unsuccessful in providing a stable open structure so far. This is du…

Models MolecularHydrogen bondingalpha7 Nicotinic Acetylcholine ReceptorProtein ConformationMolecular Sequence DataMESH: Sequence Alignmentligand gated ion channles molecular dynamics simulation epibatidine waterlcsh:MedicineSequence alignmentMESH: Amino Acid SequenceMolecular Dynamics SimulationMESH: Models Molecular*Molecular dynamicsProtein structureSequence alignmentCationsHumansMESH: Molecular Dynamics SimulationHomology modelingAmino Acid SequenceNicotinic Receptorlcsh:ScienceBiochemical simulationsIon channelAcetylcholine receptorIonsMESH: Protein Conformation*MultidisciplinaryMESH: HumansMESH: Molecular Sequence DataChemistryMESH: Protein Multimerizationlcsh:RMESH: alpha7 Nicotinic Acetylcholine Receptor/chemistry*[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]Transmembrane proteinSimulation and modelingNicotinic agonistBiochemistryBiophysicsProtein structurelcsh:QProtein MultimerizationResearch ArticleStructural Model
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Structural determinants of resveratrol for cell proliferation inhibition potency: experimental and docking studies of new analogs.

2010

International audience; Resveratrol is the subject of intense research because of the abundance of this compound in the human diet and as one of the most valuable natural chemopreventive agents. Further advances require new resveratrol analogs be used to identify the structural determinants of resveratrol for the inhibition potency of cell proliferation by comparing experimental and docking studies. Therefore, we synthesized new trans/(E)- and cis/(Z)-resveratrol - analogs not reported to date - by modifying the hydroxylation pattern of resveratrol and a double bond geometry. We included them in a larger panel of 14 molecules, including (Z)-3,5,4'-trimethoxystilbene, the most powerful molec…

Models MolecularMESH : HydroxidesMESH : DNAMESH: Cell CycleMESH: TubulinResveratrolHydroxylationchemistry.chemical_compound0302 clinical medicineTubulinMESH: StilbenesDrug DiscoveryStilbenesHydroxidesMESH : Cell ProliferationDocking studiesMESH : Colchicine0303 health sciencesCell CycleMESH: DNAStereoisomerismGeneral MedicineMESH : TubulinMESH: Hydroxides3. Good healthColon cancerBiochemistryMESH : Stereoisomerism030220 oncology & carcinogenesisMESH: Models MolecularMESH: Cell Line TumorStereochemistryMESH : Models MolecularStereoisomerismMESH : Stilbenes03 medical and health sciencesCell Line TumorMESH: Cell ProliferationMESH : Cell Cycle[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyBinding site[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyTubulin polymerization030304 developmental biologyCell ProliferationPharmacologyCombretastatinBinding SitesMESH: HumansCell growthMESH : Cell Line TumorOrganic ChemistryMESH : HumansDNAMESH: StereoisomerismMESH: ColchicinechemistryPolymethoxy-stilbenesMESH: Binding SitesDocking (molecular)Cell cultureResveratrolResveratrol; Polymethoxy-stilbenes; Tubulin polymerization; Colon cancer; Docking studiesColchicineMESH : Binding Sites
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The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin

2012

International audience; The acknowledged success of the Monod-Wyman-Changeux (MWC) allosteric model stems from its efficacy in accounting for the functional behavior of many complex proteins starting with hemoglobin (the paradigmatic case) and extending to channels and receptors. The kinetic aspects of the allosteric model, however, have been often neglected, with the exception of hemoglobin and a few other proteins where conformational relaxations can be triggered by a short and intense laser pulse, and monitored by time-resolved optical spectroscopy. Only recently the application of time-resolved wide-angle X-ray scattering (TR-WAXS), a direct structurally sensitive technique, unveiled th…

Models MolecularProtein ConformationcooperativityMESH: Catalytic DomainCooperativity01 natural sciencesMESH: Recombinant ProteinsHemoglobinsProtein structureMESH: Protein ConformationCatalytic Domainprotein structural dynamicsMESH: Allosteric Site0303 health sciencesMultidisciplinaryallosterybiologyMESH: KineticsChemistryBiological SciencesRecombinant Proteins[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsMESH: HemoglobinsAllosteric SiteMESH: Models MolecularAdultMESH: MutationStereochemistryKineticsAllosteric regulation010402 general chemistry03 medical and health sciencesprotein conformational changesflash photolysisallostery; cooperativity; flash photolysis; hemoglobin; protein conformational changes; protein structural dynamics; time-resolved wide angle x ray scattering; time-resolved x-ray scatteringHumans030304 developmental biologytime-resolved X-ray scattering; protein conformational changes; cooperativity; flash photolysisMESH: Humanstime-resolved X-ray scatteringWild typeActive sitetime-resolved wide angle x ray scatteringMESH: AdulthemoglobinSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical sciencesprotein conformational changeKineticsAllosteric enzymeMutationbiology.proteinHemoglobin
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Detailed clinical, genetic and neuroimaging characterization of OFD VI syndrome.

2012

Oral-facial-digital syndrome type VI (OFD VI) is characterized by the association of malformations of the face, oral cavity and extremities, distinguished from the 12 other OFD syndromes by cerebellar and metacarpal abnormalities. Cerebellar malformations in OFD VI have been described as a molar tooth sign (MTS), thus, including OFD VI among the "Joubert syndrome related disorders" (JSRD). OFD VI diagnostic criteria have recently been suggested: MTS and one or more of the following: 1) tongue hamartoma(s) and/or additional frenula and/or upper lip notch; 2) mesoaxial polydactyly of hands or feet; 3) hypothalamic hamartoma. In order to further delineate this rare entity, we present the neuro…

Molar tooth signNeuroimagingJoubert syndromeFrameshift mutationHypothalamic hamartomaNeuroimagingGeneticsmedicineClinical geneticHumansChildMesoaxial polydactylyGenetics (clinical)Polydactylybusiness.industryBrainInfantProteinsGeneral MedicineAnatomyOrofaciodigital Syndromesmedicine.diseaseMagnetic Resonance Imagingstomatognathic diseasesChild PreschoolMutationFemalebusinessTomography X-Ray Computed
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