Search results for "recombinant"

showing 10 items of 1150 documents

Genetic identification of neurons controlling a sexually dimorphic behaviour

2000

0960-9822 (Print) Journal Article Research Support, Non-U.S. Gov't; In the fruit fly Drosophila melanogaster, locomotor activity is sexually dimorphic: female flies constantly modulate their activity pattern whereas males show a steadier, stereotyped walking pace [1]. Here, we mapped the area of the brain controlling this behavioural dimorphism. Adult male Drosophila expressing a dominant feminising transgene in a small cluster of neurons in the pars intercerebralis exhibited a female-like pattern of locomotor activity. Genetic ablation of these neurons prevented the feminisation of the locomotor activity of transgenic males. The results suggest that this cluster of neurons modulates sex-sp…

MaleMESH: NeuronsCourtshipAnimals Genetically ModifiedSexual Behavior Animal0302 clinical medicineMESH: Saccharomyces cerevisiae ProteinsDrosophila ProteinsNervous System Physiological PhenomenaMESH: AnimalsMESH: Sexual Behavior AnimalDrosophila melanogaster/*physiologymedia_commonNeurons0303 health sciencesFungal proteinSex CharacteristicsbiologyAgricultural and Biological Sciences(all)Nuclear ProteinsAnatomyMESH: Transcription FactorsMotor Activity/*physiologyMESH: Motor ActivityDNA-Binding ProteinsFungal Proteins/geneticsNuclear Proteins/*genetics/physiologyDrosophila melanogasterMESH: Fungal Proteins[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]FemaleDrosophila melanogasterGeneral Agricultural and Biological SciencesLocomotionSex characteristicsMESH: Sex CharacteristicsNervous System PhysiologySaccharomyces cerevisiae ProteinsTransgenemedia_common.quotation_subjectRecombinant Fusion ProteinsRecombinant Fusion Proteins/biosynthesisSexual BehaviorMESH: LocomotionTranscription Factors/geneticsGenetically ModifiedMotor ActivityGeneral Biochemistry Genetics and Molecular BiologyMESH: Drosophila melanogasterFungal ProteinsMESH: Animals Genetically Modified03 medical and health sciencesMESH: Recombinant Fusion ProteinsAnimalsDrosophila030304 developmental biologyBiochemistry Genetics and Molecular Biology(all)Animalfungibiology.organism_classificationMESH: MaleSexual dimorphismMale courtship behaviourMESH: Nervous System PhysiologyNeuroscienceMESH: FemaleMESH: Nuclear ProteinsNeurons/*physiology030217 neurology & neurosurgeryTranscription Factors
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Putative role of nitric oxide synthase isoforms in the changes of nitric oxide concentration in rat brain cortex and cerebellum following sevoflurane…

2005

We have previously observed an increase in nitric oxide (NO) content in rat brain cortex following halothane, sevoflurane or isoflurane anaesthesia. This study was undertaken in order to determine whether isoform-specific nitric oxide synthase (NOS) inhibitors and inducers could modify these increases in NO contents. Rats were subjected to isoflurane and sevoflurane anaesthesia with concomitant administration of neuronal nitric oxide synthase (nNOS) inhibitor 7-Nitro-indazole (7-NI), inducible nitric oxide synthase (iNOS) inhibitor 2-amino-5,6-dihydro-6-methyl-4H-1,3-thiazine (AMT) or lipopolysaccharide. NO concentration in different organs was measured by electron paramagnetic resonance (E…

MaleMethyl Ethersmedicine.medical_specialtyCentral nervous systemNitric Oxide Synthase Type IINerve Tissue ProteinsNitric Oxide Synthase Type INitric OxideSevofluraneNitric oxidechemistry.chemical_compoundSevofluraneInternal medicineCortex (anatomy)CerebellummedicineAnimalsRats WistarPharmacologyCerebral CortexbiologyIsofluraneRecombinant ProteinsRatsNitric oxide synthaseIsoenzymesmedicine.anatomical_structureEndocrinologyIsofluranechemistryBiochemistryCerebral cortexAnesthetics Inhalationbiology.proteinHalothaneNitric Oxide Synthasemedicine.drugEuropean journal of pharmacology
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Prevention of the post-chemotherapy relapse of tuberculous infection by combined immunotherapy

2008

Summary We report that a recently developed combined immunotherapy (CIT) has the capacity to prevent a spontaneous relapse of replicating Mycobacterium tuberculosis bacilli in the lungs of BALB/c, C57Bl/6 or C3H/HeJ strains of mice, following 4 weeks of non-sterilising treatment with isoniazid and rifampicin. The CIT regimen, represented by recombinant IFNγ, anti-α crystalline monoclonal IgA antibody and IL-4 neutralizing polyclonal antibody, reduced the 8-week relapse of viable bacterial counts in the lungs most significantly, when CIT was inoculated during the 5th week post infection, i.e. during the 3rd week of chemotherapy. Although CIT enhanced lung granuloma area, nitric oxide, cytoki…

MaleMicrobiology (medical)TuberculosisTuberculosiAntibodiemedicine.medical_treatmentImmunologyAntitubercular AgentsColony Count MicrobialMicrobiologyAntibodiesMycobacterium tuberculosisInterferon-gammaMiceAdjuvants ImmunologicRecurrencemedicineAnimalsalpha-CrystallinsRelapseTuberculosis PulmonaryCytokineMice Inbred BALB CMice Inbred C3HChemotherapyLungbiologybusiness.industryTuberculosis; Cytokines; Antibodies; Immunotherapy; RelapseIsoniazidMycobacterium tuberculosisImmunotherapybiology.organism_classificationmedicine.diseaseCombined Modality TherapyRecombinant ProteinsImmunoglobulin AMice Inbred C57BLRegimenInfectious Diseasesmedicine.anatomical_structureModels AnimalImmunologyInterleukin-4ImmunotherapybusinessRifampicinmedicine.drugTuberculosis
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TBC1D24-TLDc-related epilepsy exercise-induced dystonia: rescue by antioxidants in a disease model

2019

Genetic mutations in TBC1D24 have been associated with multiple phenotypes, with epilepsy being the main clinical manifestation. The TBC1D24 protein consists of the unique association of a Tre2/Bub2/Cdc16 (TBC) domain and a TBC/lysin motif domain/catalytic (TLDc) domain. More than 50 missense and loss-of-function mutations have been described and are spread over the entire protein. Through whole genome/exome sequencing we identified compound heterozygous mutations, R360H and G501R, within the TLDc domain, in an index family with a Rolandic epilepsy exercise-induced dystonia phenotype (http://omim.org/entry/608105). A 20-year long clinical follow-up revealed that epilepsy was self-limited in…

MaleModels Molecular0301 basic medicineProtein ConformationAmino Acid Motifsalpha-TocopherolMutantCrystallography X-RayPHENOTYPECompound heterozygosityAntioxidantsAnimals Genetically ModifiedEpilepsy0302 clinical medicineCatalytic DomainDrosophila ProteinsMissense mutationoxidative stressChildTLDC DOMAINVITAMIN-EExome sequencingSequence DeletionNeuronsDystoniaGeneticsexercise-induced dystoniaTBC1D24GTPase-Activating ProteinsANNOTATIONSEpilepsy RolandicPhenotypeRecombinant ProteinsPedigree3. Good healthRolandic epilepsyDystoniaDrosophila melanogasterChild PreschoolFemaleSettore MED/26 - NeurologiaSynaptic VesiclesDrosophila melanogasterPROTEIN STABILITYLife Sciences & BiomedicineLocomotionAdolescentPhysical ExertionMutation MissenseClinical NeurologyPREDICTIONSBiology03 medical and health sciencesmedicineAnimalsHumansAmino Acid SequenceCOMPARTMENToxidative streScience & TechnologySequence Homology Amino AcidMUTATIONSNeurosciencesInfantBiological TransportDEGRADATIONmedicine.diseasebiology.organism_classificationAcetylcysteineDisease Models AnimalOxidative Stress030104 developmental biologyrab GTP-Binding ProteinsSEIZURESNeurosciences & NeurologyNeurology (clinical)Reactive Oxygen SpeciesSequence Alignment030217 neurology & neurosurgery
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Phenotypic and biochemical analysis of an international cohort of individuals with variants in NAA10 and NAA15.

2019

Abstract N-alpha-acetylation is one of the most common co-translational protein modifications in humans and is essential for normal cell function. NAA10 encodes for the enzyme NAA10, which is the catalytic subunit in the N-terminal acetyltransferase A (NatA) complex. The auxiliary and regulatory subunits of the NatA complex are NAA15 and Huntington-interacting protein (HYPK), respectively. Through a genotype-first approach with exome sequencing, we identified and phenotypically characterized 30 individuals from 30 unrelated families with 17 different de novo or inherited, dominantly acting missense variants in NAA10 or NAA15. Clinical features of affected individuals include variable levels…

MaleModels Molecular0301 basic medicineProtein ConformationMicrophthalmia0302 clinical medicineEnzyme StabilityMissense mutationN-Terminal Acetyltransferase EChildN-Terminal Acetyltransferase AExome sequencingGenetics (clinical)GeneticsbiologyGeneral MedicinePhenotypeRecombinant ProteinsChemistryPhenotypeChild PreschoolHMG-CoA reductaseCohortFemaleGeneral ArticleCorrigendumAdultNatA complexmedicine.medical_specialtyAdolescentGenotypeFrameshift mutationStructure-Activity RelationshipYoung Adult03 medical and health sciencesMolecular geneticsGeneticsmedicineHumansGenetic Predisposition to DiseaseGenetic TestingAlleleBiologyMolecular BiologyAllelesGenetic Association StudiesComputational BiologyFaciesGenetic VariationInfantmedicine.diseaseEnzyme ActivationLenz microphthalmia syndrome030104 developmental biologyGenetic LociMutationbiology.proteinHuman medicineBiomarkers030217 neurology & neurosurgeryNAA15Human molecular genetics
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The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase

2003

The mammalian soluble epoxide hydrolase (sEH) is an enzyme with multiple functions, being implicated in detoxification of xenobiotic epoxides as well as in regulation of physiological processes such as blood pressure. The enzyme is a homodimer, in which each subunit is composed of two domains. The 35-kDa C-terminal domain has an α/β hydrolase fold and harbors the catalytic center for the EH activity. The 25-kDa N-terminal domain has a different α/β fold and belongs to the haloacid dehalogenase superfamily of enzymes. The catalytic properties of the enzyme reported so far can all be explained by the action of the C-terminal domain alone. The function of the N-terminal domain, other than in …

MaleModels MolecularEpoxide hydrolase 2HydrolasesStereochemistryProtein subunitMolecular Sequence DataPhosphatase10050 Institute of Pharmacology and Toxicology610 Medicine & healthDephosphorylationHydrolaseAnimalsHumansAmino Acid SequenceDNA PrimersEpoxide Hydrolaseschemistry.chemical_classification1000 MultidisciplinaryMultidisciplinaryBase SequenceSequence Homology Amino AcidbiologyChemistryActive siteBiological SciencesPhosphoric Monoester HydrolasesRats Inbred F344Recombinant ProteinsRatsAmino acidEnzymeSolubilityBiochemistryMutagenesis Site-Directedbiology.protein570 Life sciences; biologyProceedings of the National Academy of Sciences
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The Major Conformational IgE-binding Epitopes of Hevein (Hev b6.02) Are Identified by a Novel Chimera-based Allergen Epitope Mapping Strategy

2002

A novel approach to localize and reconstruct conformational IgE-binding epitope regions of hevein (Hev b6.02), a major natural rubber latex allergen, is described. An antimicrobial protein (AMP) from the amaranth Amaranthus caudatus was used as an immunologically non-IgE-binding adaptor molecule to which terminal or central parts of hevein were fused. Hevein and AMP share a structurally identical core region but have different N-terminal and C-terminal regions. Only 1 of 16 hevein-allergic patients showed weak IgE binding to purified native or recombinant AMP. Chimeric AMP with the hevein N terminus was recognized by IgE from 14 (88%) patients, and chimeric AMP with the hevein C terminus wa…

MaleModels MolecularProtein ConformationImmunoglobulin Emedicine.disease_causeBiochemistryEpitopelaw.inventionEpitopes0302 clinical medicineAllergenlawLectinsPlant Proteins0303 health sciencesbiologyMiddle Aged3. Good healthDatabases as TopicBiochemistryRecombinant DNAFemalePlant LectinsProtein BindingAdultPeptide BiosynthesisAdolescentRecombinant Fusion ProteinsEnzyme-Linked Immunosorbent Assay03 medical and health sciencesChimera (genetics)medicineAnimalsHumansMolecular BiologyAged030304 developmental biologyDose-Response Relationship DrugC-terminusCell BiologyAllergensImmunoglobulin EMolecular biologyAdenosine MonophosphateProtein Structure TertiaryN-terminusEpitope mappingSpectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinChickensEpitope MappingAntimicrobial Cationic Peptides030215 immunologyJournal of Biological Chemistry
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Construction of hevein (Hev b 6.02) with reduced allergenicity for immunotherapy of latex allergy by comutation of six amino acid residues on the con…

2004

Abstract Recently we have established that IgE Abs bind to conformational epitopes in the N- and C-terminal regions of the major natural rubber latex allergen, hevein (Hev b 6.02). To identify the critical amino acid residues that interact with IgE, the hevein sequence was scanned by using site-specific mutations. Twenty-nine hevein mutants were designed and produced by a baculovirus expression system in insect cells and tested by IgE inhibition-ELISA using sera from 26 latex allergic patients. Six potential IgE-interacting residues of hevein (Arg5, Lys10, Glu29, Tyr30, His35, and Gln38) were identified and characterized further in detail. Based on these six residues, two triple mutants (HΔ…

MaleModels MolecularProtein ConformationMutantImmunoglobulin Emedicine.disease_causeEpitopelaw.inventionEpitopes0302 clinical medicineProtein structureAllergenlawImmunology and AllergyCombinatorial Chemistry TechniquesChild0303 health sciencesbiologyChemistryMiddle AgedRecombinant Proteins3. Good healthBiochemistryLatex allergyRecombinant DNAFemalePlant LectinsProtein BindingAdultAdolescentImmunologyMutagenesis (molecular biology technique)Binding Competitive03 medical and health sciencesLatex HypersensitivitymedicineHumansPoint Mutation030304 developmental biologyAgedAllergensImmunoglobulin Emedicine.disease030228 respiratory systemAmino Acid SubstitutionDesensitization Immunologicbiology.proteinMutagenesis Site-DirectedBinding Sites AntibodyAntimicrobial Cationic PeptidesJournal of immunology (Baltimore, Md. : 1950)
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Molecular cloning and characterization ofEchinostoma caproniheat shock protein-70 and differential expression in the parasite derived from low- and h…

2008

SUMMARYWe cloned and expressedEchinostoma caproniHSP70 inEscherichia coli. This molecule presents an open reading frame (ORF) of 655 amino acids, and a theoretical molecular weight of 71 kDa.E. caproniHSP70 protein showed a high homology to other helminth molecules, major differences being located in the C-terminal region of the molecule, with a hydrophobic portion. Studies of protein and messenger RNA (mRNA) expression revealed a distinct pattern, depending on the host (low- or high-compatible). Specific polyclonal antisera raised against the recombinant protein expressed inEscherichia colidemonstrated its selective presence in excretory/secretory products (ESP) of adult parasites obtained…

MaleMolecular Sequence DataBiologyMolecular cloningmedicine.disease_causeHost-Parasite Interactionslaw.inventionFeceslawCricetinaeEchinostomaHeat shock proteinmedicineAnimalsParasite hostingHSP70 Heat-Shock ProteinsAmino Acid SequenceCloning MolecularRats WistarParasite Egg CountEscherichia coliMessenger RNAMesocricetusImmunohistochemistryMolecular biologyRatsOpen reading frameInfectious DiseasesGene Expression RegulationPolyclonal antibodiesRecombinant DNAbiology.proteinAnimal Science and ZoologyParasitologyParasitology
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Personalized cost-effectiveness of boceprevir-based triple therapy for untreated patients with genotype 1 chronic hepatitis C

2014

Abstract Background We assessed the cost-effectiveness of boceprevir-based triple therapy compared to peginterferon alpha and ribavirin dual therapy in untreated patients with genotype 1 chronic hepatitis C; patients were discriminated according to the combination of baseline plus on-treatment predictors of boceprevir-based triple therapy. Methods Cost-effectiveness analysis performed according to data from the available published literature. The target population was composed of untreated Caucasian patients, aged 50 years, with genotype 1 chronic hepatitis C, and these were evaluated over a lifetime horizon by Markov model. The study was carried out from the perspective of the Italian Nati…

MaleNational Health ProgramsCost effectivenessCost-Benefit AnalysisHepacivirusNational Health ProgramHepacivirusPharmacologyPolyethylene GlycolPolyethylene Glycolschemistry.chemical_compoundQuality-Adjusted Life YearMedicineSettore SECS-S/05 - Statistica SocialeMultivariate AnalysiBoceprevirSettore MED/12 - GastroenterologiabiologyMedicine (all)GastroenterologyMiddle AgedRecombinant ProteinMarkov ChainsRecombinant ProteinsModels EconomicTreatment OutcomeItalyDrug Therapy CombinationFemaleQuality-Adjusted Life YearsSettore SECS-S/01 - StatisticaViral loadHumanmedicine.medical_specialtyGenotypeProlineAlpha interferonInterferon alpha-2Antiviral AgentsInternal medicineBoceprevirRibavirinHumansCost-Benefit AnalysiAntiviral AgentHepaciviruPeg-interferonHepatologybusiness.industryRibavirinInterferon-alphaHepatologyHepatitis C ChronicMarkov Chainbiology.organism_classificationQuality-adjusted life yearchemistryCost-effectiveneMultivariate AnalysisQuality of LifeCost-effectivenessbusiness
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