Search results for "1312 Molecular Biology"

showing 10 items of 45 documents

An impaired peroxisomal targeting sequence leading to an unusual bicompartmental distribution of cytosolic epoxide hydrolase

1991

AbstractTo gain an understanding of the mechanism by which the subcellular distribution of cytosolic epoxide hydrolase (cEH) is directed, we have analyzed the carboxy terminal region of rat liver cEH by means of cDNA cloning to define the structure of its possible peroxisomal targeting sequence (PTS). Purified cEH was subjected to peptide analysis following endoproteinase Glu-C digestion and HPLC-separation of the fragments. The obtained sequence information was used to perform PCR experiments resulting in the isolation of a 680 bp cDNA clone encoding the carboxy terminus of cEH. The deduced amino acid sequence displays a terminal tripeptide Ser-Lys-Ile which is highly homologous to the PTS…

MaleSignal peptidePTSanimal structures1303 BiochemistryMolecular Sequence DataBiophysics10050 Institute of Pharmacology and Toxicology610 Medicine & healthTripeptideProtein Sorting SignalsBiologyMicrobodiesBiochemistryAmino acid sequence1307 Cell BiologyCytosol1315 Structural Biology1311 GeneticsStructural BiologyComplementary DNAGenetics1312 Molecular BiologyAnimalsCloning MolecularEpoxide hydrolaseMolecular BiologyPeptide sequenceEpoxide Hydrolaseschemistry.chemical_classificationBase SequencecDNA sequenceDNACell BiologyPeroxisomeMolecular biologyRatsIsoenzymesCytosolPCREnzymeLiverchemistryBiochemistrycEH570 Life sciences; biologyPeptide analysis1304 Biophysics
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Sequence of a novel cytochrome CYP2B cDNA coding for a protein which is expressed in a sebaceous gland, but not in the liver

1992

The major phenobarbital-inducible rat hepatic cytochromes P-450, CYP2B1 and CYP2B2, are the paradigmatic members of a cytochrome P-450 gene subfamily that contains at least seven additional members. Specific oligonucleotide probes for these genomic members of the CYP2B subfamily were used to assess their tissue-specific expression. In Northern-blot analysis a probe specific to gene 4 (which is designated now as CYP2B12) hybridized to a single mRNA present in the preputial gland, an organ which is used as a model for sebaceous glands, but did not hybridize to mRNA isolated from the liver or from five other tissues of untreated or Aroclor 1254-treated rats. The cDNA sequence for the CYP2B12 R…

MaleSubfamily1303 BiochemistryMolecular Sequence Data10050 Institute of Pharmacology and Toxicology610 Medicine & healthBiologyBiochemistryRats Sprague-Dawley1307 Cell BiologySebaceous GlandsRapid amplification of cDNA endsCytochrome P-450 Enzyme SystemComplementary DNAMicrosomes1312 Molecular BiologyCoding regionAnimalsAmino Acid SequenceMolecular BiologyBase SequencecDNA librarySingle-Strand Specific DNA and RNA EndonucleasesProtein primary structureNucleic acid sequenceCell BiologyDNARibonuclease PancreaticBlotting NorthernMolecular biologyRatsOpen reading frameBiochemistryLiverMultigene FamilyMicrosomes Liver570 Life sciences; biologyFemaleOligonucleotide ProbesResearch Article
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Langerin+ DCs regulate innate IL-17 production in the oral mucosa during Candida albicans-mediated infection

2018

The opportunistic fungal pathogen Candida albicans frequently causes diseases such as oropharyngeal candidiasis (OPC) in immunocompromised individuals. Although it is well appreciated that the cytokine IL-17 is crucial for protective immunity against OPC, the cellular source and the regulation of this cytokine during infection are still a matter of debate. Here, we directly visualized IL-17 production in the tongue of experimentally infected mice, thereby demonstrating that this key cytokine is expressed by three complementary subsets of CD90+ leukocytes: RAG-dependent αβ and γδ T cells, as well as RAG-independent ILCs. To determine the regulation of IL-17 production at the onset of OPC, we…

Malemedicine.medical_treatment2405 ParasitologyPathology and Laboratory Medicine10263 Institute of Experimental ImmunologyMonocytesMice0302 clinical medicineAnimal CellsCandida albicansBiology (General)Candida albicansMononuclear Phagocyte SystemFungal PathogensInnate Immune Systemeducation.field_of_studyEukaryotaMononuclear phagocyte systemFlow CytometryCorpus albicans3. Good healthSpectrophotometryMedical MicrobiologyCytokinesCytophotometryCellular Types10244 Institute of VirologyQH301-705.5Immune CellsImmunologyMicrobiology03 medical and health sciences1311 GeneticsGenetics1312 Molecular BiologyeducationMicrobial PathogensMolecular BiologyMouth2403 ImmunologyBlood CellsOrganismsBiology and Life SciencesDendritic CellsMolecular DevelopmentYeastMice Inbred C57BLMannose-Binding Lectins030104 developmental biologyImmunologyThy-1 Antigens570 Life sciences; biologyParasitologyImmunologic diseases. AllergyDigestive SystemDevelopmental Biology0301 basic medicineNeutrophilsPhysiologyInterleukin-1betaYeast and Fungal ModelsInterleukin-23White Blood CellsSpectrum Analysis TechniquesCandidiasis OralImmune PhysiologyLeukocytesMedicine and Health SciencesCandidaStainingbiologyInterleukin-172404 MicrobiologyCell StainingSpecific Pathogen-Free OrganismsInfectious DiseasesCytokineExperimental Organism SystemsAntigens SurfaceFemaleAnatomyPathogensResearch ArticleLangerinPopulationMycologyOpportunistic InfectionsResearch and Analysis MethodsTongueImmunityVirologymedicineAnimalsLectins C-TypeInterleukin 6Interleukin-6Mouth MucosaFungiCell BiologyRC581-607biology.organism_classificationSpecimen Preparation and TreatmentImmune Systembiology.protein2406 VirologySpleen030215 immunology
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Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site

2003

Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an alpha/beta hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis, solved using single-wavelength anomalous dispersion from a selenomethionine-substituted protein and refined at 1.2 A resolution. This enzyme represents a completely different structure and a novel one-step mechanism. The fold features a highly curved six-stranded mixed beta-sheet, with four alpha-helices packed onto it to create a …

Models MolecularAFSG Stafafdelingen (WUATV)10050 Institute of Pharmacology and Toxicologydrug protein bindingEnantioselectivityEpoxide hydrolaseCrystallography X-Rayuncultured actinomyceteCatalytic Domain2400 General Immunology and Microbiologyalpha helixRhodococcuscholesterol epoxide hydrolasenaphthalene 12-dioxygenasedcl14limonene 12 epoxide hydrolaseEpoxide hydrolaseBacteria (microorganisms)delta(5)-3-ketosteroid isomeraseEpoxide HydrolasesLimonene-12-epoxide hydrolaseGeneral Neurosciencearticle2800 General NeuroscienceActinobacteria (class)Articlesagrobacterium-radiobacterEnzyme structureRecombinant Proteinsunclassified drugenzyme structurereaction analysisBiochemistrypriority journalenzyme active siteMechanism2-dioxygenaseDimerizationBiotechnologychemical reactioncrystal structureaspergillus-nigermacromolecular structuresStereochemistrybeta sheetvalpromideMolecular Sequence Data610 Medicine & healthGenetics and Molecular BiologyBiologyGeneral Biochemistry Genetics and Molecular BiologyBacterial Proteinssite directed mutagenesis1300 General Biochemistry Genetics and Molecular BiologyHydrolase1312 Molecular BiologyAmino Acid SequencedetoxificationRhodococcus erythropolisBiologyMonoterpene degradationMolecular Biologyprotein data-bankenzyme substrate complexEnzyme substrate complexnonhumancatalysisSequence Homology Amino AcidGeneral Immunology and Microbiologybacterial enzymeActive sitecrystal-structureAFSG Staff Departments (WUATV)enzyme metabolismProtein SubunitsenzymeEpoxide HydrolasesGeneral Biochemistrybiology.proteinMutagenesis Site-Directed570 Life sciences; biologyselenomethioninenaphthalene 1Alpha helix
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Insights into the catalytic mechanism of human sEH phosphatase by site-directed mutagenesis and LC-MS/MS analysis

2008

We have recently reported that human soluble epoxide hydrolase (sEH) is a bifunctional enzyme with a novel phosphatase enzymatic activity. Based on a structural relationship with other members of the haloacid dehalogenase superfamily, the sEH N-terminal phosphatase domain revealed four conserved sequence motifs, including the proposed catalytic nucleophile D9, and several other residues potentially implicated in substrate turnover and/or Mg(2+) binding. To enlighten the catalytic mechanism of dephosphorylation, we constructed sEH phosphatase active-site mutants by site-directed mutagenesis. A total of 18 mutants were constructed and recombinantly expressed in Escherichia coli as soluble pro…

Models MolecularEpoxide hydrolase 2Molecular Sequence DataPhosphatase10050 Institute of Pharmacology and Toxicology610 Medicine & healthMass SpectrometryPhosphatesDephosphorylation1315 Structural BiologyProtein structureStructural Biology1312 Molecular BiologyHumansPhosphofructokinase 2Amino Acid SequenceBinding siteProtein Structure QuaternarySite-directed mutagenesisMolecular BiologyEpoxide HydrolasesBinding SitesChemistrySubstrate (chemistry)Phosphoric Monoester HydrolasesRecombinant ProteinsProtein Structure TertiaryProtein SubunitsBiochemistryMutagenesis Site-Directed570 Life sciences; biologyDimerizationSequence AlignmentChromatography Liquid
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Structure of Aspergillus niger epoxide hydrolase at 1.8 A resolution: implications for the structure and function of the mammalian microsomal class o…

2000

AbstractBackground: Epoxide hydrolases have important roles in the defense of cells against potentially harmful epoxides. Conversion of epoxides into less toxic and more easily excreted diols is a universally successful strategy. A number of microorganisms employ the same chemistry to process epoxides for use as carbon sources.Results: The X-ray structure of the epoxide hydrolase from Aspergillus niger was determined at 3.5 Å resolution using the multiwavelength anomalous dispersion (MAD) method, and then refined at 1.8 Å resolution. There is a dimer consisting of two 44 kDa subunits in the asymmetric unit. Each subunit consists of an α/β hydrolase fold, and a primarily helical lid over the…

Models MolecularProtein ConformationStereochemistryEpoxide10050 Institute of Pharmacology and Toxicology610 Medicine & healthEpoxide hydrolasechemistry.chemical_compoundProtein structure1315 Structural BiologyStructural BiologyMicrosomesHydrolase1312 Molecular BiologyAnimalsHumansBinding siteEpoxide hydrolaseMolecular BiologyX-ray crystallographyEpoxide HydrolasesMicrosomal epoxide hydrolasesDrug metabolismBinding SitesbiologyMADChemistryAspergillus nigerbiology.organism_classificationBiochemistryEpoxide HydrolasesMicrosome570 Life sciences; biologyAspergillus nigerDimerization
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Myoglobin, expressed in brown adipose tissue of mice, regulates the content and activity of mitochondria and lipid droplets

2021

Abstract The identification of novel physiological regulators that stimulate energy expenditure through brown adipose tissue (BAT) activity in substrate catalysis is of utmost importance to understand and treat metabolic diseases. Myoglobin (MB), known to store or transport oxygen in heart and skeletal muscles, has recently been found to bind fatty acids with physiological constants in its oxygenated form (i.e., MBO2). Here, we investigated the in vivo effect of MB expression on BAT activity. In particular, we studied mitochondrial function and lipid metabolism as essential determinants of energy expenditure in this tissue. We show in a MB-null (MBko) mouse model that MB expression in BAT i…

PalmitatesOxidative phosphorylationMitochondrion1307 Cell BiologyMiceAdipose Tissue BrownLipid dropletBrown adipose tissueRespiration1312 Molecular BiologymedicineAnimalsHumansPPAR alpha11434 Center for Clinical StudiesMuscle SkeletalMolecular BiologyUncoupling Protein 1Mice KnockoutMyoglobinChemistryProteinsThermogenesisLipid metabolismLipid DropletsCell BiologyMetabolism10081 Institute of Veterinary PhysiologyPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaMitochondriaCell biologyOxygenDisease Models AnimalAdipocytes Brownmedicine.anatomical_structure10076 Center for Integrative Human Physiology570 Life sciences; biologyApoptosis Regulatory ProteinsEnergy MetabolismThermogenesisBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
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IL-6 Regulates Neutrophil Microabscess Formation in IL-17A-Driven Psoriasiform Lesions

2014

The lack of a generally accepted animal model for human psoriasis has hindered progress with respect to understanding the pathogenesis of the disease. Here we present a model in which transgenic IL-17A expression is targeted to the skin in mice, achievable after crossing our IL-17A(ind) allele to the K14-Cre strain. K14-IL-17A(ind/+) mice invariably develop an overt skin inflammation bearing many hallmark characteristics of human psoriasis including dermal infiltration of effector T cells, formation of neutrophil microabscesses, and hyperkeratosis. IL-17A expression in the skin results in upregulated granulopoiesis and migration of IL-6R-expressing neutrophils into the skin. Neutralization …

Pathologymedicine.medical_specialty1303 BiochemistryNeutrophilsT-LymphocytesHyperkeratosisGene Expression610 Medicine & healthInflammationDermatology10263 Institute of Experimental ImmunologyBiochemistryGranulopoiesis2708 Dermatology1307 Cell BiologyPathogenesisMicePsoriasis1312 Molecular BiologymedicineAnimalsPsoriasisMicroabscessMolecular BiologyMice Knockoutintegumentary systemInterleukin-6business.industryMacrophagesInterleukin-17Cell Biologymedicine.diseaseReceptors Interleukin-6AbscessDisease Models AnimalImmunology570 Life sciences; biologyEpidermismedicine.symptombusinessInfiltration (medical)GranulocytesSignal TransductionEpidermal thickeningJournal of Investigative Dermatology
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Fitness Trade-Offs Determine the Role of the Molecular Chaperonin GroEL in Buffering Mutations

2015

Molecular chaperones fold many proteins and their mutated versions in a cell and can sometimes buffer the phenotypic effect of mutations that affect protein folding. Unanswered questions about this buffering include the nature of its mechanism, its influence on the genetic variation of a population, the fitness trade-offs constraining this mechanism, and its role in expediting evolution. Answering these questions is fundamental to understand the contribution of buffering to increase genetic variation and ecological diversification. Here, we performed experimental evolution, genome resequencing, and computational analyses to determine the trade-offs and evolutionary trajectories of Escherich…

PopulationGenetic FitnessBiologyGroELCell LineChaperonin10127 Institute of Evolutionary Biology and Environmental StudiesGenetic drift1311 Geneticsmutational bufferingOperonGenetic variationGenetics1312 Molecular BiologyEscherichia coliexperimental evolutioneducationMolecular BiologyDiscoveriesEcology Evolution Behavior and Systematics2. Zero hungerGeneticseducation.field_of_studyExperimental evolutionGenetic DriftChaperonin 60Gene Expression Regulation BacterialGroEL1105 Ecology Evolution Behavior and SystematicsGenes BacterialMutation570 Life sciences; biology590 Animals (Zoology)bacteriaProtein foldingGenetic FitnessDirected Molecular EvolutionSubcellular Fractions
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Reproducible and Consistent Quantification of the Saccharomyces cerevisiae Proteome by SWATH-mass spectrometry *

2015

Targeted mass spectrometry by selected reaction monitoring (S/MRM) has proven to be a suitable technique for the consistent and reproducible quantification of proteins across multiple biological samples and a wide dynamic range. This performance profile is an important prerequisite for systems biology and biomedical research. However, the method is limited to the measurements of a few hundred peptides per LC-MS analysis. Recently, we introduced SWATH-MS, a combination of data independent acquisition and targeted data analysis that vastly extends the number of peptides/proteins quantified per sample, while maintaining the favorable performance profile of S/MRM. Here we applied the SWATH-MS t…

ProteomicsOsmosisSaccharomyces cerevisiae Proteins1303 BiochemistryOsmotic shockSaccharomyces cerevisiae610 Medicine & health10071 Functional Genomics Center ZurichSaccharomyces cerevisiaeOsmosisMass spectrometryBiochemistryMass SpectrometryAnalytical Chemistry1312 Molecular BiologyData-independent acquisitionMolecular Biology1602 Analytical ChemistryChromatographybiologySelected reaction monitoringTechnological Innovation and ResourcesReproducibility of Resultsbiology.organism_classificationTargeted mass spectrometryProteomeCarbohydrate Metabolism570 Life sciences; biologyPeptidesMolecular & Cellular Proteomics
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