Search results for " Molecular Sequence Data"

showing 10 items of 41 documents

Evaluation of acyl coenzyme A oxidase (Aox) isozyme function in the n- alkane-assimilating yeast Yarrowia lipolytica

1999

ABSTRACT We have identified five acyl coenzyme A (CoA) oxidase isozymes (Aox1 through Aox5) in the n -alkane-assimilating yeast Yarrowia lipolytica , encoded by the POX1 through POX5 genes. The physiological function of these oxidases has been investigated by gene disruption. Single, double, triple, and quadruple disruptants were constructed. Global Aox activity was determined as a function of time after induction and of substrate chain length. Single null mutations did not affect growth but affected the chain length preference of acyl-CoA oxidase activity, as evidenced by a chain length specificity for Aox2 and Aox3. Aox2 was shown to be a long-chain acyl-CoA oxidase and Aox3 was found to …

MESH : Escherichia coliMESH: Sequence Analysis DNAMESH : Molecular Sequence DataMutantGene ExpressionMESH: Base Sequencechemistry.chemical_compoundCloning Molecular[INFO.INFO-BT]Computer Science [cs]/BiotechnologyDNA FungalMESH: MutagenesisMESH : IsoenzymesOxidase testbiologyMESH: Escherichia coliMESH: Acyl-CoA OxidaseMESH : MutagenesisMESH : Cell DivisionMESH : OxidoreductasesIsoenzymesBlotEukaryotic Cells[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyFungalBiochemistryMESH: IsoenzymesMESH: Cell DivisionMESH : Acyl-CoA OxidaseOxidoreductasesSequence Analysis[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyCell DivisionMESH: Gene ExpressionMESH : Cloning MolecularGenes FungalMolecular Sequence DataMicrobiologyIsozymeWESTERN BLOTTINGAlkanes[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyEscherichia coliMESH: Cloning Molecular[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: OxidoreductasesMESH: Saccharomycetales[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular BiologyGeneMESH : AlkanesMESH: Molecular Sequence DataBase SequenceMolecularYarrowiaSequence Analysis DNAMESH : SaccharomycetalesDNAbiology.organism_classificationMolecular biologyYeastMESH : Gene ExpressionMESH: AlkanesMESH: DNA FungalOleic acid[INFO.INFO-BT] Computer Science [cs]/BiotechnologyGeneschemistryMutagenesisSaccharomycetalesMESH : Base SequenceMESH : Genes FungalAcyl-CoA OxidaseMESH : DNA FungalMESH: Genes FungalMESH : Sequence Analysis DNACloning
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Immunoaffinity purification and characterization of mitochondrial membrane-bound D-3-hydroxybutyrate dehydrogenase from Jaculus orientalis.

2008

Abstract Background The interconversion of two important energy metabolites, 3-hydroxybutyrate and acetoacetate (the major ketone bodies), is catalyzed by D-3-hydroxybutyrate dehydrogenase (BDH1: EC 1.1.1.30), a NAD+-dependent enzyme. The eukaryotic enzyme is bound to the mitochondrial inner membrane and harbors a unique lecithin-dependent activity. Here, we report an advanced purification method of the mammalian BDH applied to the liver enzyme from jerboa (Jaculus orientalis), a hibernating rodent adapted to extreme diet and environmental conditions. Results Purifying BDH from jerboa liver overcomes its low specific activity in mitochondria for further biochemical characterization of the e…

lcsh:Animal biochemistryMESH : AgedMESH : RodentiaMESH: RodentiaMESH: Base SequenceBiochemistryMESH: Lipid PeroxidationMESH : Information ServicesAntigen-Antibody ReactionsMESH: Health EducationEpitopesMESH: OrganizationsMESH: LibrariesMESH: Antigen-Antibody Reactionslcsh:QD415-436MESH: AnimalsMESH : OrganizationsMESH : Physician's RoleMESH: Bacterial ProteinsImmunosorbent Techniqueschemistry.chemical_classificationMESH: Conserved SequenceMethodology ArticleMESH : Computer Communication NetworksMESH: Chromatography AffinityMESH : Pseudomonas aeruginosaMESH : Chromatography AffinityMESH : Immunosorbent TechniquesMESH: Ethnic GroupsMESH : Ethnic GroupsMESH: EpitopesMESH : Patient SatisfactionMESH : United StatesMESH: MitochondriaMESH : Antigen-Antibody ReactionsMolecular Sequence DataMESH : Hydroxybutyrate DehydrogenaseMESH: Sequence AlignmentRodentiaMESH: Information ServicesMESH : Epitopeslcsh:BiochemistryMESH : Mitochondrial MembranesBacterial ProteinsMESH : Conserved SequenceComplementary DNAMESH : LibrariesMolecular Biology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: Immunosorbent TechniquesMESH: Molecular Sequence DataMESH: HumansMESH : Consumer ParticipationMESH : HumansMESH: AdultMESH: Patient SatisfactionMESH: Hydroxybutyrate DehydrogenaseMESH: Consumer ParticipationchemistryLipid PeroxidationMESH: FemaleMESH: LiverMESH : Sequence Analysis DNAMESH: Continental Population GroupsMESH: Sequence Analysis DNAMESH : Molecular Sequence DataDehydrogenaseChromatography AffinityMESH: Mitochondrial MembranesMESH: Antibodies BacterialMESH : Bacterial ProteinsMESH : FemaleMESH: Computer Communication NetworksConserved SequenceMESH: AgedbiologyMESH : Lipid PeroxidationMESH : Sequence AlignmentMESH: Physician's RoleMESH : AdultAntibodies BacterialMitochondriaAmino acidLiverBiochemistryMitochondrial MembranesPseudomonas aeruginosaMESH: Pseudomonas aeruginosaMESH : MitochondriaMESH : Mass MediaMESH: Mass MediaMESH : MaleHydroxybutyrate DehydrogenaseAffinity chromatographyMESH : Health Education[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: United StatesAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH : Antibodies Bacteriallcsh:QP501-801Jaculus orientalisMESH : Continental Population GroupsBase SequenceMESH : LiverSequence Analysis DNAbiology.organism_classificationMolecular biologyMESH: MaleEnzymePolyclonal antibodiesbiology.proteinMESH : Base SequenceNAD+ kinaseMESH : AnimalsSequence Alignment
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Cloning and expression of genes involved in conidiation and surface properties of Penicillium camemberti grown in liquid and solid cultures.

2008

International audience; Based on bioinformatic data on model fungi, the rodA and wetA genes encoding, respectively, a RodA hydrophobin protein and the WetA protein involved in conidiation mechanisms, were PCR-cloned and characterized for the first time in Penicillium camemberti. These results, completed by a sequence of the brlA gene (available in GenBank), which encodes a major transcriptional regulator also involved in the conidiation mechanism, were used to compare, by qRT-PCR, the expression of the three genes in liquid and solid cultures in a synthetic medium. While expression of the brlA and wetA genes increased dramatically in both culture conditions after 4 days of growth, expressio…

MESH: Sequence Analysis DNAMESH : Spores FungalMESH : Molecular Sequence DataConidiationMESH: Amino Acid SequenceMESH: Base SequenceGene Expression Regulation FungalGene expressionMESH : Fungal ProteinsCloning MolecularFungal proteinMESH : Amino Acid SequenceMESH : Sequence AlignmentGeneral MedicineSpores FungalMESH: MyceliumCell biologyWetaPenicillium camembertiMESH: Fungal ProteinsMESH : HydrophobicityHydrophobic and Hydrophilic InteractionsMESH : MyceliumMESH: Gene Expression Regulation FungalHyphaMESH : Cloning MolecularHydrophobinMolecular Sequence DataMESH: Sequence AlignmentBiologyMicrobiologyMicrobiologyFungal ProteinsMESH: Spores FungalMESH : Gene Expression Regulation FungalMESH: Cloning Molecular[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceMolecular BiologyGene[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: PenicilliumMESH: HydrophobicityMESH: Molecular Sequence DataBase SequenceMyceliumPenicilliumSequence Analysis DNAMESH : Penicilliumbiology.organism_classificationCulture MediaMESH: Culture MediaMESH : Base SequenceMESH : Culture MediaSequence AlignmentMESH : Sequence Analysis DNA
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Identification of Cpgp40/15 Type Ib as the Predominant Allele in Isolates of Cryptosporidium spp. from a Waterborne Outbreak of Gastroenteritis in So…

2006

ABSTRACT Cryptosporidium sp. isolates from a waterborne outbreak of diarrhea in France were analyzed by PCR-restriction fragment length polymorphism analysis and sequencing of the Cpgp40/15 locus. Ninety-one percent of the isolates were Cryptosporidium hominis type Ib. The results of this study and those of studies of other outbreaks suggest that the type Ib allele is the predominant allele associated with waterborne cryptosporidiosis.

MESH : France/epidemiologyEpidemiologyMESH : polymerase chain reactionMESH : molecular sequence dataProtozoan ProteinsCryptosporidiosisPolymerase Chain Reactionlaw.inventionDisease OutbreaksMESH : Cryptosporidium/geneticsMESH : water/parasitologylaw[ SDV.MP ] Life Sciences [q-bio]/Microbiology and ParasitologyMESH : gastroenteritis/parasitologyMESH : Polymorphism restriction fragment lengthwaterborne outbreakPolymerase chain reactionbiologyMESH : DNA Protozoan/analysisCryptosporidiumGastroenteritisDiarrheaMESH : Cryptosporidiosis/epidemiologyFrancemedicine.symptomMESH : Cryptosporidium/classificationCryptosporidium hominisMESH : Protozoan proteins/metabolismPolymorphism Restriction Fragment LengthMicrobiology (medical)MESH : Cryptosporidium/isolation&purificationMolecular Sequence DataCryptosporidiumLocus (genetics)MESH : Disease outbreaksMicrobiologyMESH : Cryptosporidiosis/parasitologymedicineAnimalsAlleleGenotyping[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyAllelesMESH : animalsMESH : sequence analysis DNAOutbreakWaterSequence Analysis DNADNA Protozoanbiology.organism_classificationMESH : protozoan proteins/geneticsVirologygenotypingMESH : Gastroenteritis/epidemiologyMESH : Alleles
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Yersinia pestis DNA from Skeletal Remains from the 6th Century AD Reveals Insights into Justinianic Plague

2013

Yersinia pestis, the etiologic agent of the disease plague, has been implicated in three historical pandemics. These include the third pandemic of the 19th and 20th centuries, during which plague was spread around the world, and the second pandemic of the 14th–17th centuries, which included the infamous epidemic known as the Black Death. Previous studies have confirmed that Y. pestis caused these two more recent pandemics. However, a highly spirited debate still continues as to whether Y. pestis caused the so-called Justinianic Plague of the 6th–8th centuries AD. By analyzing ancient DNA in two independent ancient DNA laboratories, we confirmed unambiguously the presence of Y. pestis DNA in…

MaleHistoryYersinia pestis590Social and Behavioral SciencesPandemicBiology (General)16th CenturyPhylogenyHistory 15th CenturybiologyBacterialHistory 19th Century20th CenturyBiological AnthropologyHistory 16th Century17th CenturyFemaleBase Sequence; Bone and Bones; DNA Bacterial; Female; Genotype; History 15th Century; History 16th Century; History 17th Century; History 19th Century; History 20th Century; History Medieval; Humans; Male; Molecular Sequence Data; Pandemics; Yersinia pestis; Phylogeny; PlagueMedievalResearch ArticleDNA BacterialGenotypeQH301-705.5ImmunologyMolecular Sequence DataPlague (disease)MicrobiologyBone and BonesNOHistory 17th CenturyVirologyGeneticsHumansBase sequenceMolecular BiologyPandemicsBiologyPlague bacillus19th CenturyPlagueBase SequenceDNARC581-607History 20th Centurybiology.organism_classificationVirologyHistory Medieval15th CenturyAncient DNAYersinia pestisAnthropologyYersinia pestis DNAParasitologyImmunologic diseases. Allergy
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Thioflavin T templates amyloid β(1–40) conformation and aggregation pathway

2015

Aβ(1-40) peptide supramolecular assembly and fibril formation processes are widely recognized to have direct implications in the progression of Alzheimer's disease. The molecular basis of this biological process is still unknown and there is a strong need of developing effective strategies to control the occurring events. To this purpose the exploitation of small molecules interacting with Aβ aggregation represents one of the possible routes. Moreover, the use specific labeling has represented so far one of the most common and effective methods to investigate such a process. This possibility in turn rests on the reliability of the probe/labels involved. Here we present evidences of the effe…

Protein StructureSecondaryAβ(1–40) peptideAmyloidProtein ConformationMolecular Sequence DataBiophysicsSupramolecular chemistryMolecular Dynamics SimulationProtein aggregationProtein Aggregation PathologicalBiochemistryProtein Structure SecondarySupramolecular assemblyProtein Aggregateschemistry.chemical_compoundProtein structureAlzheimer DiseasePathologicalSecondary structureAβ(1-40) peptideHumansBenzothiazolesAmino Acid SequenceFluorescent DyesAmyloid beta-PeptidesProtein StabilityOrganic ChemistryAlzheimer's diseaseProtein AggregationSmall moleculePeptide FragmentsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Peptide ConformationAlzheimer's disease; Aβ(1–40) peptide; Protein aggregation; Protein conformation; Secondary structure; Thioflavin T; Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Fluorescence Recovery After Photobleaching; Fluorescent Dyes; Humans; Molecular Dynamics Simulation; Molecular Sequence Data; Peptide Fragments; Protein Aggregates; Protein Aggregation Pathological; Protein Conformation; Protein Multimerization; Protein Stability; Protein Structure Secondary; ThiazolesThiazolesBiophysicBiochemistrychemistryThioflavin TBiophysicsThioflavinProtein MultimerizationFluorescence Recovery After PhotobleachingBiophysical Chemistry
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Phosphorylation of serine residues is fundamental for the calcium-binding ability of Orchestin, a soluble matrix protein from crustacean calcium stor…

2003

International audience; Orchestia cavimana is a terrestrial crustacean, which cyclically stores calcium in diverticula of the midgut, in the form of calcified amorphous concretions. These concretions are associated with a proteinaceous matrix, the main constituent of the soluble matrix is Orchestin, an acidic calcium-binding protein [Testenière et al., Biochem. J. 361 (2002) 327-335]. In the present paper, we clearly demonstrate that Orchestin is phosphorylated on serine and tyrosine residues, but that calcium binding only occurs via the phosphoserine residues. To our knowledge, this is the first example of an invertebrate mineralization for which a post-translational modification is clearl…

BiomineralizationMESH: Amino Acid SequenceMESH: Calcium-Binding ProteinsMatrix (biology)01 natural sciencesBiochemistryCalcium in biologyMESH: TyrosineSerinechemistry.chemical_compoundMESH: Structure-Activity RelationshipStructural BiologyCrustaceaSerineElectrophoresis Gel Two-DimensionalMESH: AnimalsTyrosinePhosphorylation0303 health sciencesBiochemistryMESH: CalciumPhosphorylationElectrophoresis Polyacrylamide GelOrganic matrixProtein BindingMolecular Sequence DataBiophysicschemistry.chemical_elementCrustaceanCalciumBiology010402 general chemistryMESH: Calcification Physiologic03 medical and health sciencesStructure-Activity RelationshipCalcification PhysiologicMESH: CrustaceaGeneticsAnimalsMESH: Protein Binding[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceMESH: SerineMolecular Biology030304 developmental biologyCalcium metabolismMESH: Molecular Sequence DataMESH: PhosphorylationCalcium-Binding ProteinsCell BiologyMESH: Electrophoresis Gel Two-Dimensional0104 chemical scienceschemistryPhosphoserineMESH: Protein Processing Post-TranslationalTyrosineCalciumCalcium bindingProtein Processing Post-TranslationalMESH: Electrophoresis Polyacrylamide Gel
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The Chlamydomonas genome reveals the evolution of key animal and plant functions

2007

Chlamydomonas reinhardtii is a unicellular green alga whose lineage diverged from land plants over 1 billion years ago. It is a model system for studying chloroplast-based photosynthesis, as well as the structure, assembly, and function of eukaryotic flagella (cilia), which were inherited from the common ancestor of plants and animals, but lost in land plants. We sequenced the ∼120-megabase nuclear genome of Chlamydomonas and performed comparative phylogenomic analyses, identifying genes encoding uncharacterized proteins that are likely associated with the function and biogenesis of chloroplasts or eukaryotic flagella. Analyses of the Chlamydomonas genome advance our understanding of the a…

0106 biological sciencesMESH: Sequence Analysis DNAMESH: Algal ProteinsChloroplastsProteomeMESH: PlantsChlamydomonas reinhardtii01 natural sciencesGenomeMESH: Membrane Transport ProteinsDNA AlgalMESH: DNA AlgalMESH: AnimalsGoniumPhotosynthesisMESH: PhylogenyMESH: PhotosynthesisPhylogenyGenetics0303 health sciencesGenomeMultidisciplinarybiologyMESH: Genomicsfood and beveragesGenomicsPlantsBiological EvolutionMESH: Genes[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]MESH: ProteomeFlagellaMultigene FamilyMESH: Computational BiologyMESH: Chlamydomonas reinhardtiiNuclear geneMolecular Sequence Data[SDV.BC]Life Sciences [q-bio]/Cellular BiologyFlagellumMESH: FlagellaArticle03 medical and health sciencesIntraflagellar transportMESH: EvolutionAnimalsMESH: Genome[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Gene[SDV.BC] Life Sciences [q-bio]/Cellular Biology030304 developmental biologyMESH: Molecular Sequence DataMESH: ChloroplastsAlgal ProteinsChlamydomonasComputational BiologyMembrane Transport ProteinsSequence Analysis DNAbiology.organism_classificationGenesMESH: Multigene FamilyChlamydomonas reinhardtii010606 plant biology & botany
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Protein mapping of calcium carbonate biominerals by immunogold

2007

The construction of metazoan calcium carbonate skeletons is finely regulated by a proteinaceous extracellular matrix, which remains embedded within the exoskeleton. In spite of numerous biochemical studies, the precise localization of skeletal proteins has remained for a long time as an elusive goal. In this paper, we describe a technique for visualizing shell matrix proteins on the surface of calcium carbonate crystals or within the biominerals. The technique is as follows: freshly broken pieces of biominerals or NaOCl then EDTA-etched polished surfaces are incubated with an antibody elicited against one matrix protein, then with a secondary gold-coupled antibody. After silver enhancement,…

MESH : Models ChemicalMESH : Molecular Sequence DataMESH: Sequence Homology Amino AcidMESH : Calcium CarbonateMESH : ImmunohistochemistryMESH : Aspartic AcidMESH: TrypsinMESH: Amino Acid SequenceMatrix (biology)01 natural sciencesMESH: Aspartic AcidMESH : Proteinschemistry.chemical_compoundTrypsinMESH: AnimalsMESH: ProteinsPeptide sequenceMESH: Crystallizationchemistry.chemical_classification0303 health sciencesCaspartinbiologyMESH : Amino Acid SequenceMESH : Pepsin AMESH: Models ChemicalImmunogold labellingImmunohistochemistryMESH: MolluscaMESH : Sequence Homology Amino AcidAmino acidBiochemistryMESH: Calcium CarbonateMechanics of MaterialsMESH : CrystallizationMESH: Pepsin ASEMMESH : Edetic AcidCrystallizationMESH : MolluscaCalcium carbonateProteinaceous extracellular matrixMESH: Edetic AcidMolecular Sequence DataBiophysicsBioengineering010402 general chemistryBiomaterials03 medical and health sciencesAnimalsAmino Acid Sequence[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsEdetic Acid030304 developmental biologyAspartic AcidViral matrix proteinMESH: Molecular Sequence DataSequence Homology Amino AcidMESH : SolubilityBack-scattered electronsSurface treatmenProteinsMESH: ImmunohistochemistryIR-78873[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsPepsin A0104 chemical sciences[SDV.IB.BIO] Life Sciences [q-bio]/Bioengineering/BiomaterialsMESH: SolubilityCalcium carbonatechemistryModels ChemicalSolubilityPolyclonal antibodiesMolluscaCeramics and Compositesbiology.proteinMESH : AnimalsMESH : TrypsinImmunogold
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First case in Italy of acquired resistance to oseltamivir in an immunocompromised patient with influenza A/H1N1v infection

2010

A pandemic influenza A/H1N1v strain with the neuraminidase H274Y mutation was detected in nasal secretions of a 2-year-old leukemic patient with influenza-like illness after 18 days of treatment with oseltamivir. At baseline, no drug-resistant virus was found, while 4 days after treatment initiation a mix- ture of wild-type and mutated virus was detected. After treatment interruption, the wild type influenza virus re-emerged and became prevalent in nasal secretions after a few days, suggesting the lower fitness of the mutated virus strain. The patient slowly improved concurrently with a decrease in virus load, which resulted negative 42 days after diagnosis. No other drug-resistant influenz…

Bodily SecretionsvirusesResistanceDrug ResistanceSettore MED/42 - Igiene Generale E Applicatamedicine.disease_causePandemic H1N1v Oseltamivir Resistancechemistry.chemical_compoundInfluenza A Virus H1N1 SubtypePandemicInfluenza A virusInfluenza A VirusViralChildViral LoadTreatment OutcomeInfectious DiseasesItalyChild PreschoolRNA ViralFemaleViral diseaseViral loadH1N1vSequence AnalysisH1N1v; Oseltamivir; Pandemic; Resistance; Amino Acid Substitution; Antiviral Agents; Bodily Secretions; Child Preschool; Female; Humans; Immunocompromised Host; Influenza A Virus H1N1 Subtype; Influenza Human; Italy; Molecular Sequence Data; Mutation Missense; Neuraminidase; Nose; Oseltamivir; RNA Viral; Sequence Analysis DNA; Treatment Outcome; Viral Load; Viral Proteins; Withholding Treatment; Drug Resistance Viral; Virology; Infectious DiseasesHumanOseltamivirMolecular Sequence DataMutation MissenseNeuraminidaseBiologyNoseAntiviral AgentsVirusresistanceImmunocompromised HostViral ProteinsOseltamivirVirologyDrug Resistance ViralInfluenza HumanmedicineHumansH1N1 SubtypePreschoolInfluenza-like illnessPandemicSequence Analysis DNADNAVirologyInfluenzaInfluenza; A/H1N1v; Oseltamivir; resistancechemistryAmino Acid SubstitutionWithholding TreatmentMutationbiology.proteinRNAA/H1N1vMissenseNeuraminidase
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