Search results for "sequence data"

showing 10 items of 1952 documents

Iron Induces Proliferation and Morphogenesis in Primmorphs from the Marine SpongeSuberites domuncula

2002

Dissociated cells from marine demosponges retain their proliferation capacity if they are allowed to form special aggregates, the primmorphs. On the basis of incorporation studies and septin gene expression, we show that Fe3+ ions are required for the proliferation of cells in primmorphs from Suberites domuncula. In parallel, Fe3+ induced the expression of ferritin and strongly stimulated the synthesis of spicules. This result is supported by the finding that the enzymatic activity of silicatein, converting organosilicon to silicic acid, depends on Fe3+. Moreover, the expression of a scavenger receptor molecule, possibly involved in the morphology of spicules, depends on the presence of Fe3…

inorganic chemicalsIronMolecular Sequence DataMorphogenesisFluorescent Antibody TechniqueSeptinModels BiologicalPolymerase Chain ReactionFungal ProteinsSponge spiculeGene expressionGeneticsAnimalsHistidineAmino Acid SequenceReceptors ImmunologicScavenger receptorMolecular BiologyPhylogenyReceptors LipoproteinReceptors ScavengerSequence Homology Amino AcidbiologyEcologySilicatesMembrane ProteinsDNACell BiologyGeneral MedicineScavenger Receptors Class BBlotting Northernbiology.organism_classificationCathepsinsRecombinant ProteinsPoriferaCell biologySuberites domunculaFerritinSpongeFerritinsbiology.proteinCell DivisionDNA and Cell Biology
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The fnr Gene of Bacillus licheniformis and the Cysteine Ligands of the C-Terminal FeS Cluster

1998

Many of the O2-responsive gene regulators of bacteria are members of the fumarate nitrate reductase-cyclic AMP receptor protein family of transcriptional regulators (12, 13, 15, 17) with predicted structures similar to those of the cyclic AMP receptor protein (11). The Fnr (stands for fumarate nitrate reductase regulator) protein from Escherichia coli (FnrEc) controls the expression of a variety of genes, mainly of anaerobic respiration and metabolism (5, 13). It contains a N-terminal cluster of three essential cysteine residues which are supposed to bind together with Cys122 a [4Fe 4S]2+ cluster which is required for O2 sensing (4, 7, 8, 10, 16). A wide variety of gram-negative bacteria co…

inorganic chemicalsIron-Sulfur ProteinsMolecular Sequence DataRestriction MappingMutantBacillusGenetics and Molecular BiologySequence alignmentmacromolecular substancesBacillus subtilisLigandsNitrate reductaseenvironment and public healthMicrobiologyBacterial ProteinsAmino Acid SequenceCysteineBacillus licheniformisMolecular BiologyPeptide sequenceBacillus megateriumSequence Homology Amino AcidbiologyEscherichia coli ProteinsGene Expression Regulation Bacterialbiology.organism_classificationenzymes and coenzymes (carbohydrates)KineticsBiochemistryBacillus megateriumbacteriaSequence AlignmentBacillus subtilisTranscription FactorsCysteineJournal of Bacteriology
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Truncated recombinant light harvesting complex II proteins are substrates for a protein kinase associated with photosystem II core complexes

1998

AbstractPrevious studies directed towards understanding phosphorylation of the chlorophyll a/b binding proteins comprising light harvesting complex II (LHC II) have concentrated on a single phosphorylation site located close to the N-terminus of the mature proteins. Here we show that a series of recombinant pea Lhcb1 proteins, each missing an N-terminal segment including this site, are nevertheless phosphorylated by a protein kinase associated with a photosystem II core complex preparation. An Lhcb1 protein missing the first 58 amino acid residues is not, however, phosphorylated. The results demonstrate that the LHC II proteins are phosphorylated at one or more sites, the implications of wh…

inorganic chemicalsPhotosystem IIMacromolecular SubstancesMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiophysicsmacromolecular substancesBiologyBiochemistryDNA-binding proteinProtein kinaseThylakoid membraneSubstrate Specificitylaw.inventionStructural BiologylawGeneticsProtein phosphorylationAmino Acid SequencePhosphorylationProtein kinase AMolecular BiologyPlant ProteinsKinasePeasPeaPhotosystem II Protein Complexfood and beveragesCell BiologySpinachPeptide FragmentsRecombinant Proteinsenzymes and coenzymes (carbohydrates)BiochemistryThylakoidRecombinant DNALight harvesting proteinPhosphorylationbacteriaCarrier ProteinsProtein KinasesFEBS Letters
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Receptor-mediated uptake of boron-rich neuropeptide y analogues for boron neutron capture therapy.

2014

Peptidic ligands selectively targeting distinct G protein-coupled receptors that are highly expressed in tumor tissue represent a promising approach in drug delivery. Receptor-preferring analogues of neuropeptide Y (NPY) bind and activate the human Y1 receptor subtype (hY1 receptor), which is found in 90% of breast cancer tissue and in all breast-cancer-derived metastases. Herein, novel highly boron-loaded Y1 -receptor-preferring peptide analogues are described as smart shuttle systems for carbaboranes as (10) B-containing moieties. Various positions in the peptide were screened for their susceptibility to carbaborane modification, and the most promising positions were chosen to create a mu…

inorganic chemicalsStereochemistrymedia_common.quotation_subjectMolecular Sequence Datachemistry.chemical_elementPeptideBoron Neutron Capture TherapyBreast NeoplasmsBiochemistrySolid-phase synthesisDrug DiscoveryChlorocebus aethiopsAnimalsHumansNeuropeptide YAmino Acid SequenceGeneral Pharmacology Toxicology and PharmaceuticsReceptorInternalizationBoronBoranesmedia_commonPharmacologychemistry.chemical_classificationChemistryOrganic ChemistryReceptor-mediated endocytosisNeuropeptide Y receptorReceptors Neuropeptide YHEK293 CellsDrug deliveryCOS CellsMolecular MedicineFemaleChemMedChem
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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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The transcriptome analysis of Strongyloides stercoralis L3i larvae reveals targets for intervention in a neglected disease.

2012

Background: Strongyloidiasis is one of the most neglected diseases distributed worldwide with endemic areas in developed countries, where chronic infections are life threatening. Despite its impact, very little is known about the molecular biology of the parasite involved and its interplay with its hosts. Next generation sequencing technologies now provide unique opportunities to rapidly address these questions. Principal Findings: Here we present the first transcriptome of the third larval stage of S. stercoralis using 454 sequencing coupled with semi-automated bioinformatic analyses. 253,266 raw sequence reads were assembled into 11,250 contiguous sequences, most of which were novel. 8037…

lcsh:Arctic medicine. Tropical medicineSequence analysisHaemonchus-contortuslcsh:RC955-962Molecular Sequence DataComputational biologyBiologyBioinformaticsDNA sequencingStrongyloides stercoralisTranscriptomeParasitic DiseasesmedicineAnimalsHumansDictyocaulus-viviparusGene Expression Profilinglcsh:Public aspects of medicinePublic Health Environmental and Occupational HealthNeglected DiseasesFunctional genomicslcsh:RA1-1270Sequence Analysis DNADNA Protozoanmedicine.diseasebiology.organism_classificationGene expression profilingInfectious DiseasesStrongyloidiasisLarvaHost-Pathogen InteractionsStrongyloidesStrongyloidiasisMedicineHelminth-parasitesStrongyloides stercoralisFunctional genomicsResearch ArticleNeglected Tropical DiseasesPLoS Neglected Tropical Diseases
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Solving a Bloody Mess: B-Vitamin Independent Metabolic Convergence among Gammaproteobacterial Obligate Endosymbionts from Blood-Feeding Arthropods an…

2015

Endosymbiosis is a common phenomenon in nature, especially between bacteria and insects, whose typically unbalanced diets are usually complemented by their obligate endosymbionts. While much interest and focus has been directed toward phloem-feeders like aphids and mealybugs, blood-feeders such as the Lone star tick (Amblyomma americanum), Glossina flies, and the human body louse (Pediculus humanus corporis) depend on obligate endosymbionts which complement their B-vitamin-deficient diets, and thus are required for growth and survival. Glossiphoniid leeches have also been found to harbor distinct endosymbionts housed in specialized organs. Here, we present the genome of the bacterial endosy…

leech endosymbiontDNA BacterialMolecular Sequence DataZoologyblood-feederProvidenciaBiologyProvidencia siddalliiAmblyomma americanum03 medical and health sciencesSymbiosisLeechesRNA Ribosomal 16SBotanyGammaproteobacteriaGeneticsAnimalsHumansgenome reductionSymbiosisEcology Evolution Behavior and SystematicsPhylogeny030304 developmental biology2. Zero hunger0303 health sciencesEndosymbiosisObligate030306 microbiologyHost (biology)DipterafungiVitaminsbiochemical phenomena metabolism and nutritionbiology.organism_classificationB vitaminsCandidatusB-vitaminbacteriaHaementeria officinalisGammaproteobacteriaGenome BacterialResearch ArticleGenome Biology and Evolution
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Combining Sequence Analysis and Hidden Markov Models in the Analysis of Complex Life Sequence Data

2018

Life course data often consists of multiple parallel sequences, one for each life domain of interest. Multichannel sequence analysis has been used for computing pairwise dissimilarities and finding clusters in this type of multichannel (or multidimensional) sequence data. Describing and visualizing such data is, however, often challenging. We propose an approach for compressing, interpreting, and visualizing the information within multichannel sequences by finding (1) groups of similar trajectories and (2) similar phases within trajectories belonging to the same group. For these tasks we combine multichannel sequence analysis and hidden Markov modelling. We illustrate this approach with an …

longitudinal datasekvensointisequence analysisSequence analysisComputer scienceMarkovin ketjutMarkov modelspitkittäistutkimuselämänkaari01 natural sciences010104 statistics & probability03 medical and health sciencesData sequencespopulation dynamicsSannolikhetsteori och statistik0101 mathematicsfamily and work trajectoriesProbability Theory and StatisticsHidden Markov modellife course030505 public healthhidden Markov modelslatent Markov modelsbusiness.industryPattern recognitionTvärvetenskapliga studier inom samhällsvetenskaplife sequence dataLife domainLife course approachPairwise comparisonArtificial intelligenceSocial Sciences Interdisciplinary0305 other medical sciencebusinessväestötilastot
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Molecular cloning and characterization of the complementary DNA coding for the B-chain of murine Clq

1989

AbstractcDNA clones coding for the B-chain of murine Clq were isolated from a mouse macrophage library. The characterized clones include the total coding region plus a leader sequence. High homology was found with human Clq B-chain in the coding region (81%). Northern blot analysis of total RNA from different tissues of Balb/c mice showed one band of approximately 1.2 kb. The highest signal was found in RNA preparations of thioglycolate-activated peritoneal macrophages. The probe also hybridized with mRNA from spleen, thymus and heart. Extremely weak signals were found in liver, kidney, lung and intestine tissues.

mRNAMolecular Sequence DataBiophysicsProtein Sorting SignalsMolecular cloningBiologyBiochemistryMiceStructural BiologySequence Homology Nucleic AcidComplementary DNAGeneticsAnimalsHumansCoding regionGenomic libraryRNA MessengerNorthern blotCloning MolecularPromoter Regions GeneticMolecular BiologyGeneMice Inbred BALB CMessenger RNAComplement C1qNucleic Acid HybridizationRNADNARNA ProbesCell BiologyBlotting NorthernMolecular biologyClqNucleotide sequenceCloningFEBS Letters
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Dissimilar Regulation of Antimicrobial Proteins in the Midgut of Spodoptera exigua Larvae Challenged with Bacillus thuringiensis Toxins or Baculoviru…

2015

Antimicrobial peptides (AMPs) and lysozymes are the main effectors of the insect immune system, and they are involved in both local and systemic responses. Among local responses, midgut immune reaction plays an important role in fighting pathogens that reach the insect body through the oral route, as do many microorganisms used in pest control. Under this point of view, understanding how insects defend themselves locally during the first phases of infections caused by food-borne pathogens is important to further improve microbial control strategies. In the present study, we analyzed the transcriptional response of AMPs and lysozymes in the midgut of Spodoptera exigua (Lepidoptera: Noctuidae…

media_common.quotation_subjectAntimicrobial peptidesMolecular Sequence DataBacillus thuringiensislcsh:MedicineInsectSpodopteraSpodopteraMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisExiguaHemolymphAnimalsAmino Acid SequencePest Control Biologicallcsh:SciencePhylogenymedia_commonMultidisciplinarybiologyBacillus thuringiensis ToxinsSequence Homology Amino AcidMonophenol Monooxygenasefungilcsh:RMidgutbiology.organism_classificationEndotoxinsSettore AGR/11 - ENTOMOLOGIA GENERALE E APPLICATALarvaNoctuidaeInsect ProteinsMuramidaselcsh:QBaculoviridaeDigestive SystemAntimicrobial Cationic PeptidesResearch ArticlePLoS ONE
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