Search results for "Molecular sequence"

showing 10 items of 1972 documents

Gypsy homologous sequences in Drosophila subobscura (gypsyDS).

1993

Characterization of sequences homologous to the Drosophila melanogaster gypsy transposable element was carried out in Drosophila subobscura (gypsyDS). They were found to be widely distributed among natural populations of this species. From Southern blot and in situ analyses, these sequences appear to be mobile in this species. GypsyDS sequences are located in both euchromatic and heterochromatic regions. A complete gypsyDS sequence was isolated from a D. subobscura genomic library, and a 1.3-kb fragment which aligns with the ORF2 of the D. melanogaster gypsy element was sequenced. Comparisons of this sequence in three species (D. subobscura, D. melanogaster, and D. virilis) indicate that th…

HeterochromatinMolecular Sequence DataTransfectionHomology (biology)Species SpecificityMolecular evolutionDrosophilidaeSequence Homology Nucleic AcidGeneticsMelanogasterAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyEcology Evolution Behavior and SystematicsSouthern blotGeneticsbiologyBase SequenceSequence Homology Amino AcidNucleic acid sequenceChromosome MappingDNAbiology.organism_classificationBiological EvolutionDrosophila subobscuraDrosophila melanogasterDNA Transposable ElementsDrosophilaJournal of molecular evolution
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RCS1, a gene involved in controlling cell size inSaccharomyces cerevisiae

1991

Cloning and sequencing of RCS1, Saccharomyces cerevisiae gene whose product seems to be involved in timing the budding event of the cell cycle, is described. A haploid strain in which the 3'-terminal region of the chromosomal copy of the gene has been disrupted produces cells that are, on average, twice the size of cells of the parental strain. The critical size for budding in the mutant is similarly increased, and the disruption mutation is dominant in a diploid heterozygous for the RCS1 gene. Spores from this diploid have a reduced ability to germinate, the effect being more pronounced in the spores carrying the disrupted copy of RCS1. However, disrupted cells recover from alpha-factor tr…

HeterozygoteMolecular Sequence DataSaccharomyces cerevisiaeMutantBioengineeringSaccharomyces cerevisiaemedicine.disease_causeApplied Microbiology and BiotechnologyBiochemistryGeneticsSpore germinationmedicineAmino Acid SequenceCloning MolecularDNA FungalGeneGene LibraryGeneticsBuddingMutationMembrane GlycoproteinsBase SequencebiologyCell CyclefungiSpores Fungalbiology.organism_classificationYeastMutationPloidyPlasmidsBiotechnologyYeast
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Intraspecific and within-isolate sequence variation in the ITS rRNA gene region of Pythium mercuriale sp. nov. (Pythiaceae)

2008

Belbahri, Lassaad et al.

HeterozygoteNuclear geneGenotypeMolecular Sequence DataPythiumBiologyDNA RibosomalMicrobiologyDNA AlgalPeptide Elongation Factor 1Intergenic regionTubulinPhylogeneticsDNA Ribosomal SpacerGeneticsCluster AnalysisPythiumInternal transcribed spacerMolecular BiologyAllelesPhylogenyGeneticsPolymorphism GeneticPhylogenetic treeAlgal ProteinsGenes rRNASequence Analysis DNARibosomal RNAbiology.organism_classificationPythiaceaePhenotype
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Mutations in LMX1B cause abnormal skeletal patterning and renal dysplasia in nail patella syndrome

1998

The LIM-homeodomain protein Lmxlb plays a central role in dorso-ventral patterning of the vertebrate limb1. Targeted disruption of Lmxlb results in skeletal defects including hypoplas-tic nails, absent patellae and a unique form of renal dysplasia (see accompanying manuscript by H. Chen et al.; ref. 2). These features are reminiscent of the dominantly inherited skeletal malformation nail patella syndrome (NFS). We show that LMX1B maps to the NFS locus and that three independent NFS patients carry de novo heterozygous mutations in this gene. Functional studies show that one of these mutations disrupts sequence-specific DNA binding, while the other two mutations result in premature terminatio…

HeterozygotePathologymedicine.medical_specialtyLIM-Homeodomain ProteinsMolecular Sequence DataLocus (genetics)BiologyKidneyBone and BonesMiceGene mappingNail-Patella SyndromeGeneticsmedicineAnimalsHumansAmino Acid SequenceGeneBody PatterningNail patella syndromeHomeodomain ProteinsGeneticsBase SequenceDysostosismedicine.diseasePhenotypeRenal dysplasiaMutationHomeotic geneTranscription FactorsNature Genetics
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Mapping the cell binding site on high molecular weight kininogen domain 5.

1995

Investigations mapped the region(s) on the light chain of high molecular weight kininogen (HK) that participates in cell binding. Sequential and overlapping peptides of domain 5 (D5H) were synthesized to determine its cell binding site(s). Three peptides from non-overlapping regions on D5H were found to inhibit biotin-HK binding to endothelial cells. Peptides GKE19 and HNL 21 weakly inhibited biotin-HK binding with IC50 of 792 and 215 microM, respectively. Peptide HKH20 inhibited biotin-HK binding with an IC50 of 0.2 microM. Two peptides, GGH18 and HVL24, which overlapped HKH20, also inhibited biotin-HK binding to endothelial cells with IC50 values of 108 and 0.8 microM, respectively. Bioti…

High-molecular-weight kininogenMolecular Sequence DataBiotinPeptideBiochemistryHumansAmino Acid SequenceBinding siteMolecular BiologyCells Culturedchemistry.chemical_classificationKininogenBinding SitesbiologyCoagulantsKininogensCell BiologyMolecular biologyPeptide FragmentsMolecular WeightEnzymechemistryPolyclonal antibodiesBiotinylationbiology.proteinEndothelium VascularAntibodyProtein BindingThe Journal of biological chemistry
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Evolutionary history of the OmpR/IIIA family of signal transduction two component systems in Lactobacillaceae and Leuconostocaceae

2011

15 pages, 3 tables, 7 figures.

Histidine KinaseEvolutionMolecular Sequence DataSignal transductionEvolution MolecularBacterial ProteinsPhylogeneticsQH359-425Lactic acid bacteriaAmino Acid SequenceGeneEcology Evolution Behavior and SystematicsPhylogenyGeneticsTwo component systemLeuconostocaceaebiologyPhylogenetic treeLactobacillalesfungiLactobacillaceaebiology.organism_classificationTwo-component regulatory systemResponse regulatorLactobacillaceaeMultigene FamilyLeuconostocaceaeProtein KinasesSequence AlignmentOmpR/IIIA familyResearch Article
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Evolution of tissue-specific keratins as deduced from novel cDNA sequences of the lungfish Protopterus aethiopicus.

2005

Lungfishes are possibly the closest extant relatives of the land vertebrates (tetrapods). We report here the cDNA and predicted amino acid sequences of 13 different keratins (ten type I and three type II) of the lungfish Protopterus aethiopicus. These keratins include the orthologs of human K8 and K18. The lungfish keratins were also identified in tissue extracts using two-dimensional polyacrylamide gel electrophoresis, keratin blot binding assays and immunoblotting. The identified keratin spots were analyzed by peptide mass fingerprinting which assigned seven sequences (inclusively Protopterus K8 and K18) to their respective protein spot. The peptide mass fingerprints also revealed the fac…

HistologyDNA ComplementaryMolecular Sequence DataFluorescent Antibody Techniquemacromolecular substancesPeptide MappingPathology and Forensic MedicineEvolution MolecularPeptide mass fingerprintingComplementary DNAKeratinAnimalsElectrophoresis Gel Two-DimensionalAmino Acid SequencePolyacrylamide gel electrophoresisLungfishchemistry.chemical_classificationProtopterusintegumentary systembiologyPhylogenetic treeLampreyFishesCell BiologyGeneral MedicineAnatomybiology.organism_classificationchemistryEvolutionary biologySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationKeratinsEuropean journal of cell biology
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Tracing keratin evolution: catalog, expression patterns and primary structure of shark (Scyliorhinus stellaris) keratins.

1998

We have studied individual keratins of an elasmobranch, the shark Scyliorhinus stellaris (the lesser-spotted dogfish). From various shark tissues, notably skin and stomach, cytoskeletal proteins were isolated and then separated by two-dimensional polyacrylamide gel electrophoresis. Using complementary keratin blot-binding assays and immunoblotting, among these proteins we identified a variety of type I and type II keratins. According to their tissue-specific expression, we distinguished Is and IIs keratins from IE and IIE keratins ("S" and "E" from "simple epithelial" and "epidermal", respectively). Guinea pig antibodies which in immunoblots specifically labeled the entire range of identifi…

HistologyDNA ComplementaryMolecular Sequence Datamacromolecular substancesPathology and Forensic MedicineKeratinAnimalsHumansAmino Acid SequenceIntermediate filamentPolyacrylamide gel electrophoresisPeptide sequencechemistry.chemical_classificationintegumentary systemPhylogenetic treebiologyBase SequenceProtein primary structureCell BiologyGeneral MedicineKeratin 6Abiology.organism_classificationMolecular biologyBiological EvolutionchemistryMicroscopy FluorescenceSharksKeratinshuman activitiesScyliorhinus stellarisEuropean journal of cell biology
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Sequence, evolution and tissue expression patterns of an epidermal type I keratin from the shark Scyliorhinus stellaris.

2004

From the shark Scyliorhinus stellaris we cloned and sequenced a cDNA encoding a novel type I keratin, termed SstK10. By MALDI-MS peptide mass fingerprinting of cytoskeletal proteins separated on polyacrylamide gels, we assigned SstK10 to a 46-kDa protein which is the major epidermal type I (“IE”) keratin in this fish and is specifically expressed in stratified epithelia. In a phylogenetic tree based on type I keratin sequences and with lamprey keratins applied as outgroup, SstK10 branches off in a rather basal position. This tree strongly supports the concept that teleost keratins and tetrapod keratins resulted from two independent gene radiation processes. The only exception is human K18 b…

HistologyDNA ComplementaryType I keratinMolecular Sequence Datamacromolecular substancesMass SpectrometryPathology and Forensic MedicineSequence Analysis Proteinbiology.animalKeratinAnimalsAmino Acid SequenceCloning MolecularPhylogenychemistry.chemical_classificationintegumentary systemPhylogenetic treebiologyLampreyVertebrateCell BiologyGeneral MedicineGnathostomataKeratin 6AAnatomybiology.organism_classificationImmunohistochemistryCell biologychemistryEpidermal CellsGene Expression RegulationOrgan SpecificitySharksKeratinsElectrophoresis Polyacrylamide GelEpidermisScyliorhinus stellarisEuropean journal of cell biology
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Origin of neuronal-like receptors in Metazoa: cloning of a metabotropic glutamate/GABA-like receptor from the marine sponge Geodia cydonium.

1999

To date, no conclusive evidence has been presented for the existence of neuronal-like elements in Porifera (sponges). In the present study, isolated cells from the marine sponge Geodia cydonium are shown to react to the excitatory amino acid glutamate with an increase in the concentration of intracellular calcium [Ca2+]i. This effect can also be observed when the compounds L-quisqualic acid (L-QA) or L-(+)-2-amino-4-phosphonobutyric acid (L-AP-4) are used. The effect of L-QA and L-AP-4, both agonists for metabotropic glutamate receptors (mGluRs), can be abolished by the antagonist of group I mGluRs, (RS)-alpha-methyl-4-carboxyphenylglycine. These data suggest that sponge cells contain an mG…

HistologyMolecular Sequence DataGlutamic AcidClass C GPCRBiologyReceptors Metabotropic GlutamatePathology and Forensic MedicineMiceReceptors GABAAnimalsAmino Acid SequenceCloning MolecularSequence Homology Amino AcidMetabotropic glutamate receptor 4Metabotropic glutamate receptor 7Metabotropic glutamate receptor 6Cell BiologyRecombinant ProteinsPoriferaRatsKineticsDrosophila melanogasternervous systemBiochemistryMetabotropic glutamate receptorMetabotropic glutamate receptor 1CalciumMetabotropic glutamate receptor 3Metabotropic glutamate receptor 2Excitatory Amino Acid AntagonistsSequence AlignmentCell and tissue research
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