Search results for "Base Sequence"

showing 10 items of 1146 documents

Human Endometrial Side Population Cells Exhibit Genotypic, Phenotypic and Functional Features of Somatic Stem Cells

2010

During reproductive life, the human endometrium undergoes around 480 cycles of growth, breakdown and regeneration should pregnancy not be achieved. This outstanding regenerative capacity is the basis for women's cycling and its dysfunction may be involved in the etiology of pathological disorders. Therefore, the human endometrial tissue must rely on a remarkable endometrial somatic stem cells (SSC) population. Here we explore the hypothesis that human endometrial side population (SP) cells correspond to somatic stem cells. We isolated, identified and characterized the SP corresponding to the stromal and epithelial compartments using endometrial SP genes signature, immunophenotyping and char…

Pathologymedicine.medical_specialtyStromal cellGenotypeCellular differentiationSciencePopulationTransplantation HeterologousMice SCIDBiologyEndometriumPolymerase Chain ReactionMolecular Biology/BioinformaticsImmunophenotypingEndometriumMiceImmunophenotypingSide populationCell Biology/Membranes and SortingMice Inbred NODmedicineAnimalsHumanseducationMolecular BiologyCell Biology/Gene Expressioneducation.field_of_studyMultidisciplinaryBase SequenceStem CellsQRCell DifferentiationCell BiologyCell biologyObstetricsmedicine.anatomical_structureWomen's HealthMedicineFemaleStem cellAdult stem cellResearch Article
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The analysis of modified peroxisome proliferator responsive elements of the peroxisomal bifunctional enzyme in transfected HepG2 cells reveals two re…

1995

AbstractPeroxisome proliferators (PPs) are non-genotoxic carcinogens in rodents. They can induce the expression of numerous genes via the heterodimerization of two members of the steroid hormone receptor superfamily, called the peroxisome proliferator-activated receptor (PPAR) and the 9-cis retinoic acid receptor (RXR). Many of the PP responsive genes possess a peroxisome proliferator response element (PPRE) formed by two TGACCT-related motifs. The bifunctional enzyme (HD) PPRE contains 3 such motifs, creating DR1 and DR2 sequences. PPAR and RXR regulate transcription via the DR1 element while DR2 modulates the expression of the gene via auxiliary factors in HepG2 cells.

Peroxisome proliferator-activated receptor gammaReceptors Retinoic AcidSteroid hormone receptorMolecular Sequence DataResponse elementBiophysicsReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorchemical and pharmacologic phenomenaIn Vitro TechniquesRegulatory Sequences Nucleic AcidRetinoid X receptorBiologyPeroxisomal Bifunctional EnzymeTransfectionMicrobodiesBiochemistryGene Expression Regulation EnzymologicTranscriptional activationPeroxisomal Bifunctional EnzymeMultienzyme ComplexesStructural BiologyPeroxisome proliferator response element9-cis Retinoic acid receptor alphaTumor Cells CulturedGeneticsHumansRNA MessengerIsomerasesEnoyl-CoA HydrataseMolecular Biologychemistry.chemical_classificationBinding SitesBase Sequence3-Hydroxyacyl CoA DehydrogenasesPeroxisome proliferator-activated receptorCell BiologyDNA-Binding ProteinsRetinoic acid receptorRetinoid X ReceptorsLiverOligodeoxyribonucleotidesBiochemistrychemistryRat peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenaseEnzyme InductionPeroxisome proliferator-activated receptor alphaTranscription FactorsFEBS Letters
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The main determinant of furosemide inhibition on GABA(A) receptors is located close to the first transmembrane domain.

1998

Inhibitory GABA(A) receptors are regulated by numerous allosteric modulators, the most receptor-subtype specific of which is furosemide. It recognises receptors of the subunit composition alpha6beta2/3gamma2, restricted to cerebellar granule cells. To locate furosemide's site of action we constructed chimeras of the furosemide-sensitive alpha6 and the furosemide-insensitive alpha1 subunit, and expressed and studied them together with the beta3 and gamma2 subunits in Xenopus oocytes by the two-electrode voltage clamp technique. The inhibition of GABA-induced currents by furosemide mainly depended on a short domain proximal to the first transmembrane region of the alpha6 subunit.

PharmacologyBase SequenceGABAA receptorVoltage clampProtein subunitXenopusAllosteric regulationCell MembraneMolecular Sequence DataXenopusBiologyIn Vitro Techniquesbiology.organism_classificationGABAA-rho receptorCell biologyGABA AntagonistsTransmembrane domainBiochemistryAllosteric RegulationFurosemideOocytesAnimalsGABA-A Receptor AntagonistsReceptorEuropean journal of pharmacology
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Structure of the phenylalanine hydroxylase gene in Drosophila melanogaster and evidence of alternative promoter usage.

1996

The complete Drosophila melanogaster phenylalanine hydroxylase gene isolated from a genomic library was sequenced. Gene structure consisted of five exons covering a region of around 3 kb. Position of introns in the C-terminal domain was conserved with mammalian aromatic amino acid hydroxylase genes. Putative promoter sequences in the 5'UTR and intron 1 were identified. A novel transcript was detected differing from that previously reported by the inclusion of a part of the intron 1 sequence. It could be produced using an alternative promoter. The deduced open reading frame would code a protein with a small difference at the N-terminus. Expression of the alternative transcripts was examined …

Phenylalanine hydroxylaseTranscription GeneticMolecular Sequence DataBiophysicsGenes InsectBiochemistryPolymerase Chain ReactionExonchemistry.chemical_compoundAromatic amino acidsAnimalsGenomic libraryAmino Acid SequenceRNA MessengerPromoter Regions GeneticMolecular BiologyGeneDNA PrimersGeneticsGenomic LibrarybiologyBase SequenceIntronPhenylalanine HydroxylaseCell BiologyExonsbiology.organism_classificationMolecular biologyIntronsOpen reading frameDrosophila melanogasterchemistrybiology.proteinDrosophila melanogasterBiochemical and biophysical research communications
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Polyphasic taxonomy of a novel yeast isolated from antarctic environment; description of Cryptococcus victoriae sp. nov.

1999

In 1992 some samples of mosses, lichens and soils were collected from Botany Bay, Southern Victoria Land (77 degrees 01' S 162 degrees 32' E) and, as a result of a routine screening programme some yeasts were isolated. One of them, designated as strain G5, showed marked differences when compared to other antarctic yeasts. According to morphological and physiological characteristics, we were able to identify the strain G5 as a yeast belonging to the genus Cryptococcus. Some characteristics of this genus are the growth response to myo-inositol, celobiose, raffinose and D-glucuronate, no-fermentation, the absence of mycelium and pseudomycelium, asexual reproduction, Diazolium blue B test (DBB)…

Phylogenetic treeBase SequenceMolecular Sequence DataFungi imperfectiRibosomal RNABiologybiology.organism_classificationApplied Microbiology and BiotechnologyMicrobiologyPolymerase Chain ReactionYeastCryptococcusPhenotypePhylogeneticsBotanyTaxonomy (biology)LichenDNA FungalEcology Evolution Behavior and SystematicsMyceliumPolymorphism Restriction Fragment LengthSystematic and applied microbiology
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Complete Genome Sequence of Acidaminococcus intestini RYC-MR95, a Gram-Negative Bacterium from the Phylum Firmicutes

2011

ABSTRACT Acidaminococcus intestini belongs to the family Acidaminococcaceae , order Selenomonadales , class Negativicutes , phylum Firmicutes . Negativicutes show the double-membrane system of Gram-negative bacteria, although their chromosomal backbone is closely related to that of Gram-positive bacteria of the phylum Firmicutes . The complete genome of a clinical A. intestini strain is here presented.

Phylum FirmicutesMolecular Sequence DataVeillonellaceaeBiologyMicrobiologyGenomeMicrobiologyEvolution Molecular03 medical and health sciencesGram negative bacteriumHumansAcidaminococcusMolecular Biology030304 developmental biologyGeneticsWhole genome sequencing0303 health sciencesAcidaminococcus intestiniNegativicutesBase Sequence030306 microbiologybiology.organism_classificationGenome AnnouncementsGram-Negative Bacterial InfectionsGenome BacterialBacteriaJournal of Bacteriology
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Functioning of DcuC as the C 4 -Dicarboxylate Carrier during Glucose Fermentation by Escherichia coli

1999

ABSTRACT The dcuC gene of Escherichia coli encodes an alternative C 4 -dicarboxylate carrier (DcuC) with low transport activity. The expression of dcuC was investigated. dcuC was expressed only under anaerobic conditions; nitrate and fumarate caused slight repression and stimulation of expression, respectively. Anaerobic induction depended mainly on the transcriptional regulator FNR. Fumarate stimulation was independent of the fumarate response regulator DcuR. The expression of dcuC was not significantly inhibited by glucose, assigning a role to DcuC during glucose fermentation. The inactivation of dcuC increased fumarate-succinate exchange and fumarate uptake by DcuA and DcuB, suggesting a…

Physiology and MetabolismMolecular Sequence DataMutantStimulationBiologymedicine.disease_causeMicrobiologyBacterial ProteinsFumaratesConsensus SequenceEscherichia colimedicineTranscriptional regulationDicarboxylic AcidsAnaerobiosisPromoter Regions GeneticMolecular BiologyEscherichia coliPsychological repressionDicarboxylic Acid TransportersBinding SitesBase SequenceEscherichia coli ProteinsSuccinatesGene Expression Regulation BacterialKineticsResponse regulatorGlucoseBiochemistryFermentationFermentationEffluxCarrier ProteinsRibosomesJournal of Bacteriology
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F-type lectin from serum of the Antarctic teleost fish Trematomus bernacchii (Boulenger, 1902): Purification, structural characterization, and bacter…

2021

Abstract The increasing availability of sequenced genomes has enabled a deeper understanding of the complexity of fish lectin repertoires involved in early development and immune recognition. The teleost fucose-type lectin (FTL) family includes proteins that preferentially bind fucose and display tandemly arrayed carbohydrate-recognition domains (CRDs) or are found in mosaic combinations with other domains. They function as opsonins, promoting phagocytosis and the clearance of microbial pathogens. The Antarctic fish Trematomus bernacchii is a Perciforme living at extremely low temperatures (−1.68 °C) which is considered a model for studying adaptability to the variability of environmental w…

PhysiologyAntarctic fishLectins F-type lectin Antarctic fish Trematomus bernacchii Bacterial agglutinationAntarctic RegionsTrematomus bernacchiiBiochemistryAntarctic fish; Bacterial agglutination; F-type lectin; Lectins; Trematomus bernacchii; Amino Acid Sequence; Animals; Antarctic Regions; Bacteria; Base Sequence; Fucose; Lectins; Perciformes; PhylogenyFucose03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAffinity chromatographyWestern blotLectinsTrematomusmedicineAnimalsAmino Acid SequenceSea bassPerciformeMolecular BiologyOpsoninPhylogeny030304 developmental biologyFucoseAntarctic Region0303 health sciencesbiologyMolecular massmedicine.diagnostic_testBacteriaBase SequenceAnimalLectinBacterial agglutinationbiology.organism_classificationPerciformesBiochemistrychemistrybiology.proteinLectinF-type lectin030215 immunologyComparative biochemistry and physiology. Part B, Biochemistrymolecular biology
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Are elicitins cryptograms in plant-oomycete communications?

1999

Stimulation of plant natural defenses is an important challenge in phytoprotection prospects. In that context, elicitins, which are small proteins secreted by Phytophthora and Pythium species, have been shown to induce a hypersensitive-like reaction in tobacco plants. Moreover, these plants become resistant to their pathogens, and thus this interaction constitutes an excellent model to investigate the signaling pathways leading to plant resistance. However, most plants are not reactive to elicitins, although they possess the functional signaling pathways involved in tobacco responses to elicitin. The understanding of factors involved in this reactivity is needed to develop agronomic applica…

Phytophthora0106 biological sciences[SDV]Life Sciences [q-bio]Molecular Sequence DataMutagenesis (molecular biology technique)Context (language use)01 natural sciencesHost-Parasite InteractionsEvolution MolecularFungal Proteins03 medical and health sciencesCellular and Molecular NeuroscienceErgosterolGene Expression Regulation FungalTobaccoPlant defense against herbivoryAmino Acid SequenceMolecular BiologyPhylogenyComputingMilieux_MISCELLANEOUSPlant Diseases030304 developmental biologyPharmacologyOomycete0303 health sciencesBase SequencebiologyAlgal Proteinsfungifood and beveragesElicitinCell Biologybiology.organism_classification[SDV] Life Sciences [q-bio]Plants ToxicOomycetesBiochemistryMolecular MedicinePhytophthoraSequence AlignmentPlant lipid transfer proteinsFunction (biology)BiotechnologySignal Transduction010606 plant biology & botany
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Identification of a plasminogen-binding motif in PAM, a bacterial surface protein.

1995

Surface-associated plasmin(ogen) may contribute to the invasive properties of various cells. Analysis of plasmin(ogen)-binding surface proteins is therefore of interest. The N-terminal variable regions of M-like (ML) proteins from five different group A streptococcal serotypes (33, 41, 52, 53 and 56) exhibiting the plasminogen-binding phenotype were cloned and expressed in Escherichia coli. The recombinant proteins all bound plasminogen with high affinity. The binding involved the kringle domains of plasminogen and was blocked by a lysine analogue, 6-aminohexanoic acid, indicating that lysine residues in the M-like proteins participate in the interaction. Sequence analysis revealed that the…

PlasminStreptococcus pyogenesMolecular Sequence DataPlasma protein bindingBiologyMicrobiologyKringle domainBacterial ProteinsKringlesmedicineEscherichia coliAmino Acid SequenceBinding siteCloning MolecularMolecular BiologyPeptide sequenceBinding SitesBase SequenceLysinePlasminogenFusion proteinMolecular biologyRecombinant ProteinsPhenotypeBiochemistryCarrier ProteinsPlasminogen activatorSequence AlignmentBinding domainmedicine.drugProtein BindingMolecular microbiology
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