Search results for "Conserved sequence"

showing 10 items of 103 documents

Fast comparison of DNA sequences by oligonucleotide profiling

2008

Provisional abstact and full-text PDF files correspond to the article as it appeared upon acceptance. Fully formatted PDF and final abstract will be made available soon.

BioinformaticsFast speedADNOligonucleotide Profilinglcsh:MedicineGenomicsComputational biologyBiologyBioinformaticsGenomeGeneral Biochemistry Genetics and Molecular BiologyDNA sequencingConserved sequencechemistry.chemical_compoundTechnical NoteProfiling (information science)lcsh:Science (General)lcsh:QH301-705.5Medicine(all)OligonucleotideBiochemistry Genetics and Molecular Biology(all)lcsh:RGenomicsGeneral MedicineGenòmicaUVWORDchemistrylcsh:Biology (General)DNA sequence comparisonComputingMethodologies_DOCUMENTANDTEXTPROCESSINGDNAlcsh:Q1-390BMC Research Notes
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Production and characterisation of recombinant forms of human pulmonary surfactant protein C (SP-C):Structure and surface activity

2006

  Udgivelsesdato: 2006-Apr Surfactant protein C (SP-C) is an essential component for the surface tension-lowering activity of the pulmonary surfactant system. It contains a valine-rich alpha helix that spans the lipid bilayer, and is one of the most hydrophobic proteins known so far. SP-C is also an essential component of various surfactant preparations of animal origin currently used to treat neonatal respiratory distress syndrome (NRDS) in preterm infants. The limited supply of this material and the risk of transmission of infectious agents and immunological reactions have prompted the development of synthetic SP-C-derived peptides or recombinant humanized SP-C for inclusion in new prepar…

BioquímicaRecombinant membrain proteinSurface PropertiesSize-exclusion chromatographyMolecular Sequence DataPhospholipidBiophysicsBiologyBiochemistrylaw.inventionchemistry.chemical_compoundAffinity chromatographyPulmonary surfactantMembranes (Biologia)lawAnimalsHumansPulmonary surfactant-associated protein CAmino Acid SequenceLipid bilayerConserved SequencePhospholipidsMammalsDrug CarriersChromatographySequence Homology Amino AcidSP-CProteïnes de membranaSurfactant protein CPulmonary surfactantCell BiologyPulmonary Surfactant-Associated Protein CRecombinant ProteinsKineticschemistryBiochemistryRecombinant DNALipid-protein interactionPeptidesSequence Alignment
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A urochordate putative homolog of human EB1, the protein which binds APC1

1996

Abstract The human EB1 protein has been cloned by virtue of its interaction with the C-terminus of the APC (adenomatous polyposis coli) protein, whose C-terminal truncated forms have been shown to accompany sporadic and familial forms of colorectal cancer. We have cloned a putative EB1 homolog from Botryllus schlosseri (Urochordata, Ascidiacea). The deduced protein is 287 amino acids long, and is identical with 48% of the residues in human EB1 and 24–25% in two yeast hypothetical proteins. We propose that such a high degree of conservation among EB1 homologs is indicative of an essential regulatory mechanism in eukaryotic cells.

Cancer ResearchAdenomatous polyposis coliMolecular Sequence Datamacromolecular substancesBotryllus schlosseriPolymerase Chain ReactionHomology (biology)Conserved sequenceBacterial ProteinsComplementary DNAAnimalsHumansAmino Acid SequenceUrochordataGeneticschemistry.chemical_classificationBase SequencebiologyfungiNucleic acid sequenceProteinsSequence Analysis DNAbiology.organism_classificationYeastAmino acidOncologychemistrybiology.proteinSequence AlignmentCancer Letters
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Two Enhancers Control Transcription of Drosophila muscleblind in the Embryonic Somatic Musculature and in the Central Nervous System

2014

The phylogenetically conserved family of Muscleblind proteins are RNA-binding factors involved in a variety of gene expression processes including alternative splicing regulation, RNA stability and subcellular localization, and miRNA biogenesis, which typically contribute to cell-type specific differentiation. In humans, sequestration of Muscleblind-like proteins MBNL1 and MBNL2 has been implicated in degenerative disorders, particularly expansion diseases such as myotonic dystrophy type 1 and 2. Drosophila muscleblind was previously shown to be expressed in embryonic somatic and visceral muscle subtypes, and in the central nervous system, and to depend on Mef2 for transcriptional activatio…

Central Nervous SystemTranscription Geneticlcsh:MedicineEnhancer RNAsMechanical Treatment of SpecimensExonGenes ReporterMolecular Cell BiologyMorphogenesisPattern Formationlcsh:SciencePromoter Regions GeneticConserved SequenceGeneticsRegulation of gene expressionMultidisciplinaryMusclesDrosophila MelanogasterGene Expression Regulation DevelopmentalRNA-Binding ProteinsCell DifferentiationGenomicsAnimal ModelsInsectsEnhancer Elements GeneticElectroporationSpecimen DisruptionOrgan SpecificityRegulatory sequenceDrosophilaResearch ArticleMef2ArthropodaMolecular Sequence DataDNA transcriptionBiologyResearch and Analysis MethodsGenètica molecularModel OrganismsGeneticsAnimalsHumansEnhancerTranscription factorBase SequenceBiology and life scienceslcsh:ROrganismsPromoterCell BiologyInvertebratesSpecimen Preparation and Treatmentlcsh:QGene expressionAnimal GeneticsDevelopmental BiologyNeurosciencePLoS ONE
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RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin

2005

The ORF15 isoform of RPGR (RPGR(ORF15)) and RPGR interacting protein 1 (RPGRIP1) are mutated in a variety of retinal dystrophies but their functions are poorly understood. Here, we show that in cultured mammalian cells both RPGR(ORF15) and RPGRIP1 localize to centrioles. These localizations are resistant to the microtubule destabilizing drug nocodazole and persist throughout the cell cycle. RPGR and RPGRIP1 also co-localize at basal bodies in cells with primary cilia. The C-terminal (C2) domain of RPGR(ORF15) (ORF15(C2)) is highly conserved across 13 mammalian species, suggesting that it is a functionally important domain. Using matrix-assisted laser desorption ionization time-of-flight mas…

CentrioleFluorescent Antibody TechniqueMicechemistry.chemical_compoundChlorocebus aethiopsGuanine Nucleotide Exchange FactorsProtein IsoformsBasal bodyConserved SequenceGenetics (clinical)CentriolesGlutathione Transferaseintegumentary systemNuclear ProteinsExonsGeneral MedicineRetinitis pigmentosa GTPase regulatorImmunohistochemistryNocodazoleCOS CellsNucleophosminCell NucleolusRecombinant Fusion ProteinsMolecular Sequence DataBiologyOpen Reading FramesMicrotubuleTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceEye ProteinsMolecular BiologyNucleophosminSequence Homology Amino AcidProteinsPrecipitin TestsMolecular biologyeye diseasesProtein Structure TertiaryMice Inbred C57BLCytoskeletal ProteinschemistryCentrosomeCytoplasmSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMutationCattleHeLa CellsHuman Molecular Genetics
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The nucleosome remodeling factor ISWI functionally interacts with an evolutionarily conserved network of cellular factors

2010

Abstract ISWI is an evolutionarily conserved ATP-dependent chromatin remodeling factor playing central roles in DNA replication, RNA transcription, and chromosome organization. The variety of biological functions dependent on ISWI suggests that its activity could be highly regulated. Our group has previously isolated and characterized new cellular activities that positively regulate ISWI in Drosophila melanogaster. To identify factors that antagonize ISWI activity we developed a novel in vivo eye-based assay to screen for genetic suppressors of ISWI. Our screen revealed that ISWI interacts with an evolutionarily conserved network of cellular and nuclear factors that escaped previous genetic…

Chromatin Remodeling FactorInvestigationsBiologyEyemedicine.disease_causeConserved sequenceEvolution MolecularGeneticsmedicineAnimalsDrosophila ProteinsNucleosomeFluorometryGenetic TestingGenes SuppressorTranscription factorConserved SequenceAdenosine TriphosphatasesGeneticsMutationCell CycleDNA replicationbiology.organism_classificationNucleosomesChromatinDrosophila melanogasterPhenotypeMutationBiological AssayDrosophila melanogasterchromatin drosophila ISWIProtein BindingTranscription Factors
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Detailed characterization of human Mycobacterium tuberculosis specific HLA-E restricted CD8+T cells

2018

HLA-E presented antigens are interesting targets for vaccination given HLA-Es’ essentially monomorphic nature. We have shown previously that Mycobacterium tuberculosis (Mtb) peptides are presented by HLA-E to CD8+effector T cells, but the precise phenotype and functional capacity of these cells remains poorly characterized. We have developed and utilized in this study a new protocol combining HLA-E tetramer with intracellular staining for cytokines, transcription factors and cytotoxic molecules to characterize these cells in depth. We confirm in this study the significantly increased ex vivo frequency of Mtb-peptide/HLA-E-TM+CD8+T cells in the circulation of patients with active tubercu…

Cytotoxicity Immunologic0301 basic medicineTetramersImmunologyHuman leukocyte antigenCD8-Positive T-LymphocytesLymphocyte ActivationCD8+TÂ&nbspArticleImmunophenotypingMycobacterium tuberculosis03 medical and health sciencesTh2Th2 CellsAntigenHLA-A2 AntigenmedicineHumansTuberculosisCytotoxic T cellImmunology and AllergyGranulysinTuberculosis VaccinesCytokineCells CulturedConserved SequenceCell ProliferationAntigens BacterialbiologyLatent tuberculosisHistocompatibility Antigens Class IMycobacterium tuberculosisActive TBcellCD8(+) TcellsFlow Cytometrybiology.organism_classificationmedicine.disease3. Good health030104 developmental biologyPerforinImmunologybiology.proteinCytokinesPeptidesCD8Tetramer
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Clostridium difficile toxin A carries a C-terminal repetitive structure homologous to the carbohydrate binding region of streptococcal glycosyltransf…

1990

A detailed analysis of the 8130-bp open reading frame (ORF) of gene toxA and of an upstream ORF designated utxA, indicates the presence of a transcription terminator stem-loop for toxA, promoter sequences, and Shine-Dalgarno boxes for toxA and utxA. No transcription terminator between toxA and utxA is suggested by the sequence. ToxA contains two domains, one-third (C-terminal) with a repetitive structure and the residual two-thirds with no repetitions. The 2499-bp sequence encoding the repetitive structure is composed of nine groups of different short repetitive oligodeoxyribonucleotides (SRONs). A combination of these SRONs codes for five groups of combined repetitive oligopeptides (CROPs)…

DNA BacterialTranscription GeneticSequence analysisBacterial ToxinsMolecular Sequence DataRestriction MappingBiologyHomology (biology)Conserved sequenceEnterotoxinsOpen Reading FramesSequence Homology Nucleic AcidGeneticsAmino Acid SequencePeptide sequenceGeneRepetitive Sequences Nucleic AcidGeneticsBase SequenceNucleic acid sequenceStreptococcusGeneral MedicineMolecular biologyOpen reading frameTerminator (genetics)Genes BacterialGlucosyltransferasesGene
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Abscisic acid and desiccation-dependent expression of a novel putative SNF5-type chromatin-remodeling gene in Pisum sativum.

2006

Snf5-like proteins are components of multiprotein chromatin remodeling complexes involved in the ATP-dependent alteration of DNA-histone contacts. Mostly described in yeast and animals, the only plant SNF5-like gene characterized so far has been BSH from Arabidopsis thaliana (L.) Heynh. We report the cloning and characterization of expression of a SNF5-like gene from pea (Pisum sativum L. cv. Lincoln), which has been designated PsSNF5. Southern analysis showed a single copy of the gene in the pea genome. The cDNA contained a 723bp open reading frame encoding a 240 amino acid protein of 27.4kDa with a potential nuclear localization signal. PsSNF5 protein sequence closely resembled BSH, with …

DNA ComplementaryDNA PlantPhysiologyChromosomal Proteins Non-HistoneMolecular Sequence DataArabidopsisPlant ScienceChromatin remodelingComplementary DNAArabidopsisGeneticsArabidopsis thalianaAmino Acid SequenceCloning MolecularDesiccationPeptide sequenceGeneCells CulturedConserved SequencePhylogenyGeneticsExpressed sequence tagbiologyBase SequenceSequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionPeasbiology.organism_classificationChromatinRecombinant ProteinsChromatinCell biologyPlant LeavesSeedsAbscisic AcidPlant physiology and biochemistry : PPB
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An insect juvenile hormone-specific epoxide hydrolase is related to vertebrate microsomal epoxide hydrolases.

1996

Abstract We describe the first cDNA sequence encoding a juvenile hormone-specific epoxide hydrolase from an insect. A full-length cDNA clone revealed a 462-amino-acid open reading frame encoding an amino acid sequence with 44% identity and 64% similarity to human microsomal epoxide hydrolase. All residues in the catalytic triad (residues Asp 227 -His 428 -Asp 350 in the M. sexta protein) were present, as was the conserved Trp 154 corresponding to the oxyanion hole. The surprising similarity of insect juvenile hormone epoxide hydrolase to vertebrate microsomal epoxide hydrolases, coupled with the ancient lineage of the epoxide hydrolases and haloalkane dehalogenases, suggests that this catab…

DNA ComplementaryMolecular Sequence DataBiophysicsSequence HomologyBiologyBiochemistryPolymerase Chain ReactionMiceOpen Reading FramesComplementary DNAMicrosomesCatalytic triadAnimalsHumansAmino Acid SequenceEpoxide hydrolaseMolecular BiologyPeptide sequenceConserved SequenceEpoxide HydrolasesBase SequenceCell BiologyRatsJuvenile HormonesBiochemistryMicrosomal epoxide hydrolaseEpoxide HydrolasesJuvenile hormoneRabbitsOxyanion holeBiochemical and biophysical research communications
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