Search results for "Molecular sequence"

showing 10 items of 1972 documents

Study of the Evolutionary Relationships among Limonium Species (Plumbaginaceae) Using Nuclear and Cytoplasmic Molecular Markers

2000

The genus Limonium, due to the patchiness of the natural habitats of its species as well as the high frequency of hybridization and polyploidy and the possibility of reproduction by apomixis, provides an example of all the principal mechanisms of rapid speciation of plants. As an initial study of evolution in this genus, we have analyzed intra- and interspecific variability in 17 species from section Limonium, the largest in the genus, based on RFLPs of cpDNA and nuclear rDNA ITS sequences. In the cpDNA analysis, 21 restriction enzymes were used, resulting in 779 fragments, 490 of which were variable and 339 parsimony informative. L. furfuraceum exhibited two relatively divergent cpDNA hapl…

CytoplasmChloroplastsLimoniumMolecular Sequence DataBiologyDNA RibosomalPhylogeneticsSequence Homology Nucleic AcidApomixisPolyphylyBotanyGeneticsMolecular BiologyPhylogenyPlant Physiological PhenomenaEcology Evolution Behavior and SystematicsCell NucleusBase SequencePhylogenetic treeMediterranean RegionReproductionGenetic VariationPlantsbiology.organism_classificationBiological EvolutionReticulate evolutionChloroplast DNARestriction fragment length polymorphismPolymorphism Restriction Fragment LengthMolecular Phylogenetics and Evolution
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2'-O-methyl-5-formylcytidine (f5Cm), a new modified nucleotide at the 'wobble' of two cytoplasmic tRNAs Leu (NAA) from bovine liver.

1996

The nucleotide analysis of a cytoplasmic tRNA(Leu) isolated from bovine liver revealed the presence of an unknown modified nucleotide N. The corresponding N nucleoside was isolated by different enzymatic and chromatographic protocols from a partially purified preparation of this tRNA(Leu). Its chemical characterization was determined from its chromatographic properties, UV-absorption spectroscopy and mass spectrometric measurements, as well as from those of the borohydride reduced N nucleoside and its etheno-trimethylsilyl derivative. The structure of N was established as 2'-O-methyl-5-formylcytidine (f5CM), and its reduced derivative as 2'-O-methyl-5-hydroxy-methylcytidine (om5Cm). By sequ…

CytoplasmMolecular Sequence DataWobble base pairBorohydridesCytidineBiologyRNA Transfer Amino AcylGas Chromatography-Mass Spectrometrychemistry.chemical_compoundGeneticsAnimalsHumansNucleotidechemistry.chemical_classificationBase SequenceMolecular StructureNucleic acid sequenceCytidineUridinechemistryBiochemistryLiverTransfer RNANucleic Acid ConformationCattleLeucineNucleosideHeLa CellsResearch ArticleNucleic acids research
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Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia.

2004

Cytoglobin is a recently discovered vertebrate globin distantly related to myoglobin, and its function is unknown. Here we present the first detailed analysis of the distribution and expression of cytoglobin. Northern and Western blotting experiments show the presence of cytoglobin mRNA and protein in a broad range of tissues. Quantitative PCR demonstrates an up-regulation of cytoglobin mRNA levels in rat heart and liver under hypoxic conditions (22 and 44 h of 9% oxygen). Immunofluorescence studies with three antibodies directed against different epitopes of the protein consistently show cytoglobin in connective tissue fibroblasts as well as in hepatic stellate cells. Cytoglobin is also pr…

CytoplasmRespiratory SystemFluorescent Antibody TechniqueBiochemistryMiceAntibody SpecificityChlorocebus aethiopsRespiratory functionHypoxiaNeuronsMice Inbred BALB CReverse Transcriptase Polymerase Chain ReactionCytoglobinNuclear ProteinsImmunohistochemistryGlobinsRespiratory proteinTracheamedicine.anatomical_structureLiverConnective TissueNeuroglobinRecombinant Fusion ProteinsGreen Fluorescent ProteinsMolecular Sequence DataConnective tissueBiologyTransfectionAntibodiesBone and BonesmedicineAnimalsHumansGlobinAmino Acid SequenceRNA MessengerMolecular BiologyVero CellsCell NucleusMessenger RNAMyocardiumCytoglobinCell BiologyFibroblastsMolecular biologyPeptide FragmentsRatsOxygenLuminescent ProteinsGene Expression RegulationHepatic stellate cellHeLa CellsThe Journal of biological chemistry
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Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1.

1999

AbstractThe interaction of cytoplasmic dynein with its cargoes is thought to be indirectly mediated by dynactin, a complex that binds to the dynein intermediate chain. However, the roles of other dynein subunits in cargo binding have been unknown. Here we demonstrate that dynein translocates rhodopsin-bearing vesicles along microtubules. This interaction occurs directly between the C-terminal cytoplasmic tail of rhodopsin and Tctex-1, a dynein light chain. C-terminal rhodopsin mutations responsible for retinitis pigmentosa inhibit this interaction. Our results point to an alternative docking mechanism for cytoplasmic dynein, provide novel insights into the role of motor proteins in the pola…

CytoplasmRhodopsingenetic structuresMicrotubule-associated proteinRecombinant Fusion ProteinsDyneinMolecular Sequence DataReceptors Cell Surfacemacromolecular substancesBiologyT-Complex Genome RegionMicrotubulesGeneral Biochemistry Genetics and Molecular BiologyMotor protein03 medical and health sciencesMice0302 clinical medicineMicrotubuleAnimalsAmino Acid Sequence030304 developmental biologyt-Complex Genome Region0303 health sciencesBinding SitesBiochemistry Genetics and Molecular Biology(all)DyneinsNuclear ProteinsBiological Transport3. Good healthCell biologyCytoplasmRhodopsinMutagenesisDynactinbiology.proteinMicrotubule ProteinsCattlesense organsMicrotubule-Associated Proteins030217 neurology & neurosurgeryPhotoreceptor Cells VertebrateCell
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Inverse relationship of melanocyte differentiation antigen expression in melanoma tissues and CD8+ cytotoxic-T-cell responses: evidence for immunosel…

1996

Antigenic peptides derived from differentiation antigens of the melanocyte lineage were recently identified in human melanomas as targets for MHC-restricted cytotoxic T lymphocytes (CTL). CTL directed against peptides derived from the Melan A/MART-1, tyrosinase and gp100/Pmel17 antigens can be detected in melanoma patients and in healthy controls. The presence of defined antigenic peptides and corresponding precursor CTL in patients with metastatic melanoma opens perspectives for the development of antigen-specific tumor vaccines. In this study, we examined the expression of Melan A/MART-1, tyrosinase and gp100lPmel17 in fresh melanoma tissues of HLA-A2+ patients and the spontaneous CTL rea…

Cytotoxicity ImmunologicCancer ResearchTyrosinaseMolecular Sequence Data10050 Institute of Pharmacology and Toxicology610 Medicine & healthchemical and pharmacologic phenomenaBiologyMelanocyteCD8-Positive T-LymphocytesEpitopesImmune systemMART-1 AntigenAntigenMelanocyte differentiationAntigens NeoplasmmedicineTumor Cells CulturedCytotoxic T cellHumans1306 Cancer ResearchAmino Acid SequenceneoplasmsMelanomaDNA PrimersImmunity CellularMembrane GlycoproteinsBase SequenceMonophenol MonooxygenaseMelanomaProteinsCell Differentiationmedicine.diseaseNeoplasm ProteinsCTL*medicine.anatomical_structureOncologyImmunology570 Life sciences; biologyMelanocytes2730 Oncologygp100 Melanoma AntigenInternational journal of cancer
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Cloning and expression of the complement receptor glycoprotein C from Herpesvirus simiae (herpes B virus): protection from complement-mediated cell l…

2003

Simian herpes B virus (SHBV) is the herpes simplex virus (HSV) homologue for the species MACACA: Unlike in its natural host, and unlike other animal herpesviruses, SHBV causes high mortality in accidentally infected humans. SHBV-infected cells, like those infected with HSV-1 and equine herpesvirus types 1 and 4, express complement C3 receptor activity. To study immunoregulatory functions involved in susceptibility/resistance against interspecies transmission, the SHBV glycoprotein C (gC(SHBV)) gene (encoding 467 aa) was isolated. Sequence analysis revealed amino acid identity with gC proteins from HSV-2 (46.9 %), HSV-1 (44.5 %) and pseudorabies virus (21.2 %). Highly conserved cysteine resi…

Cytotoxicity ImmunologicHerpes B virusvirusesComplement Pathway AlternativeMolecular Sequence DataHerpesvirus 1 CercopithecineComplement receptorBiologyTransfectionmedicine.disease_causeVirusCell LineViral Envelope ProteinsVirologymedicineAnimalsHumansAmino Acid SequenceCloning MolecularPeptide sequenceSequence Analysis DNAbiology.organism_classificationVirologyComplement systemHerpes simplex virusCell cultureComplement C3bReceptors Complement 3bAlternative complement pathwayJournal of General Virology
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Two tyrosinase nonapeptides recognized on HLA-A2 melanomas by autologous cytolytic T lymphocytes

1994

A number of cytolytic T lymphocyte (CTL) clones derived from several melanoma patients have been found to recognize a majority of melanomas from HLA-A2 patients. We have reported previously that two such CTL clones recognize a product of the tyrosinase gene that is presented by HLA-A2. Here we show that one of these CTL clones recognizes a peptide encoded by the first nine amino acids of the putative signal sequence of tyrosinase. The other CTL clone recognizes a different tyrosinase peptide corresponding to amino acids 368-376. Both peptides contain consensus motifs of HLA-A2 binding peptides.

Cytotoxicity ImmunologicSignal peptideTyrosinaseMolecular Sequence DataImmunologyClone (cell biology)Tyrosinase PeptidePeptideIn Vitro TechniquesBiologyHLA-A2 AntigenTumor Cells CulturedConsensus sequenceHumansImmunology and AllergyAmino Acid SequenceMelanomaPeptide sequenceDNA Primerschemistry.chemical_classificationBase SequenceMonophenol MonooxygenaseVirologyRecombinant ProteinsCTL*chemistryPeptidesT-Lymphocytes CytotoxicEuropean Journal of Immunology
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The sequence alteration associated with a mutational hotspot in p53 protects cells from lysis by cytotoxic T lymphocytes specific for a flanking pept…

1998

A high proportion of tumors arise due to mutation of the p53 tumor suppressor protein. A p53 hotspot mutation at amino acid position 273 from R to H, flanking a peptide epitope that spans residues 264–272, renders cells resistant to killing by human histocompatibility leukocyte antigen (HLA)-A*0201–restricted cytotoxic T lymphocytes (CTLs) specific for this epitope. Acquisition of the R to H mutation at residue 273 of the human p53 protein promotes tumor growth in vivo by selective escape from recognition by p53.264–272 peptide-specific CTLs. Synthetic 27-mer p53 polypeptides covering the antigenic nonamer region 264–272 of p53 were used as proteasome substrates to investigate whether the R…

Cytotoxicity Immunologicp53Epitopes T-LymphocyteEpitopeSubstrate SpecificityMice0302 clinical medicineTumor Cells CulturedImmunology and AllergyCytotoxic T cellPeptide sequence0303 health sciencesAntigen PresentationproteasomesHydrolysisArticles3. Good healthCysteine Endopeptidasestumor antigensCell DivisionProteasome Endopeptidase ComplexImmunologyAntigen presentationMolecular Sequence DataMice TransgenicBiologyArgininecytotoxic T lymphocytes03 medical and health sciencesAntigenMultienzyme Complexesantigen processingAnimalsHumansPoint MutationHistidineAmino Acid Sequence030304 developmental biologyBinding SitesLinear epitopeHLA-A AntigensPoint mutationCytotoxicity Tests ImmunologicMolecular biologyPeptide FragmentsCTL*Tumor Suppressor Protein p53Peptides030215 immunologyT-Lymphocytes CytotoxicThe Journal of experimental medicine
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Nuclear Localization of PTEN by a Ran-dependent Mechanism Enhances Apoptosis: Involvement of an N-Terminal Nuclear Localization Domain and Multiple N…

2006

The targeting of the tumor suppressor PTEN protein to distinct subcellular compartments is a major regulatory mechanism of PTEN function, by controlling its access to substrates and effector proteins. Here, we investigated the molecular basis and functional consequences of PTEN nuclear/cytoplasmic distribution. PTEN accumulated in the nucleus of cells treated with apoptotic stimuli. Nuclear accumulation of PTEN was enhanced by mutations targeting motifs in distinct PTEN domains, and it was dependent on an N-terminal nuclear localization domain. Coexpression of a dominant negative Ran GTPase protein blocked PTEN accumulation in the nucleus, which was also affected by coexpression of importin…

Cèl·lulesAmino Acid MotifsMolecular Sequence DataNuclear Localization SignalsApoptosisBiologyModels BiologicalCatalysislaw.inventionMicelawChlorocebus aethiopsmedicineAnimalsHumansPTENAmino Acid SequenceProteïnes supressores de tumorsMolecular BiologyCells CulturedSequence DeletionCell NucleusCOS cellsEffectorPTEN Phosphohydrolase3T3 CellsArticlesCell BiologyProtein Structure TertiaryRatsTransport proteinProtein TransportCell nucleusran GTP-Binding Proteinmedicine.anatomical_structureCOS CellsRanbiology.proteinCancer researchSuppressorNuclear localization sequenceHeLa CellsMolecular Biology of the Cell
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Establishment and functional validation of a structural homology model for human DNA methyltransferase 1

2003

Changes in DNA methylation patterns play an important role in tumorigenesis. The DNA methyltransferase 1 (DNMT1) protein represents a major DNA methyltransferase activity in human cells and is therefore a prominent target for experimental cancer therapies. However, there are only few available inhibitors and their high toxicity and low specificity have so far precluded their broad use in chemotherapy. Based on the strong conservation of catalytic DNA methyltransferase domains we have used a homology modeling approach to determine the three-dimensional structure of the DNMT1 catalytic domain. Our results suggest an overall structural conservation with other DNA methyltransferases but also in…

DNA (Cytosine-5-)-Methyltransferase 1Models MolecularMethyltransferaseMolecular Sequence DataBiophysicsDNA Methyltransferase InhibitorComputational biologyBiologymedicine.disease_causeModels BiologicalBiochemistryDNA methyltransferasechemistry.chemical_compoundCatalytic DomainTumor Cells CulturedmedicineHumansAmino Acid SequenceDNA (Cytosine-5-)-MethyltransferasesHomology modelingEnzyme InhibitorsMolecular BiologyGeneticsSequence Homology Amino AcidCell BiologyDNA MethylationModels ChemicalchemistryDNA methylationAzacitidineDNMT1Nucleic Acid ConformationCarcinogenesisDNABiochemical and Biophysical Research Communications
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