Search results for "Peptide sequence"

showing 10 items of 330 documents

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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Amino acid substitutions at position 97 in HLA-A2 segregate cytolysis from cytokine release in MART-1/Melan-A peptide AAGIGILTV-specific cytotoxic T …

1996

CD8+ T lymphocytes recognize antigenic peptides presented by major histocompatibility complex (MHC) class I molecules. Individual peptide termini appear to be fixed at the C- and N-terminal ends. In contrast, central peptide side chains residues may point in different directions and exhibit limited flexibility, dependent on the MHC class I structural variation. For instance, position 97 in HLA-A201 has been shown to shift individual peptide species into different coordinations, one oriented towards the peptide N terminus, or more towards the C-terminal end. The conformational shape of such non-anchor peptide residues may affect the affinity of MHC/peptide/TCR interaction, resulting in quant…

Cytotoxicity ImmunologicT cellImmunologyPeptide bindingMajor histocompatibility complexMART-1 AntigenAntigens NeoplasmMHC class IHLA-A2 AntigenmedicineTumor Cells CulturedImmunology and AllergyCytotoxic T cellHumansAmino Acid SequencePeptide sequenceMelanomabiologyMHC restrictionMolecular biologyNeoplasm Proteinsmedicine.anatomical_structureBiochemistrybiology.proteinCytokinesCD8Protein BindingT-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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Identification of a third secondary carrier (DcuC) for anaerobic C4-dicarboxylate transport in Escherichia coli: roles of the three Dcu carriers in u…

1996

In Escherichia coli, two carriers (DcuA and DcuB) for the transport of C4 dicarboxylates in anaerobic growth were known. Here a novel gene dcuC was identified encoding a secondary carrier (DcuC) for C4 dicarboxylates which is functional in anaerobic growth. The dcuC gene is located at min 14.1 of the E. coli map in the counterclockwise orientation. The dcuC gene combines two open reading frames found in other strains of E. coli K-12. The gene product (DcuC) is responsible for the transport of C4 dicarboxylates in DcuA-DcuB-deficient cells. The triple mutant (dcuA dcuB dcuC) is completely devoid of C4-dicarboxylate transport (exchange and uptake) during anaerobic growth, and the bacteria are…

DNA BacterialMutantMolecular Sequence DataBiologymedicine.disease_causeMicrobiologyGene productBacterial ProteinsmedicineEscherichia coliDicarboxylic AcidsAmino Acid SequenceAnaerobiosisMolecular BiologyEscherichia coliPeptide sequenceGeneDicarboxylic Acid TransportersBase SequenceSequence Homology Amino AcidEscherichia coli ProteinsChromosome MappingBiological Transportbiology.organism_classificationIsoenzymesOpen reading frameMutagenesis InsertionalBiochemistryC4-dicarboxylate transportCarrier ProteinsBacteriaResearch ArticleJournal of bacteriology
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Concomitant loss of conformation and superantigenic activity of staphylococcal enterotoxin B deletion mutant proteins.

1993

The T-cell-stimulating activity of staphylococcal enterotoxin B (SEB) is an important factor in the pathogenesis of certain staphylococcal diseases. To investigate the immunologically active domains of the SEB molecule, we have produced truncated fragments of recombinant SEB by C-terminal and N-terminal deletions. The fragments were expressed as fusion proteins with protein A, including a cleavage site to remove the protein A part. Mutant proteins were tested for the ability to stimulate human resting T cells and SEB-reactive T-cell clones. Deletion of only 9 amino acids from the C terminus leads to complete loss of T-cell-stimulating activity. Removing further amino acids from the SEB mole…

DNA BacterialStaphylococcus aureusRecombinant Fusion ProteinsImmunologyMutantMolecular Sequence DataBiologyMicrobiologyEpitopeEnterotoxinsMiceStructure-Activity RelationshipMutant proteinAnimalsAmino Acid SequencePeptide sequencechemistry.chemical_classificationAntigens BacterialMice Inbred BALB CBase SequenceC-terminusFusion proteinMolecular biologyAmino acidInfectious DiseaseschemistryMutationParasitologyGene DeletionConformational epitopeResearch Article
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Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties.

1998

A gene encoding a novel cell wall-associated protein of Staphylococcus saprophyticus that binds fibronectin and to sheep erythrocytes has been cloned and sequenced. The 4392 bp open reading frame codes for an amino acid sequence that is quite similar to the Atl, an autolysin, of Staphylococcus aureus and to the AtlE of S. epidermidis. The two regions of most pronounced homology code for an N-acetyl-muramyl-L-alanine amidase and for an endo-beta-N-acetyl-D-glucosaminidase. The cloned protein lysed cells of S. saprophyticus and Micrococcus luteus exogenously. Subcloning localized the enzymatic activities to the regions of high homology and demonstrated that the interposed sequence is responsi…

DNA BacterialStaphylococcusMolecular Sequence DataBiologyMicrobiologyHomology (biology)BacteriolysisAmino Acid SequenceCloning MolecularAdhesins BacterialMolecular BiologyGenePeptide sequenceAllelesStaphylococcus saprophyticusBinding SitesBase SequenceAutolysinSequence Analysis DNAbiology.organism_classificationMolecular biologyFibronectinsBacterial adhesinOpen reading frameSubcloningHemagglutininsBiochemistryGenes BacterialMolecular microbiology
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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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Origin of the metazoan bodyplan: characterization and functional testing of the promoter of the homeobox gene EmH-3 from the freshwater sponge Ephyda…

1998

Porifera [sponges] represent the lowest metazoan phylum, probably already existing prior to the 'Cambrian explosion'. Based on amino acid sequences deduced from cDNAs that code for structural proteins, the monophyly of Metazoa was established. Now we analyzed for the first time a promoter of a sponge gene for its activity in a heterologous cell system from higher Metazoa. The promoter of the homeobox gene EmH-3 was cloned and sequenced from a genomic library of the freshwater sponge Ephydatia muelleri. For the determination of functional promoter activity, transient transfection experiments in mouse NIH 3T3 cells were performed; the promoter was fused with the luciferase reporter gene. The …

DNA ComplementaryClinical BiochemistryMolecular Sequence DataHeterologousBiochemistryMiceSequence Homology Nucleic AcidAnimalsGenomic libraryAmino Acid SequenceCloning MolecularPromoter Regions GeneticMolecular BiologyGeneTranscription factorPeptide sequenceCloningHomeodomain ProteinsbiologyBase SequenceSequence Homology Amino AcidGenes Homeobox3T3 Cellsbiology.organism_classificationMolecular biologyPoriferaSpongeHomeoboxBiological chemistry
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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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Molecular characterization of a phosphoenolpyruvate carboxylase in the gymnosperm Picea abies (Norway spruce)

1996

Phosphoenolpyruvate carboxylase (PEPC) genes and cDNA sequences have so far been isolated from a broad range of angiosperm but not from gymnosperm species. We constructed a cDNA library from seedlings of Norway spruce (Picea abies) and identified cDNAs coding for PEPC. A full-length PEPC cDNA was sequenced. It consists of 3522 nucleotides and has an open reading frame (ORF) that encodes a polypeptide (963 amino acids) with a molecular mass of 109551. The deduced amino acid sequence revealed a higher similarity to the C3-form PEPC of angiosperm species (86-88%) than to the CAM and C4 forms (76-84%). The putative motif (Lys/Arg-X-X-Ser) for serine kinase, which is conserved in all angiosperm …

DNA ComplementaryDNA PlantProtein ConformationMolecular Sequence DataPlant ScienceBiologyTreesEvolution MolecularGymnospermComplementary DNABotanyGeneticsAmino Acid SequenceRNA MessengerCloning MolecularPeptide sequencePhylogenySouthern blotBase SequenceSequence Homology Amino AcidcDNA libraryHybridization probefungifood and beveragesPicea abiesGeneral MedicineBlotting Northernbiology.organism_classificationPhosphoenolpyruvate CarboxylaseBlotting SouthernBiochemistryPhosphoenolpyruvate carboxylaseAgronomy and Crop SciencePlant Molecular Biology
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