Search results for "Peptide sequence"

showing 10 items of 330 documents

Therapeutic application of T cell receptor mimic peptides or cDNA in the treatment of T cell-mediated skin diseases

2000

An 8-amino acid peptide encoding a sequence of the transmembrane region of the T cell receptor alpha chain (TCR-alpha) was shown to inhibit T cell function by preventing functional assembly of the T cell receptor (mimic peptide). To avoid systemic immunosuppression by peptide application in vivo, we used a topical application of the peptide. In the system of murine contact sensitivity, topical application of the peptide inhibited the elicitation of contact sensitivity following application of a contact allergen in sensitized animals. Alternatively, when naked DNA encoding the peptide sequence was injected into skin before application of a contact allergen to sensitized animals, local immuno…

DNA ComplementaryReceptors Antigen T-Cell alpha-betaT-LymphocytesT cellGenetic enhancementPeptidePharmacologyBiologySkin DiseasesDermatitis AtopicMiceAntigenVaccines DNAGeneticsmedicineAnimalsHumansReceptorMolecular BiologyPeptide sequenceImmunosuppression Therapychemistry.chemical_classificationMice Inbred BALB CT-cell receptorAllergensPeptide Fragmentsmedicine.anatomical_structurechemistryNaked DNADermatitis Allergic ContactImmunologyMolecular MedicineGene Therapy
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Identification of a novel Drosophila melanogaster gene, angel, a member of a nested gene cluster at locus 59F4,5.

1996

The identification of a novel Drosophila melanogaster gene, angel, is presented in this study. angel is located on the right arm of the second chromosome at locus 59F5, close to the nested genes l(2)tid, l(2)not, l(2)rot and l(2)dtl. We describe the genetic and molecular localization of angel and present its temporal expression in the wild-type. The deduced amino acid sequence of the ANG39 protein is characterized by a nuclear localization signal. Furthermore, the central part of the predicted ANG39 protein shows significant homology to the C-terminal portion of the yeast transcriptional effector CCR4.

DNA ComplementarySaccharomyces cerevisiae ProteinsMolecular Sequence DataRestriction MappingBiophysicsLocus (genetics)Genes InsectBiochemistryHomology (biology)ChromosomesFungal ProteinsRibonucleasesStructural BiologyGeneticsAnimalsDrosophila ProteinsAmino Acid SequenceCloning MolecularGenePeptide sequenceGeneticsbiologyBase SequenceEffectorChromosome MappingGene Expression Regulation Developmentalbiology.organism_classificationBlotting NorthernNested geneDrosophila melanogasterMultigene FamilyInsect ProteinsDrosophila melanogasterSequence AlignmentNuclear localization sequenceTranscription FactorsBiochimica et biophysica acta
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Molecular cloning and characterization of aCandida albicansgene (EFB1) coding for the elongation factor EF-1β

1996

A Candida albicans gene homologous to Saccharomyces cerevisiae elongation factor 1 beta was isolated by screening a genomic DNA library using a C. albicans cDNA as a probe. This cDNA was previously obtained by immunoscreening of an expression library with polyclonal antibodies raised against candidal cell wall components. Sequence analysis of the cDNA and the whole C. albicans gene (EMBL accession number X96517) revealed an intron-interrupted open reading frame of 639 base pairs that encodes a 213 amino acid protein. Exon sequences are highly homologous (74%) to S. cerevisiae EFB1, whereas intron sequence is less conserved (34% identity), and the predicted amino acid sequence shares about 7…

DNA ComplementarySequence analysisGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeMolecular cloningMicrobiologyFungal ProteinsPeptide Elongation Factor 1ImmunoscreeningComplementary DNACandida albicansGeneticsAnimalsCloning MolecularCandida albicansMolecular BiologyPeptide sequenceGeneGeneticsGenomeBase SequenceSequence Homology Amino AcidbiologySequence Analysis DNABlotting NorthernPeptide Elongation Factorsbiology.organism_classificationMolecular biologyElongation factorBlotting SouthernRabbitsFEMS Microbiology Letters
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Identification and Expression of the SOS Response, aidB-Like, Gene in the Marine Sponge Geodia cydonium: Implication for the Phylogenetic Relationshi…

1998

Sponges (Porifera) are the phylogenetically oldest metazoan organisms. From one member of the siliceous sponges, Geodia cydonium, the cDNA encoding a putative SOS protein, the AidB-like protein of the Ada system from bacteria, was isolated and characterized. The cDNA, GCaidB, comprises an open reading frame of 446 amino acid (aa) residues encoding a polypeptide with a calculated Mr of 49,335. This molecule shows high similarity to the bacterial AidB proteins from Mycobacterium tuberculosis and Escherichia coli and somewhat lower similarities to acyl-CoA dehydrogenases (ADHs) and acyl-CoA oxidases (AOXs). Northern blot analysis confirmed the presence of the complete transcript. The deduced s…

DNA ComplementarySequence analysisMolecular Sequence DataSequence alignmentBiologymedicine.disease_causeAcyl-CoA DehydrogenaseEvolution MolecularBacterial ProteinsPhylogeneticsComplementary DNAGeneticsmedicineAnimalsAmino Acid SequenceSOS Response GeneticsMolecular BiologyGeneEscherichia coliPeptide sequencePhylogenyEcology Evolution Behavior and SystematicsGeneticsBase SequenceEscherichia coli ProteinsAcyl-CoA Dehydrogenase Long-ChainSequence Analysis DNABlotting NorthernInvertebratesPoriferaOpen reading frameBiochemistryOxidoreductasesSequence AlignmentJournal of Molecular Evolution
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Acetyltransfer in natural product biosynthesis--functional cloning and molecular analysis of vinorine synthase.

2004

Vinorine synthase (EC 2.3.1.160) catalyses the acetyl-CoA- or CoA-dependent reversible formation of the alkaloids vinorine (or 11-methoxy-vinorine) and 16-epi-vellosimine (or gardneral). The forward reaction leads to vinorine, which is a direct biosynthetic precursor along the complex pathway to the monoterpenoid indole alkaloid ajmaline, an antiarrhythmic drug from the Indian medicinal plant Rauvolfia serpentina. Based on partial peptide sequences a cDNA clone was isolated and functionally expressed in Escherichia coli. The Km values of the native enzyme for gardneral and acetyl-CoA were determined to be 7.5 and 57 microM. The amino acid sequence of vinorine synthase has highest level of i…

DNA ComplementaryStereochemistrySequence analysisClinical BiochemistryMolecular Sequence DataPharmaceutical ScienceSequence alignmentBiochemistryRauwolfiaIndole AlkaloidsSubstrate Specificitychemistry.chemical_compoundBiosynthesisAcetyltransferasesSequence Analysis ProteinDrug DiscoveryConsensus sequenceAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequencechemistry.chemical_classificationATP synthasebiologyChemistryOrganic ChemistryAcetylationAmino acidBiochemistryAcetyltransferasebiology.proteinMutagenesis Site-DirectedMolecular MedicineSequence AlignmentBioorganicmedicinal chemistry
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Characterization of a cDNA encoding RP43, a CUB-domain-containing protein from the tube of Riftia pachyptila (Vestimentifera), and distribution of it…

2000

A major 43kDa protein from the protective tube of Riftiapachyptila (Vestimentifera), named RP43, was partly microsequenced after isolation by SDS/PAGE from the protein fraction of tubes collected around the hydrothermal vents at the East Pacific Rise. On the basis of the partial peptide sequences obtained, experiments using reverse-transcriptase-mediated PCR and rapid amplification of cDNA ends led to the complete cDNA sequence. Analysis of deduced amino acid sequence of RP43 showed the presence of CUB domains (100–110-residue-spanning domains first reported in the complement subcomponents C1r/C1s, epidermal-growth-factor-related sea urchin protein and bone morphogenetic protein 1) that se…

DNA ComplementaryTranscription GeneticAnnelidaMolecular Sequence DataChitinPeptideBioinformaticsBiochemistryEpitheliumBone morphogenetic protein 1Rapid amplification of cDNA endsSequence Analysis ProteinComplementary DNAbiology.animalAnimalsAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyPeptide sequenceSea urchinChromatography High Pressure LiquidIn Situ Hybridizationchemistry.chemical_classificationMessenger RNABase SequenceSequence Homology Amino AcidbiologyReverse Transcriptase Polymerase Chain ReactionHelminth ProteinsSequence Analysis DNACell BiologyBlotting NorthernCUB domainProtein Structure TertiaryCell biologychemistryElectrophoresis Polyacrylamide GelEpidermisProtein BindingResearch ArticleBiochemical Journal
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Immunoglobulin-like domain is present in the extracellular part of the receptor tyrosine kinase from the marine sponge Geodia cydonium.

1994

We have isolated and characterized two cDNAs from the marine sponge Geodia cydonium coding for a new member of a receptor tyrosine kinase of class II. The deduced amino acid sequence shows two characteristic domains: (i) the tyrosine kinase domain; and (ii) and immunoglobulin-like domain. The latter part shows high homology to the vertebrate C2 type immunoglobulin domain. This result demonstrates that immunoglobulin domains are not recent achievements of higher animals but exist also in those animals which have diverged from other organisms about 800 million years ago.

DNA ComplementarybiologySequence Homology Amino AcidMolecular Sequence DatamyrImmunoglobulinsReceptor Protein-Tyrosine KinasesImmunoglobulin domainSH2 domainBiological EvolutionReceptor tyrosine kinasePoriferaProtein Structure TertiaryBiochemistryStructural BiologyPhylogeneticsMultigene FamilyROR1biology.proteinAnimalsAmino Acid SequenceMolecular BiologyPeptide sequenceTyrosine kinaseSequence AlignmentJournal of molecular recognition : JMR
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Abalone (Haliotis tuberculata) hemocyanin type 1 (HtH1) . Organization of the = 400 kDa subunit, and amino acid sequence of its functional units f, g…

1999

We have identified two separate hemocyanin types (HtH1 and HtH2) in the European abalone Haliotis tuberculata. HtH1/HtH2 hybrid molecules were not found. By selective dissociation of HtH2 we isolated HtH1 which, as revealed by electron microscopy and SDS/PAGE, is present as didecamers of a approximately 400 kDa subunit. Immunologically, HtH1 and HtH2 correspond to keyhole limpet hemocyanin (KLH)1 and KLH2, respectively, the two well-studied hemocyanin types of the closely related marine gastropod Megathura crenulata. On the basis of limited proteolytic cleavage, two-dimensional immunoelectrophoresis, SDS/PAGE and N-terminal sequencing, we identified eight different 40-60 kDa functional unit…

DNA Complementaryfood.ingredientmedicine.medical_treatmentMolecular Sequence DataMegathura crenulataBiochemistryfoodmedicineAnimalsAmino Acid SequenceHaliotisCloning MolecularPeptide sequenceSequence Homology Amino AcidbiologycDNA libraryHemocyaninAnatomyHelix pomatiabiology.organism_classificationCephalopodMicroscopy ElectronBiochemistryMolluscaHemocyaninsbiology.proteinRabbitsKeyhole limpet hemocyaninEuropean Journal of Biochemistry
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Identification of a novel VP4 genotype carried by a serotype G5 porcine rotavirus strain

2006

AbstractRotavirus genome segment 4, encoding the spike outer capsid VP4 protein, of a porcine rotavirus (PoRV) strain, 134/04-15, identified in Italy was sequenced, and the predicted amino acid (aa) sequence was compared to those of all known VP4 (P) genotypes. The aa sequence of the full-length VP4 protein of the PoRV strain 134/04-15 showed aa identity values ranging from 59.7% (bovine strain KK3, P8[11]) to 86.09% (porcine strain A46, P[13]) with those of the remaining 25 P genotypes. Moreover, aa sequence analysis of the corresponding VP8* trypsin cleavage fragment revealed that the PoRV strain 134/04-15 shared low identity, ranging from 37.52% (bovine strain 993/83, P[17]) to 73.6% (po…

DiarrheaRotavirusSerotypeP genotypeGenotypeSwineSequence analysisvirusesMolecular Sequence DataViral Nonstructural ProteinsBiologymedicine.disease_causeGenetic diversityRotavirus InfectionsVirologyRotavirusGenetic variationGenotypemedicineAnimalsAmino Acid SequenceSerotypingAntigens ViralPeptide sequenceGenePhylogenyGlycoproteinsToxins BiologicalSwine DiseasesSequence Homology Amino AcidPhylogenetic treeGenetic Variationvirus diseasesSequence Analysis DNAVirologyMolecular biologyItalyVP4PigsCapsid Proteins
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Identification of protein IT of the intestinal cytoskeleton as a novel type I cytokeratin with unusual properties and expression patterns.

1990

A major cytoskeletal polypeptide (Mr approximately 46,000; protein IT) of human intestinal epithelium was characterized by biochemical and immunological methods. The polypeptide, which was identified as a specific and genuine mRNA product by translation in vitro, reacted, in immunoblotting after SDS-PAGE, only with one of numerous cytokeratin (CK) antisera tested but with none of many monoclonal CK antibodies. In vitro, it formed heterotypic complexes with the type II CK 8, as shown by blot binding assays and gel electrophoresis in 4 M urea, and these complexes assembled into intermediate filaments (IFs) under appropriate conditions. A chymotrypsin-resistant Mr approximately 38,000 core fra…

DuodenumImmunoblottingMolecular Sequence DataBiologyPeptide MappingEpitheliumCytokeratinIntestinal mucosaSequence Homology Nucleic AcidKeratinProtein biosynthesisAnimalsHumansElectrophoresis Gel Two-DimensionalAmino Acid SequenceRNA MessengerIntestinal MucosaIntermediate filamentCytoskeletonPeptide sequenceCytoskeletonchemistry.chemical_classificationArticlesCell BiologyMolecular biologyRatsBlotCytoskeletal ProteinsMicroscopy ElectronBiochemistrychemistryProtein BiosynthesisKeratinsJournal of Cell Biology
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