Search results for "mapping"

showing 10 items of 1508 documents

Asp333, Asp495, and His52.3 Form the Catalytic Triad of Rat Soluble Epoxide Hydrolase

1996

On the basis of the sequence similarity between mammalian epoxide hydrolases and bacterial haloalkane dehalogenase reported earlier (Arand, M., Grant, D. F., Beetham, J. K., Friedberg, T., Oesch, F., and Hammock, B. D. (1994) FEBS Lett. 338, 251-256; Beetham, J. K., Grant, D., Arand, M., Garbarino, J., Kiyosue, T., Pinot, F., Oesch, F., Belknap, W. R., Shinozaki, K., and hammock, B. D. (1995) DNA Cell. Biol. 14, 61-71) we selected candidate amino acid residues for the putative catalytic triad of the rat soluble epoxide hydrolase. The predicted amino acid residues were exchanged by site-directed mutagenesis of the epoxide hydrolase cDNA, followed by the expression of the respective mutant en…

Models MolecularEpoxide hydrolase 2StereochemistryMolecular Sequence DataRestriction MappingPolymerase Chain ReactionBiochemistryCatalysisProtein Structure SecondaryCatalytic triadEscherichia coliAnimalsHumansPoint MutationHistidineAmino Acid SequenceCloning MolecularEpoxide hydrolaseMolecular BiologyPeptide sequenceDNA PrimersEpoxide Hydrolaseschemistry.chemical_classificationAspartic AcidBinding SitesSequence Homology Amino AcidChemistryCell BiologyRecombinant ProteinsRatsAmino acidEpoxide hydrolase activityKineticsBiochemistryEpoxide HydrolasesMutagenesis Site-DirectedHaloalkane dehalogenaseJournal of Biological Chemistry
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Plasmonic Nanosensors for Simultaneous Quantification of Multiple Protein–Protein Binding Affinities

2014

Most of current techniques used for the quantification of protein-protein interactions require the analysis of one pair of binding partners at a time. Herein we present a label-free, simple, fast, and cost-effective route to characterize binding affinities between multiple macromolecular partners simultaneously, using optical dark-field spectroscopy and individual protein-functionalized gold nanorods as sensing elements. Our NanoSPR method could easily become a simple and standard tool in biological, biochemical, and medical laboratories.

Models MolecularNanotubesBacteriaChemistryMechanical EngineeringProtein proteinBioengineeringNanotechnologyGeneral ChemistrySurface Plasmon ResonanceCondensed Matter PhysicsCytoskeletal ProteinsBacterial ProteinsNanosensorProtein Interaction MappingGeneral Materials ScienceNanorodGoldPlasmonProtein BindingBinding affinitiesMacromoleculeNano Letters
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Multiple IgE recognition on the major allergen of the Parietaria pollen Par j 2

2015

The interaction between IgE antibodies and allergens is a key event in triggering an allergic reaction. The characterization of this region provides information of paramount importance for diagnosis and therapy. Par j 2 Lipid Transfer Protein is one of the most important allergens in southern Europe and a well-established marker of sensitization in Parietaria pollen allergy. The main aim of this study was to map the IgE binding regions of this allergen and to study the pattern of reactivity of individual Parietaria-allergic patients. By means of gene fragmentation, six overlapping peptides were expressed in Escherichia coli, and their IgE binding activity was evaluated by immunoblotting in …

Models MolecularParietariaAdolescentBlotting WesternImmunoblottingMolecular Sequence DataEpitope mappingImmunologyProtein domainImmunoglobulin Emedicine.disease_causeEpitopelaw.inventionEpitopesAllergenlawmedicineHumansComputer SimulationAmino Acid SequenceCloning MolecularChildParietaria IgE Epitope mapping Molecular biology.Molecular BiologybiologyRhinitis Allergic SeasonalAllergensImmunoglobulin Ebiology.organism_classificationRecombinant ProteinsParietariaEpitope mappingImmunologybiology.proteinRecombinant DNAPollenElectrophoresis Polyacrylamide GelIgEPlant lipid transfer proteinsMolecular Immunology
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Participation of Two Ser-Ser-Phe-Tyr Repeats in Interleukin-6 (IL-6)-Binding Sites of the Human IL-6 Receptor

1996

The alpha-subunit of interleukin-6 (IL-6) receptor is a member of the hematopoietin receptor family. The alignment of its amino acid sequence with those of other members of this family (human somatotropin receptor/murine IL-3 receptor beta and human IL-2 receptor beta) has suggested that amino acids included in two SSFY repeats found in each of its hematopoietin receptor domains, contribute to the binding of the ligand. The involvement of these amino acids in IL-6 binding and signal transduction was studied by site-directed mutagenesis and molecular modelling. We present a computer-derived three-dimensional model of the IL-6/IL-6 receptor complex based on the structure of the human somatotr…

Models MolecularReceptor complexMolecular Sequence DataB-cell receptorInterleukin 5 receptor alpha subunitBiologyBiochemistryMiceAntigens CDTumor Cells CulturedEnzyme-linked receptorAnimalsHumans5-HT5A receptorAmino Acid SequenceNuclear receptor co-repressor 1Binding SitesBase SequenceInterleukin-6Antibodies MonoclonalReceptors InterleukinInterleukin-13 receptorReceptors Interleukin-6Molecular biologyBiochemistryMutationRabbitsEpitope MappingRelaxin/insulin-like family peptide receptor 2Signal TransductionEuropean Journal of Biochemistry
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cDNA Cloning and Functional Expression of Jerdostatin, a Novel RTS-disintegrin from Trimeresurus jerdonii and a Specific Antagonist of the α1β1 Integ…

2005

Jerdostatin represents a novel RTS-containing short disintegrin cloned by reverse transcriptase-PCR from the venom gland mRNA of the Chinese Jerdons pit viper Trimeresurus jerdonii. The jerdostatins precursor cDNA contained a 333-bp open reading frame encoding a signal peptide, a pre-peptide, and a 43-amino acid disintegrin domain, whose amino acid sequence displayed 80% identity with that of the KTS-disintegrins obtustatin and viperistatin. The jerdostatin cDNA structure represents the first complete open reading frame of a short disintegrin and points to the emergence of jerdostatin from a short-coding gene. The different residues between jerdostatin and obtustatin/viperistatin are segreg…

Models MolecularSignal peptideProtein FoldingDNA ComplementaryMagnetic Resonance SpectroscopyProtein ConformationDisintegrinsMolecular Sequence DataIntegrinMutantGene ExpressionPeptide MappingBiochemistryIntegrin alpha1beta1Open Reading FramesExocrine GlandsComplementary DNACrotalid VenomsDisintegrinAnimalsTrimeresurusTrypsinAmino Acid SequenceCysteineDisulfidesCloning MolecularMolecular BiologyPeptide sequenceMessenger RNABase SequencebiologyCell BiologyMolecular biologyRecombinant ProteinsOpen reading frameMutagenesis Site-Directedbiology.proteinJournal of Biological Chemistry
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Cloning of a DNA fragment encoding part of a 70-kDa heat shock protein ofCandida albicans

1995

Immunoscreening of a mycelial expression library with polyclonal antibodies raised against mycelial cell wall resulted in the detection of a cDNA encoding a heat shock protein of Candida albicans. Sequence analysis of a 0.8-kb cDNA subclone, 2M-1, revealed an open reading frame encoding 244 amino acids. Southern blot analysis with this fragment as a probe demonstrated hybridization to C. albicans DNA. Northern analysis showed a substantial increase in 2M RNA expression levels after cells were subjected to heat shock. Western blot analysis with 2M monospecific antibodies recognized a 70-kDa protein which was present in membrane particles and cytosolic fractions.

Molecular Sequence DataMicrobiologyWestern blotImmunoscreeningHeat shock proteinComplementary DNACandida albicansGeneticsmedicineHSP70 Heat-Shock ProteinsAmino Acid SequenceRNA MessengerCloning MolecularHeat shockDNA FungalCandida albicansMolecular BiologySouthern blotBase Sequencebiologymedicine.diagnostic_testChromosome MappingSequence Analysis DNAbiology.organism_classificationMolecular biologyBiochemistryPolyclonal antibodiesbiology.proteinFEMS Microbiology Letters
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Molecular characterization of the zerknüllt region of the Antennapedia complex of D. subobscura.

1995

We have characterized at the molecular level the zerknullt (zen) region of the Drosophila subobscura Antennapedia complex. The sequence comparison between D. subobscura and D. melanogaster shows an irregular distribution of the conserved and diverged regions, with the homeobox and a putative activating domain completely conserved. Comparisons of the promoter sequence and pattern of expression of the gene during development suggest that the regulation of zen has been conserved during evolution. The conservation of zen expression in a subpopulation of the polar cells indicates the existence of an important role in such cells. We describe a transitory segmented pattern of expression of zen in …

Molecular Sequence DataPair-rule geneGenes InsectAntennapediaGenomeChromosomesGeneticsMelanogasterAnimalsDrosophila ProteinsAmino Acid SequenceRNA MessengerCloning MolecularPromoter Regions GeneticGeneGenetics (clinical)In Situ HybridizationGeneticsHomeodomain ProteinsbiologyBase SequencefungiGenes HomeoboxChromosomeChromosome MappingGene Expression Regulation DevelopmentalNuclear Proteinsbiology.organism_classificationDrosophila subobscuraDNA-Binding ProteinsRepressor ProteinsInsect HormonesAntennapedia Homeodomain ProteinHomeoboxDrosophilaSequence AlignmentTranscription FactorsChromosoma
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Plasmid-encoded anthranilate synthase (TrpEG) in Buchnera aphidicola from aphids of the family pemphigidae

1999

Aphids are dependent on an intracellular symbiont (Buchnera aphidicola, Proteobacteria) for normal growth and reproduction (7, 19, 45). The bacteria reside in specialized cells in the aphid hemocele and are transmitted maternally through infection of eggs or embryos (11, 26). Phylogenetic studies have revealed two major characteristics of the evolutionary history of the association (37, 39); (i) the symbiosis had a single origin, dated about 150 million to 250 million years ago; and (ii) host and symbiont lineages have since diverged strictly in parallel. The association, like other symbioses in insects feeding on restricted and unbalanced diets, is thought to have a nutritional basis (5–7,…

Molecular Sequence DataPemphigus spyrothecaePolymerase Chain ReactionApplied Microbiology and BiotechnologyEvolution MolecularPlasmidPhylogeneticsInvertebrate MicrobiologyAnimalsAmino Acid SequenceRepliconCloning MolecularSymbiosisPhylogenyAnthranilate SynthaseDNA PrimersGeneticsAphidBacteriaBase SequenceSequence Homology Amino AcidEcologybiologyfood and beveragesAphididaebiochemical phenomena metabolism and nutritionPhysical Chromosome Mappingbiology.organism_classificationBiochemistryAphidsbiology.proteinAnthranilate synthaseBuchneraPlasmidsFood ScienceBiotechnology
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Mapping of a binding site for ATP within the extracellular region of the Torpedo nicotinic acetylcholine receptor beta-subunit.

1997

Using 2,8,5'-[H-3]ATP as a direct photoaffinity label for membrane-bound nicotinic acetylcholine receptor (nAChR) from Torpedo marmorata, we have identified a binding site for ATP in the extracellular region of the beta-subunit of the receptor. Photolabeling was completely inhibited in the presence of saturating concentrations of nonradioactive ATP, whereas neither the purinoreceptor antagonists suramin, theophyllin, and caffeine nor the nAChR antagonists alpha-bungarotoxin and d-tubocurarine affected the labeling reaction. Competitive and noncompetitive nicotinic agonists and Ca2+ increased the yield of the photoreaction by up to 50%, suggesting that the respective binding sites are allost…

Molecular Sequence DataPhotoaffinity LabelsReceptors NicotinicTorpedoTritiumBiochemistryPeptide Mappingchemistry.chemical_compoundGanglion type nicotinic receptorAdenosine TriphosphateAdenine nucleotideAnimalsChymotrypsinTrypsinAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisCell MembranePeptide FragmentsNicotinic acetylcholine receptorNicotinic agonistBiochemistrychemistrybiology.proteinAlpha-4 beta-2 nicotinic receptorExtracellular SpaceAdenosine triphosphateSequence AnalysisATP synthase alpha/beta subunitsBiochemistry
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Isolation of the DNA minisatellite probe MZ 1.3 and its application to DNA ‘fingerprinting’ analysis

1990

Abstract A minisatellite probe, MZ 1.3, detecting hypervariable fragment patterns was isolated from a human genomic library. A repetitive sequence of 27 bp length was identified which is contained in the probe approx. 40 times. The MZ 1.3 repeat shows variable homology of 53–73% to the repetitive sequence of the protein III gene of the bacteriophage M13 genome. Polymorphic restriction fragment patterns were found with MZ 1.3 using the enzymes Hinf I, BstN I, Hae III, Mbo I, PstI PvuII , and Rsa I. An average of 18 polymorphic fragments was observed using Hinf I as enzyme. The band sharing frequency after Hinf I digestion among unrelated individuals was determined to be 23.8 ± 7.2%. An examp…

Molecular Sequence DataRestriction MappingDNA SatelliteHomology (biology)Pathology and Forensic MedicineRestriction fragmentchemistry.chemical_compoundHumansGenomic libraryGeneRepetitive Sequences Nucleic AcidGeneticsGenomic LibraryBase SequencebiologyNucleotide MappingDNAMolecular biologyBlotting SouthernVariable number tandem repeatMinisatelliteDNA profilingchemistrybiology.proteinDNA ProbesLawPolymorphism Restriction Fragment LengthDNAForensic Science International
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