Search results for " Complement"

showing 10 items of 753 documents

Identification, molecular cloning, and phylogenetic analysis of a non-respiratory pseudo-hemocyanin of Homarus americanus.

1999

Copper-containing hemocyanins serve to transport oxygen in many arthropod species. Here I describe the identification and cDNA cloning of a structurally closely related non-respiratory pseudo-hemocyanin (PHc) of the American lobster, Homarus americanus. This protein has lost the ability to bind copper and, therefore, oxygen because a histidine residue in copper-binding site A is replaced by tyrosine. Like many arthropod hemocyanins, PHc forms a hexamer. It consists of two different subunit types of 660 and 661 amino acids, respectively, that share a 94.4% sequence identity. Whereas Homarus hemocyanin is produced in the hepatopancreas, PHc is synthesized by the ovaries and the heart tissue. …

DNA ComplementaryProtein subunitmedicine.medical_treatmenteducationMolecular Sequence Datachemical and pharmacologic phenomenaMolecular cloningBiologybehavioral disciplines and activitiesBiochemistryPhylogeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequencePhylogenychemistry.chemical_classificationHomarusBase SequenceSequence Homology Amino AcidEcologyHemocyaninCell BiologyProtein superfamilybiology.organism_classificationAmino acidNephropidaeMicroscopy ElectronBiochemistrychemistryHemocyaninsThe Journal of biological chemistry
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The nuclear autoantigen La/SS-B: Mapping and sequencing of the gene and the three retropseudogenes

1997

One target of autoantibodies in sera of patients with systemic lupus erythematosus or primary Sjogren's syndrome is the nuclear autoantigen La/SS-B. Lambda clones and cosmids were isolated, which contained the sequences of the La gene and the three La pseudogenes. They were used for preparation of a physical map. Finally, the La gene and pseudogenes were sequenced. The pseudogenes were characterized as retropseudogenes. Their evolutionary ages were estimated to be approx. 4, 4.5 and 5 million years. Inserts of 4, 16 and 24 nucleotides, which were mostly A-residues, were found in exon 7 of the respective pseudogene. The oldest pseudogene contained the longest insert, the youngest pseudogene …

DNA ComplementaryPseudogeneMolecular Sequence DataBiologyAutoantigensSingle-stranded binding proteinEvolution MolecularExonGeneticsmedicineHumansGeneRibonucleoproteinGeneticsCell NucleusBase SequenceOligonucleotideChromosome MappingGeneral MedicineExonsMolecular biologyCell nucleusmedicine.anatomical_structureRibonucleoproteinsMutationCosmidbiology.proteinPseudogenes
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Overexpression and functional characterization of kinin receptors reveal subtype-specific phosphorylation.

1999

G protein-coupled receptors such as the receptors for bradykinin are present in low copy numbers in most natural cells. To overcome the problems associated with the analysis of these receptors at the protein level, we used highly efficient expression systems such as the baculovirus/insect cell system. However, the structural and functional statuses of recombinant receptors have often remained elusive. We have expressed the two types of human kinin receptors, B1 and B2, in Sf9 cells. Both receptors are found on the surface of infected cells where they display the same pharmacological profiles as their cognate receptors of native cells. The functional analysis of kinin receptors coupled to th…

DNA ComplementaryReceptor Bradykinin B2ImmunoprecipitationSf9SpodopteraBradykininReceptor Bradykinin B1TransfectionBiochemistryAnimalsHumansBinding siteCloning MolecularPhosphorylationReceptorMicroscopy ConfocalKinaseChemistryReceptors BradykininCell MembraneKininMolecular biologyRecombinant ProteinsCell biologyKineticsPhosphorylationCalciumIntracellularBiochemistry
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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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Retinoid X receptor and retinoic acid response in the marine sponge Suberites domuncula

2003

SUMMARY To date no nuclear receptors have been identified or cloned from the phylogenetically oldest metazoan phylum, the Porifera (sponges). We show that retinoic acid causes tissue regression in intact individuals of the demosponge Suberites domuncula and in primmorphs, special three-dimensional cell aggregates. Primmorphs were cultivated on a galectin/poly-L-lysine matrix in order to induce canal formation. In the presence of 1 or 50 μmol l–1 retinoic acid these canals undergo regression, a process that is reversible. We also cloned the cDNA from S. domunculaencoding the retinoid X receptor (RXR), which displays the two motifs of nuclear hormone receptors, the ligand-binding and the DNA-…

DNA ComplementaryRetinoid X receptor; Suberites domuncula; marine spongesCroatiaReceptors Retinoic AcidPhysiologyMolecular Sequence DataRetinoic acidGene ExpressionApoptosisEnzyme-Linked Immunosorbent AssayTretinoinRetinoic acid receptor betaAquatic ScienceRetinoic acid-inducible orphan G protein-coupled receptorchemistry.chemical_compoundAnimalsCluster AnalysisAmino Acid SequenceMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsbiologySequence Analysis DNARetinoic acid receptor gammaBlotting Northernbiology.organism_classificationRetinoid X receptor gammaPoriferaCell biologySuberites domunculaRetinoic acid receptorRetinoid X ReceptorschemistryBiochemistryRetinoic acid receptor alphaInsect ScienceAnimal Science and ZoologySequence AlignmentTranscription FactorsJournal of Experimental Biology
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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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Cloning and expression of a cDNA copy of the viral K28 killer toxin gene in yeast

1995

The killer toxin K28, secreted by certain killer strains of the yeast Saccharomyces cerevisiae is genetically encoded by a 1.9 kb double-stranded RNA, M-dsRNA (M28), that is present within the cell as a cytoplasmically inherited virus-like particle (VLP). For stable maintenance and replication, M28-VLPs depend on a second dsRNA virus (LA), which has been shown to encode the major capsid protein (cap) and a capsid-polymerase fusion protein (cap-pol) that provides the toxin-coding M-satellites with their transcription and replicase functions. K28 toxin-coding M28-VLPs were isolated, purified and used in vitro for the synthesis of the single-stranded M28 transcript, which was shown to be of pl…

DNA ComplementarySaccharomyces cerevisiae ProteinsTranscription GeneticMolecular Sequence DataGene ExpressionRNA-dependent RNA polymeraseSaccharomyces cerevisiaeBiologyOpen Reading FramesTranscription (biology)Complementary DNAGene expressionGeneticsAmino Acid SequenceCloning MolecularProtein PrecursorsMolecular BiologyGeneRNA Double-StrandedBase SequenceSequence Analysis RNANucleic acid sequenceRNARNA FungalDNA-Directed RNA PolymerasesSequence Analysis DNAMycotoxinsMolecular biologyKiller Factors YeastOpen reading frameProtein BiosynthesisNucleic Acid ConformationRNA ViralMolecular and General Genetics MGG
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Tumor suppression inDrosophila is causally related to the function of thelethal(2)tumorous imaginal discs gene, adnaJ homolog

1995

The Drosophila melanogaster tumor suppressor gene lethal(2)tumorous imaginal discs (l(2)tid) causes in homozygotes malignant growth of cells of the imaginal discs and the death of the mutant larvae at the time of puparium formation. We describe the molecular cloning of the l(2)tid+ gene and its temporal expression pattern in the wild-type and mutant alleles. Germ line rescue of the tumor phenotype was achieved with a 7.0 kb Hindlll-fragment derived from the polytene chromosome band 59F5. The l(2)tid+ gene spans approximately 2.5 kb of genomic DNA. The protein coding region, 1,696 bps long, is divided by an intron into two exons. The predicted Tid56 protein contains 518 amino acids and posse…

DNA ComplementarySaccharomyces cerevisiae ProteinsTumor suppressor geneMolecular Sequence DataMutantGenes InsectSaccharomyces cerevisiaeAnimals Genetically ModifiedFungal ProteinsMitochondrial ProteinsSpecies SpecificityEscherichia coliGeneticsAnimalsDrosophila ProteinsHumansGenes Tumor SuppressorAmino Acid SequenceCloning MolecularGeneAllelesHeat-Shock ProteinsPolytene chromosome bandBase SequenceSequence Homology Amino AcidbiologyEscherichia coli ProteinsPupaChromosome MappingExonsNeoplasms ExperimentalCell BiologyHSP40 Heat-Shock Proteinsbiology.organism_classificationMolecular biologyImaginal discDrosophila melanogasterLarvaDNAJA2Drosophila melanogasterSequence AlignmentDrosophila ProteinDevelopmental BiologyDevelopmental Genetics
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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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Structure of MHC class I and class II cDNAs and possible immunodeficiency linked to class II expression in the Mexican axolotl

1998

Despite the fact that the axolotl (Ambystoma spp. a urodele amphibian) displays a large T-cell repertoire and a reasonable B-cell repertoire, its humoral immune response is slow (60 days), non-anamnestic, with a unique IgM class. The cytotoxic immune response is slow as well (21 days) with poor mixed lymphocyte reaction stimulation. Therefore, this amphibian can be considered as immunodeficient. The reason for this subdued immune response could be an altered antigenic presentation by major histocompatibility complex (MHC) molecules. This article summarizes our work on axolotl MHC genes. Class I genes have been characterized and the cDNA sequences show a good conservation of non-polymorphic …

DNA ComplementarySequence analysisGenes MHC Class IIMolecular Sequence DataImmunologyGenes MHC Class IPeptide bindingMajor histocompatibility complexEpitopeAntigenAxolotlMHC class IAnimalsHumansImmunology and AllergyAmino Acid SequenceRNA MessengerGeneticsPolymorphism GeneticBase SequencebiologyHistocompatibility Antigens Class IIbiology.organism_classificationAmbystoma mexicanumbiology.proteinAlpha chainImmunological Reviews
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