Search results for "Peptide sequence"

showing 10 items of 330 documents

Cloning of a cDNA fragment encoding part of the protein moiety of the 58-kDa fibrinogen-binding mannoprotein of Candida albicans

2006

Immunoscreening of a Candida albicans expression library with antibodies against the 58 kDa fibrinogen-binding mannoprotein (mp58) of the fungus resulted in the isolation of clones encoding the protein moiety of this molecule. Sequence of the 0.9 kb cDNA of one of the clones selected for further analysis, revealed an open reading frame coding for 292 amino acids, which displays sequence similarity to proteins belonging to a family of immunodominant antigens of Aspergillus spp. The gene corresponding to this cDNA was named FBP1 (fibrinogen-binding protein). These results represent the first report on the identification of C. albicans genes encoding surface receptors for host proteins.

DNA ComplementaryGenes FungalMolecular Sequence DataSequence alignmentMicrobiologyFungal ProteinsCell WallComplementary DNAImmunoscreeningCandida albicansCell AdhesionGeneticsAmino Acid SequenceCloning MolecularCandida albicansMolecular BiologyPeptide sequenceBase SequenceSequence Homology Amino AcidbiologyFibrinogenFibrinogen bindingbiology.organism_classificationMolecular biologyCorpus albicansMolecular WeightBlotting SouthernOpen reading frameCell Adhesion MoleculesSequence AlignmentFEMS Microbiology Letters
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A frame shift mutation in a hot spot region of the nuclear autoantigen La (SS-B).

1996

A hot spot region was identified in the exon 7 of the nuclear autoantigen La (SS-B). Two La cDNAs were identified which contained a frame shift mutation in the hot spot region. One La cDNA was isolated from a cDNA library made from peripheral blood lymphocytes of an autoimmune patient with primary Sjogren's Syndrome, the other La cDNA was isolated from a human liver cDNA library. The patient's La cDNA had a deletion and the liver La cDNA had an insert of an (A)-residue at the same position. Inserts of 4, 16 and 24 more or less homogeneous (A)-residues were found at the same site in the three La retropseudogenes. The hot spot region located in one of the major autoepitope regions of the La a…

DNA ComplementaryImmunologyMolecular Sequence DataRNA-dependent RNA polymeraseBiologyTransfectionAutoantigensFrameshift mutationExonMiceComplementary DNAImmunology and AllergyAnimalsHumansAmino Acid SequenceRNA MessengerFrameshift MutationPeptide sequenceDNA PrimersMessenger RNABase SequencecDNA library3T3 CellsExonsVirologyMolecular biologyStop codonSjogren's SyndromeRibonucleoproteinsPseudogenesJournal of autoimmunity
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Isolation and cloning of a C-type lectin from the hexactinellid sponge Aphrocallistes vastus: a putative aggregation factor

2001

Among the sponges (Porifera), the oldest group of metazoans in phylogenetic terms, the Hexactinellida is considered to have diverged earliest from the two other sponge classes, the Demospongiae and Calcarea. The Hexactinellida are unusual among all Metazoa in possessing mostly syncytial rather than cellular tissues. Here we describe the purification of a cell adhesion molecule with a size of 34 kDa (in its native form; 24 kDa after deglycosylation) from the hexactinellid sponge Aphrocallistes vastus. This adhesion molecule was previously found to agglutinate preserved cells and membranes in a non-species-specific manner (Müller, W. E. G., Zahn, R. K, Conrad, J., Kurelec, B., and Uhlenbruck,…

DNA ComplementaryMolecular Sequence DataBiologyBiochemistryMicrobiologyCell membraneC-type lectinLectinsmedicineAnimalsLectins C-TypeAmino Acid SequenceCloning MolecularPeptide sequencePhylogenyDNA Primerschemistry.chemical_classificationBase SequenceSequence Homology Amino AcidCell adhesion moleculeLectinbiology.organism_classificationPoriferaAmino acidSpongemedicine.anatomical_structurechemistryBiochemistrybiology.proteinGlycoproteinGlycobiology
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An insect juvenile hormone-specific epoxide hydrolase is related to vertebrate microsomal epoxide hydrolases.

1996

Abstract We describe the first cDNA sequence encoding a juvenile hormone-specific epoxide hydrolase from an insect. A full-length cDNA clone revealed a 462-amino-acid open reading frame encoding an amino acid sequence with 44% identity and 64% similarity to human microsomal epoxide hydrolase. All residues in the catalytic triad (residues Asp 227 -His 428 -Asp 350 in the M. sexta protein) were present, as was the conserved Trp 154 corresponding to the oxyanion hole. The surprising similarity of insect juvenile hormone epoxide hydrolase to vertebrate microsomal epoxide hydrolases, coupled with the ancient lineage of the epoxide hydrolases and haloalkane dehalogenases, suggests that this catab…

DNA ComplementaryMolecular Sequence DataBiophysicsSequence HomologyBiologyBiochemistryPolymerase Chain ReactionMiceOpen Reading FramesComplementary DNAMicrosomesCatalytic triadAnimalsHumansAmino Acid SequenceEpoxide hydrolaseMolecular BiologyPeptide sequenceConserved SequenceEpoxide HydrolasesBase SequenceCell BiologyRatsJuvenile HormonesBiochemistryMicrosomal epoxide hydrolaseEpoxide HydrolasesJuvenile hormoneRabbitsOxyanion holeBiochemical and biophysical research communications
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Cloning and sequencing of the cDNA encoding human glutaredoxin.

1994

Glutaredoxin (thioltransferase) is a small, heat-stable protein, which is involved in thiol/disulfide exchange reactions. We have isolated a cDNA that encodes glutaredoxin from a human brain cDNA library. The encoded protein contains 106 amino acids with a calculated molecular mass of 11.76 kDa and an isoelectric point of 8.09. The amino acid sequence deduced from the cDNA is more than 80% identical to those of other mammalian glutaredoxins.

DNA ComplementaryMolecular Sequence DataBiophysicsSequence alignmentMolecular cloningBiologyBiochemistryStructural BiologyGlutaredoxinComplementary DNAGeneticsHumansAmino Acid SequenceCloning MolecularPeptide sequenceGlutaredoxinschemistry.chemical_classificationBase SequencecDNA libraryNucleic acid sequenceBrainProteinsMolecular biologyAmino acidchemistryBiochemistryOxidoreductasesBiochimica et biophysica acta
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Evolutionary relationships of the metazoan βγ–crystallins, including that from the marine spongeGeodia cydonium

1997

beta gamma-crystallins are one major component of vertebrate lenses. Here the isolation and characterization of a cDNA, coding for the first beta gamma-crystallin molecule from an invertebrate species, the marine sponge Geodia cydonium, is described. The size of the transcript as determined by Northern blotting was 0.7 kb in length. The deduced amino acid sequence consists of 163 aa residues and comprises four repeated motifs which compose the two domains of the beta gamma-crystallin. Motif 3 contains the characteristic beta gamma-crystallin 'Greek key' motif signature, while in each of the three other repeats, one aa residue is replaced by an aa with the same physico-chemical property. The…

DNA ComplementaryMolecular Sequence DataPhysarum polycephalumSequence alignmentPolymerase Chain ReactionGeneral Biochemistry Genetics and Molecular BiologyEvolution MolecularFungal ProteinsPhysarum polycephalumPhylogeneticsComplementary DNAAnimalsHumansAmino Acid SequencePeptide sequencePhylogenyDNA PrimersGene LibraryGeneral Environmental Sciencechemistry.chemical_classificationGeneticsFungal proteinBase SequenceSequence Homology Amino AcidGeneral Immunology and MicrobiologybiologyCoccidioidinGeneral Medicinebiology.organism_classificationCrystallinseye diseasesPoriferaAmino acidSpongechemistryEvolutionary biologysense organsGeneral Agricultural and Biological SciencesSequence AlignmentResearch ArticleProceedings of the Royal Society of London. Series B: Biological Sciences
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Evolutionary relationships of Metazoa within the eukaryotes based on molecular data from Porifera

1999

Recent molecular data provide strong support for the view that all metazoan phyla, including Porifera, are of monophyletic origin. The relationship of Metazoa, including the Porifera, to Plantae, Fungi and unicellular eukaryotes has only rarely been studied by using cDNAs coding for proteins. Sequence data from rDNA suggested a relationship of Porifera to unicellular eukaryotes (choanoflagellates). However, ultrastructural studies of choanocytes did not support these findings. In the present study, we compared amino acid sequences that are found in a variety of metazoans (including sponges) with those of Plantae, Fungi and unicellular eukaryotes, to obtain an answer to this question. We use…

DNA ComplementaryMolecular Sequence DataProtein Serine-Threonine KinasesBiologyGeneral Biochemistry Genetics and Molecular BiologyEvolution MolecularMonophylyCalmodulinTubulinPhylogeneticsAnimalsHSP70 Heat-Shock ProteinsAmino Acid SequenceCloning MolecularPeptide sequencePhylogenyProtein Kinase CDNA PrimersGeneral Environmental ScienceBase SequenceGeneral Immunology and MicrobiologyPhylogenetic treePhylumChoanocytefungiGeneral Medicinebiology.organism_classificationMolecular biologyPoriferaSpongeEukaryotic CellsEvolutionary biologyMolecular phylogeneticsGeneral Agricultural and Biological SciencesResearch ArticleProceedings of the Royal Society of London. Series B: Biological Sciences
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Isolation and characterization of a cDNA encoding a potential morphogen from the marine sponge Geodia cydonium that is conserved in higher metazoans.

1998

Species belonging to the lowest metazoan phylum, the sponges (Porifera), exhibit a surprisingly complex and multifaceted Bauplan (body plan). Recently, key molecules have been isolated from sponges which demonstrate that the cells of these animals are provided with characteristic metazoan adhesion and signal transduction molecules, allowing tissue formation. In order to understand which factors control the spatial organization of these cells in the sponge body plan, we screened for a cDNA encoding a soluble modulator of the behaviour of endothelial cells. A cDNA encoding a putative protein, which is highly similar to the human and mouse endothelial monocyte-activating polypeptide (EMAP) II …

DNA ComplementaryMolecular Sequence DataSequence alignmentGeneral Biochemistry Genetics and Molecular BiologyConserved sequenceMiceComplementary DNAMorphogenesisAnimalsHumansAmino Acid SequencePeptide sequenceCaenorhabditis elegansConserved SequencePhylogenyGeneral Environmental ScienceGeneral Immunology and MicrobiologybiologyProteinsRNA-Binding ProteinsGeneral Medicinebiology.organism_classificationMolecular biologyNeoplasm ProteinsPoriferaSpongeOpen reading frameBiochemistryCosmidCytokinesGeneral Agricultural and Biological SciencesSequence AlignmentResearch ArticleProceedings. Biological sciences
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Key Disulfide Bonds in an Insect Hormone Binding Protein: cDNA Cloning of a Juvenile Hormone Binding Protein of Heliothis virescens and Ligand Bindin…

1995

The hemolymph juvenile hormone binding protein (JHBP) from the early fifth instar larvae of Heliothis virescens (Lepidoptera, Noctuidae) has been purified, and three cDNA clones for this protein have been isolated from a fat body cDNA library constructed in bacteriophage λZAP XR. The deduced amino acid sequence of the full-length clone predicts a mature protein consisting of 224 residues, a molecular mass of 24 976 Da, and a p/ of 5.29. Comparison of the amino acid sequence to that of the previously described JHBP from Manduca sexta shows 51 % overall identity with highly conserved N- and C-terminal regions. One of the three clones bound photoactivatable analogs of juvenile hormones with mu…

DNA ComplementaryPhotochemistryphenylalanineMolecular Sequence DataMutantcomplementary DNAMothsBiochemistryHemolymphComplementary DNAAnimalsAmino Acid SequenceDisulfidesCloning MolecularcysteinePeptide sequencehormone binding proteinhormone analogHormone binding proteinBase SequencePhotoaffinity labelingMolecular massjuvenile hormoneChemistrycDNA libraryAffinity LabelsMolecular biologyJuvenile HormonesBiochemistryLarvaJuvenile hormoneMutagenesis Site-DirectedInsect ProteinsalanineCarrier ProteinsBiochemistry
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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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