Search results for "sequence data"

showing 10 items of 1952 documents

Cross-Reactivity of Antibodies Immunoadsorbed to Laminin with Recombinant Human La (SS-B) Protein

1998

Anti-La (SS-B) antibodies cross-reacting with mouse B1 laminin were reported in sera of patients with systemic lupus erythematosus. However, the common epitope had not been characterized. Immunoblotting conditions were established, allowing detection and elution of anti-La (SS-B)/laminin cross-reacting antibodies. Antibodies adsorbed to mouse B1 laminin represented a subclass of anti-La antibodies. They strongly reacted with human full length recombinant La protein. However, they failed to react with either an N-terminal La peptide consisting of amino acids 1-192 or a C-terminal La peptide starting at methionine 223, while they still reacted with recombinant La peptides consisting of the am…

Recombinant Fusion ProteinsMolecular Sequence DataImmunologyPeptideCross ReactionsBiologyAutoantigensEpitopeAutoimmune Diseaseslaw.inventionEpitopesMiceSpecies SpecificityAntigenAntibody SpecificitylawLamininConsensus SequenceAnimalsHumansImmunology and AllergyAmino Acid SequenceElméleti orvostudományokPeptide sequenceImmunosorbent TechniquesAutoantibodieschemistry.chemical_classificationOrvostudományokMolecular biologyPeptide FragmentsAmino acidRibonucleoproteinschemistryRecombinant DNAbiology.proteinKidney DiseasesLamininAntibodyJournal of Autoimmunity
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The yeast putative transcriptional repressor RGM1 is a proline-rich zinc finger protein.

1991

Abstract I have cloned a yeast gene, RGM1, which encodes a proline-rich zinc, finger protein. rgm1 mutants do not show any obvious phenotype but overexpression of RGM1 gene greatly impairs cell growth. The proline-rich region of RGM1 attached to a heterologous DNA binding domain is able to repress the expression of the target gene. RGM1 shares similar zinc finger motifs with the mammalian Egr (early growth response) proteins as well as proline-rich sequences with a high serine and threonine content, suggesting that RGM1 and Egr proteins could have functional similarities.

Recombinant Fusion ProteinsMolecular Sequence DataRestriction MappingGene ExpressionSaccharomyces cerevisiaeBiologyZIC2TransfectionSequence Homology Nucleic AcidGene expressionGeneticsAmino Acid SequenceCloning MolecularLIM domainSIN3BZinc fingerBase SequenceZinc FingersDNA-binding domainZinc finger nucleaseRING finger domainbody regionsRepressor ProteinsBiochemistryMutagenesisCarbohydrate MetabolismPlasmidsNucleic acids research
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The Tobacco mosaic virus movement protein associates with but does not integrate into biological membranes

2014

Plant positive-strand RNA viruses require association with plant cell endomembranes for viral translation and replication, as well as for intra- and intercellular movement of the viral progeny. The membrane association and RNA binding of the Tobacco mosaic virus (TMV) movement protein (MP) are vital for orchestrating the macromolecular network required for virus movement. A previously proposed topological model suggests that TMV MP is an integral membrane protein with two putative -helical transmembrane (TM) segments. Here we tested this model using an experimental system that measured the efficiency with which natural polypeptide segments were inserted into the ER membrane under conditions…

Recombinant Fusion ProteinsvirusesMolecular Sequence DataImmunologyGene ExpressionMicrobiologiaBiologyEndoplasmic ReticulumMicrobiologyCell membraneGenes ReporterPlant CellsVirologymedicineTobacco mosaic virusAmino Acid SequenceMovement proteinIntegral membrane proteinStructure and AssemblyCell MembraneViral translationfungifood and beveragesBiological membraneVirologyTransmembrane proteinTransport proteinCell biologyVirusPlant Viral Movement ProteinsTobacco Mosaic VirusProtein Transportmedicine.anatomical_structureInsect ScienceHydrophobic and Hydrophilic InteractionsProtein Binding
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Production of biologically active light chain of tetanus toxin inEscherichia coli

1993

AbstractThe activity of the light (L) chain of tetanus toxin, and of mutants constructed by site-directed mutagenesis, was studied by expression and purification of the proteins from E. coli. Wild-type recombinant L chain (pTet87) was active in the inhibition of exocytosis from cultured bovine adrenal chromaffin cells, although at a level 5–15% of that of L chain purified from tetanus toxin. L chain mutants which terminated at Leu-438 (pTet89), or which contained a Cys-to-Ser mutation at residue 439 (pTet88) were equally as active as the full-length recombinant protein. The reduced activity of pTet87 L chain correlated with C-terminal proteolysis of the protein upon purification. A tryptic …

Recombinant proteinMacromolecular SubstancesProteolysisMolecular Sequence DataRestriction MappingDNA RecombinantBiophysicsBiologymedicine.disease_causeImmunoglobulin light chainBiochemistryExocytosislaw.inventionNorepinephrineTetanus ToxinStructural BiologylawEscherichia coliGeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularSite-directed mutagenesisMolecular BiologyEscherichia coliCells Culturedchemistry.chemical_classificationBase Sequencemedicine.diagnostic_testToxinBiological activityCell BiologyMolecular biologyRecombinant ProteinsE. coli Chromaffin cellAmino acidKineticsOligodeoxyribonucleotideschemistryBiochemistryAdrenal MedullaMutagenesis Site-DirectedRecombinant DNACalciumCattleElectrophoresis Polyacrylamide GelSite directed mutagenesisFEBS Letters
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DRB1*0401-restricted human T cell clone specific for the major proinsulin73-90 epitope expresses a down-regulatory T helper 2 phenotype.

2006

Recently, we have identified proinsulin (P-Ins) 73-90 as an immunodominant T cell epitope of HLA-DRB1*0401 (DR4) subjects with β-islet cell autoimmunity and of HLA-DR4/CD4 double-transgenic mice immunized with human P-Ins. We have compared the fine specificities of one human CD4 T cell clone and two mouse T cell hybridoma clones recognizing this epitope, and, although these three clones all recognized the same core region (LALEGSLQK), there were major differences in how they interacted with the peptide (p)/HLA complex, reflecting the fact that human P-Ins is a foreign antigen in the mouse and an autoantigen in the type 1 diabetes patient. The human T cell clone was forkhead transcription f…

Regulatory T cellT cellT-LymphocytesMolecular Sequence DataClone (cell biology)Mice TransgenicHuman leukocyte antigenBiologyEpitopeEpitopesMiceAntigenT-Lymphocyte SubsetsmedicineCytotoxic T cellAnimalsHumansAmino Acid SequenceAmino AcidsMultidisciplinaryFOXP3Forkhead Transcription FactorsHLA-DR AntigensBiological SciencesMolecular biologyPeptide Fragmentsmedicine.anatomical_structurePhenotypeHLA-DRB1 ChainsProinsulinProceedings of the National Academy of Sciences of the United States of America
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Mapping and structure of DMXL1, a human homologue of the DmX gene from Drosophila melanogaster coding for a WD repeat protein.

2000

The DmX gene was recently isolated from the X chromosome of Drosophila melanogaster. TBLASTN searches of the dbEST databases revealed sequences with a high level of similarity to DmX in a variety of different species, including insects, nematodes, and mammals showing that DmX is an evolutionarily highly conserved gene. Here we describe the cloning of the cDNA and the chromosomal localization of one of the human homologues of DmX, Dmx-like 1 (DMXL1). The human DMXL1 gene codes for a large mRNA of 11 kb with an open reading frame of 3027 amino acids. The putative protein belongs to the superfamily of WD repeat proteins, which have mostly regulatory functions. The DMXL1 protein contains an exc…

Repetitive Sequences Amino AcidDNA ComplementaryMolecular Sequence DataBiologyConserved sequenceMiceGene mappingComplementary DNAGeneticsAnimalsDrosophila ProteinsHumansRadiation hybrid mappingAmino Acid SequenceDinucleotide RepeatsGeneIn Situ Hybridization FluorescenceGeneticsBase SequenceChromosome MappingProteinsbiology.organism_classificationOpen reading frameDrosophila melanogasterChromosomes Human Pair 5Insect ProteinsDrosophila melanogasterDrosophila ProteinGenomics
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ZFWD: a novel subfamily of plant proteins containing a C3H zinc finger and seven WD40 repeats

2000

We describe a new subfamily of WD repeat proteins characterised by the presence of a C3H zinc finger at the N-terminal part of the protein associated with seven WD40 repeats. We have identified four members of this subfamily in Arabidopsis thaliana, one of them with associated expressed sequence tags (ESTs). We have also identified homologous ESTs in rice, cotton, maize, poplar, pine tree and the ice plant. We do not observe animal homologues, suggesting that this subfamily could be specific for plants. Our data suggest an important role for these proteins. Based on the high sequence conservation within the conserved domains, we suggest that these proteins could have a regulatory function.

Repetitive Sequences Amino AcidDNA ComplementarySubfamilyDNA PlantMolecular Sequence DataArabidopsisSequence alignmentBiologyEvolution MolecularWD40 repeatGeneticsProtein IsoformsArabidopsis thalianaAmino Acid SequencePeptide sequencePhylogenyPlant ProteinsExpressed Sequence TagsGeneticsZinc fingerExpressed sequence tagProtein subfamilySequence Homology Amino AcidArabidopsis Proteinsfungifood and beveragesZinc FingersSequence Analysis DNAGeneral Medicinebiology.organism_classificationSequence AlignmentGene
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Stimulation of protein (collagen) synthesis in sponge cells by a cardiac myotrophin‐related molecule from Suberites domuncula

2000

The body wall of sponges (Porifera), the lowest metazoan phylum, is formed by two epithelial cell layers of exopinacocytes and endopinacocytes, both of which are associated with collagen fibrils. Here we show that a myotrophin-like polypeptide from the sponge Suberites domuncula causes the expression of collagen in cells from the same sponge in vitro. The cDNA of the sponge myotrophin was isolated; the potential open reading frame of 360 nt encodes a 120 aa long protein (Mr of 12,837). The sequence SUBDOMYOL shares high similarity with the known metazoan myotrophin sequences. The expression of SUBDOMYOL is low in single cells but high after formation of primmorph aggregates as well as in in…

Repetitive Sequences Amino AcidMolecular Sequence DataLysinePolymerase Chain ReactionBiochemistryMyotrophinComplementary DNAGeneticsProtein biosynthesisAnimalsAmino Acid SequenceCloning MolecularGrowth SubstanceseducationMolecular BiologyPhylogenyCell Sizeeducation.field_of_studyDose-Response Relationship DrugSequence Homology Amino AcidbiologySequence Analysis DNAbiology.organism_classificationRecombinant ProteinsIn vitroPoriferaUp-RegulationCell biologySuberites domunculaOpen reading frameSpongeIntercellular Signaling Peptides and ProteinsCollagenBiotechnologyThe FASEB Journal
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Tumor-Associated MUC1 Tandem-Repeat Glycopeptide Microarrays to Evaluate Serum- and Monoclonal-Antibody Specificity

2009

Repetitive Sequences Amino Acidmedicine.drug_classMolecular Sequence DataMonoclonal antibodyCatalysisMiceTandem repeatAntibody SpecificityNeoplasmsmedicineAnimalsAmino Acid SequencePeptide sequenceMUC1biologyMicroarray analysis techniquesChemistryImmune SeraMucin-1GlycopeptidesAntibodies MonoclonalGeneral MedicineGeneral ChemistryMicroarray AnalysisMolecular biologyGlycopeptideBiochemistrybiology.proteinAntibodyDNA microarrayAngewandte Chemie International Edition
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The putative sponge aggregation receptor. Isolation and characterization of a molecule composed of scavenger receptor cysteine-rich domains and short…

1998

Porifera (sponges) are the oldest extant metazoan phylum. Dissociated sponge cells serve as a classic system to study processes of cell reaggregation. The reaggregation of dissociated cells is mediated by an extracellularly localized aggregation factor (AF), based on heterophilic interactions of the third order; the AF bridges two cells by ligating a cell-surface-bound aggregation receptor (AR). In the present study we report cloning, expression and immunohistochemical localization of a polypeptide from the marine sponge Geodia cydonium, which very likely represents the AR. The presumed AR gene gives rise to at least three forms of alternatively spliced transcripts of 6.5, 4.9 and 3.9 kb, a…

Repetitive Sequences Amino Acidmedicine.drug_classMolecular Sequence DataReceptors Cell SurfaceCell CommunicationMonoclonal antibodyPolymerase Chain Reactionlaw.inventionAntigenlawComplementary DNAConsensus SequencemedicineAnimalsAmino Acid SequenceCloning MolecularReceptors ImmunologicReceptorCell AggregationReceptors LipoproteinRepetitive Sequences Nucleic AcidReceptors ScavengerbiologyMolecular massBase SequenceSequence Homology Amino AcidMembrane ProteinsCell BiologySequence Analysis DNAScavenger Receptors Class BMolecular biologyRecombinant ProteinsPoriferaTransmembrane domainBiochemistrybiology.proteinRecombinant DNAAntibodyProtein Binding
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