Search results for " Homology"

showing 10 items of 633 documents

Vimentin and desmin of a cartilaginous fish, the shark Scyliorhinus stellaris: Sequence, expression patterns and in vitro assembly

2002

In the shark Scyliorhinus stellaris we have biochemically identified and cDNA-cloned orthologs of human vimentin and desmin, SstV and SstD, as deduced from immunoblotting and sequence alignment with teleost, frog and human vimentin and desmin, respectively. This allowed us to further clarify the relationship of previously identified lower vertebrate intermediate filament proteins to mammalian vimentin and desmin. Immunofluorescence microscopy with antibodies H5 and VIM13.2 showed vimentin expression in shark eye and brain and absence in epithelia, which resembles the situation in higher vertebrates. In addition, SstV is expressed in many mesenchymal cell types which corresponds to the case …

HistologyNeurofilamentMolecular Sequence DataIntermediate FilamentsGene ExpressionVimentinmacromolecular substancesDesminPathology and Forensic MedicineEvolution MolecularProtein filamentKeratinAnimalsVimentinIntermediate filamentPhylogenychemistry.chemical_classificationSequence Homology Amino AcidbiologyProtein primary structureCell BiologyGeneral Medicinebiology.organism_classificationMolecular biologyMicroscopy ElectronchemistrySharksbiology.proteinDesminScyliorhinus stellarisEuropean Journal of Cell Biology
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Differentiation capacity of epithelial cells in the sponge Suberites domuncula.

2004

Sponges (phylum Porifera) represent the oldest metazoans. Their characteristic metazoan adhesion molecules and transcription factors enable them to establish a complex "Bauplan" ; three major differentiated cell types (epithelial cells, skeletal cells/sclerocytes, and contractile cells) can be distinguished. Since no molecular markers are as yet available to distinguish these somatic cells or the corresponding embryonic cells from which they originate, we have selected the following three genes for their characterization: noggin (a signaling molecule in development), a caspase that encodes an apoptotic molecule, and silicatein. Silicatein is an enzyme that is involved in the synthesis of si…

HistologySuberites domuncula; sponges; cell differentiationCellular differentiationMolecular Sequence DataPinacodermBiologyPathology and Forensic MedicineEvolution MolecularDemospongeMesohylAnimalsAmino Acid SequenceNogginCloning MolecularPhylogenySclerocyteCell AggregationSequence Homology Amino AcidSilicatesProteinsCell DifferentiationCell BiologyAnatomybiology.organism_classificationCell biologySuberites domunculaSpongeCaspasesCarrier ProteinsSuberitesCell and tissue research
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Zebrafish vimentin: molecular characterization, assembly properties and developmental expression

1998

To provide a basis for the investigation of the intermediate filament (IF) protein vimentin in one of the most promising experimental vertebrate systems, the zebrafish (Danio rerio), we have isolated a cDNA clone of high sequence identity to and with the characteristic features of human vimentin. Using this clone we produced recombinant zebrafish vimentin and studied its assembly behaviour. Unlike other vimentins, zebrafish vimentin formed unusually thick filaments when assembled at temperatures below 21 degrees C. At 37 degrees C few filaments were observed, which often also terminated in aggregated masses, indicating that its assembly was severely disturbed at this temperature. Between 21…

HistologyTroutMolecular Sequence DataCellDanioClone (cell biology)Vimentinmacromolecular substancesPathology and Forensic MedicineMyosinmedicineAnimalsHumansVimentinTissue DistributionAmino Acid SequenceRNA MessengerCloning MolecularIntermediate filamentPeptide sequenceZebrafishZebrafishSequence Homology Amino AcidbiologyTemperatureGene Expression Regulation DevelopmentalCell BiologyGeneral Medicinebiology.organism_classificationImmunohistochemistryMolecular biologyCell biologyMicroscopy Electronmedicine.anatomical_structurebiology.protein
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Algebraic de Rham Cohomology

2017

Let k be a field of characteristic zero. We are going to define relative algebraic de Rham cohomology for general varieties over k, not necessarily smooth.

Hodge conjecturePure mathematicsChern–Weil homomorphismMathematics::K-Theory and HomologyGroup cohomologyCyclic homologyDe Rham cohomologyEquivariant cohomologyMathematics::Algebraic TopologyCohomologyMathematicsMotivic cohomology
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Sponge Bcl-2 homologous protein (BHP2-GC) confers distinct stress resistance to human HEK-293 cells

2001

It is established that sponges, the phylogenetically oldest still extant phylum of Metazoa, possess key molecules of the apoptotic pathways, that is members from the Bcl-2 family and a pro-apoptotic molecule with death domains. Here we report on transfection studies of human cells with a sponge gene, GCBHP2. Sponge tissue was exposed to heat shock and tributyltin, which caused an upregulation of gene expression of GCBHP2. The cDNA GCBHP2 was introduced into human HEK-293 cells and mouse NIH-3T3 cells; the stable transfection was confirmed by the identification of the transcripts, by Western blotting as well as by immunofluorescence using antibodies raised against the recombinant polypeptide…

Hot Temperatureanimal structuresCell SurvivalvirusesMolecular Sequence DataDrug ResistanceApoptosisAntibodiesCell LineMiceComplementary DNAGene expressionAnimalsHumansAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyPhylogenySequence Homology Amino AcidbiologyCaspase 3ChemistryfungiHEK 293 cellsCell BiologyTransfectionbiology.organism_classificationMolecular biologyPoriferaProtein Structure TertiaryUp-RegulationEnzyme ActivationBlotSpongeProto-Oncogene Proteins c-bcl-2Cell cultureCaspasesembryonic structuresbiology.proteinTrialkyltin CompoundsAntibodySequence AlignmentHeat-Shock ResponseCell Death & Differentiation
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Genetic rearrangement of the atzAB atrazine-degrading gene cassette from pADP1::Tn5 to the chromosome of Variovorax sp. MD1 and MD2

2007

International audience; We report the characterization of the rearrangement phenomena responsible for the movement of the atrazine-degrading atzA and B genes from pADP1::Tn5 to the chromosome of Variovorax sp. MD1 and MD2. Long PCRs and Southern blot analyses revealed that the two genes forming a gene cassette moved in a unique rearrangement event. It also revealed that the boundaries of the plasmid sequence inserted in the chromosome correspond to IS1071or to sequences close to IS1071. It suggests that this genetic rearrangement could result from the transposition of the composite transposon delimited by IS1071 insertion sequences and containing atzA and atzB genes. In addition, for MD1 an…

HydrolasesATRAZINEMolecular Sequence DataTransposasesBiologyTranslocation GeneticHOMOLOGOUS RECOMBINATION03 medical and health sciencesPlasmidSequence Homology Nucleic AcidGeneticsInsertion sequenceGeneTransposase030304 developmental biologySouthern blotGenetics0303 health sciences[SDV.GEN]Life Sciences [q-bio]/GeneticsBase Sequence030306 microbiologyGeneral MedicineChromosomes BacterialMolecular biologyGene cassetteComposite transposonAgrobacterium tumefaciensGenes BacterialATZ GENEINSERTION SEQUENCETRANSPOSITIONTransformation BacterialHomologous recombinationVARIOVORAX SPECIES
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Mutilation of RNA phage Qβ virus-like particles: from icosahedrons to rods

2000

Icosahedral virus-like particles (VLPs) of RNA phage Qbeta are stabilized by four disulfide bonds of cysteine residues 74 and 80 within the loop between beta-strands F and G (FG loop) of the monomeric subunits, which determine the five-fold and quasi-six-fold symmetry contacts of the VLPs. In order to reduce the stability of Qbeta VLPs, we mutationally converted the amino acid stretch 76-ANGSCD-81 within the FG loop into the 76-VGGVEL-81 sequence. It led to production in Escherichia coli cells of aberrant rod-like Qbeta VLPs, along with normal icosahedral capsids. The length of the rod-like particles exceeded 4-30 times the diameter of icosahedral Qbeta VLPs.

Icosahedral symmetryvirusesGenetic VectorsMolecular Sequence DataBiophysicsBiologymedicine.disease_causecomplex mixturesBiochemistryVirus-like particleStructural BiologyGeneticsmedicineAmino Acid SequenceCysteineMolecular BiologyEscherichia coliPeptide sequenceIcosahedronAlloleviviruschemistry.chemical_classificationSequence Homology Amino AcidRod-like structureVirionvirus diseasesRNASelf-assemblyCell Biologybiochemical phenomena metabolism and nutritionAmino acidCrystallographyCapsidchemistryMutagenesis Site-DirectedRNA ViralRNA phage QβVirus-like particleCysteineFEBS Letters
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Sodium Solute Symporter and Cadherin Proteins Act as Bacillus thuringiensis Cry3Ba Toxin Functional Receptors in Tribolium castaneum*

2013

Understanding how Bacillus thuringiensis (Bt) toxins interact with proteins in the midgut of susceptible coleopteran insects is crucial to fully explain the molecular bases of Bt specificity and insecticidal action. In this work, aminopeptidase N (TcAPN-I), E-cadherin (TcCad1), and sodium solute symporter (TcSSS) have been identified by ligand blot as putative Cry3Ba toxin-binding proteins in Tribolium castaneum (Tc) larvae. RNA interference knockdown of TcCad1 or TcSSS proteins resulted in decreased susceptibility to Cry3Ba toxin, demonstrating the Cry toxin receptor functionality for these proteins. In contrast, TcAPN-I silencing had no effect on Cry3Ba larval toxicity, suggesting that th…

ImmunoblottingMolecular Sequence DataReceptors Cell SurfacePlasma protein bindingBiologyCD13 Antigensmedicine.disease_causeBiochemistrySodium-solute symporterdigestive systemMicrobiologyEpitopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensisparasitic diseasesmedicineAnimalsAmino Acid SequenceReceptorMolecular BiologyPeptide sequenceTriboliumBinding SitesBacillus thuringiensis ToxinsSequence Homology Amino AcidSymportersCadherinToxinfungiSodiumCell Biologybiology.organism_classificationCadherinsEndotoxinsBiochemistrySymporterbacteriaInsect ProteinsRNA InterferenceProtein Binding
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Molecular basis of filamin a-filGAP interaction and its impairment in congenital disorders associated with filamin a mutations

2008

Background Mutations in filamin A (FLNa), an essential cytoskeletal protein with multiple binding partners, cause developmental anomalies in humans. Methodology/Principal Findings We determined the structure of the 23rd Ig repeat of FLNa (IgFLNa23) that interacts with FilGAP, a Rac-specific GTPase-activating protein and regulator of cell polarity and movement, and the effect of the three disease-related mutations on this interaction. A combination of NMR structural analysis and in silico modeling revealed the structural interface details between the C and D β-strands of the IgFLNa23 and the C-terminal 32 residues of FilGAP. Mutagenesis of the predicted key interface residues confirmed the b…

ImmunoprecipitationFilaminsMolecular Sequence Dataeducationlcsh:MedicineComputational Biology/Protein Structure PredictionBiologyFilaminCell Biology/Cell SignalingCongenital AbnormalitiesBiochemistry/Protein Folding03 medical and health sciences0302 clinical medicineProtein structureContractile ProteinsCell Biology/CytoskeletonFLNAHumansFLNBFLNCAmino Acid Sequencelcsh:Science030304 developmental biologyGenetics0303 health sciencesMultidisciplinaryBinding SitesMolecular StructureSequence Homology Amino AcidPoint mutationlcsh:RGTPase-Activating ProteinsMicrofilament Proteins3. Good healthBiochemistry/BioinformaticsMutationProtein foldinglcsh:Q118 Biological sciences030217 neurology & neurosurgeryResearch Article
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Quaternary and subunit structure of Calliphora arylphorin as deduced from electron microscopy, electrophoresis, and sequence similarities with arthro…

1992

Arylphorin was purified from larvae of the blowfly Calliphora vicina and studied in its oligomeric form and after dissociation at pH 9.6 into native subunits. In accordance with earlier literature, it was electrophoretically shown to be a 500 kDa hexamer (1 x 6) consisting of 78 kDa polypeptides (= subunits). Electron micrographs of negatively stained hexamers show a characteristic curvilinear, equilateral triangle of 12 nm in diameter (top view) and a rectangle measuring 10 x 12 nm (side view). Alternatively, particles in the top view orientation exhibit a roughly circular shape 12 nm in diameter. Crossed immunoelectrophoresis revealed the presence of a major subunit type; the nature of a …

Insectaanimal structuresCalliphora vicinaProtein ConformationPhysiologyStereochemistryProtein subunitmedicine.medical_treatmentMolecular Sequence DataBiologyRandom hexamerBiochemistryCalliphoraEndocrinologyHemolymphmedicineAnimalsAmino Acid SequenceEcology Evolution Behavior and SystematicsGlycoproteinsSequence Homology Amino AcidProtein primary structureSpidersHemocyaninbiology.organism_classificationNephropidaeMicroscopy ElectronBiochemistryInsect HormonesLarvaHemocyaninsInsect ProteinsElectrophoresis Polyacrylamide GelAnimal Science and ZoologyProtein quaternary structureJournal of Comparative Physiology B
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