Search results for "fusion [photon photon]"

showing 10 items of 724 documents

Isolation of carcinoembryonic antigen N-terminal domains (N-A1) from soluble aggregates

2011

Abstract Carcinoembryonic antigen (CEA) was identified as a prominent tumor-associated antigen in human colorectal cancer and it is still intensively investigated. However, its physiological role remains unclear. The CEA molecule is composed of seven highly hydrophobic, immunoglobulin-like domains, six of which contain a single disulphide bridge. The production of recombinant protein containing Ig-like domains in bacterial expression systems often results in partial degradation or insolubility due to aggregation hampering the analysis of their native structure and function. Here, we present a new method of expression and purification of CEA N-terminal domains (N-A1) fused to MBP in Escheric…

Guanidinium chlorideCircular dichroismRecombinant Fusion Proteinsmedicine.disease_causeMaltose-Binding Proteinslaw.inventionchemistry.chemical_compoundCarcinoembryonic antigenlawProtein purificationEscherichia colimedicineTEV proteaseHumansDisulfidesEscherichia coliGuanidinebiologyProtein StabilityCircular DichroismFusion proteinCarcinoembryonic AntigenProtein Structure TertiarySolubilitychemistryBiochemistryChromatography GelRecombinant DNAbiology.proteinElectrophoresis Polyacrylamide GelBiotechnologyProtein Expression and Purification
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A constitutive model for the thermo-mechanical behaviour of fusion-relevant pebble beds and its application to the simulation of HELICA mock-up exper…

2007

Abstract Within the framework of the R&D activities promoted by EFDA on the Helium-Cooled Pebble Bed Test Blanket Module to be irradiated in ITER, attention has been focused on the modelling of the thermo-mechanical behaviour of both beryllium and lithiated ceramic pebble beds that are envisaged to be used respectively as neutron multiplier and tritium breeder. This behaviour depends, mainly, on the reactor-relevant conditions, the pebble sizes and the breeder cell geometries and a general constitutive model has not yet been validated, especially for fusion-relevant applications. ENEA-Brasimone and the Department of Nuclear Engineering (DIN) of the University of Palermo have performed inten…

HCPB–TBMFusionMaterials scienceLithiated ceramic breederPebble-bed reactorMechanical EngineeringNuclear engineeringConstitutive equationThermo-mechanical constitutive modelBlanketFusion powerNuclear Energy and EngineeringMockupPebble bedGeneral Materials SciencePebbleThermo mechanicalSettore ING-IND/19 - Impianti NucleariCivil and Structural Engineering
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Behavior of a Short preS1 Epitope on the Surface of Hepatitis B Core Particles

1999

The major immunodominant region of hepatitis B core particles is widely recognized as the most prospective target for the insertion of foreign epitopes, ensuring their maximal antigenicity and immunogenicity. This region was mapped around amino acid residues 79-81, which were shown by electron cryo-microscopy to be located on the tips of the spikes protruding from the surface of hepatitis B core shells. Here we tried to expose a model sequence, the short immunodominant hepatitis B preS1 epitope 31-DPAFR-35, onto the tip of the spike, with simultaneous deletion of varying stretches from the major immunodominant region of the HBc molecule. Accessibility to the monoclonal anti-preS1 antibody M…

Hepatitis B virusAntigenicityRecombinant Fusion ProteinsGenetic VectorsMolecular Sequence DataClinical BiochemistryAntigen presentationmedicine.disease_causeBiochemistryEpitopeMicemedicineAnimalsHumansAmino Acid SequenceProtein PrecursorsMolecular BiologyPeptide sequenceHepatitis B virusAntigen PresentationMice Inbred BALB CHepatitis B Surface AntigensbiologyImmunodominant EpitopesChemistryImmunogenicityHepatitis B Core AntigensVirologyPolyclonal antibodiesbiology.proteinEpitopes B-LymphocyteFemaleRabbitsAntibodyPlasmidsBiological Chemistry
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Mosaic hepatitis B virus core particles presenting the complete preS sequence of the viral envelope on their surface

2004

The sequence of the preS domain of the hepatitis B virus (HBV, genotype D) envelope was inserted into the major immunodominant region (MIR) of the C-terminally truncated HBV core (HBc) protein. In Escherichia coli, the HBc–preS fusion protein was partially soluble and did not produce particles. Co-expression of the wild-type HBc as a helper protein along with the fusion protein led to the formation of mosaic HBc particles that exhibited HBc, preS1 and preS2 antigenicity. Two alternative combinations of medium- and high-copy plasmids were used for co-expression of fusion and helper proteins, in an attempt to improve mosaic particle production. However, the preS fusion content of the particle…

Hepatitis B virusAntigenicityvirusesAntibodies ViralProtein Engineeringmedicine.disease_causeVirusMiceViral Envelope ProteinsOrthohepadnavirusViral envelopeVirologyEscherichia colimedicineAnimalsProtein PrecursorsHepatitis B virusHepatitis B Surface AntigensbiologyViral Core Proteinsvirus diseasesProtein engineeringHepatitis Bbiology.organism_classificationVirologyFusion proteindigestive system diseasesHepadnaviridaeFemaleImmunizationReassortant VirusesPlasmidsJournal of General Virology
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Sequence-Specific Repression of Cotranslational Translocation of the Hepatitis B Virus Envelope Proteins Coincides with Binding of Heat Shock Protein…

1997

AbstractThe large L envelope protein of the hepatitis B virus has the peculiar capacity to adopt two transmembrane topologies. The N-terminal preS domain of L initially remains in the cytosol while the S domain is cotranslationally inserted into the endoplasmic reticulum membrane. The preS region of about half of the L molecules is posttranslationally translocated to the lumenal space. We now demonstrate that the repression of cotranslational translocation of preS is conferred by a preS1-specific sequence. By analysis of L deletion mutants, the cytosolic anchorage determinant was mapped to amino acid sequence 70 to 94 of L. The intrinsic potential of this determinant to suppress cotranslati…

Hepatitis B virusHSC70 Heat-Shock ProteinsRecombinant Fusion ProteinsPlasma protein bindingBiologyGenes envCytosolViral Envelope ProteinsHeat shock proteinVirologyHumansHSP70 Heat-Shock ProteinsBinding sitePromoter Regions GeneticPeptide sequenceBinding SitesBase SequenceCell-Free SystemEndoplasmic reticulumHSC70 Heat-Shock ProteinsOligonucleotides AntisenseMolecular biologyTransmembrane proteinChaperone (protein)Protein Biosynthesisbiology.proteinMutagenesis Site-DirectedMetallothioneinCarrier ProteinsProtein BindingVirology
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Stop codon insertion restores the particle formation ability of hepatitis B virus core-hantavirus nucleocapsid protein fusions.

2003

In recent years, epitopes of various origin have been inserted into the core protein of hepatitis B virus (HBc), allowing the formation of chimeric HBc particles. Although the C-terminus of a C-terminally truncated HBc (HBcΔ) tolerates the insertion of extended foreign sequences, the insertion capacity is still a limiting factor for the construction of multivalent vaccines. Previously, we described a new system to generate HBcΔ mosaic particles based on a read-through mechanism in an <i>Escherichia coli</i> suppressor strain [J Gen Virol 1997;78:2049–2053]. Those mosaic particles allowed the insertion of a 114-amino acid (aa)-long segment of a Puumala hantavirus (PUUV) nucleocap…

Hepatitis B virusHepatitis B virus DNA polymerasevirusesRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeEpitopeHepatitis B virus PRE betaMiceVirologyparasitic diseasesmedicineAnimalsNucleocapsidHantavirusHepatitis B virusMice Inbred BALB CBase SequenceChemistryHepatitis B virus coreVirionvirus diseasesNucleocapsid ProteinsVirologyMolecular biologyHepatitis B Core Antigensdigestive system diseasesStop codonNS2-3 proteaseInfectious DiseasesCodon TerminatorImmunizationIntervirology
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Functional incorporation of green fluorescent protein into hepatitis B virus envelope particles

2004

AbstractThe envelope of hepatitis B virus (HBV), containing the L, M, and S proteins, is essential for virus entry and maturation. For direct visualization of HBV, we determined whether envelope assembly could accommodate the green fluorescent protein (GFP). While the C-terminal addition of GFP to S trans-dominant negatively inhibited empty envelope particle secretion, the N-terminal GFP fusion to S (GFP.S) was co-integrated into the envelope, giving rise to fluorescent particles. Microscopy and topogenesis analyses demonstrated that the proper intracellular distribution and folding of GFP.S, required for particle export were rescued by interprotein interactions with wild-type S. Thereby, a…

Hepatitis B virusRecombinant Fusion ProteinsGreen Fluorescent ProteinsRestriction MappingEnzyme-Linked Immunosorbent AssayBiologyTransfectionmedicine.disease_causeHBsAg particlesArticleViral envelopeGreen fluorescent proteinViral Envelope ProteinsViral envelopeViral entryVirologyChlorocebus aethiopsmedicineAnimalsHumansGreen fluorescent proteinSecretionPromoter Regions GeneticHepatitis B virusCOS cellsfungiTransfectionMolecular biologyCell biologyKineticsCOS CellsMetallothioneinVirus assembly and secretionProtein KinasesIntracellularVirology
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Activation of oligodendroglial Fyn kinase enhances translation of mRNAs transported in hnRNP A2-dependent RNA granules.

2008

Central nervous system myelination requires the synthesis of large amounts of myelin basic protein (MBP) at the axon–glia contact site. MBP messenger RNA (mRNA) is transported in RNA granules to oligodendroglial processes in a translationally silenced state. This process is regulated by the trans-acting factor heterogeneous nuclear ribonucleoprotein (hnRNP) A2 binding to the cis-acting A2 response element (A2RE). Release of this repression of MBP mRNA translation is thus essential for myelination. Mice deficient in the Src family tyrosine kinase Fyn are hypomyelinated and contain reduced levels of MBP. Here, we identify hnRNP A2 as a target of activated Fyn in oligodendrocytes. We show that…

Heterogeneous nuclear ribonucleoproteinCell Adhesion Molecules NeuronalRecombinant Fusion ProteinsBiologyHeterogeneous ribonucleoprotein particleCytoplasmic GranulesProto-Oncogene Proteins c-fynResponse Elementsenvironment and public healthRNA TransportCell LineMiceFYNContactinsGenes ReporterReportHeterogeneous-Nuclear Ribonucleoprotein Group A-BProtein biosynthesisAnimalsRNA MessengerPhosphorylationLuciferasesNeural Cell Adhesion MoleculesResearch ArticlesMessenger RNARNATranslation (biology)Cell BiologyMolecular biologyMyelin basic proteinEnzyme ActivationOligodendroglianervous systemProtein Biosynthesisbiology.proteinProtein BindingThe Journal of cell biology
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Dissection of keratin dynamics: different contributions of the actin and microtubule systems.

2005

It has only recently been recognized that intermediate filaments (IFs) and their assembly intermediates are highly motile cytoskeletal components with cell-type- and isotype-specific characteristics. To elucidate the cell-type-independent contribution of actin filaments and microtubules to these motile properties, fluorescent epithelial IF keratin polypeptides were introduced into non-epithelial, adrenal cortex-derived SW13 cells. Time-lapse fluorescence microscopy of stably transfected SW13 cell lines synthesizing fluorescent human keratin 8 and 18 chimeras HK8-CFP and HK18-YFP revealed extended filament networks that are entirely composed of transgene products and exhibit the same dynamic…

HistologyRecombinant Fusion ProteinsArp2/3 complexAntineoplastic Agentsmacromolecular substancesBiologyMicrotubulesPathology and Forensic MedicineGenes ReporterKeratinHumansIntermediate filamentCytoskeletonchemistry.chemical_classificationKeratin FilamentNocodazoleActin remodelingCell BiologyGeneral MedicineBridged Bicyclo Compounds HeterocyclicActinsCell biologyActin CytoskeletonProtein TransportThiazoleschemistryMicroscopy Fluorescencebiology.proteinKeratin 8KeratinsThiazolidinesLamellipodiumEuropean journal of cell biology
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In vivo detection of cytokeratin filament network breakdown in cells treated with the phosphatase inhibitor okadaic acid.

2001

We have previously described vulva carcinoma-derived A-431 subclone AK13-1, which stably expresses fluorescently labeled cytokeratin filaments (CKFs). Time-lapse fluorescence microscopy of these cells permits the continuous monitoring of the dynamics of the CKF cytoskeleton in vivo. To study mechanisms and principles of CKF disassembly as it occurs, e.g., during mitosis and liver disease, we have treated cells with the phosphatase inhibitor okadaic acid (OA), which induces complete CKF network breakdown within 3–5 h without significantly affecting the organization of the actin- and tubulin-based cytofilaments. In time-lapse movies, we find that the network breakdown starts at the cell perip…

HistologyTime FactorsRecombinant Fusion ProteinsGreen Fluorescent ProteinsPathology and Forensic Medicinechemistry.chemical_compoundCytokeratinAdenosine TriphosphateStress FibersOkadaic AcidFluorescence microscopeTumor Cells CulturedHumansEnzyme InhibitorsPhosphorylationCytoskeletonMitosisActinCytoskeletonbiologyVulvar NeoplasmsEpithelial CellsCell BiologyOkadaic acidCell biologyCytoskeletal ProteinsLuminescent ProteinsTubulinchemistryDesmoplakinsMicroscopy FluorescenceCytoplasmbiology.proteinKeratinsFemaleIndicators and ReagentsCell and tissue research
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