Search results for "Microscopy"

showing 10 items of 3390 documents

Small-angle X-ray scattering reveals differences between the quaternary structures of oxygenated and deoxygenated tarantula hemocyanin

1996

Small-angle X-ray scattering (SAXS) curves have been recorded for the oxygenated and deoxygenated states of the 4 x 6-meric hemocyanin from the tarantula Eurypelma californicum. A comparison of the curves shows that the quaternary structures of the two states are different by three criteria, which all indicate that the hemocyanin is less compact in the oxygenated compared to the deoxygenated form: (a) The radius of gyration is 8.65 +/- 0.05 nm for the deoxy- and 8.80 +/- 0.05 nm for the oxy-form. (b) The maximum particle dimension amounts to 25.0 +/- 0.5 nm for the deoxy- and to 27.0 +/- 0.5 nm for the oxy-form. (c) A dip in the intramolecular distance distribution function p(r) is more pro…

Protein Conformationmedicine.medical_treatmentBiophysicsElectronBiochemistrylaw.inventionX-Ray DiffractionStructural BiologylawGeneticsmedicineAnimalsMolecular BiologyChemistrySmall-angle X-ray scatteringScatteringSpidersHemocyaninCell BiologyModels StructuralMicroscopy ElectronCrystallographyIntramolecular forceHemocyaninsRadius of gyrationProtein quaternary structureElectron microscopeOxidation-ReductionFEBS Letters
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Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex.

2002

Folding and post-translational modification of the thyroid hormone precursor, thyroglobulin (Tg), in the endoplasmic reticulum (ER) of the thyroid epithelial cells is facilitated by several molecular chaperones and folding enzymes, such as BiP, GRP94, calnexin, protein disulfide isomerase, ERp72, and others. They have been shown to associate simultaneously and/or sequentially with Tg in the course of its maturation, thus forming large heterocomplexes in the ER of thyrocytes. Here we present evidence that such complexes include a novel member, an ER-resident lumenal protein, ERp29, which is present in all mammalian tissues with exceptionally high levels of expression in the secretory cells. …

Protein DenaturationProtein FoldingImmunoprecipitationmedicine.medical_treatmentBlotting WesternThyroid GlandThyrotropinBiologyEndoplasmic ReticulumLigandsBiochemistryThyroglobulinRats Sprague-DawleyCalnexinmedicineCentrifugation Density GradientAnimalsUreaSecretionProtein disulfide-isomeraseMolecular BiologyCells CulturedHeat-Shock ProteinsThyroid Epithelial CellsChromatographyEndoplasmic reticulumCell BiologyPrecipitin TestsRatsCross-Linking ReagentsBiochemistryLiverMicroscopy FluorescenceMicrosomes LiverProtein foldingThyroglobulinProtein BindingThe Journal of biological chemistry
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Clustering induces a lateral redistribution of α2β1 integrin from membrane rafts to caveolae and subsequent protein kinase C-dependent internalization

2004

Integrin alpha 2 beta 1 mediates the binding of several epithelial and mesenchymal cell types to collagen. The composition of the surrounding plasma membrane, especially caveolin-1- and cholesterol-containing membrane structures called caveolae, may be important to integrin signaling. On cell surface alpha 2 beta 1 integrin was located in the raft like membrane domain, rich in GPI-anchored proteins, rather than in caveolae. However, when antibodies were used to generate clusters of alpha 2 beta 1 integrin, they started to move laterally on cell surface along actin filaments. During the lateral movement small clusters fused together. Finally alpha 2 beta 1 integrin was found inside caveolae …

Protein Kinase C-alphaEndosomeintegrinkinasemedia_common.quotation_subjectCaveolin 1IntegrinCoated VesiclesEndosomesCaveolaeCaveolinsCell Membrane StructuresCD49cCollagen receptorCell membraneCaveolaemedicineHumansantibodiesMicroscopy ImmunoelectronInternalizationMolecular BiologyCells CulturedProtein Kinase Cmedia_commonbiologyCell MembraneArticlesCell BiologyIntegrin alphaVproteinsEnterovirus B HumanCell biologyActin Cytoskeletonmedicine.anatomical_structureIntegrin alphaVcaveolaebiology.proteinIntegrin alpha2beta1
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Electronic and mechanical characterization of self-assembled alkanethiol monolayers by scanning tunneling microscopy combined with interaction-force-…

1993

We have used scanning tunneling microscopy to study self-assembled monolayers of mercaptohexadecanol in ultrigh vacuum. In addition to tunneling, the interaction force gradient acting between tip and sample was measured. Analysis of the force-gradient data shows that the tip is in mechanical contact with the surface of the monolayer which, in turn, is elastically compressed. The lateral dimensions of the mechanical contact are substantially (approximately five times) larger than the width of the tunneling-current filament. The results suggest that the compression of the monolayer constitutes an integral part of tunneling through the molecules

Protein filamentMaterials sciencelawMonolayerMoleculeNanotechnologyConductive atomic force microscopyScanning tunneling microscopeMolecular physicsQuantum tunnellingElectrochemical scanning tunneling microscopelaw.inventionCharacterization (materials science)Physical review. B, Condensed matter
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Immuno-electron microscopic localization of the alpha(1) and beta(1)-subunits of soluble guanylyl cyclase in the guinea pig organ of corti.

2000

Guanylyl cyclases (GC) catalyze the formation of the intracellular signal molecule cyclic GMP from GTP. For some years it has been known that the heme-containing soluble guanylyl cyclase (sGC) is stimulated by NO and NO-containing compounds. The sGC enzyme consists of two subunits (alpha(1) and beta(1)). In the present study, the alpha(1) and beta(1)-subunits were identified in the guinea pig cochlea at the electron microscopic level using a post-embedding immuno-labeling procedure. Ultrathin sections of LR White embedded specimens were incubated with various concentrations of two rabbit polyclonal antibodies to the alpha(1)- and beta(1)-subunit, respectively. The immunoreactivity was visua…

Protein subunitImmunocytochemistryGuinea PigsAntibodiesmedicineAnimalsMicroscopy ImmunoelectronMolecular BiologyHair Cells Auditory InnerbiologyTissue EmbeddingGeneral NeuroscienceMolecular biologyPrimary and secondary antibodiesHair Cells Auditory Outermedicine.anatomical_structureBiochemistrySolubilityOrgan of CortiCytoplasmGuanylate Cyclasebiology.proteinDeiters cellssense organsNeurology (clinical)Hair cellNitric Oxide SynthaseSoluble guanylyl cyclaseDevelopmental BiologySignal TransductionBrain research
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Three-dimensional structure of the anaphase-promoting complex.

2001

The anaphase-promoting complex (APC) is a cell cycle-regulated ubiquitin-protein ligase, composed of at least 11 subunits, that controls progression through mitosis and G1. Using cryo-electron microscopy and angular reconstitution, we have obtained a three-dimensional model of the human APC at a resolution of 24 A. The APC has a complex asymmetric structure 140 A x 140 A x 135 A in size, in which an outer protein wall surrounds a large inner cavity. We discuss the possibility that this cavity represents a reaction chamber in which ubiquitination reactions take place, analogous to the inner cavities formed by other protein machines such as the 26S proteasome and chaperone complexes. This cag…

Protein subunitUbiquitin-Protein LigasesAnaphase-Promoting Complex-CyclosomeLigasesProtein structureUbiquitinHumansProtein Structure QuaternaryMitosisMolecular Biologychemistry.chemical_classificationDNA ligasebiologyCryoelectron MicroscopyG1 PhaseUbiquitin-Protein Ligase ComplexesCell BiologyPrecipitin TestsCell biologyProtein Structure TertiaryProteasomechemistryChaperone (protein)biology.proteinAnaphase-promoting complexHeLa CellsMolecular cell
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Peroxisomal and mitochondrial status of two murine oligodendrocytic cell lines (158N, 158JP): potential models for the study of peroxisomal disorders…

2009

International audience; In some neurodegenerative disorders (leukodystrophies) characterized by myelin alterations, the defect of peroxisomal functions on myelin-producing cells (oligodendrocytes) are poorly understood. The development of in vitro models is fundamental to understanding the physiopathogenesis of these diseases. We characterized two immortalized murine oligodendrocyte cell lines: a normal (158N) and a jimpy (158JP) cell line mutated for the proteolipid protein PLP/DM20. Fluorescence microscopy, flow cytometry, and western blotting analysis allow to identify major myelin proteins (PLP colocalizing with mitochondria; myelin basic protein), oligodendrocyte (CNPase and myelin oli…

Proteolipid protein 1BiochemistryMiceMyelinMESH : PhenylbutyratesperoxisomeIsomerasesMESH : Myelin Basic ProteinsEnoyl-CoA HydrataseCell Line TransformedUltrasonographybiologyMESH : Gene Expression RegulationMESH : Myelin Proteolipid Protein3-Hydroxyacyl CoA DehydrogenasesMESH : Myelin-Associated GlycoproteinMESH : Cell Line TransformedPeroxisomeMESH : Multienzyme ComplexesMESH : OligodendrogliaMESH : Enoyl-CoA HydrataseCatalaseFlow CytometryMESH : 3-Hydroxyacyl CoA DehydrogenasesPhenylbutyratesmitochondriaMyelin-Associated GlycoproteinOligodendrogliamyelinMESH : Antineoplastic Agentsmedicine.anatomical_structureMESH : Microscopy Electron TransmissionBiochemistryACOX1MESH : MitochondriaMESH : Acyl-CoA Oxidase2'3'-Cyclic-Nucleotide PhosphodiesterasesMESH : IsomerasesOxidation-ReductionMyelin ProteinsMESH : Flow CytometryAntineoplastic AgentsPeroxisomal Bifunctional EnzymeStatistics NonparametricMyelin oligodendrocyte glycoproteinCellular and Molecular NeuroscienceMicroscopy Electron TransmissionMultienzyme ComplexesMESH : CatalaseMESH : MicePeroxisomesmedicineAnimalsMESH : ATP-Binding Cassette TransportersMyelin Proteolipid ProteinMESH : Statistics Nonparametric[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH : Oxidation-ReductionMyelin Basic Proteinmurine oligodendrocytesMESH : 2'3'-Cyclic-Nucleotide PhosphodiesterasesPeroxisomal transportOligodendrocyteMyelin basic proteinGene Expression Regulationbiology.proteinATP-Binding Cassette TransportersMyelin-Oligodendrocyte GlycoproteinAcyl-CoA OxidaseMESH : AnimalsMESH : Peroxisomes
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Acute cytotoxicity and apoptotic effects after l-Pam exposure in different cocultures of the proximal and distal respiratory system.

2009

Abstract Sulphur and nitrogen mustard are strong alkylating agents which can cause after inhalation acute lung injury in the larynx, trachea and large bronchi and can lead to alveolar edema. In our study we tested the N-Lost l -Phenylalanine Mustard ( l -Pam). Therefore we seeded the alveolar type II cell line NCI H441 on the upper membrane of a Transwell filter plate and the endothelial cell line ISO-Has-1 on the lower side of the membrane for the alveolar model and combined the human bronchial explant-outgrowth cells and fibroblasts in the bronchial model and exposed both models with various concentrations of l -Pam. Treatment with l -Pam led to a concentration-dependent decrease of the t…

ProteomeIntracellular SpaceBioengineeringApoptosisBronchiBiologyLung injuryApplied Microbiology and BiotechnologyCell Linechemistry.chemical_compoundMicroscopy Electron TransmissionmedicineElectric ImpedanceToxicity Tests AcuteHumansRespiratory systemMelphalanOrganellesAnalysis of VarianceLungCytotoxinsEndothelial CellsGeneral Medicinerespiratory systemMolecular biologyWI-38Nitrogen mustardCoculture TechniquesEndothelial stem cellPulmonary Alveolimedicine.anatomical_structurechemistryApoptosisImmunologyVacuolesIntracellularBiotechnologyJournal of biotechnology
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SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear transfer of tri-snRNP complexes

2021

Abstract Splicing is catalyzed by the spliceosome, a compositionally dynamic complex assembled stepwise on pre-mRNA. We reveal links between splicing machinery components and the intrinsically disordered ciliopathy protein SANS. Pathogenic mutations in SANS/USH1G lead to Usher syndrome—the most common cause of deaf-blindness. Previously, SANS was shown to function only in the cytosol and primary cilia. Here, we have uncovered molecular links between SANS and pre-mRNA splicing catalyzed by the spliceosome in the nucleus. We show that SANS is found in Cajal bodies and nuclear speckles, where it interacts with components of spliceosomal sub-complexes such as SF3B1 and the large splicing cofact…

ProteomicsAcademicSubjects/SCI00010Ribonucleoprotein U4-U6 Small NuclearSF3B1 GeneMass Spectrometry0302 clinical medicineRNA Small NuclearRNA PrecursorsIn Situ Hybridization FluorescenceRibonucleoprotein0303 health sciencesChemistryRibonucleoproteins Small NuclearImmunohistochemistryCell biologyDNA-Binding Proteinsmedicine.anatomical_structureGene Knockdown TechniquesRNA splicingRNA Splicing FactorsUsher SyndromesSpliceosomeCoiled BodiesNerve Tissue ProteinsBiologyMinor Histocompatibility Antigens03 medical and health sciencesMicroscopy Electron TransmissionRNA and RNA-protein complexesGeneticsmedicineHumanssnRNPEye ProteinsGeneCell Proliferation030304 developmental biologyCell NucleusRNAmedicine.diseasePhosphoproteinsCiliopathyAlternative SplicingCell nucleusHEK293 CellsCajal bodyCytoplasmSpliceosomesNucleus030217 neurology & neurosurgeryTranscription FactorsNucleic Acids Research
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Insights in ChAdOx1 nCoV-19 vaccine-induced immune thrombotic thrombocytopenia

2021

Abstract SARS-CoV-2 vaccine ChAdOx1 nCoV-19 (AstraZeneca) causes a thromboembolic complication termed vaccine-induced immune thrombotic thrombocytopenia (VITT). Using biophysical techniques, mouse models, and analysis of VITT patient samples, we identified determinants of this vaccine-induced adverse reaction. Super-resolution microscopy visualized vaccine components forming antigenic complexes with platelet factor 4 (PF4) on platelet surfaces to which anti-PF4 antibodies obtained from VITT patients bound. PF4/vaccine complex formation was charge-driven and increased by addition of DNA. Proteomics identified substantial amounts of virus production-derived T-REx HEK293 proteins in the ethyle…

ProteomicsAntigen-Antibody ComplexPlatelet Factor 4Extracellular TrapsBiochemistryEpitopesMiceSinus Thrombosis IntracranialMedicinePlateletCell Line TransformedMicroscopybiologyHematologymedicine.anatomical_structureSpike Glycoprotein CoronavirusAntibodyDrug ContaminationVirus CultivationGenetic VectorsImmunologyAdenoviridaeProinflammatory cytokineImaging Three-DimensionalImmune systemAntigenChAdOx1 nCoV-19AnimalsHumansPlatelet activationB cellAutoantibodiesInflammationPurpura Thrombocytopenic IdiopathicSARS-CoV-2business.industryCOVID-19Cell BiologyPlatelet ActivationPlatelets and ThrombopoiesisDynamic Light ScatteringHEK293 CellsImmunoglobulin GImmunologybiology.proteinCapsid ProteinsbusinessCapillary Leak SyndromePlatelet factor 4Extravasation of Diagnostic and Therapeutic MaterialsBlood
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