Search results for "Intracellular"

showing 10 items of 821 documents

Optogenetic Control of Intracellular Signaling: Class II Opsins

2017

Class (computer programming)OpsinChemistryOptogeneticsNeuroscienceIntracellular
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Organelle pH studies using targeted avidin and fluorescein–biotin

2000

Abstract Background: Mammalian organelles of the secretory pathway are of differing pH. The pH values form a decreasing gradient: the endoplasmic reticulum (ER) is nearly neutral, the Golgi is mildly acidic and the secretory granules are more acidic still (∼pH 5). The mechanisms that regulate pH in these organelles are still unknown. Results: Using a novel method, we tested whether differences in H + ‘leak' and/or counterion conductances contributed to the pH difference between two secretory pathway organelles. A pH-sensitive, membrane-permeable fluorescein–biotin was targeted to endoplasmic-reticulum- and Golgi-localized avidin-chimera proteins in HeLa cells. In live, intact cells, ER pH (…

Clinical BiochemistryBiotinGolgi ApparatusEndoplasmic ReticulumBiochemistrysymbols.namesakechemistry.chemical_compoundChloridesBiotinOrganelleDrug DiscoveryHumansMicroscopy ImmunoelectronMolecular BiologySecretory pathwayFluorescent DyesOrganellesPharmacologyIon TransportFlubi-2ChemistryEndoplasmic reticulumBafilomycinIntracellular MembranesGeneral MedicineHydrogen-Ion ConcentrationProton PumpsGolgi apparatusAvidinCytosolTargeted fluorescenceMembraneBiochemistryH+ pumpPotassiumsymbolsMolecular MedicineFluoresceinHeLa CellsH+ leakChemistry & Biology
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Reorganization of Nuclear Domain 10 Induced by Papillomavirus Capsid Protein L2

2002

AbstractNuclear domains (ND) 10 are associated with proteins implicated in transcriptional regulation, growth suppression, and apoptosis. We now show that the minor capsid protein L2 of human papillomavirus (HPV) type 33 induces a reorganization of ND10-associated proteins. Whereas the promyelocytic leukemia protein, the major structural component of ND10, was unaffected by L2, Sp100 was released from ND10 upon L2 expression. The total cellular amount of Sp100, but not of Sp100 mRNA, decreased significantly, suggesting degradation of Sp100. Proteasome inhibitors induced the dispersal of Sp100 and inhibited the nuclear translocation of L2. In contrast to Sp100, Daxx was recruited to ND10 by …

Co-Repressor ProteinsImmunoprecipitationFluorescent Antibody TechniqueVaccinia virusPromyelocytic Leukemia ProteinAutoantigenspapillomavirusCell LinePromyelocytic leukemia proteinCapsidDeath-associated protein 6DaxxVirologyHumansSp100RNA MessengerAdaptor Proteins Signal TransducingCell NucleusRecombination GeneticbiologyTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsND10Signal transducing adaptor proteinAntigens NuclearOncogene Proteins ViralL2biochemical phenomena metabolism and nutritionBlotting NorthernMolecular biologyNeoplasm ProteinsTransport proteinCell biologyProtein TransportProteasomeCapsidbiology.proteinRNACapsid ProteinsFemaleCarrier ProteinsCo-Repressor ProteinsMolecular ChaperonesTranscription FactorsVirology
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Heat shock and Cd2+ exposure regulate PML and Daxx release from ND10 by independent mechanisms that modify the induction of heat-shock proteins 70 an…

2003

Nuclear domains called ND10 or PML bodies might function as nuclear depots by recruiting or releasing certain proteins. Although recruitment of proteins through interferon-induced upregulation and SUMO-1 modification level of PML had been defined, it is not known whether release of proteins is regulated and has physiological consequences. Exposure to sublethal environmental stress revealed a sequential release of ND10-associated proteins. Upon heat shock Daxx and Sp100 were released but PML remained, whereas exposure to subtoxic concentrations of CdCl2 induced the release of ND10-associated proteins, including PML, with Sp100 remaining in a few sites. In both cases,recovery times were simil…

Co-Repressor ProteinsMAP Kinase Signaling SystemMacromolecular SubstancesSUMO-1 ProteinPromyelocytic Leukemia ProteinMicePromyelocytic leukemia proteinDeath-associated protein 6Stress PhysiologicalHeat shock proteinEndopeptidasesAnimalsHSP70 Heat-Shock ProteinsEnzyme InhibitorsHeat shockTranscription factorCells CulturedHeat-Shock ProteinsbiologyTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsCell BiologyCell Nucleus StructuresNeoplasm ProteinsCell biologyHsp70Cysteine EndopeptidasesEukaryotic CellsGene Expression RegulationImmunologybiology.proteinSignal transductionCarrier ProteinsCo-Repressor ProteinsHeat-Shock ResponseCadmiumMolecular ChaperonesTranscription FactorsJournal of Cell Science
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Computing the Cell

2015

Here I call for the need to revisit cell theory. The idea that the cell is the basic unit of life is well-known and foundational to Biology, but it has not received sufficient attention. We have increasingly detailed knowledge of the intracellular world and all its components, but these are often considered independently. On the other hand, there is excessive theorising about the cell on the basis of its being a black box. The time is ripe to formulate an integrative cell theory .

Cognitive sciencemedicine.anatomical_structureBasis (linear algebra)Cell theoryBlack boxCellExplanatory theorymedicineIntracellular
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TopoCell – An image analysis tool to study intracellular topography

2012

Computer sciencebusiness.industryGeneticsComputer visionArtificial intelligencebusinessMolecular BiologyBiochemistryIntracellularBiotechnologyImage (mathematics)The FASEB Journal
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Fluorescent nanodiamonds encapsulated byCowpea Chlorotic Mottle Virus(CCMV) proteins for intracellular 3D-trajectory analysis

2021

Long-term tracking of nanoparticles to resolve intracellular structures and motions is essential to elucidate fundamental parameters as well as transport processes within living cells. Fluorescent nanodiamond (ND) emitters provide cell compatibility and very high photostability. However, high stability, biocompatibility, and cellular uptake of these fluorescent NDs under physiological conditions are required for intracellular applications. Herein, highly stable NDs encapsulated with Cowpea chlorotic mottle virus capsid proteins (ND-CP) are prepared. A thin capsid protein layer is obtained around the NDs, which imparts reactive groups and high colloidal stability, while retaining the opto-ma…

Cowpea chlorotic mottle virusbiologyBiocompatibilityChemistryBiomedical EngineeringUT-Hybrid-DNanoparticle02 engineering and technologyGeneral ChemistryGeneral Medicine010402 general chemistry021001 nanoscience & nanotechnologybiology.organism_classificationEndocytosis01 natural sciencesExocytosis0104 chemical sciences3. Good healthCapsidBiophysicsGeneral Materials Science0210 nano-technologyNanodiamondIntracellular
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The efficient bovine insulin presentation capacity of bone marrow-derived macrophages activated by granulocyte-macrophage colony-stimulating factor c…

1993

Bone marrow-derived macrophages (BMM phi) were shown before to function as antigen-presenting cells. We show here, that the antigen presentation capacity of BMM phi depends on the nature of the antigen and is differently regulated by the lymphokines interferon-gamma (IFN-gamma) and granulocyte/macrophage-colony-stimulating factor (GM-CSF). When bovine insulin (BI) was employed as antigen, only BMM phi treated with GM-CSF (GM-CSF-M phi) were efficient presenters, but when presentation of the antigens ovalbumin and conalbumin was tested, IFN-gamma-pulsed BMM phi (IFN-gamma-M phi) proved superior to GM-CSF-M phi. The lack of efficient BI presentation function of IFN-gamma-M phi was only obviou…

CytoplasmImmunologyAntigen presentationAntigen-Presenting CellsBone Marrow CellsBiologyInterferon-gammachemistry.chemical_compoundAntigenmedicineAnimalsInsulinImmunology and AllergyCysteineSulfhydryl CompoundsAntigen-presenting cellAntigen processingMacrophagesLymphokineGranulocyte-Macrophage Colony-Stimulating FactorGlutathioneMacrophage ActivationGlutathioneCell biologyGranulocyte macrophage colony-stimulating factorBiochemistrychemistryCattleIntracellularmedicine.drugEuropean Journal of Immunology
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Intracellular pH-dependent efflux of the fluorescent probe pyranine in the yeast Yarrowia lipolytica.

2001

International audience; 8-Hydroxypyrene-1,3,6-trisulfonic acid (pyranine) can be used as a vital intracellular pH (pH(i)) indicator. In the yeast Yarrowia lipolytica, a partial efflux of the probe was detected by using the pH-independent wavelength of 415 nm. A simplified correction of the fluorescent signals was applied, enabling to show for this species a good near-neutral pH(i) maintenance capacity in a pH 3.9 medium. Octanoic acid, which is known to have toxic effects on yeast, decreased the pH(i) and increased the 260-nm-absorbing compounds leakage. However, this acid inhibited the fluorescent probe efflux linearly with its concentration suggesting a pH(i)-dependent efflux of pyranine …

CytoplasmMESH: Hydrogen-Ion ConcentrationCell Membrane Permeability[SDV.BIO]Life Sciences [q-bio]/BiotechnologyOctanoic Acidschemistry.chemical_compoundMESH : Fluorescent DyesMESH: Cell Membrane PermeabilityArylsulfonates[INFO.INFO-BT]Computer Science [cs]/BiotechnologyMESH: ArylsulfonatesMESH : Octanoic AcidsbiologyCaprylic acidHydrogen-Ion ConcentrationMESH: Fluorescent DyesFluorescenceBiochemistryEffluxCaprylates[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyIntracellularMESH : CytoplasmIntracellular pHMESH: Biological Transport[SDV.BC]Life Sciences [q-bio]/Cellular BiologyMicrobiologyPyranineMESH : ArylsulfonatesMESH : Hydrogen-Ion ConcentrationGeneticsMESH: SaccharomycetalesMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyFluorescent Dyes[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyMESH: Cytoplasm[ SDV.BIO ] Life Sciences [q-bio]/BiotechnologyYarrowiaBiological TransportMESH : Saccharomycetalesbiology.organism_classificationMESH: Octanoic AcidsYeast[SDV.BIO] Life Sciences [q-bio]/BiotechnologyMESH : Biological Transport[INFO.INFO-BT] Computer Science [cs]/BiotechnologychemistryMESH : Cell Membrane PermeabilitySaccharomycetales
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Intracellular location of DNA nucleotidyltransferase.

1962

CytoplasmMultidisciplinaryChemistryTransferasesDNA NucleotidyltransferasesNucleotidyltransferasesIntracellularDNA NucleotidyltransferasesCell biologyNature
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