Search results for "nucleus"

showing 10 items of 1803 documents

Nuclear-mitochondrial interaction.

2007

The biogenesis of mitochondria depends on the coordinated expression of nuclear and mitochondrial genomes. Consequently, the control of mitochondrial biogenesis and function depends on extremely complex processes requiring a variety of well orchestrated regulatory mechanisms. It is clear that the interplay of transcription factors and coactivators contributes to the expression of both nuclear and mitochondrial respiratory genes. In addition, the regulation of mitochondria biogenesis depends on proteins that, interacting with messenger RNAs for mitochondrial proteins, influence their metabolism and expression. Moreover, a tight regulation of the import and final assembly of mitochondrial pro…

Cell NucleusRNA-binding proteinRNA-binding proteinsCell BiologyCell CommunicationBiologyMitochondrionCell biologyEpigenesis GeneticMitochondriamitochondrial fusionMitochondrial biogenesisNeoplasmsMolecular MedicineAnimalsHumansMitochondrial fissionMolecular BiologyTranscription factorPost-transcriptional regulationBiogenesistranscriptional factorpost-transcriptional regulationTranscription FactorsMitochondrion
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ALS-linked FUS mutations confer loss and gain of function in the nucleus by promoting excessive formation of dysfunctional paraspeckles

2019

Mutations in the FUS gene cause amyotrophic lateral sclerosis (ALS-FUS). Mutant FUS is known to confer cytoplasmic gain of function but its effects in the nucleus are less understood. FUS is an essential component of paraspeckles, subnuclear bodies assembled on a lncRNA NEAT1. Paraspeckles may play a protective role specifically in degenerating spinal motor neurons. However it is still unknown how endogenous levels of mutant FUS would affect NEAT1/paraspeckles. Using novel cell lines with the FUS gene modified by CRISPR/Cas9 and human patient fibroblasts, we found that endogenous levels of mutant FUS cause accumulation of NEAT1 isoforms and paraspeckles. However, despite only mild cytoplasm…

Cell NucleusResearchAmyotrophic Lateral SclerosisIntranuclear Inclusion BodiesNEAT1lcsh:RC346-429Cell LineLoss of Function MutationCell Line TumorFused in sarcoma (FUS)ParaspeckleHumansProtein IsoformsRNA-Binding Protein FUSRNA Long NoncodingAmyotrophic lateral sclerosis (ALS)CRISPR-Cas Systemslcsh:Neurology. Diseases of the nervous systemActa Neuropathologica Communications
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Live cell imaging of duplex siRNA intracellular trafficking.

2015

Intracellular distribution of siRNA after in vitro transfection typically depends on lipopolyplexes, which must release the siRNA into the cytosol. Here, the fate of siRNAs was monitored by FRET-based live cell imaging. Subsequent to in situ observation of uptake and release processes, this approach allowed the observation of a number of hitherto uncharacterized intracellular distribution and degradation processes, commencing with a burst of endosomal releases, followed, in some cases, by fast siRNA influx into the nucleus. The continued observation of intact siRNA against a background of free fluorophores resulting from advanced degradation was possible by a specifically developed imaging …

Cell NucleusSmall interfering RNAMicroscopy ConfocalEndosomeTransfectionEndosomesBiologyTransfectionRNA TransportCell biologyCell LineRatsCytosolLive cell imagingCell cultureRNA interferenceGeneticsFluorescence Resonance Energy TransferAnimalsRNARNA Small InterferingIntracellularNucleic acids research
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Kinetic models for nucleocytoplasmic transport of messenger RNA

1995

Abstract Much is known about the mechanism by which mRNAs cross the nuclear envelope (the translocation stage of nucleocytoplasmic transport), but far less is known about the preceding (intranuclear migration/release) and succeeding (cytoplasmic binding) stages. Therefore, existing information suffices for articulating detailed kinetic models of translocation, but not models for the overall mRNA transport process. In this paper, we show that simple kinetic models of translocation can (i) accommodate date about nucleocytoplasmic distributions of endogenous transcripts; (ii) predict the overall effects on these distributions of effectors such as insulin and epidermal growth factor; (iii) thro…

Cell NucleusStatistics and ProbabilityCytoplasmMessenger RNAModels GeneticGeneral Immunology and MicrobiologyMechanism (biology)EffectorApplied MathematicsChromosomal translocationGeneral MedicineBiologyTranslocation GeneticGeneral Biochemistry Genetics and Molecular BiologyCell biologyKineticsBiochemistryNucleocytoplasmic TransportEpidermal growth factorCytoplasmModeling and SimulationAnimalsMRNA transportRNA MessengerGeneral Agricultural and Biological SciencesJournal of Theoretical Biology
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Tightly bound to DNA proteins: possible universal substrates for intranuclear processes.

2011

Tightly bound to DNA proteins (TBPs) are a protein group that remains attached to DNA after its deproteinization by phenol, chloroform or salting-out. TBP are bound to DNA with covalent phosphotriester or non-covalent ion and hydrogen bonds. They appear to be a vast protein group involved in numerous intranuclear processes. The TBPs fraction co-purified with DNA deproteinized by mild procedures is extremely heterogeneous, tissue and species-specific. The protein fraction co-purified with DNA after harsh deproteinization procedures appears to be formed from few polypeptides common to different species and tissues. Interaction sites between DNA and TBPs depend on the physiological status of t…

Cell NucleusTranscription GeneticHydrogen bondPhosphataseCellGeneral MedicineBiologyNuclear matrixModels BiologicalPhosphoric Monoester HydrolasesDNA-Binding Proteinschemistry.chemical_compoundmedicine.anatomical_structurechemistryBiochemistrySpecies SpecificityTranscription (biology)Covalent bondOrgan SpecificityGeneticsmedicineAnimalsBinding siteDNASerpinsGene
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Concepts to Reveal Parvovirus–Nucleus Interactions

2021

Parvoviruses are small single-stranded (ss) DNA viruses, which replicate in the nucleoplasm and affect both the structure and function of the nucleus. The nuclear stage of the parvovirus life cycle starts at the nuclear entry of incoming capsids and culminates in the successful passage of progeny capsids out of the nucleus. In this review, we will present past, current, and future microscopy and biochemical techniques and demonstrate their potential in revealing the dynamics and molecular interactions in the intranuclear processes of parvovirus infection. In particular, a number of advanced techniques will be presented for the detection of infection-induced changes, such as DNA modification…

Cell Nucleusanalysis of virus–chromatin interactionsHost Microbial InteractionsviruksetparvovirusesvirusesnucleusReviewmikroskopiaanalysis of protein–protein interactionsVirus ReplicationinfektiotMicrobiologyimaging of viral interactions and dynamicsQR1-502Parvoviridae InfectionsParvovirusMicekuvantaminentumaAnimalsHumansCapsid ProteinsproteiinitparvoviruksetViruses
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Yeast mRNA cap-binding protein Cbc1/Sto1 is necessary for the rapid reprogramming of translation after hyperosmotic shock.

2011

Global translation is inhibited in Saccharomyces cerevisiae cells under osmotic stress; nonetheless, osmostress-protective proteins are synthesized. We found that translation mediated by the mRNA cap-binding protein Cbc1 is stress-resistant and necessary for the rapid translation of osmostress-protective proteins under osmotic stress.

Cell PhysiologySaccharomyces cerevisiae ProteinsOsmotic shockRNA StabilitySaccharomyces cerevisiaeCycloheximideBiology03 medical and health scienceschemistry.chemical_compoundGene Knockout TechniquesEukaryotic translationOsmotic PressureStress PhysiologicalPolysomeGene Expression Regulation FungalProtein biosynthesisRNA MessengerMolecular Biology030304 developmental biologyCell Nucleus0303 health sciencesMicrobial ViabilityOsmotic concentration030302 biochemistry & molecular biologyEIF4ENuclear ProteinsTranslation (biology)Cell BiologyArticlesAdaptation PhysiologicalProtein TransportEukaryotic Initiation Factor-4EchemistryBiochemistryRNA Cap-Binding ProteinsPolyribosomesProtein BiosynthesisProtein BindingMolecular biology of the cell
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Genotoxicity of 1,4-benzoquinone and 1,4-naphthoquinone in relation to effects on glutathione and NAD(P)H levels in V79 cells.

1989

1,4-Benzoquinone is cytotoxic in V79 Chinese hamster cells and induces gene mutations and micronuclei. The cell-damaging effects of quinones are usually attributed to thiol depletion, oxidation of NAD(P)H, and redox-cycling involving the formation of semiquinone radicals and reactive oxygen species. To elucidate the role of these mechanisms in the genotoxicity of 1,4-benzoquinone, we measured various genotoxic effects, cytotoxicity, and the levels of glutathione, NADPH, NADH, and their oxidized forms all in the same experiment. 1,4-Naphthoquinone, which does not induce gene mutations in V79 cells, was investigated for comparative reasons. The quinones had a similar effect on the levels of c…

Cell SurvivalHealth Toxicology and MutagenesisGlutathione reductaseGene mutationBiologymedicine.disease_causeCell Linechemistry.chemical_compoundBenzoquinonesmedicineAnimalschemistry.chemical_classificationReactive oxygen speciesMutagenicity TestsQuinonesPublic Health Environmental and Occupational HealthGlutathioneNADGlutathioneBiochemistrychemistryMicronucleus testNAD+ kinaseOxidation-ReductionNADPGenotoxicityOxidative stressMutagensNaphthoquinonesResearch ArticleEnvironmental Health Perspectives
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Recruitment of glutathione into the nucleus during cell proliferation adjusts whole-cell redox homeostasis in Arabidopsis thaliana and lowers the oxi…

2010

Summary Cellular redox homeostasis and signalling are important in progression of the eukaryotic cell cycle. In animals, the low-molecular-weight thiol tripeptide glutathione (GSH) is recruited into the nucleus early in the cell proliferation cycle. To determine whether a similar process occurs in plants, we studied cell proliferation in Arabidopsis thaliana. We show that GSH co-localizes with nuclear DNA during the proliferation of A. thaliana cells in culture. Moreover, GSH localization in the nucleus was observed in dividing pericycle cells of the lateral root meristem. There was pronounced accumulation of GSH in the nucleus at points in the growth cycle at which a high percentage of the…

Cell growthCellCell BiologyPlant ScienceGlutathioneCell cycleBiologyCell biologychemistry.chemical_compoundCell nucleusmedicine.anatomical_structurechemistryBiochemistryCytoplasmGeneticsmedicineNuclear proteinNucleusThe Plant Journal
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Zur Ultrastruktur des Neurofibroms

1970

Elektronenmikroskopische Untersuchung eines Neurofibroms von einem 72 jahrigen Mann mit Morbus Recklinghausen. Der Tumor besteht aus verzweigten Schwannschen Zellen, die in ein kollagenfasriges Zwischengewebe eingelagert sind. Die Schwannschen Zellen sind von einer Basalmembran und einen Reticulinfasernetz umgeben. Wahrscheinlich sind die Schwannschen Zellen eines Neurofibroms befahigt fibrillare Zwischensubstanz zu bilden.

Cell membraneBasement membraneCell nucleusmedicine.anatomical_structureChemistryCytoplasmmedicineDermatologyGeneral MedicineMolecular biologyCytoplasmic granulesArchiv f�r Klinische und Experimentelle Dermatologie
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