Search results for "Imitation SWI"

showing 2 items of 2 documents

ISWI Regulates Higher-Order Chromatin Structure and Histone H1 Assembly In Vivo

2007

Imitation SWI (ISWI) and other ATP-dependent chromatin-remodeling factors play key roles in transcription and other processes by altering the structure and positioning of nucleosomes. Recent studies have also implicated ISWI in the regulation of higher-order chromatin structure, but its role in this process remains poorly understood. To clarify the role of ISWI in vivo, we examined defects in chromosome structure and gene expression resulting from the loss of Iswi function in Drosophila. Consistent with a broad role in transcriptional regulation, the expression of a large number of genes is altered in Iswi mutant larvae. The expression of a dominant-negative form of ISWI leads to dramatic a…

Imitation SWINucleosome assemblyTranscription GeneticQH301-705.5RNA-POLYMERASE-IIPROTEINCHROMOSOME ARCHITECTUREGeneral Biochemistry Genetics and Molecular BiologyHistones03 medical and health sciencesNUCLEOSOME REMODELING FACTORHigher Order Chromatin StructureHistone H1NucleosomeAnimalsTRANSCRIPTIONBiology (General)LIVING CELLSMolecular Biology030304 developmental biologyGENE-EXPRESSIONRegulation of gene expressionGeneticsAdenosine Triphosphatases0303 health sciencesGeneral Immunology and MicrobiologybiologyGeneral Neuroscience030302 biochemistry & molecular biologyGenetics and GenomicsCell BiologyChromatin Assembly and DisassemblyChromatinChromatinCell biologyDROSOPHILAHistoneGene Expression RegulationLarvaMutationbiology.proteinLINKER HISTONEGeneral Agricultural and Biological SciencesResearch ArticleDevelopmental BiologyTranscription FactorsDOSAGE COMPENSATION
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Loss of ISWI Function in Drosophila Nuclear Bodies Drives Cytoplasmic Redistribution of Drosophila TDP-43

2018

Over the past decade, evidence has identified a link between protein aggregation, RNA biology, and a subset of degenerative diseases. An important feature of these disorders is the cytoplasmic or nuclear aggregation of RNA-binding proteins (RBPs). Redistribution of RBPs, such as the human TAR DNA-binding 43 protein (TDP-43) from the nucleus to cytoplasmic inclusions is a pathological feature of several diseases. Indeed, sporadic and familial forms of amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration share as hallmarks ubiquitin-positive inclusions. Recently, the wide spectrum of neurodegenerative diseases characterized by RBPs functions’ alteration and loss was coll…

0301 basic medicineCytoplasmCytoplasmic inclusionFluorescent Antibody TechniqueProtein aggregationHeterogeneous ribonucleoprotein particleHeterogeneous-Nuclear Ribonucleoproteinslcsh:Chemistry0302 clinical medicineDrosophila Proteinsneurodegenerative diseasesnuclear bodylcsh:QH301-705.5SpectroscopyGeneral MedicinehnRNPsComputer Science ApplicationsCell biologyChromatinTransport proteinDNA-Binding ProteinsProtein Transportmedicine.anatomical_structureDrosophilaDrosophila ProteinProtein BindingImitation SWIBiologyCatalysisArticleInorganic Chemistryomega speckles03 medical and health sciencesmedicineAnimalsPhysical and Theoretical ChemistryMolecular BiologyGenetic Association StudiesCell NucleusOrganic Chemistryta1182Chromatin Assembly and DisassemblyCell nucleus030104 developmental biologylcsh:Biology (General)lcsh:QD1-999gene expression<i>Drosophila</i>; nuclear body; omega speckles; dTDP-43; hnRNPs; omega speckles; neurodegenerative diseases; gene expression; gene regulationdTDP-43gene regulation030217 neurology & neurosurgeryInternational Journal of Molecular Sciences
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