0000000000292804

AUTHOR

Rosa Bonaccorso

0000-0003-2731-8556

showing 3 related works from this author

ISWI ATP-dependent remodeling of nucleoplasmic ω-speckles in the brain of Drosophila melanogaster.

2017

Heterogeneous nuclear ribonucleoproteins (hnRNPs) belong to the RNA-binding proteins family. They are involved in processing heterogeneous nuclear RNAs (hnRNAs) into mature mRNAs. These proteins participate in every step of mRNA cycle, such as mRNA export, localization, translation, stability and alternative splicing. At least 14 major hnRNPs, which have structural and functional homologues in mammals, are expressed in Drosophila melanogaster. Until now, six of these hnRNPs are known to be nucleus-localized and associated with the long non-coding RNA (lncRNA) heat shock responsive ω (hsrω) in the omega speckle compartments (ω-speckles). The chromatin remodeler ISWI is the catalytic subunit …

0301 basic medicineTranscription GeneticBiologyHeterogeneous ribonucleoprotein particleHeterogeneous-Nuclear RibonucleoproteinsNuclear body03 medical and health scienceslncRNAAdenosine TriphosphateChromatin remodelersGene expressionGeneticsOmega speckleAnimalsMolecular BiologyGeneticsAdenosine TriphosphatasesCell NucleusAlternative splicingChromatin remodelers; hnRNPs; lncRNA; Nuclear body; Omega speckles; Molecular Biology; GeneticsRNABrainTranslation (biology)biology.organism_classificationChromatin Assembly and DisassemblyhnRNPsChromatinCell biology030104 developmental biologyDrosophila melanogasterGene Expression RegulationOmega specklesDrosophila melanogasterTranscription FactorsJournal of genetics and genomics = Yi chuan xue bao
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Nuclear and Cytoplasmic Soluble Proteins Extraction from a Small Quantity of Drosophila’s Whole Larvae and Tissues

2015

The identification and study of protein’s function in several model organisms is carried out using both nuclear and cytoplasmic extracts. For a long time, Drosophila’s embryos have represented the main source for protein extractions, although in the last year, the importance of collecting proteins extracts also from larval tissues has also been understood. Here we report a very simple protocol, improved by a previously developed method, to produce in a single extraction both highly stable nuclear and cytoplasmic protein extracts from a small quantity of whole Drosophila’s larvae or tissues, suitable for biochemical analyses like co-immunoprecipitation.

Cytoplasmanimal structuresved/biology.organism_classification_rank.speciesBiologyCell FractionationCatalysislcsh:ChemistryInorganic ChemistryCytoplasmic proteinBotanyTechnical NoteAnimalsDrosophila ProteinsPhysical and Theoretical ChemistryModel organismlcsh:QH301-705.5Molecular BiologyDrosophilaSpectroscopyCell NucleusLarvaved/biologyOrganic ChemistryExtraction (chemistry)fungiproteins extractionEmbryoGeneral Medicinebiology.organism_classificationhnRNPsComputer Science ApplicationsDrosophila melanogasterlcsh:Biology (General)lcsh:QD1-999BiochemistryCytoplasmLarvaDrosophilaFunction (biology)International Journal of Molecular Sciences
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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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