Search results for "RNA-binding protein"

showing 10 items of 194 documents

Role of RNA-binding proteins in the replication-independent expression of H1° and H3.3 histone variants

2012

histone variantRNA-binding proteinSettore BIO/10 - BiochimicaLPISettore BIO/06 - Anatomia Comparata E CitologiaCSD-C2PEP-19
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RNA-Binding Proteins as Epigenetic Regulators of Brain Functions and Their Involvement in Neurodegeneration.

2022

A central aspect of nervous system development and function is the post-transcriptional regulation of mRNA fate, which implies time- and site-dependent translation, in response to cues originating from cell-to-cell crosstalk. Such events are fundamental for the establishment of brain cell asymmetry, as well as of long-lasting modifications of synapses (long-term potentiation: LTP), responsible for learning, memory, and higher cognitive functions. Post-transcriptional regulation is in turn dependent on RNA-binding proteins that, by recognizing and binding brief RNA sequences, base modifications, or secondary/tertiary structures, are able to control maturation, localization, stability, and tr…

learningsynaptic plasticityOrganic ChemistryneurodegenerationRNA-Binding ProteinsBrainGeneral MedicineCatalysisComputer Science ApplicationsmemoryInorganic ChemistryIntrinsically Disordered ProteinsGene Expression RegulationSettore BIO/10 - BiochimicaRNA-binding proteins (RBPs)Settore MED/26 - NeurologiaNervous System Physiological PhenomenaRNA Messengerpost-transcriptional regulation of gene expressionSettore BIO/06 - Anatomia Comparata E CitologiaPhysical and Theoretical ChemistryEVsMolecular Biologyintrinsically disordered regions (IDRs)SpectroscopyInternational journal of molecular sciences
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Role of RNA Motifs in RNA Interaction with Membrane Lipid Rafts: Implications for Therapeutic Applications of Exosomal RNAs

2021

RNA motifs may promote interactions with exosomes (EXO-motifs) and lipid rafts (RAFT-motifs) that are enriched in exosomal membranes. These interactions can promote selective RNA loading into exosomes. We quantified the affinity between RNA aptamers containing various EXO- and RAFT-motifs and membrane lipid rafts in a liposome model of exosomes by determining the dissociation constants. Analysis of the secondary structure of RNA molecules provided data about the possible location of EXO- and RAFT-motifs within the RNA structure. The affinity of RNAs containing RAFT-motifs (UUGU, UCCC, CUCC, CCCU) and some EXO-motifs (CCCU, UCCU) to rafted liposomes is higher in comparison to aptamers withou…

liposomesFRET spectroscopyQH301-705.5AptamerRNA-binding proteinexosomesRNA motifsArticleCatalysisInorganic ChemistryMembrane LipidsMembrane MicrodomainsmicroRNAHumansRNA aptamersNucleotide MotifsBiology (General)Physical and Theoretical ChemistryNucleic acid structureQD1-999Molecular BiologyLipid raftSpectroscopyChemistryOrganic ChemistryRNAGeneral MedicineAptamers NucleotideNon-coding RNAMicrovesiclesComputer Science ApplicationsCell biologyChemistryNucleic Acid ConformationRNAlipids (amino acids peptides and proteins)International Journal of Molecular Sciences
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Binding of RNA Aptamers to Membrane Lipid Rafts: Implications for Exosomal miRNAs Transfer from Cancer to Immune Cells

2020

Intraluminal vesicles (ILVs) are released into the extracellular space as exosomes after the fusion of multivesicular bodies (MVBs) with the plasma membrane. miRNAs are delivered to the raft-like region of MVB by RNA-binding proteins (RBPs). RNA loading into exosomes can be either through direct interaction between RNA and the raft-like region of the MVB membrane, or through interaction between an RBP&ndash

liposomesendocrine systemmacromolecular substancesexosomesArticleCatalysisraftslcsh:ChemistryInorganic ChemistryMembrane LipidsMembrane Microdomainsimmune cellsCell Line TumorNeoplasmsmicroRNAHumansRNA aptamersPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologyLipid raftSpectroscopyChemistrySELEXMacrophagesVesicleCell MembraneOrganic ChemistryMultivesicular BodiesRNA-Binding ProteinsRNADendritic CellsGeneral MedicineRaftAptamers NucleotideMicrovesiclesComputer Science ApplicationsCell biologyKiller Cells NaturalMicroRNAslcsh:Biology (General)lcsh:QD1-999Cancer cellmiRNAslipids (amino acids peptides and proteins)Systematic evolution of ligands by exponential enrichmentInternational Journal of Molecular Sciences
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IGF2BP3 Associates with Proliferative Phenotype and Prognostic Features in B-Cell Acute Lymphoblastic Leukemia

2021

Simple Summary Although the prognosis of acute lymphoblastic leukemia (ALL) has improved significantly during the past decades, ALL remains a major cause of pediatric cancer mortality, and more accurate risk-stratification is required. We investigated IGF2BP3, which has previously been associated with aggressive cancers, and found high and subtype-specific expression of IGF2BP3 in B-cell ALL, that was associated with good outcome in high-risk patients. Results suggest that IGF2BP3 could be useful to improve stratification and prognosis of B-ALL. Abstract The oncofetal protein insulin-like growth factor 2 mRNA-binding protein 3 (IGF2BP3) belongs to a family of RNA-binding proteins involved i…

lähetti-RNAmRNAproliferation3122 Cancersleukemiabiomarkkeritennusteetlcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensinsulin-like growth factor 2 mRNA-binding protein 3 (IGF2BP3)lcsh:RC254-282Articleinsulin-like growth factor 2 mRNA-binding protein 3 (<i>IGF2BP3</i>)akuutti lymfaattinen leukemiapediatric B-cell acute lymphoblastic leukemia1182 Biochemistry cell and molecular biologysyöpätauditproteiinitprognosisproteinCancers
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Translocation (10;11;22)(p14;q24;q12) Characterized by Fluorescence in Situ Hybridization in a Case of Ewing's Tumor

2001

It is well recognized that the identification by classic cytogenetics of t(11;22)(q24;q12) is a useful aid in the accurate diagnosis of Ewing's sarcoma and related tumors. This translocation induces the EWS/FLI-1 fusion transcript, which can be detected by reverse transcription-polymerase chain reaction. Recent studies have also used fluorescence in situ hybridization (FISH) to demonstrate the translocation. The authors coupled classic cytogenetics and FISH on tumor cells from the original specimen, the local recurrence, and the pulmonary metastasis as well as from the xenografted tumors in a case of extraosseous Ewing's sarcoma. FISH analysis not only confirmed the cytogenetic results but …

medicine.medical_specialtyLung NeoplasmsOncogene Proteins FusionChromosomes Human Pair 22Bone NeoplasmsChromosomal translocationSarcoma EwingBiologyTranslocation GeneticPathology and Forensic MedicineImmunoenzyme TechniquesFatal OutcomemedicineHumansChildMolecular BiologyIn Situ Hybridization FluorescenceLegmedicine.diagnostic_testChromosomes Human Pair 10Proto-Oncogene Protein c-fli-1Reverse Transcriptase Polymerase Chain ReactionChromosomes Human Pair 11CytogeneticsChromosomeEwing's tumorDNA NeoplasmSequence Analysis DNACell Biologymedicine.diseaseCombined Modality TherapyFusion transcriptKaryotypingCancer researchFemaleInterphaseSarcomaRNA-Binding Protein EWSTranscription FactorsFluorescence in situ hybridizationDiagnostic Molecular Pathology
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PGC-1α: a master gene that is hard to master

2012

Peroxisome proliferator-activated receptor-γ coactivator-1α (PGC-1α) is a transcriptional coactivator that favorably affects mitochondrial function. This concept is supported by an increasing amount of data including studies in PGC-1α gene-deleted mice, suggesting that PGC-1α is a rescue factor capable of boosting cell metabolism and promoting cell survival. However, this view has now been called into question by a recent study showing that adeno-associated virus-mediated PGC-1α overexpression causes overt cell degeneration in dopaminergic neurons. How is this to be understood, and can these seemingly conflicting findings tell us something about the role of PGC-1α in cell stress and in cont…

medicine.medical_specialtyModels NeurologicalSettore BIO/11 - Biologia MolecolareRNA-binding proteinBiologyMitochondrionSettore BIO/09 - FisiologiaMiceCellular and Molecular NeuroscienceHeat shock proteinInternal medicinemedicineAnimalsHomeostasisHumansReceptorMolecular BiologyTranscription factorHeat-Shock ProteinsMice KnockoutPharmacologyPGC-1α Mitochondria Dopaminergic neurons Transgenic animal Adenovirus Parkinson’s diseaseDopaminergic NeuronsDopaminergicRNA-Binding ProteinsParkinson DiseaseCell BiologyPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaMitochondriaEndocrinologyCell metabolismNerve DegenerationTrans-ActivatorsMolecular MedicineNeuroscienceHomeostasisTranscription FactorsCellular and Molecular Life Sciences
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Thyroid hormones induce sumoylation of the cold shock domain-containing protein PIPPin in developing rat brain and in cultured neurons.

2006

We previously identified a cold shock domain (CSD)-containing protein (PIPPin), expressed at high level in brain cells. PIPPin has the potential to undergo different post-translational modifications and might be a good candidate to regulate the synthesis of specific proteins in response to extracellular stimuli. Here we report the effects of thyroid hormone (T3) on PIPPin expression in developing rat brain. We found that a significant difference among euthyroid- and hypothyroid- newborn rats concerns sumoylation of nuclear PIPPin, that is abolished by hypothyroidism. Moreover, T3-dependence of PIPPin sumoylation has been confirmed in cortical neurons purified from brain cortices and culture…

medicine.medical_specialtySUMO-1 ProteinSUMO proteinDeveloping rat brainNerve Tissue ProteinsEndocrinologyAntithyroid AgentsHypothyroidismPregnancyInternal medicinemedicineExtracellularAnimalsRats WistarCells CulturedCell NucleusCerebral CortexNeuronsbiologyRNA-Binding ProteinsCold-shock domainChromatinProtein Structure TertiaryRatsThyroid hormoneChemically defined mediumCell nucleusmedicine.anatomical_structureHistoneEndocrinologyAnimals NewbornPropylthiouracilPrenatal Exposure Delayed Effectsbiology.proteinTriiodothyronineRNA-binding proteins (RBPs)FemaleRabbitsNucleusEndocrinology
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Sense and Antisense DMPK RNA Foci Accumulate in DM1 Tissues during Development.

2015

International audience; Myotonic dystrophy type 1 (DM1) is caused by an unstable expanded CTG repeat located within the DMPK gene 3'UTR. The nature, severity and age at onset of DM1 symptoms are very variable in patients. Different forms of the disease are described, among which the congenital form (CDM) is the most severe. Molecular mechanisms of DM1 are well characterized for the adult form and involve accumulation of mutant DMPK RNA forming foci in the nucleus. These RNA foci sequester proteins from the MBNL family and deregulate CELF proteins. These proteins are involved in many cellular mechanisms such as alternative splicing, transcriptional, translational and post-translational regul…

musculoskeletal diseasesCCAAT-Enhancer-Binding Protein-deltacongenital hereditary and neonatal diseases and abnormalities[SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiologylcsh:MedicineMice Transgenic[SDV.GEN.GH] Life Sciences [q-bio]/Genetics/Human genetics[SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyMyotonin-Protein KinaseMice[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]AnimalsHumansMyotonic DystrophyRNA AntisenseRNA Messengerlcsh:ScienceMuscle SkeletalCell NucleusMyocardiumlcsh:R[SDV.NEU.NB] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/NeurobiologyBrainGene Expression Regulation DevelopmentalRNA-Binding Proteins[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyEmbryo MammalianAlternative SplicingDisease Models Animal[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human geneticsAnimals Newborn[SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]lcsh:QTrinucleotide Repeat ExpansionSignal TransductionResearch ArticlePloS one
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Muscleblind, BSF and TBPH are mislocalized in the muscle sarcomere of a Drosophila myotonic dystrophy model

2012

SummaryMyotonic dystrophy type 1 (DM1) is a genetic disease caused by the pathological expansion of a CTG trinucleotide repeat in the 3' UTR of the DMPK gene. In the DMPK transcripts, the CUG expansions sequester RNA-binding proteins into nuclear foci, including transcription factors and alternative splicing regulators such as MBNL1. MBNL1 sequestration has been associated with key features of DM1. However, the basis behind a number of molecular and histological alterations in DM1 remain unclear. To help identify new pathogenic components of the disease, we carried out a genetic screen using a Drosophila model of DM1 that expresses 480 interrupted CTG repeats, i(CTG)480, and a collection of…

musculoskeletal diseasesSarcomerescongenital hereditary and neonatal diseases and abnormalitiesNeuroscience (miscellaneous)lcsh:MedicineMedicine (miscellaneous)RNA-binding proteinGenes InsectBiologyMyotonic dystrophyGeneral Biochemistry Genetics and Molecular BiologyAnimals Genetically Modifiedchemistry.chemical_compoundImmunology and Microbiology (miscellaneous)RNA interferencelcsh:PathologymedicineMBNL1AnimalsDrosophila ProteinsHumansMyotonic DystrophyGeneticsMuscleslcsh:RAlternative splicingNuclear ProteinsRNA-Binding ProteinsEpistasis Geneticmedicine.diseaseDisease Models AnimalchemistryGene Knockdown TechniquesDrosophilaFemaleRNA InterferenceTrinucleotide repeat expansionTrinucleotide Repeat ExpansionDrosophila Proteinlcsh:RB1-214Genetic screenResearch ArticleDisease Models & Mechanisms
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