Search results for "Protein Aggregate"

showing 10 items of 29 documents

Introduction

2009

BiochemistryMuscular Diseasesbusiness.industryGeneral NeuroscienceMedicineAnimalsHumansNeurology (clinical)Protein aggregationMINI‐SYMPOSIUM: Protein Aggregate MyopathiesbusinessPathology and Forensic Medicine
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Automatic Counting of Intra-Cellular Ribonucleo-Protein Aggregates in Saccharomyces cerevisiae Using a Textural Approach.

2019

AbstractIn the context of microbiology, recent studies show the importance of ribonucleo-protein aggregates (RNPs) for the understanding of mechanisms involved in cell responses to specific environmental conditions. The assembly and disassembly of aggregates is a dynamic process, the characterization of the stage of their evolution can be performed by the evaluation of their number. The aim of this study is to propose a method to automatically determine the count of RNPs. We show that the determination of a precise count is an issue by itself and hence, we propose three textural approaches: a classical point of view using Haralick features, a frequency point of view with generalized Fourier…

CytoplasmSaccharomyces cerevisiae ProteinsZernike polynomialsComputer scienceSaccharomyces cerevisiaeGreen Fluorescent Proteins0211 other engineering and technologiessub-cellular structuresContext (language use)02 engineering and technologySaccharomyces cerevisiaeProtein aggregationribonucleo-protein aggregatesCytoplasmic GranulesModels BiologicalPoly(A)-Binding Proteins03 medical and health sciencessymbols.namesakeProtein Aggregates[SDV.IDA]Life Sciences [q-bio]/Food engineeringGeneralized Fourier descriptorsInstrumentation030304 developmental biology021110 strategic defence & security studies0303 health sciencesFusionHaralickbiologyZernikeA proteinbiology.organism_classificationFourier transformMicroscopy FluorescenceRibonucleoproteinssymbolsBiological systemMicroscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada
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Blue autofluorescence in protein aggregates “lighted on” by UV induced oxidation

2019

Oxidation of amino acid side chains in protein structure can be induced by UV irradiation leading to critical changes in molecular structure possibly modifying protein stability and bioactivity. Here we show, by using a combination of multiple spectroscopic techniques and Fluorescence Lifetime Imaging, that UV-light exposure induces irreversible oxidation processes in Ubiquitin structure. In particular, the growth of a new autofluorescence peak in the blue region is detected, that we attribute to tyrosine oxidation products. Blue autofluorescence intensity is found to progressively increase also during aggregation processes leading to the formation of aggregates of non-amyloid nature. Signi…

Dityrosine formation0301 basic medicineAmyloidUltraviolet RaysBiophysicsPeptideProtein aggregationAmyloid autofluorescence; Dityrosine formation; Fluorescence lifetime imaging; Oxidative stress; UbiquitinFluorescence lifetime imagingBiochemistryFluorescenceAnalytical ChemistryProtein Aggregates03 medical and health sciences0302 clinical medicineProtein structureHumansTyrosineMolecular Biologychemistry.chemical_classificationAmyloid beta-PeptidesUbiquitinChemistryFluorescenceAmino acidAutofluorescence030104 developmental biologyBiophysicsOxidative streAmyloid autofluorescenceOxidation-Reduction030217 neurology & neurosurgeryBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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The dark side of foetal bovine serum in extracellular vesicle studies

2022

Extracellular vesicles (EVs) have been shown to be involved in cell-cell communication and to take part in both physiological and pathological processes. Thanks to their exclusive cargo, which includes proteins, lipids, and nucleic acids from the originating cells, they are gaining interest as potential biomarkers of disease. In recent years, their appealing features have been fascinating researchers from all over the world, thus increasing the number of in vitro studies focused on EV release, content, and biological activities. Cultured cell lines are the most-used source of EVs; however, the EVs released in cell cultures are influenced by the cell culture conditions, such as the use of fo…

Extracellular VesiclesProtein AggregatesHistologyNucleic AcidsRNASerum Albumin BovineCell Biologycell culture contaminants extracellular vesicles foetal bovine serumLipidsBiomarkersCulture Media
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Phasor FLIM analysis of Thioflavin T fluorescence in protein amyloid aggregates: Mapping molecular interactions.

Thioflavin T (ThT) is a worldwide used dye to monitor protein aggregation as it stains with a certain specificity amyloid structures. The interactions between ThT and its hosts are largely studied suggesting that fluorescence properties of this dye critically depend both on the environment rigidity, electrostatic and hydrophobic properties as well as on molecular details binding site structure. Here FLIM and phasor approach analysis are used to exploit ThT amyloid interactions and, in turn, to address polymorphism and structural heterogeneity of amyloid species mapping aggregate-to-aggregate structural differences and revealing details of molecular architecture within the same aggregate.

FLIMprotein aggregateThioflavin Tphasor amyloidSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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Probing ensemble polymorphism and single aggregate structural heterogeneity in insulin amyloid self-assembly.

2020

Ensembles of protein aggregates are characterized by a nano- and micro-scale heterogeneity of the species. This diversity translates into a variety of effects that protein aggregates may have in biological systems, both in connection to neurodegenerative diseases and immunogenic risk of protein drug products. Moreover, this naturally occurring variety offers unique opportunities in the field of protein-based biomaterials. In the above-mentioned fields, the isolation and structural analysis of the different amyloid types within the same ensemble remain a priority, still representing a significant experimental challenge. Here we address such complexity in the case of insulin for its relevance…

Fluorescence-lifetime imaging microscopyAmyloidFIBRIL POLYMORPHISMPHASOR APPROACHSURFACESpheruliteProtein ConformationSurface Propertiesmedicine.medical_treatmentBETATHIOFLAVIN-T FLUORESCENCE02 engineering and technologyMicro-FTIRProtein aggregation010402 general chemistryFibril01 natural sciencesFluorescence lifetime imagingBiomaterialsProtein AggregatesColloid and Surface ChemistryBINDINGHuman insulinmedicineInsulinParticle SizeSECONDARY STRUCTURESPHERULITESChemistryInsulinAmyloidosisOptical ImagingMICROSCOPY021001 nanoscience & nanotechnologymedicine.disease0104 chemical sciencesSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsBiopharmaceuticalMicroscopy FluorescenceAmyloid structureVisible and subvisible particlesBiophysicsThioflavin TSelf-assemblyHeterogeneity0210 nano-technologyInfrared microscopyPROTEIN AGGREGATIONJournal of colloid and interface science
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Histopathology of Skeletal Muscle in a Distal Motor Neuropathy Associated with a Mutant CCT5 Subunit: Clues for Future Developments to Improve Differ…

2023

Genetic chaperonopathies are rare but, because of misdiagnosis, there are probably more cases than those that are recorded in the literature and databases. This occurs because practitioners are generally unaware of the existence and/or the symptoms and signs of chaperonopathies. It is necessary to educate the medical community about these diseases and, with research, to unveil their mechanisms. The structure and functions of various chaperones in vitro have been studied, but information on the impact of mutant chaperones in humans, in vivo, is scarce. Here, we present a succinct review of the most salient abnormalities of skeletal muscle, based on our earlier report of a patient who carried…

General Immunology and Microbiologymuscle pathologydesminmolecular dynamics simulationsmolecular chaperonehuman CCTGeneral Biochemistry Genetics and Molecular BiologyCCT5 mutationdistal neuropathieprotein aggregatechaperone systemimmunohistochemistrychaperonopathieskeletal muscleimmunofluorescenceGeneral Agricultural and Biological Sciencesapical domainBiology
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Garcinoic acid prevents β-amyloid (Aβ) deposition in the mouse brain

2020

Garcinoic acid (GA or δ-T3-13'COOH), is a natural vitamin E metabolite that has preliminarily been identified as a modulator of nuclear receptors involved in β-amyloid (Aβ) metabolism and progression of Alzheimer's disease (AD). In this study, we investigated GA's effects on Aβ oligomer formation and deposition. Specifically, we compared them with those of other vitamin E analogs and the soy isoflavone genistein, a natural agonist of peroxisome proliferator–activated receptor γ (PPARγ) that has therapeutic potential for managing AD. GA significantly reduced Aβ aggregation and accumulation in mouse cortical astrocytes. Similarly to genistein, GA up-regulated PPARγ expression and apolipoprote…

Male0301 basic medicineApolipoprotein EBiologiamedicine.medical_treatmentMetaboliteGenisteinFisiologiavitamin EPharmacologyProtein Aggregation PathologicalBiochemistry)protein aggregationgenisteinMiceProtein Aggregates03 medical and health scienceschemistry.chemical_compoundperoxisome proliferator-activated receptor gamma (PPARγ)neurodegenerative diseaseNeurobiologygarcinoic acidmedicineAnimalsBenzopyranstocotrienolReceptorMolecular BiologyPregnane X receptorAmyloid beta-Peptidespregnane X receptor (PXR)peroxisome proliferator-activated receptor (PPAR)030102 biochemistry & molecular biologyVitamin EBrainCell BiologyAlzheimer's diseasetocopherol030104 developmental biologyNuclear receptorchemistryperoxisome proliferator-activated receptor gamma (PPAR gamma)amyloid-beta (AB)apolipoprotein E (ApoETocotrienolAlzheimer diseaseapolipoprotein E (ApoE)
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The Anti-amyloid Compound DO1 Decreases Plaque Pathology and Neuroinflammation-Related Expression Changes in 5xFAD Transgenic Mice

2018

Self-propagating amyloid-β (Aβ) aggregates or seeds possibly drive pathogenesis of Alzheimer's disease (AD). Small molecules targeting such structures might act therapeutically in vivo. Here, a fluorescence polarization assay was established that enables the detection of compound effects on both seeded and spontaneous Aβ42 aggregation. In a focused screen of anti-amyloid compounds, we identified Disperse Orange 1 (DO1) ([4-((4-nitrophenyl)diazenyl)-N-phenylaniline]), a small molecule that potently delays both seeded and non-seeded Aβ42 polymerization at substoichiometric concentrations. Mechanistic studies revealed that DO1 disrupts preformed fibrillar assemblies of synthetic Aβ42 peptides …

MaleGenetically modified mouse1303 BiochemistryAmyloid10017 Institute of AnatomyClinical BiochemistryMice TransgenicPlaque Amyloid610 Medicine & healthBiologyProtein aggregation1308 Clinical Biochemistry01 natural sciencesBiochemistryPolymerizationPathogenesisMiceProtein AggregatesStructure-Activity RelationshipAlzheimer DiseaseGene expressionDrug Discovery1312 Molecular BiologyAnimalsColoring AgentsMolecular BiologyNeuroinflammationInflammationPharmacologyAmyloid beta-PeptidesDose-Response Relationship DrugMolecular Structure010405 organic chemistry3002 Drug DiscoveryBrainSmall moleculeMolecular medicine0104 chemical sciencesCell biologyMice Inbred C57BL3004 Pharmacology10036 Medical Clinic1313 Molecular Medicine570 Life sciences; biologyMolecular MedicineFemaleAzo Compounds
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The route to protein aggregate superstructures: Particulates and amyloid-like spherulites.

2015

AbstractDepending on external conditions, native proteins may change their structure and undergo different association routes leading to a large scale polymorphism of the aggregates. This feature has been widely observed but is not fully understood yet. This review focuses on morphologies, physico-chemical properties and mechanisms of formation of amyloid structures and protein superstructures. In particular, the main focus will be on protein particulates and amyloid-like spherulites, briefly summarizing possible experimental methods of analysis. Moreover, we will highlight the role of protein conformational changes and dominant forces in driving association together with their connection w…

Models MolecularAmyloidAmyloid Superstructures Protein aggregation spectroscopyProtein superstructureProtein ConformationBiophysicsNanotechnologyProtein aggregationProtein particulateBiochemistryProtein Aggregation PathologicalProtein AggregatesX-Ray DiffractionStructural BiologyElectrostaticsGeneticsHumansMolecular BiologyAmyloid likeAmyloid-like spheruliteChemistryCell BiologyConformational changeSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Microscopy Fluorescence MultiphotonModels ChemicalAggregate structureThermodynamicsExperimental methodsProtein aggregationFEBS letters
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