Search results for " Amy"

showing 10 items of 242 documents

Amyloid precursor protein in platelets of patients with Alzheimer disease: effect of acetylcholinesterase inhibitor treatment.

2001

BACKGROUND:Amyloid precursor protein (APP) forms with apparent molecular weights of 130, 110, and 106 kd are present in human platelets. It has been demonstrated that Alzheimer disease (AD) is specifically associated with a decreased APP forms ratio in platelets. OBJECTIVE:To investigate whether acetylcholinesterase (AChE) inhibitor treatment modifies the ratio of platelet APP forms in patients with AD. PATIENTS AND METHODS:From a large sample of patients with probable AD, 30 with mild to moderate AD were selected. Each patient underwent a clinical evaluation including the Mini-Mental State Examination (MMSE) and platelet APP forms analysis at baseline and after 30 days. During this interva…

Blood PlateletsMalemedicine.medical_specialtyIsoformmedicine.drug_classBlotting WesternAlzheimer disease; biomarker; platelet; Amyloid Precursor Protein; Isoformchemistry.chemical_compoundAmyloid beta-Protein PrecursorArts and Humanities (miscellaneous)PiperidinesDonepezil HydrochlorideInternal medicinemental disordersAmyloid precursor proteinMedicineHumansPlateletDonepezilLongitudinal StudiesDonepezilCholinesteraseAgedamyloid alzheimer diseaseplateletbiologybusiness.industryMiddle AgedAcetylcholinesteraseEndocrinologychemistryAcetylcholinesterase inhibitorEnzyme inhibitorIndansAmyloid Precursor Proteinbiology.proteinbiomarkerSettore MED/26 - NeurologiaFemaleNeurology (clinical)Cholinesterase InhibitorsAlzheimer diseasebusinessmedicine.drugFollow-Up Studies
researchProduct

SERUM CREATINE KINASE LEVEL IN AMYOTROPHIC LATERAL SCLEROSIS: A USEFUL DIAGNOSTIC AID?

2008

...

CK - ALSSettore MED/26 - NeurologiaSERUM CREATINE KINASE AMYOTROPHIC LATERAL SCLEROSIS
researchProduct

Glucagon fibril polymorphism reflects differences in protofilament backbone structure

2010

Amyloid fibrils formed by the 29-residue peptide hormone glucagon at different concentrations have strikingly different morphologies when observed by transmission electron microscopy. Fibrils formed at low concentration (0.25 mg/mL) consist of two or more protofilaments with a regular twist, while fibrils at high concentration (8 mg/mL) consist of two straight protofilaments. Here, we explore the structural differences underlying glucagon polymorphism using proteolytic degradation, linear and circular dichroism, Fourier transform infrared spectroscopy (FTIR), and X-ray fiber diffraction. Morphological differences are perpetuated at all structural levels, indicating that the two fibril class…

Circular dichroismAmyloidProtein FoldingChemistryProtein StabilityCircular DichroismProteolytic enzymesmacromolecular substancesLinear dichroismFibrilGlucagonSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein Structure SecondaryCrystallographyX-Ray DiffractionStructural BiologySpectroscopy Fourier Transform InfraredSide chainFourier transform infrared spectroscopyProtein MultimerizationFiber diffractionMolecular BiologyProtein secondary structurePolymorphism Amyloid Glucagon Structural changesPeptide Hydrolases
researchProduct

Valorization of apple peels through the study of the effects on the amyloid aggregation process of ?-casein

2021

Waste valorization represents one of the main social challenges when promoting a circular economy and environmental sustainability. Here, we evaluated the effect of the polyphenols extracted from apple peels, normally disposed of as waste, on the amyloid aggregation process of ?-casein from bovine milk, a well-used amyloidogenic model system. The effect of the apple peel extract on protein aggregation was examined using a thioflavin T fluorescence assay, Congo red binding assay, circular dichroism, light scattering, and atomic force microscopy. We found that the phenolic extract from the peel of apples of the cultivar "Fuji", cultivated in Sicily (Caltavuturo, Italy), inhibited ?-casein fib…

Circular dichroismMalusAmyloidAmyloidSettore CHIM/10 - Chimica Degli Alimenti&#954INHIBITIONPharmaceutical ScienceOrganic chemistryPROTEINProtein aggregationMicroscopy Atomic ForceFIBRIL FORMATIONArticleAnalytical Chemistry03 medical and health scienceschemistry.chemical_compound0302 clinical medicineQD241-441OLIGOMERSCaseinTRANSTHYRETIN AMYLOIDOSISANTIOXIDANTDrug Discovery-casein amyloid aggregationFood sciencePhysical and Theoretical Chemistrypolyphenolic extract030304 developmental biology0303 health sciencesbiologyChemistryNATURAL POLYPHENOLSCaseinsκ-casein amyloid aggregationbiology.organism_classificationSTATECongo redfruit wasteChemistry (miscellaneous)PolyphenolFIBRILLOGENESISMalusFruit waste; Polyphenolic extract; ?-casein amyloid aggregationMolecular MedicineThioflavinTHIOFLAVIN-T030217 neurology & neurosurgery
researchProduct

Bovine Serum Albumin protofibril-like aggregates formation: Solo but not simple mechanism

2011

We report an experimental study on the model protein Bovine Serum Albumin (BSA), with the aim of elucidating the mechanisms by which a fully folded globular protein undergoes different aggregation pathways leading to the formation of amyloid fibrils or amorphous aggregates. We observe thermally induced formation of fibrillar structures at pH far from the protein isoelectric point. The increase of electrostatic repulsion results in protein destabilization and in modifications of inter and intra-molecular interactions leading to the growth of fibril-like aggregates stabilized by inter-molecular-β sheets. The aggregation kinetics is studied by means of fluorescence techniques, light scattering…

Circular dichroismProtein ConformationGlobular proteinStatic ElectricityBiophysicsProtein aggregationBiochemistryprotein aggregation amyloid fibril fluorescence conformational changeschemistry.chemical_compoundProtein structureAnimalsBenzothiazolesBovine serum albuminMolecular Biologychemistry.chemical_classificationbiologyTemperatureTryptophanSerum Albumin BovineHydrogen-Ion ConcentrationSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)KineticsThiazolesCrystallographyIsoelectric pointchemistryProtein destabilizationbiology.proteinThermodynamicsCattleThioflavinProtein Multimerization
researchProduct

2021

In humans and mammals, effort-based decision-making for monetary or food rewards paradigms contributes to the study of adaptive goal-directed behaviours acquired through reinforcement learning. Chronic distress modelled by repeated exposure to glucocorticoids in rodents induces suboptimal decision-making under uncertainty by impinging on instrumental acquisition and prompting negative valence behaviours. In order to further disentangle the motivational tenets of adaptive decision-making, this study addressed the consequences of enduring distress on relevant effort and reward-processing dimensions. Experimentally, appetitive and consummatory components of motivation were evaluated in adult C…

Cognitive NeuroscienceNoveltyInsular cortexBehavioral NeuroscienceDistresschemistry.chemical_compoundNeuropsychology and Physiological Psychologymedicine.anatomical_structurechemistryCorticosteronemedicineValence (psychology)ReinforcementPsychologyNeuroscienceFOSBBasolateral amygdalaFrontiers in Behavioral Neuroscience
researchProduct

Chronic Distress in Male Mice Impairs Motivation Compromising Both Effort and Reward Processing With Altered Anterior Insular Cortex and Basolateral …

2021

AbstractIn humans and mammals, effort-based decision-making for monetary or food rewards paradigms contribute to the study of adaptive goal-directed behaviours acquired through reinforcement learning. Chronic distress modelled by repeated exposure to glucocorticoids in rodents induces suboptimal decision-making under uncertainty by impinging on instrumental acquisition and prompting negative valence behaviours. In order to further disentangle the motivational tenets of adaptive decision-making, this study addressed the consequences of enduring distress on relevant effort and reward processing dimensions. Experimentally, appetitive and consummatory components of motivation were evaluated in …

Cognitive NeuroscienceeffortInsular cortexBehavioral Neurosciencechemistry.chemical_compoundmotivationCorticosteronemedicineValence (psychology)Reinforcementreward processingOriginal ResearchglucocorticoidsNoveltyDistressNeuropsychology and Physiological Psychologymedicine.anatomical_structurechemistryinsular cortexchronic distressPsychologyNeurosciencebasolateral amygdalaFOSBBasolateral amygdalaNeuroscienceFrontiers in behavioral neuroscience
researchProduct

Survival Strategy of Erwinia amylovora against Copper: Induction of the Viable-but-Nonculturable State

2006

Copper compounds, widely used to control plant-pathogenic bacteria, have traditionally been employed against fire blight, caused by Erwinia amylovora. However, recent studies have shown that some phytopathogenic bacteria enter into the viable-but-nonculturable (VBNC) state in the presence of copper. To determine whether copper kills E. amylovora or induces the VBNC state, a mineral medium without copper or supplemented with 0.005, 0.01, or 0.05 mM Cu2+ was inoculated with 107 CFU/ml of this bacterium and monitored over 9 months. Total and viable cell counts were determined by epifluorescence microscopy using the LIVE/DEAD kit and by flow cytometry with 5-cyano-2,3-ditolyl tetrazolium chlori…

Colony Count MicrobialVirulencechemistry.chemical_elementErwiniaApplied Microbiology and BiotechnologyViable but nonculturableMicrobiologyPyruschemistry.chemical_compoundPlant MicrobiologyErwinia amylovoraPlant DiseasesVirulenceEcologybiologyTetrazolium chloridebiology.organism_classificationEnterobacteriaceaeCopperCulture MediaEriobotryachemistryMicroscopy Electron ScanningBacterial cellular morphologiesCopperBacteriaFood ScienceBiotechnologyApplied and Environmental Microbiology
researchProduct

Molecular mechanisms in thermally induced amyloid formation of Concanavalin A

2008

Concanavalin A amyloid formation
researchProduct

Interacting processes in protein coagulation

1999

A strong interest is currently focused on protein self-association and deposit. This usually involves conformational changes of the entire protein or of a fragment. It can occur even at low concentrations and is responsible for pathologies such as systemic amyloidosis, Alzheimer's and Prion diseases, and other neurodegenerative pathologies. Readily available proteins, exhibiting at low concentration self-association properties related to conformational changes, offer very convenient model systems capable of providing insight into this class of problems. Here we report experiments on bovine serum albumin, showing that the process of conformational change of this protein towards an intermedia…

Conformational changeIntermediate formbiologyChemistryBiochemistrySystemic amyloidosisProtein coagulationBiochemistryStructural Biologybiology.proteinCoagulation (water treatment)Bovine serum albuminMolecular BiologyVolume concentrationProteins: Structure, Function, and Genetics
researchProduct