0000000000064313

AUTHOR

Silvia Morante

showing 2 related works from this author

IRIDE: Interdisciplinary research infrastructure based on dual electron linacs and lasers

2014

This paper describes the scientific aims and potentials as well as the preliminary technical design of RUDE, an innovative tool for multi-disciplinary investigations in a wide field of scientific, technological and industrial applications. IRIDE will be a high intensity "particles factory", based on a combination of high duty cycle radio-frequency superconducting electron linacs and of high energy lasers. Conceived to provide unique research possibilities for particle physics, for condensed matter physics, chemistry and material science, for structural biology and industrial applications, IRIDE will open completely new research possibilities and advance our knowledge in many branches of sci…

Nuclear and High Energy PhysicsHigh energySC Linac;Neutron source;FEL;Compton source;Advanced accelerators concepts;Particle physicsSettore FIS/07 - FISICA APPLICATA (A BENI CULTURALI AMBIENTALI BIOLOGIA E MEDICINA)Advanced accelerators conceptTechnical designNOAdvanced accelerators conceptsParticle physicSC Linac; FEL; Particle physics; Neutron source; Compton source; Advanced accelerators conceptsInstrumentationFELPhysicsSC LinacSettore FIS/01 - Fisica SperimentaleAdvanced accelerators concepts; Compton source; FEL; Neutron source; Particle physics; SC Linac; Instrumentation; Nuclear and High Energy PhysicsParticle physicsAdvanced accelerators concepts; Compton source; FEL; Neutron source; Particle physics; SC Linac; Nuclear and High Energy Physics; InstrumentationCompton sourceNeutron sourceWide fieldSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Dual (category theory)Free Electron LaserAdvanced accelerators concepts Compton source FEL Neutron source Particle physics SC LinacAdvanced accelerators concepts; Compton source; FEL; Neutron source; Particle physics; SC Linacadvanced accelerators concepts; particle physics; sc linac; compton source; fel; neutron sourceneutron sourcefree electron lasersSystems engineeringFactory (object-oriented programming)Free electron laser
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Thioflavin T templates amyloid β(1–40) conformation and aggregation pathway

2015

Aβ(1-40) peptide supramolecular assembly and fibril formation processes are widely recognized to have direct implications in the progression of Alzheimer's disease. The molecular basis of this biological process is still unknown and there is a strong need of developing effective strategies to control the occurring events. To this purpose the exploitation of small molecules interacting with Aβ aggregation represents one of the possible routes. Moreover, the use specific labeling has represented so far one of the most common and effective methods to investigate such a process. This possibility in turn rests on the reliability of the probe/labels involved. Here we present evidences of the effe…

Protein StructureSecondaryAβ(1–40) peptideAmyloidProtein ConformationMolecular Sequence DataBiophysicsSupramolecular chemistryMolecular Dynamics SimulationProtein aggregationProtein Aggregation PathologicalBiochemistryProtein Structure SecondarySupramolecular assemblyProtein Aggregateschemistry.chemical_compoundProtein structureAlzheimer DiseasePathologicalSecondary structureAβ(1-40) peptideHumansBenzothiazolesAmino Acid SequenceFluorescent DyesAmyloid beta-PeptidesProtein StabilityOrganic ChemistryAlzheimer's diseaseProtein AggregationSmall moleculePeptide FragmentsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Peptide ConformationAlzheimer's disease; Aβ(1–40) peptide; Protein aggregation; Protein conformation; Secondary structure; Thioflavin T; Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Fluorescence Recovery After Photobleaching; Fluorescent Dyes; Humans; Molecular Dynamics Simulation; Molecular Sequence Data; Peptide Fragments; Protein Aggregates; Protein Aggregation Pathological; Protein Conformation; Protein Multimerization; Protein Stability; Protein Structure Secondary; ThiazolesThiazolesBiophysicBiochemistrychemistryThioflavin TBiophysicsThioflavinProtein MultimerizationFluorescence Recovery After PhotobleachingBiophysical Chemistry
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