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Oxidation enhances human serum albumin thermal stability and changes the routes of amyloid fibril formationThe Inhibitory Effect of Natural Products on Protein Fibrillation May Be Caused by Degradation Products--A Study Using Aloin and InsulinUnlocked concanavalin A forms amyloid-like fibrils from coagulation of long-lived "crinkled" intermediates.Penetratin-Mediated Transepithelial Insulin Permeation: Importance of Cationic Residues and pH for Complexation and Permeation.The route to protein aggregate superstructures: Particulates and amyloid-like spherulites.Thioflavin T templates amyloid β(1-40) conformation and aggregation pathway.Direct Correlation Between Ligand-Induced α-Synuclein Oligomers and Amyloid-like Fibril Growth.Protein/lipid coaggregates are formed during α-synuclein-induced disruption of lipid bilayers.Self-organization pathways and spatial heterogeneity in insulin amyloid fibril formation.Interaction with prefibrillar species and amyloid-like fibrils changes the stiffness of lipid bilayers.Thioflavin T hydroxylation at basic pH and its effect on amyloid fibril detection.Trifluoroethanol modulates α-synuclein amyloid-like aggregate formation, stability and dissolution.Observation of the Early Structural Changes Leading to the Formation of Protein Superstructures.Secondary nucleation and accessible surface in insulin amyloid fibril formation.Tracking the heterogeneous distribution of amyloid spherulites and their population balance with free fibrils.Electrostatics controls the formation of amyloid superstructures in protein aggregation.An amphiphilic-DNA platform for the design of crystalline frameworks with programmable structure and functionalityMicrofluidics Reveals a Flow-Induced Large-Scale Polymorphism of Protein AggregatesFactors affecting the formation of insulin amyloid spherulitesEthanol Controls the Self-Assembly and Mesoscopic Properties of Human Insulin Amyloid SpherulitesEarly Stage Alpha-Synuclein Amyloid Fibrils are Reservoirs of Membrane-Binding SpeciesBovine Serum Albumin protofibril-like aggregates formation: Solo but not simple mechanismEffects of confinement on insulin amyloid fibrils formationOxidation processes in Sicilian olive oils investigated by a combination of optical and EPR spectroscopy
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
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հետազոտող
@hy
name
Vito Foderà
@ast
Vito Foderà
@en
Vito Foderà
@es
Vito Foderà
@nl
Vito Foderà
@sl
type
label
Vito Foderà
@ast
Vito Foderà
@en
Vito Foderà
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Vito Foderà
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Vito Foderà
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prefLabel
Vito Foderà
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Vito Foderà
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Vito Foderà
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Vito Foderà
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Vito Foderà
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P1053
F-9029-2010
P106
P1153
22979384600
P1960
LGheQ08AAAAJ
P2038
Vito_Fodera
P21
P31
P3829
P496
0000-0003-2855-0568