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The structure of fibrils from ‘misfolded’ proteins

Current Opinion in Structural Biology, 2015
Recent developments in solid-state NMR have opened the way to the structural analysis of protein fibrils, with the power of studying them at atomic resolution. Solid-state NMR is a relatively new player in the field of structural biology, and reliable approaches to successfully tackle 3D structures have been developed and applied recently.
Meier, Beat H, Böckmann, Anja
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Modulation of Tau Protein Fibrillization by Oleocanthal

Journal of Natural Products, 2012
Among the phenolic compounds extracted from extra virgin olive oil, oleocanthal (1) has attracted considerable attention in the modulation of many human diseases, such as inflammation and Alzheimer's disease (AD). Indeed, 1 is capable of altering the fibrillization of tau protein, which is one of the key factors at the basis of neurodegenerative ...
MONTI, Maria Chiara   +3 more
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Plasma Protein Constituents of Amyloid Fibrils

The Journal of Immunology, 1967
Summary Rabbits immunized with crude whole fibrils from three amyloidotic spleens formed antibodies to the following plasma proteins: γ-A-immunoglobulin, γ-G-immunoglobulin, fibrinogen, a protein with β-globulin mobility and a protein with α-1-globulin mobility (P-component).
E S, Cathcart, F A, Wollheim, A S, Cohen
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Characterization of fibrillated antioxidant whey protein hydrolysate and comparison with fibrillated protein solution

Food Hydrocolloids, 2016
Abstract Whey proteins were hydrolyzed to reach maximum in vitro antioxidant activity, followed by fibrillation via heating at pH 2.0. Heating of either whey protein isolate (WPI) or its antioxidant hydrolysate (WPH) formed fibrillar structures with ...
Mehdi Mohammadian, Ashkan Madadlou
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The biochemical genetics of amyloid fibril proteins

La Ricerca in Clinica e in Laboratorio, 1989
Amyloidoses are a very heterogeneous set of diseases, characterized by extracellular deposition of fibrillar proteins in different tissues. It is still a matter of debate whether the different forms of amyloidosis can share some common etiological mechanisms, or they are completely unrelated. The biochemical characterization of the protein component of
A O, Carbonara, A, Bottaro
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SAS-Based Studies of Protein Fibrillation

2017
Protein fibrillation is associated with a number of fatal amyloid diseases (e.g. Alzheimer's and Parkinson's diseases). From a structural point of view, the aggregation process starts from an ensemble of native states that convert into transiently formed oligomers, higher order assemblies and protofibrils and, finally, fibrils.
Marasini, Carlotta, Vestergaard, Bente
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Kinetics of protein fibrillation controlled by fibril elongation.

Proteins, 2015
Numerous proteins have the ability to assemble into fibrillar aggregates which are of great interest, because they feature in scores of human diseases and many technological products. In the present work, we analyze the kinetics of protein fibrillation when the process is governed solely by elongation of initially appeared fibrils in the protein ...
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Kinetics of protein fibril formation: Methods and mechanisms

International Journal of Biological Macromolecules, 2017
Amyloid fibril formation is a self-assembly reaction induced by favourable conformational changes of proteins leading to a stable, structurally organized aggregates. The deposition of stable protein fibrils in organs and tissues results in many diseases which are generally referred as amyloidosis.
E. Kiran Kumar   +2 more
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White Light with Phosphorescent Protein Fibrils in OLEDs

Nano Letters, 2010
Red and yellow phosphorescent insulin amyloid fibrils are used as guest-emitting species within a blue-emitting polyfluorene matrix in light-emitting diodes. The integration of the phosphorescent Ir-complex into the amyloid structures strongly improves the triplet exciton confinement and allows the fabrication of white-emitting device with a very low ...
Aurora, Rizzo   +4 more
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