Intense efforts to detect, diagnose, and analyze the kinetic and structural properties of
amyloid fibrils have generated a powerful toolkit of amyloid-specific molecular probes. Since …

Noncovalent, extrinsic fluorescent dyes are applied in various fields of protein analysis, eg to
characterize folding intermediates, measure surface hydrophobicity, and detect aggregation …

Formation of amyloid fibrils underlies a wide range of human disorders, including
Alzheimer's and prion diseases. The amyloid fibrils can be readily detected thanks to …

The formation of amyloid fibrils by the intrinsically disordered protein α-synuclein is a
hallmark of Parkinson disease. To characterize the microscopic steps in the mechanism of …

Control and analysis of protein aggregation is an increasing challenge to pharmaceutical
research and development. Due to the nature of protein interactions, protein aggregation …

Because understanding amyloid fibrillation in molecular detail is essential for development
of strategies to control amyloid formation and overcome neurodegenerative disorders …

In this review, we attempt to give a concise overview of recent progress made in mechanistic
understanding of protein aggregation, particulate formation and protein solution rheology …

Amyloid fibrillation of proteins is associated with a great variety of pathologic conditions.
Development of new molecules that can monitor amyloidosis kinetics and inhibit fibril …

Over the past two decades, there has been considerable research interest in the use of
nanoparticles in the study of protein and peptide aggregation, and of amyloid-related …

Protein aggregation leading to the formation of amyloid fibrils has various adverse effects on
human health ranging from fatigue and numbness to organ failure and death in extreme …