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A critical concentration of N-terminal pyroglutamylated amyloid beta drives the misfolding of Ab1-42 into more toxic aggregates

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A critical concentration of N-terminal pyroglutamylated amyloid beta drives the misfolding of Ab1-42 into more toxic aggregates

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Structural differences of amyloid-beta fibrils revealed by antibodies from phage display

Influence of the β-sheet content on the mechanical properties of aggregates during amyloid fibrillization

Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity

Self-Assembly of ß-Amyloid Peptides in Cells and on Solid Supports

Fibrillar vs Crystalline Full-Length beta-2-Microglobulin Studied by High-Resolution Solid-State NMR Spectroscopy

Understanding amyloid aggregation by statistical analysis of atomic force microscopy images

1) Trace copper(II) or zinc(II) ions drastically modify the aggregation behaviour of Aβ1–42: an AFM study

Novel Pentameric Thiophene Derivatives for in Vitro and in Vivo Optical Imaging of a Plethora of Protein Aggregates in Cerebral Amyloidoses

Solute energy based REMD

Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrils