Oligomers which form during amyloid fibril assembly are considered to be key contributors
towards amyloid disease. However, understanding how such intermediates form, their …

The study of protein misfolding and aggregation saw resurgence in the last decade.
Aggregation is the main cause of several human neurodegenerative diseases which makes …

Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human
diseases. Recent advances in electron microscopy and solid state NMR have allowed the …

Amyloid disorders cause debilitating illnesses through the formation of toxic protein
aggregates. The mechanisms of amyloid toxicity and the nature of species responsible for …

Highlights•A range of functionally and structurally unrelated proteins form amyloid.•Toxic
intermediates remain elusive, making their targeting a significant challenge.•Design and …

Evolutionary pressure for protein function leads to unavoidable sampling of conformational
states that are at risk of misfolding and aggregation. The resulting tension between …

Depending on external conditions, native proteins may change their structure and undergo
different association routes leading to a large scale polymorphism of the aggregates. This …

Transient oligomers are commonly formed in the early stages of amyloid assembly.
Determining the structure (s) of these species and defining their role (s) in assembly is key to …

α-, β-, and γ-Synuclein are intrinsically disordered proteins implicated in physiological
processes in the nervous system of vertebrates. α-synuclein (αSyn) is the amyloidogenic …

Protein molecules are highly diverse communication platforms and their interaction
repertoire stretches from atoms over small molecules such as sugars and lipids to …