This review article provides an overview of the different species that α‐synuclein aggregates
can populate. It also attempts to reconcile conflicting views regarding the cytotoxic roles of …

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

We describe the isolation and detailed structural characterization of stable toxic oligomers of
α-synuclein that have accumulated during the process of amyloid formation. Our approach …

Aggregation of the 140-residue protein α-synuclein (αSN) is a key factor in the etiology of
Parkinson's disease. Although the intensely anionic C-terminal domain (CTD) of αSN does …

Studies of proteins' formation of amyloid fibrils have revealed that potentially cytotoxic
oligomers frequently accumulate during fibril formation. An important question in the context …

Parkinson's disease (PD) is an age-related movement disorder characterized by a
progressive degeneration of dopaminergic neurons in the midbrain. Although the presence …

Oligomeric species of various proteins are linked to the pathogenesis of different
neurodegenerative disorders. Consequently, there is intense focus on the discovery of novel …

Oligomeric forms of amyloid aggregates have been detected in the brains and tissues of
patients suffering from neurodegenerative disorders such as Parkinson's disease, and it is …

Amyloid fibril formation of α-synuclein (αS) is associated with multiple neurodegenerative
diseases, including Parkinson's disease (PD). Growing evidence suggests that progression …

Alpha synuclein (αS) is a~ 14 kDa intrinsically disordered protein. Decades of research have
increased our knowledge on αS yet its physiological function remains largely elusive. The …