While misfolding of alpha-synuclein (αSyn) is central to the pathogenesis of Parkinson's
disease (PD), fundamental questions about its structure and function at the synapse remain …

Peripheral membrane proteins associate reversibly with biological membranes that,
compared to protein binding partners, are structurally labile and devoid of specific binding …

The fibrillation of food proteins into amyloid fibrils, which possess unique structures, is
widely acknowledged as a reliable method to enhance protein functionality. Hofmeister ions …

The interactions between proteins and membranes play critical roles in signal transduction,
cell motility, and transport, and they are involved in many types of diseases. Molecular …

Dysregulation of the biosynthesis of cholesterol and other lipids has been implicated in
many neurological diseases, including Parkinson's disease. Misfolding of α‐synuclein (α …

The physical interactome of a protein can be altered upon perturbation, modulating cell
physiology and contributing to disease. Identifying interactome differences of normal and …

The spontaneous self-assembly of α-synuclein (α-syn) into aggregates of different
morphologies is associated with the development of Parkinson's disease. However, the …

Alpha-synuclein (aSyn) is a vertebrate protein, normally found within the presynaptic nerve
terminal and nucleus, which is known to form somatic and neuritic aggregates in certain …

α-Synuclein is an intrinsically disordered protein abundant in presynaptic terminals in
neurons and in synaptic vesicles. α-Synuclein's interaction with lipid bilayers is important not …

Parkinson's disease (PD) is an increasingly prevalent and currently incurable
neurodegenerative disorder linked to the accumulation of α-synuclein (αS) protein …