α-Synuclein (αsyn) is an abundant brain neuronal protein that can misfold and polymerize to
form toxic fibrils coalescing into pathologic inclusions in neurodegenerative diseases …

The misfolding and pathological aggregation of α-synuclein forming insoluble amyloid
deposits is associated with Parkinson's disease, the second most common …

Small molecules that bind with high affinity and specificity to fibrils of the α-synuclein (αS)
protein have the potential to serve as positron emission tomography (PET) imaging probes …

Excitation energy migration via homo-FRET (Förster resonance energy transfer) is a unique
variant of traditional FRET that involves a non-radiative energy transfer between the dipoles …

Post-translational modifications (PTMs) impact the pathological aggregation of α-synuclein
(αS), a hallmark of Parkinson's disease (PD). Here, we synthesize αS phosphorylated at …

α‐synuclein (αsyn) forms pathologic inclusions in several neurodegenerative diseases
termed synucleinopathies. The inclusions are comprised of αsyn fibrils harboring prion‐like …

Synucleinopathies comprise a diverse group of neurodegenerative diseases including
Parkinson's disease (PD), dementia with Lewy bodies, and multiple system atrophy. These …

Background α-Synuclein (aSyn) aggregation is thought to play a central role in
neurodegenerative disorders termed synucleinopathies, including Parkinson's disease (PD) …

Amyloid fibrils are highly ordered nanoscopic protein aggregates comprising a cross-β
amyloid core and are associated with deadly human diseases. Structural studies have …

Abstract Background: α-Synuclein (aSyn) aggregation is thought to play a central role in
neurodegenerative disorders termed synucleinopathies, including Parkinson's disease (PD) …