Abstract α-Synuclein (α-Syn) has been extensively studied for its structural and biophysical
properties owing to its pathophysiological role in Parkinson's disease (PD). Lewy bodies …

The present advances in biology are related to progress in genomics, proteomics, and other
“-omics”, including glycomics, working with a large amount of data regarding human and …

Here, we use single-molecule techniques to study the aggregation of α-synuclein, the
protein whose misfolding and deposition is associated with Parkinson's disease. We identify …

Aggregation of α-synuclein (α-syn) has been linked to the pathogenesis of Parkinson's
disease (PD) and other neurodegenerative diseases. Increasing evidence suggests that …

Amyloids, fibrillar assembly of (poly) peptide chains, are associated with neurodegenerative
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …

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 development of atomic force microscopy (AFM) has opened up a wide range of novel
opportunities in nanoscience and new modalities of observation in complex biological …

The aggregation of α-synuclein, involved in the pathogenesis of several neurodegenerative
disorders such as Parkinson's disease, is enhanced in vitro by biogenic polyamines binding …

Although trace levels of phosphorylated α-synuclein (α-syn) are detectable in normal brains,
nearly all α-syn accumulated within Lewy bodies in Parkinson disease brains is …

The self-assembly of normally soluble proteins into fibrillar amyloid structures is associated
with a range of neurodegenerative disorders, such as Parkinson's and Alzheimer's diseases …