The accumulation of an inherently disordered protein α-synuclein (α-syn) aggregates in
brain tissue play a pivotal role in the pathology and etiology of Parkinson's disease …

The aberrant formation of α-synuclein (Syn) aggregates, varying in size, structure and
morphology, has been linked to the development of Parkinson's disease. In the early stages …

The aggregation of α-synuclein (A-syn) has been implicated strongly in Parkinson's disease
(PD). In vitro studies established A-syn to be a member of the intrinsically disordered protein …

Intraneuronal aggregation of the intrinsically disordered protein α-synuclein is at the core of
Parkinson's disease and related neurodegenerative disorders. Several reports show that the …

Aggregation of α-Synuclein (α-Syn) into amyloid fibrils is known to be associated with the
pathogenesis of Parkinson's disease (PD). Several missense mutations of the α-Syn gene …

Aggregation of α-synuclein (α-syn) is associated with the manifestation of various
pathogenic synucleinopathies, including Parkinson's disease attributed to both genetic and …

Abstract Alpha-synuclein (α-Syn) is a small presynaptic protein of 140 amino acids. Its
pathologic intracellular aggregation within the central nervous system yields protein fibrillar …

The synucleins are a family of natively unstructured proteins consisting of α-, β-, and γ-
synuclein which are primarily expressed in neurons. They have been linked to a wide variety …

Human α-Synuclein (αSyn) is a natively unfolded protein whose aggregation into amyloid
fibrils is involved in the pathology of Parkinson disease. A full comprehension of the …

Misfolding and aggregation of proteins are common threads linking a number of important
human health problems, including various neurodegenerative disorders such as Parkinson's …