α-Synuclein pathology as a target in neurodegenerative diseases
Abstract α-Synuclein misfolds into pathological forms that lead to various neurodegenerative
diseases known collectively as α-synucleinopathies. In this Review, we provide a …
diseases known collectively as α-synucleinopathies. In this Review, we provide a …
Flanking regions, amyloid cores, and polymorphism: the potential interplay underlying structural diversity
The β-sheet–rich amyloid core is the defining feature of protein aggregates associated with
neurodegenerative disorders. Recent investigations have revealed that there exist multiple …
neurodegenerative disorders. Recent investigations have revealed that there exist multiple …
Mass photometric detection and quantification of nanoscale α-synuclein phase separation
Protein liquid–liquid phase separation can lead to disease-related amyloid fibril formation.
The mechanisms of conversion of monomeric protein into condensate droplets and of the …
The mechanisms of conversion of monomeric protein into condensate droplets and of the …
Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein
T Ohgita, H Kono, I Morita, H Oyama, T Shimanouchi… - Scientific reports, 2023 - nature.com
Regulation of α-synuclein (αS) fibril formation is a potent therapeutic strategy for αS-related
neurodegenerative disorders. αS, an intrinsically disordered 140-residue intraneural protein …
neurodegenerative disorders. αS, an intrinsically disordered 140-residue intraneural protein …
Substitution of Met-38 to Ile in γ-synuclein found in two patients with amyotrophic lateral sclerosis induces aggregation into amyloid
LD Aubrey, N Ninkina, SM Ulamec… - Proceedings of the …, 2024 - National Acad Sciences
α-, β-, and γ-Synuclein are intrinsically disordered proteins implicated in physiological
processes in the nervous system of vertebrates. α-synuclein (αSyn) is the amyloidogenic …
processes in the nervous system of vertebrates. α-synuclein (αSyn) is the amyloidogenic …
Mechanisms of enhanced aggregation and fibril formation of Parkinson's disease-related variants of α-synuclein
T Ohgita, N Namba, H Kono, T Shimanouchi, H Saito - Scientific reports, 2022 - nature.com
Aggregation of α-synuclein (α-syn) into amyloid fibrils is closely associated with Parkinson's
disease (PD). Familial mutations or posttranslational truncations in α-syn are known as risk …
disease (PD). Familial mutations or posttranslational truncations in α-syn are known as risk …
Taking charge: metal ions accelerate amyloid aggregation in sequence variants of α-synuclein
Αlpha-synuclein (αS) is an intrinsically disordered protein which exhibits a high degree of
conformational heterogeneity. In vivo, αS experiences various environments which cause …
conformational heterogeneity. In vivo, αS experiences various environments which cause …
Multifaceted interactions mediated by intrinsically disordered regions play key roles in alpha synuclein aggregation
Abstract The aggregation of Alpha Synuclein (α-Syn) into fibrils is associated with the
pathology of several neurodegenerative diseases. Pathologic aggregates of α-Syn adopt …
pathology of several neurodegenerative diseases. Pathologic aggregates of α-Syn adopt …
Millisecond hydrogen/deuterium-exchange mass spectrometry approach to correlate local structure and aggregation in α-synuclein
In Parkinson's disease and other synucleinopathies, α-synuclein misfolds and aggregates.
Its intrinsically disordered nature, however, causes it to adopt several meta-stable …
Its intrinsically disordered nature, however, causes it to adopt several meta-stable …
Dissecting the self-assembly dynamics of imperfect repeats in α-Synuclein
The pathological aggregation of α-synuclein (αS) into amyloid fibrils is the hallmark of
Parkinson's disease (PD). The self-assembly and membrane interactions of αS are mainly …
Parkinson's disease (PD). The self-assembly and membrane interactions of αS are mainly …