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 …

Modification of C terminus provides new insights into the mechanism of α-synuclein aggregation

K Afitska, A Fucikova, VV Shvadchak, DA Yushchenko - Biophysical journal, 2017 - cell.com
Aggregation of neuronal protein α-synuclein leads to the formation of amyloid fibrils, which
are associated with the development of Parkinson's disease. The mechanism of α-synuclein …

Role of α-synuclein regions in nucleation and elongation of amyloid fiber assembly

J Gallardo, C Escalona-Noguero… - ACS chemical …, 2020 - ACS Publications
α-Synuclein is an intrinsically disordered protein whose aggregation in the form of amyloid
fibers is directly implicated in Parkinson's disease and other neurological disorders. α …

Dynamic properties of human α-synuclein related to propensity to amyloid fibril formation

S Fujiwara, F Kono, T Matsuo, Y Sugimoto… - Journal of molecular …, 2019 - Elsevier
Abstract α-Synuclein (αSyn) is an intrinsically disordered protein that can form amyloid
fibrils. Fibrils of αSyn are implicated with the pathogenesis of Parkinson's disease and other …

Study of molecular mechanisms of α-synuclein assembly: Insight into a cross-β structure in the N-termini of new α-synuclein fibrils

DN Bloch, Y Miller - ACS omega, 2017 - ACS Publications
Parkinson's disease is characterized by the self-assembly of α-synuclein (AS), in which its
aggregates accumulate in the substantia nigra. The molecular mechanisms of the self …

The effect of truncation on prion-like properties of α-synuclein

M Terada, G Suzuki, T Nonaka, F Kametani… - Journal of Biological …, 2018 - ASBMB
Increasing evidence suggests that α-synuclein (αS) aggregates in brains of individuals with
Parkinson's disease and dementia with Lewy bodies can spread in a prion-like manner …

[HTML][HTML] Sequence-and seed-structure-dependent polymorphic fibrils of alpha-synuclein

G Tanaka, T Yamanaka, Y Furukawa… - … et Biophysica Acta (BBA …, 2019 - Elsevier
Synucleinopathies comprise a diverse group of neurodegenerative diseases including
Parkinson's disease (PD), dementia with Lewy bodies, and multiple system atrophy. These …

The conformation and the aggregation kinetics of α-synuclein depend on the proline residues in its C-terminal region

J Meuvis, M Gerard, L Desender, V Baekelandt… - Biochemistry, 2010 - ACS Publications
The neuronal protein α-synuclein (α-syn) plays a central role in Parkinson's disease (PD).
The pathological features of PD are the loss of dopaminergic neurons in the substantia nigra …

Aromaticity at position 39 in α‐synuclein: A modulator of amyloid fibril assembly and membrane‐bound conformations

FA Buratti, N Boeffinger, HA Garro, JS Flores… - Protein …, 2022 - Wiley Online Library
Recent studies revealed that molecular events related with the physiology and pathology of
αS might be regulated by specific sequence motifs in the primary sequence of αS. The …

NMR unveils an N-terminal interaction interface on acetylated-α-synuclein monomers for recruitment to fibrils

X Yang, B Wang, CL Hoop… - Proceedings of the …, 2021 - National Acad Sciences
Amyloid fibril formation of α-synuclein (αS) is associated with multiple neurodegenerative
diseases, including Parkinson's disease (PD). Growing evidence suggests that progression …