Interactions between the intrinsically disordered proteins β‐Synuclein and α‐Synuclein

JK Williams, X Yang, J Baum - Proteomics, 2018 - Wiley Online Library
Several intrinsically disordered proteins have been implicated in the process of amyloid fibril
formation in neurodegenerative disease, and developing approaches to inhibit the …

Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies

CH Lo, CKW Lim, Z Ding, SP Wickramasinghe… - Alzheimer's & …, 2019 - Elsevier
Objective Understanding the heterogeneous pathology in Alzheimer's disease and related
tauopathies is one of the most urgent and fundamental challenges facing the discovery of …

Critical nucleus of Greek-key-like core of α-synuclein protofibril and its disruption by dopamine and norepinephrine

Y Zou, Z Qian, Y Gong, Y Tang, G Wei… - Physical Chemistry …, 2020 - pubs.rsc.org
The formation of amyloid fibrils by α-synuclein (αS) protein inside the Lewy bodies and Lewy
neurites is the prominent pathological hallmark of Parkinson's disease (PD). The fibrillation …

Potent inhibitors of toxic alpha-synuclein identified via cellular time-resolved FRET biosensors

AR Braun, EE Liao, M Horvath, P Kalra… - npj Parkinson's …, 2021 - nature.com
We have developed a high-throughput drug discovery platform, measuring fluorescence
resonance energy transfer (FRET) with fluorescent alpha-synuclein (αSN) biosensors, to …

[HTML][HTML] Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity

A Carija, F Pinheiro, J Pujols, IC Brás, DF Lázaro… - Redox biology, 2019 - Elsevier
The aggregation of α-synuclein (α-syn) into amyloid fibrils is a major pathological hallmark of
Parkinson's disease (PD) and other synucleinopathies. The mechanisms underlying the …

CMT-3 targets different α-synuclein aggregates mitigating their toxic and inflammogenic effects

F González-Lizárraga, D Ploper, CL Ávila, SB Socías… - Scientific reports, 2020 - nature.com
Parkinson's disease (PD) is a neurodegenerative disorder for which only symptomatic
treatments are available. Repurposing drugs that target α-synuclein aggregation …

Threonine cavities are targetable motifs that control alpha-synuclein fibril growth

N Nathan Kochen, V Vasandani… - ACS chemical …, 2022 - ACS Publications
Recent high-resolution structures of alpha-synuclein (aSyn) fibrils offer promise for rational
approaches to drug discovery for Parkinson's disease and Lewy body dementia. Harnessing …

Post-translational modification sites are present in hydrophilic cavities of alpha-synuclein, tau, FUS, and TDP-43 fibrils: A molecular dynamics study

NN Kochen, D Seaney, V Vasandani, MG Murray… - Biophysical …, 2024 - cell.com
The molecular determinants of protein aggregation into amyloid fibrils are currently poorly
understood and are required to develop targeted therapies capable of modulating this …

The Interaction of Curcumin and Rosmarinic Acid with Non‐Amyloid‐Component Domain of Alpha‐Synuclein: A Molecular Dynamics Study

M Rezaei Kamelabad, J Jahanbin Sardroodi… - …, 2020 - Wiley Online Library
One notable phenomenon in the Parkinson's disease (PD) treatment is the identification of
inhibitors of the self‐assembly of Alpha‐Synuclein (AS) protein. Here, the interactions of two …

Structural influence and interactive binding behavior of dopamine and norepinephrine on the greek-key-like core of α-Synuclein protofibril revealed by molecular …

Y Zou, Z Liu, Z Zhu, Z Qian - Processes, 2019 - mdpi.com
The pathogenesis of Parkinson's disease (PD) is closely associated with the aggregation of
α-synuclein (αS) protein. Finding the effective inhibitors of αS aggregation has been …