Amyloid oligomers: A joint experimental/computational perspective on Alzheimer's disease, Parkinson's disease, type II diabetes, and amyotrophic lateral sclerosis

PH Nguyen, A Ramamoorthy, BR Sahoo… - Chemical …, 2021 - ACS Publications
Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Alpha-synuclein oligomers: a new hope

N Bengoa-Vergniory, RF Roberts, R Wade-Martins… - Acta …, 2017 - Springer
Alpha-synuclein is a protein implicated in Parkinson's disease and thought to be one of the
main pathological drivers in the disease, although it remains unclear how this protein elicits …

Lewy pathology in Parkinson's disease consists of crowded organelles and lipid membranes

SH Shahmoradian, AJ Lewis, C Genoud, J Hench… - Nature …, 2019 - nature.com
Parkinson's disease, the most common age-related movement disorder, is a progressive
neurodegenerative disease with unclear etiology. Key neuropathological hallmarks are …

Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers

G Fusco, SW Chen, PTF Williamson, R Cascella… - Science, 2017 - science.org
Oligomeric species populated during the aggregation process of α-synuclein have been
linked to neuronal impairment in Parkinson's disease and related neurodegenerative …

Widespread occurrence of the droplet state of proteins in the human proteome

M Hardenberg, A Horvath, V Ambrus… - Proceedings of the …, 2020 - National Acad Sciences
A wide range of proteins have been reported to condensate into a dense liquid phase,
forming a reversible droplet state. Failure in the control of the droplet state can lead to the …

Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2

TR Alderson, I Pritišanac, Đ Kolarić… - Proceedings of the …, 2023 - National Acad Sciences
The AlphaFold Protein Structure Database contains predicted structures for millions of
proteins. For the majority of human proteins that contain intrinsically disordered regions …

C-terminal calcium binding of α-synuclein modulates synaptic vesicle interaction

J Lautenschläger, AD Stephens, G Fusco… - Nature …, 2018 - nature.com
Alpha-synuclein is known to bind to small unilamellar vesicles (SUVs) via its N terminus,
which forms an amphipathic alpha-helix upon membrane interaction. Here we show that …

[HTML][HTML] Amyloid structures: much more than just a cross-β fold

R Gallardo, NA Ranson, SE Radford - Current opinion in structural biology, 2020 - Elsevier
Highlights•New structures have shown that there is a remarkable diversity and complexity of
the amyloid fold.•The same sequence forms different amyloid structures in different …

Implications of peptide assemblies in amyloid diseases

PC Ke, MA Sani, F Ding, A Kakinen, I Javed… - Chemical Society …, 2017 - pubs.rsc.org
Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the
quality of life of millions worldwide, with profound social and economic implications. Despite …

A short motif in the N-terminal region of α-synuclein is critical for both aggregation and function

CPA Doherty, SM Ulamec, R Maya-Martinez… - Nature structural & …, 2020 - nature.com
Aggregation of human α-synuclein (αSyn) is linked to Parkinson's disease (PD) pathology.
The central region of the αSyn sequence contains the non-amyloid β-component (NAC) …