[HTML][HTML] Half a century of amyloids: past, present and future

PC Ke, R Zhou, LC Serpell, R Riek… - Chemical Society …, 2020 - pubs.rsc.org
Amyloid diseases are global epidemics with profound health, social and economic
implications and yet remain without a cure. This dire situation calls for research into the …

A new era for understanding amyloid structures and disease

MG Iadanza, MP Jackson, EW Hewitt… - … reviews Molecular cell …, 2018 - nature.com
The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …

[HTML][HTML] The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells

R Cascella, SW Chen, A Bigi, JD Camino… - Nature …, 2021 - nature.com
The self-assembly of α-synuclein (αS) into intraneuronal inclusion bodies is a key
characteristic of Parkinson's disease. To define the nature of the species giving rise to …

Amyloid toxicity in Alzheimer's disease

AB Reiss, HA Arain, MM Stecker… - Reviews in the …, 2018 - degruyter.com
A major feature of Alzheimer's disease (AD) pathology is the plaque composed of
aggregated amyloid-β (Aβ) peptide. Although these plaques may have harmful properties …

[HTML][HTML] Evaluation of peptide/protein self-assembly and aggregation by spectroscopic methods

MF Pignataro, MG Herrera, VI Dodero - Molecules, 2020 - mdpi.com
The self-assembly of proteins is an essential process for a variety of cellular functions
including cell respiration, mobility and division. On the other hand, protein or peptide …

Early diagnosis and treatment of Alzheimer's disease by targeting toxic soluble Aβ oligomers

M Habashi, S Vutla, K Tripathi… - Proceedings of the …, 2022 - National Acad Sciences
Transient soluble oligomers of amyloid-β (Aβ) are toxic and accumulate early prior to
insoluble plaque formation and cognitive impairment in Alzheimer's disease (AD). Synthetic …

[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 …

[HTML][HTML] Effects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies

R Cascella, A Bigi, N Cremades, C Cecchi - Cellular and Molecular Life …, 2022 - Springer
Protein misfolding is a general hallmark of protein deposition diseases, such as Alzheimer's
disease or Parkinson's disease, in which different types of aggregated species (oligomers …

[HTML][HTML] Visualizing and trapping transient oligomers in amyloid assembly pathways

EE Cawood, TK Karamanos, AJ Wilson… - Biophysical chemistry, 2021 - Elsevier
Oligomers which form during amyloid fibril assembly are considered to be key contributors
towards amyloid disease. However, understanding how such intermediates form, their …

[HTML][HTML] Stability matters, too–the thermodynamics of amyloid fibril formation

AK Buell - Chemical Science, 2022 - pubs.rsc.org
Amyloid fibrils are supramolecular homopolymers of proteins that play important roles in
biological functions and disease. These objects have received an exponential increase in …