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 amyloid-β oligomer hypothesis: beginning of the third decade

EN Cline, MA Bicca, KL Viola… - Journal of Alzheimer's …, 2018 - content.iospress.com
The amyloid-β oligomer (AβO) hypothesis was introduced in 1998. It proposed that the brain
damage leading to Alzheimer's disease (AD) was instigated by soluble, ligand-like AβOs …

Proteostasis of islet amyloid polypeptide: a molecular perspective of risk factors and protective strategies for type II diabetes

D Milardi, E Gazit, SE Radford, Y Xu… - Chemical …, 2021 - ACS Publications
The possible link between hIAPP accumulation and β-cell death in diabetic patients has
inspired numerous studies focusing on amyloid structures and aggregation pathways of this …

A guide to studying protein aggregation

JAJ Housmans, G Wu, J Schymkowitz… - The FEBS …, 2023 - Wiley Online Library
Disrupted protein folding or decreased protein stability can lead to the accumulation of
(partially) un‐or misfolded proteins, which ultimately cause the formation of protein …

Aβ-oligomers: A potential therapeutic target for Alzheimer's disease

S Ghosh, R Ali, S Verma - International Journal of Biological …, 2023 - Elsevier
The cascade of amyloid formation relates to multiple complex events at the molecular level.
Previous research has established amyloid plaque deposition as the leading cause of …

[HTML][HTML] Atomic force microscopy for single molecule characterisation of protein aggregation

FS Ruggeri, T Šneideris, M Vendruscolo… - Archives of biochemistry …, 2019 - Elsevier
The development of atomic force microscopy (AFM) has opened up a wide range of novel
opportunities in nanoscience and new modalities of observation in complex biological …

Lipids uniquely alter rates of insulin aggregation and lower toxicity of amyloid aggregates

M Matveyenka, S Rizevsky, JP Pellois… - Biochimica et Biophysica …, 2023 - Elsevier
Amyloid formation is a hallmark of many medical diseases including diabetes type 2,
Alzheimer's and Parkinson diseases. Under these pathological conditions, misfolded …

Unsaturation in the fatty acids of phospholipids drastically alters the structure and toxicity of insulin aggregates grown in their presence

M Matveyenka, S Rizevsky… - The journal of physical …, 2022 - ACS Publications
Lipid bilayers play an important role in the pathological assembly of amyloidogenic proteins
and peptides. This assembly yields oligomers and fibrils, which are highly toxic protein …

Complete aggregation pathway of amyloid β (1-40) and (1-42) resolved on an atomically clean interface

PN Nirmalraj, J List, S Battacharya, G Howe, L Xu… - Science …, 2020 - science.org
To visualize amyloid β (Aβ) aggregates requires an uncontaminated and artifact-free
interface. This paper demonstrates the interface between graphene and pure water (verified …

The degree of unsaturation of fatty acids in phosphatidylserine alters the rate of insulin aggregation and the structure and toxicity of amyloid aggregates

M Matveyenka, S Rizevsky, D Kurouski - FEBS letters, 2022 - Wiley Online Library
Phosphatidylserine (PS) in the plasma membrane plays an important role in cell signaling
and apoptosis. Cell degeneration is also linked to numerous amyloid diseases, pathologies …