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 …

Amyloid-type protein aggregation and prion-like properties of amyloids

D Willbold, B Strodel, GF Schröder, W Hoyer… - Chemical …, 2021 - ACS Publications
This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

Mechanistic insight into the design of chemical tools to control multiple pathogenic features in Alzheimer's disease

J Han, Z Du, MH Lim - Accounts of Chemical Research, 2021 - ACS Publications
Conspectus Alzheimer's disease (AD) is the most common form of dementia and is
characterized by memory loss and cognitive decline. Approximately 50 million people …

Imaging Amyloid‐β Membrane Interactions: Ion‐Channel Pores and Lipid‐Bilayer Permeability in Alzheimer's Disease

JH Viles - Angewandte Chemie International Edition, 2023 - Wiley Online Library
The accumulation of the amyloid‐β peptides (Aβ) is central to the development of
Alzheimer's disease. The mechanism by which Aβ triggers a cascade of events that leads to …

A mechanistic survey of Alzheimer's disease

Y Tang, D Zhang, X Gong, J Zheng - Biophysical chemistry, 2022 - Elsevier
Alzheimer's disease (AD) is the most common, age-dependent neurodegenerative disorder.
While AD has been intensively studied from different aspects, there is no effective cure for …

Experimental NOE, chemical shift, and proline isomerization data provide detailed insights into amelotin oligomerization

SC Chiliveri, Y Shen, JL Baber, J Ying… - Journal of the …, 2023 - ACS Publications
Amelotin is an intrinsically disordered protein (IDP) rich in Pro residues and is involved in
hydroxyapatite mineralization. It rapidly oligomerizes under physiological conditions of pH …

[HTML][HTML] Mixing Aβ (1–40) and Aβ (1–42) peptides generates unique amyloid fibrils

L Cerofolini, E Ravera, S Bologna… - Chemical …, 2020 - pubs.rsc.org
Recent structural studies show distinct morphologies for the fibrils of Aβ (1–42) and Aβ (1–
40), which are believed not to co-fibrillize. We describe here a novel, structurally-uniform 1: 1 …

[HTML][HTML] Advances in aptamers against Aβ and applications in Aβ detection and regulation for Alzheimer's disease

Y Zheng, L Zhang, J Zhao, L Li, M Wang, P Gao… - Theranostics, 2022 - ncbi.nlm.nih.gov
Alzheimer's disease (AD) is an irreversible neurodegenerative disease, causing profound
social and economic implications. Early diagnosis and treatment of AD have faced great …

Kinetics theories to understand the mechanism of aggregation of a protein and to design strategies for its inhibition

S Sharma, P Modi, G Sharma, S Deep - Biophysical Chemistry, 2021 - Elsevier
Protein aggregation phenomenon is closely related to the formation of amyloids which
results in many neurodegenerative diseases like Alzheimer's, Parkinson's, Huntington's, and …

High-throughput screening at the membrane interface reveals inhibitors of amyloid-β

SJ Cox, B Lam, A Prasad, HA Marietta, NV Stander… - Biochemistry, 2020 - ACS Publications
Aggregation and the formation of oligomeric intermediates of amyloid-β (Aβ) at the
membrane interface of neuronal cells are implicated in the cellular toxicity and pathology of …