Amyloid β oligomers in Alzheimer's disease pathogenesis, treatment, and diagnosis

KL Viola, WL Klein - Acta neuropathologica, 2015 - Springer
Protein aggregation is common to dozens of diseases including prionoses, diabetes,
Parkinson's and Alzheimer's. Over the past 15 years, there has been a paradigm shift in …

Amyloid β protein and Alzheimer's disease: When computer simulations complement experimental studies

J Nasica-Labouze, PH Nguyen, F Sterpone… - Chemical …, 2015 - ACS Publications
Alzheimer's disease (AD) challenges our society with an annual estimated cost of $1.08
trillion in the United States alone by 2050. 1 AD is a progressive irreversible neurological …

Aβ (1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

Y Xiao, B Ma, D McElheny, S Parthasarathy… - Nature structural & …, 2015 - nature.com
Increasing evidence has suggested that formation and propagation of misfolded aggregates
of 42-residue human amyloid β (Aβ (1–42)), rather than of the more abundant Aβ (1–40) …

[HTML][HTML] Amyloid polymorphism: structural basis and neurobiological relevance

R Tycko - Neuron, 2015 - cell.com
Our understanding of the molecular structures of amyloid fibrils that are associated with
neurodegenerative diseases, of mechanisms by which disease-associated peptides and …

Function and toxicity of amyloid beta and recent therapeutic interventions targeting amyloid beta in Alzheimer's disease

K Rajasekhar, M Chakrabarti… - Chemical …, 2015 - pubs.rsc.org
Amyloidogenesis has been implicated in a broad spectrum of diseases in which amyloid
protein is invariably misfolded and deposited in cells and organs. Alzheimer's disease is one …

Structure-based inhibitors of amyloid beta core suggest a common interface with tau

SL Griner, P Seidler, J Bowler, KA Murray, TP Yang… - Elife, 2019 - elifesciences.org
Alzheimer's disease (AD) pathology is characterized by plaques of amyloid beta (Aβ) and
neurofibrillary tangles of tau. Aβ aggregation is thought to occur at early stages of the …

Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics

A Abedini, A Plesner, P Cao, Z Ridgway, J Zhang… - Elife, 2016 - elifesciences.org
Islet amyloidosis by IAPP contributes to pancreatic β-cell death in diabetes, but the nature of
toxic IAPP species remains elusive. Using concurrent time-resolved biophysical and …

High-resolution probing of early events in amyloid-β aggregation related to Alzheimer's disease

BR Sahoo, SJ Cox, A Ramamoorthy - Chemical Communications, 2020 - pubs.rsc.org
In Alzheimer's disease (AD), soluble oligomers of amyloid-β (Aβ) are emerging as a crucial
entity in driving disease progression as compared to insoluble amyloid deposits. The lacuna …

Key residue for aggregation of amyloid-β peptides

SG Itoh, M Yagi-Utsumi, K Kato… - ACS Chemical …, 2022 - ACS Publications
It is known that oligomers of amyloid-β (Aβ) peptide are associated with Alzheimer's disease.
Aβ has two isoforms: Aβ40 and Aβ42. Although the difference between Aβ40 and Aβ42 is …

Successive stages of amyloid-β self-assembly characterized by solid-state nuclear magnetic resonance with dynamic nuclear polarization

A Potapov, WM Yau, R Ghirlando… - Journal of the …, 2015 - ACS Publications
Self-assembly of amyloid-β (Aβ) peptides in human brain tissue leads to neurodegeneration
in Alzheimer's disease (AD). Amyloid fibrils, whose structures have been extensively …