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 …

Solid-state NMR: Methods for biological solids

S Ahlawat, KR Mote, NA Lakomek… - Chemical Reviews, 2022 - ACS Publications
In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

A solid beta-sheet structure is formed at the surface of FUS droplets during aging

L Emmanouilidis, E Bartalucci, Y Kan, M Ijavi… - Nature Chemical …, 2024 - nature.com
Phase transitions are important to understand cell dynamics, and the maturation of liquid
droplets is relevant to neurodegenerative disorders. We combined NMR and Raman …

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 …

[HTML][HTML] Mechanisms of amyloid formation revealed by solution NMR

TK Karamanos, AP Kalverda, GS Thompson… - Progress in nuclear …, 2015 - Elsevier
Amyloid fibrils are proteinaceous elongated aggregates involved in more than fifty human
diseases. Recent advances in electron microscopy and solid state NMR have allowed the …

Application of NMR to studies of intrinsically disordered proteins

EB Gibbs, EC Cook, SA Showalter - Archives of biochemistry and …, 2017 - Elsevier
The prevalence of intrinsically disordered protein regions, particularly in eukaryotic proteins,
and their clear functional advantages for signaling and gene regulation have created an …

High-resolution NMR characterization of low abundance oligomers of amyloid-β without purification

SA Kotler, JR Brender, S Vivekanandan, Y Suzuki… - Scientific reports, 2015 - nature.com
Alzheimer's disease is characterized by the misfolding and self-assembly of the
amyloidogenic protein amyloid-β (Aβ). The aggregation of Aβ leads to diverse oligomeric …

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 …

New applications of solid-state NMR in structural biology

PCA van der Wel - Emerging topics in life sciences, 2018 - portlandpress.com
Various recent developments in solid-state nuclear magnetic resonance (ssNMR)
spectroscopy have enabled an array of new insights regarding the structure, dynamics, and …

The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway

A Abelein, JP Abrahams, J Danielsson… - JBIC Journal of …, 2014 - Springer
The amyloid β (Aβ) peptides are 39–42 residue-long peptides found in the senile plaques in
the brains of Alzheimer's disease (AD) patients. These peptides self-aggregate in aqueous …