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 …
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 …
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
Phase transitions are important to understand cell dynamics, and the maturation of liquid
droplets is relevant to neurodegenerative disorders. We combined NMR and Raman …
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
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 …
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 …
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 …
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
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 …
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 …
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 …
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
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 …
the brains of Alzheimer's disease (AD) patients. These peptides self-aggregate in aqueous …