[HTML][HTML] Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR

I Matlahov, PCA van der Wel - Methods, 2018 - Elsevier
Solid-state nuclear magnetic resonance (ssNMR) spectroscopy enables the structural
characterization of a diverse array of biological assemblies that include amyloid fibrils, non …

[HTML][HTML] Mechanosensitive Piezo1 channel in physiology and pathophysiology of the central nervous system

B Zong, F Yu, X Zhang, Y Pang, W Zhao, P Sun… - Ageing Research …, 2023 - Elsevier
Since the discovery of the mechanosensitive Piezo1 channel in 2010, there has been a
significant amount of research conducted to explore its regulatory role in the physiology and …

Water distribution, dynamics, and interactions with Alzheimer's β-amyloid fibrils investigated by solid-state NMR

T Wang, H Jo, WF DeGrado… - Journal of the American …, 2017 - ACS Publications
Water is essential for protein folding and assembly of amyloid fibrils. Internal water cavities
have been proposed for several amyloid fibrils, but no direct structural and dynamical data …

Raman Spectroscopic Insights of Phase-Separated Insulin Aggregates

S Dolui, A Roy, U Pal, S Kundu, E Pandit… - ACS Physical …, 2024 - ACS Publications
Phase-separated protein accumulation through the formation of several aggregate species
is linked to the pathology of several human disorders and diseases. Our current …

Light, water, and melatonin: the synergistic regulation of phase separation in dementia

D Loh, RJ Reiter - International journal of molecular sciences, 2023 - mdpi.com
The swift rise in acceptance of molecular principles defining phase separation by a broad
array of scientific disciplines is shadowed by increasing discoveries linking phase …

Advances in studying protein disorder with solid-state NMR

AB Siemer - Solid state nuclear magnetic resonance, 2020 - Elsevier
Solution NMR is a key tool to study intrinsically disordered proteins (IDPs), whose
importance for biological function is widely accepted. However, disordered proteins are not …

Molecular structure of an N-terminal phosphorylated β-amyloid fibril

ZW Hu, L Vugmeyster, DF Au… - Proceedings of the …, 2019 - National Acad Sciences
The structural polymorphism in β-amyloid (Aβ) plaques from Alzheimer disease (AD) has
been recognized as an important pathological factor. Plaques from sporadic AD patients …

Solvent relaxation NMR: a tool for real-time monitoring water dynamics in protein aggregation landscape

I Chakraborty, RK Kar, D Sarkar, S Kumar… - ACS Chemical …, 2021 - ACS Publications
Solvent dynamics strongly induce the fibrillation of an amyloidogenic system. Probing the
solvation mechanism is crucial as it enables us to predict different proteins' functionalities …

Thermodynamics of amyloid-β fibril elongation: Atomistic details of the transition state

RA Rodriguez, LY Chen… - ACS Chemical …, 2017 - ACS Publications
Amyloid-β (Aβ) fibrils and plaques are one of the hallmarks of Alzheimer's disease. While the
kinetics of fibrillar growth of Aβ have been extensively studied, several vital questions …

The Aggregation Pattern of Aβ1–40 is Altered by the Presence of N‐Truncated Aβ4–40 and/or CuII in a Similar Way through Ionic Interactions

E Stefaniak, E Atrian‐Blasco, W Goch… - … A European Journal, 2021 - Wiley Online Library
Alzheimer's disease (AD) is one of the most common of the multifactorial diseases and is
characterized by a range of abnormal molecular processes, such as the accumulation of …