Recent progress on understanding the mechanisms of amyloid nucleation

E Chatani, N Yamamoto - Biophysical reviews, 2018 - Springer
Amyloid fibrils are supramolecular protein assemblies with a fibrous morphology and cross-
β structure. The formation of amyloid fibrils typically follows a nucleation-dependent …

Current understanding of the structure, stability and dynamic properties of amyloid fibrils

E Chatani, K Yuzu, Y Ohhashi, Y Goto - International journal of molecular …, 2021 - mdpi.com
Amyloid fibrils are supramolecular protein assemblies represented by a cross-β structure
and fibrous morphology, whose structural architecture has been previously investigated …

Familial Alzheimer's disease mutations within the amyloid precursor protein alter the aggregation and conformation of the amyloid-β peptide

A Hatami, S Monjazeb, S Milton, CG Glabe - Journal of Biological Chemistry, 2017 - ASBMB
Most cases of Alzheimer's disease (AD) are sporadic, but a small percentage of AD cases,
called familial AD (FAD), are associated with mutations in presenilin 1, presenilin 2, or the …

Direct observation of amyloid fibril growth, propagation, and adaptation

T Ban, K Yamaguchi, Y Goto - Accounts of chemical research, 2006 - ACS Publications
Amyloid fibrils form through nucleation and growth. To clarify the mechanism involved, direct
observations of both processes are important. First, seed-dependent fibril growth of β2 …

Hydrogen/deuterium exchange-mass spectrometry: a powerful tool for probing protein structure, dynamics and interactions

Y Tsutsui, PL Wintrode - Current medicinal chemistry, 2007 - ingentaconnect.com
Knowledge of the structure and dynamics of proteins and protein assemblies is critical both
for understanding the molecular basis of physiological and patho-physiological processes …

Water molecular system dynamics associated with amyloidogenic nucleation as revealed by real time near infrared spectroscopy and aquaphotomics

E Chatani, Y Tsuchisaka, Y Masuda, R Tsenkova - PLoS One, 2014 - journals.plos.org
The formation of amyloid fibrils proceeds via a nucleation-dependent mechanism in which
nucleation phase is generally associated with a high free energy resulting in the rate-limiting …

Early aggregation preceding the nucleation of insulin amyloid fibrils as monitored by small angle X-ray scattering

E Chatani, R Inoue, H Imamura, M Sugiyama, M Kato… - Scientific reports, 2015 - nature.com
The nucleation event of amyloid fibrils is one of the most crucial processes that dictate the
timing and rate of the pathology of diseases; however, information regarding how protein …

Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism

Y Goto, M Adachi, H Muta, M So - Biophysical reviews, 2018 - Springer
Amyloid fibrils are misfolded forms of proteins and are involved in various diseases. They
have been studied extensively with the aim to obtain a comprehensive understanding of …

Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility

A De Simone, A Dhulesia, G Soldi… - Proceedings of the …, 2011 - National Acad Sciences
The identification of the factors that enable normally folded proteins to remain in their soluble
and functional states is crucial for a comprehensive understanding of any biological system …

Magic Angle Spinning NMR Analysis of β2-Microglobulin Amyloid Fibrils in Two Distinct Morphologies

GT Debelouchina, GW Platt, MJ Bayro… - Journal of the …, 2010 - ACS Publications
β2-Microglobulin (β2m) is the major structural component of amyloid fibrils deposited in a
condition known as dialysis-related amyloidosis. Despite numerous studies that have …