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 …

Structural evidence of amyloid fibril formation in the putative aggregation domain of TDP-43

M Mompeán, R Hervás, Y Xu, TH Tran… - The journal of …, 2015 - ACS Publications
TDP-43 can form pathological proteinaceous aggregates linked to ALS and FTLD. Within the
putative aggregation domain, engineered repeats of residues 341–366 can recruit …

Molecular Insights into the Dynamics of Amyloid Fibril Growth: Elongation and Lateral Assembly of GNNQQNY Protofibrils

T John, A Rampioni, D Poger… - ACS Chemical …, 2024 - ACS Publications
The self-assembly of peptides and proteins into β-sheet rich amyloid fibrils is linked to both
functional and pathological states. In this study, the growth of fibrillar structures of the short …

Primary nucleation kinetics of short fibril-forming amyloidogenic peptides

JA Luiken, PG Bolhuis - The Journal of Physical Chemistry B, 2015 - ACS Publications
The primary nucleation step in amyloid fibril formation can, depending on the nature of
peptide sequence, occur in one step, straight from a dilute solution, or in multiple steps, via …

Dysregulation of TDP‐43 intracellular localization and early onset ALS are associated with a TARDBP S375G variant

K Newell, F Paron, M Mompean, J Murrell… - Brain …, 2019 - Wiley Online Library
Abstract We investigated the Central Nervous System (CNS) and skeletal muscle tissue from
A woman was clinically diagnosed with amyotrophic lateral sclerosis (ALS) at the age of 22 …

Inhibition of amyloid peptide fibril formation by gold–sulfur complexes

W Wang, C Zhao, D Zhu, G Gong, W Du - Journal of inorganic biochemistry, 2017 - Elsevier
Amyloid-related diseases are characterized by protein conformational change and amyloid
fibril deposition. Metal complexes are potential inhibitors of amyloidosis. Nitrogen …

Inhibition of GNNQQNY prion peptide aggregation by trehalose: a mechanistic view

N Katyal, S Deep - Physical Chemistry Chemical Physics, 2017 - pubs.rsc.org
Deposition of amyloid fibrils is the seminal event in the pathogenesis of numerous
neurodegenerative diseases. The formation of this amyloid assembly is the manifestation of …

Prediction of a stable associated liquid of short amyloidogenic peptides

JA Luiken, PG Bolhuis - Physical Chemistry Chemical Physics, 2015 - pubs.rsc.org
Amyloid fibril formation is believed to be a nucleation-controlled process. Depending on the
nature of peptide sequence, fibril nucleation can occur in one step, straight from a dilute …

Influence of gold–bipyridyl derivants on aggregation and disaggregation of the prion neuropeptide PrP106–126

C Zhao, X Wang, L He, D Zhu, B Wang, W Du - Metallomics, 2014 - academic.oup.com
Metal complexes can effectively inhibit the aggregation of amyloid peptides, such as Aβ,
human islet amyloid polypeptide, and prion neuropeptide PrP106–126. Gold (Au) …

Roles of DMSO-type ruthenium complexes in disaggregation of prion neuropeptide PrP106–126

D Zhu, C Zhao, X Wang, W Wang, B Wang, W Du - RSC advances, 2016 - pubs.rsc.org
Ruthenium complexes are potential anticancer metallodrugs and inhibitors of various
proteins, such as enzymes and even amyloid peptides. Studies on Aβ protein, human islet …