Unsupervised learning methods for molecular simulation data

A Glielmo, BE Husic, A Rodriguez, C Clementi… - Chemical …, 2021 - ACS Publications
Unsupervised learning is becoming an essential tool to analyze the increasingly large
amounts of data produced by atomistic and molecular simulations, in material science, solid …

Amyloid beta: structure, biology and structure-based therapeutic development

G Chen, T Xu, Y Yan, Y Zhou, Y Jiang… - Acta pharmacologica …, 2017 - nature.com
Amyloid beta peptide (Aβ) is produced through the proteolytic processing of a
transmembrane protein, amyloid precursor protein (APP), by β-and γ-secretases. Aβ …

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 ensembles of intrinsically disordered proteins depend strongly on force field: a comparison to experiment

S Rauscher, V Gapsys, MJ Gajda… - Journal of chemical …, 2015 - ACS Publications
Intrinsically disordered proteins (IDPs) are notoriously challenging to study both
experimentally and computationally. The structure of IDPs cannot be described by a single …

Simulation studies of amyloidogenic polypeptides and their aggregates

IM Ilie, A Caflisch - Chemical reviews, 2019 - ACS Publications
Amyloids, fibrillar assembly of (poly) peptide chains, are associated with neurodegenerative
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …

Role of water in protein aggregation and amyloid polymorphism

D Thirumalai, G Reddy, JE Straub - Accounts of chemical …, 2012 - ACS Publications
A variety of neurodegenerative diseases are associated with amyloid plaques, which begin
as soluble protein oligomers but develop into amyloid fibrils. Our incomplete understanding …

Monomeric Aβ1–40 and Aβ1–42 Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil

J Roche, Y Shen, JH Lee, J Ying, A Bax - Biochemistry, 2016 - ACS Publications
The pathogenesis of Alzheimer's disease is characterized by the aggregation and fibrillation
of amyloid peptides Aβ1–40 and Aβ1–42 into amyloid plaques. Despite strong potential …

Aβ monomers transiently sample oligomer and fibril-like configurations: Ensemble characterization using a combined MD/NMR approach

DJ Rosenman, CR Connors, W Chen, C Wang… - Journal of molecular …, 2013 - Elsevier
Amyloid β (Aβ) peptides are a primary component of fibrils and oligomers implicated in the
etiology of Alzheimer's disease (AD). However, the intrinsic flexibility of these peptides has …

Describing intrinsically disordered proteins at atomic resolution by NMR

MR Jensen, RWH Ruigrok, M Blackledge - Current opinion in structural …, 2013 - Elsevier
There is growing interest in the development of physical methods to study the
conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In …

Cerebrospinal fluid: A specific biofluid for the biosensing of Alzheimer's diseases biomarkers

A Mirzaie, H Nasrollahpour, B Khalilzadeh… - TrAC Trends in …, 2023 - Elsevier
Alzheimer's disease (AD) is the most prevalent neurodegenerative disorder with an
irreversible, progressive, and untreatable nature that causes progressive deterioration, loss …