Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade

F Chiti, CM Dobson - Annual review of biochemistry, 2017 - annualreviews.org
Peptides and proteins have been found to possess an inherent tendency to convert from
their native functional states into intractable amyloid aggregates. This phenomenon is …

Secondary nucleation in amyloid formation

M Törnquist, TCT Michaels, K Sanagavarapu… - Chemical …, 2018 - pubs.rsc.org
Nucleation of new peptide and protein aggregates on the surfaces of amyloid fibrils of the
same peptide or protein has emerged in the past two decades as a major pathway for both …

Alzheimer disease pathogenesis: insights from molecular and cellular biology studies of oligomeric Aβ and tau species

XQ Chen, WC Mobley - Frontiers in Neuroscience, 2019 - frontiersin.org
Alzheimer disease (AD) represents an oncoming epidemic that without an effective
treatment promises to exact extraordinary human and financial burdens. Studies of …

Calcium dyshomeostasis in Alzheimer's disease pathogenesis

R Cascella, C Cecchi - International journal of molecular sciences, 2021 - mdpi.com
Alzheimer's disease (AD) is the most common age-related neurodegenerative disorder that
is characterized by amyloid β-protein deposition in senile plaques, neurofibrillary tangles …

Early diagnosis and treatment of Alzheimer's disease by targeting toxic soluble Aβ oligomers

M Habashi, S Vutla, K Tripathi… - Proceedings of the …, 2022 - National Acad Sciences
Transient soluble oligomers of amyloid-β (Aβ) are toxic and accumulate early prior to
insoluble plaque formation and cognitive impairment in Alzheimer's disease (AD). Synthetic …

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 …

[HTML][HTML] Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue

JX Lu, W Qiang, WM Yau, CD Schwieters, SC Meredith… - Cell, 2013 - cell.com
In vitro, β-amyloid (Aβ) peptides form polymorphic fibrils, with molecular structures that
depend on growth conditions, plus various oligomeric and protofibrillar aggregates. Here …

A multi-step nucleation process determines the kinetics of prion-like domain phase separation

EW Martin, TS Harmon, JB Hopkins… - Nature …, 2021 - nature.com
Compartmentalization by liquid-liquid phase separation (LLPS) has emerged as a
ubiquitous mechanism underlying the organization of biomolecules in space and time. Here …

Near‐Infrared Aggregation‐Induced Emission Luminogens for In Vivo Theranostics of Alzheimer's Disease

T Zhang, X Chen, C Yuan, X Pang… - Angewandte Chemie …, 2023 - Wiley Online Library
Optimized theranostic strategies for Alzheimer's disease (AD) remain almost absent from
bench to clinic. Current probes and drugs attempting to prevent β‐amyloid (Aβ) fibrosis …

The amyloid beta peptide: a chemist's perspective. Role in Alzheimer's and fibrillization

IW Hamley - Chemical reviews, 2012 - ACS Publications
This review is concerned with the role of fibrillization of the amyloid β (Aβ)-peptide in
Alzheimer's disease (AD). The perspective is that of a physical chemist, and one aim is to …