Lost in translation: Inconvenient truths on the utility of mouse models in Alzheimer's disease research

A Granzotto, B Vissel, SL Sensi - Elife, 2024‏ - elifesciences.org
The recent, controversial approval of antibody-based treatments for Alzheimer's disease
(AD) is fueling a heated debate on the molecular determinants of this condition. The …

Lipid rafts and Alzheimer's disease: protein-lipid interactions and perturbation of signaling

DA Hicks, NN Nalivaeva, AJ Turner - Frontiers in physiology, 2012‏ - frontiersin.org
Lipid rafts are membrane domains, more ordered than the bulk membrane and enriched in
cholesterol and sphingolipids. They represent a platform for protein-lipid and protein–protein …

[HTML][HTML] Interactions between amyloid β peptide and lipid membranes

Z Niu, Z Zhang, W Zhao, J Yang - Biochimica et Biophysica Acta (BBA) …, 2018‏ - Elsevier
The presence of amyloid plaques in the brain is a typical characteristic of Alzheimer's
disease (AD). Amyloid plaques are formed from the deposits of aggregated amyloid β …

Metal binding to the amyloid-β peptides in the presence of biomembranes: Potential mechanisms of cell toxicity

SKTS Wärmländer, N Österlund, C Wallin, J Wu… - JBIC Journal of …, 2019‏ - Springer
The amyloid-β (Aβ) peptides are key molecules in Alzheimer's disease (AD) pathology. They
interact with cellular membranes, and can bind metal ions outside the membrane. Certain …

The coordination chemistry of aluminium in neurodegenerative disease

C Exley - Coordination Chemistry Reviews, 2012‏ - Elsevier
The coordination chemistry of a metal ion defines its optimal association with a biomolecule
such that its binding by specific ligands on that molecule confers function and biological …

Cholesterol and metal ions in Alzheimer's disease

HJ Lee, KJ Korshavn, A Kochi, JS Derrick… - Chemical Society …, 2014‏ - pubs.rsc.org
Cholesterol and metal ions have been suggested to be associated with the onset and
progression of Alzheimer's disease (AD). Moreover, recent findings have demonstrated a …

Molecular mechanisms of amylin turnover, misfolding and toxicity in the pancreas

DC Bhowmick, Z Kudaibergenova, L Burnett… - Molecules, 2022‏ - mdpi.com
Amyloidosis is a common pathological event in which proteins self-assemble into misfolded
soluble and insoluble molecular forms, oligomers and fibrils that are often toxic to cells …

Evidence of cadmium and mercury involvement in the Aβ42 aggregation process

D Meleleo, C Sblano, MM Storelli, R Mallamaci - Biophysical Chemistry, 2020‏ - Elsevier
Aβ42 is a small peptide formed from 42 aminoacids that presents a great propensity to
aggregate until it forms fibrils. Aβ42 aggregation and fibrillation are very complex processes …

AβP1-42 incorporation and channel formation in planar lipid membranes: the role of cholesterol and its oxidation products

D Meleleo, A Galliani, G Notarachille - Journal of bioenergetics and …, 2013‏ - Springer
Amyloid beta peptide (AβP) is a natural peptide, normally released into the cerebrospinal
fluid (CSF), that plays a key role in Alzheimer's disease. The conversion of the peptide from …

Role of cholesterol and phospholipids in amylin misfolding, aggregation and etiology of islet amyloidosis

S Singh, S Trikha, DC Bhowmick, AA Sarkar… - Lipids in Protein …, 2015‏ - Springer
Amyloidosis is a biological event in which proteins undergo structural transitions from
soluble monomers and oligomers to insoluble fibrillar aggregates that are often toxic to cells …