Common molecular mechanism of amyloid pore formation by Alzheimer's β-amyloid peptide and α-synuclein

C Di Scala, N Yahi, S Boutemeur, A Flores… - Scientific reports, 2016 - nature.com
Calcium-permeable pores formed by small oligomers of amyloid proteins are the primary
pathologic species in Alzheimer's and Parkinson's diseases. However, the molecular …

Differential membrane toxicity of amyloid-β fragments by pore forming mechanisms

C Peters, D Bascunan, C Opazo… - Journal of Alzheimer's …, 2016 - content.iospress.com
A major characteristic of Alzheimer's disease (AD) is the presence of amyloid-β peptide (Aβ)
oligomers and aggregates in the brain. It is known that Aβ oligomers interact with the …

Interaction of Alzheimer's β-amyloid peptides with cholesterol: mechanistic insights into amyloid pore formation

C Di Scala, H Chahinian, N Yahi, N Garmy… - Biochemistry, 2014 - ACS Publications
Brain cholesterol plays a critical role in Alzheimer's disease and other neurodegenerative
diseases. The molecular mechanisms linking cholesterol to neurotoxicity have remained …

Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments

M Serra-Batiste, M Ninot-Pedrosa… - Proceedings of the …, 2016 - National Acad Sciences
The formation of amyloid-β peptide (Aβ) oligomers at the cellular membrane is considered to
be a crucial process underlying neurotoxicity in Alzheimer's disease (AD). Therefore, it is …

Membrane Incorporation, Channel Formation, and Disruption of Calcium Homeostasis by Alzheimer′s β‐Amyloid Protein

M Kawahara, I Ohtsuka, S Yokoyama… - International Journal …, 2011 - Wiley Online Library
Oligomerization, conformational changes, and the consequent neurodegeneration of
Alzheimer′ s β‐amyloid protein (AβP) play crucial roles in the pathogenesis of Alzheimer …

Structure of amyloid β25–35 in lipid environment and cholesterol-dependent membrane pore formation

N Kandel, JO Matos, SA Tatulian - Scientific reports, 2019 - nature.com
The amyloid β (Aβ) peptide and its shorter variants, including a highly cytotoxic Aβ25–35
peptide, exert their neurotoxic effect during Alzheimer's disease by various mechanisms …

The effect of Alzheimer's Aβ aggregation state on the permeation of biomimetic lipid vesicles

TL Williams, IJ Day, LC Serpell - Langmuir, 2010 - ACS Publications
Alzheimer's disease is characterized by the aggregation and deposition of the Aβ peptide.
This 40 or 42 residue peptide is the product of the proteolysis of the amyloid precursor …

Amyloid-β membrane binding and permeabilization are distinct processes influenced separately by membrane charge and fluidity

PT Wong, JA Schauerte, KC Wisser, H Ding… - Journal of molecular …, 2009 - Elsevier
The 40 and 42 residue amyloid-β (Aβ) peptides are major components of the proteinaceous
plaques prevalent in the Alzheimer's disease-afflicted brain and have been shown to have …

β-amyloid causes depletion of synaptic vesicles leading to neurotransmission failure

J Parodi, FJ Sepulveda, J Roa, C Opazo… - Journal of Biological …, 2010 - ASBMB
Alzheimer disease is a progressive neurodegenerative brain disorder that leads to major
debilitating cognitive deficits. It is believed that the alterations capable of causing brain …

Ion channel formation by amyloid-β42 oligomers but not amyloid-β40 in cellular membranes

DC Bode, MD Baker, JH Viles - Journal of Biological Chemistry, 2017 - ASBMB
A central hallmark of Alzheimer's disease is the presence of extracellular amyloid plaques
chiefly consisting of amyloid-β (Aβ) peptides in the brain interstitium. Aβ largely exists in two …