[HTML][HTML] Aβ–ganglioside interactions in the pathogenesis of Alzheimer's disease

K Matsuzaki - Biochimica et Biophysica Acta (BBA)-Biomembranes, 2020 - Elsevier
It is widely accepted that the abnormal self-association of amyloid β-protein (Aβ) is central to
the pathogenesis of Alzheimer's disease, the most common form of dementia. Accumulating …

The role of lipid environment in ganglioside GM1-induced amyloid β aggregation

V Rudajev, J Novotny - Membranes, 2020 - mdpi.com
Ganglioside GM1 is the most common brain ganglioside enriched in plasma membrane
regions known as lipid rafts or membrane microdomains. GM1 participates in many …

Key residue for aggregation of amyloid-β peptides

SG Itoh, M Yagi-Utsumi, K Kato… - ACS Chemical …, 2022 - ACS Publications
It is known that oligomers of amyloid-β (Aβ) peptide are associated with Alzheimer's disease.
Aβ has two isoforms: Aβ40 and Aβ42. Although the difference between Aβ40 and Aβ42 is …

Dissecting the molecular mechanisms of the co-aggregation of Aβ40 and Aβ42 peptides: a REMD simulation study

X Li, Z Yang, Y Chen, S Zhang, G Wei… - The Journal of Physical …, 2023 - ACS Publications
The aggregation of amyloid-β protein (Aβ) into oligomers and amyloid fibrils is closely
related to Alzheimer's disease (AD). Aβ40 and Aβ42, as two most prominent isoforms of Aβ …

Molecular dynamics simulation studies on the aggregation of amyloid-β peptides and their disaggregation by ultrasonic wave and infrared laser irradiation

H Okumura, SG Itoh - Molecules, 2022 - mdpi.com
Alzheimer's disease is understood to be caused by amyloid fibrils and oligomers formed by
aggregated amyloid-β (Aβ) peptides. This review article presents molecular dynamics (MD) …

A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on Aβ42 Aggregation

KN Baumann, G Šneiderienė… - ACS Chemical …, 2022 - ACS Publications
The aggregation of the amyloid β (Aβ) peptide is one of the molecular hallmarks of
Alzheimer's disease (AD). Although Aβ deposits have mostly been observed extracellularly …

The double-layered structure of amyloid-β assemblage on GM1-containing membranes catalytically promotes fibrillization

M Yagi-Utsumi, SG Itoh, H Okumura… - ACS Chemical …, 2023 - ACS Publications
Alzheimer's disease (AD) is associated with progressive accumulation of amyloid-β (Aβ)
cross-β fibrils in the brain. Aβ species tightly associated with GM1 ganglioside, a …

Time-resolved atomistic imaging and statistical analysis of daptomycin oligomers with and without calcium ions

T Nakamuro, K Kamei, K Sun, JW Bode… - Journal of the …, 2022 - ACS Publications
Daptomycin (DP) is effective against multiple drug-resistant Gram-positive pathogens
because of its distinct mechanism of action. An accepted mechanism includes Ca2+ …

Dissociation process of polyalanine aggregates by free electron laser irradiation

H Okumura, SG Itoh, H Zen, K Nakamura - PLoS One, 2023 - journals.plos.org
Polyalanine (polyA) disease-causative proteins with an expansion of alanine repeats can be
aggregated. Although curative treatments for polyA diseases have not been explored, the …

Perspective for Molecular Dynamics Simulation Studies of Amyloid-β Aggregates

H Okumura - The Journal of Physical Chemistry B, 2023 - ACS Publications
The cause of Alzheimer's disease is related to aggregates such as oligomers and amyloid
fibrils consisting of amyloid-β (Aβ) peptides. Molecular dynamics (MD) simulation studies …