Molecular dynamics simulation studies on the aggregation of amyloid-β peptides and their disaggregation by ultrasonic wave and infrared laser irradiation
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) …
aggregated amyloid-β (Aβ) peptides. This review article presents molecular dynamics (MD) …
State-of-the-art molecular dynamics simulation studies of RNA-dependent RNA polymerase of SARS-CoV-2
Molecular dynamics (MD) simulations are powerful theoretical methods that can reveal
biomolecular properties, such as structure, fluctuations, and ligand binding, at the level of …
biomolecular properties, such as structure, fluctuations, and ligand binding, at the level of …
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 …
Aβ has two isoforms: Aβ40 and Aβ42. Although the difference between Aβ40 and Aβ42 is …
The double-layered structure of amyloid-β assemblage on GM1-containing membranes catalytically promotes fibrillization
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 …
cross-β fibrils in the brain. Aβ species tightly associated with GM1 ganglioside, a …
Dissociation process of polyalanine aggregates by free electron laser irradiation
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 …
aggregated. Although curative treatments for polyA diseases have not been explored, the …
Structural and fluctuational difference between two ends of Aβ amyloid fibril: MD simulations predict only one end has open conformations
A β amyloid fibrils, which are related to Alzheimer's disease, have a cross-β structure
consisting of two β-sheets: β 1 and β 2. The A β peptides are thought to be serially arranged …
consisting of two β-sheets: β 1 and β 2. The A β peptides are thought to be serially arranged …
Effects of a hydrophilic/hydrophobic interface on amyloid-β peptides studied by molecular dynamics simulations and NMR experiments
SG Itoh, M Yagi-Utsumi, K Kato… - The Journal of Physical …, 2018 - ACS Publications
Oligomer formation of amyloid-β peptides (Aβ) is accelerated at a hydrophilic/hydrophobic
interface. However, details of the acceleration mechanism have not been elucidated. To …
interface. However, details of the acceleration mechanism have not been elucidated. To …
Role of water molecules and helix structure stabilization in the laser-induced disruption of amyloid fibrils observed by nonequilibrium molecular dynamics simulations
Water plays a crucial role in the formation and destruction of biomolecular structures. The
mechanism for destroying biomolecular structures was thought to be an active breaking of …
mechanism for destroying biomolecular structures was thought to be an active breaking of …
Replica-permutation molecular dynamics simulations of an amyloid-β (16–22) peptide and polyphenols
Aggregates of amyloid-β (Aβ) peptides, such as oligomers and amyloid fibrils, are related to
Alzheimer's disease. Polyphenols are known to inhibit the aggregation of Aβ peptides. We …
Alzheimer's disease. Polyphenols are known to inhibit the aggregation of Aβ peptides. We …
Why Is Arginine the Only Amino Acid That Inhibits Polyglutamine Monomers from Taking on Toxic Conformations?
S Tanimoto, H Okumura - ACS Chemical Neuroscience, 2024 - ACS Publications
Polyglutamine (polyQ) diseases are devastating neurodegenerative disorders characterized
by abnormal expansion of glutamine repeats within specific proteins. The aggregation of …
by abnormal expansion of glutamine repeats within specific proteins. The aggregation of …