Amyloid oligomers: A joint experimental/computational perspective on Alzheimer's disease, Parkinson's disease, type II diabetes, and amyotrophic lateral sclerosis
Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …
Tetrameric Aβ40 and Aβ42 β-barrel structures by extensive atomistic simulations. II. In aqueous solution
PH Nguyen, JM Campanera, ST Ngo… - The Journal of …, 2019 - ACS Publications
Alzheimer's disease (AD) is characterized by the accumulation of extracellular Aβ42 and
Aβ40 oligomers and plaques. In a recent computational study, we found that the presence of …
Aβ40 oligomers and plaques. In a recent computational study, we found that the presence of …
Effect of Terahertz Waves on the Structure of the Aβ42 Monomer, Dimer, and Protofibril: Insights from Molecular Dynamics Simulations
Amyloid-β (Aβ) and its assemblies play important roles in the pathogenesis of Alzheimer's
disease (AD). Recent studies conducted by experimental and computational researchers …
disease (AD). Recent studies conducted by experimental and computational researchers …
Molecular dynamics simulations reveal the mechanism of graphene oxide nanosheet inhibition of Aβ 1–42 peptide aggregation
The aggregation of the amyloid-beta (Aβ) peptides into toxic β-sheet-rich oligomers,
protofibrils and mature fibrils is the major pathological hallmark of Alzheimer's disease (AD) …
protofibrils and mature fibrils is the major pathological hallmark of Alzheimer's disease (AD) …
Mechanistic insights into the mitigation of Aβ aggregation and protofibril destabilization by ad-enantiomeric decapeptide rk10
According to clinical studies, the development of Alzheimer's disease (AD) is linked to the
abnormal aggregation of amyloid-β (Aβ) peptides into toxic soluble oligomers, protofibrils as …
abnormal aggregation of amyloid-β (Aβ) peptides into toxic soluble oligomers, protofibrils as …
Amyloid β dodecamer disrupts the neuronal membrane more strongly than the mature fibril: Understanding the role of oligomers in neurotoxicity
The amyloid cascade hypothesis states that senile plaques, composed of amyloid β (Aβ)
fibrils, play a key role in Alzheimer's disease (AD). However, recent experiments have …
fibrils, play a key role in Alzheimer's disease (AD). However, recent experiments have …
The role of structural polymorphism in driving the mechanical performance of the alzheimer's beta amyloid fibrils
Alzheimer's Disease (AD) is related with the abnormal aggregation of amyloid β-peptides
Aβ1− 40 and Aβ1− 42, the latter having a polymorphic character which gives rise to U-or S …
Aβ1− 40 and Aβ1− 42, the latter having a polymorphic character which gives rise to U-or S …
Emergence of barrel motif in amyloid-β trimer: a computational study
Amyloid-β (Aβ) peptides form assemblies that are pathological hallmarks of Alzheimer's
disease. Aβ oligomers are soluble, mobile, and toxic forms of the peptide that act in the …
disease. Aβ oligomers are soluble, mobile, and toxic forms of the peptide that act in the …
Structures and Dynamics of β-Rich Oligomers of ATTR (105–115) Assembly
L Liang, Y Zhang, Y Zhu, J Bai, Y Ni… - ACS Chemical …, 2024 - ACS Publications
Transthyretin (TTR) is a tetrameric homologous protein that can dissociate into monomers.
Misfolding and aggregation of TTR can lead to amyloid transthyretin amyloidosis (ATTR) …
Misfolding and aggregation of TTR can lead to amyloid transthyretin amyloidosis (ATTR) …
Distinguishing the effect on the rate and yield of Aβ42 aggregation by green tea polyphenol EGCG
G Park, C Xue, H Wang, Z Guo - ACS omega, 2020 - ACS Publications
Deposition of Aβ42 aggregates in the form of amyloid plaques is a pathological hallmark of
Alzheimer's disease. A desired avenue of intervention is the inhibition of Aβ42 aggregation …
Alzheimer's disease. A desired avenue of intervention is the inhibition of Aβ42 aggregation …