Molecular mechanism of misfolding and aggregation of Aβ (13–23)
The misfolding and self-assembly of the amyloid-beta (Aβ) peptide into aggregates is a
molecular signature of the development of Alzheimer's disease, but molecular mechanisms …
molecular signature of the development of Alzheimer's disease, but molecular mechanisms …
A Study of the α-Helical Intermediate Preceding the Aggregation of the Amino-Terminal Fragment of the β Amyloid Peptide (Aβ1–28)
The β amyloid (Aβ) peptide aggregates to form β-rich structures that are known to trigger
Alzheimer's disease. Experiments suggest that an α-helical intermediate precedes the …
Alzheimer's disease. Experiments suggest that an α-helical intermediate precedes the …
Spontaneous self-assembly of amyloid β (1–40) into dimers
The self-assembly and fibrillation of amyloid β (Aβ) proteins is the neuropathological
hallmark of Alzheimer's disease. However, the molecular mechanism of how disordered …
hallmark of Alzheimer's disease. However, the molecular mechanism of how disordered …
Structure of ring-shaped Aβ42 oligomers determined by conformational selection
The oligomerization of amyloid beta (Aβ) peptides into soluble non-fibrillar species plays a
critical role in the pathogenesis of Alzheimer's disease. However, it has been challenging to …
critical role in the pathogenesis of Alzheimer's disease. However, it has been challenging to …
Why Is the C-terminus of Aβ (1− 42) More Unfolded than That of Aβ (1− 40)? Clues from Hydrophobic Interaction
L Shen, HF Ji, HY Zhang - The Journal of Physical Chemistry B, 2008 - ACS Publications
Aβ (1− 40) and Aβ (1− 42) are the main forms of amyloid β (Aβ) peptides in the brain of
Alzheimer's patients; however, the latter possesses much stronger aggregation and …
Alzheimer's patients; however, the latter possesses much stronger aggregation and …
[HTML][HTML] Role of β-hairpin formation in aggregation: the self-assembly of the amyloid-β (25–35) peptide
L Larini, JE Shea - Biophysical journal, 2012 - cell.com
Abstract The amyloid-β (25–35) peptide plays a key role in the etiology of Alzheimer's
disease due to its extreme toxicity even in the absence of aging. Because of its high …
disease due to its extreme toxicity even in the absence of aging. Because of its high …
Effect of the English familial disease mutation (H6R) on the monomers and dimers of Aβ40 and Aβ42
MH Viet, PH Nguyen, P Derreumaux… - ACS chemical …, 2014 - ACS Publications
The self-assembly of the amyloid beta (Aβ) peptides into senile plaques is the hallmark of
Alzheimer's disease. Recent experiments have shown that the English familial disease …
Alzheimer's disease. Recent experiments have shown that the English familial disease …
Different force fields give rise to different amyloid aggregation pathways in molecular dynamics simulations
S Samantray, F Yin, B Kav… - Journal of chemical …, 2020 - ACS Publications
The progress toward understanding the molecular basis of Alzheimers's disease is strongly
connected to elucidating the early aggregation events of the amyloid-β (Aβ) peptide …
connected to elucidating the early aggregation events of the amyloid-β (Aβ) peptide …
Stability and structure of oligomers of the Alzheimer peptide Aβ16–22: from the dimer to the 32-mer
Several neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's
diseases are associated with amyloid fibrils formed by different polypeptides. We probe the …
diseases are associated with amyloid fibrils formed by different polypeptides. We probe the …
Characterization of the conformations of amyloid beta 42 in solution that may mediate its initial hydrophobic aggregation
K Sonar, RL Mancera - The Journal of Physical Chemistry B, 2022 - ACS Publications
Intrinsically disordered peptides, such as amyloid β42 (Aβ42), lack a well-defined structure
in solution. Aβ42 can undergo abnormal aggregation and amyloidogenesis in the brain …
in solution. Aβ42 can undergo abnormal aggregation and amyloidogenesis in the brain …