The aggregation of the amyloid β‐peptide into fibrils is a complex process that involves
mechanisms such as primary and secondary nucleation, fibril elongation and fibril …

We propose the replica permutation with solute tempering (RPST) by combining the replica-
permutation method (RPM) and the replica exchange with solute tempering (REST) …

Soluble amyloid oligomers are a cytotoxic species in Alzheimer's disease, and the recent
discovery that trehalose can prohibit aggregation of amyloid β-peptide (Aβ) has received …

Because of their association with debilitating diseases and their potential applications in
developing novel bionanomaterials, highly ordered amyloid fibrils have recently received …

The accumulation of amyloid-β (Aβ) peptides is a major hallmark of Alzheimer's disease
(AD) and plays a crucial role in its pathogenesis. Particularly, the structured oligomeric …

The residue lysine 28 (K28) is known to form an important salt bridge that stabilizes the Aβ
amyloid structure, and acetylation of lysine 28 (K28Ac) slows the Aβ42 fibrillization rate but …

To systematically construct a low-dimensional free-energy landscape of RNA systems from a
classical molecular dynamics simulation, various versions of the principal component …

The aggregation of amyloid-β (Aβ), which involves the formation of small oligomers and
mature fibrils, has received considerable attention in the past few decades due to its close …

Polymorphism of amyloid-β (Aβ) fibrils, implying different fibril structures, may play important
pathological roles in Alzheimer's disease (AD). Morphologies of Aβ fibrils were found to be …

The transition from a disordered to an assembly-competent monomeric state (N*) in
amyloidogenic sequences is a crucial event in the aggregation cascade. Using a well …