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 …

The binding pose and affinity between a ligand and enzyme are very important pieces of
information for computer-aided drug design. In the initial stage of a drug discovery project …

Understanding the atomistic resolution changes during the self-assembly of amyloid
peptides or proteins is important to develop compounds or conditions to alter the …

Intrinsically disordered proteins (IDPs) play many biological roles in the human proteome
ranging from vesicular transport, signal transduction to neurodegenerative diseases. The Aβ …

Soluble low-molecular-weight oligomers formed during the early aggregation of amyloid
peptides have been hypothesized as a major toxic species of amyloidogenesis. Herein, we …

The imbalance of amyloid‐β (Aβ) production and clearance causes aggregation of Aβ1‐42
monomers to form fibrils and amyloid plaques, which is an indispensable process in the …

Fused in sarcoma (FUS), a nuclear RNA binding protein, can not only undergo liquid–liquid
phase separation (LLPS) to form dynamic biomolecular condensates but also aggregate into …

Oligomeric aggregates of the amyloid-beta peptide (1-42)(Aβ42) are regarded as a primary
cause of cytotoxicity related to membrane damage in Alzheimer's disease. However, a …

Alzheimer's disease (AD) pathology is characterized by loss of memory cognitive and
behavioral deterioration. One of the hallmarks of AD is amyloid β (Aβ) plaques in the brain …

Perturbation of cell membranes by amyloid β (Ab) peptide oligomers is one possible
mechanism of cytotoxicity in Alzheimer's disease, but the structure of such Ab–membrane …