Abstract Formyl peptide receptor 2 (FPR2) has been shown to mediate the cytotoxic effects
of the β amyloid peptide Aβ42 and serves as a receptor for humanin, a peptide that protects …

The formation of amyloid fibrils and oligomers is a hallmark of several neurodegenerative
disorders, including Alzheimer's disease (AD), and contributes to the disease pathway. To …

Lung endothelia in the arteries, capillaries, and veins are heterogeneous in structure and
function. Lung capillaries in particular represent a unique vascular niche, with a thin yet …

Atomic-resolution structure determination is crucial for understanding protein function. Cryo-
EM and NMR spectroscopy both provide structural information, but currently cryo-EM does …

The accumulation of the amyloid‐β peptides (Aβ) is central to the development of
Alzheimer's disease. The mechanism by which Aβ triggers a cascade of events that leads to …

Central to Alzheimer's disease (AD) is the assembly of the amyloid‐beta peptide (Aβ) into
fibrils. A reduction in pH accompanying inflammation or subcellular compartments, may …

Self-assembly of amyloid-β peptides leads to oligomers, protofibrils, and fibrils that are likely
instigators of neurodegeneration in Alzheimer's disease. We report results of time-resolved …

Aberrant α-synuclein aggregation is strongly associated with the onset and development of
Parkinson's disease (PD). Therefore, characterizing the structure of toxic intermediate …

Nuclear import receptors (NIRs) not only transport RNA-binding proteins (RBPs) but also
modify phase transitions of RBPs by recognizing nuclear localization signals (NLSs). Toxic …

The structural polymorphism and the physiological and pathophysiological roles of two
important proteins, β-amyloid (Aβ) and tau, that play a key role in Alzheimer's disease (AD) …