The deposition of proteins in the form of amyloid fibrils and plaques is the characteristic
feature of more than 20 degenerative conditions affecting either the central nervous system …

The technique of ion mobility mass spectrometry (IM-MS) has become of increasing interest
for rapid analysis of the conformations adopted by biological macromolecules. It is currently …

Purpose: Recent studies have shown that 7% to 12% of endometrial cancers are
ultramutated due to somatic mutation in the proofreading exonuclease domain of the DNA …

All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from
proteins associated with different diseases remains unclear. Here, we combine cryo-EM and …

Engineered fusion proteins containing two or more functional polypeptides joined by a
peptide or protein linker are important for many fields of biological research. The separation …

Although most proteins can assemble into amyloid-like fibrils in vitro under extreme
conditions, how proteins form amyloid fibrils in vivo remains unresolved. Identifying rare …

Numerous studies of amyloid assembly have indicated that partially folded protein species
are responsible for initiating aggregation. Despite their importance, the structural and …

Hierarchical self-assembly of synthetic polypeptides has attracted increasing interests due to
its protein-mimetic structure and great potential in nanotechnology and biomedical …

Many polypeptides can self-associate into linear, aggregated assemblies termed amyloid
fibers. High-resolution structural insights into the mechanism of fibrillogenesis are elusive …

Investigation of factors that modulate amyloid formation of proteins is important to
understand and mitigate amyloid-related diseases. To understand the role of electrostatic …