Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …

Protein aggregation is the main hallmark of neurodegenerative diseases. Many proteins
found in pathological inclusions are known to undergo liquid-liquid phase separation, a …

The aggregation of proteins into amyloid fibrils and their deposition into plaques and
intracellular inclusions is the hallmark of amyloid disease. The accumulation and deposition …

Amyloid fibrils have traditionally been considered only as pathological aggregates in human
neurodegenerative diseases, but it is increasingly becoming clear that the propensity to form …

Fluorescence nanoscopy uniquely combines minimally invasive optical access to the
internal nanoscale structure and dynamics of cells and tissues with molecular detection …

Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

Protein misfolding and aggregation, a key contributor to the progression of numerous
neurodegenerative diseases, results in functional deficiencies and the creation of harmful …

Super-resolution fluorescence imaging by photoactivation or photoswitching of single
fluorophores and position determination (single-molecule localization microscopy, SMLM) …

Alpha-synuclein is known to bind to small unilamellar vesicles (SUVs) via its N terminus,
which forms an amphipathic alpha-helix upon membrane interaction. Here we show that …

Many proteins contain large structurally disordered regions or are entirely disordered under
physiological conditions. The functions of these intrinsically disordered proteins (IDPs) often …