β 2-Microglobulin is responsible for systemic amyloidosis affecting patients undergoing long-
term hemodialysis. Its genetic variant D76N causes a very rare form of familial systemic …

Several protein misfolding diseases are associated with the conversion of native proteins
into ordered protein aggregates known as amyloid. Studies of amyloid assemblies have …

Atomic-level structural investigation of the key conformational intermediates of
amyloidogenesis remains a challenge. Here we demonstrate the utility of nanobodies to trap …

The forces acting in colloidal suspensions and affecting their stability and aggregation
kinetics are considered. The approximations used for these forces in numerical simulations …

Systemic amyloidosis is a fatal disease caused by misfolding of native globular proteins,
which then aggregate extracellularly as insoluble fibrils, damaging the structure and function …

The tissue specificity of fibrillar deposition in dialysis-related amyloidosis is most likely
associated with the peculiar interaction of β 2-microglobulin (β 2-m) with collagen fibers …

The inability of a protein to adopt its native and soluble conformation (protein misfolding) is
the origin of an increasing number of human diseases. The misfolding of a protein is often …

Protein aggregation is a hallmark of many diseases, including amyotrophic lateral sclerosis
(ALS) where aggregation of copper/zinc superoxide dismutase (SOD1) is implicated in …

Dispersions of particles with short-range attractive and long-range repulsive interactions
exhibit rich equilibrium microstructures and a complex phase behavior. We present …

The amyloidogenic variant of β 2-microglobulin, D76N, can readily convert into genuine
fibrils under physiological conditions and primes in vitro the fibrillogenesis of the wild-type β …