A protein can fold efficiently with high fidelity if on average native contacts survive longer
than non-native ones. If native contacts survive long enough to obtain a certain level of …

Protein-protein interactions control and coordinate a wide range of biological processes, but
can also occur aberrantly and with toxic consequences. In amyloid diseases, exposure of …

The self-assembly of amyloid proteins into fibrils is thought to be the cause of many
diseases, including Alzheimer's disease, Huntingtons disease, and prion-related disease …

Protein aggregation occurs in vivo as a result of improper folding or misfolding. Diverse
diseases arise from protein misfolding and are now grouped under the term “protein …

Data gathered on this topic in the recent years show that an increasing number of
pathologies are associated with protein aggregation and that aggregation often occurs …

It is well accepted that to function proteins must fold into specific threedimensional
structures. Even under physiological conditions the functionally competent states of proteins …

The issue of protein aggregation represents a wide ensemble of results from biological,
biochemical and biophysical studies carried out to date. Under some pathological …

Protein adsorption onto surfaces of diverse materials of both natural and artificial origin is of
utmost relevance in many areas of research and technology: medicine, pharmaceutical …

The large-scale aggregation of proteins is responsible for a number of human and animal
diseases. The morphology of aggregates is largely fibrillar, and similar for proteins of various …