The phenomenon of protein aggregation and amyloid formation has become the subject of
rapidly increasing research activities across a wide range of scientific disciplines. Such …

The intracellular interactions of biomolecules can be maneuvered to redirect signaling,
reprogram the cell cycle, or decrease infectivity using only a few dozen atoms. Such …

The transthyretin amyloidoses (ATTR) are invariably fatal diseases characterized by
progressive neuropathy and/or cardiomyopathy. ATTR are caused by aggregation of …

The aggregation of specific proteins is hypothesized to underlie several degenerative
diseases, which are collectively known as amyloid disorders. However, the mechanistic …

Since Hedin's characterization of trypsin and antitrypsin in 1906,(1) arguably the first
account of a regulatory protein–protein interaction (PPI), contemporary understanding of …

Control of protein levels by nucleic-acid-based technologies has proven to be a useful
research tool but lacks the advantages of small molecules with respect to cell permeability …

Protein folding is a complex, error-prone process that often results in an irreparable protein
by-product. These by-products can be recognized by cellular quality control machineries …

Target-based drug discovery is the dominant paradigm of drug discovery; however, a
comprehensive evaluation of its real-world efficiency is lacking. Here, a manual systematic …

For a protein to function appropriately, it must first achieve its proper conformation and
location within the crowded environment inside the cell. Multiple chaperone systems are …

Tafamidis, a transthyretin (TTR) kinetic stabilizer, delayed neuropathic progression in
patients with Val30Met TTR familial amyloid polyneuropathy (TTR-FAP) in an 18-month …