Transthyretin (TTR) is one of the many proteins that are known to misfold and aggregate (ie,
undergo amyloidogenesis) in vivo. The process of TTR amyloidogenesis causes nervous …

The relevance of protein stability for biological function and molecular evolution is widely
recognized. Protein stability, however, comes in two flavours: thermodynamic stability, which …

Amyloid is aggregated protein in the form of insoluble fibrils. Amyloid deposition in human
tissue—amyloidosis—is associated with a number of diseases including all common …

Abstract Transthyretin (TTR)(formerly, thyroxine binding prealbumin) is an evolutionarily
conserved serum and cerebrospinal fluid protein that transports holo-retinol-binding protein …

Maintaining the proteome to preserve the health of an organism in the face of developmental
changes, environmental insults, infectious diseases, and rigors of aging is a formidable task …

Molecules that bind selectively to a given protein and then undergo a rapid chemoselective
reaction to form a covalent conjugate have utility in drug development. Herein a library of 1 …

Small molecules that bind to normally unoccupied thyroxine (T4) binding sites within
transthyretin (TTR) in the blood stabilize the tetrameric ground state of TTR relative to the …

There are more than 30 human proteins whose aggregation appears to cause degenerative
maladies referred to as amyloid diseases or amyloidoses. These disorders are named after …

Fluorogenic probes, due to their often greater spatial and temporal sensitivity in comparison
to permanently fluorescent small molecules, represent powerful tools to study protein …

Thyroid disruption by xenobiotics is associated with a broad spectrum of severe adverse
outcomes. One possible molecular target of thyroid hormone disrupting chemicals (THDCs) …