Mass spectrometry footprinting reveals how kinetic stabilizers counteract transthyretin dynamics altered by pathogenic mutations

Proceedings of the National Academy of Sciences, Volume 123, Number 1, January 2026.
SignificanceTransthyretin (TTR) misfolding and aggregation cause a group of life-threatening diseases known as TTR amyloidosis. Pathogenic mutations decrease the stability of the protein, thereby increasing the amyloidogenicity of TTR. While the stabilizing molecules of TTR prevent…