Article
Mass spectrometry footprinting reveals how kinetic stabilizers counteract transthyretin dynamics altered by pathogenic mutations.
Proceedings of the National Academy of Sciences of the United States of America - 6 Jan 2026
Pinheiro Francisca, Kant Ravi, Chemuru Saketh, Varejão Nathalia, Velázquez-Campoy Adrián, Reverter David, Pallarès Irantzu, Gross Michael L, Ventura Salvador
Abstract excerpt
The aggregation of transthyretin (TTR) results in life-threatening transthyretin amyloidosis. Familial forms of the disease arise from point mutations that destabilize the TTR tetramer, leading to its dissociation and/or monomer unfolding and subsequent formation of amyloid fibrils. Small molecules that kinetically stabilize the native tetramer effectively inhibit this aggregation. Although over 300 X-ray crystal...
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