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. 2022 Mar 7;93(6):668–678. doi: 10.1136/jnnp-2021-327909

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© Author(s) (or their employer(s)) 2022. Re-use permitted under CC BY-NC. No commercial re-use. See rights and permissions. Published by BMJ.

This is an open access article distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited, appropriate credit is given, any changes made indicated, and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/.

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Mechanisms by which TTR mutants exert pathogenesis and therapeutic strategies for ATTRv. TTR is predominantly produced by the liver. The conversion of TTR tetramer into insoluble amyloid fibrils is a multistep dynamic process, with dissociation of TTR tetramers into misfolded monomers being the rate-limiting step for the formation of amyloid fibrils. TTR gene mutations destabilise quaternary and tertiary TTR structures and induce thermodynamic instability, resulting in the formation of misfolded monomers. Amyloid fibril formation occurs by nucleation-dependent polymerisation and is influenced by a variety of physiological factors. Therapeutic strategies aimed at different stages of amyloid formation have shown efficacy in ATTRv. ATTRv, hereditary transthyretin amyloidosis; TTR, transthyretin.