title: Mechanisms of transthyretin aggregation and toxicity.
abstract: Amyloidoses are characterised by the deposition of insoluble protein that occurs in the extracellular compartment of various tissues. One form of amyloidosis is caused by transthyretin (TTR) misfolding and deposition in target tissues. It is clear that many amyloidoses share common features of fibrillogenesis and toxicity. This chapter examines the mechanisms of TTR aggregation with a view to understanding the possible therapeutic interventions in amyloid disease.
authors.affiliation: Menzies Research Institute, University of Tasmania, Liverpool Street, 7001, Hobart, TAS, Australia, robert.gasperini@utas.edu.au.
authors.forename: Robert J
authors.initials: RJ
authors.lastname: Gasperini
authors.forename: David W
authors.initials: DW
authors.lastname: Klaver
authors.forename: Xu
authors.initials: X
authors.lastname: Hou
authors.forename: Marie-Isabel
authors.initials: MI
authors.lastname: Aguilar
authors.forename: David H
authors.initials: DH
authors.lastname: Small
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism*; D028227:Amyloid Neuropathies, Familial / Q000378:metabolism* / Q000473:pathology; D000818:Animals; D006801:Humans; D011228:Prealbumin / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding
chemical_list: D000682:Amyloid; D011228:Prealbumin