Mechanisms of transthyretin aggregation and toxicity

Robert Gasperini, David W Klaver, Xu Hou, Mibel [Marie-Isabel] Aguilar, David H Small

Research output: Chapter in Book/Report/Conference proceedingChapter (Book)Researchpeer-review

7 Citations (Scopus)

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.
Original languageEnglish
Title of host publicationProtein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease
EditorsJ Robin Harris
Place of PublicationUSA
PublisherSpringer
Pages211 - 224
Number of pages14
Edition1st
ISBN (Print)9789400754157
DOIs
Publication statusPublished - 2012

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