Mechanisms of transthyretin aggregation and toxicity

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

doi:10.1007/978-94-007-5416-4_9

Mechanisms of transthyretin aggregation and toxicity

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

Biochemistry & Molecular Biology

Research output: Chapter in Book/Report/Conference proceeding › Chapter (Book) › Research › peer-review

11 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 language	English
Title of host publication	Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease
Editors	J Robin Harris
Place of Publication	USA
Publisher	Springer
Pages	211 - 224
Number of pages	14
Edition	1st
ISBN (Print)	9789400754157
DOIs	https://doi.org/10.1007/978-94-007-5416-4_9
Publication status	Published - 2012

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AB - 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.

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ER -

Mechanisms of transthyretin aggregation and toxicity

Abstract

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