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Mechanisms of Transthyretin Aggregation and Toxicity

Citation

Gasperini, RJ and Klaver, DW and Hou, X and Aguilar, MI and Small, DH, Mechanisms of Transthyretin Aggregation and Toxicity, Protein Aggregation and Fibrillogenesis in Cerebral and Systematic Amyloid Disease, Subcellular Biochemistry 65, Springer, JR Harris (ed), Dordrecht, pp. 211-224. ISBN 978-94-007-5415-7 (2012) [Research Book Chapter]

Copyright Statement

Copyright 2012 Springer Science+Business Media Dordrecht

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

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.

Item Details

Item Type:Research Book Chapter
Keywords:amyloid, familial amyloidotic polyneuropathy, fibrillogenesis, amyloidosis, calcium, glycosoaminoglycans
Research Division:Medical and Health Sciences
Research Group:Neurosciences
Research Field:Neurosciences not elsewhere classified
Objective Division:Health
Objective Group:Clinical Health (Organs, Diseases and Abnormal Conditions)
Objective Field:Neurodegenerative Disorders Related to Ageing
Author:Gasperini, RJ (Dr Rob Gasperini)
Author:Small, DH (Professor David Small)
ID Code:82322
Year Published:2012
Deposited By:Menzies Institute for Medical Research
Deposited On:2013-01-24
Last Modified:2017-11-06
Downloads:0

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