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Protein misfolding and aggregation in ageing and disease: molecular processes and therapeutic perspectives

Tuite, Mick F., Melki, Ronald (2007) Protein misfolding and aggregation in ageing and disease: molecular processes and therapeutic perspectives. Prion, 1 (2). pp. 116-120. ISSN 1933-6896. (doi:10.4161/pri.1.2.4651) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:12952)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
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https://doi.org/10.4161/pri.1.2.4651

Abstract

Although intensively researched, the fundamental mechanism of protein misfolding that leads to protein aggregation and associated diseases remains somewhat enigmatic. The failure of a protein to correctly fold de novo or to remain correctly folded can have profound consequences on a living system especially when the cellular quality control processes fail to eliminate the rogue proteins. Over 20 different human diseases have now been designated as ‘conformational diseases’ and include neurodegenerative diseases such as Alzheimer’s disease (AD), Huntington’s disease (HD) and Creutzfeldt Jakob disease (CJD) that are becoming increasingly prevalent in an ageing human population. Such diseases are usually characterised by the deposition of specific misfolded proteins as amyloid fibrils and hence are often referred to as the amyloidoses.

Item Type: Article
DOI/Identification number: 10.4161/pri.1.2.4651
Subjects: Q Science > QH Natural history > QH426 Genetics
Divisions: Faculties > Sciences > School of Biosciences > Protein Science Group
Depositing User: Michael Tuite
Date Deposited: 16 Sep 2008 07:30 UTC
Last Modified: 06 May 2020 03:03 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/12952 (The current URI for this page, for reference purposes)
Tuite, Mick F.: https://orcid.org/0000-0002-5214-540X
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