Format

Send to

Choose Destination
See comment in PubMed Commons below
Mol Biotechnol. 2005 Oct;31(2):141-50.

Protein misfolding, aggregation, and degradation in disease.

Author information

1
Research Unit for Molecular Medicine, Institute for Clinical Medicine, Aarhus University Hospital SKS, Brendstrupgaardsvej, 8200 Arhus N, Denmark.

Abstract

Pathologies associated with protein misfolding have been observed in neurodegenerative diseases such as Alzheimer's disease, metabolic diseases like phenylketonuria, and diseases affecting structural proteins like collagen or keratin. Misfolding of mutant proteins in these and many other diseases may result in premature degradation, formation of toxic aggregates, or incorporation of toxic conformations into structures. We review common traits of these diverse diseases under the unifying view of protein misfolding. The molecular pathogenesis is discussed in the context of protein quality control systems consisting of molecular chaperones and intracellular proteases that assist the folding and supervise the maintenance of the folded structure. Furthermore, genetic and environmental factors that may modify the severity of these diseases are underscored.

PMID:
16170215
DOI:
10.1385/MB:31:2:141
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer
    Loading ...
    Support Center