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- Title
The role of molecular chaperones in human misfolding diseases
- Authors
Broadley, Sarah A.; Hartl, F. Ulrich
- Abstract
Abstract: Human misfolding diseases arise when proteins adopt non-native conformations that endow them with a tendency to aggregate and form intra- and/or extra-cellular deposits. Molecular chaperones, such as Hsp70 and TCP-1 Ring Complex (TRiC)/chaperonin containing TCP-1 (CCT), have been implicated as potent modulators of misfolding disease. These chaperones suppress toxicity of disease proteins and modify early events in the aggregation process in a cooperative and sequential manner reminiscent of their functions in de novo protein folding. Further understanding of the role of Hsp70, TRiC, and other chaperones in misfolding disease is likely to provide important insight into basic pathomechanistic principles that could potentially be exploited for therapeutic purposes.
- Subjects
MOLECULAR chaperones; PROTEIN folding; DEGENERATION (Pathology); CELL aggregation; PROTEINS; TOXICOLOGY; HEAT shock proteins
- Publication
FEBS Letters, 2009, Vol 583, Issue 16, p2647
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.04.029