title: The role of molecular chaperones in human misfolding diseases.
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.
authors.affiliation: Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.
authors.forename: Sarah A
authors.initials: SA
authors.lastname: Broadley
authors.forename: F Ulrich
authors.initials: FU
authors.lastname: Hartl
mesh_terms: D056404:Chaperonin Containing TCP-1; D018833:Chaperonins / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D019636:Neurodegenerative Diseases / Q000378:metabolism*; D017510:Protein Folding
chemical_list: D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins