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The role of molecular chaperones in human misfolding diseases
Author(s) -
Broadley Sarah A.,
Hartl F. Ulrich
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.04.029
Subject(s) - chaperonin , protein folding , co chaperone , chemical chaperone , chaperone (clinical) , protein aggregation , folding (dsp implementation) , hsp70 , biology , proteostasis , computational biology , microbiology and biotechnology , heat shock protein , chemistry , biochemistry , unfolded protein response , medicine , endoplasmic reticulum , gene , engineering , pathology , electrical engineering
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.