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Science 3 December 1999:
Vol. 286. no. 5446, pp. 1888 - 1893
DOI: 10.1126/science.286.5446.1888
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Review

Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins

Sue Wickner, 1 Michael R. Maurizi, 2 Susan Gottesman 1*

Polypeptides emerging from the ribosome must fold into stable three-dimensional structures and maintain that structure throughout their functional lifetimes. Maintaining quality control over protein structure and function depends on molecular chaperones and proteases, both of which can recognize hydrophobic regions exposed on unfolded polypeptides. Molecular chaperones promote proper protein folding and prevent aggregation, and energy-dependent proteases eliminate irreversibly damaged proteins. The kinetics of partitioning between chaperones and proteases determines whether a protein will be destroyed before it folds properly. When both quality control options fail, damaged proteins accumulate as aggregates, a process associated with amyloid diseases.

1 Laboratory of Molecular Biology, National Cancer Institute, Bethesda, MD 20892-4255, USA.
2 Laboratory of Cell Biology, National Cancer Institute, Bethesda, MD 20892-4255, USA.
*   To whom correspondence should be addressed: E-mail: susang{at}helix.nih.gov

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T. Shoham, R. Rajapaksa, C. Boucheix, E. Rubinstein, J. C. Poe, T. F. Tedder, and S. Levy (2003)
J. Immunol. 171, 4062-4072
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An Intron Is Required for Dihydrofolate Reductase Protein Stability.
V. Noe, S. MacKenzie, and C. J. Ciudad (2003)
J. Biol. Chem. 278, 38292-38300
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The Future of Regulatory Toxicology: Impact of the Biotechnology Revolution.
J. T. MacGregor (2003)
Toxicol. Sci. 75, 236-248
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Dependence of Endoplasmic Reticulum-associated Degradation on the Peptide Binding Domain and Concentration of BiP.
M. Kabani, S. S. Kelley, M. W. Morrow, D. L. Montgomery, R. Sivendran, M. D. Rose, L. M. Gierasch, and J. L. Brodsky (2003)
Mol. Biol. Cell 14, 3437-3448