Review
Nature Reviews Molecular Cell Biology 5, 781-791 (October 2004) | doi:10.1038/nrm1492
Pathways of chaperone-mediated protein folding in the cytosol
Jason C. Young1, Vishwas R. Agashe2, Katja Siegers2 & F. Ulrich Hartl2 About the authors
Abstract
Cells are faced with the task of folding thousands of different polypeptides into a wide range of conformations. For many proteins, the folding process requires the action of molecular chaperones. In the cytosol of prokaryotic and eukaryotic cells, molecular chaperones of different structural classes form a network of pathways that can handle substrate polypeptides from the point of initial synthesis on ribosomes to the final stages of folding.
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Author affiliations
- Department of Biochemistry, McIntyre Medical Sciences Building, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec H3G 1Y6, Canada.
- Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18A, D-82152 Martinsried, Germany.
Correspondence to: F. Ulrich Hartl2 Email: uhartl@biochem.mpg.de
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