Molecular chaperones are generally thought to protect newly synthesized proteins and ensure that they fold into the correct shape. But it seems that two chaperones also help to target certain proteins to mitochondria.
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References
Young, J. C., Hoogenraad, N. J. & Hartl, F. U. Cell 112, 41–50 (2003).
Deshaies, R. J. et al. Nature 332, 800–805 (1988).
Murakami, H., Pain, D. & Blobel, G. J. Cell Biol. 107, 2051–2057 (1988).
Ellis, R. J. Biochem. Biophys. Res. Commun. 238, 687–692 (1997).
Pfanner, N. & Geissler, A. Nature Rev. Mol. Cell Biol. 2, 339–349 (2001).
Brix, J., Dietmeier, K. & Pfanner, N. J. Biol. Chem. 272, 20730–20735 (1997).
Frydman, J. Annu. Rev. Biochem. 70, 603–649 (2001).
Young, J. C., Moarefi, I. & Hartl, F. U. J. Cell Biol. 154, 267–273 (2001).
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Ellis, R. Plugging the transport gap. Nature 421, 801–802 (2003). https://doi.org/10.1038/421801a
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DOI: https://doi.org/10.1038/421801a
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