Protein folding and quality control in the endoplasmic reticulum.

@article{Kleizen2004ProteinFA,
  title={Protein folding and quality control in the endoplasmic reticulum.},
  author={Bertrand Kleizen and Ineke Braakman},
  journal={Current opinion in cell biology},
  year={2004},
  volume={16 4},
  pages={343-9}
}
The endoplasmic reticulum (ER) is a highly versatile protein factory that is equipped with chaperones and folding enzymes essential for protein folding. ER quality control guided by these chaperones is essential for life. Whereas correctly folded proteins are exported from the ER, misfolded proteins are retained and selectively degraded. At least two main chaperone classes, BiP and calnexin/calreticulin, are active in ER quality control. Folding factors usually are found in complexes. Recent… CONTINUE READING
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High S: The primary substrate binding site in the b’ domain of ERp57 is adapted for ER lectin association

  • SJ Russell, LW Ruddock, +6 authors J Myllyharju
  • J Biol Chem
  • 2004
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