Abstract
Our understanding of eukaryotic protein folding in the endoplasmic reticulum has increased enormously over the last 5 years. In this review, we summarize some of the major research themes that have captivated researchers in this field during the last years of the 20th century. We follow the path of a typical protein as it emerges from the ribosome and enters the reticular environment. While many of these events are shared between different polypeptide chains, we highlight some of the numerous differences between proteins, between cell types, and between the chaperones utilized by different ER glycoproteins. Finally, we consider the likely advances in this field as the new century unfolds and we address the prospect of a unified understanding of how protein folding, degradation, and translation are coordinated within a cell.
| Original language | English |
|---|---|
| Pages (from-to) | 433-473 |
| Journal | Critical reviews in biochemistry and molecular biology |
| Volume | 35 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2000 |
| Externally published | Yes |
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