Protein Disulfide Isomerase and Assisted Protein Folding
Open Access
- 1 November 1997
- journal article
- review article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (47) , 29399-29402
- https://doi.org/10.1074/jbc.272.47.29399
Abstract
No abstract availableThis publication has 74 references indexed in Scilit:
- Protein folding in the endoplasmic reticulum: Lessons from the human chorionic gonadotropin β subunitProtein Science, 1996
- Principles of Chaperone-Assisted Protein Folding: Differences Between in Vitro and in Vivo MechanismsScience, 1996
- Disulfide bond formation and eukaryotic secretory productivityCurrent Opinion in Biotechnology, 1995
- Folding of an Enzyme into an Active Conformation While Bound as Peptidyl-tRNA to the RibosomeBiochemistry, 1995
- Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulumCell, 1995
- Calnexin, Calreticulin, and Bip/Kar2p in Protein FoldingCold Spring Harbor Symposia on Quantitative Biology, 1995
- Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperonesNature, 1994
- Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus.The Journal of cell biology, 1994
- Oxidized Redox State of Glutathione in the Endoplasmic ReticulumScience, 1992
- Protein folding in the cellNature, 1992