A Possible Role of ER-60 Protease in the Degradation of Misfolded Proteins in the Endoplasmic Reticulum
Open Access
- 1 June 1995
- journal article
- Published by Elsevier
- Vol. 270 (25) , 14958-14961
- https://doi.org/10.1074/jbc.270.25.14958
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- The endoplasmic reticulum as a protein-folding compartmentTrends in Cell Biology, 1992
- Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly.Proceedings of the National Academy of Sciences, 1992
- Molecular cloning of a membrane-associated human FK506- and rapamycin-binding protein, FKBP-13.Proceedings of the National Academy of Sciences, 1991
- Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules.The Journal of cell biology, 1991
- Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence.Proceedings of the National Academy of Sciences, 1991
- Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteinsCell, 1989
- Degradation from the endoplasmic reticulum: Disposing of newly synthesized proteinsCell, 1988
- An hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding proteinCell, 1986
- Sequence of protein disulphide isomerase and implications of its relationship to thioredoxinNature, 1985
- Immunoglobulin heavy chain binding proteinNature, 1983