Degradation of a Mutant Secretory Protein, α1-Antitrypsin Z, in the Endoplasmic Reticulum Requires Proteasome Activity
Open Access
- 1 September 1996
- journal article
- Published by Elsevier
- Vol. 271 (37), 22791-22795
- https://doi.org/10.1074/jbc.271.37.22791
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- The Endoplasmic Reticulum Degradation Pathway for Mutant Secretory Proteins α1-Antitrypsin Z and S Is Distinct from That for an Unassembled Membrane ProteinPublished by Elsevier ,1996
- Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.The Journal of cell biology, 1996
- Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment.The Journal of cell biology, 1995
- Ubiquitin-mediated Processing of NF-κB Transcriptional Activator Precursor p105Journal of Biological Chemistry, 1995
- Calnexin Influences Folding of Human Class I Histocompatibility Proteins but Not Their Assembly with β2-MicroglobulinJournal of Biological Chemistry, 1995
- Calnexin: a membrane-bound chaperone of the endoplasmic reticulumTrends in Biochemical Sciences, 1994
- Regulation of MHC Class I Transport by the Molecular Chaperone, Calnexin (p88, IP90)Science, 1994
- Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocationCell, 1993
- Degradation from the endoplasmic reticulum: Disposing of newly synthesized proteinsCell, 1988
- alpha 1-Antitrypsin: molecular pathology, leukocytes, and tissue damage.Journal of Clinical Investigation, 1986