Intracellular Disposal of Incompletely Folded Human α1-Antitrypsin Involves Release from Calnexin and Post-translational Trimming of Asparagine-linked Oligosaccharides
Open Access
- 1 March 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (12) , 7946-7951
- https://doi.org/10.1074/jbc.272.12.7946
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- Calnexin Associates Exclusively with Individual CD3δ and T Cell Antigen Receptor (TCR) α Proteins Containing Incompletely Trimmed Glycans That Are Not Assembled into Multisubunit TCR ComplexesJournal of Biological Chemistry, 1996
- Calnexin Fails to Associate with Substrate Proteins in Glucosidase-deficient Cell LinesJournal of Biological Chemistry, 1995
- Calnexin Influences Folding of Human Class I Histocompatibility Proteins but Not Their Assembly with β2-MicroglobulinJournal of Biological Chemistry, 1995
- Effect of substrate structure on the activity of Man9‐mannosidase from pig liver involved in N‐linked oligosaccharide processingEuropean Journal of Biochemistry, 1992
- Genetic variants of alpha‐1‐antitrypsin (AAT)Liver International, 1992
- Protein folding in the cellNature, 1992
- Nonlysosomal, pre-Golgi degradation of unassembled asialoglycoprotein receptor subunits: a TLCK- and TPCK-sensitive cleavage within the ER.The Journal of cell biology, 1991
- Protein degradation in the endoplasmic reticulumCell, 1990
- Complete sequence of the cDNA for human .alpha.1-antitrypsin and the gene for the S variantBiochemistry, 1984
- Protein translocation across the endoplasmic reticulumCell, 1984