Protein disulfide isomerase associates with misfolded human lysozyme in vivo.
Open Access
- 1 March 1994
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (9), 6874-6877
- https://doi.org/10.1016/s0021-9258(17)37456-2
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- PDI and glutathione-mediated reduction of the glutathionylated variant of human lysozymeFEBS Letters, 1993
- Non‐lysosomal degradation of misfolded human lysozymes with and without an asparagine‐linked glycosylation siteEuropean Journal of Biochemistry, 1992
- HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells.The Journal of Experimental Medicine, 1992
- Accelerated secretion of human lysozyme with a disulfide bond mutationEuropean Journal of Biochemistry, 1992
- Behavior of cysteine mutants of human lysozyme in de novo synthesis and in vivo secretionEuropean Journal of Biochemistry, 1991
- Formation and intracellular transport of a heterodimeric viral spike protein complex.The Journal of cell biology, 1991
- Protein degradation in the endoplasmic reticulumCell, 1990
- Intracellular degradation of unassembled asialoglycoprotein receptor subunits: a pre-Golgi, nonlysosomal endoproteolytic cleavage.The Journal of cell biology, 1989
- Role of disulfide bonds in folding and secretion of human lysozyme in saccharomycescerevisiaeBiochemical and Biophysical Research Communications, 1988
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970