Degradation of Mutated Bovine Pancreatic Trypsin Inhibitor in the Yeast Vacuole Suggests Post-endoplasmic Reticulum Protein Quality Control
Open Access
- 1 April 2004
- journal article
- Published by Elsevier
- Vol. 279 (15), 15289-15297
- https://doi.org/10.1074/jbc.m309673200
Abstract
No abstract availableKeywords
This publication has 73 references indexed in Scilit:
- Behavior in the Eukaryotic Secretory Pathway of Insulin-containing Fusion Proteins and Single-chain Insulins Bearing Various B-chain MutationsPublished by Elsevier ,2003
- Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases.The Journal of cell biology, 1996
- A kinetic explanation for the rearrangement pathway of BPTI foldingNature Structural & Molecular Biology, 1995
- Accelerated secretion of human lysozyme with a disulfide bond mutationEuropean Journal of Biochemistry, 1992
- Multifunctional yeast high-copy-number shuttle vectorsGene, 1992
- (14–38, 30–51) Double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: A two-dimensional 1H nuclear magnetic resonance studyJournal of Molecular Biology, 1991
- Role of disulfide bonds in folding and secretion of human lysozyme in saccharomycescerevisiaeBiochemical and Biophysical Research Communications, 1988
- Structure of form III crystals of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1987
- Reinvestigation of the aromatic side-chains in the basic pancreatic trypsin inhibitor by heteronuclear two-dimensional nuclear magnetic resonanceJournal of Molecular Biology, 1987
- Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1984