Short peptide domains target proteins to plant vacuoles
- 21 February 1992
- Vol. 68 (4), 613-616
- https://doi.org/10.1016/0092-8674(92)90134-x
Abstract
No abstract availableThis publication has 25 references indexed in Scilit:
- Vicilin with carboxy‐terminal KDEL is retained in the endoplasmic reticulum and accumulates to high levels in the leaves of transgenic plantsThe Plant Journal, 1992
- The barley lectin carboxyl-terminal propeptide is a vacuolar protein sorting determinant in plants.Plant Cell, 1991
- The Signal Peptide of a Vacuolar Protein Is Necessary and Sufficient for the Efficient Secretion of a Cytosolic ProteinPlant Physiology, 1991
- Expression and regulation of lectin genes in cereals and riceDevelopmental Genetics, 1991
- In Vitro Processing of Aleurain, a Barley Vacuolar Thiol Protease.Plant Cell, 1990
- In vitro Processing of Aleurain, a Barley Vacuolar Thiol ProteasePlant Cell, 1990
- Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids.The Journal of cell biology, 1990
- The amino acid sequence of a novel inhibitor of cathepsin D from potatoFEBS Letters, 1990
- A short domain of the plant vacuolar protein phytohemagglutinin targets invertase to the yeast vacuole.Plant Cell, 1990
- Role of propeptide glycan in post-translational processing and transport of barley lectin to vacuoles in transgenic tobacco.Plant Cell, 1990