A novel Kex2 enzyme can process the proregion of the yeast alpha-factor leader in the endoplasmic reticulum instead of in the Golgi
- 28 February 1992
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 183 (1) , 212-219
- https://doi.org/10.1016/0006-291x(92)91630-9
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Mammalian subtilisins: The long-sought dibasic processing endoproteasesCell, 1991
- The pro domain of pre-pro-transforming growth factor .beta.1 when independently expressed is a functional binding protein for the mature growth factorBiochemistry, 1990
- Intracellular Targeting and Structural Conservation of a Prohormone-Processing EndoproteaseScience, 1989
- The αlytic protease pro-region does not require a physical linkage to activate the protease domain in vivoNature, 1989
- Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular processNature, 1989
- Enzymes Required for Yeast Prohormone ProcessingAnnual Review of Physiology, 1988
- Signal sequencesJournal of Molecular Biology, 1985
- Protein translocation across the endoplasmic reticulumCell, 1984
- Conversion of a secretory protein into a transmembrane protein results in its transport to the golgi complex but not to the cell surfaceCell, 1984
- POLYPROTEIN GENE EXPRESSION: Generation of Diversity of Neuroendocrine PeptidesAnnual Review of Biochemistry, 1984