Cargando…
Active Site Mutations in Yeast Protein Disulfide Isomerase Cause Dithiothreitol Sensitivity and a Reduced Rate of Protein Folding in the Endoplasmic Reticulum
Aspects of protein disulfide isomerase (PDI) function have been studied in yeast in vivo. PDI contains two thioredoxin-like domains, a and a′, each of which contains an active-site CXXC motif. The relative importance of the two domains was analyzed by rendering each one inactive by mutation to SGAS....
| Autores principales: | , , |
|---|---|
| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
The Rockefeller University Press
1997
|
| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132551/ https://www.ncbi.nlm.nih.gov/pubmed/9298979 |