The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein
- 1 April 1988
- Vol. 53 (2) , 273-283
- https://doi.org/10.1016/0092-8674(88)90389-3
Abstract
No abstract availableThis publication has 61 references indexed in Scilit:
- Phosphodiester bond cleavage outside mitochondria is required for the completion of protein import into the mitochondrial matrixCell, 1987
- Mitochondrial protein import: Nucleoside triphosphates are involved in conferring import-competence to precursorsCell, 1987
- Cotranslational and Posttranslational Protein Translocation in Prokaryotic SystemsAnnual Review of Cell Biology, 1986
- In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent post-translational translocation of the prepro-α-factorCell, 1986
- Intragenic suppressor mutations that restore export of maltose binding protein with a truncated signal peptideCell, 1984
- How mitochondria import proteinsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1984
- Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein.The Journal of cell biology, 1981
- Different exported proteins in E. coli show differences in the temporal mode of processing in vivoCell, 1981
- Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and MuJournal of Molecular Biology, 1976
- IN VITRO SYNTHESIS OF PROTEIN IN MICROBIAL SYSTEMSAnnual Review of Genetics, 1973