Sequences beyond the cleavage site influence signal peptide function.
Open Access
- 1 October 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (30) , 15791-15798
- https://doi.org/10.1016/s0021-9258(19)37658-6
Abstract
No abstract availableThis publication has 26 references indexed in Scilit:
- Translocation of globin fusion proteins across the endoplasmic reticulum membrane in Xenopus laevis oocytes.The Journal of cell biology, 1987
- Direct probing of the interaction between the signal sequence of nascent preprolactin and the signal recognition particle by specific cross-linking.The Journal of cell biology, 1987
- Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein.The Journal of cell biology, 1986
- A stop transfer sequence recognizes receptors for nascent chain translocation across the endoplasmic reticulum membraneCell, 1986
- The signal recognition particle receptor is a complex that contains two distinct polypeptide chains.The Journal of cell biology, 1986
- Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intactNature, 1986
- A former amino terminal signal sequence engineered to an internal location directs translocation of both flanking protein domains.The Journal of cell biology, 1985
- Signal sequencesJournal of Molecular Biology, 1985
- Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor.The Journal of cell biology, 1982
- Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle.The Journal of cell biology, 1982