Truncations of a secretory protein define minimum lengths required for binding to signal recognition particle and translocation across the endoplasmic reticulum membrane.
Open Access
- 1 May 1990
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 265 (13), 7478-7484
- https://doi.org/10.1016/s0021-9258(19)39138-0
Abstract
No abstract availableThis publication has 39 references indexed in Scilit:
- A lower size limit exists for export of fragments of an outer membrane protein (OmpA) of Escherichia coli K-12Journal of Molecular Biology, 1989
- Mathematical modeling of the effects of the signal recognition particle on translation and translocation of proteins across the endoplasmic reticulum membraneJournal of Molecular Biology, 1987
- Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbantsCell, 1985
- Signal sequencesJournal of Molecular Biology, 1985
- Transient involvement of signal recognition particle and its receptor in the microsomal membrane prior to protein translocationCell, 1983
- Patterns of Amino Acids near Signal‐Sequence Cleavage SitesEuropean Journal of Biochemistry, 1983
- 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
- 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
- Synchronised transmembrane insertion and glycosylation of a nascent membrane proteinNature, 1977