The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The Translocon: A Dynamic Gateway at the ER Membrane
Abstract
▪ Abstract Cotranslational protein translocation across and integration into the membrane of the endoplasmic reticulum (ER) occur at sites termed translocons. Translocons are composed of several ER membrane proteins that associate to form an aqueous pore through which secretory proteins and lumenal domains of membrane proteins pass from the cytoplasm to the ER lumen. These sites are not passive holes in the bilayer, but instead are quite dynamic both structurally and functionally. Translocons cycle between ribosome-bound and ribosome-free states, and convert between translocation and integration modes of operation. These changes in functional state are accompanied by structural rearrangements that alter translocon conformation, composition, and interactions with ligands such as the ribosome and BiP. Recent studies have revealed that the translocon is a complex and sophisticated molecular machine that regulates the movement of polypeptides through the bilayer, apparently in both directions as well as laterally into the bilayer, all while maintaining the membrane permeability barrier.
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Structure of the conserved GTPase domain of the signal recognition particle.
Freymann, D. M., Keenan, R. J., Stroud, R. M., & Walter, P. (1997) · Nature · doi:10.1038/385361a0 · Cited by 228
Crystal structure of the NG domain from the signal-recognition particle receptor FtsY.
Montoya, G., Svensson, C., Luirink, J., & Sinning, I. (1997) · Nature · doi:10.1038/385365a0 · Cited by 210
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Holaska, J. M., Black, B. E., Love, D. C., Hanover, J. A., Leszyk, J., & Paschal, B. M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.1.127 · Cited by 277
Metadata
- Authors
- Johnson, A. E., & van Waes, M. A.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 1999-11
- Volume
- 15
- Issue
- 1
- Pages
- 799-842
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2117761303
- Cited by
- 603
- References
- 3
- FWCI
- 2.13
- Type
- journal article
- Language
- en
- Open access
- closed
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