The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
The Signal Recognition Particle
Abstract
▪ Abstract The signal recognition particle (SRP) and its membrane-associated receptor (SR) catalyze targeting of nascent secretory and membrane proteins to the protein translocation apparatus of the cell. Components of the SRP pathway and salient features of the molecular mechanism of SRP-dependent protein targeting are conserved in all three kingdoms of life. Recent advances in the structure determination of a number of key components in the eukaryotic and prokaryotic SRP pathway provide new insight into the molecular basis of SRP function, and they set the stage for future work toward an integrated picture that takes into account the dynamic and contextual properties of this remarkable cellular machine.
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Citations
Cites
The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392
Ulbrandt, N. D., Newitt, J. A., & Bernstein, H. D. (1997) · Cell · doi:10.1016/s0092-8674(00)81839-5 · Cited by 332
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
Self-citationCrystal 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
Protein translocation in the three domains of life: variations on a theme.
Pohlschröder, M., Prinz, W. A., Hartmann, E., & Beckwith, J. (1997) · Cell · doi:10.1016/s0092-8674(00)80443-2 · Cited by 187
Cited by
Stanley, S. A., Raghavan, S., Hwang, W. W., & Cox, J. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2235593100 · Cited by 570
Mutations in progranulin are a major cause of ubiquitin-positive frontotemporal lobar degeneration
Gass, J., Cannon, A., Mackenzie, I. R., Boeve, B., Baker, M., Adamson, J., Crook, R., Melquist, S., Kuntz, K., Petersen, R., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl241 · Cited by 580
Recombinant protein secretion in Escherichia coli
Mergulhão, F. J. M., Summers, D. K., & Monteiro, G. A. (2005) · Biotechnology Advances · doi:10.1016/j.biotechadv.2004.11.003 · Cited by 485
Biochemistry and Molecular Biology of Flaviviruses
Barrows, N. J., Campos, R. K., Liao, K.-C., Prasanth, K. R., Soto-Acosta, R., Yeh, S.-C., Schott-Lerner, G., Pompon, J., Sessions, O. M., Bradrick, S. S., et al. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00719 · Cited by 341
Substrate twinning activates the signal recognition particle and its receptor
Egea, P. F., Shan, S.-O., Napetschnig, J., Savage, D. F., Walter, P., & Stroud, R. M. (2004) · Nature · doi:10.1038/nature02250 · Cited by 288
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Metadata
- Authors
- Keenan, R. J., Freymann, D. M., Stroud, R. M., & Walter, P.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2001-06
- Volume
- 70
- Issue
- 1
- Pages
- 755-775
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2137032962
- Cited by
- 633
- References
- 5
- FWCI
- 2.88
- Type
- journal article
- Language
- en
- Open access
- closed
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