The DOI matches its Crossref record; 139 of the 139 references it cites were found in a registry or an index.
Assembly of Bacterial Ribosomes
Abstract
The assembly of ribosomes from a discrete set of components is a key aspect of the highly coordinated process of ribosome biogenesis. In this review, we present a brief history of the early work on ribosome assembly in Escherichia coli, including a description of in vivo and in vitro intermediates. The assembly process is believed to progress through an alternating series of RNA conformational changes and protein-binding events; we explore the effects of ribosomal proteins in driving these events. Ribosome assembly in vivo proceeds much faster than in vitro, and we outline the contributions of several of the assembly cofactors involved, including Era, RbfA, RimJ, RimM, RimP, and RsgA, which associate with the 30S subunit, and CsdA, DbpA, Der, and SrmB, which associate with the 50S subunit.
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Cites
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Brown, C. T., Hug, L. A., Thomas, B. C., Sharon, I., Castelle, C. J., Singh, A., Wilkins, M. J., Wrighton, K. C., Williams, K. H., & Banfield, J. F. (2015) · Nature · doi:10.1038/nature14486 · Cited by 1,216
Ribosome Biogenesis in the Yeast Saccharomyces cerevisiae
Woolford, J. L., & Baserga, S. J. (2013) · Genetics · doi:10.1534/genetics.113.153197 · Cited by 757
Chloroplast Translation: Structural and Functional Organization, Operational Control, and Regulation
Zoschke, R., & Bock, R. (2018) · The Plant Cell · doi:10.1105/tpc.18.00016 · Cited by 285
Root of the Tree: The Significance, Evolution, and Origins of the Ribosome
Bowman, J. C., Petrov, A. S., Frenkel-Pinter, M., Penev, P. I., & Williams, L. D. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00742 · Cited by 197
Reducing Ribosome Biosynthesis Promotes Translation during Low Mg 2+ Stress
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Metadata
- Authors
- Shajani, Z., Sykes, M. T., & Williamson, J. R.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2011-07-07
- Volume
- 80
- Issue
- 1
- Pages
- 501-526
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2142055951
- Cited by
- 507
- References
- 139
- FWCI
- 2.41
- Type
- journal article
- Language
- en
- Open access
- closed
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