The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Ribosome Biogenesis and the Translation Process in Escherichia coli
Open accessAbstract
SUMMARY: Translation, the decoding of mRNA into protein, is the third and final element of the central dogma. The ribosome, a nucleoprotein particle, is responsible and essential for this process. The bacterial ribosome consists of three rRNA molecules and approximately 55 proteins, components that are put together in an intricate and tightly regulated way. When finally matured, the quality of the particle, as well as the amount of active ribosomes, must be checked. The focus of this review is ribosome biogenesis in Escherichia coli and its cross-talk with the ongoing protein synthesis. We discuss how the ribosomal components are produced and how their synthesis is regulated according to growth rate and the nutritional contents of the medium. We also present the many accessory factors important for the correct assembly process, the list of which has grown substantially during the last few years, even though the precise mechanisms and roles of most of the proteins are not understood.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Crystal structure of the ribosome at 5.5 Å resolution
Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H. D., & Noller, H. F. (2001) · Science · doi:10.1126/science.1060089 · Cited by 1,944
Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution
Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janell, D., Bashan, A., Bartels, H., Agmon, I., Franceschi, F., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00084-2 · Cited by 979
Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements
Korostelev, A., Trakhanov, S., Laurberg, M., & Noller, H. F. (2006) · Cell · doi:10.1016/j.cell.2006.08.032 · Cited by 498
rRNA Transcription in Escherichia coli
Paul, B. J., Ross, W., Gaal, T., & Gourse, R. L. (2004) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.091347 · Cited by 336
Cited by
An evolutionarily conserved mechanism for controlling the efficiency of protein translation
Tuller, T., Carmi, A., Vestsigian, K., Navon, S., Dorfan, Y., Zaborske, J., Pan, T., Dahan, O., Furman, I., & Pilpel, Y. (2010) · Cell · doi:10.1016/j.cell.2010.03.031 · Cited by 874
Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans
Ge, W., Wolf, A., Feng, T., Ho, C.-H., Sekirnik, R., Zayer, A., Granatino, N., Cockman, M. E., Loenarz, C., Loik, N. D., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1093 · Cited by 154
Translate to divide: сontrol of the cell cycle by protein synthesis
Department of Biochemistry and Biophysics, T. A. U., Polymenis, M., Aramayo, R., & Department of Biology, T. A. U. (2015) · Microbial Cell · doi:10.15698/mic2015.04.198 · Cited by 91
From Water and Ions to Crowded Biomacromolecules: In Vivo Structuring of a Prokaryotic Cell
Spitzer, J. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00010-11 · Cited by 77
Chen, S. S., Sperling, E., Silverman, J. M., Davis, J. H., & Williamson, J. R. (2012) · Molecular BioSystems · doi:10.1039/c2mb25310k · Cited by 65
Metadata
- Authors
- Kaczanowska, M., & Rydén-Aulin, M.
- Venue
- Microbiology and Molecular Biology Reviews
- Publisher
- American Society for Microbiology
- Published
- 2007-09
- Volume
- 71
- Issue
- 3
- Pages
- 477-494
- ISSN
- 1092-2172 (ISSN-L)
- 1098-5557
- OpenAlex
- W2100638358
- Cited by
- 400
- References
- 4
- FWCI
- 1.15
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
