The DOI matches its Crossref record; 129 of the 129 references it cites were found in a registry or an index.
Ribosomal proteins: Structure, function, and evolution
Abstract
The question concerning reasons for the variety of ribosomal proteins that arose for more than 40 years ago is still open. Ribosomes of modern organisms contain 50-80 individual proteins. Some are characteristic for all domains of life (universal ribosomal proteins), whereas others are specific for bacteria, archaea, or eucaryotes. Extensive information about ribosomal proteins has been obtained since that time. However, the role of the majority of ribosomal proteins in the formation and functioning of the ribosome is still not so clear. Based on recent data of experiments and bioinformatics, this review presents a comprehensive evaluation of structural conservatism of ribosomal proteins from evolutionarily distant organisms. Considering the current knowledge about features of the structural organization of the universal proteins and their intermolecular contacts, a possible role of individual proteins and their structural elements in the formation and functioning of ribosomes is discussed. The structural and functional conservatism of the majority of proteins of this group suggests that they should be present in the ribosome already in the early stages of its evolution.
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“Four of the overlapping putative targets with the highest betweenness centrality play a role in protein translation [82, 83] (RPL3, EIF4A2), MAPK signaling (MAPK3) and p53 signaling [84] (DAZAP2) (Fig. 5E) (Supplementary Table 7).”
From microRNA-132 attenuates inflammation in induced pluripotent stem cell-derived microglia from Alzheimer’s disease patients (2026) · cites this paper as [82]
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Cites
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Research works printed but not linked: 1
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Altered Machinery of Protein Synthesis in Alzheimer's: From the Nucleolus to the Ribosome
Hernández‐Ortega, K., Garcia‐Esparcia, P., Gil, L., Lucas, J. J., & Ferrer, I. (2016) · Brain Pathology · doi:10.1111/bpa.12335 · Cited by 245
The Peptidyl Transferase Center: a Window to the Past
Tirumalai, M. R., Rivas, M., Tran, Q., & Fox, G. E. (2021) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00104-21 · Cited by 53
On the possible origin of protein homochirality, structure, and biochemical function
Skolnick, J., Zhou, H., & Gao, M. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1908241116 · Cited by 45
Li, Q., Chang, R., Sun, Y., & Li, B. (2016) · PLOS ONE · doi:10.1371/journal.pone.0166876 · Cited by 19
Penning, A., Snoeck, S., Ormaechea, O. R., Ayyildiz, D., Polzer, O., Buitrago-Arango, M., Capobianco, R., de Winter, F., Balusu, S., Verhaagen, J., et al. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02228-8 · Cited by 6
Metadata
- Authors
- Korobeinikova, A. V., Garber, M. B., & Gongadze, G. M.
- Venue
- Biochemistry (Moscow)
- Publisher
- Pleiades Publishing Ltd
- Published
- 2012-06
- Volume
- 77
- Issue
- 6
- Pages
- 562-574
- ISSN
- 0006-2979
- 1608-3040
- Cited by
- 63
- References
- 129
- Language
- en
- Licence
- www.springernature.com/gp/researchers/text-and-data-mining (tdm)
- www.springernature.com/gp/researchers/text-and-data-mining (vor)
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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.
