The DOI matches its Crossref record; 35 of the 36 references it cites were found in a registry or an index.
RNA, the first macromolecular catalyst: the ribosome is a ribozyme
Abstract
Recently, the atomic structures of the large ribosomal subunit from Haloarcula marismortui and its complexes with substrates have been determined. These have provided exciting new insights into the principles of RNA structure, the mechanism of the peptidyl-transferase reaction and early events in the evolution of this RNA-protein complex assembly that is essential in all cells. The structures of the large subunit bound to a variety of antibiotics explain the effects of antibiotic resistance mutations and provide promise for the development of new antibiotics.
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“The central role of RNA in modern cellular biochemistry, and especially the role of the large ribosomal RNA as the catalyst of protein synthesis (Steitz and Moore 2003), provides a powerful argument in support of RNA as the dominant genetic and functional biopolymer at an early stage in the evolution of life.”
From Protocells and RNA Self-Replication (2018) · cites this paper as Steitz and Moore 2003
Citations
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The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution
Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327
Self-citationThe RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., & Altman, S. (1983) · Cell · doi:10.1016/0092-8674(83)90117-4 · Cited by 2,684
The Structural Basis of Ribosome Activity in Peptide Bond Synthesis
Nissen, P., Hansen, J., Ban, N., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.920 · Cited by 2,269
Self-citationRecognition of Cognate Transfer RNA by the 30 S Ribosomal Subunit
Ogle, J. M., Brodersen, D. E., Clemons, W. M., Tarry, M. J., Carter, A. P., & Ramakrishnan, V. (2001) · Science · doi:10.1126/science.1060612 · Cited by 1,162
Schlünzen, F., Zarivach, R., Harms, J., Bashan, A., Tocilj, A., Albrecht, R., Yonath, A., & Franceschi, F. J. (2001) · Nature · doi:10.1038/35101544 · Cited by 1,057
A SMALL PARTICULATE COMPONENT OF THE CYTOPLASM
Palade, G. E. (1955) · The Journal of Cell Biology · doi:10.1083/jcb.1.1.59 · Cited by 1,014
High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium
Harms, J. M., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Franceschi, F. J., & Yonath, A. (2001) · Cell · doi:10.1016/s0092-8674(01)00546-3 · Cited by 899
Cech, T. R., Zaug, A. J., & Grabowski, P. J. (1981) · Cell · doi:10.1016/0092-8674(81)90390-1 · Cited by 879
The kink‐turn: a new RNA secondary structure motif
Klein, D. J., Schmeing, T. M., Moore, P. B., & Steitz, T. A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.15.4214 · Cited by 740
Self-citationRNA tertiary interactions in the large ribosomal subunit: The A-minor motif
Nissen, P., Ippolito, J. A., Ban, N., Moore, P. B., & Steitz, T. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081082398 · Cited by 659
Self-citation
Research works printed but not linked: 1
- Yonath, 1980, Crystallization of the large ribosomal subunits from Bacillus stearothermophilus, Biochem. Internat., 1, 428
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Ribosomal proteins L5 and L15 : Functional characterisation of important features, in vivo
Simoff, I. (2009) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
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Khatter, H. (2014) · theses.fr (ABES) · doi:10.70675/576d1963z5f06z4969z8e92za6c59db0443a
Rôle de la RNase III dans l'adaptation d'Escherichia coli à son environnement
Lejars, M. (2020) · theses.fr (ABES) · doi:10.70675/2219a318z5d00z4fa5zade7z2e6ecc40516c
Deep learning methods for long RNA secondary structure prediction
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RNA Dynamics in the Evolution of RNA Function
Ebermann, C., & Müller, S. (2026) · Springer eBooks · doi:10.1007/978-3-032-24295-2_13
Recurring RNA motifs: from A-minor to ribose zipper
Law, M. V., Kiliushik, D., Zablonski, E. J., Jenkins, J. L., & Wedekind, J. E. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113668
Computational methods for understanding RNA catalysis: a molecular approach
Radak, B. K. (2014) · University of Minnesota Digital Conservancy (University of Minnesota)
Metadata
- Authors
- Steitz, T. A., & Moore, P. B.
- Affiliations
- Howard Hughes Medical Institute (US)
- Yale University (US)
- Corresponding author
- Steitz, Thomas A
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2003-08
- Volume
- 28
- Issue
- 8
- Pages
- 411-418
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2162522101
- Cited by
- 319
- References
- 36
- Citations by year
- 2026: 5 · 2025: 10 · 2024: 7 · 2023: 10 · 2022: 7 · 2021: 8 · 2020: 10 · 2019: 7 · 2018: 11 · 2017: 10 · 2016: 13 · 2015: 10 · 2014: 20 · 2013: 10 · 2012: 15
- FWCI
- 1.87
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Agouron Institute
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- ribosome, ribozymes, peptidyl transferase, RNA catalysis, large ribosomal subunit, Haloarcula marismortui, antibiotic resistance, antibiotic binding sites, RNA structure
- MeSH terms
- Drug Resistance, Microbial, Microscopy, Electron, Models, Chemical, Models, Molecular, Nucleic Acid Conformation, Peptide Elongation Factor Tu, Peptidyl Transferases, Protein Binding, Ribosomes, RNA, RNA, Messenger, RNA, Ribosomal, 23S, RNA, Transfer, RNA, Catalytic, Haloarcula marismortui
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