The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome
Open accessAbstract
Protein synthesis is catalyzed in the peptidyl transferase center (PTC), located in the large (50S) subunit of the ribosome. No high-resolution structure of the intact ribosome has contained a complete active site including both A- and P-site tRNAs. In addition, although past structures of the 50S subunit have found no ordered proteins at the PTC, biochemical evidence suggests that specific proteins are capable of interacting with the 3′ ends of tRNA ligands. Here we present structures, at 3.6-Å and 3.5-Å resolution respectively, of the 70S ribosome in complex with A- and P-site tRNAs that mimic pre- and post-peptidyl-transfer states. These structures demonstrate that the PTC is very similar between the 50S subunit and the intact ribosome. They also reveal interactions between the ribosomal proteins L16 and L27 and the tRNA substrates, helping to elucidate the role of these proteins in peptidyl transfer.
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 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
Cited by
The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State
Gao, Y.-G., Selmer, M., Dunham, C. M., Weixlbaumer, A., Kelley, A. C., & Ramakrishnan, V. (2009) · Science · doi:10.1126/science.1179709 · Cited by 513
Self-citationRevisiting the structures of several antibiotics bound to the bacterial ribosome
Bulkley, D., Innis, C. A., Blaha, G., & Steitz, T. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008685107 · Cited by 308
Protein synthesis by ribosomes with tethered subunits
Orelle, C., Carlson, E. D., Szal, T., Florin, T., Jewett, M. C., & Mankin, A. S. (2015) · Nature · doi:10.1038/nature14862 · Cited by 231
Jenner, L., Starosta, A. L., Terry, D. S., Mikolajka, A., Filonava, L., Yusupov, M., Blanchard, S. C., Wilson, D. N., & Yusupova, G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216691110 · Cited by 204
Structural and functional insights into the mode of action of a universally conserved Obg GTPase.
Feng, B., Mandava, C. S., Guo, Q., Wang, J., Cao, W., Li, N., Zhang, Y., Zhang, Y., Wang, Z., Wu, J., et al. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001866 · Cited by 129
Ribosomal proteins: Structure, function, and evolution
Korobeinikova, A. V., Garber, M. B., & Gongadze, G. M. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912060028 · Cited by 63
Negamycin interferes with decoding and translocation by simultaneous interaction with rRNA and tRNA
Polikanov, Y. S., Szal, T., Jiang, F., Gupta, P., Matsuda, R., Shiozuka, M., Steitz, T. A., Vázquez-Laslop, N., & Mankin, A. S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.021 · Cited by 57
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
Mutational characterization and mapping of the 70S ribosome active site
d’Aquino, A. E., Azim, T., Aleksashin, N. A., Hockenberry, A. J., Krüger, A., & Jewett, M. C. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa001 · Cited by 40
The Ribosome: Some Hard Facts about Its Structure and Hot Air about Its Evolution
Ramakrishnan, V. (2009) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2009.74.032 · Cited by 27
Self-citationLomakin, I. B., Devarkar, S. C., Patel, S., Grada, A., & Bunick, C. G. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad103 · Cited by 25
Metadata
- Authors
- Voorhees, R. M., Weixlbaumer, A., Loakes, D., Kelley, A. C., & Ramakrishnan, V
- Venue
- Nature Structural & Molecular Biology
- Published
- 2009-04-12
- Volume
- 16
- Issue
- 5
- Pages
- 528-533
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2152425069
- Cited by
- 371
- References
- 1
- FWCI
- 14.64
- 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.
