The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Mutations Outside the Anisomycin-Binding Site Can Make Ribosomes Drug-Resistant
Open accessAbstract
Eleven mutations that make Haloarcula marismortui resistant to anisomycin, an antibiotic that competes with the amino acid side chains of aminoacyl tRNAs for binding to the A-site cleft of the large ribosomal unit, have been identified in 23S rRNA. The correlation observed between the sensitivity of H. marismortui to anisomycin and the affinity of its large ribosomal subunits for the drug indicates that its response to anisomycin is determined primarily by the binding of the drug to its large ribosomal subunit. The structures of large ribosomal subunits containing resistance mutations show that these mutations can be divided into two classes: (1) those that interfere with specific drug-ribosome interactions and (2) those that stabilize the apo conformation of the A-site cleft of the ribosome relative to its drug-bound conformation. The conformational effects of some mutations of the second kind propagate through the ribosome for considerable distances and are reversed when A-site substrates bind to the ribosome.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Dye-labeled tRNAs prepared in this manner are fully competent in tRNA selection, translocation, and peptide bond formation.
“Dye-labeled tRNAs prepared in this manner are fully competent in tRNA selection, translocation, and peptide bond formation (10).”
From Resistance mutations generate divergent antibiotic susceptibility profiles against translation inhibitors (2016) · cites this paper as [10]
Citations
Cites
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
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 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-citationCannone, J. J., Subramanian, S., Schnare, M. N., Collett, J. R., D'Souza, L. M., Du, Y., Feng, B. Y., Lin, N., Madabusi, L. V., Müller, K. M., et al. (2002) · BMC Bioinformatics · doi:10.1186/1471-2105-3-2 · Cited by 1,614
Structure of the 70S Ribosome Complexed with mRNA and tRNA
Selmer, M., Dunham, C., Murphy, F., Weixlbaumer, A., Petry, S., Kelley, A. C., Weir, J., & Ramakrishnan, V. (2006) · Science · doi:10.1126/science.1131127 · Cited by 1,352
The Molecular Basis of Antibiotic Action
Gale, E. F. (1981) · Medical Entomology and Zoology · Cited by 1,217
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
Tu, D., Blaha, G., Moore, P., & Steitz, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.005 · Cited by 439
Self-citationHansen, J. L., Moore, P. B., & Steitz, T. A. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00668-5 · Cited by 392
Self-citationAn induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA
Schmeing, T. M., Huang, K. S., Strobel, S. A., & Steitz, T. A. (2005) · Nature · doi:10.1038/nature04152 · Cited by 351
Self-citationYoungman, E. M., Brunelle, J. L., Kochaniak, A. B., & Green, R. (2004) · Cell · doi:10.1016/s0092-8674(04)00411-8 · Cited by 335
Genome sequence of Haloarcula marismortui : A halophilic archaeon from the Dead SeaPreprint
Baliga, N. S., Bonneau, R., Facciotti, M. T., Pan, M., Glusman, G., Deutsch, E. W., Shannon, P. T., Chiu, Y., Weng, R. R., Gan, R.-C. R., et al. (2004) · Genome Research · doi:10.1101/gr.2700304 · Cited by 303
Structural insights into peptide bond formation
Hansen, J., Schmeing, T., Moore, P., & Steitz, T. (2002) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.172404099 · Cited by 278
Self-citationThe Site of Action of Oxazolidinone Antibiotics in Living Bacteria and in Human Mitochondria
Leach, K. L., Swaney, S. M., Colca, J. R., McDonald, W. G., Blinn, J. R., Thomasco, L. M., Gadwood, R. C., Shinabarger, D. L., Xiong, L., & Mankin, A. S. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.04.005 · Cited by 278
A 9 Å Resolution X-Ray Crystallographic Map of the Large Ribosomal Subunit
Ban, N., Freeborn, B., Nissen, P., Penczek, P. A., Grassucci, R. A., Sweet, R. M., Frank, J., Moore, P. B., & Steitz, T. A. (1998) · Cell · doi:10.1016/s0092-8674(00)81455-5 · Cited by 275
Self-citationLin, A. H., Murray, R. W., Vidmar, T. J., & Marotti, K. R. (1997) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.41.10.2127 · Cited by 261
Schlünzen, F., Pyetan, E., Fucini, P., Yonath, A., & Harms, J. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04346.x · Cited by 240
Kloss, P., Xiong, L., Shinabarger, D. L., et al. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3247 · Cited by 214
Schmeing, T. M., Seila, A. C., Hansen, J. L., Freeborn, B., Strauss-Soukup, J. K., Scaringe, S. A., Strobel, S. A., Moore, P. B., & Steitz, T. A. (2002) · Nature Structural Biology · doi:10.1038/nsb758 · Cited by 195
Self-citationThompson, J., Kim, D. F., O'Connor, M., Lieberman, K. R., Bayfield, M. A., Gregory, S. T., Green, R., Noller, H. F., & Dahĺberg, A. E. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151257098 · Cited by 190
Structural basis for mRNA and tRNA positioning on the ribosome
Berk, V., Zhang, W., Pai, R. D., & Cate, J. H. D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607541103 · Cited by 180
Xiong, L., Kloss, P., Douthwaite, S. R., Andersen, N. M., Swaney, S. M., Shinabarger, D. L., & Mankin, A. S. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.19.5325-5331.2000 · Cited by 169
Cannone, J. J., Subramanian, S., Schnare, M. N., et al. (2002) · BMC Bioinformatics · doi:10.1186/1471-2105-3-15 · Cited by 147
Wilson, D. N., Schluenzen, F., Harms, J. M., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600525 · Cited by 108
Species-specific antibiotic-ribosome interactions: implications for drug development
Wilson, D. N., Harms, J., Nierhaus, K. H., Schlünzen, F., & Fucini, P. (2005) · Biological Chemistry · doi:10.1515/bc.2005.141 · Cited by 84
Mankin, A. S., & Garrett, R. A. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.11.3559-3563.1991 · Cited by 72
Comprehensive genetic selection revealed essential bases in the peptidyl-transferase center
Sato, N. S., Hirabayashi, N., Agmon, I., Yonath, A., & Suzuki, T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605970103 · Cited by 69
Hummel, H. S., & Boück, A. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.6.2431 · Cited by 65
Mutational Analysis of 16S and 23S rRNA Genes of Thermus thermophilus
Gregory, S. T., Carr, J. F., Rodriguez-Correa, D. T., & Dahĺberg, A. E. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.14.4804-4812.2005 · Cited by 59
Rakauskaitė, R., & Dinman, J. D. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkm1179 · Cited by 39
Tu, D., Blaha, G. M., Moore, P. B., et al. (2005) · Extremophiles · doi:10.1007/s00792-005-0459-y · Cited by 26
Self-citationFunctional analysis of seven ribosomal systems from extremely halophilic archaea
Sanz, J. L., Marı́n, I., Ureña, D., et al. (1993) · Canadian Journal of Microbiology · doi:10.1139/m93-044 · Cited by 19
Flagged first, then by citations
Cited by
Sorted by citations
The A-Z of bacterial translation inhibitors
Wilson, D. N. (2009) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409230903307311 · Cited by 322
Revisiting 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
Self-citationCocozaki, A. I., Altman, R. B., Huang, J., Buurman, E. T., Kazmirski, S. L., Doig, P., Prince, D. B., Blanchard, S. C., Cate, J. H. D., & Ferguson, A. D. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605127113 · Cited by 56
Metadata
- Authors
- Blaha, G., Gürel, G., Schroeder, S. J., Moore, P. B., & Steitz, T. A.
- Affiliations
- Yale University (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Moore, Peter B.
- Steitz, Thomas A.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2008-06
- Volume
- 379
- Issue
- 3
- Pages
- 505-519
- ISSN
- 0022-2836 (ISSN-L)
- PMC
- PMC2442718
- OpenAlex
- W2106886734
- Cited by
- 88
- References
- 34
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 4 · 2020: 5 · 2018: 4 · 2017: 2 · 2016: 4 · 2015: 8 · 2014: 5 · 2013: 6 · 2012: 5
- FWCI
- 4.79
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (F32GM067354, P01GM022778)
- 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 › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- anisomycin, antibiotic resistance, ribosome, 23S rRNA mutations, Haloarcula marismortui, large ribosomal subunit, drug binding, ribosome conformation, apo conformation, aminoacyl-tRNA binding, ribosome structure
- MeSH terms
- Anisomycin, Binding Sites, Drug Resistance, Microbial, Models, Molecular, Mutation, Protein Synthesis Inhibitors, Ribosomes, RNA, Ribosomal, 23S, Molecular Structure, Protein Structure, Tertiary, Haloarcula marismortui, Protein Subunits
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
