Chemically related 4,5-linked aminoglycoside antibiotics drive subunit rotation in opposite directions
Open accessAbstract
Dynamic remodelling of intersubunit bridge B2, a conserved RNA domain of the bacterial ribosome connecting helices 44 (h44) and 69 (H69) of the small and large subunit, respectively, impacts translation by controlling intersubunit rotation. Here we show that aminoglycosides chemically related to neomycin—paromomycin, ribostamycin and neamine—each bind to sites within h44 and H69 to perturb bridge B2 and affect subunit rotation. Neomycin and paromomycin, which only differ by their ring-I 6′-polar group, drive subunit rotation in opposite directions. This suggests that their distinct actions hinge on the 6′-substituent and the drug’s net positive charge. By solving the crystal structure of the paromomycin–ribosome complex, we observe specific contacts between the apical tip of H69 and the 6′-hydroxyl on paromomycin from within the drug’s canonical h44-binding site. These results indicate that aminoglycoside actions must be framed in the context of bridge B2 and their regulation of subunit rotation.
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
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.
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?
Optical clocks have orders of magnitude better precision and accuracy than microwave counterparts realizing the SI-second.
“Optical clocks are—due to their orders of magnitude better precision1 and accuracy234 than their microwave counterparts realizing the definition of the SI-second—new sensors with highest resolving power”
From A clock network for geodesy and fundamental science (2016) · cites this paper as [2]
The Results discuss aminoglycoside effects on E. coli ribosome rotation, while the Methods describe fluorescence measurements of ribosome complexes; no page numbers are available in our copy. Searches for optical clocks, microwave clocks, and the SI-second found no passage comparing clock precision or accuracy. (LLM, conf=0.78)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works
<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147 · see citing works
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463 · see citing works
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334 · see citing works
Genome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling
Ingolia, N. T., Ghaemmaghami, S., Newman, J. R. S., & Weissman, J. S. (2009) · Science · doi:10.1126/science.1168978 · Cited by 3,853 · see citing works
Carter, A. P., Clemons, W. M., Brodersen, D. E., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030019 · Cited by 1,615 · see citing works
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 · see citing works
Interaction of antibiotics with functional sites in 16S ribosomal RNA
Moazed, D., & Noller, H. F. (1987) · Nature · doi:10.1038/327389a0 · Cited by 1,150 · see citing works
The Structure of the Eukaryotic Ribosome at 3.0 Å Resolution
Shem, A. B., de Loubresse, N. G., Melnikov, S. V., Jenner, L. B., Yusupova, G. Z., & Yusupov, M. (2011) · Science · doi:10.1126/science.1212642 · Cited by 1,114 · see citing works
Aitken, C. E., Marshall, R. A., & Puglisi, J. D. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.117689 · Cited by 846 · see citing works
Analysis of Single-Molecule FRET Trajectories Using Hidden Markov Modeling
McKinney, S., Joo, C., & Ha, T. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.082487 · Cited by 760 · see citing works
Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form
Ogle, J. M., Murphy, F. V., Tarry, M. J., & Ramakrishnan, V. (2002) · Cell · doi:10.1016/s0092-8674(02)01086-3 · Cited by 663 · see citing works
Locking and Unlocking of Ribosomal Motions
Valle, M., Zavialov, A. V., Sengupta, J., Rawat, U. B. S., Ehrenberg, M., & Frank, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00476-8 · Cited by 590 · see citing works
STRUCTURAL INSIGHTS INTO TRANSLATIONAL FIDELITY
Ogle, J. M., & Ramakrishnan, V. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.061903.155440 · Cited by 586 · see citing works
Mechanism of bactericidal action of aminoglycosides
Davis, B. D. (1987) · Microbiological Reviews · doi:10.1128/mr.51.3.341-350.1987 · Cited by 511 · see citing works
tRNA dynamics on the ribosome during translation
Blanchard, S. C., Kim, H. D., Gonzalez, R. L., Puglisi, J. D., & Chu, S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403884101 · Cited by 469 · see citing works
Self-citationRibosome dynamics and tRNA movement by time-resolved electron cryomicroscopy
Fischer, N., Konevega, A. L., Wintermeyer, W., Rodnina, M. V., & Stark, H. (2010) · Nature · doi:10.1038/nature09206 · Cited by 434 · see citing works
Aminoglycoside Antibiotics in the 21st Century
Becker, B., & Cooper, M. A. (2012) · ACS Chemical Biology · doi:10.1021/cb3005116 · Cited by 420 · see citing works
Ultra-stable organic fluorophores for single-molecule research
Zheng, Q., Juette, M. F., Jockusch, S., Wasserman, M. R., Zhou, Z., Altman, R. B., & Blanchard, S. C. (2013) · Chemical Society Reviews · doi:10.1039/c3cs60237k · Cited by 402 · see citing works
Self-citationMisreading of RNA Codewords Induced by Aminoglycoside Antibiotics
DAVIES, J. E., Gorini, L., & Davis, B. D. (1965) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)14722-6 · Cited by 402 · see citing works
Spontaneous Intersubunit Rotation in Single Ribosomes
Cornish, P. V., Ermolenko, D. N., Noller, H. F., & Ha, T. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.004 · Cited by 393 · see citing works
Structures of the Bacterial Ribosome in Classical and Hybrid States of tRNA Binding
Dunkle, J. A., Wang, L., Feldman, M. B., Pulk, A., Chen, V. B., Kapral, G. J., Noeske, J., Richardson, J. S., Blanchard, S. C., & Cate, J. H. D. (2011) · Science · doi:10.1126/science.1202692 · Cited by 373 · see citing works
Self-citationStructural basis for aminoglycoside inhibition of bacterial ribosome recycling
Borovinskaya, M. A., Pai, R., Zhang, W., Schuwirth, B., Holton, J., Hirokawa, G., Kaji, H., Kaji, A., & Cate, J. H. D. (2007) · Nature Structural &Molecular Biology · doi:10.1038/nsmb1271 · Cited by 366 · see citing works
The puromycin reaction and its relation to protein synthesis
Traut, R. R., & Monro, R. E. (1964) · Journal of Molecular Biology · doi:10.1016/s0022-2836(64)80028-0 · Cited by 363 · see citing works
Head swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites
Ratje, A. H., Loerke, J., Mikolajka, A., Brunner, M. J., Hildebrand, P. W., Starosta, A. L., Dönhöfer, A., Connell, S. R., Fucini, P., Mielke, T., et al. (2010) · Nature · doi:10.1038/nature09547 · Cited by 358 · see citing works
Fidelity of Aminoacyl-tRNA Selection on the Ribosome: Kinetic and Structural Mechanisms
Rodnina, M. V., & Wintermeyer, W. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.415 · Cited by 334 · see citing works
The Ribosome, Structure, Function, Antibiotics, and Cellular Interactions
Garrett, R. A. (2000) · Research at the University of Copenhagen (University of Copenhagen) · Cited by 325 · see citing works
Coupling of Ribosomal L1 Stalk and tRNA Dynamics during Translation Elongation
Fei, J., Kosuri, P., MacDougall, D. D., & Gonzalez, R. L. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.012 · Cited by 316 · see citing works
Identification of Two Distinct Hybrid State Intermediates on the Ribosome
Munro, J. B., Altman, R. B., O’Connor, N., & Blanchard, S. C. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.022 · Cited by 262 · see citing works
Self-citationZhou, Z., Cironi, P., Lin, A. J., Xu, Y., Hrvatin, S., Golan, D. E., Silver, P. A., Walsh, C. T., & Yin, J. (2007) · ACS Chemical Biology · doi:10.1021/cb700054k · Cited by 228 · see citing works
Self-citationGreenberg, W. A., Priestley, E. S., Sears, P. S., Alper, P. B., Rosenbohm, C., Hendrix, M., Hung, S., & Wong, C. (1999) · Journal of the American Chemical Society · doi:10.1021/ja9910356 · Cited by 218 · see citing works
Burke, J. F., & Mogg, A. E. (1985) · Nucleic Acids Research · doi:10.1093/nar/13.17.6265 · Cited by 218 · see citing works
Blaha, G. M., Stelzl, U., Spahn, C. M. T., Agrawal, R. K., Frank, J., & Nierhaus, K. H. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)17021-1 · Cited by 215 · see citing works
Mitigating Unwanted Photophysical Processes for Improved Single-Molecule Fluorescence Imaging
Dave, R., Terry, D. S., Munro, J. B., & Blanchard, S. C. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.11.061 · Cited by 210 · see citing works
Self-citationBasis for prokaryotic specificity of action of aminoglycoside antibiotics
Recht, M. I., Douthwaite, S. R., & Puglisi, J. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.11.3133 · Cited by 201 · see citing works
Following movement of the L1 stalk between three functional states in single ribosomes
Cornish, P. V., Ermolenko, D. N., Staple, D. W., Hoang, L., Hickerson, R. P., Noller, H. F., & Ha, T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813180106 · Cited by 186 · see citing works
Peske, F., Savelsbergh, A., Katunin, V. I., Rodnina, M. V., & Wintermeyer, W. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.08.097 · Cited by 185 · see citing works
The structure of the eukaryotic ribosome at 3.0 A resolution.
Shem, A. B., de Loubresse, N. G., Melnikov, S. V., Jenner, L. B., Yusupova, G. Z., & Yusupov, M. (2011) · Worldwide Protein Data Bank · doi:10.2210/pdb4v88/pdb · Cited by 182 · see citing works
How the ribosome hands the A-site tRNA to the P site during EF-G–catalyzed translocation
Zhou, J., Lancaster, L., Donohue, J. P., & Noller, H. F. (2014) · Science · doi:10.1126/science.1255030 · Cited by 174 · see citing works
Afonine, P. V., Moriarty, N. W., Mustyakimov, M., Sobolev, O. V., Terwilliger, T. C., Türk, V., Urzhumtsev, A., & Adams, P. D. (2015) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004714028132 · Cited by 170 · see citing works
Structural rearrangements of the ribosome at the tRNA proofreading step
Jenner, L. B., Demeshkina, N., Yusupova, G. Z., & Yusupov, M. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1880 · Cited by 151 · see citing works
Agrawal, R. K., Sharma, M. R., Kiel, M. C., Hirokawa, G., Booth, T. M., Spahn, C. M. T., Grassucci, R. A., Kaji, A., & Frank, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401904101 · Cited by 147 · see citing works
Kaul, M., & Pilch, D. S. (2002) · Biochemistry · doi:10.1021/bi020130f · Cited by 144 · see citing works
Intersubunit movement is required for ribosomal translocation
Horan, L. H., & Noller, H. F. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700762104 · Cited by 141 · see citing works
Fei, J., Bronson, J. E., Hofman, J. M., Srinivas, R. L., Wiggins, C. H., & Gonzalez, R. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908077106 · Cited by 140 · see citing works
Allosteric control of the ribosome by small-molecule antibiotics
Wang, L., Pulk, A., Wasserman, M. R., Feldman, M. B., Altman, R. B., Cate, J. H. D., & Blanchard, S. C. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2360 · Cited by 136 · see citing works
Self-citationRotation of the head of the 30S ribosomal subunit during mRNA translocation
Guo, Z., & Noller, H. F. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218999109 · Cited by 127 · see citing works
Irreversible chemical steps control intersubunit dynamics during translation
Marshall, R. A., Dorywalska, M., & Puglisi, J. D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805299105 · Cited by 119 · see citing works
Structure and Dynamics of the Mammalian Ribosomal Pretranslocation Complex
Budkevich, T. V., Giesebrecht, J., Altman, R. B., Munro, J. B., Mielke, T., Nierhaus, K. H., Blanchard, S. C., & Spahn, C. M. T. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.040 · Cited by 115 · see citing works
Self-citationInhibition of ribosomal translocation by aminoglycoside antibiotics
Cabañas, M. J., Vázquez, D., & Modolell, J. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91493-6 · Cited by 114 · see citing works
Aminoglycoside activity observed on single pre-translocation ribosome complexes
Feldman, M. B., Terry, D. S., Altman, R. B., & Blanchard, S. C. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.274 · Cited by 109 · see citing works
Self-citationSystematic Chromosomal Deletion of Bacterial Ribosomal Protein Genes
Shoji, S., Dambacher, C. M., Shajani, Z., Williamson, J. R., & Schultz, P. G. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.09.004 · Cited by 109 · see citing works
Benveniste, R. Ė., & Davies, J. (1973) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.4.4.402 · Cited by 107 · see citing works
Misumi, M., Nishimura, T., Komai, T., & Tanaka, N. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)90178-x · Cited by 95 · see citing works
A ribosomal ambiguity mulation in the 530 loop ofE.coli16S rRNA
O'Connor, M., Göringer, H. U., & Dahiberg, A. E. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.16.4221 · Cited by 88 · see citing works
A fast dynamic mode of the EF‐G‐bound ribosome
Munro, J. B., Altman, R. B., Tung, C., Sanbonmatsu, K. Y., & Blanchard, S. C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.384 · Cited by 85 · see citing works
Self-citationAffinity purification of in vivo-assembled ribosomes for in vitro biochemical analysis
Youngman, E. M., & Green, R. (2005) · Methods · doi:10.1016/j.ymeth.2005.04.007 · Cited by 79 · see citing works
Green, K. D., Chen, W., Houghton, J. L., Fridman, M., & Garneau‐Tsodikova, S. (2009) · ChemBioChem · doi:10.1002/cbic.200900584 · Cited by 79 · see citing works
Self-citation4′-O-substitutions determine selectivity of aminoglycoside antibiotics
Perez‐Fernandez, D., Shcherbakov, D., Matt, T., Ng, C. L., Kudyba, I., Duscha, S., Boukari, H., Patak, R., Dubbaka, S. R., Lang, K., et al. (2014) · Nature Communications · doi:10.1038/ncomms4112 · Cited by 75 · see citing works
Hobbie, S. N., Pfister, P., Bruell, C. M., Sander, P., François, B., Westhof, É., & Böttger, E. C. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.50.4.1489-1496.2006 · Cited by 72 · see citing works
Stochastic Gating and Drug–Ribosome Interactions
Vaiana, A. C., & Sanbonmatsu, K. Y. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.12.035 · Cited by 68 · see citing works
Mutagenesis of 16S rRNA C1409-G1491 Base-pair Differentiates Between 6′OH and 6′NH3+ Aminoglycosides
Pfister, P., Hobbie, S. N., Bruell, C. M., Corti, N., Vasella, A. T., Westhof, É., & Böttger, E. C. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.11.073 · Cited by 65 · see citing works
Effects of Apramycin, a Novel Aminoglycoside Antibiotic on Bacterial Protein Synthesis
Perzyński, S., Cannon, M., Cundliffe, E., Chahwala, S. B., & DAVIES, J. E. (1979) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1979.tb13295.x · Cited by 56 · see citing works
Conformational Changes in the Ribosome Induced by Translational Miscoding Agents
Jerinic, O., & Joseph, S. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4269 · Cited by 52 · see citing works
Binding of aminoglycoside antibiotics to helix 69 of 23S rRNA
Scheunemann, A., Graham, W. D., Vendeix, F. A. P., & Agris, P. F. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp1253 · Cited by 49 · see citing works
Biddlecome, S., Haas, M. J., DAVIES, J. E., Miller, G. H., Rane, D. F., & Daniels, P. J. L. (1976) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.9.6.951 · Cited by 49 · see citing works
Definition of bases in 23S rRNA essential for ribosomal subunit association
Maiväli, Ü., & Rèmme, J. (2004) · RNA · doi:10.1261/rna.5220504 · Cited by 48 · see citing works
Watson, B. S., Hazlett, T. L., Eccleston, J. F., Davis, C. T., Jameson, D. M., & Johnson, A. E. (1995) · Biochemistry · doi:10.1021/bi00024a015 · Cited by 43 · see citing works
Insights into the molecular determinants of EF-G catalyzed translocation
Wang, L., Altman, R. B., & Blanchard, S. C. (2011) · RNA · doi:10.1261/rna.029033.111 · Cited by 35 · see citing works
Self-citationPathak, R., Böttger, E. C., & Vasella, A. T. (2005) · Helvetica Chimica Acta · doi:10.1002/hlca.200590240 · Cited by 19 · see citing works
Death rates of bacterial mutants
Jörgensen, F., & Kurland, C. G. (1987) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1987.tb01979.x · Cited by 13 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Mechanisms of resistance to aminoglycoside antibiotics: overview and perspectives
Garneau‐Tsodikova, S., & Labby, K. J. (2015) · MedChemComm · doi:10.1039/c5md00344j · Cited by 582 · see citing works
Self-citationA clock network for geodesy and fundamental science
Lisdat, C., Grosche, G., Quintin, N., Shi, C., Raupach, S. M. F., Grebing, C., Nicolodi, D., Stefani, F., Al-Masoudi, A., Dörscher, S., et al. (2016) · Nature Communications · doi:10.1038/ncomms12443 · Cited by 460 · see citing works
Single-molecule imaging of non-equilibrium molecular ensembles on the millisecond timescale
Juette, M. F., Terry, D. S., Wasserman, M. R., Altman, R. B., Zhou, Z., Zhao, H. C., & Blanchard, S. C. (2016) · Nature Methods · doi:10.1038/nmeth.3769 · Cited by 268 · see citing works
Self-citationStructure of the bacterial ribosome at 2 Å resolution
Watson, Z. L., Ward, F. R., Méheust, R., Ad, O., Schepartz, A., Banfield, J. F., & Cate, J. H. (2020) · eLife · doi:10.7554/elife.60482 · Cited by 263 · see citing works
Aminoglycoside interactions and impacts on the eukaryotic ribosome
Prokhorova, I., Altman, R. B., Djumagulov, M., Shrestha, J. P., Urzhumtsev, A., Ferguson, A., Chang, C. T., Yusupov, M., Blanchard, S. C., & Yusupova, G. Z. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1715501114 · Cited by 210 · see citing works
Self-citationHu, J., Quan, Y., Lai, Y., Zheng, Z., Hu, Z., Wang, X., Dai, T., Zhang, Q., & Cheng, Y. (2017) · Journal of Controlled Release · doi:10.1016/j.jconrel.2017.01.003 · Cited by 203 · see citing works
Wang, N., Luo, J., Deng, F., Huang, Y.-S., & Zhou, H. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.839808 · Cited by 156 · see citing works
Multiperspective smFRET reveals rate-determining late intermediates of ribosomal translocation
Wasserman, M. R., Alejo, J. L. P., Altman, R. B., & Blanchard, S. C. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3177 · Cited by 117 · see citing works
Self-citationtRNA Translocation by the Eukaryotic 80S Ribosome and the Impact of GTP Hydrolysis
Flis, J., Holm, M., Rundlet, E. J., Loerke, J., Hilal, T., Dabrowski, M., Bürger, J., Mielke, T., Blanchard, S. C., Spahn, C. M. T., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.11.040 · Cited by 95 · see citing works
Self-citationAtomic resolution snapshot of Leishmania ribosome inhibition by the aminoglycoside paromomycin
Shalev-Benami, M., Zhang, Y., Rozenberg, H., Nobe, Y., Taoka, M., Matzov, D., Zimmerman, E., Bashan, A., Isobe, T., Jaffe, C. L., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01664-4 · Cited by 94 · see citing works
Destination of aminoglycoside antibiotics in the ‘post-antibiotic era’
Takahashi, Y., & Igarashi, M. (2017) · The Journal of Antibiotics · doi:10.1038/ja.2017.117 · Cited by 90 · see citing works
Structural basis of early translocation events on the ribosome
Rundlet, E. J., Holm, M., Schacherl, M., Natchiar, S. K., Altman, R. B., Spahn, C. M. T., Myasnikov, A. G., & Blanchard, S. C. (2021) · Nature · doi:10.1038/s41586-021-03713-x · Cited by 89 · see citing works
Self-citationWachino, J.-I., Doi, Y., & Arakawa, Y. (2020) · Infectious Disease Clinics of North America · doi:10.1016/j.idc.2020.06.002 · Cited by 82 · see citing works
Translation error clusters induced by aminoglycoside antibiotics
Wohlgemuth, I., Garofalo, R., Samatova, E., Günenç, A. N., Lenz, C., Urlaub, H., & Rodnina, M. V. (2021) · Nature Communications · doi:10.1038/s41467-021-21942-6 · Cited by 82 · see citing works
Chandrika, N. T., & Garneau‐Tsodikova, S. (2018) · Chemical Society Reviews · doi:10.1039/c7cs00407a · Cited by 73 · see citing works
Self-citationGxalo, O., Digban, T. O., Igere, B. E., Olapade, O. A., Okoh, A. I., & Nwodo, U. U. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.732001 · Cited by 66 · see citing works
A photo-cleavable polyprodrug-loaded wound dressing with UV-responsive antibacterial property
Pang, Q., Zheng, X., Luo, Y., Ma, L., & Gao, C. (2017) · Journal of Materials Chemistry B · doi:10.1039/c7tb01696d · Cited by 60 · see citing works
A review of patents (2011–2015) towards combating resistance to and toxicity of aminoglycosides
Chandrika, N. T., & Garneau‐Tsodikova, S. (2015) · MedChemComm · doi:10.1039/c5md00453e · Cited by 54 · see citing works
Self-citationZanon-Willette, T., Lefèvre, R., Metzdorff, R., Sillitoe, N., Almonacil, S., Minissale, M., de Clercq, E., Тайченачев, А. В., Yudin, V. I., & Arimondo, E. (2018) · Reports on Progress in Physics · doi:10.1088/1361-6633/aac9e9 · Cited by 54 · see citing works
A simple approach to fabricate the rose petal-like hierarchical surfaces for droplet transportation
Yuan, C., Huang, M., Yu, X., Ma, Y., & Luo, X. (2016) · Applied Surface Science · doi:10.1016/j.apsusc.2016.05.128 · Cited by 40 · see citing works
Real-time measurements of aminoglycoside effects on protein synthesis in live cells
Rivera, J. A., Larsson, J., Volkov, I. L., Seefeldt, A. C., Sanyal, S., & Johansson, M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2013315118 · Cited by 38 · see citing works
Structure of Pseudomonas aeruginosa ribosomes from an aminoglycoside-resistant clinical isolate
Halfon, Y., Jiménez‐Fernández, A., Rosa, R. L., Espinosa, R., Johansen, H. K., Matzov, D., Eyal, Z., Bashan, A., Zimmerman, E., Belousoff, M. J., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1909831116 · Cited by 37 · see citing works
Sati, G. C., Sarpe, V. A., Furukawa, T., Mondal, S., Mantovani, M., Hobbie, S. N., Vasella, A. T., Böttger, E. C., & Crich, D. (2019) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.9b00128 · Cited by 36 · see citing works
Identifying targets to prevent aminoglycoside ototoxicity
Kim, J., Hemachandran, S., Cheng, A. G.-L., & Ricci, A. J. (2022) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2022.103722 · Cited by 34 · see citing works
Probe light-shift elimination in generalized hyper-Ramsey quantum clocks
Zanon-Willette, T., de Clercq, E., & Arimondo, E. (2016) · Physical Review A · doi:10.1103/physreva.93.042506 · Cited by 32 · see citing works
Miscoding-induced stalling of substrate translocation on the bacterial ribosome
Alejo, J. L., & Blanchard, S. C. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707539114 · Cited by 32 · see citing works
Self-citationZhang, R., Huang, X., Wu, Q., Chu, S., Bai, X., Zhou, Y., You, J., Yang, C., & Tan, H. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.130172 · Cited by 29 · see citing works
Inhibitors of Eukaryotic Translational Machinery as Therapeutic Agents
Fan, A. P., & Sharp, P. P. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01746 · Cited by 29 · see citing works
Yu, Y., Li, H., Wang, Y., Zhang, Z., Liao, M., Rong, X., Li, B., Wang, C., Ge, J., & Zhang, X. (2022) · Marine Pollution Bulletin · doi:10.1016/j.marpolbul.2022.114219 · Cited by 29 · see citing works
Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome
Seely, S. M., Parajuli, N. P., Tarafder, A. D., Ge, X., Sanyal, S., & Gagnon, M. G. (2023) · Nature Communications · doi:10.1038/s41467-023-40416-5 · Cited by 28 · see citing works
Chemical Modifications Reduce Auditory Cell Damage Induced by Aminoglycoside Antibiotics
Zada, S. L., Baruch, B. B., Simhaev, L., Engel, H., & Fridman, M. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b12420 · Cited by 28 · see citing works
Mechanistic insights into translation inhibition by aminoglycoside antibiotic arbekacin
Parajuli, N. P., Mandava, C. S., Pavlov, M. Y., & Sanyal, S. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab495 · Cited by 20 · see citing works
Zanon-Willette, T., Lefèvre, R., Taǐchenachev, A. V., & Yudin, V. I. (2017) · Physical Review A · doi:10.1103/physreva.96.023408 · Cited by 18 · see citing works
Chemical probing for examining the structure of modified RNAs and ligand binding to RNA
Waduge, P., Sakakibara, Y., & Chow, C. S. (2018) · Methods · doi:10.1016/j.ymeth.2018.10.015 · Cited by 18 · see citing works
Pellegrino, S., Terrosu, S., Yusupova, G. Z., & Yusupov, M. (2021) · Cancers · doi:10.3390/cancers13174392 · Cited by 18 · see citing works
Sati, G. C., Shcherbakov, D., Hobbie, S. N., Vasella, A. T., Böttger, E. C., & Crich, D. (2017) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.6b00214 · Cited by 17 · see citing works
Optical Atomic Clocks for Redefining SI Units of Time and Frequency
Sharma, L., Rathore, H. K., Utreja, S., Neelam, N., Roy, A., De, S., & Panja, S. (2020) · MAPAN · doi:10.1007/s12647-020-00397-y · Cited by 16 · see citing works
Perturbation of ribosomal subunit dynamics by inhibitors of tRNA translocation
Belardinelli, R., Sharma, H., Peske, F., & Rodnina, M. V. (2021) · RNA · doi:10.1261/rna.078758.121 · Cited by 16 · see citing works
Interactions of aminoglycoside antibiotics with rRNA
Trylska, J., & Kulik, M. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160087 · Cited by 16 · see citing works
Zhao, Y., Wu, J., Wei, C., Li, L., Liang, F., Man, Y., Zhang, H., Han, L., Fang, H., Zheng, Y., et al. (2026) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2026.141062 · Cited by 14 · see citing works
Nishima, W., Girodat, D. J., Holm, M., Rundlet, E. J., Alejo, J. L., Fischer, K., Blanchard, S. C., & Sanbonmatsu, K. Y. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac597 · Cited by 14 · see citing works
Self-citationGirodat, D. J., Wieden, H., Blanchard, S. C., & Sanbonmatsu, K. Y. (2023) · Nature Communications · doi:10.1038/s41467-023-40404-9 · Cited by 13 · see citing works
Self-citationA Single Folded Beam Magneto-Optical Trap System for Neutral Mercury Atoms
Liu, K., Zhao, R.-C., Gou, W., Fu, X., Liu, H., Yin, S.-Q., Sun, J., Xu, Z., & Wang, Y. (2016) · Chinese Physics Letters · doi:10.1088/0256-307x/33/7/070602 · Cited by 12 · see citing works
Morphological Entanglement in Living Systems
Day, T. C., Zamani-Dahaj, S. A., Bozdag, G. O., Burnetti, A., Bingham, E. P., Conlin, P. L., Ratcliff, W. C., & Yunker, P. J. (2024) · Physical Review X · doi:10.1103/physrevx.14.011008 · Cited by 11 · see citing works
Santos, M. H. C., Santos, V. F., Freitas, P. R., Silva, R. R. D. S., Roma, R. R., Santos, A. L. E., Ribeiro, D. A., Coutinho, H. D. M., Rocha, B. A. M., Oliveira, M. M. E., et al. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.123941 · Cited by 11 · see citing works
Yuce, M., Ates, B., Yasar, N. İ., Sungur, F. A., & Kürkçüoğlu, Ö. (2024) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2024.108817 · Cited by 10 · see citing works
Mechanism of read-through enhancement by aminoglycosides and mefloquine
Kolosova, O., Zgadzay, Y., Stetsenko, A., Sukhinina, A. P., Atamas, A., Validov, S. Z., Rogachev, A. V., Usachev, K. S., Jenner, L. B., Dmitriev, S. E., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2420261122 · Cited by 9 · see citing works
Dastidar, N. G., Freyer, N. S., Petrychenko, V., Schwarzer, A. C. D. A. P., Peng, B., Samatova, E., Kothe, C., Schmidt, M., Peske, F., Politi, A. Z., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65298-7 · Cited by 8 · see citing works
Parajuli, N. P., Emmerich, A., Mandava, C. S., Pavlov, M. Y., & Sanyal, S. (2023) · Nature Communications · doi:10.1038/s41467-023-36528-7 · Cited by 8 · see citing works
Huang, S., Zhu, X., & Melançon, C. E. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00779 · Cited by 8 · see citing works
Human ribosomes interactions reveal the binding landscape of neomycinPreprint
Wu, M., Zhu, L., Wu, M., Jia, C., Zhang, X., Zhao, Z., Liu, H., Yi, C., Sun, S., Liu, K., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.22.666027 · Cited by 8 · see citing works
Casy, W., Prater, A. R., & Cornish, P. V. (2018) · Biochemistry · doi:10.1021/acs.biochem.7b00824 · Cited by 7 · see citing works
Preparation of ribosomes for smFRET studies: A simplified approach
Shebl, B., Menke, D. E., Pennella, M., Poudyal, R. R., Burke, D. H., & Cornish, P. V. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.05.010 · Cited by 6 · see citing works
Vinal, K., & Conn, G. L. (2017) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00077-17 · Cited by 6 · see citing works
A fitness landscape instability governs the morphological diversity of tip-growing cells
Ohairwe, M. E., Živanović, B. D., & Rojas, E. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113961 · Cited by 6 · see citing works
Engineering of Streptoalloteichus tenebrarius 2444 for Sustainable Production of Tobramycin
Mitousis, L., Maier, H., Martinovic, L., Kulik, A., Stockert, S., Wohlleben, W., Stiefel, A., & Musiol-Kroll, E. M. (2021) · Molecules · doi:10.3390/molecules26144343 · Cited by 6 · see citing works
Majumdar, S., Parajuli, N. P., Ge, X., & Sanyal, S. (2025) · Scientific Reports · doi:10.1038/s41598-025-02391-3 · Cited by 4 · see citing works
Feng, Y., Jiang, Y., Chen, X., Zhu, L., Xue, H., Wu, M., Yang, L., Yu, H., & Lin, J. (2024) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-024-13141-2 · Cited by 4 · see citing works
Meng, F., Zhou, X., Hou, Y., Zhao, H., Zhang, J., Huang, Q. B., Zhang, M., Adams, E., Yuan, Y., & Shi, H. C. (2024) · Talanta · doi:10.1016/j.talanta.2024.126359 · Cited by 3 · see citing works
Jawad, S. S., & Al-Azawi, I. H. (2024) · Medical Journal of Babylon · doi:10.4103/mjbl.mjbl_694_23 · Cited by 3 · see citing works
Pirrone, M. G., Hobbie, S. N., Vasella, A. T., Böttger, E. C., & Crich, D. (2021) · RSC Medicinal Chemistry · doi:10.1039/d1md00214g · Cited by 3 · see citing works
Senelle, G., Guyeux, C., Refrégier, G., & Sola, C. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.12.526393 · Cited by 3 · see citing works
Structural basis for hygromycin B inhibition of yeast pseudouridine-deficient ribosomes
Zhao, Y., Xu, C., Chen, X., Jin, H., & Li, H. (2025) · Science Advances · doi:10.1126/sciadv.adu0151 · Cited by 1 · see citing works
Plat: A Web Based Protein Local Alignment Tool
Jaegle, S. (2017) · doi:10.23860/thesis-jaegle-stephen-2017 · Cited by 1 · see citing works
Mesa, P., Jiménez‐Fernández, A., Rosa, R. L., Espinosa, R., Johansen, H. K., Molin, S., & Montoya, G. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.13.544509 · Cited by 1 · see citing works
Synthetic Receptors for RNA Recognition
Bhaduri, S., Spano, M. N., & Arya, D. P. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12550-8
Zero ac Stark frequency shift of an atom trapped in pulsed laser light*
Afanasiev, A. E., & Balykin, V. I. (2021) · Quantum Electronics · doi:10.1070/qel17500
Analysis of translational fidelity in cellular proteins
Garofalo, R. (2019) · doi:10.53846/goediss-7371
Kovalevsky, A. Y., & Armbruster, E. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734549733.793557363
Ribosome inhibition : cryo-EM and advancements in X-ray crystallography
Kolosova, O. A. (2023) · theses.fr (ABES) · doi:10.70675/fac7636bz91a9z4dbazb803z20817e06b018
Antitumor effect of the AP5Z1 small-molecule inhibitor PGG in hepatocellular carcinoma
Quan, Z., Hu, Q., Liu, M. R., Ma, G., He, Z., Liu, Y., Wei, Y., Wei, Y., Zheng, X., Qin, C., et al. (2026) · Medical Oncology · doi:10.1007/s12032-026-03322-6
Wan, K., Ling, X., & Tan, L. (2026) · Inorganica Chimica Acta · doi:10.1016/j.ica.2026.123412
BindingDB Entry 50018392: Inhibitors of Eukaryotic Translational Machinery as Therapeutic Agents.
BindingDB (2024) · UC San Diego · doi:10.7270/q2t43z96
- Authors
- Wasserman, M. R., Pulk, A., Zhou, Z., Altman, R. B., Zinder, J. C., Green, K. D., Garneau-Tsodikova, S., Doudna Cate, J. H., & Blanchard, S. C.
- Affiliations
- Weill Cornell Medicine (US)
- University of California, Berkeley (US)
- Memorial Sloan Kettering Cancer Center (US)
- University of Kentucky (US)
- Corresponding author
- Blanchard, Scott C.
- Venue
- Nature Communications
- Published
- 2015-07-30
- Volume
- 6
- Issue
- 1
- Pages
- 7896-7896
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC4522699
- OpenAlex
- W2202200434
- Cited by
- 77
- References
- 72
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 7 · 2023: 8 · 2022: 4 · 2021: 11 · 2020: 5 · 2019: 4 · 2018: 5 · 2017: 12 · 2016: 9 · 2015: 3
- FWCI
- 4.20
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- UKnowledge (University of Kentucky) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- National Science Foundation
- U.S. Department of Energy (DEAC03-76SF00098)
- Wayne State University
- University of Missouri
- Johns Hopkins University
- University of Missouri-Kansas City
- National Institutes of Health (CA92584)
- National Cancer Institute (CA92584, P01CA092584)
- National Institute on Deafness and Other Communication Disorders (F31DC012026)
- National Institute of General Medical Sciences (R01GM079238, 1R01GM65050, R01GM105404, R01GM065050, R01GM098859)
- National Institute of Allergy and Infectious Diseases (R01AI090048)
- Lawrence Berkeley National Laboratory
- 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
- aminoglycosides, ribosome, neomycin, paromomycin, ribostamycin, neamine, crystal structure, net positive charge, translational regulation
- MeSH terms
- Aminoglycosides, Anti-Bacterial Agents, Binding Sites, Escherichia coli, Framycetin, Neomycin, Paromomycin, Ribosomes, Ribostamycin, RNA, Bacterial, Rotation, Escherichia coli Proteins, Ribosome Subunits, Small, Bacterial, Ribosome Subunits, Large, Bacterial
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