The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Sequence selectivity of macrolide-induced translational attenuation
Open accessAbstract
Significance: By globally mapping the position of stalled ribosomes in macrolide-treated Staphylococcus aureus , we identified the proteins whose synthesis is affected by this antibiotic. Rather than acting as a nonselective inhibitor, the binding of macrolides to the ribosome tunnel only induces stalling at a few unique sites that are enriched in proline and charged residues. The sequences that flank the stalling sites are highly variable but are essential for efficient stalling. Although it has long been assumed that macrolides inhibit translation after the synthesis of a few residues, we found that stalling could occur at any point during translation. Our results reveal a striking conservation of stalling motifs among all known arrest peptides that strongly suggests a universal ribosome stalling mechanism.
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.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Recent studies on NPET binding translation inhibitors like macrolides and Tetracenomycin X have established that the sequence of the nascent peptide plays a crucial role in the binding affinity and efficacy of these inhibitors14,26,27.”
From Dual site targeting of the bacterial 70S ribosome by tetracyclines (2026) · cites this paper as [26]
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.
Citations
Cites
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
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
The world of subinhibitory antibiotic concentrations
DAVIES, J. E., Spiegelman, G. B., & Yim, G. (2006) · Current Opinion in Microbiology · doi:10.1016/j.mib.2006.08.006 · Cited by 740
Brandman, O., Stewart-Ornstein, J., Wong, D., Larson, A. G., Williams, C. C., Li, G., Zhou, S., King, D., Shen, P. S., Weibezahn, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.044 · Cited by 650
The anti-Shine–Dalgarno sequence drives translational pausing and codon choice in bacteria
Li, G., Oh, E., & Weissman, J. S. (2012) · Nature · doi:10.1038/nature10965 · Cited by 644
eIF5A Promotes Translation of Polyproline Motifs
Gutierrez, E., Shin, B., Woolstenhulme, C. J., Kim, J.-R., Saini, P., Buskirk, A. R., & Dever, T. E. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.021 · Cited by 544
The Ribosomal Exit Tunnel Functions as a Discriminating Gate
Nakatogawa, H., & Ito, K. (2002) · Cell · doi:10.1016/s0092-8674(02)00649-9 · Cited by 533
EF-P Is Essential for Rapid Synthesis of Proteins Containing Consecutive Proline Residues
Doerfel, L. K., Wohlgemuth, I., Kothe, C., Peske, F., Urlaub, H., & Rodnina, M. V. (2012) · Science · doi:10.1126/science.1229017 · Cited by 490
Selective Ribosome Profiling Reveals the Cotranslational Chaperone Action of Trigger Factor In Vivo
Oh, E., Becker, A. H., Sandikci, A., Huber, D., Chaba, R., Gloge, F., Nichols, R. J., Typas, A., Gross, C. A., Krämer, G., et al. (2011) · Cell · doi:10.1016/j.cell.2011.10.044 · Cited by 468
Tenson, T., Lovmar, M., & Ehrenberg, M. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00662-4 · Cited by 461
Cited by
Sorted by citations
Ribosome profiling reveals the what, when, where and how of protein synthesis
Brar, G. A., & Weissman, J. S. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4069 · Cited by 559
The macrolide antibiotic renaissance
Dinos, G. P. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13936 · Cited by 512
How Macrolide Antibiotics Work
Vázquez‐Laslop, N., & Mankin, A. S. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.06.011 · Cited by 460
Lin, J., Zhou, D., Steitz, T. A., Polikanov, Y. S., & Gagnon, M. G. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-011942 · Cited by 414
Genome-wide Survey of Ribosome Collision
Han, P., Shichino, Y., Schneider‐Poetsch, T., Mito, M., Hashimoto, S., Udagawa, T., Kohno, K., Yoshida, M., Mishima, Y., Inada, T., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107610 · Cited by 183
Proline Metabolism in Tumor Growth and Metastatic Progression
D’Aniello, C., Patriarca, E. J., Phang, J. M., & Minchiotti, G. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00776 · Cited by 172
Marks, J., Kannan, K., Roncase, E. J., Klepacki, D., Kefi, A., Orelle, C., Vázquez-Laslop, N., & Mankin, A. S. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613055113 · Cited by 159
Translation regulation via nascent polypeptide-mediated ribosome stalling
Wilson, D. N., Arenz, S., & Beckmann, R. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.01.008 · Cited by 158
Flourishing Antibacterial Strategies for Osteomyelitis Therapy
Wang, X., Zhang, M., Zhu, T., Wei, Q., Liu, G., & Ding, J. (2023) · Advanced Science · doi:10.1002/advs.202206154 · Cited by 132
How Streptococcus suis escapes antibiotic treatments
Uruén, C., García, C., Fraile, L. J., Tommassen, J., & Arenas, J. (2022) · Veterinary Research · doi:10.1186/s13567-022-01111-3 · Cited by 116
Ribosome protection by antibiotic resistance ATP-binding cassette protein
Su, W., Kumar, V., Ding, Y., Ero, R., Serra, A., Lee, B. S. T., Wong, A. S. W., Shi, J. R., Sze, S. K., Yang, L., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1803313115 · Cited by 104
Structural and mechanistic basis for translation inhibition by macrolide and ketolide antibiotics
Beckert, B., Leroy, E., Sothiselvam, S., Bock, L. V., Svetlov, M. S., Graf, M., Arenz, S., Abdelshahid, M., Seip, B., Grubmüller, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24674-9 · Cited by 100
Differences in the path to exit the ribosome across the three domains of life
Duc, K. D., Batra, S. S., Bhattacharya, N., Cate, J. H. D., & Song, Y. S. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz106 · Cited by 90
Clauwaert, J., Menschaert, G., & Waegeman, W. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz061 · Cited by 90
The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus
Matzov, D., Aibara, S., Basu, A., Zimmerman, E., Bashan, A., Yap, M.-N. F., Amunts, A., & Yonath, A. (2017) · Nature Communications · doi:10.1038/s41467-017-00753-8 · Cited by 85
Self-citationContext-Specific Action of Ribosomal Antibiotics
Vázquez‐Laslop, N., & Mankin, A. S. (2018) · Annual Review of Microbiology · doi:10.1146/annurev-micro-090817-062329 · Cited by 87
Basu, A., & Yap, M.-N. F. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1709588114 · Cited by 70
Self-citationRibosome hibernation factor promotesStaphylococcalsurvival and differentially represses translation
Basu, A., & Yap, M.-N. F. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw180 · Cited by 77
Self-citationMichel, A. M., Kiniry, S. J., O’Connor, P. B. F., Mullan, J. P. A., & Baranov, P. V. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx790 · Cited by 70
Kinetics of drug–ribosome interactions defines the cidality of macrolide antibiotics
Svetlov, M. S., Vázquez‐Laslop, N., & Mankin, A. S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1717168115 · Cited by 73
Survival of the drowsiest: the hibernating 100S ribosome in bacterial stress management
Gohara, D. W., & Yap, M.-N. F. (2017) · Current Genetics · doi:10.1007/s00294-017-0796-2 · Cited by 74
Self-citationArenz, S., & Wilson, D. N. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.10.019 · Cited by 67
Klebsazolicin inhibits 70S ribosome by obstructing the peptide exit tunnel
Metelev, M., Osterman, I. А., Ghilarov, D., Khabibullina, N. F., Yakimov, A. P., Shabalin, K. A., Utkina, I., Travin, D. Y., Komarova, E. S., Serebryakova, M. V., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2462 · Cited by 63
Identification of Unannotated Small Genes in Salmonella
Baek, J., Lee, J., Yoon, K., & Lee, H.-W. (2017) · G3 Genes Genomes Genetics · doi:10.1534/g3.116.036939 · Cited by 67
Understanding the evolution of macrolides resistance: A mini review
Amdan, N. A. N., Shahrulzamri, N. A., Hashim, R., & Jamil, N. M. (2024) · Journal of Global Antimicrobial Resistance · doi:10.1016/j.jgar.2024.07.016 · Cited by 65
The regulon of the RNA chaperone CspA and its auto-regulation in Staphylococcus aureus
Caballero, C. J., Menendez-Gil, P., Catalan‐Moreno, A., Vergara-Irigaray, M., García, B., Segura, V., Irurzun, N., Villanueva, M., Mozos, I. R. D. L., Solano, C., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1284 · Cited by 57
Dzyubak, E., & Yap, M.-N. F. (2016) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01806-16 · Cited by 61
Self-citationThe Role of Proteomics in Bacterial Response to Antibiotics
Tsakou, F., Jersie-Christensen, R., Jenssen, H., & Mojsoska, B. (2020) · Pharmaceuticals · doi:10.3390/ph13090214 · Cited by 60
Assessment of Bona Fide sRNAs in Staphylococcus aureus
Liu, W., Rochat, T., Toffano‐Nioche, C., Lam, T. N. L., Bouloc, P., & Morvan, C. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00228 · Cited by 66
Evolving medicinal chemistry strategies in antibiotic discovery
Pawlowski, A. C., Johnson, J. W., & Wright, G. D. (2016) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2016.04.006 · Cited by 53
Dalhoff, A. (2020) · Infection · doi:10.1007/s15010-020-01536-y · Cited by 60
Garai, P., & Blanc‐Potard, A. (2020) · Molecular Microbiology · doi:10.1111/mmi.14564 · Cited by 51
Nascent peptide assists the ribosome in recognizing chemically distinct small molecules
Gupta, P., Liu, B., Klepacki, D., Gupta, V., Schulten, K. J., Mankin, A. S., & Vázquez‐Laslop, N. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.1998 · Cited by 49
Sothiselvam, S., Neuner, S., Rigger, L., Klepacki, D., Micura, R., Vázquez‐Laslop, N., & Mankin, A. S. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.018 · Cited by 48
Bacterial Small Membrane Proteins: the Swiss Army Knife of Regulators at the Lipid Bilayer
Yadavalli, S. S., & Yuan, J. (2021) · Journal of Bacteriology · doi:10.1128/jb.00344-21 · Cited by 49
Regulation of antibiotic-resistance by non-coding RNAs in bacteria
Dar, D., & Sorek, R. (2017) · Current Opinion in Microbiology · doi:10.1016/j.mib.2017.02.005 · Cited by 47
How Widespread is Metabolite Sensing by Ribosome-Arresting Nascent Peptides?
Seip, B., & Innis, C. A. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.04.019 · Cited by 49
Obana, N., Takada, H., Crowe-McAuliffe, C., Iwamoto, M., Egorov, A. A., Wu, K. J. Y., Chiba, S., Murina, V., Paternoga, H., Tresco, B. I. C., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad193 · Cited by 42
Almutairi, M. M., Svetlov, M. S., Hansen, D. A., Khabibullina, N. F., Klepacki, D., Kang, H., Sherman, D. H., Vázquez‐Laslop, N., Polikanov, Y. S., & Mankin, A. S. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx673 · Cited by 41
A Bright Future for Antibiotics?
Matzov, D., Bashan, A., & Yonath, A. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044617 · Cited by 41
da Cunha, B. R., Fonseca, L. P., & Calado, C. R. C. (2020) · Metabolites · doi:10.3390/metabo10040145 · Cited by 40
Deng, K., Li, C., Huang, H., & Li, X. (2016) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2016.09.107 · Cited by 39
Context-specific action of macrolide antibiotics on the eukaryotic ribosome
Svetlov, M. S., Koller, T. O., Meydan, S., Shankar, V. G., Klepacki, D., Polacek, N., Guydosh, N. R., Vázquez‐Laslop, N., Wilson, D. N., & Mankin, A. S. (2021) · Nature Communications · doi:10.1038/s41467-021-23068-1 · Cited by 38
Macrolones target bacterial ribosomes and DNA gyrase and can evade resistance mechanisms
Aleksandrova, E. V., Ma, C.-X., Klepacki, D., Alizadeh, F., Vázquez‐Laslop, N., Liang, J., Polikanov, Y. S., & Mankin, A. S. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01685-3 · Cited by 37
Takada, H., Mandell, Z. F., Yakhnin, H., Glazyrina, A., Chiba, S., Kurata, T., Wu, K. J. Y., Tresco, B. I. C., Myers, A. G., Atkinson, G. C., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac497 · Cited by 36
Lipońska, A., & Yap, M.-N. F. (2021) · mBio · doi:10.1128/mbio.00334-21 · Cited by 34
Self-citationAlmutairi, M. M., Park, S. R., Rose, S., Hansen, D. A., Vázquez‐Laslop, N., Douthwaite, S. R., Sherman, D. H., & Mankin, A. S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512090112 · Cited by 32
Yakhnin, H., Yakhnin, A. V., Mouery, B. L., Mandell, Z. F., Karbasiafshar, C., Kashlev, M., & Babitzke, P. (2019) · mBio · doi:10.1128/mbio.02665-19 · Cited by 31
Conserved heterodimeric GTPase Rbg1/Tma46 promotes efficient translation in eukaryotic cells
Zeng, F., Li, X., Pires-Alves, M., Chen, X., Hawk, C. W., & Jin, H. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109877 · Cited by 30
da Cunha, B. R., Fonseca, L. P., & Calado, C. R. C. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11102-7 · Cited by 30
Zhang, Y., Aleksashin, N. A., Klepacki, D., Anderson, C. M., Vázquez‐Laslop, N., Gross, C. A., & Mankin, A. S. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2118553119 · Cited by 28
Atlas of mRNA translation and decay for bacteria
Huch, S., Nersisyan, L., Ropat, M., Barrett, D., Wu, M., Wang, J., Valeriano, V. D., Vardazaryan, N., Huerta‐Cepas, J., Wu, W., et al. (2023) · Nature Microbiology · doi:10.1038/s41564-023-01393-z · Cited by 28
The Ribosomal Protein uL22 Modulates the Shape of the Protein Exit Tunnel
Wekselman, I., Zimmerman, E., Davidovich, C., Belousoff, M. J., Matzov, D., Krupkin, M., Rozenberg, H., Bashan, A., Friedlander, G., Kjeldgaard, J. S., et al. (2017) · Structure · doi:10.1016/j.str.2017.06.004 · Cited by 31
Binding and Action of Triphenylphosphonium Analog of Chloramphenicol upon the Bacterial Ribosome
Chen, C., Pavlova, J. A., Lukianov, D. A., Tereshchenkov, A. G., Makarov, G. I., Khairullina, Z. Z., Tashlitsky, V. N., Paleskava, A., Konevega, A. L., Bogdanov, A. A., et al. (2021) · Antibiotics · doi:10.3390/antibiotics10040390 · Cited by 27
Streptococcus suis: Epidemiology and resistance evolution of an emerging zoonotic bacteria
Liu, F., Zhang, S., Erdeljan, M., Zhang, Y., Chen, D., Li, J., Ding, L., Zhang, L., Sun, W., Yu, J., et al. (2025) · One Health · doi:10.1016/j.onehlt.2025.101098 · Cited by 28
Thermal and Nutritional Regulation of Ribosome Hibernation in Staphylococcus aureus
Basu, A., Shields, K. E., Eickhoff, C. S., Hoft, D. F., & Yap, M.-N. F. (2018) · Journal of Bacteriology · doi:10.1128/jb.00426-18 · Cited by 26
Self-citationBasu, A., Shields, K. E., & Yap, M.-N. F. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012307 · Cited by 30
Self-citationYakhnin, A. V., Kashlev, M., & Babitzke, P. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1828261 · Cited by 24
Tetracenomycin X sequesters peptidyl-tRNA during translation of QK motifs
Leroy, E. C., Perry, T. N., Renault, T. T., & Innis, C. A. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01343-0 · Cited by 22
Ribosome Hibernation as a Stress Response of Bacteria
Wang, T., Liang, C., Zheng, M., Liu, L., An, Y., Xu, H., Xiao, S., & Nie, L. (2020) · Protein and Peptide Letters · doi:10.2174/0929866527666200610142118 · Cited by 20
Ribosomal stalling landscapes revealed by high-throughput inverse toeprinting of mRNA libraries
Seip, B., Sacheau, G., Dupuy, D., & Innis, C. A. (2018) · Life Science Alliance · doi:10.26508/lsa.201800148 · Cited by 19
The kinetic mechanism of bacterial ribosome recycling
Chen, Y., Kaji, A., Kaji, H. K., & Cooperman, B. S. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx694 · Cited by 18
Shields, K. E., Ranava, D., Tan, Y., Zhang, D., & Yap, M.-N. F. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1011968 · Cited by 16
Self-citationDomon, H., Maekawa, T., Yonezawa, D., Nagai, K., Oda, M., Yanagihara, K., & Terao, Y. (2018) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00161-18 · Cited by 17
Mechanism of translation inhibition by type II GNAT toxin AtaT2
Ovchinnikov, S. V., Bikmetov, D., Livenskyi, A., Serebryakova, M. V., Wilcox, B., Mangano, K., Shiriaev, D. I., Osterman, I. А., Владимирович, С. П., Borukhov, S. I., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa551 · Cited by 17
Context-based sensing of orthosomycin antibiotics by the translating ribosome
Mangano, K., Marks, J., Klepacki, D., Saha, C. K., Atkinson, G. C., Vázquez‐Laslop, N., & Mankin, A. S. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01138-9 · Cited by 16
Chiba, S., Fujiwara, K., Chadani, Y., & Taguchi, H. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad007 · Cited by 16
Activity-Based DNA-Encoded Library Screening for Selective Inhibitors of Eukaryotic Translation
Barhoosh, H., Dixit, A., Cochrane, W. G., Cavett, V. J., Prince, R. N., Blair, B. O., Ward, F. R., McClure, K. F., Patten, P. A., Paulick, M. G., et al. (2024) · ACS Central Science · doi:10.1021/acscentsci.4c01218 · Cited by 16
Macrolide resistance through uL4 and uL22 ribosomal mutations in Pseudomonas aeruginosa
Goltermann, L., Laborda, P., Irazoqui, O., Pogrebnyakov, I., Bendixen, M. P., Molin, S., Johansen, H. K., & Rosa, R. L. (2024) · Nature Communications · doi:10.1038/s41467-024-53329-8 · Cited by 16
The Role of Lower Airway Dysbiosis in Asthma: Dysbiosis and Asthma
Lu, J., Xiong, L., Zhang, X., Liu, Z., Wang, S., Zhang, C., Zheng, J., Wang, G., Zheng, R., Simpson, J. L., et al. (2017) · Mediators of Inflammation · doi:10.1155/2017/3890601 · Cited by 17
Shirokikh, N. E. (2021) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2021.2006599 · Cited by 14
Evguenieva‐Hackenberg, E. (2021) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1696 · Cited by 15
Konikkat, S., Scribner, M. R., Eutsey, R. A., Hiller, N. L., Cooper, V. S., & McManus, C. J. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009634 · Cited by 15
Tracking of single tRNAs for translation kinetics measurements in chloramphenicol treated bacteria
Volkov, I. L., Seefeldt, A. C., & Johansson, M. (2019) · Methods · doi:10.1016/j.ymeth.2019.02.004 · Cited by 14
The ribosome as a small-molecule sensor
Bhattacharya, A., Renault, T. T., & Innis, C. A. (2023) · Current Opinion in Microbiology · doi:10.1016/j.mib.2023.102418 · Cited by 13
Compounds for selective translational inhibition
Shichino, Y., & Iwasaki, S. (2022) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2022.102158 · Cited by 11
Nguyen, H. L., Pham, D. L., O’Brien, E. P., & Li, M. S. (2018) · Scientific Reports · doi:10.1038/s41598-018-24344-9 · Cited by 12
Toward the rational design of macrolide antibiotics to combat resistance
Pavlova, À., Parks, J. M., Oyelere, A. K., & Gumbart, J. C. (2017) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13004 · Cited by 12
Malainer, C., Schachner, D., Sangiovanni, E., Atanasov, A. G., Schwaiger, S., Stuppner, H., Heiß, E. H., & Dirsch, V. M. (2017) · Journal of Natural Products · doi:10.1021/acs.jnatprod.7b00503 · Cited by 11
Ranava, D., Scheidler, C. M., Pfanzelt, M., Fiedler, M. K., Sieber, S. A., Schneider, S., & Yap, M.-N. F. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2207257119 · Cited by 10
Self-citationStructural insights into context-specific inhibition of bacterial translation by macrolides
Syroegin, E. A., Aleksandrova, E. V., Kruglov, A. A., Paranjpe, M. N., Svetlov, M. S., & Polikanov, Y. S. (2025) · Nature Communications · doi:10.1038/s41467-025-64692-5 · Cited by 8
Volynkina, I. A., Бычкова, Е. Н., Karakchieva, A. O., Tikhomirov, A. S., Zatonsky, G. V., Solovieva, S. E., Martynov, M. M., Grammatikova, N. E., Tereshchenkov, A. G., Paleskava, A., et al. (2024) · Pharmaceuticals · doi:10.3390/ph17020187 · Cited by 8
Prospects for antimicrobial development in the cryo-EM era – a focus on the ribosome
del Valle, A. H., & Innis, C. A. (2020) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaa032 · Cited by 8
Isozaki, Y., Makikawa, T., Kimura, K., Nishihara, D., Fujino, M., Tanaka, Y., Hayashi, C., Ishizaki, Y., Igarashi, M., Yokoyama, T., et al. (2025) · Science Advances · doi:10.1126/sciadv.adt2352 · Cited by 7
Lipońska, A., Lee, H., & Yap, M.-N. F. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae596 · Cited by 6
Self-citationDirect Measurements of Erythromycin’s Effect on Protein Synthesis Kinetics in Living Bacterial Cells
Seefeldt, A. C., Rivera, J. A., & Johansson, M. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166942 · Cited by 6
Ren, S., Li, Y., & Zhou, Z. (2025) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2025.04.010 · Cited by 5
Dual effect of chloramphenicol peptides on ribosome inhibition
Bougas, A., Vlachogiannis, I. A., Gatos, D., Arenz, S., & Dinos, G. P. (2017) · Amino Acids · doi:10.1007/s00726-017-2406-5 · Cited by 5
Xu, C., Feng, J., Zhou, Y., Ren, H., Pan, X., Chen, S., Liu, X., Li, G., Li, J., Geng, B., et al. (2025) · Journal of Bacteriology · doi:10.1128/jb.00552-24 · Cited by 4
iTP-seq: a scalable profiling workflow to characterize bacterial translation landscapes in vitro
Gillard, M., Renault, T. T., & Innis, C. A. (2026) · Nature Protocols · doi:10.1038/s41596-025-01294-x · Cited by 4
Extended Shine-Dalgarno motifs govern translation initiation in Staphylococcus aureus
Kohl, M. P., Bahena-Ceron, R., Chane-Woon-Ming, B., Kompatscher, M., Erlacher, M. D., Barchet, C., von Loeffelholz, O., Romby, P., Klaholz, B. P., & Marzi, S. (2026) · Nature Communications · doi:10.1038/s41467-026-69079-8 · Cited by 8
Three Stages of Nascent Protein Translocation Through the Ribosome Exit Tunnel
Kolář, M. H., McGrath, H., Nepomuceno, F. C., & Černeková, M. (2024) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1873 · Cited by 5
Shoji, T., Takaya, A., Kusuya, Y., Takahashi, H., & Kawashima, H. (2021) · Genetics & Genomic Sciences · doi:10.24966/ggs-2485/100024 · Cited by 4
A method to enrich polypeptidyl-tRNAs to capture snapshots of translation in the cell
Yamakawa, A., Niwa, T., Chadani, Y., Kobo, A., & Taguchi, H. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1276 · Cited by 4
Ribosomes make sweeping arrests
Alonzo, D. A., & Schmeing, T. M. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2027 · Cited by 3
Toeprint Assays for Detecting RNA Structure and Protein–RNA Interactions
Yakhnin, H., & Babitzke, P. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2413-5_16 · Cited by 3
A bacterial regulatory uORF senses multiple classes of ribosome-targeting antibioticsPreprint
Baniulyte, G., & Wade, J. T. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/682021 · Cited by 5
Konikkat, S., Scribner, M. R., Eutsey, R., Hiller, N. L., Cooper, V. S., & McManus, C. J. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.16.155515 · Cited by 3
Dual site targeting of the bacterial 70S ribosome by tetracyclines
Devarkar, S. C., Lomakin, I. B., Wang, J., Grada, A., & Bunick, C. G. (2026) · Nature Communications · doi:10.1038/s41467-026-72788-9 · Cited by 2
“Recent studies on NPET binding translation inhibitors like macrolides and Tetracenomycin X have established that the sequence of the nascent peptide plays a crucial role in the binding af fi nity and ef fi cacy of these inhibitors 14,26,27 .”
Isozaki, Y., Muzahid, A. A., Wakata, T., Fujino, M., Tanaka, Y., Hayashi, C., Ishizaki, Y., Ohishi, T., Morita, A., Ohba, S., et al. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.118520 · Cited by 2
Metadata
- Authors
- Davis, A. R., Gohara, D. W., & Yap, M.-N. F.
- Affiliations
- Saint Louis University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-10-13
- Volume
- 111
- Issue
- 43
- Pages
- 15379-15384
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4217412
- OpenAlex
- W2165035045
- Cited by
- 123
- References
- 46
- Citations by year
- 2026: 13 · 2025: 10 · 2024: 10 · 2023: 6 · 2022: 8 · 2021: 14 · 2020: 12 · 2019: 8 · 2018: 11 · 2017: 18 · 2016: 10 · 2015: 3
- FWCI
- 4.23
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Saint Louis University
- National Institutes of Health
- National Institute of General Medical Sciences (R00GM094212)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Microbial Natural Products and Biosynthesis
- Keywords
- macrolide antibiotics, azithromycin, translational attenuation, ribosome stalling, Staphylococcus aureus, proline-rich sequences, charged residues, translational arrest
- MeSH terms
- Peptides, Proline, Ribosomes, Staphylococcus aureus, Protein Biosynthesis, Open Reading Frames, Azithromycin, Macrolides, Sequence Analysis, Protein
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