Sequence selectivity of macrolide-induced translational attenuation

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

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 · see citing works

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 · see citing works

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 640 · see citing works

A Ribosome-Bound Quality Control Complex Triggers Degradation of Nascent Peptides and Signals Translation Stress

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 631 · see citing works

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 534 · see citing works

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 525 · see citing works

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 · see citing works

The Mechanism of Action of Macrolides, Lincosamides and Streptogramin B Reveals the Nascent Peptide Exit Path in the Ribosome

Tenson, T., Lovmar, M., & Ehrenberg, M. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00662-4 · Cited by 461 · see citing works

Translation Elongation Factor EF-P Alleviates Ribosome Stalling at Polyproline Stretches

Ude, S., Lassak, J., Starosta, A. L., Kraxenberger, T., Wilson, D. N., & Jung, K. (2012) · Science · doi:10.1126/science.1228985 · Cited by 460 · see citing works

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 445 · see citing works

Dom34 Rescues Ribosomes in 3′ Untranslated Regions

Guydosh, N. R., & Green, R. (2014) · Cell · doi:10.1016/j.cell.2014.02.006 · Cited by 355 · see citing works

Electrostatics in the Ribosomal Tunnel Modulate Chain Elongation Rates

Lu, J., & DEUTSCH, C. J. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.08.089 · Cited by 328 · see citing works

Slow peptide bond formation by proline and other N -alkylamino acids in translation

Pavlov, M. Y., Watts, R. E., Tan, Z., Cornish, V. W., Ehrenberg, M., & Forster, A. C. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809211106 · Cited by 316 · see citing works

Positively Charged Residues Are the Major Determinants of Ribosomal Velocity

Charneski, C. A., & Hurst, L. D. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001508 · Cited by 293 · see citing works

Escherichia coli ribosomes translate in vivo with variable rate.

Pedersen, S. B. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb02227.x · Cited by 270 · see citing works

Arrest Peptides: Cis -Acting Modulators of Translation

Ito, K., & Chiba, S. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-080211-105026 · Cited by 265 · see citing works

Molecular Mechanism of Drug-Dependent Ribosome Stalling

Vazquez-Laslop, N., Thum, C., & Mankin, A. S. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.026 · Cited by 260 · see citing works

Nascent Peptide-dependent Translation Arrest Leads to Not4p-mediated Protein Degradation by the Proteasome

Dimitrova-Paternoga, L., Kuroha, K., Tatematsu, T., & Inada, T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808840200 · Cited by 252 · see citing works

How Hibernation Factors RMF, HPF, and YfiA Turn Off Protein Synthesis

Polikanov, Y. S., Blaha, G. M., & Steitz, T. A. (2012) · Science · doi:10.1126/science.1218538 · Cited by 236 · see citing works

α-Helical nascent polypeptide chains visualized within distinct regions of the ribosomal exit tunnel

Bhushan, S., Gartmann, M., Halić, M., Armache, J., Jarasch, A., Mielke, T., Berninghausen, O., Wilson, D. N., & Beckmann, R. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1756 · Cited by 210 · see citing works

Nascent peptides that block protein synthesis in bacteria

Woolstenhulme, C. J., Parajuli, S. P., Healey, D., Valverde, D. P., Petersen, E. N., Starosta, A. L., Guydosh, N. R., Johnson, W. E., Wilson, D. N., & Buskirk, A. R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1219536110 · Cited by 167 · see citing works

Programmed drug‐dependent ribosome stalling

Ramu, H., Mankin, A. S., & Vázquez‐Laslop, N. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06576.x · Cited by 165 · see citing works

Modulation of the Rate of Peptidyl Transfer on the Ribosome by the Nature of Substrates

Wohlgemuth, I., Brenner, S., Beringer, M., & Rodnina, M. V. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805316200 · Cited by 164 · see citing works

Selective Protein Synthesis by Ribosomes with a Drug-Obstructed Exit Tunnel

Kannan, K., Vázquez‐Laslop, N., & Mankin, A. S. (2012) · Cell · doi:10.1016/j.cell.2012.09.018 · Cited by 154 · see citing works

SecM-Stalled Ribosomes Adopt an Altered Geometry at the Peptidyl Transferase Center

Bhushan, S., Hoffmann, T., Seidelt, B., Frauenfeld, J., Mielke, T., Berninghausen, O., Wilson, D. N., & Beckmann, R. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000581 · Cited by 154 · see citing works

The key function of a conserved and modified rRNA residue in the ribosomal response to the nascent peptide

Vázquez‐Laslop, N., Ramu, H., Klepacki, D., Kannan, K., & Mankin, A. S. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.180 · Cited by 148 · see citing works

Dynamics of translation by single ribosomes through mRNA secondary structures

Chen, C., Zhang, H., Broitman, S. L., Reiche, M., Farrell, I., Cooperman, B. S., & Goldman, Y. E. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2544 · Cited by 147 · see citing works

Molecular basis for erythromycin-dependent ribosome stalling during translation of the ErmBL leader peptide

Arenz, S., Ramu, H., Gupta, P., Berninghausen, O., Beckmann, R., Vázquez‐Laslop, N., Mankin, A. S., & Wilson, D. N. (2014) · Nature Communications · doi:10.1038/ncomms4501 · Cited by 142 · see citing works

Features of Ribosome-Peptidyl-tRNA Interactions Essential for Tryptophan Induction of tna Operon Expression

Cruz-Vera, L. R., Rajagopal, S., Squires, C. L., & Yanofsky, C. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.013 · Cited by 133 · see citing works

Selective ribosome profiling as a tool for studying the interaction of chaperones and targeting factors with nascent polypeptide chains and ribosomes

Becker, A. H., Oh, E., Weissman, J. S., Krämer, G., & Bukau, B. (2013) · Nature Protocols · doi:10.1038/nprot.2013.133 · Cited by 128 · see citing works

Nascent Peptide in the Ribosome Exit Tunnel Affects Functional Properties of the A-Site of the Peptidyl Transferase Center

Ramu, H., Vázquez‐Laslop, N., Klepacki, D., Dai, Q., Piccirilli, J. A., Micura, R., & Mankin, A. S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.031 · Cited by 127 · see citing works

Translation Arrest Requires Two-Way Communication between a Nascent Polypeptide and the Ribosome

Woolhead, C. A., Johnson, A. E., & Bernstein, H. D. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.021 · Cited by 117 · see citing works

Macrolide antibiotics allosterically predispose the ribosome for translation arrest

Sothiselvam, S., Liu, B., Han, W., Ramu, H., Klepacki, D., Atkinson, G. C., Brauer, A., Remm, M., Tenson, T., Schulten, K. J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403586111 · Cited by 110 · see citing works

The Plasticity of a Translation Arrest Motif Yields Insights into Nascent Polypeptide Recognition inside the Ribosome Tunnel

Yap, M.-N. F., & Bernstein, H. D. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.002 · Cited by 99 · see citing works

Secondary Structure Formation of a Transmembrane Segment in Kv Channels

Lu, J., & DEUTSCH, C. J. (2005) · Biochemistry · doi:10.1021/bi050372q · Cited by 97 · see citing works

A ribosome–nascent chain sensor of membrane protein biogenesis in Bacillus subtilis

Chiba, S., Lamsa, A., & Pogliano, K. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.280 · Cited by 92 · see citing works

A nascent polypeptide domain that can regulate translation elongation

Peng, F., Spevak, C. C., Wu, C., & Sachs, M. S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400554101 · Cited by 87 · see citing works

Formation of 100S ribosomes in Staphylococcus aureus by the hibernation promoting factor homolog SaHPF

Ueta, M., Wada, C., & Wada, A. (2009) · Genes to Cells · doi:10.1111/j.1365-2443.2009.01364.x · Cited by 85 · see citing works

Interplay between the Ribosomal Tunnel, Nascent Chain, and Macrolides Influences Drug Inhibition

Starosta, A. L., Karpenko, V. V., Shishkina, A. V., Mikolajka, A., Sumbatyan, N. V., Schluenzen, F., Korshunova, G. A., Bogdanov, A. A., & Wilson, D. N. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.04.008 · Cited by 79 · see citing works

Peptidyl-prolyl-tRNA at the ribosomal P-site reacts poorly with puromycin

Muto, H., & Ito, K. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.12.072 · Cited by 66 · see citing works

Role of antibiotic ligand in nascent peptide-dependent ribosome stalling

Vázquez‐Laslop, N., Klepacki, D., Mulhearn, D. C., Ramu, H., Krasnykh, O., Franzblau, S. G., & Mankin, A. S. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103474108 · Cited by 61 · see citing works

rRNA:mRNA pairing alters the length and the symmetry of mRNA-protected fragments in ribosome profiling experiments

O’Connor, P. B. F., Li, G., Weissman, J. S., Atkins, J. F., & Baranov, P. V. (2013) · Bioinformatics · doi:10.1093/bioinformatics/btt184 · Cited by 55 · see citing works

Effects on Translation Pausing of Alterations in Protein and RNA Components of the Ribosome Exit Tunnel

Lawrence, M. G., Lindahl, L., & Zengel, J. M. (2008) · Journal of Bacteriology · doi:10.1128/jb.00632-08 · Cited by 54 · see citing works

The Molecular Mechanism of Peptide-mediated Erythromycin Resistance

Lovmar, M., Nilsson, K., Vimberg, V., Tenson, T., Nervall, M., & Ehrenberg, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511918200 · Cited by 46 · see citing works

The synthesis of polyphenylalanine on ribosomes to which erythromycin is bound

ODOM, O. W., Picking, W. D., Tsalkova, T. N., & HARDESTY, B. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16071.x · Cited by 32 · see citing works

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 535 · see citing works

The macrolide antibiotic renaissance

Dinos, G. P. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13936 · Cited by 476 · see citing works

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 414 · see citing works

Ribosome-Targeting Antibiotics: Modes of Action, Mechanisms of Resistance, and Implications for Drug Design

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 · see citing works

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 187 · see citing works

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 165 · see citing works

Context-specific inhibition of translation by ribosomal antibiotics targeting the peptidyl transferase center

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 · see citing works

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 · see citing works

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 124 · see citing works

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 109 · see citing works

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 103 · see citing works

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 94 · see citing works

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 · see citing works

DeepRibo: a neural network for precise gene annotation of prokaryotes by combining ribosome profiling signal and binding site patterns

Clauwaert, J., Menschaert, G., & Waegeman, W. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz061 · Cited by 87 · see citing works

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 · see citing works

Context-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 83 · see citing works

Disassembly of the Staphylococcus aureus hibernating 100S ribosome by an evolutionarily conserved GTPase

Basu, A., & Yap, M.-N. F. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1709588114 · Cited by 74 · see citing works

Ribosome hibernation factor promotesStaphylococcalsurvival and differentially represses translation

Basu, A., & Yap, M.-N. F. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw180 · Cited by 74 · see citing works

GWIPS-viz: 2018 update

Michel, 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 · see citing works

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 · see citing works

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 72 · see citing works

Blast from the Past: Reassessing Forgotten Translation Inhibitors, Antibiotic Selectivity, and Resistance Mechanisms to Aid Drug Development

Arenz, S., & Wilson, D. N. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.10.019 · Cited by 66 · see citing works

Klebsazolicin inhibits 70S ribosome by obstructing the peptide exit tunnel

Metelev, M., Osterman, I. А., Ghilarov, D., Khabibullina, N. F., Yakimov, A., 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 64 · see citing works

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 63 · see citing works

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 62 · see citing works

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 58 · see citing works

The Expression of Antibiotic Resistance Methyltransferase Correlates with mRNA Stability Independently of Ribosome Stalling

Dzyubak, E., & Yap, M.-N. F. (2016) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01806-16 · Cited by 56 · see citing works

The 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 56 · see citing works

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 54 · see citing works

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 · see citing works

Selective toxicity of antibacterial agents—still a valid concept or do we miss chances and ignore risks?

Dalhoff, A. (2020) · Infection · doi:10.1007/s15010-020-01536-y · Cited by 55 · see citing works

Uncovering small membrane proteins in pathogenic bacteria: Regulatory functions and therapeutic potential

Garai, P., & Blanc‐Potard, A. (2020) · Molecular Microbiology · doi:10.1111/mmi.14564 · Cited by 51 · see citing works

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 · see citing works

Binding of Macrolide Antibiotics Leads to Ribosomal Selection against Specific Substrates Based on Their Charge and Size

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 · see citing works

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 · see citing works

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 · see citing works

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 44 · see citing works

Genome-encoded ABCF factors implicated in intrinsic antibiotic resistance in Gram-positive bacteria: VmlR2, Ard1 and CplR

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 · see citing works

Co-produced natural ketolides methymycin and pikromycin inhibit bacterial growth by preventing synthesis of a limited number of proteins

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 · see citing works

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 40 · see citing works

Metabolic Fingerprinting with Fourier-Transform Infrared (FTIR) Spectroscopy: Towards a High-Throughput Screening Assay for Antibiotic Discovery and Mechanism-of-Action Elucidation

da Cunha, B. R., Fonseca, L. P., & Calado, C. R. C. (2020) · Metabolites · doi:10.3390/metabo10040145 · Cited by 40 · see citing works

Rolling circle amplification based on signal-enhanced electrochemical DNA sensor for ultrasensitive transcription factor detection

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 · see citing works

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 · see citing works

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 · see citing works

Expression of Bacillus subtilis ABCF antibiotic resistance factor VmlR is regulated by RNA polymerase pausing, transcription attenuation, translation attenuation and (p)ppGpp

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 35 · see citing works

Hibernation-Promoting Factor Sequesters Staphylococcus aureus Ribosomes to Antagonize RNase R-Mediated Nucleolytic Degradation

Lipońska, A., & Yap, M.-N. F. (2021) · mBio · doi:10.1128/mbio.00334-21 · Cited by 34 · see citing works

Resistance to ketolide antibiotics by coordinated expression of rRNA methyltransferases in a bacterial producer of natural ketolides

Almutairi, 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 · see citing works

NusG-Dependent RNA Polymerase Pausing and Tylosin-Dependent Ribosome Stalling Are Required for Tylosin Resistance by Inducing 23S rRNA Methylation in Bacillus subtilis

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 · see citing works

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 · see citing works

Simultaneous elucidation of antibiotic mechanism of action and potency with high-throughput Fourier-transform infrared (FTIR) spectroscopy and machine learning

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 · see citing works

The context of the ribosome binding site in mRNAs defines specificity of action of kasugamycin, an inhibitor of translation initiation

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 30 · see citing works

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 · see citing works

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 28 · see citing works

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 · see citing works

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 26 · see citing works

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 · see citing works

The hibernating 100S complex is a target of ribosome-recycling factor and elongation factor G in Staphylococcus aureus

Basu, A., Shields, K. E., & Yap, M.-N. F. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012307 · Cited by 25 · see citing works

NusG-dependent RNA polymerase pausing is a frequent function of this universally conserved transcription elongation factor

Yakhnin, A. V., Kashlev, M., & Babitzke, P. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1828261 · Cited by 24 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Epitranscriptional m6A modification of rRNA negatively impacts translation and host colonization in Staphylococcus aureus

Shields, K. E., Ranava, D., Tan, Y., Zhang, D., & Yap, M.-N. F. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1011968 · Cited by 17 · see citing works

Mechanism of Macrolide-Induced Inhibition of Pneumolysin Release Involves Impairment of Autolysin Release in Macrolide-Resistant Streptococcus pneumoniae

Domon, 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 · see citing works

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 · see citing works

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 · see citing works

Nascent chain-mediated translation regulation in bacteria: translation arrest and intrinsic ribosome destabilization

Chiba, S., Fujiwara, K., Chadani, Y., & Taguchi, H. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad007 · Cited by 16 · see citing works

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 · see citing works

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 · see citing works

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 16 · see citing works

Translation complex stabilization on messenger RNA and footprint profiling to study the RNA responses and dynamics of protein biosynthesis in the cells

Shirokikh, N. E. (2021) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2021.2006599 · Cited by 14 · see citing works

Riboregulation in bacteria: From general principles to novel mechanisms of the trp attenuator and its sRNA and peptide products

Evguenieva‐Hackenberg, E. (2021) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1696 · Cited by 15 · see citing works

Quantitative mapping of mRNA 3’ ends in Pseudomonas aeruginosa reveals a pervasive role for premature 3’ end formation in response to azithromycin

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 14 · see citing works

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 · see citing works

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 · see citing works

Compounds for selective translational inhibition

Shichino, Y., & Iwasaki, S. (2022) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2022.102158 · Cited by 13 · see citing works

Erythromycin leads to differential protein expression through differences in electrostatic and dispersion interactions with nascent proteins

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 · see citing works

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 · see citing works

Eurycomalactone Inhibits Expression of Endothelial Adhesion Molecules at a Post-Transcriptional Level

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 · see citing works

Bidirectional sequestration between a bacterial hibernation factor and a glutamate metabolizing protein

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 · see citing works

Structural 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 · see citing works

Hybrid Molecules of Azithromycin with Chloramphenicol and Metronidazole: Synthesis and Study of Antibacterial Properties

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 · see citing works

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 7 · see citing works

Creation of a macrolide antibiotic against non-tuberculous Mycobacterium using late-stage boron-mediated aglycon delivery

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 · see citing works

Staphylococcal exoribonuclease YhaM destabilizes ribosomes by targeting the mRNA of a hibernation factor

Lipońska, A., Lee, H., & Yap, M.-N. F. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae596 · Cited by 6 · see citing works

Direct 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 · see citing works

RiboParser/RiboShiny: an integrated platform for comprehensive analysis and visualization of Ribo-seq data

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 · see citing works

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 · see citing works

Azithromycin represses evolution of ceftazidime/avibactam resistance by translational repression of rpoS in Pseudomonas aeruginosa

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 · see citing works

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 · see citing works

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 4 · see citing works

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 4 · see citing works

Ribosome Profiling in Streptococcus pneumoniae Reveals the Role of Methylation of 23S rRNA Nucleotide G748 on Ribosome Stalling

Shoji, T., Takaya, A., Kusuya, Y., Takahashi, H., & Kawashima, H. (2021) · Genetics & Genomic Sciences · doi:10.24966/ggs-2485/100024 · Cited by 4 · see citing works

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 · see citing works

Ribosomes make sweeping arrests

Alonzo, D. A., & Schmeing, T. M. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2027 · Cited by 3 · see citing works

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 · see citing works

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 3 · see citing works

Quantitative mapping of mRNA 3’ ends in Pseudomonas aeruginosa reveals a pervasive role for premature 3’ end formation in response to azithromycinPreprint

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 · see citing works

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 · see citing works

Synthesis and structure-activity relationship of azithromycin derivatives against non-tuberculous mycobacteria

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 · see citing works

The general mode of translation inhibition by macrolide antibiotics

Kannan, K., Kanabar, P. N., Schryer, D. W., Florin, T., Oh, E., Bahroos, N., Tenson, T., Weissman, J. S., & Mankin, A. S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417334111 · Cited by 176 · see citing works

Macrolide antibiotics allosterically predispose the ribosome for translation arrest

Sothiselvam, S., Liu, B., Han, W., Ramu, H., Klepacki, D., Atkinson, G. C., Brauer, A., Remm, M., Tenson, T., Schulten, K. J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403586111 · Cited by 110 · see citing works

Triggering Peptide-Dependent Translation Arrest by Small Molecules: Ribosome Stalling Modulated by Antibiotics

Vázquez‐Laslop, N., & Mankin, A. S. (2014) · Springer eBooks · doi:10.1007/978-4-431-55052-5_10 · Cited by 8 · see citing works

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 · see citing works

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 94 · see citing works