Mycobacterial HflX is a ribosome splitting factor that mediates antibiotic resistance
Open accessAbstract
Significance: The erm41 gene is considered the primary mechanism of intrinsic resistance to macrolides in Mycobacterium abscessus . Here we demonstrate that the hflX gene plays a significant and equally important role as erm41 . We further describe an unusual mechanism of resistance to macrolide-lincosamide antibiotics mediated by the mycobacterial HflX that likely involves the dissociation of antibiotic-stalled ribosomes. An understanding of the various mechanisms employed by bacteria for resistance to an antibiotic is critical in predicting an effective therapeutic regimen against a pathogenic isolate, and can also inform the development of novel drugs.
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Tn-seq, recombineering and CRISPR tools applied to M. abscessus have begun to define genes that make M. abscessus intrinsically resistant to many antibiotics.
“For example, Tn-seq, recombineering and CRISPR tools applied to M. abscessus have begun to define those genes that make M. abscessus intrinsically resistant to many antibiotics (167–170).”
From Mycobacterium smegmatis: The Vanguard of Mycobacterial Research (2023) · cites this paper as [170]
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Griffith, D. E., Aksamit, T., Brown-Elliott, B. A., Catanzaro, A., Daley, C., Gordin, F., Holland, S. M., Horsburgh, R., Huitt, G., Iademarco, M. F., et al. (2007) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200604-571st · Cited by 6,110 · see citing works
Leclercq, R. (2002) · Clinical Infectious Diseases · doi:10.1086/324626 · Cited by 1,102 · see citing works
Schlünzen, F., Zarivach, R., Harms, J., Bashan, A., Tocilj, A., Albrecht, R., Yonath, A., & Franceschi, F. J. (2001) · Nature · doi:10.1038/35101544 · Cited by 1,057 · see citing works
Mycobacterium abscessus: a new antibiotic nightmare
Nessar, R., Cambau, E., Reyrat, J., Murray, A., & Gicquel, B. (2012) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkr578 · Cited by 800 · see citing works
Experimental Determination and System Level Analysis of Essential Genes in Escherichia coli MG1655
Gerdes, S., Scholle, M., Campbell, J., Balázsi, G., Ravasz, E., Daugherty, M., Somera, A., Kyrpides, N., Anderson, I., Gelfand, M., et al. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.19.5673-5684.2003 · Cited by 788 · see citing works
Nash, K. A., Brown‐Elliott, B. A., & Wallace, R. J. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01275-08 · Cited by 639 · see citing works
The bacterial ribosome as a target for antibiotics
Poehlsgaard, J., & Douthwaite, S. R. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1265 · Cited by 604 · see citing works
Recombineering in Mycobacterium tuberculosis
van Kessel, J. C., & Hatfull, G. F. (2006) · Nature Methods · doi:10.1038/nmeth996 · Cited by 582 · see citing works
Mycobacterium abscessus Complex Infections in Humans
Lee, M., Sheng, W., Hung, C., Yu, C., Lee, L., & Hsueh, P. (2015) · Emerging infectious diseases · doi:10.3201/2109.141634 · Cited by 571 · see citing works
Floto, R. A., Olivier, K. N., Saiman, L. M., Daley, C. L., Herrmann, J., Nick, J. A., Noone, P. G., Bilton, D., Corris, P. A., Gibson, R. L., et al. (2015) · Thorax · doi:10.1136/thoraxjnl-2015-207983 · Cited by 463 · see citing works
Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance
Connell, S. R., Tracz, D. M., Nierhaus, K. H., & Taylor, D. E. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.12.3675-3681.2003 · Cited by 449 · see citing works
Tu, D., Blaha, G., Moore, P., & Steitz, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.005 · Cited by 439 · see citing works
Roberts, M. C. (2008) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2008.01145.x · Cited by 392 · see citing works
Ross, J. I., Eady, E. A., Cove, J. H., Cunliffe, W. J., Baumberg, S., & Wootton, J. C. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb00696.x · Cited by 358 · see citing works
Ancestral antibiotic resistance in Mycobacterium tuberculosis
Morris, R. P., Nguyen, L., Gatfield, J., Visconti, K. C., Nguyen, K. T., Schnappinger, D., Ehrt, S., Liu, Y., Heifets, L. B., Pieters, J., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505446102 · Cited by 334 · see citing works
The A-Z of bacterial translation inhibitors
Wilson, D. N. (2009) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409230903307311 · Cited by 322 · see citing works
ABC-F Proteins Mediate Antibiotic Resistance through Ribosomal Protection
Sharkey, L. K. R., Edwards, T. A., & O’Neill, A. J. (2016) · mBio · doi:10.1128/mbio.01975-15 · Cited by 281 · see citing works
Structural insight into the role of the ribosomal tunnel in cellular regulation
Berisio, R., Schluenzen, F., Harms, J. M., Bashan, A., Auerbach, T., Baram, D., & Yonath, A. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb915 · Cited by 178 · see citing works
DNA interstrand cross-link repair requires replication-fork convergence
Zhang, J., Dewar, J. M., Budzowska, M., Motnenko, A., Cohn, M. A., & Walter, J. C. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2956 · Cited by 154 · see citing works
Molecular Basis of Intrinsic Macrolide Resistance in the Mycobacterium tuberculosis Complex
Buriánková, K., Doucet‐Populaire, F., Dorson, O., Gondran, A., Ghnassia, J. C., Weiser, J., & Pernodet, J. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.1.143-150.2004 · Cited by 148 · see citing works
The ABC-F protein EttA gates ribosome entry into the translation elongation cycle
Boël, G., Smith, P., Ning, W., Englander, M. T., Chen, B., Hashem, Y., Testa, A. J., Fischer, J. J., Wieden, H., Frank, J., et al. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2740 · Cited by 129 · see citing works
Hurst-Hess, K., Rudra, P., & Ghosh, P. (2017) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01347-17 · Cited by 115 · see citing works
Self-citationMacrolide antibiotics in the ribosome exit tunnel: species‐specific binding and action
Kannan, K., & Mankin, A. S. (2011) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2011.06315.x · Cited by 108 · see citing works
Antibiotic Resistance ABC-F Proteins: Bringing Target Protection into the Limelight
Sharkey, L. K. R., & O’Neill, A. J. (2018) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.7b00251 · Cited by 98 · see citing works
HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions
Zhang, Y., Mandava, C. S., Cao, W., Li, X., Zhang, D., Li, N., Zhang, Y., Zhang, X., Qin, Y., Mi, K., et al. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3103 · Cited by 97 · see citing works
Sanchez-Pescador, R., Brown, J. T., Roberts, M., & Urdea, M. S. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.3.1218 · Cited by 87 · see citing works
Lau, C., van Engelen, K., Gordon, S., Renaud, J., & Topp, E. (2017) · Applied and Environmental Microbiology · doi:10.1128/aem.00989-17 · Cited by 76 · see citing works
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
Burian, J., Ramón-García, S., Howes, C. G., & Thompson, C. (2012) · Expert Review of Anti-Infective Therapy · doi:10.1586/eri.12.90 · Cited by 59 · see citing works
Translational Attenuation and mRNA Stabilization as Mechanisms of erm (B) Induction by Erythromycin
Min, Y.-H., Kwon, A., Yoon, E.-J., Shim, M.-J., & Choi, E. (2008) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01376-07 · Cited by 59 · see citing works
Mougari, F., Amarsy, R., Véziris, N., Bastian, S., Brossier, F., Berçot, B., Raskine, L., & Cambau, E. (2016) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkw130 · Cited by 59 · see citing works
HflXr, a homolog of a ribosome-splitting factor, mediates antibiotic resistance
Duval, M., Dar, D., Carvalho, F., Rocha, E. P. C., Sorek, R., & Cossart, P. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1810555115 · Cited by 56 · see citing works
Plaza, J. J. G., Šimatović, A., Milaković, M., Bielen, A., Wichmann, F., & Udiković‐Kolić, N. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02675 · Cited by 53 · see citing works
E. coli HflX interacts with 50S ribosomal subunits in presence of nucleotides
Jain, N., Dhimole, N., Rafay, A., De, D., Tomar, S. K., Sajish, M., Dutta, D., Parrack, P., & Prakash, B. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.12.072 · Cited by 49 · see citing works
Coatham, M. L., Brandon, H. E., Fischer, J. J., Schümmer, T., & Wieden, H. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1524 · Cited by 44 · see citing works
Mehta, P., Woo, P., Venkataraman, K., & Karzai, A. W. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-949-5_18 · Cited by 43 · see citing works
Polkinghorne, A., Ziegler, U., Hernández, Y. G., Pospischil, A., Timms, P., & Vaughan, L. (2008) · Microbiology · doi:10.1099/mic.0.2008/022137-0 · Cited by 33 · see citing works
Properties of HflX, an Enigmatic Protein from Escherichia coli
Dutta, D., Bandyopadhyay, K., Datta, A. B., Sardesai, A. A., & Parrack, P. (2009) · Journal of Bacteriology · doi:10.1128/jb.01353-08 · Cited by 32 · see citing works
Regulation of the macrolide-lincosamide-streptogramin B resistance gene ermD
Hue, K. K., & Bechhofer, D. H. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.18.5860-5868.1992 · Cited by 29 · see citing works
Blombach, F., Launay, H. M. M., Zorraquino, V., Swarts, D. C., Cabrita, L. D., Benelli, D., Christodoulou, J. C., Londei, P., & John van der, O. O. S. T. (2011) · Journal of Bacteriology · doi:10.1128/jb.01552-10 · Cited by 24 · see citing works
A new beginning of the end of translation
Ehrenberg, M., & Tenson, T. (2002) · Nature Structural Biology · doi:10.1038/nsb0202-85 · Cited by 23 · see citing works
Burian, J., & Thompson, C. (2018) · Molecular Microbiology · doi:10.1111/mmi.13890 · Cited by 22 · see citing works
Jain, N., Vithani, N., Rafay, A., & Prakash, B. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt705 · Cited by 16 · see citing works
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Sorted by citations
Target protection as a key antibiotic resistance mechanism
Wilson, D. N., Hauryliuk, V., Atkinson, G. C., & O’Neill, A. J. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-020-0386-z · Cited by 213 · see citing works
Mycobacterium smegmatis: The Vanguard of Mycobacterial Research
Sparks, I. L., Derbyshire, K. M., Jacobs, W. R., & Morita, Y. S. (2023) · Journal of Bacteriology · doi:10.1128/jb.00337-22 · Cited by 149 · see citing works
Dove, N. C., Taş, N., & Hart, S. C. (2022) · The ISME Journal · doi:10.1038/s41396-022-01232-9 · Cited by 106 · see citing works
Bhattacharjee, S., Feng, X., Maji, S., Dadhwal, P., Zhang, Z., Brown, Z. P., & Frank, J. (2024) · Cell · doi:10.1016/j.cell.2023.12.027 · Cited by 56 · see citing works
Dual function of GTPBP6 in biogenesis and recycling of human mitochondrial ribosomes
Lavdovskaia, E., Denks, K., Nadler, F., Steube, E., Linden, A., Urlaub, H., Rodnina, M. V., & Richter‐Dennerlein, R. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1132 · Cited by 48 · see citing works
Egorova, A., Jackson, M., Gavrilyuk, V., & Makarov, V. (2021) · Medicinal Research Reviews · doi:10.1002/med.21798 · Cited by 48 · see citing works
Bezrukov, F., Prados, J., Renzoni, A., & Panasenko, O. O. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1292 · Cited by 34 · see citing works
Unraveling the mechanisms of intrinsic drug resistance in Mycobacterium tuberculosis
Poulton, N. C., & Rock, J. M. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.997283 · Cited by 31 · see citing works
Lee, J., Yoo, J., Kim, Y., Kim, J., Lee, E., & Roe, J. (2020) · mBio · doi:10.1128/mbio.00625-20 · Cited by 28 · see citing works
Mycobacterium Abscessus HelR Interacts with RNA Polymerase to Confer Intrinsic Rifamycin Resistance
Hurst-Hess, K. R., Saxena, A., Rudra, P., Yang, Y., & Ghosh, P. (2021) · Molecular Cell · doi:10.1016/j.molcel.2022.06.034 · Cited by 27 · see citing works
Self-citationLi, Y., Sharma, M. R., Koripella, R. K., Banavali, N. K., Agrawal, R. K., & Ojha, A. K. (2021) · Microbiology · doi:10.1099/mic.0.001035 · Cited by 24 · see citing works
Developmentally regulated GTPases: structure, function and roles in disease
Westrip, C. A. E., Zhuang, Q., Hall, C., Eaton, C. D., & Coleman, M. L. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03961-0 · Cited by 25 · see citing works
Svetlov, M. S., Dunand, C. F., Nakamoto, J. A., Atkinson, G. C., Safdari, H. A., Wilson, D. N., Vázquez‐Laslop, N., & Mankin, A. S. (2024) · Molecular Cell · doi:10.1016/j.molcel.2023.12.002 · Cited by 24 · see citing works
Poulton, N. C., DeJesus, M. A., Munsamy, V., Kanai, M., Roberts, C. G., Azadian, Z. A., Bosch, B., Lin, K. M., Li, S., & Rock, J. M. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2023.12.020 · Cited by 24 · see citing works
Hurst-Hess, K. R., McManaman, C. L., Yong, Y., Gupta, S., & Ghosh, P. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1011060 · Cited by 22 · see citing works
Self-citationStructural basis for HflXr-mediated antibiotic resistance in Listeria monocytogenes
Koller, T. O., Turnbull, K. J., Vaitkevicius, K., Crowe‐McAuliffe, C., Roghanian, M., Bulvas, O., Nakamoto, J. A., Kurata, T., Julius, C., Atkinson, G. C., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac934 · Cited by 19 · see citing works
Maintaining mitochondrial ribosome function: The role of ribosome rescue and recycling factors
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Yue, C., Wang, L., Wang, X., Cen, R., Chen, J., Li, L., Yang, W., Tan, Y., & Lei, X. (2022) · Photodiagnosis and Photodynamic Therapy · doi:10.1016/j.pdpdt.2022.102802 · Cited by 19 · see citing works
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Kumar, N., Sharma, S., & Kaushal, P. S. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.101002 · Cited by 19 · see citing works
Mechanisms of ribosome recycling in bacteria and mitochondria: a structural perspective
Seely, S. M., & Gagnon, M. G. (2022) · RNA Biology · doi:10.1080/15476286.2022.2067712 · Cited by 16 · see citing works
Mechanistic insights into the alternative ribosome recycling by HflXr
Seely, S. M., Basu, R. S., & Gagnon, M. G. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae128 · Cited by 15 · see citing works
Ribosome Protection as a Mechanism of Lincosamide Resistance in Mycobacterium abscessus
Hurst-Hess, K. R., Rudra, P., & Ghosh, P. (2021) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01184-21 · Cited by 14 · see citing works
Self-citationFishbein, S. R. S., Tomasi, F. G., Wolf, I. D., Dulberger, C. L., Wang, A., Keshishian, H., Wallace, L., Carr, S. A., Ioerger, T. R., Rego, E. H., et al. (2020) · Journal of Bacteriology · doi:10.1128/jb.00604-20 · Cited by 13 · see citing works
HflX-mediated drug resistance through ribosome splitting and rRNA disordering in mycobacteria
Majumdar, S., Kashyap, A., Koripella, R. K., Sharma, M. R., Hurst-Hess, K. R., Manjari, S. R., Banavali, N. K., Ghosh, P., & Agrawal, R. K. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2419826122 · Cited by 12 · see citing works
Self-citationVarshney, A., Jia, Z., Howe, M. D., Keiler, K. C., & Baughn, A. D. (2025) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00963 · Cited by 12 · see citing works
WhiB-like proteins: Diversity of structure, function and mechanism
Beltran, D. G., Wan, T., & Zhang, L. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119787 · Cited by 10 · see citing works
Role of a cryptic tRNA gene operon in survival under translational stress
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Cushman, J., Freeman, E., McCallister, S., Schumann, A., Hutchison, K. W., & Molloy, S. D. (2021) · BMC Microbiology · doi:10.1186/s12866-021-02224-z · Cited by 9 · see citing works
HflX is a GTPase that controls hypoxia-induced replication arrest in slow-growing mycobacteria
Ngan, J. Y. G., Pasunooti, S., Tse, W., Meng, W., Ngan, S. F. C., Jia, H., Lin, J., Ng, S. W., Jaafar, M. T., Cho, S. L. S., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2006717118 · Cited by 9 · see citing works
Hu, W., Huo, X., Bai, H., Chen, Z., Zhang, J., Yang, H., & Feng, S. (2024) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-024-03924-0 · Cited by 6 · see citing works
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van der Niet, S., Green, K. D., Schimmel, I. M., de Bakker, J., Lodder, B., Reits, E. A., Garneau‐Tsodikova, S., & van der Wel, N. N. (2024) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00029-24 · Cited by 4 · see citing works
Srinivasan, K., Banerjee, A., & Sengupta, J. (2024) · Structure · doi:10.1016/j.str.2024.06.016 · Cited by 4 · see citing works
Wu, D., Dai, Y., & Gao, N. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.25.517942 · Cited by 4 · see citing works
Tahmasebinia, F., & Wu, Z. (2025) · BioEssays · doi:10.1002/bies.70054 · Cited by 3 · see citing works
Mehrez, M., Lecampion, C., Ke, H., Gorsane, F., & Field, B. (2024) · Plant Direct · doi:10.1002/pld3.559 · Cited by 3 · see citing works
Quality Control Mechanisms in Bacterial Translation
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Genotypic detection of clindamycin resistance in locally isolated Staphylococcus aureus
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Self-citationTakada, H. (2026) · Bioscience Biotechnology and Biochemistry · doi:10.1093/bbb/zbag015 · Cited by 3 · see citing works
Yue, X., Liao, Q., He, H., Li, H., Xie, J., & Fu, Z. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.2c04851 · Cited by 2 · see citing works
HflX controls hypoxia-induced non-replicating persistence in slow growing mycobacteriaPreprint
Ngan, J. Y. G., Pasunooti, S., Tse, W., Meng, W., Ngan, S. F. C., Ng, S. W., Jaafar, M. T., Jia, H., Cho, S. L. S., Lim, J., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.13.990168 · Cited by 2 · see citing works
Geng, H., Qi, M., Su, M., Zhi, F., & Chu, Y. (2026) · Frontiers in Microbiology · doi:10.3389/fmicb.2026.1823866 · Cited by 1 · see citing works
Hierarchy and networks in the transcriptional response of Mycobacterium abscessus to antibioticsPreprint
Hurst-Hess, K. R., McManaman, C. L., Yong, Y., Gupta, S., & Ghosh, P. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.16.533064 · Cited by 1 · see citing works
Self-citationKumar, A., Agarwal, P., Shivangi, S., & Meena, L. S. (2021) · Gene Reports · doi:10.1016/j.genrep.2021.101418
Mehrez, M., Lecampion, C., Ke, H., Gorsane, F., & Field, B. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.03.530967
Drug resistance through ribosome splitting and rRNA disordering in mycobacteriaPreprint
Majumdar, S., Kashyap, A., Koripella, R. K., Sharma, M. R., Hurst-Hess, K. R., Manjari, S. R., Banavali, N. K., Ghosh, P., & Agrawal, R. K. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.13.598844
Self-citationMultifaceted roles of mycobacterial HflX: ribosome splitting, rRNA disordering, and drug resistance
Majumdar, S., Ghosh, P., & Agrawal, R. K. (2025) · Biochemical Society Transactions · doi:10.1042/bst20253084
Self-citationKosulnikov, Y. V., Kryukov, A. A., Berdysheva, K. N., Kovalchuk, A. I., Yurkov, A. P., & Laktionov, Y. V. (2026) · Vavilov Journal of Genetics and Breeding · doi:10.18699/vjgb-26-47
Meyer, M. D., Bergkessel, M., & DePas, W. H. (2026) · Journal of Bacteriology · doi:10.1128/jb.00076-26
Zhou, H., Wang, W., Fan, D., Liu, X., Peng, L., Shang, X., Li, H. Y., Dai, L., Cai, L., & Yang, T. (2026) · Journal of Global Antimicrobial Resistance · doi:10.1016/j.jgar.2026.07.007
Amin, N. H., Troian, E. A., Maldonado, H., & Woychik, N. A. (2026) · mSystems · doi:10.1128/msystems.00934-26
- Authors
- Rudra, P., Hurst-Hess, K. R., Cotten, K. L., Partida-Miranda, A., & Ghosh, P.
- Affiliations
- New York State Department of Health (US)
- Corresponding author
- Ghosh, Pallavi
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2019-12-23
- Volume
- 117
- Issue
- 1
- Pages
- 629-634
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC6955381
- OpenAlex
- W2997798310
- Cited by
- 53
- References
- 43
- Citations by year
- 2026: 7 · 2025: 5 · 2024: 10 · 2023: 6 · 2022: 6 · 2021: 12 · 2020: 7
- FWCI
- 4.76
- 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
- Office of Extramural Research, National Institutes of Health (1 R21 AI146774)
- Cystic Fibrosis Foundation (GHOSH18G0)
- Topics
- Health Sciences › Medicine › Epidemiology › Mycobacterium research and diagnosis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Keywords
- Mycobacterium abscessus, macrolide resistance, lincosamide resistance, antibiotic resistance mechanisms, ribosome dissociation, ribosome stalling, ribosome-associated chaperones
- MeSH terms
- Protein Domains, Mycobacterium abscessus, Anti-Bacterial Agents, Bacterial Proteins, Humans, Mutation, Mycobacterium Infections, Nontuberculous, Ribosomal Proteins, RNA, Bacterial, RNA, Messenger, Protein Biosynthesis, Gene Expression Regulation, Bacterial, Macrolides, GTP-Binding Proteins, Mycobacterium smegmatis, Drug Resistance, Bacterial, Ribosome Subunits, Large, Bacterial, Lincosamides
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 ›
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