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Genes required for mycobacterial growth defined by high density mutagenesis
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Summary: Despite over a century of research, tuberculosis remains a leading cause of infectious death worldwide. Faced with increasing rates of drug resistance, the identification of genes that are required for the growth of this organism should provide new targets for the design of antimycobacterial agents. Here, we describe the use of transposon site hybridization (TraSH) to comprehensively identify the genes required by the causative agent, Mycobacterium tuberculosis , for optimal growth. These genes include those that can be assigned to essential pathways as well as many of unknown function. The genes important for the growth of M. tuberculosis are largely conserved in the degenerate genome of the leprosy bacillus, Mycobacterium leprae , indicating that non‐essential functions have been selectively lost since this bacterium diverged from other mycobacteria. In contrast, a surprisingly high proportion of these genes lack identifiable orthologues in other bacteria, suggesting that the minimal gene set required for survival varies greatly between organisms with different evolutionary histories.
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“While space does not allow a detailed discussion, loss of glycosylation in plants, fungi or prokaryotes can also lead to cell death.”
From Biological roles of glycans (2017) · cites this paper as [435]
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“The F1Fo-ATP synthase in M. tuberculosis and M. smegmatis has been shown to be essential for optimal growth (29, 103).”
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Cites
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847
Massive gene decay in the leprosy bacillus.
Cole, S. T., Eiglmeier, K., Parkhill, J., James, K. D., Thomson, N. R., Wheeler, P. R., Honoré, N., Garnier, T., Churcher, C., Harris, D., et al. (2001) · Nature · doi:10.1038/35059006 · Cited by 1,777
Global Transposon Mutagenesis and a Minimal Mycoplasma Genome
Hutchison, C. A., Peterson, S. N., Gill, S. R., Cline, R. T., White, O. R., Fraser, C. M., Smith, H. O., & Venter, J. C. (1999) · Science · doi:10.1126/science.286.5447.2165 · Cited by 925
Karp, P. D., Paley, S., & Romero, P. (2002) · Bioinformatics · doi:10.1093/bioinformatics/18.suppl_1.s225 · Cited by 661
Comprehensive identification of conditionally essential genes in mycobacteria
Sassetti, C. M., Boyd, D. H., & Rubin, E. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231275498 · Cited by 604
Self-citationDe Voss, J. J., Rutter, K., Schroeder, B. G., Su, H., Zhu, Y., & Barry, C. E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.3.1252 · Cited by 532
Rodríguez, G. M., Voskuil, M. I., Gold, B., Schoolnik, G. K., & Smith, I. (2002) · Infection and Immunity · doi:10.1128/iai.70.7.3371-3381.2002 · Cited by 493
A purified mariner transposase is sufficient to mediate transposition in vitro.
Lampe, D. J., Churchill, M. E. A., & Robertson, H. M. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00930.x · Cited by 457
Quadri, L. E. N., Sello, J. K., Keating, T. A., Weinreb, P. H., & Walsh, C. T. (1998) · Chemistry & Biology · doi:10.1016/s1074-5521(98)90291-5 · Cited by 418
Ji, Y., Zhang, B., Van, S. F., Horn, Warren, P. V., Woodnutt, G., Burnham, M. K. R., & Rosenberg, M. J. (2001) · Science · doi:10.1126/science.1063566 · Cited by 414
Research works printed but not linked: 1
- Zalkin H., 1996, Escherichia Coli and Salmonella: Cellular and Molecular Biololgy
Cited by
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Items 401–500 of 1,003
Low, K. L., Shui, G., Natter, K., Yeo, W. K., Kohlwein, S. D., Dick, T., Rao, S. P. S., & Wenk, M. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.135731 · Cited by 85
Webby, C. J., Baker, H. M., Lott, J. S., Baker, E. N., & Parker, E. J. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.09.093 · Cited by 85
Genome Sequence of the Fleming Strain of Micrococcus luteus , a Simple Free-Living Actinobacterium
Young, M. R., Artsatbanov, V., Beller, H. R., Chandra, G., Chater, K. F., Dover, L. G., Goh, E.-B., Kahan, T., Kaprelyants, A. S., Kyrpides, N. C., et al. (2009) · Journal of Bacteriology · doi:10.1128/jb.01254-09 · Cited by 89
Bacterial caseinolytic proteases as novel targets for antibacterial treatment
Brötz‐Oesterhelt, H., & Saß, P. (2013) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2013.09.001 · Cited by 85
Comparison of membrane proteins of Mycobacterium tuberculosisH37Rv and H37Ra strains
Målen, H., de Souza, G. A., Pathak, S., Søfteland, T., & Wiker, H. G. (2011) · BMC Microbiology · doi:10.1186/1471-2180-11-18 · Cited by 83
Salina, E. G., Waddell, S. J., Hoffmann, N. A., Rosenkrands, I., Butcher, P. D., & Kaprelyants, A. S. (2014) · Open Biology · doi:10.1098/rsob.140106 · Cited by 85
Gene expression diversity among Mycobacterium tuberculosis clinical isolates
Gao, Q., Kripke, K. E., Saldanha, A. J., Yan, W., Holmes, S., & Small, P. M. (2005) · Microbiology · doi:10.1099/mic.0.27539-0 · Cited by 85
Regulation of proline metabolism in mycobacteria and its role in carbon metabolism under hypoxia
Berney, M., Weimar, M. R., Heikal, A., & Cook, G. M. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08053.x · Cited by 76
Benedict, M. N., Mundy, M. B., Henry, C. S., Chia, N., & Price, N. D. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003882 · Cited by 87
Kumari, M., Singh, R., & Subbarao, N. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.1989040 · Cited by 84
Kushwaha, S. K., & Shakya, M. (2009) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2009.09.029 · Cited by 85
Huang, H., Scherman, M. S., D’Haeze, W., Vereecke, D., Holsters, M., Crick, D. C., & McNeil, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504068200 · Cited by 84
Doyle, M., Gasser, R. B., Woodcroft, B. J., Hall, R. S., & Ralph, S. A. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-222 · Cited by 84
Raju, R. M., Jedrychowski, M. P., Wei, J.-R., Pinkham, J. T., Park, A. S., O’Brien, K. M., Rehren, G., Schnappinger, D., Gygi, S. P., & Rubin, E. J. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003994 · Cited by 84
Self-citationChhabra, A., Haque, A. S., Pal, R. K., Goyal, A., Rai, R., Joshi, S., Panjikar, S., Pasha, S., Sankaranarayanan, R., & Gokhale, R. S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118680109 · Cited by 84
Signaling mechanisms of the Mycobacterium tuberculosis receptor Ser/Thr protein kinases
Alber, T. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.10.017 · Cited by 90
The Cryptic Consortium, & Wilson, D. J. (2022) · PLoS Biology · doi:10.1371/journal.pbio.3001755 · Cited by 83
Shi, F., Kawai, S., Mori, S., Kono, E., & Murata, K. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04749.x · Cited by 83
Effective inhibitors of the essential kinase PknB and their potential as anti-mycobacterial agents
Lougheed, K. E. A., Osborne, S. A., SAXTY, B. A., Whalley, D. P., Chapman, T., Bouloc, N. S., Chugh, J., Nott, T. J., Patel, D., Rowlands, V., et al. (2011) · Tuberculosis · doi:10.1016/j.tube.2011.03.005 · Cited by 83
The ins and outs of Mycobacterium tuberculosis protein export
Ligon, L. S., Hayden, J., & Braunstein, M. (2011) · Tuberculosis · doi:10.1016/j.tube.2011.11.005 · Cited by 88
Shin, S. J., Wu, C.-W., Steinberg, H. N., & Talaat, A. M. (2006) · Infection and Immunity · doi:10.1128/iai.01742-05 · Cited by 83
Commandeur, S., van Meijgaarden, K. E., Prins, C., Pichugin, A. V., Dijkman, K., van den Eeden, S. J. F., Friggen, A. H., Franken, K. L. M. C., Dolganov, G., Kramnik, I., et al. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1201593 · Cited by 83
Chaudhuri, R. R., Peters, S. E., Pleasance, S. J., Northen, H., Willers, C., Paterson, G. K., Cone, D. B., Allen, A. G., Owen, P., Shalom, G., et al. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000529 · Cited by 82
Lun, S., & Bishai, W. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700035200 · Cited by 82
Seki, M., Honda, I., Fujita, I., Yano, I., Yamamoto, S., & Koyama, A. (2009) · Vaccine · doi:10.1016/j.vaccine.2009.01.034 · Cited by 82
DeJesus, M. A., & Ioerger, T. R. (2013) · BMC Bioinformatics · doi:10.1186/1471-2105-14-303 · Cited by 82
Bayesian analysis of gene essentiality based on sequencing of transposon insertion libraries
DeJesus, M. A., Zhang, Y. J., Sassetti, C. M., Rubin, E. J., Sacchettini, J. C., & Ioerger, T. R. (2013) · Bioinformatics · doi:10.1093/bioinformatics/btt043 · Cited by 82
Self-citationSchué, M., Maurin, D., Dhouib, R., N’Goma, J. B., Delorme, V., Lambeau, G. J., Carrière, F., & Canaan, S. (2010) · The FASEB Journal · doi:10.1096/fj.09-144766 · Cited by 82
Parvez, M., Qhanya, L. B., Mthakathi, N. T., Kgosiemang, I. K. R., Bamal, H. D., Pagadala, N. S., Xie, T., Yang, H., Chen, H., Theron, C. W., et al. (2016) · Scientific Reports · doi:10.1038/srep33099 · Cited by 82
Plasticity of Mycobacterium tuberculosis NADH dehydrogenases and their role in virulence
Vilchèze, C., Weinrick, B. C., Leung, L. W., & Jacobs, W. R. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1721545115 · Cited by 81
Simultaneous Analysis of Multiple Mycobacterium tuberculosis Knockdown Mutants In Vitro and In Vivo
Blumenthal, A., Trujillo, C., Ehrt, S., & Schnappinger, D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015667 · Cited by 81
Güzel-Akdemir, Ö., Maresca, A., Scozzafava, A., Salman, A., Balaban, A. T., & Supuran, C. T. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm9004016 · Cited by 81
What do microarrays really tell us about M. tuberculosis?
Kendall, S. L., Rison, S., Movahedzadeh, F., Frita, R., & Stoker, N. G. (2004) · Trends in Microbiology · doi:10.1016/j.tim.2004.10.005 · Cited by 81
Ergothioneine Is a Secreted Antioxidant in Mycobacterium smegmatis
Sao Emani, C., Williams, M. J., Wiid, I. J., Hiten, N. F., Viljoen, A. J., Pietersen, R.-D. D., van Helden, P. D., & Baker, B. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02572-12 · Cited by 81
Kim, P., Zhang, Y., Shenoy, G. G., Nguyen, Q.-A., Boshoff, H. I., Manjunatha, U. H., Goodwin, M. B., Lonsdale, J., Price, A. C., Miller, D. J., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050825p · Cited by 81
Lipid hydrolizing enzymes in virulence:Mycobacterium tuberculosisas a model system
Singh, G., Singh, G., Jadeja, D., & Kaur, J. (2010) · Critical Reviews in Microbiology · doi:10.3109/1040841x.2010.482923 · Cited by 80
Murugesan, D., Ray, P. C., Bayliss, T., Prosser, G. A., Harrison, J. R., Green, K., de Melo, C. S., Feng, T., Street, L. J., Chibale, K., et al. (2018) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.7b00275 · Cited by 80
Proteome-wide Profiling of Isoniazid Targets in Mycobacterium tuberculosis
Argyrou, A., Jin, L., Siconolfi-Baez, L., Angeletti, R. H., & Blanchard, J. S. (2006) · Biochemistry · doi:10.1021/bi061874m · Cited by 80
Kohli, S., Singh, Y., Sharma, K., Mittal, A., Ehtesham, N. Z., & Hasnain, S. E. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks465 · Cited by 78
Fortuin, S., Tomazella, G. G., Nagaraj, N., Sampson, S. L., van Pittius, N. C. G., Soares, N. C., Wiker, H. G., de Souza, G. A., & Warren, R. M. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00006 · Cited by 81
Individual Mycobacterium tuberculosis universal stress protein homologues are dispensable in vitro
Hingley‐Wilson, S., Lougheed, K. E. A., Ferguson, K., Leiva, S., & Williams, H. D. (2010) · Tuberculosis · doi:10.1016/j.tube.2010.03.013 · Cited by 80
de Wet, T. J., Winkler, K. R., Mhlanga, M., Mizrahi, V., & Warner, D. F. (2020) · eLife · doi:10.7554/elife.60083 · Cited by 79
Kato‐Maeda, M., Ho, C. S., Passarelli, B., Banaei, N., Grinsdale, J. A., Flores, L., Anderson, J., Murray, M. B., Rose, G., Kawamura, L. M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058235 · Cited by 79
Siméone, R., Bottai, D., Frigui, W., Majlessi, L., & Brosch, R. (2015) · Tuberculosis · doi:10.1016/j.tube.2015.02.019 · Cited by 79
Bedaquiline Targets the ε Subunit of Mycobacterial F-ATP Synthase
Kundu, S., Biuković, G., Grüber, G., & Dick, T. (2016) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01291-16 · Cited by 83
Novel targets in M. tuberculosis: search for new drugs
Lamichhane, G. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.10.004 · Cited by 81
Shenoy, A. R., SREENATH, N. P., Podobnik, M., Kovačević, M., & Visweswariah, S. S. (2005) · Biochemistry · doi:10.1021/bi0512391 · Cited by 81
Ladenstein, R., Fischer, M. J., & Bacher, A. (2013) · FEBS Journal · doi:10.1111/febs.12255 · Cited by 80
Lee, R. B. (2004) · Glycobiology · doi:10.1093/glycob/cwh150 · Cited by 79
Sajid, A., Arora, G., Gupta, M., Singhal, A., Chakraborty, K., Nandicoori, V. K., & Singh, Y. P. (2011) · Journal of Bacteriology · doi:10.1128/jb.05469-11 · Cited by 79
Tallman, K. R., Levine, S. R., & Beatty, K. E. (2016) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.6b00135 · Cited by 80
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Jones, G. W., Doyle, S., & Fitzpatrick, D. A. (2014) · Gene · doi:10.1016/j.gene.2014.07.065 · Cited by 79
Mycolicibacterium cell factory for the production of steroid-based drug intermediates
Zhao, A., Zhang, X., Li, Y., Wang, Z., Lv, Y., Liu, J., Alam, M. A., Xiong, W., & Xu, J. (2021) · Biotechnology Advances · doi:10.1016/j.biotechadv.2021.107860 · Cited by 80
Chen, Q., Wu, H., & Fives-Taylor, P. M. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04116.x · Cited by 78
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Rodríguez, S., Schürch, A. C., Dale, J., Lohan, A. J., Cunha, M. V., Botelho, A., de Cruz, K., Boschiroli, M.-L., Boniotti, M. B., Pacciarini, M. L., et al. (2011) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2011.09.004 · Cited by 77
Ta, P., Buchmeier, N. A., Newton, G. L., Rawat, M., & Fahey, R. C. (2011) · Journal of Bacteriology · doi:10.1128/jb.01402-10 · Cited by 78
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Sajid, A., Arora, G., Singhal, A., Kalia, V. C., & Singh, Y. P. (2015) · Annual Review of Microbiology · doi:10.1146/annurev-micro-020415-111342 · Cited by 78
Podust, L. M., von Kries, J. P., Eddine, A. N., Kim, Y., Yermalitskaya, L. V., Kühne, R., Ouellet, H., Warrier, T., Alteköster, M., Lee, J. S., et al. (2007) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00311-07 · Cited by 78
Kögler, M., Vanderhoydonck, B., Jonghe, S. D., Rozenski, J., Belle, K. V., Herman, J., Louat, T., Parchina, A., Sibley, C. H., Lescrinier, E., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm2004688 · Cited by 78
Haydel, S. E., & Clark‐Curtiss, J. E. (2004) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2004.06.010 · Cited by 78
Price, P. A., Jin, J., & Goldman, W. E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1112729109 · Cited by 77
Dubois, V., Pawlik, A., Bories, A., Moigne, V. L., Sismeiro, O., Legendre, R., Varet, H., Rodríguez-Ordóñez, M. D. P., Herrmann, J., Coppée, J., et al. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1008069 · Cited by 82
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Sasso, S., Ramakrishnan, C., Gamper, M., Hilvert, D., & Kast, P. (2004) · FEBS Journal · doi:10.1111/j.1742-4658.2004.04478.x · Cited by 77
Crystal Structure of Full-length Mycobacterium tuberculosis H37Rv Glycogen Branching Enzyme
Pal, K., Kumar, S., Sharma, S., Garg†, S. K., Alam, M. S., Xu, H. E., Agrawal, P., & Swaminathan, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.121707 · Cited by 77
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Hughes, M. A., Silva, J. C., Geromanos, S. J., & Townsend, C. A. (2005) · Journal of Proteome Research · doi:10.1021/pr050248t · Cited by 77
Lu, X., Zhang, H., Tonge, P. J., & Tan, D. S. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.07.130 · Cited by 77
Proteins unique to intraphagosomally grown Mycobacterium tuberculosis
Mattow, J., Siejak, F., Hagens, K., Becher, D., Albrecht, D., Krah, A., Schmidt, F., Jungblut, P. R., Kaufmann, S. H. E., & Schaible, U. E. (2006) · PROTEOMICS · doi:10.1002/pmic.200500547 · Cited by 77
The Antibiotic Potential of Prokaryotic IMP Dehydrogenase Inhibitors
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Gupta, A. (2008) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2008.01400.x · Cited by 77
Lehmann, J., Cheng, T., Aggarwal, A., Park, A. S., Zeiler, E., Raju, R. M., Akopian, T., Kandror, O., Bach, N., Sacchettini, J., et al. (2017) · Angewandte Chemie · doi:10.1002/anie.201709365 · Cited by 68
Self-citationA novel drug discovery concept for tuberculosis: inhibition of bacterial and host cell signalling.
Székely, R., Wáczek, F., Szabadkai, I., Németh, G., Hegymegi-Barakonyi, B., Erős, D., Szokol, B., Pató, J., Hafenbradl, D., Satchell, J. F., et al. (2008) · Immunology Letters · doi:10.1016/j.imlet.2007.12.005 · Cited by 79
Triacylglycerols: Fuelling the Hibernating Mycobacterium tuberculosis
Maurya, R. K., Bharti, S., & Krishnan, M. Y. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00450 · Cited by 76
Re-Understanding the Mechanisms of Action of the Anti-Mycobacterial Drug Bedaquiline
Sarathy, J. P., Grüber, G., & Dick, T. (2019) · Antibiotics · doi:10.3390/antibiotics8040261 · Cited by 84
Manina, G., Bellinzoni, M., Pasca, M. R., Neres, J., Milano, A., Ribeiro, A., Buroni, S., Škovierová, H., Dianišková, P., Mikušová, K., et al. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07277.x · Cited by 76
Sherrid, A. M., Rustad, T. R., Cangelosi, G. A., & Sherman, D. R. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011622 · Cited by 76
The complex architecture of mycobacterial promoters
Newton-Foot, M., & van Pittius, N. C. G. (2012) · Tuberculosis · doi:10.1016/j.tube.2012.08.003 · Cited by 83
Genes Required for Intrinsic Multidrug Resistance in Mycobacterium avium
Philalay, J. S., Palermo, C. O., Hauge, K. A., Rustad, T. R., & Cangelosi, G. A. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.9.3412-3418.2004 · Cited by 76
Schmitz, K. R., & Sauer, R. T. (2014) · Molecular Microbiology · doi:10.1111/mmi.12694 · Cited by 76
Adenylating Enzymes in Mycobacterium tuberculosis as Drug Targets
Duckworth, B. P., Nelson, K. M., & Aldrich, C. C. (2012) · Current Topics in Medicinal Chemistry · doi:10.2174/156802612799984571 · Cited by 76
Mycobacterium Tuberculosis: Drug Resistance and Future Perspectives
Riccardi, G., Pasca, M. R., & Buroni, S. (2009) · Future Microbiology · doi:10.2217/fmb.09.20 · Cited by 77
McEvoy, C., van Helden, P. D., Warren, R. M., & van Pittius, N. C. G. (2009) · BMC Evolutionary Biology · doi:10.1186/1471-2148-9-237 · Cited by 76
Ribosomal mutations promote the evolution of antibiotic resistance in a multidrug environment
Gomez, J. E., Kaufmann-Malaga, B., Wivagg, C. N., Kim, P. B., Silvis, M. R., Renedo, N., Ioerger, T. R., Ahmad, R., Livny, J., Fishbein, S. R. S., et al. (2017) · eLife · doi:10.7554/elife.20420 · Cited by 71
The plasmid-mediated evolution of the mycobacterial ESX (Type VII) secretion systems
Newton-Foot, M., Warren, R. M., Sampson, S. L., van Helden, P. D., & Gey van Pittius, N. C. (2016) · BMC Evolutionary Biology · doi:10.1186/s12862-016-0631-2 · Cited by 75
Identification and validation of novel drug targets in Mycobacterium tuberculosis
Singh, V., & Mizrahi, V. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.09.010 · Cited by 75
Yan, M., Li, S., Ding, X.-Y., Guo, X.-P., Jin, Q., & Sun, Y. (2020) · mBio · doi:10.1128/mbio.02364-19 · Cited by 75
The survival kit of Mycobacterium tuberculosis
Warner, D. F., & Mizrahi, V. (2007) · Nature Medicine · doi:10.1038/nm0307-282 · Cited by 74
Zou, P., Chang, M. X., Xue, N., Liu, X. Q., Li, J. H., Fu, J. P., Chen, S. N., & Nie, P. (2013) · Immunology · doi:10.1111/imm.12179 · Cited by 74
Leodolter, J., Warweg, J., & Weber-Ban, E. U. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125345 · Cited by 75
Sampathkumar, P., Turley, S., Ulmer, J. E., Rhie, H. G., Sibley, C. H., & Hol, W. G. J. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.07.071 · Cited by 75
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Self-citationMetaferia, B. B., Fetterolf, B., Shahzad‐ul‐Hussan, S., Moravec, M. D., Smith, J. A., Ray, S., Gutierrez‐Lugo, M., & Bewley, C. A. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm070669h · Cited by 74
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Metadata
- Authors
- Sassetti, C. M., Boyd, D. H., & Rubin, E. J.
- Affiliations
- Harvard University (US)
- Corresponding author
- Rubin, Eric J.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2003-03-25
- Volume
- 48
- Issue
- 1
- Pages
- 77-84
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2128482141
- Cited by
- 2,544
- References
- 25
- Citations by year
- 2026: 43 · 2025: 71 · 2024: 99 · 2023: 77 · 2022: 87 · 2021: 94 · 2020: 114 · 2019: 137 · 2018: 111 · 2017: 129 · 2016: 129 · 2015: 154 · 2014: 149 · 2013: 154 · 2012: 128
- FWCI
- 45.74
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Damon Runyon Cancer Research Foundation
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (AI 48704, R01AI048704, R01AI051929, AI51929)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Epidemiology › Mycobacterium research and diagnosis
- Keywords
- Mycobacterium tuberculosis, Mycobacterium leprae, essential genes, bacterial growth, gene essentiality, drug resistance, gene loss, minimal gene set, orthologs
- MeSH terms
- DNA Transposable Elements, Genes, Bacterial, Mycobacterium leprae, Mycobacterium tuberculosis, Mutagenesis, Evolution, Molecular
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