The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Genes required for mycobacterial growth defined by high density mutagenesis
Open accessAbstract
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.
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
“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]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“The F1Fo-ATP synthase in M. tuberculosis and M. smegmatis has been shown to be essential for optimal growth (29, 103).”
From Energetics of Respiration and Oxidative Phosphorylation in Mycobacteria (2014) · cites this paper as [29]
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
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
Sorted by citations
Items 301–400 of 1,003
Manson, A. L., Weiner, B., Park, S. T., Wapinski, I., Raman, S., Dolganov, G., Peterson, M., Riley, R. W., Zucker, J., Abeel, T., et al. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-120 · Cited by 102
Natural Product-Based Phenols as Novel Probes for Mycobacterial and Fungal Carbonic Anhydrases
Davis, R. A., Hofmann, A., Osman, A., Hall, R. A., Mühlschlegel, F. A., Vullo, D., Innocenti, A., Supuran, C. T., & Poulsen, S. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm1013242 · Cited by 102
Veyrier, F. J., Pletzer, D., Turenne, C. Y., & Behr, M. A. (2009) · BMC Evolutionary Biology · doi:10.1186/1471-2148-9-196 · Cited by 102
Harrison, A. J., Yu, M., Gårdenborg, T., Middleditch, M., Ramsay, R. J., Baker, E. N., & Lott, J. S. (2006) · Journal of Bacteriology · doi:10.1128/jb.00338-06 · Cited by 102
Identifying Essential Genes in Mycobacterium tuberculosis by Global Phenotypic Profiling
Long, J. E., DeJesus, M. A., Ward, D. V., Baker, R. E., Ioerger, T. R., & Sassetti, C. M. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2398-4_6 · Cited by 101
Self-citationSingh, V., Donini, S., Pacitto, A., Sala, C., Hartkoorn, R. C., Dhar, N., Kéri, G., Ascher, D. B., Mondésert, G., Vocat, A., et al. (2016) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.6b00102 · Cited by 101
Microbe Profile: Mycobacterium tuberculosis: Humanity's deadly microbial foe
Gordon, S. V., & Parish, T. (2018) · Microbiology · doi:10.1099/mic.0.000601 · Cited by 101
Mycobacterium tuberculosis Pathogenesis, Infection Prevention and Treatment
Miggiano, R., Rizzi, M., & Ferraris, D. M. (2020) · Pathogens · doi:10.3390/pathogens9050385 · Cited by 101
Prosser, G. A., & de Carvalho, L. P. S. (2013) · FEBS Journal · doi:10.1111/febs.12108 · Cited by 101
Type VII Secretion: A Highly Versatile Secretion System
Ates, L. S., Houben, E. N. G., & Bitter, W. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.vmbf-0011-2015 · Cited by 100
Macheras, E., Roux, A., Neulat-Ripoll, F., Sivadon‐Tardy, V., Gutierrez, C., Gaillard, J., & Heym, B. (2009) · Journal of Clinical Microbiology · doi:10.1128/jcm.00037-09 · Cited by 100
Bedaquiline: Current status and future perspectives
Khoshnood, S., Goudarzi, M., Taki, E., Darbandi, A., Kouhsari, E., Heidary, M., Motahar, M., Moradi, M., & Bazyar, H. (2021) · Journal of Global Antimicrobial Resistance · doi:10.1016/j.jgar.2021.02.017 · Cited by 100
Lea‐Smith, D. J., Pyke, J. S., Tull, D., McConville, M. J., Coppel, R. L., & Crellin, P. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608686200 · Cited by 100
Kim, J.-H., Wei, J.-R., Wallach, J. B., Robbins, R. S., Rubin, E. J., & Schnappinger, D. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1149 · Cited by 100
Self-citationHickey, T. B. M., Thorson, L., Speert, D. P., Daffé, M., & Stokes, R. W. (2009) · Infection and Immunity · doi:10.1128/iai.00143-09 · Cited by 100
Natural Products, Small Molecules, and Genetics in Tuberculosis Drug Development
Gutierrez‐Lugo, M., & Bewley, C. A. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm070719i · Cited by 101
Molecular Genetics of Mycobacteriophages
Hatfull, G. F. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.mgm2-0032-2013 · Cited by 100
Targeting bacterial energetics to produce new antimicrobials
Hards, K., & Cook, G. M. (2017) · Drug Resistance Updates · doi:10.1016/j.drup.2017.11.001 · Cited by 102
Haagsma, A. C., Driessen, N. N., Hahn, M., Lill, H., & Bald, D. (2010) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2010.02123.x · Cited by 102
The Complex Mechanism of Antimycobacterial Action of 5-Fluorouracil
Singh, V., Brecik, M., Mukherjee, R., Evans, J. C., Svetlíková, Z., Blaško, J., Surade, S. B., Blackburn, J. M., Warner, D. F., Mikušová, K., et al. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.11.006 · Cited by 96
Marri, P. R., Bannantine, J. P., & Golding, G. B. (2006) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00041.x · Cited by 107
Nguyen, H. T., Wolff, K., Cartabuke, R. H., Ogwang, S., & Nguyen, L. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07110.x · Cited by 101
Minato, Y., Thiede, J. M., Kordus, S. L., McKlveen, E. J., Turman, B. J., & Baughn, A. D. (2015) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00647-15 · Cited by 98
Serine threonine protein kinases of mycobacterial genus: phylogeny to function
Narayan, A., Sachdeva, P., Sharma, K., Saini, A. K., Tyagi, A. K., & Singh, Y. P. (2006) · Physiological Genomics · doi:10.1152/physiolgenomics.00221.2006 · Cited by 99
Goldman, R. C. (2013) · Tuberculosis · doi:10.1016/j.tube.2013.09.003 · Cited by 94
Saint‐Joanis, B., Demangel, C., Jackson, M., Brodin, P. M., Marsollier, L., Boshoff, H. I., & Cole, S. T. (2006) · Journal of Bacteriology · doi:10.1128/jb.00631-06 · Cited by 97
Buchmeier, N. A., Newton, G. L., & Fahey, R. C. (2006) · Journal of Bacteriology · doi:10.1128/jb.00393-06 · Cited by 97
The impact of genomics on vaccine design
Scarselli, M., Giuliani, M. M., Adu‐Bobie, J., Pizza, M., & Rappuoli, R. (2004) · Trends in biotechnology · doi:10.1016/j.tibtech.2004.12.008 · Cited by 96
Clinical value of whole-genome sequencing of Mycobacterium tuberculosis
Takiff, H. E., & Feo, O. (2015) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(15)00071-7 · Cited by 96
The Mycobacterium tuberculosis cytochrome P450 system
Ouellet, H., Johnston, J. B., & de Montellano, P. R. O. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.07.011 · Cited by 98
Biosynthesis of mycobacterial lipids by polyketide synthases and beyond
Quadri, L. E. N. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2014.896859 · Cited by 95
Kawai, S., & Murata, K. (2008) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.70738 · Cited by 96
The Mycobacterium tuberculosis ino1 gene is essential for growth and virulence
Movahedzadeh, F., Smith, D. A., Norman, R. A., Dinadayala, P., Murray‐Rust, J., Russell, D. G., Kendall, S. L., Rison, S. C. G., McAlister, M. S. B., Bancroft, G. J., et al. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03900.x · Cited by 96
Hervás‐Stubbs, S., Majlessi, L., Simsova, M., Morová, J., Rojas, M.-J., Nouzé, C., Brodin, P. M., Šebo, P., & Leclerc, C. (2006) · Infection and Immunity · doi:10.1128/iai.02086-05 · Cited by 96
Structure/Function Studies of Ser/Thr and Tyr Protein Phosphorylation in Mycobacterium tuberculosis
Greenstein, A. E., Grundner, C., Echols, N., Gay, L. M., Lombana, T. N., Miecskowski, C. A., Pullen, K. E., Sung, P.-Y., & Alber, T. (2005) · Microbial Physiology · doi:10.1159/000089645 · Cited by 102
Stanley, S. A., Kawate, T., Iwase, N., Shimizu, M., Clatworthy, A. E., Kazyanskaya, E., Sacchettini, J. C., Ioerger, T. R., Siddiqi, N., Minami, S., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302114110 · Cited by 95
Self-citationA vitamin B 12 transporter in Mycobacterium tuberculosis
Gopinath, K., Venclovas, Č., Ioerger, T. R., Sacchettini, J. C., McKinney, J. D., Mizrahi, V., & Warner, D. F. (2013) · Open Biology · doi:10.1098/rsob.120175 · Cited by 95
The nonredundant roles of two 4′-phosphopantetheinyl transferases in vital processes of Mycobacteria
Chalut, C., Botella, L., d’Auria, C. D. S., Houssin, C., & Guilhot, C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511129103 · Cited by 92
A Redox Regulatory System Critical for Mycobacterial Survival in Macrophages and Biofilm Development
Wolff, K., de la Peña, A. H., Nguyen, H. T., Pham, T. H., Amzel, L. M., Gabelli, S. B., & Nguyen, L. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004839 · Cited by 91
Xavier, J. C., Patil, K. R., & Rocha, I. (2016) · Metabolic Engineering · doi:10.1016/j.ymben.2016.12.002 · Cited by 94
Comprehensive analysis of iron utilization by Mycobacterium tuberculosis
Zhang, L., Hendrickson, R. C., Meikle, V., Lefkowitz, E. J., Ioerger, T. R., & Niederweis, M. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008337 · Cited by 94
Improved tetracycline repressors for gene silencing in mycobacteria
Klotzsche, M., Ehrt, S., & Schnappinger, D. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp015 · Cited by 94
Cappelli, G., Volpe, E., Grassi, M., Liseo, B., Colizzi, V., & Mariani, F. (2006) · Research in Microbiology · doi:10.1016/j.resmic.2005.10.007 · Cited by 94
Bashiri, G., Squire, C. J., Moreland, N. J., & Baker, E. N. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801854200 · Cited by 93
Release of mycobacterial antigens
Majlessi, L., Prados‐Rosales, R., Casadevall, A., & Brosch, R. (2015) · Immunological Reviews · doi:10.1111/imr.12251 · Cited by 93
Prosser, G. A., & de Carvalho, L. P. S. (2013) · ACS Medicinal Chemistry Letters · doi:10.1021/ml400349n · Cited by 93
Negatu, D. A., Yamada, Y., Xi, Y., Go, M., Zimmerman, M. D., Ganapathy, U. S., Dartois, V. A., Gengenbacher, M., & Dick, T. (2019) · mBio · doi:10.1128/mbio.02781-18 · Cited by 97
Structure, function and selective inhibition of bacterial acetyl-coa carboxylase
Polyak, S. W., Abell, A. D., Wilce, M. C. J., Zhang, L., & Booker, G. W. (2011) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-011-3796-z · Cited by 91
Fivian-Hughes, A. S., Houghton, J., & Davis, E. O. (2011) · Microbiology · doi:10.1099/mic.0.053983-0 · Cited by 93
Detecting selection using a single genome sequence of M. tuberculosis and P. falciparum
Plotkin, J. B., Dushoff, J. G., & Fraser, H. B. (2004) · Nature · doi:10.1038/nature02458 · Cited by 96
Schmitz, K. R., Carney, D. W., Sello, J. K., & Sauer, R. T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417120111 · Cited by 92
Pasca, M. R., Degiacomi, G., Ribeiro, A., Zara, F., Mori, P. D., Heym, B., Mirrione, M., Brerra, R., Pagani, L., Pucillo, L. P., et al. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01676-09 · Cited by 92
Recent insights into the genotype–phenotype relationship from massively parallel genetic assays
Kemble, H. E., Nghe, P., & Tenaillon, O. (2019) · Evolutionary Applications · doi:10.1111/eva.12846 · Cited by 94
Enzymology of mammalian NAD metabolism in health and disease
Magni, G. (2008) · Frontiers in bioscience · doi:10.2741/3143 · Cited by 93
Alderwick, L. J., Birch, H. L., Mishra, A. K., Eggeling, L., & Besra, G. S. (2007) · Biochemical Society Transactions · doi:10.1042/bst0351325 · Cited by 92
Solution Structure of the Mycobacterium tuberculosis EsxG·EsxH Complex
Ilghari, D., Lightbody, K. L., Veverka, V., Waters, L. C., Muskett, F. W., Renshaw, P. S., & Carr, M. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.248732 · Cited by 92
Bartek, I. L., Woolhiser, L. K., Baughn, A. D., Basaraba, R. J., Jacobs, W. R., Lenaerts, A. J. M., & Voskuil, M. I. (2014) · mBio · doi:10.1128/mbio.01106-14 · Cited by 94
Mills, J. A., Motichka, K., Jucker, M., Wu, H. P., Uhlik, B. C., Stern, R. J., Scherman, M. S., Vissa, V., Pan, F., Kundu, M., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407782200 · Cited by 91
Novel role of Wag31 in protection of mycobacteria under oxidative stress
Mukherjee, P., Sureka, K., Datta, P., Hossain, T., Barik, S., Das, K. P., Kundu, M., & Basu, J. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06750.x · Cited by 88
Luckner, S. R., Machutta, C. A., Tonge, P. J., & Kisker, C. (2009) · Structure · doi:10.1016/j.str.2009.04.012 · Cited by 91
Tubercle bacilli rely on a type VII army for pathogenicity
Stoop, E. J. M., Bitter, W., & van der Sar, A. M. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2012.07.001 · Cited by 90
Gasse, C., Douguet, D., Huteau, V., Marchal, G., Munier‐Lehmann, H., & Pochet, S. (2008) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2008.04.045 · Cited by 90
Kolly, G. S., Boldrin, F., Sala, C., Dhar, N., Hartkoorn, R. C., Ventura, M., Serafini, A., McKinney, J. D., Manganelli, R., & Cole, S. T. (2014) · Molecular Microbiology · doi:10.1111/mmi.12546 · Cited by 90
Vitamin B6 biosynthesis is essential for survival and virulence of Mycobacterium tuberculosis
Dick, T., Manjunatha, U. H., Kappes, B., & Gengenbacher, M. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07381.x · Cited by 93
Targeting the Proteostasis Network for Mycobacterial Drug Discovery
Lupoli, T. J., Vaubourgeix, J., Burns-Huang, K. E., & Gold, B. S. (2018) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.7b00231 · Cited by 91
Evolution and emergence ofMycobacterium tuberculosis
Orgeur, M., Sous, C., Madacki, J., & Brosch, R. (2024) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuae006 · Cited by 97
Brown, A. K., Papaemmanouil, A., Bhowruth, V., Bhatt, A., Dover, L. G., & Besra, G. S. (2007) · Microbiology · doi:10.1099/mic.0.2007/009936-0 · Cited by 89
Bordes, P., Cirinesi, A.-M., Ummels, R., Sala, A. J., Sakr, S., Bitter, W., & Genevaux, P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101189108 · Cited by 90
Downing, K. J., Betts, J. C., Young, D. I., McAdam, R. A., Kelly, F., Young, M., & Mizrahi, V. (2004) · Tuberculosis · doi:10.1016/j.tube.2003.12.004 · Cited by 89
Jones, G., & Dyson, P. (2006) · Journal of Bacteriology · doi:10.1128/jb.00800-06 · Cited by 96
Pyrimidine Salvage Pathway in Mycobacterium tuberculosis
Villela, A. D., Sánchez-Quitian, Z. A., Ducati, R. G., Santos, D. S., & Basso, L. A. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711795029555 · Cited by 88
Famulla, K., Saß, P., Malik, I. T., Akopian, T. N., Kandror, O., Alber, M., Hinzen, B., Ruebsamen‐Schaeff, H., Kalscheuer, R., Goldberg, A. L., et al. (2016) · Molecular Microbiology · doi:10.1111/mmi.13362 · Cited by 89
Lead Optimization of 1,4-Azaindoles as Antimycobacterial Agents
Shirude, P. S., Shandil, R. K., Manjunatha, M. R., Sadler, C., Panda, M., Panduga, V., Reddy, J., Saralaya, R., Nanduri, R., Ambady, A., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500571f · Cited by 89
van Opijnen, T., Lazinski, D. W., & Camilli, A. (2014) · Current Protocols in Molecular Biology · doi:10.1002/0471142727.mb0716s106 · Cited by 92
AdnAB: a new DSB-resecting motor–nuclease from mycobacteriaPreprint
Sinha, K. M., Unciuleac, M.-C., Glickman, M. S., & Shuman, S. (2009) · Genes & Development · doi:10.1101/gad.1805709 · Cited by 89
Gandotra, S., Lebron, M. B., & Ehrt, S. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001040 · Cited by 88
Breaking down the cell wall: Still an attractive antibacterial strategy
Zhou, J., Cai, Y., Liu, Y., An, H., Deng, K., Ashraf, M. A., Zou, L., & Wang, J. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.952633 · Cited by 99
Mishra, A. K., Alderwick, L. J., Rittmann, D., Tatituri, R. V. V., Nigou, J., Gilleron, M., Eggeling, L., & Besra, G. S. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05884.x · Cited by 88
Gago, G., Kurth, D. G., Diacovich, L., Tsai, S., & Gramajo, H. C. (2005) · Journal of Bacteriology · doi:10.1128/jb.188.2.477-486.2006 · Cited by 88
Calamita, H., Ko, C. G., Tyagi, S. K., Yoshimatsu, T., Morrison, N. E., & Bishai, W. R. (2004) · Cellular Microbiology · doi:10.1111/j.1462-5822.2004.00454.x · Cited by 88
Stall no more at polyproline stretches with the translation elongation factors EF‐P and IF‐5A
Lassak, J., Wilson, D. N., & Jung, K. (2015) · Molecular Microbiology · doi:10.1111/mmi.13233 · Cited by 88
A review on host–pathogen interactions: classification and prediction
Sen, R., Nayak, L., & De, R. K. (2016) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/s10096-016-2716-7 · Cited by 91
Redox Biology of Tuberculosis Pathogenesis
Trivedi, A., Singh, N., Bhat, S. A., Gupta, P., & Kumar, A. (2012) · Advances in Microbial Physiology · doi:10.1016/b978-0-12-398264-3.00004-8 · Cited by 88
Mycobacterial Esx-3 Requires Multiple Components for Iron Acquisition
Siegrist, M. S., Steigedal, M., Ahmad, R., Mehra, A., Dragset, M. S., Schuster, B. M., Philips, J. A., Carr, S. A., & Rubin, E. J. (2014) · mBio · doi:10.1128/mbio.01073-14 · Cited by 87
Self-citationGinda, K., Bezulska‐Ditkowska, M., Ziolkiewicz, M., Dziadek, J., Zakrzewska‐Czerwińska, J., & Jakimowicz, D. (2013) · Molecular Microbiology · doi:10.1111/mmi.12146 · Cited by 92
The Molecular Genetics of Mycolic Acid Biosynthesis
Pawełczyk, J., & Kremer, L. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.mgm2-0003-2013 · Cited by 94
Ates, L. S., van der Woude, A. D., Bestebroer, J., van Stempvoort, G., Musters, R. J. P., García-Vallejo, J. J., Picavet, D. I., van de Weerd, R., Maletta, M., Kuijl, C. P., et al. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005696 · Cited by 91
Respiratory ATP synthesis: the new generation of mycobacterial drug targets?
Bald, D., & Koul, A. (2010) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2010.01959.x · Cited by 87
M. tuberculosis Ser/Thr Protein Kinase D Phosphorylates an Anti-Anti–Sigma Factor Homolog
Greenstein, A. E., MacGurn, J. A., Baer, C. E., Falick, A. M., Cox, J. S., & Alber, T. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030049 · Cited by 89
Zhao, F., Wang, X.-D., Erber, L. N., Luo, M., Guo, A.-Z., Yang, S.-S., Gu, J., Turman, B. J., Gao, Y.-R., Li, D., et al. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01775-13 · Cited by 87
Krajewski, W. W., Jones, T. A., & Mowbray, S. L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502248102 · Cited by 87
Bentley, S. D., Corton, C. H., Brown, S. E., Barron, A., Clark, L., Doggett, J., Harris, B. R., Ormond, D., Quail, M. A., May, G., et al. (2008) · Journal of Bacteriology · doi:10.1128/jb.01598-07 · Cited by 87
Harris, N. C., Sato, M., Herman, N. A., Twigg, F. F., Cai, W., Liu, J., Zhu, X., Downey, J., Khalaf, R., Martin, J., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1705016114 · Cited by 87
Inhibition of the β-class carbonic anhydrases fromMycobacterium tuberculosiswith carboxylic acids
Maresca, A., Vullo, D., Scozzafava, A., Manole, G., & Supuran, C. T. (2012) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2011.650168 · Cited by 86
Conformational control of the bacterial Clp protease by natural product antibiotics
Malik, I. T., & Brötz‐Oesterhelt, H. (2017) · Natural Product Reports · doi:10.1039/c6np00125d · Cited by 86
Côtes, K., Dhouib, R., Douchet, I., Chahinian, H., Caro, A. M. D., Carrière, F., & Canaan, S. (2007) · Biochemical Journal · doi:10.1042/bj20070745 · Cited by 86
Expansion of the mycobacterial “PUPylome”
Watrous, J. D., Burns, K. E., Liu, W.-T., Patel, A. D., HOOK, V. Y. H., Bafna, V., Barry, C. E., Bark, S., & Dorrestein, P. C. (2009) · Molecular BioSystems · doi:10.1039/b916104j · Cited by 86
Warner, D. F., Savvi, S., Mizrahi, V., & Dawes, S. S. (2007) · Journal of Bacteriology · doi:10.1128/jb.00040-07 · Cited by 86
Sukheja, P., Kumar, P., Mittal, N., Li, S.-G., Singleton, E., Russo, R., Perryman, A. L., Shrestha, R., Awasthi, D., Husain, S., et al. (2017) · mBio · doi:10.1128/mbio.02022-16 · Cited by 86
Toxin–antitoxin systems and regulatory mechanisms in Mycobacterium tuberculosis
Slayden, R. A., Dawson, C. C., & Cummings, J. E. (2018) · Pathogens and Disease · doi:10.1093/femspd/fty039 · Cited by 82
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
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