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 201–300 of 1,003
Resistance mechanisms of Mycobacterium tuberculosis against phagosomal copper overload
Rowland, J. L., & Niederweis, M. (2012) · Tuberculosis · doi:10.1016/j.tube.2011.12.006 · Cited by 131
Seidel, M., Alderwick, L. J., Birch, H. L., Sahm, H., Eggeling, L., & Besra, G. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700271200 · Cited by 131
The role of IS6110 in the evolution of Mycobacterium tuberculosis
McEvoy, C. R. E., Falmer, A. A., van Pittius, N. C. G., Victor, T. C., van Helden, P. D., & Warren, R. M. (2007) · Tuberculosis · doi:10.1016/j.tube.2007.05.010 · Cited by 136
The molecular mechanism of bacterial lipoprotein modification—How, when and why?
Buddelmeijer, N. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuu006 · Cited by 132
Validation of the Essential ClpP Protease in Mycobacterium tuberculosis as a Novel Drug Target
Ollinger, J., O’Malley, T., Kesicki, E. A., Odingo, J. O., & Parish, T. (2011) · Journal of Bacteriology · doi:10.1128/jb.06142-11 · Cited by 136
Developmental biology ofStreptomycesfrom the perspective of 100 actinobacterial genome sequences
Chandra, G., & Chater, K. F. (2013) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12047 · Cited by 132
Stucki, D., Malla, B., Hostettler, S. M., Huna, T., Feldmann, J., Yeboah‐Manu, D., Borrell, S., Fenner, L., Comas, I., Coscollá, M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041253 · Cited by 136
Genomewide Assessment of Mycobacterium tuberculosis Conditionally Essential Metabolic Pathways
Minato, Y., Gohl, D. M., Thiede, J. M., Chacón, J. M., Harcombe, W. R., Maruyama, F., & Baughn, A. D. (2019) · mSystems · doi:10.1128/msystems.00070-19 · Cited by 127
Prospects for new antitubercular drugs
Duncan, K., & Barry, C. E. (2004) · Current Opinion in Microbiology · doi:10.1016/j.mib.2004.08.011 · Cited by 132
The Role of Selection in Shaping Diversity of Natural M. tuberculosis Populations
Pepperell, C. S., Casto, A. M., Kitchen, A., Granka, J. M., Cornejo, O. E., Holmes, E. C., Birren, B. W., Galagan, J. E., & Feldman, M. W. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003543 · Cited by 133
Pathway-Selective Sensitization of Mycobacterium tuberculosis for Target-Based Whole-Cell Screening
Abrahams, G. L., Kumar, A., Savvi, S., Hung, A. W., Wen, S., Abell, C., Barry, C. E., Sherman, D. R., Boshoff, H. I., & Mizrahi, V. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.05.020 · Cited by 127
The Secret Lives of Mycobacteriophages
Hatfull, G. F. (2012) · Advances in virus research · doi:10.1016/b978-0-12-394621-8.00015-7 · Cited by 131
Satta, G., Lipman, M. C. I., Smith, G. P., Arnold, C., Kon, O. M., & McHugh, T. D. (2017) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2017.10.030 · Cited by 131
A genetic locus required for iron acquisition in Mycobacterium tuberculosis
Krithika, R., Marathe, U., Saxena, P., Ansari, M. Z., Mohanty, D., & Gokhale, R. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507924103 · Cited by 129
Zvi, A., Ariel, N., Fulkerson, J., SADOFF, J. C., & Avigdor Shafferman, C. (2008) · BMC Medical Genomics · doi:10.1186/1755-8794-1-18 · Cited by 129
Cook, G. M., Hards, K., Dunn, E. A., Heikal, A., Nakatani, Y., Greening, C., Crick, D. C., Fontes, F. L., Pethe, K., Hasenoehrl, E., et al. (2017) · Microbiology Spectrum · doi:10.1128/microbiolspec.tbtb2-0014-2016 · Cited by 131
Structural Basis of Mycobacterial Inhibition by Cyclomarin A
Vasudevan, D., Rao, S. P. S., & Noble, C. G. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.493767 · Cited by 129
Schnoes, A. M., Ream, D. C., Thorman, A. W., Babbitt, P. C., & Friedberg, I. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003063 · Cited by 129
Xu, J., Laine, O., Masciocchi, M., Manoranjan, J., Smith, J., Du, S., Edwards, N., Zhu, X., Fenselau, C., & Gao, L. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05959.x · Cited by 127
Papavinasasundaram, K. G., Chan, B. H. Y., Chung, J.-H., Colston, M. J., Davis, E. O., & Av‐Gay, Y. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.16.5751-5760.2005 · Cited by 129
Increasing the structural coverage of tuberculosis drug targets
Baugh, L., Phan, I. Q., Begley, D. W., Clifton, M. C., Armour, B. L., Dranow, D. M., Taylor, B. M., Muruthi, M. M., Abendroth, J. A., Fairman, J. W., et al. (2014) · Tuberculosis · doi:10.1016/j.tube.2014.12.003 · Cited by 128
The DprE1 enzyme, one of the most vulnerable targets of Mycobacterium tuberculosis
Riccardi, G., Pasca, M. R., Chiarelli, L. R., Manina, G., Mattevi, A., & Binda, C. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-5218-x · Cited by 130
McLean, K. J., Carroll, P., Lewis, D. G., Dunford, A. J., Seward, H. E., Neeli, R., Cheesman, M. R., Marsollier, L., Douglas, P., Smith, W. E., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802115200 · Cited by 128
Smith, L. J., Stapleton, M. R., Fullstone, G., Crack, J. C., THOMSON, A. J., Brun, N. E. L., Hunt, D. M., Harvey, E., Adinolfi, S., Buxton, R. S., et al. (2010) · Biochemical Journal · doi:10.1042/bj20101440 · Cited by 128
Hubin, E. A., Fay, A., Xu, C. K., Bean, J. M., Saecker, R. M., Glickman, M. S., Darst, S. A., & Campbell, E. A. (2017) · eLife · doi:10.7554/elife.22520 · Cited by 122
Zoraghi, R., Worrall, L. J., See, R. H., Strangman, W. K., Popplewell, W. L., Gong, H., Samaai, T., Swayze, R. D., Kaur, S., Vuckovic, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.289033 · Cited by 130
Iron Acquisition in Mycobacterium tuberculosis
Chao, A., Sieminski, P. J., Owens, C. P., & Goulding, C. W. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00285 · Cited by 130
The pan-genome: towards a knowledge-based discovery of novel targets for vaccines and antibacterials
Muzzi, A., Masignani, V., & Rappuoli, R. (2007) · Drug Discovery Today · doi:10.1016/j.drudis.2007.04.008 · Cited by 127
Crystal structure of LeuA from Mycobacterium tuberculosis , a key enzyme in leucine biosynthesis
Koon, N., Squire, C. J., & Baker, E. N. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400820101 · Cited by 127
Energetics of Pathogenic Bacteria and Opportunities for Drug Development
Cook, G. M., Greening, C., Hards, K., & Berney, M. (2014) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2014.08.001 · Cited by 129
Mathys, V., Wintjens, R. T., Lefevre, P., Bertout, J., Singhal, A., Kiass, M., Kurepina, N. E., Wang, X., Mathema, B., Baulard, A. R., et al. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01197-08 · Cited by 126
A new twist on an old pathway – accessory secretion systems
Rigel, N. W., & Braunstein, M. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06294.x · Cited by 126
ClpP Protease, a Promising Antimicrobial Target
Moreno-Cinos, C., Goossens, K., Salado, I. G., der Veken, P. V., Winter, H. L. D., & Augustyns, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092232 · Cited by 125
Brown, A. C., & Parish, T. (2008) · BMC Microbiology · doi:10.1186/1471-2180-8-78 · Cited by 126
Bhatt, A., Kremer, L., Dai, A. Z., Sacchettini, J. C., & Jacobs, W. R. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.22.7596-7606.2005 · Cited by 127
Interference of Mycobacterium tuberculosis cell division by Rv2719c, a cell wall hydrolase
Chauhan, A., Lofton, H., Maloney, E., Moore, J., Fol, M., Madiraju, M. V. V. S., & Rajagopalan, M. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05333.x · Cited by 116
Sun, J., Singh, V., Lau, A., Stokes, R. W., Obregón‐Henao, A., Orme, I. M., Wong, D., Av‐Gay, Y., & Hmama, Z. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003499 · Cited by 126
Sharma, G., Upadhyay, S., Srilalitha, M., Nandicoori, V. K., & Khosla, S. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv261 · Cited by 123
Raman, S., Hazra, R., Dascher, C. C., & Husson, R. N. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.19.6605-6616.2004 · Cited by 124
Moreira, W., Ngan, G., Low, J. L., Poulsen, A., Chia, B. C. S., Ang, M. J. Y., Yap, A., Fulwood, J., Lakshmanan, U., Lim, J., et al. (2015) · mBio · doi:10.1128/mbio.00253-15 · Cited by 119
Self-citationIshizaki, Y., Hayashi, C., Inoue, K., Igarashi, M., Takahashi, Y., Pujari, V., Crick, D. C., Brennan, P. J., & Nomoto, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.492173 · Cited by 121
Mycobacteriophages: Genes and Genomes
Hatfull, G. F. (2010) · Annual Review of Microbiology · doi:10.1146/annurev.micro.112408.134233 · Cited by 121
Zemansky, J., Kline, B. C., Woodward, J. J., Leber, J. H., Marquis, H., & Portnoy, D. A. (2009) · Journal of Bacteriology · doi:10.1128/jb.00016-09 · Cited by 121
Recent advancements in the development of anti-tuberculosis drugs
Chetty, S., Ramesh, M., Singh, P., & Soliman, M. E. S. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.11.084 · Cited by 123
Insights on biology and evolution from microbial genome sequencingPreprint
Fraser, C. M. (2005) · Genome Research · doi:10.1101/gr.3724205 · Cited by 119
Proteasomal Control of Cytokinin Synthesis Protects Mycobacterium tuberculosis against Nitric Oxide
Samanovic, M. I., Tu, S., Novák, O., Iyer, L. M., McAllister, F. E., Aravind, L., Gygi, S. P., Hubbard, S. R., Strnad, M., & Darwin, K. H. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.024 · Cited by 119
Mycobacterium tuberculosis Serine/Threonine Protein Kinases
Prišić, S., & Husson, R. N. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.mgm2-0006-2013 · Cited by 117
Chawla, Y. K., Upadhyay, S., Khan, S., Nagarajan, S. N., Forti, F., & Nandicoori, V. K. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.563536 · Cited by 118
Beste, D. J. V., Bonde, B. K., Hawkins, N. D., Ward, J. L., Beale, M. H., Noack, S., Nöh, K., Kruger, N. J., Ratcliffe, R. G., & McFadden, J. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002091 · Cited by 119
Wehenkel, A., Fernandez, P., Bellinzoni, M., Catherinot, V., Barilone, N., Labesse, G., Jackson, M., & Alzari, P. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.04.046 · Cited by 121
Silencing Essential Protein Secretion in Mycobacterium smegmatis by Using Tetracycline Repressors
Guo, X. V., Monteleone, M. M., Klotzsche, M., Kamionka, A., Hillen, W., Braunstein, M., Ehrt, S., & Schnappinger, D. (2007) · Journal of Bacteriology · doi:10.1128/jb.00216-07 · Cited by 118
Carta, F., Maresca, A., Covarrubias, A. S., Mowbray, S. L., Jones, T. A., & Supuran, C. T. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.10.009 · Cited by 119
Bai, G., McCue, L. A., & McDonough, K. A. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.22.7795-7804.2005 · Cited by 120
Schnell, R., Sandalova, T., Hellman, U., Lindqvist, Y., & Schneider, G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502560200 · Cited by 117
A comprehensive characterization of PncA polymorphisms that confer resistance to pyrazinamide
Yadon, A. N., Maharaj, K., Adamson, J., Lai, Y.-P., Sacchettini, J. C., Ioerger, T. R., Rubin, E. J., & Pym, A. S. (2017) · Nature Communications · doi:10.1038/s41467-017-00721-2 · Cited by 118
Self-citationHost-pathogen genetic interactions underlie tuberculosis susceptibility in genetically diverse mice
Smith, C. M., Baker, R. E., Proulx, M. K., Mishra, B. B., Long, J. E., Park, S. W., Lee, H.-N., Kiritsy, M. C., Bellerose, M. M., Olive, A. J., et al. (2022) · eLife · doi:10.7554/elife.74419 · Cited by 126
Self-citationNishimori, I., Minakuchi, T., Vullo, D., Scozzafava, A., Innocenti, A., & Supuran, C. T. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm9003126 · Cited by 117
Fit for consumption: zebrafish as a model for tuberculosis
Cronan, M. R., & Tobin, D. M. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.016089 · Cited by 114
Parikh, A., Verma, S. K., Khan, S., Prakash, B., & Nandicoori, V. K. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.12.031 · Cited by 119
The F 1 F o -ATP Synthase of Mycobacterium smegmatis Is Essential for Growth
Tran, S. L., & Cook, G. M. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.14.5023-5028.2005 · Cited by 116
McEvoy, C. R. E., Cloete, R. E. A., Müller, B., Schürch, A. C., van Helden, P. D., Gagneux, S., Warren, R. M., & van Pittius, N. C. G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030593 · Cited by 120
The Structure of Mycobacterium tuberculosis CYP125
McLean, K. J., Lafite, P., Levy, C., Cheesman, M. R., Mast, N., Pikuleva, I. A., Leys, D., & Munro, A. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.032706 · Cited by 116
From essential to persistent genes: a functional approach to constructing synthetic life
Acevedo-Rocha, C., Fang, G., Schmidt, M., Ussery, D., & Danchin, A. (2013) · Trends in Genetics · doi:10.1016/j.tig.2012.11.001 · Cited by 107
Targeting Mycobacterium tuberculosis nucleoid-associated protein HU with structure-based inhibitors
Bhowmick, T., Ghosh, S., Dixit, K., Ganesan, V., Ramagopal, U. A., Dey, D., Sarma, S. P., Ramakumar, S., & Nagaraja, V. (2014) · Nature Communications · doi:10.1038/ncomms5124 · Cited by 116
Antigen 84, an Effector of Pleiomorphism in Mycobacterium smegmatis
Nguyen, L. D., Scherr, N., Gatfield, J., Walburger, A., Pieters, J., & Thompson, C. (2007) · Journal of Bacteriology · doi:10.1128/jb.00726-07 · Cited by 121
Tian, J., Bryk, R., Shi, S., Erdjument‐Bromage, H., Tempst, P., & Nathan, C. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04741.x · Cited by 117
Hu, Y., Henderson, B. E., Lund, P. A., Tormay, P., Ahmed, M. T., Gurcha, S. S., Besra, G. S., & Coates, A. R. M. (2008) · Infection and Immunity · doi:10.1128/iai.01078-07 · Cited by 116
ATP synthase in mycobacteria: Special features and implications for a function as drug target
Lü, P., Lill, H., & Bald, D. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.01.022 · Cited by 115
Arginine-deprivation–induced oxidative damage sterilizes Mycobacterium tuberculosis
Tiwari, S., van Tonder, A. J., Vilchèze, C., Mendes, V., Thomas, S. E., Malek, A., Chen, B., Chen, M., Kim, J., Blundell, T. L., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1808874115 · Cited by 115
Pang, X., Vu, P., Byrd, T. F., Ghanny, S., Soteropoulos, P., Mukamolova, G. V., Wu, S., Samten, B., & Howard, S. T. (2007) · Microbiology · doi:10.1099/mic.0.29281-0 · Cited by 115
Identification of substrates of the Mycobacterium tuberculosis proteasome
Pearce, M. J., Arora, P., Festa, R. A., Butler‐Wu, S. M., Gokhale, R. S., & Darwin, K. H. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601405 · Cited by 114
TB database 2010: Overview and update
Galagan, J. E., Sisk, P., Stolte, C., Weiner, B., Koehrsen, M., Wymore, F., Reddy, T. B. K., Zucker, J., Engels, R., Gellesch, M., et al. (2010) · Tuberculosis · doi:10.1016/j.tube.2010.03.010 · Cited by 114
Rathnaiah, G., Zinniel, D. K., Bannantine, J. P., Reffett, J. K., Grohn, Y. T., Collins, M. T., & Barletta, R. G. (2017) · Frontiers in Veterinary Science · doi:10.3389/fvets.2017.00187 · Cited by 114
The Enigmatic Esx Proteins: Looking Beyond Mycobacteria
Unnikrishnan, M., Constantinidou, C., Palmer, T., & Pallen, M. J. (2016) · Trends in Microbiology · doi:10.1016/j.tim.2016.11.004 · Cited by 117
Singh, P., Rao, R. N., Reddy, J. R. C., Prasad, R., Kotturu, S. K., Ghosh, S., & Mukhopadhyay, S. (2016) · Scientific Reports · doi:10.1038/srep21624 · Cited by 114
Essential genes on metabolic maps
Gerdes, S., Edwards, R. A., Kubal, M., Fonstein, M., Stevens, R. L., & Osterman, A. L. (2006) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2006.08.006 · Cited by 111
Revisiting the Evolution of Mycobacterium bovis
Mostowy, S., Inwald, J., Gordon, S., Martı́n, C., Warren, R. M., Kremer, K., Cousins, D., & Behr, M. A. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.18.6386-6395.2005 · Cited by 112
Non-coding RNA and its potential role in Mycobacterium tuberculosis pathogenesis
Arnvig, K. B., & Young, D. B. (2012) · RNA Biology · doi:10.4161/rna.20105 · Cited by 113
Protein Export Systems of Mycobacterium Tuberculosis : Novel Targets for Drug Development?
Feltcher, M. E., Sullivan, J. T., & Braunstein, M. (2010) · Future Microbiology · doi:10.2217/fmb.10.112 · Cited by 116
The Polyketide Pks1 Contributes to Biofilm Formation in Mycobacterium tuberculosis
Pang, J. M., Layre, E., Sweet, L., Sherrid, A. M., Moody, D. B., Ojha, A. K., & Sherman, D. R. (2011) · Journal of Bacteriology · doi:10.1128/jb.06304-11 · Cited by 111
Mycobacterial manipulation of the host cell
Hestvik, A. L. K., Hmama, Z., & Av‐Gay, Y. (2005) · FEMS Microbiology Reviews · doi:10.1016/j.femsre.2005.04.013 · Cited by 109
van Opijnen, T., & Camilli, A. (2010) · Current Protocols in Microbiology · doi:10.1002/9780471729259.mc01e03s19 · Cited by 110
Boradia, V. M., Malhotra, H., Thakkar, J. S., Tillu, V. A., Vuppala, B., Patil, P., Sheokand, N., Sharma, P., Chauhan, A. S., Raje, M., et al. (2014) · Nature Communications · doi:10.1038/ncomms5730 · Cited by 108
de Carvalho, L. P. S., Zhao, H., Dickinson, C. E., Arango, N., Lima, C. D., Fischer, S. M., Ouerfelli, O., Nathan, C., & Rhee, K. Y. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.03.009 · Cited by 107
Buchmeier, N. A., & Fahey, R. C. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2006.00441.x · Cited by 107
Biotin, a universal and essential cofactor: synthesis, ligation and regulation
Sirithanakorn, C., & Cronan, J. E. (2021) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuab003 · Cited by 106
Prasad, M. S., Bhole, R. P., Khedekar, P. B., & Chikhale, R. V. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105242 · Cited by 111
Dihydrolipoamide Acyltransferase Is Critical forMycobacterium tuberculosisPathogenesis
Shi, S., & Ehrt, S. (2005) · Infection and Immunity · doi:10.1128/iai.74.1.56-63.2006 · Cited by 107
Targeting the Formation of the Cell Wall Core of M. tuberculosis
Barry, C. E., Crick, D. C., & McNeil, M. (2007) · Infectious Disorders - Drug Targets · doi:10.2174/187152607781001808 · Cited by 106
Mycobacterium tuberculosis MetabolismPreprint
Warner, D. F. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a021121 · Cited by 108
Function Prediction and Analysis of Mycobacterium tuberculosis Hypothetical Proteins
Mazandu, G. K., & Mulder, N. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13067283 · Cited by 105
Ahidjo, B. A., Diane, K., McKenzie, J. L., Machowski, E. E., Gordhan, B. G., Arcus, V. L., Abrahams, G. L., & Mizrahi, V. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021738 · Cited by 103
Bisson, G. P., Mehaffy, C., Broeckling, C. D., Prenni, J. E., Rifat, D., Lun, D. S., Burgos, M. V., Weissman, D., Karakousis, P. C., & Dobos, K. M. (2012) · Journal of Bacteriology · doi:10.1128/jb.01013-12 · Cited by 105
Minakuchi, T., Nishimori, I., Vullo, D., Scozzafava, A., & Supuran, C. T. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm9000488 · Cited by 104
The Mycobacterium tuberculosis Drugome and Its Polypharmacological Implications
Kinnings, S., Xie, L., Fung, K. H., Jackson, R. M., Xie, L., & Bourne, P. E. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000976 · Cited by 104
DNA topoisomerase I and DNA gyrase as targets for TB therapy
Nagaraja, V., Godbole, A. A., Henderson, S. R., & Maxwell, A. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.11.006 · Cited by 103
Hit Generation in TB Drug Discovery: From Genome to Granuloma
Yuan, T., & Sampson, N. S. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00602 · Cited by 104
Mycothiol-dependent proteins in actinomycetes
Rawat, M., & Av‐Gay, Y. (2007) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00062.x · Cited by 103
Biosynthesis of mycobacterial lipoarabinomannan: Role of a branching mannosyltransferase
Kaur, D., Berg, S., Dinadayala, P., Gicquel, B., Chatterjee, D., McNeil, M., Vissa, V., Crick, D. C., Jackson, M., & Brennan, P. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603049103 · Cited by 103
Mycobacteriophages: Windows into Tuberculosis
Hatfull, G. F. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003953 · Cited by 103
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