Cited by 2,544Tuberculosis Research and EpidemiologyBacterial Genetics and BiotechnologyMycobacterium research and diagnosis

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 access

Sassetti, Christopher M., Boyd, Dana H., Rubin, Eric J.·2003·Molecular Microbiology

DOI 10.1046/j.1365-2958.2003.03425.x

Open this paper in CoChat — free account Open PDF

Abstract

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.

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

Crossref · 10.1046/j.1365-2958.2003.03425.x

Cites

25 of 25 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
The Pathway Tools software
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-citation
The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages
De 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
ideR , an Essential Gene in Mycobacterium tuberculosis : Role of IdeR in Iron-Dependent Gene Expression, Iron Metabolism, and Oxidative Stress Response
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
Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin
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
Identification of Critical Staphylococcal Genes Using Conditional Phenotypes Generated by Antisense RNA
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

Show all 25 references

Research works printed but not linked: 1

Zalkin H., 1996, Escherichia Coli and Salmonella: Cellular and Molecular Biololgy

Sorted by citations

Items 601–700 of 1,003

AccD6, a Member of the Fas II Locus, Is a Functional Carboxyltransferase Subunit of the Acyl-Coenzyme A Carboxylase in Mycobacterium tuberculosis
Daniel, J., Oh, T., Lee, C., & Kolattukudy, P. E. (2006) · Journal of Bacteriology · doi:10.1128/jb.01019-06 · Cited by 61
Quantitative Proteomic and Phosphoproteomic Analysis of H37Ra and H37Rv Strains of Mycobacterium tuberculosis
Verma, R., Pinto, S. M., Patil, A. H., Advani, J., Subba, P., Kumar, M., Sharma, J. N., Dey, G., Ravikumar, R., Buggi, S., et al. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00983 · Cited by 62
A Mycothiol Synthase Mutant of Mycobacterium smegmatis Produces Novel Thiols and Has an Altered Thiol Redox Status
Newton, G. L., Ta, P., & Fahey, R. C. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.21.7309-7316.2005 · Cited by 62
Transcriptomic Signatures Predict Regulators of Drug Synergy and Clinical Regimen Efficacy against Tuberculosis
Ma, S., Jaipalli, S., Larkins‐Ford, J., Lohmiller, J., Aldridge, B. B., Sherman, D. R., & Chandrasekaran, S. (2019) · mBio · doi:10.1128/mbio.02627-19 · Cited by 59
Profiling Pretomanid as a Therapeutic Option for TB Infection: Evidence to Date
Stancil, S. L., Mirzayev, F., & Abdel‐Rahman, S. M. (2021) · Drug Design Development and Therapy · doi:10.2147/dddt.s281639 · Cited by 61
Expression of the ompATb operon accelerates ammonia secretion and adaptation of Mycobacterium tuberculosis to acidic environments
Song, H., Huff, J., Janik, K., Walter, K., Keller, C., Ehlers, S., Bossmann, S. H., & Niederweis, M. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07619.x · Cited by 62
Pathogenicity in the tubercle bacillus: molecular and evolutionary determinants
Gordon, S. V., Bottai, D., Siméone, R., Stinear, T. P., & Brosch, R. (2009) · BioEssays · doi:10.1002/bies.200800191 · Cited by 64
Acetylation of Trehalose Mycolates Is Required for Efficient MmpL-Mediated Membrane Transport in Corynebacterineae
Yamaryo‐Botté, Y., Rainczuk, A. K., Lea‐Smith, D. J., Brammananth, R., van der Peet, P. L., Meikle, P. J., Ralton, J. E., Rupasinghe, T., Williams, S. J., Coppel, R. L., et al. (2014) · ACS Chemical Biology · doi:10.1021/cb5007689 · Cited by 61
Compounds targeting disulfide bond forming enzyme DsbB of Gram-negative bacteria
Landeta, C., Blazyk, J. L., Hatahet, F., Meehan, B. M., Eser, M., Myrick, A., Bronstain, L., Minami, S., Arnold, H. K., Ke, N., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1752 · Cited by 61
Self-citation
Allosteric Activation Mechanism of the Mycobacterium tuberculosis Receptor Ser/Thr Protein Kinase, PknB
Lombana, T. N., Echols, N., Good, M. C., Thomsen, N. D., Ng, H. L., Greenstein, A. E., Falick, A. M., King, D., & Alber, T. (2010) · Structure · doi:10.1016/j.str.2010.09.019 · Cited by 61
Essential Metabolites of Mycobacterium tuberculosis and Their Mimics
Lamichhane, G., Freundlich, J. S., Ekins, S., Wickramaratne, N. A., Nolan, S. T., & Bishai, W. R. (2011) · mBio · doi:10.1128/mbio.00301-10 · Cited by 60
Coenzyme A Biosynthesis and Enzymology
Strauss, E. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00141-6 · Cited by 60
Targeting DNA Replication and Repair for the Development of Novel Therapeutics against Tuberculosis
Reiche, M., Warner, D. F., & Mizrahi, V. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00075 · Cited by 62
In-host population dynamics of Mycobacterium tuberculosis complex during active disease
Vargas, R., Freschi, L., Marin, M. G., Epperson, L. E., Smith, M. L., Oussenko, I. A., Durbin, D., Strong, M., Salfinger, M., & Farhat, M. R. (2021) · eLife · doi:10.7554/elife.61805 · Cited by 60
Targeting the ATP synthase in bacterial and fungal pathogens: beyond Mycobacterium tuberculosis
Vestergaard, M. R., Bald, D., & Ingmer, H. (2022) · Journal of Global Antimicrobial Resistance · doi:10.1016/j.jgar.2022.01.026 · Cited by 62
Functional Analysis, Overexpression, and Kinetic Characterization of Pyruvate Kinase from Methicillin-ResistantStaphylococcus aureus
Zoraghi, R., See, R. H., Gong, H., Lian, T., Swayze, R., Finlay, B. B., Brunham, R. C., McMaster, W. R., & Reiner, N. E. (2010) · Biochemistry · doi:10.1021/bi100780t · Cited by 60
Stable Analogues of OSB‐AMP: Potent Inhibitors of MenE, the o‐Succinylbenzoate‐CoA Synthetase from Bacterial Menaquinone Biosynthesis
Lu, X., Zhou, R., Sharma, I., Li, X., Kumar, G., Swaminathan, S., Tonge, P. J., & Tan, D. S. (2011) · ChemBioChem · doi:10.1002/cbic.201100585 · Cited by 60
A truncated lipoglycan from mycobacteria with altered immunological properties
Birch, H. L., Alderwick, L. J., Appelmelk, B. J., Maaskant, J. J., Bhatt, A., Singh, A., Nigou, J., Eggeling, L., Geurtsen, J., & Besra, G. S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0915082107 · Cited by 60
Systems-Based Approaches to Probing Metabolic Variation within the Mycobacterium tuberculosis Complex
Lofthouse, E. K., Wheeler, P. R., Beste, D. J. V., Khatri, B. L., Wu, H., Mendum, T. A., Kierzek, A. M., & McFadden, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075913 · Cited by 60
Comparative Whole-Genome Analysis of Clinical Isolates Reveals Characteristic Architecture of Mycobacterium tuberculosis Pangenome
Periwal, V., Patowary, A., Vellarikkal, S. K., Gupta, A., Singh, M., Mittal, A., Jeyapaul, S., Chauhan, R. K., Singh, A. V., Singh, P. K., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122979 · Cited by 59
Components of the Rv0081-Rv0088 Locus, Which Encodes a Predicted Formate Hydrogenlyase Complex, Are Coregulated by Rv0081, MprA, and DosR in Mycobacterium tuberculosis
He, H., Bretl, D. J., Penoske, R. M., Anderson, D. M., & Zahrt, T. C. (2011) · Journal of Bacteriology · doi:10.1128/jb.05562-11 · Cited by 60
Cleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease and Identification of Novel Peptide Substrates and Boronate Inhibitors with Anti-bacterial Activity
Akopian, T. N., Kandror, O., Tsu, C. A., Lai, J. H.-S., Wu, W., Liu, Y., Zhao, P., Park, A., Wolf, L., Dick, L. R., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.625640 · Cited by 59
Self-citation
DNA repair systems and the pathogenesis of Mycobacterium tuberculosis: varying activities at different stages of infection
Minias, A. E., Bowater, R. P., & Dziadek, J. (2010) · Clinical Science · doi:10.1042/cs20100041 · Cited by 59
Decaprenyl Diphosphate Synthesis in Mycobacterium tuberculosis
Kaur, D., Brennan, P. J., & Crick, D. C. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.22.7564-7570.2004 · Cited by 59
Proteomic analysis of streptomycin resistant and sensitive clinical isolates of Mycobacterium tuberculosis
Sharma, P., Kumar, B., Gupta, Y., Singhal, N., Katoch, V., Venkatesan, K., & Bisht, D. (2010) · Proteome Science · doi:10.1186/1477-5956-8-59 · Cited by 54
Characterization of the mycobacterial chromosome segregation protein ParB and identification of its target in Mycobacterium smegmatis
Jakimowicz, D., Brzostek, A. M., Rumijowska-Galewicz, A., Żydek, P., Dołzbłasz, A., Smulczyk-Krawczyszyn, A., Zimniak, T., Wojtasz, Ł., Zawilak-Pawlik, A. M., Kois, A., et al. (2007) · Microbiology · doi:10.1099/mic.0.2007/011619-0 · Cited by 58
Genome-wide exploration of the drug action of capreomycin on Mycobacterium tuberculosis using Affymetrix oligonucleotide GeneChips
Fu, L., & Shinnick, T. M. (2006) · Journal of Infection · doi:10.1016/j.jinf.2006.05.012 · Cited by 60
A Conserved Dimer and Global Conformational Changes in the Structure of apo-PknE Ser/Thr Protein Kinase from Mycobacterium tuberculosis
Gay, L. M., Ng, H. L., & Alber, T. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.05.015 · Cited by 60
Predicting antimicrobial resistance using conserved genes
Nguyen, M., Olson, R., Shukla, M. P., VanOeffelen, M., & Davis, J. J. (2020) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1008319 · Cited by 56
Conditional silencing of topoisomerase I gene ofMycobacterium tuberculosisvalidates its essentiality for cell survival
Ahmed, W., Menon, S., Godbole, A. A., Pullela, K., & Nagaraja, V. (2014) · FEMS Microbiology Letters · doi:10.1111/1574-6968.12412 · Cited by 58
Acinetobacter baylyi ADP1 as a model for metabolic system biology
de Berardinis, V., Durot, M., Weissenbach, J., & Salanoubat, M. (2009) · Current Opinion in Microbiology · doi:10.1016/j.mib.2009.07.005 · Cited by 62
Mycobacterial tuberculosis Enzyme Targets and their Inhibitors
Saxena, A. K., & Singh, A. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190219105722 · Cited by 61
Protein kinases PknA and PknB independently and coordinately regulate essential Mycobacterium tuberculosis physiologies and antimicrobial susceptibility
Zeng, J., Platig, J., Cheng, T., Ahmed, S., Skaf, Y., Potluri, L., Schwartz, D., Steen, H., Moody, D. B., & Husson, R. N. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008452 · Cited by 58
Iron acquisition, assimilation and regulation in mycobacteria
Banerjee, S., Farhana, A., Ehtesham, N. Z., & Hasnain, S. E. (2011) · Infection, Genetics and Evolution · doi:10.1016/j.meegid.2011.02.016 · Cited by 57
Induced ectopic expression of HigB toxin in M ycobacterium tuberculosis results in growth inhibition, reduced abundance of a subset of mRNAs and cleavage of tmRNA
Schuessler, D. L., Cortes, T., Fivian-Hughes, A. S., Lougheed, K. E. A., Harvey, E., Buxton, R. S., Davis, E. O., & Young, D. B. (2013) · Molecular Microbiology · doi:10.1111/mmi.12358 · Cited by 61
Superessential reactions in metabolic networks
Barve, A., Rodrigues, J. F. M., & Wagner, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113065109 · Cited by 55
A Noncompetitive Inhibitor forMycobacterium tuberculosis’s Class IIa Fructose 1,6-Bisphosphate Aldolase
Capodagli, G. C., Sedhom, W. G., Jackson, M., Ahrendt, K. A., & Pegan, S. D. (2013) · Biochemistry · doi:10.1021/bi401022b · Cited by 59
A Point Mutation in cycA Partially Contributes to the D-cycloserine Resistance Trait of Mycobacterium bovis BCG Vaccine Strains
Chen, J. M., Uplekar, S. M., Gordon, S. V., & Cole, S. T. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043467 · Cited by 57
Improved mycobacterial tetracycline inducible vectors
Williams, K. J., Joyce, G., & Robertson, B. D. (2010) · Plasmid · doi:10.1016/j.plasmid.2010.04.003 · Cited by 57
Targeting the trehalose utilization pathways of Mycobacterium tuberculosis
Thanna, S., & Sucheck, S. J. (2015) · MedChemComm · doi:10.1039/c5md00376h · Cited by 49
Screening of antitubercular compound library identifies novel ATP synthase inhibitors of Mycobacterium tuberculosis
Kumar, S., Mehra, R., Sharma, S., Bokolia, N. P., Raina, D., Nargotra, A., Singh, P. P., & Khan, I. A. (2017) · Tuberculosis · doi:10.1016/j.tube.2017.10.008 · Cited by 57
MtrA Response Regulator Controls Cell Division and Cell Wall Metabolism and Affects Susceptibility of Mycobacteria to the First Line Antituberculosis Drugs
Gorla, P., Płocińska, R., Sarva, K., Satsangi, A. T., Pandeeti, E., DONNELLY, R. J., Dziadek, J., Rajagopalan, M. R., & Madiraju, M. V. V. S. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02839 · Cited by 54
A Glycosyltransferase Involved in Biosynthesis of Triglycosylated Glycopeptidolipids inMycobacterium smegmatis: Impact on Surface Properties
Deshayes, C., Laval, F., Montrozier, H. L., Daffé, M., Etienne, G., & Reyrat, J. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.21.7283-7291.2005 · Cited by 57
Examination of Mycobacterium tuberculosis sigma factor mutants using low-dose aerosol infection of guinea pigs suggests a role for SigC in pathogenesis
Karls, R. K., Guarner, J., McMurray, D. N., BIRKNESS, K. A., & Quinn, F. D. (2006) · Microbiology · doi:10.1099/mic.0.28591-0 · Cited by 57
Macrophage-specific Mycobacterium tuberculosis genes: identification by green fluorescent protein and kanamycin resistance selection
Srivastava, V., Rouanet, C., Srivastava, R., Bethunaickan, R., Locht, C., & Srivastava, B. S. (2007) · Microbiology · doi:10.1099/mic.0.2006/000547-0 · Cited by 57
The Critical Role ofembCinMycobacterium tuberculosis
Goude, R., Amin, A. G., Chatterjee, D., & Parish, T. (2008) · Journal of Bacteriology · doi:10.1128/jb.01825-07 · Cited by 57
Bioenergetic Inhibitors: Antibiotic Efficacy and Mechanisms of Action in Mycobacterium tuberculosis
Hasenoehrl, E., Wiggins, T. J., & Berney, M. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.611683 · Cited by 54
Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking
Capdevila, D. A., Rondón, J. J., Edmonds, K. A., Rocchio, J. S., Dujovne, M. V., & Giedroc, D. P. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00264 · Cited by 64
Structure and Function of the Virulence-Associated High-Temperature Requirement A of Mycobacterium tuberculosis
Mohamedmohaideen, N. N., Palaninathan, S. K., Morin, P. M., Williams, B. J., Braunstein, M., Tichy, S. E., Locker, J. D., Russell, D. H., Jacobs, W. R., & Sacchettini, J. C. (2008) · Biochemistry · doi:10.1021/bi701929m · Cited by 56
Protein Kinase A (PknA) of Mycobacterium tuberculosis Is Independently Activated and Is Critical for Growth in Vitro and Survival of the Pathogen in the Host
Nagarajan, S. N., Upadhyay, S., Chawla, Y. K., Khan, S., Naz, S., Subramanian, J., Gandotra, S., & Nandicoori, V. K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.611822 · Cited by 58
Purification and Characterization of Mycobacterial Phospholipase A: an Activity Associated with Mycobacterial Cutinase
Parker, S. K., Curtin, K. M., & Vasil, M. L. (2007) · Journal of Bacteriology · doi:10.1128/jb.01909-06 · Cited by 56
Control of Cell Wall Assembly by a Histone-Like Protein in Mycobacteria
Katsube, T., Matsumoto, S., Takatsuka, M., Okuyama, M., Ozeki, Y., Naito, M., Nishiuchi, Y., Fujiwara, N., Yoshimura, M., Tsuboi, T., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.00550-07 · Cited by 56
Identification of Pyruvate Kinase in Methicillin-Resistant Staphylococcus aureus as a Novel Antimicrobial Drug Target
Zoraghi, R., See, R. H., Axerio-Cilies, P., Kumar, N. S., Gong, H., Moreau, A., Hsing, M., Kaur, S., Swayze, R. D., Worrall, L. J., et al. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01250-10 · Cited by 56
Mtb PKNA/PKNB Dual Inhibition Provides Selectivity Advantages for Inhibitor Design To Minimize Host Kinase Interactions
Wang, T., Bemis, G. W., Hanzelka, B. L., Zuccola, H. J., Wynn, M., Moody, C. S., Green, J., Locher, C. P., Liu, A., Gao, H., et al. (2017) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.7b00239 · Cited by 58
The Abyssomicin C family as in vitro inhibitors of Mycobacterium tuberculosis
Freundlich, J. S., Lalgondar, M., Wei, J., Swanson, S., Sorensen, E. J., Rubin, E. J., & Sacchettini, J. C. (2010) · Tuberculosis · doi:10.1016/j.tube.2010.08.002 · Cited by 56
Self-citation
A comprehensive map of genome-wide gene regulation in Mycobacterium tuberculosis
Turkarslan, S., Peterson, E. J. R., Rustad, T. R., Minch, K. J., Reiss, D. J., Morrison, R., Ma, S., Price, N. D., Sherman, D. R., & Baliga, N. S. (2015) · Scientific Data · doi:10.1038/sdata.2015.10 · Cited by 56
Small RNAs in mycobacteria: an unfolding story
Haning, K., Cho, S. H., & Contreras, L. M. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00096 · Cited by 54
Characterization of Mycobacterium tuberculosis NAD Kinase: Functional Analysis of the Full-Length Enzyme by Site-Directed Mutagenesis
Raffaelli, N., Finaurini, L., Mazzola, F., Pucci, L., Sorci, L., Amici, A., & Magni, G. (2004) · Biochemistry · doi:10.1021/bi049650w · Cited by 55
New Classes of Alanine Racemase Inhibitors Identified by High-Throughput Screening Show Antimicrobial Activity against Mycobacterium tuberculosis
Anthony, K., Strych, U., Yeung, K. R., Shoen, C., Perez, O. A., Krause, K. L., Cynamon, M. H., Aristoff, P. A., & Koski, R. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020374 · Cited by 55
Target Prediction for an Open Access Set of Compounds Active against Mycobacterium tuberculosis
Martínez-Jiménez, F., Papadatos, G., Yang, L., Wallace, I. M., Kumar, V. D., Pieper, U., Šali, A., Brown, J. R., Overington, J. P., & Martı́-Renom, M. A. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003253 · Cited by 56
A distinct role of formamidopyrimidine DNA glycosylase (MutM) in down-regulation of accumulation of G, C mutations and protection against oxidative stress in mycobacteria
Jain, R., Kumar, P., & Varshney, U. (2007) · DNA repair · doi:10.1016/j.dnarep.2007.06.009 · Cited by 55
A philosophy of anti-infectives as a guide in the search for new drugs for tuberculosis
Nathan, C., Gold, B. S., Lin, G., Stegman, M. A., de Carvalho, L. P. S., Vandal, O. H., Venugopal, A., & Bryk, R. (2008) · Tuberculosis · doi:10.1016/s1472-9792(08)70034-9 · Cited by 55
Cyclipostins and Cyclophostin analogs as promising compounds in the fight against tuberculosis
Nguyen, P. C., Delorme, V., Bénarouche, A., Martin, B. P., Paudel, R. R., Gnawali, G. R., Madani, A., Puppo, R., Landry, V., Kremer, L., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-11843-4 · Cited by 56
Peptide Deformylase Inhibitors as Potent Antimycobacterial Agents
Teo, J. W. P., Thayalan, P., Beer, D., Yap, A., Nanjundappa, M., Ngew, X., Duraiswamy, J., Liung, S., Dartois, V. A., Schreiber, M. J., et al. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00555-06 · Cited by 55
Discovery of a Novel Mycobacterial F‐ATP Synthase Inhibitor and its Potency in Combination with Diarylquinolines
Hotra, A., Ragunathan, P., Ng, P. S., Seankongsuk, P., Harikishore, A., Sarathy, J. P., Saw, W. G., Lakshmanan, U., Sae‐Lao, P., Kalia, N. P., et al. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202002546 · Cited by 54
d ‐Alanine metabolism is essential for growth and biofilm formation of Streptococcus mutans
Qiu, W., Zheng, X. M., Wei, Y., Zhou, X., Zhang, K., Wang, S., Cheng, L., Li, Y., Ren, B., Xu, X., et al. (2015) · Molecular Oral Microbiology · doi:10.1111/omi.12146 · Cited by 54
The Alanine Racemase of Mycobacterium smegmatis Is Essential for Growth in the Absence of d -Alanine
Milligan, D. L., Tran, S. L., Strych, U., Cook, G. M., & Krause, K. L. (2007) · Journal of Bacteriology · doi:10.1128/jb.01201-07 · Cited by 54
Comparative Genomic Analysis of Mycobacterium tuberculosis Drug Resistant Strains from Russia
Ilina, E. N., Shitikov, E. A., Ikryannikova, L. N., Alekseev, D. G., Kamashev, D., Malakhova, M. V., Parfenova, T. V., Афанасьев, М. В., Ischenko, D. S., Bazaleev, N. A., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056577 · Cited by 54
Single nucleotide polymorphisms in Mycobacterium tuberculosis and the need for a curated database
Stucki, D., & Gagneux, S. (2012) · Tuberculosis · doi:10.1016/j.tube.2012.11.002 · Cited by 61
Selective Inhibitors of Bacterial t-RNA-(N 1 G37) Methyltransferase (TrmD) That Demonstrate Novel Ordering of the Lid Domain
Hill, P., Abibi, A., Albert, R., Andrews, B. M., Gagnon, M. M., Gao, N., Grebe, T. P., Hajec, L. I., Huang, J., Livchak, S., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400718n · Cited by 54
Viable screening targets related to the bacterial cell wall
Silver, L. L. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12006 · Cited by 53
Molecular properties, functions, and potential applications of NAD kinases
Shi, F., Li, Y., Li, Y., & Wang, X. (2009) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmp029 · Cited by 54
Targeting tuberculosis through a small focused library of 1,2,3-triazoles
Labadié, G. R., de la Iglesia, A., & Morbidoni, H. R. (2011) · Molecular Diversity · doi:10.1007/s11030-011-9319-0 · Cited by 54
Transcription termination factor Rho: a hub linking diverse physiological processes in bacteria
Grylak-Mielnicka, A., Bidnenko, V., Bardowski, J. K., & Bidnenko, E. (2016) · Microbiology · doi:10.1099/mic.0.000244 · Cited by 58
The Mycobacterium tuberculosis transcriptional landscape under genotoxic stress
Namouchi, A., Gómez-Muñoz, M., Frye, S. A., Moen, L. V., Rognes, T., Tønjum, T., & Balasingham, S. V. (2016) · BMC Genomics · doi:10.1186/s12864-016-3132-1 · Cited by 53
Mechanism-Based Inhibition of the Mycobacterium tuberculosis Branched-Chain Aminotransferase by d - and l -Cycloserine
Franco, T. M. A., Favrot, L., Vergnolle, O., & Blanchard, J. S. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00142 · Cited by 54
Remote homology searches identify bacterial homologues of eukaryotic lipid transfer proteins, including Chorein-N domains in TamB and AsmA and Mdm31p
Levine, T. P. (2019) · BMC Molecular and Cell Biology · doi:10.1186/s12860-019-0226-z · Cited by 56
Oxidative Phosphorylation—an Update on a New, Essential Target Space for Drug Discovery in Mycobacterium tuberculosis
Foo, C. S.-Y., Pethe, K., & Lupien, A. (2020) · Applied Sciences · doi:10.3390/app10072339 · Cited by 55
LipG a bifunctional phospholipase/thioesterase involved in mycobacterial envelope remodeling
Santucci, P., Point, V., Poncin, I., Guy, A., Crauste, C., Serveau, C., Galano, J., Spilling, C. D., Cavalier, J., & Canaan, S. (2018) · Bioscience Reports · doi:10.1042/bsr20181953 · Cited by 53
Bibliometric Analysis on Tuberculosis and Tuberculosis-Related Research Trends in Africa: A Decade-Long Study
Igwaran, A., & Edoamodu, C. E. (2021) · Antibiotics · doi:10.3390/antibiotics10040423 · Cited by 53
The Phosphatidyl- myo -Inositol Mannosyltransferase PimA Is Essential for Mycobacterium tuberculosis Growth In Vitro and In Vivo
Boldrin, F., Ventura, M., Degiacomi, G., Ravishankar, S., Sala, C., Svetlíková, Z., Ambady, A., Dhar, N., Korduláková, J., Zhang, M., et al. (2014) · Journal of Bacteriology · doi:10.1128/jb.01346-13 · Cited by 53
D-3-Phosphoglycerate Dehydrogenase from Mycobacterium tuberculosis Is a Link between the Escherichia coli and Mammalian Enzymes
Dey, S., Hu, Z., Xu, X. L., Sacchettini, J. C., & Grant, G. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414488200 · Cited by 53
Characterization of Phosphofructokinase Activity in Mycobacterium tuberculosis Reveals That a Functional Glycolytic Carbon Flow Is Necessary to Limit the Accumulation of Toxic Metabolic Intermediates under Hypoxia
Phong, W. Y., Lin, W., Rao, S. P. S., Dick, T., Alonso, S., & Pethe, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056037 · Cited by 55
Proteomic analysis of the proteins regulated by HrpB from the plant pathogenic bacterium Burkholderia glumae
Kang, Y., Kim, J., Kim, S.-H., Kim, H., Lim, J. Y., Kim, M., Kwak, J., Moon, J. S., & Hwang, I. (2007) · PROTEOMICS · doi:10.1002/pmic.200700244 · Cited by 53
Fumarase Deficiency Causes Protein and Metabolite Succination and Intoxicates Mycobacterium tuberculosis
Ruecker, N., Jansen, R. S., Trujillo, C., Puckett, S. E., Jayachandran, P., Piroli, G. G., Frizzell, N., Molina, H., Rhee, K. Y., & Ehrt, S. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.01.005 · Cited by 56
DNA Replication in Mycobacterium tuberculosis
Ditse, Z., Lamers, M. H., & Warner, D. F. (2017) · Microbiology Spectrum · doi:10.1128/microbiolspec.tbtb2-0027-2016 · Cited by 54
Antimycobacterial Rufomycin Analogues from Streptomyces atratus Strain MJM3502
Zhou, B., Shetye, G. S., Yang, Y., Santarsiero, B. D., Klein, L. L., Abad‐Zapatero, C., Wolf, N. M., Cheng, J., Jin, Y., Lee, H., et al. (2020) · Journal of Natural Products · doi:10.1021/acs.jnatprod.9b01095 · Cited by 53
Regulation of Arginine Acquisition and Virulence Gene Expression in the Human Pathogen Streptococcus pneumoniae by Transcription Regulators ArgR1 and AhrC
Kloosterman, T. G., & Kuipers, O. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.295832 · Cited by 51
Molybdenum cofactor: A key component ofMycobacterium tuberculosispathogenesis?
Williams, M. J., Mizrahi, V., & Kana, B. D. (2013) · Critical Reviews in Microbiology · doi:10.3109/1040841x.2012.749211 · Cited by 54
Drug Design and Identification of Potent Leads Against Mycobacterium tuberculosis Thymidine Monophosphate Kinase
Calenbergh, S. V., Pochet, S., & Munier‐Lehmann, H. (2012) · Current Topics in Medicinal Chemistry · doi:10.2174/156802612799984580 · Cited by 52
The Accessory SecA2 System of Mycobacteria Requires ATP Binding and the Canonical SecA1
Rigel, N. W., Gibbons, H. S., McCann, J. R., McDonough, J. A., Kurtz, S. L., & Braunstein, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900325200 · Cited by 55
Expression and characterization of α-(1,4)-glucan branching enzyme Rv1326c of Mycobacterium tuberculosis H37Rv
Garg†, S. K., Alam†, M. S., Kishan, K. V. R., & Agrawal, P. (2006) · Protein Expression and Purification · doi:10.1016/j.pep.2006.08.005 · Cited by 52
Identification of Widespread Adenosine Nucleotide Binding in Mycobacterium tuberculosis
Ansong, C. K., Ortega, C., Payne, S., Haft, D. H., Chauvignè-Hines, L. M., Lewis, M. P., Ollodart, A. R., Purvine, S. O., Shukla, A. K., Fortuin, S., et al. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.11.008 · Cited by 52
Comparative genomic assessment of novel broad‐spectrum targets for antibacterial drugs
White, T. A., & Kell, D. B. (2004) · Comparative and Functional Genomics · doi:10.1002/cfg.411 · Cited by 51
Functional Analysis of Molybdopterin Biosynthesis in Mycobacteria Identifies a Fused Molybdopterin Synthase in Mycobacterium tuberculosis
Williams, M. J., Kana, B. D., & Mizrahi, V. (2010) · Journal of Bacteriology · doi:10.1128/jb.00774-10 · Cited by 54
Proteomic analysis of ofloxacin-mono resistant Mycobacterium tuberculosis isolates
Lata, M., Sharma, D., Deo, N., Tiwari, P. K., Bisht, D., & Venkatesan, K. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.07.031 · Cited by 52
Toxic Activation of an AAA+ Protease by the Antibacterial Drug Cyclomarin A
Maurer, M. J., Linder, D., Franke, K. B., Jäger, J., Taylor, G., Gloge, F., Guttzeit, S., Breton, L. L., Mayer, M. P., Weber-Ban, E. U., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.05.008 · Cited by 52
A Novel Fold Revealed by Mycobacterium tuberculosis NAD Kinase, a Key Allosteric Enzyme in NADP Biosynthesis
Garavaglia, S., Raffaelli, N., Finaurini, L., Magni, G., & Rizzi, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406586200 · Cited by 52
Characterization of the Mycobacterium tuberculosis 4-Diphosphocytidyl-2- C -Methyl- d -Erythritol Synthase: Potential for Drug Development
Eoh, H., Brown, A. C., Buetow, L., Hunter, W. N., Parish, T., Kaur, D., Brennan, P. J., & Crick, D. C. (2007) · Journal of Bacteriology · doi:10.1128/jb.00925-07 · Cited by 52
The Crystal Structure of Rv1347c, a Putative Antibiotic Resistance Protein from Mycobacterium tuberculosis, Reveals a GCN5-related Fold and Suggests an Alternative Function in Siderophore Biosynthesis
Card, G. L., Peterson, N. A., Smith, C. A., Rupp, B., Schick, B., & Baker, E. N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413904200 · Cited by 52

Authors: Sassetti, C. M., Boyd, D. H., & Rubin, E. J.
Affiliations: Harvard University (US)
Corresponding author: Rubin, Eric J.
ORCID: Sassetti, Christopher M.
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
DOI: 10.1046/j.1365-2958.2003.03425.x
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
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
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

Genes required for mycobacterial growth defined by high density mutagenesis

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks