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To catch a killer. What can mycobacterial models teach us about Mycobacterium tuberculosis pathogenesis?
Open accessAbstract
Mycobacterium tuberculosis is the causative agent of the global tuberculosis epidemic. To combat this successful human pathogen we need a better understanding of the basic biology of mycobacterial pathogenesis. The use of mycobacterial model systems has the potential to greatly facilitate our understanding of how M. tuberculosis causes disease. Recently, studies using mycobacterial models, including M. bovis BCG, M. marinum, and M. smegmatis have significantly contributed to understanding M. tuberculosis. Specifically, there have been advances in genetic manipulation of M. tuberculosis using inducible promoters and recombineering that alleviate technical limitations in working with mycobacteria. Model systems have helped elucidate how secretion systems function at both the molecular level and during virulence. Mycobacterial models have also led to interesting hypotheses about how M. tuberculosis mediates latent infection and host response. While there is utility in using model systems to understand tuberculosis, each of these models represent distinct mycobacterial species with unique environmental adaptations. Directly comparing findings in model mycobacteria to those in M. tuberculosis will illuminate the similarities and differences between these species and increase our understanding of why M. tuberculosis is such a potent human pathogen.
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“Two alternative, slow-growing mycobacteria that are more closely related to M. tuberculosis and used in a BSL-2 laboratory are M. bovis BCG, the attenuated vaccine strain, and M. marinum, a fish pathogen, each with advantages for host infection studies over M. smegmatis (182, 183).”
From Mycobacterium smegmatis: The Vanguard of Mycobacterial Research (2023) · cites this paper as [183]
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“each with advantages for host infection studies over M. smegmatis (182, 183)”
From Mycobacterium smegmatis: The Vanguard of Mycobacterial Research (2023) · cites this paper as [183]
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Cites
Snapper, S. B., Melton, R. E., Mustafa, S., Kieser, T., & Jr, W. R. J. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb02040.x · Cited by 1,237
Inhibition of Respiration by Nitric Oxide Induces a Mycobacterium tuberculosis Dormancy Program
Voskuil, M. I., Schnappinger, D., Visconti, K. C., Harrell, M. I., Dolganov, G., Sherman, D. R., & Schoolnik, G. K. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20030205 · Cited by 975
Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages
Rengarajan, J., Bloom, B. R., & Rubin, E. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503272102 · Cited by 679
Recombineering in Mycobacterium tuberculosis
van Kessel, J. C., & Hatfull, G. F. (2006) · Nature Methods · doi:10.1038/nmeth996 · Cited by 586
Mukamolova, G. V., Kaprelyants, A. S., Young, D. I., Young, M. R., & Kell, D. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.15.8916 · Cited by 452
The ESAT-6 gene cluster of Mycobacterium tuberculosis and other high G+C Gram-positive bacteria
Gey van Pittius, N. C., Gamieldien, J., Hide, W., Brown, G. D., Siezen, R. J., & Beyers, A. D. (2001) · Genome Biology · doi:10.1186/gb-2001-2-10-research0044 · Cited by 375
Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition
Siegrist, M. S., Unnikrishnan, M., McConnell, M. J., Borowsky, M. L., Cheng, T., Siddiqi, N., Fortune, S. M., Moody, D. B., & Rubin, E. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900589106 · Cited by 347
Comparative pathogenesis of Mycobacterium marinum and Mycobacterium tuberculosis
Tobin, D. M., & Ramakrishnan, L. (2008) · Cellular Microbiology · doi:10.1111/j.1462-5822.2008.01133.x · Cited by 343
Lysosomal killing of Mycobacterium mediated by ubiquitin-derived peptides is enhanced by autophagy
Alonso, S., Pethe, K., Russell, D. G., & Purdy, G. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700036104 · Cited by 318
Kana, B. D., Gordhan, B. G., Downing, K. J., Sung, N., Vostroktunova, G., Machowski, E. E., Tsenova, L., Young, M. R., Kaprelyants, A. S., Kaplan, G., et al. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.06078.x · Cited by 297
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Smoum, R., Rubinstein, A., Dembitsky, V. M., & Srebnik, M. (2012) · Chemical Reviews · doi:10.1021/cr608202m · Cited by 454
Pathogenesis, Immunology, and Diagnosis of LatentMycobacterium tuberculosisInfection
Ahmad, S. (2010) · Clinical and Developmental Immunology · doi:10.1155/2011/814943 · Cited by 292
Mycobacterium smegmatis: The Vanguard of Mycobacterial Research
Sparks, I. L., Derbyshire, K. M., Jacobs, W. R., & Morita, Y. S. (2023) · Journal of Bacteriology · doi:10.1128/jb.00337-22 · Cited by 149
The Professional Phagocyte Dictyostelium discoideum as a Model Host for Bacterial Pathogens
Bozzaro, S., & Eichinger, L. (2011) · Current Drug Targets · doi:10.2174/138945011795677782 · Cited by 122
T, J., J, R., Rajan, A., & Shankar, V. (2020) · Journal of Infection and Public Health · doi:10.1016/j.jiph.2020.06.023 · Cited by 105
Gunn-Moore, D. A., McFarland, S. E., Brewer, J. I., Crawshaw, T. R., Clifton‐Hadley, R. S., Kovalik, M., & Shaw, D. J. (2011) · Journal of Feline Medicine and Surgery · doi:10.1016/j.jfms.2011.07.012 · Cited by 101
Mycoredoxin‐1 is one of the missing links in the oxidative stress defence mechanism of M ycobacteria
Laer, K. V., Buts, L., Foloppe, N., Vertommen, D., Belle, K. V., Wahni, K., Roos, G., Nilsson, L., Mateos, L. M., Rawat, M., et al. (2012) · Molecular Microbiology · doi:10.1111/mmi.12030 · Cited by 91
New approaches in the diagnosis and treatment of latent tuberculosis infection
Ahmad, S. (2010) · Respiratory Research · doi:10.1186/1465-9921-11-169 · Cited by 94
Intercellular communication and conjugation are mediated by ESX secretion systems in mycobacteria
Gray, T. A., Clark, R. R., Boucher, N., Lapierre, P., Smith, C., & Derbyshire, K. M. (2016) · Science · doi:10.1126/science.aag0828 · Cited by 84
Antimycobacterial activity in vitro of pigments isolated from Antarctic bacteria
Mojib, N., Philpott, R., Huang, J. P., Niederweis, M., & Bej, A. K. (2010) · Antonie van Leeuwenhoek · doi:10.1007/s10482-010-9470-0 · Cited by 76
Blending genomes: distributive conjugal transfer in mycobacteria, a sexier form of HGT
Gray, T. A., & Derbyshire, K. M. (2018) · Molecular Microbiology · doi:10.1111/mmi.13971 · Cited by 70
Unexpected N-acetylation of capreomycin by mycobacterial Eis enzymes
Houghton, J. L., Green, K. D., Pricer, R. E., Mayhoub, A. S., & Garneau‐Tsodikova, S. (2012) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dks497 · Cited by 65
Gunn-Moore, D. A., McFarland, S. E., Schock, A., Brewer, J. I., Crawshaw, T. R., Clifton‐Hadley, R. S., & Shaw, D. J. (2011) · Journal of Feline Medicine and Surgery · doi:10.1016/j.jfms.2011.09.009 · Cited by 57
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
Hussain, A., Singh, S., Das, S. S., AnjiReddy, K., Karpagam, S., & Shakeel, F. (2019) · Current Drug Delivery · doi:10.2174/1567201816666190201144815 · Cited by 52
Agrawal, P., Miryala, S., & Varshney, U. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122076 · Cited by 51
Küçükyıldırım, S., Long, H., Sung, W., Miller, S. F., Doak, T. G., & Lynch, M. (2016) · G3 Genes Genomes Genetics · doi:10.1534/g3.116.030130 · Cited by 57
Dragset, M. S., Ioerger, T. R., Zhang, Y. J., Mærk, M., Ginbot, Z., Sacchettini, J. C., Flo, T. H., Rubin, E. J., & Steigedal, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-47905-y · Cited by 49
Chen, W., Green, K. D., Tsodikov, O. V., & Garneau‐Tsodikova, S. (2012) · Biochemistry · doi:10.1021/bi3004473 · Cited by 49
Kennedy, G. M., Hooley, G. C., Champion, M. M., Medie, F. M., & Champion, P. A. D. (2014) · Journal of Bacteriology · doi:10.1128/jb.01502-14 · Cited by 47
A Mycobacterial Systems Resource for the Research Community
Judd, J. A., Canestrari, J., Clark, R., Joseph, A., Lapierre, P., Lasek-Nesselquist, E., Mir, M., Palumbo, M., Smith, C., Stone, M., et al. (2021) · mBio · doi:10.1128/mbio.02401-20 · Cited by 45
Selective targeting of Mycobacterium smegmatis with trehalose-functionalized nanoparticles
Jayawardana, K. W., Jayawardena, H. S. N., Wijesundera, S. A., Zoysa, T. D., Sundhoro, M., & Yan, M. (2015) · Chemical Communications · doi:10.1039/c5cc04251h · Cited by 44
Chofor, R., Sooriyaarachchi, S., Risseeuw, M., Bergfors, T., Pouyez, J., Johny, C., Haymond, A. N., Everaert, A., Dowd, C. S., Maes, L. J. R. M., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm5014264 · Cited by 46
Esx Systems and the Mycobacterial Cell Envelope: What's the Connection?
Bosserman, R. E., & Champion, P. A. (2017) · Journal of Bacteriology · doi:10.1128/jb.00131-17 · Cited by 42
Nakedi, K. C., Nel, A. J. M., Garnett, S., Blackburn, J. M., & Soares, N. C. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00237 · Cited by 42
Mycogenic Metal Nanoparticles for the Treatment of Mycobacterioses
Simões, M. F., Ottoni, C. A., & Antunes, A. (2020) · Antibiotics · doi:10.3390/antibiotics9090569 · Cited by 41
Trofimov, V., Kicka, S., Mucaria, S., Hanna, N., Ramón, F., Peral, L. V.-G. D., Lelièvre, J., Ballell, L., Scapozza, L., Besra, G. S., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-22228-6 · Cited by 35
Gunn-Moore, D. A., Gaunt, C., & Shaw, D. J. (2012) · Transboundary and Emerging Diseases · doi:10.1111/j.1865-1682.2012.01352.x · Cited by 38
Bosserman, R. E., Nicholson, K. R., Champion, M. M., & Champion, P. A. D. (2019) · Journal of Bacteriology · doi:10.1128/jb.00760-18 · Cited by 38
Multi-Omics Technologies Applied to Tuberculosis Drug Discovery
Goff, A., Cantillon, D. M., Wildner, L. M., & Waddell, S. J. (2020) · Applied Sciences · doi:10.3390/app10134629 · Cited by 38
Sanchez, K. G., Ferrell, M. J., Chirakos, A. E., Nicholson, K. R., Abramovitch, R. B., Champion, M. M., & Champion, P. A. D. (2020) · mBio · doi:10.1128/mbio.02807-19 · Cited by 38
Aro, A. O., Dzoyem, J. P., Hlokwe, T. M., Madoroba, E., Eloff, J. N., & McGaw, L. J. (2015) · Phytotherapy Research · doi:10.1002/ptr.5338 · Cited by 35
Homeostasis of N-α-Terminal Acetylation of EsxA Correlates with Virulence in Mycobacterium marinum
Medie, F. M., Champion, M. M., Williams, E. A., & Champion, P. A. D. (2014) · Infection and Immunity · doi:10.1128/iai.02153-14 · Cited by 34
Noble Metal Organometallic Complexes Display Antiviral Activity against SARS-CoV-2
Chuong, C., DuChane, C. M., Webb, E. M., Rai, P., Marano, J. M., Bernier, C. M., Merola, J. S., & Weger‐Lucarelli, J. (2021) · Viruses · doi:10.3390/v13060980 · Cited by 31
Cao, B., Chen, X., Yamaryo‐Botté, Y., Richardson, M. B., Martin, K. L., Khairallah, G. N., Rupasinghe, T., O’Flaherty, R., O’Hair, R. A. J., Ralton, J. E., et al. (2013) · The Journal of Organic Chemistry · doi:10.1021/jo302508e · Cited by 30
Donini, S., Garavaglia, S., Ferraris, D. M., Miggiano, R., Mori, S., Shibayama, K., & Rizzi, M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0175815 · Cited by 28
Baronian, G., Ginda, K., Berry, L., Cohen‐Gonsaud, M., Zakrzewska‐Czerwińska, J., Jakimowicz, D., & Molle, V. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119907 · Cited by 30
Knobloch, P., Koliwer‐Brandl, H., Arnold, F. M., Hanna, N., Gonda, I., Adenau, S., Personnic, N., Barisch, C., Seeger, M. A., Soldati, T., et al. (2020) · Cellular Microbiology · doi:10.1111/cmi.13163 · Cited by 27
Butler, R. E., Smith, A. A., Mendum, T. A., Chandran, A., Wu, H., Lefrançois, L. H., Chambers, M. A., Soldati, T., & Stewart, G. R. (2020) · The ISME Journal · doi:10.1038/s41396-019-0572-z · Cited by 28
Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis
Tan, Y. Z., Rodrigues, J., Keener, J. E., Zheng, R. B., Brunton, R., Kloss, B., Giacometti, S. I., Rosário, A. L., Zhang, L., Niederweis, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17202-8 · Cited by 26
Banda, S., Cao, N., & Tse‐Dinh, Y. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.08.011 · Cited by 24
Unique structural features of the Mycobacterium ribosome
Kushwaha, A. K., & Bhushan, S. (2019) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2019.12.001 · Cited by 24
Proteome turnover in bacteria: current status for C orynebacterium glutamicum and related bacteria
Trötschel, C., Albaum, S. P., & Poetsch, A. (2013) · Microbial Biotechnology · doi:10.1111/1751-7915.12035 · Cited by 25
Thompson, C. R., Champion, M. M., & Champion, P. A. D. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00373 · Cited by 21
Wray, R., Herrera, N., Iscla, I., Wang, J., & Blount, P. (2019) · Molecular Microbiology · doi:10.1111/mmi.14325 · Cited by 22
The Caenorhabditis elegans p38 MAPK Gene plays a key role in protection from mycobacteria
Galbadage, T., Shepherd, T. F., Cirillo, S. L. G., Gumienny, T. L., & Cirillo, J. D. (2016) · MicrobiologyOpen · doi:10.1002/mbo3.341 · Cited by 21
A single regulator NrtR controls bacterial NAD+ homeostasis via its acetylation
Gao, R., Wei, W., Hassan, B. H., Li, J., Deng, J., & Feng, Y. (2019) · eLife · doi:10.7554/elife.51603 · Cited by 21
Kumar, N., Sharma, S., & Kaushal, P. S. (2024) · Nature Communications · doi:10.1038/s41467-024-44879-y · Cited by 20
Namanja-Magliano, H. A., Evans, G. B., Harijan, R. K., Tyler, P. C., & Schramm, V. L. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00576 · Cited by 20
Characteristics of Mycobacterium smegmatis J15cs strain lipids
Fujiwara, N., Naka, T., Ogawa, M., Yamamoto, R., Ogura, H., & Taniguchi, H. (2011) · Tuberculosis · doi:10.1016/j.tube.2011.10.001 · Cited by 19
Yang, Y., Xu, Y., Yue, Y., Wang, H., Cui, Y., Pan, M., Zhang, X., Zhang, L., Li, H., Xu, M., et al. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00394 · Cited by 19
Protein synthesis in Mycobacterium tuberculosis as a potential target for therapeutic interventions
Kumar, N., Sharma, S., & Kaushal, P. S. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.101002 · Cited by 19
Child, S. A., Ghith, A., Bruning, J. B., & Bell, S. G. (2020) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2020.111116 · Cited by 17
Bychenko, O. S., Skvortsova, Y. V., Ziganshin, R., Grigorov, A., Aseev, L. V., Ostrik, A., Kaprelyants, A. S., Salina, E. G., & Azhikina, T. L. (2021) · Microorganisms · doi:10.3390/microorganisms9020414 · Cited by 16
Bao, L., Hu, J., Zhan, B., Chi, M., Li, Z., Wang, S., Shan, C., Zhao, Z., Guo, Y., Ding, X., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38045-z · Cited by 16
de la Peña, L., Schlembach, I., Lackner, G., & Regestein, L. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.593781 · Cited by 16
Gupta, R. K., Chauhan, S., & Tyagi, J. S. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08130.x · Cited by 13
Mathematical models of drug-resistant tuberculosis lack bacterial heterogeneity: A systematic review
Fuller, N. M., McQuaid, C. F., Harker, M. J., Weerasuriya, C. K., McHugh, T. D., & Knight, G. M. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1011574 · Cited by 12
Factores de virulencia de Mycobacterium tuberculosis
Maulén, N. P. (2011) · Revista médica de Chile · doi:10.4067/s0034-98872011001200012 · Cited by 12
Nyinoh, I. W., & McFadden, J. (2018) · Drug Development Research · doi:10.1002/ddr.21497 · Cited by 14
Kopiasz, R. J., ZABOST, A. T., Myszka, M., Kuźmińska, A., Drężek, K., Mierzejewska, J., Tomaszewski, W., Iwańska, A., AUGUSTYNOWICZ-KOPEĆ, E. M., Ciach, T., et al. (2022) · RSC Advances · doi:10.1039/d2ra04121a · Cited by 11
Pal, R., Hameed, S., Kumar, P., Singh, S., & Fatima, Z. (2019) · 3 Biotech · doi:10.1007/s13205-019-1645-4 · Cited by 11
Carvalho, C. D. S., Kasmapour, B., Gronow, A., Rohde, M., Rabinovitch, M., & Gutierrez, M. G. (2011) · Cellular Microbiology · doi:10.1111/j.1462-5822.2011.01615.x · Cited by 10
Small RNA F6 Provides Mycobacterium smegmatis Entry into Dormancy
Grigorov, A., Bychenko, O. S., Salina, E. G., Skvortsova, Y. V., Мазурова, А. С., Skvortsov, T., Kaprelyants, A. S., & Azhikina, T. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111536 · Cited by 10
Sagong, H.-Y., Hong, J., & Kim, K. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.07.117 · Cited by 10
Wen, Z., Fang, C., Liu, X., Liu, Y., Li, M., Yuan, Y., Han, Z., Wang, C., Zhang, T., & Sun, C. (2023) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2023.2171233 · Cited by 9
The genetic proteome: Using genetics to inform the proteome of mycobacterial pathogens
Nicholson, K. R., Mousseau, C. B., Champion, M. M., & Champion, P. A. D. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009124 · Cited by 8
Host–pathogen systems for early drug discovery against tuberculosis
Trofimov, V., Costa-Gouveia, J., Hoffmann, E., & Brodin, P. M. (2017) · Current Opinion in Microbiology · doi:10.1016/j.mib.2017.11.017 · Cited by 8
Mohamed, H., Child, S. A., Bruning, J. B., & Bell, S. G. (2022) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2022.106097 · Cited by 8
Ghith, A., Doherty, D. Z., Bruning, J. B., Russell, R. A., Voss, J. J. D., & Bell, S. G. (2022) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.2c00215 · Cited by 7
Neumann, A.-C., Bauer, D., Höelscher, M., Haisch, C., & Wieser, A. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b03646 · Cited by 8
Bao, Y., Wang, L., & Sun, J. (2020) · Virulence · doi:10.1080/21505594.2020.1867438 · Cited by 7
Draft Genome Sequence of MKD8, a Conjugal Recipient Mycobacterium smegmatis Strain
Gray, T. A., Palumbo, M. J., & Derbyshire, K. M. (2013) · Genome Announcements · doi:10.1128/genomea.00148-13 · Cited by 7
Anti-biofilm potential of human senescence marker protein 30 against Mycobacterium smegmatis
Yadav, P., Goel, M., & Gupta, T. (2023) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-023-03843-6 · Cited by 6
Valente, E., Simões, M. F., Testa, B., & Constantino, L. (2011) · Journal of Microbiological Methods · doi:10.1016/j.mimet.2011.02.003 · Cited by 6
Gao, S., He, Y., Deng, X., Lu, N., Bao, J., Li, A., He, X., He, S., Fu, N., Hosyanto, F. F., et al. (2025) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00856 · Cited by 5
Karade, S. S., Pandey, S., Ansari, A., Das, S., Tripathi, S., Arora, A., Chopra, S., Pratap, J. V., & Dasgupta, A. (2018) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2018.10.011 · Cited by 5
Lienard, J., Munke, K., & Carlsson, F. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3243-7_21 · Cited by 5
Golla, A. C., Chaumontet, J., Voorde, R. V., & Danelishvili, L. (2024) · Antibiotics · doi:10.3390/antibiotics13111009 · Cited by 4
Agarwal, A. A., Georgiades, J. D., Dranow, D. M., Lorimer, D. D., Edwards, T. E., Barrett, K. F., Craig, J. K., A, W. C. V. V., Myler, P. J., & Smith, C. L. (2025) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x25000858 · Cited by 4
Antimycobacterial Activity of Sida hermaphrodita (L.) Rusby (Malvaceae) Seed Extract
Lewtak, K., Czaplewska, P., Wydrych, J., Keller, R., Nowicka, A., Skrzypiec, K., & Fiołka, M. J. (2023) · Cells · doi:10.3390/cells12030397 · Cited by 4
Cell wall and immune modulation by Rv1800 (PPE28) helps M. smegmatis to evade intracellular killing
Anand, P. K., Saini, V., Kaur, J., Kumar, A., & Kaur, J. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.125837 · Cited by 4
The oxidation of steroid derivatives by the CYP125A6 and CYP125A7 enzymes from Mycobacterium marinum
Ghith, A., & Bell, S. G. (2023) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2023.106406 · Cited by 4
Judd, J., Boucher, N., Roey, E. V., Gray, T. A., & Derbyshire, K. M. (2017) · Journal of Bacteriology · doi:10.1128/jb.00410-17 · Cited by 4
Quantifying and Characterizing Distributive Conjugal Transfer in Mycobacterium smegmatis
Clark, R. R., Gray, T. A., & Derbyshire, K. M. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9877-7_9 · Cited by 4
Khan, S. S., Sudasinghe, T. D., Landgraf, A. D., Ronning, D. R., & Sucheck, S. J. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.1c00283 · Cited by 4
Ghith, A., Bruning, J. B., & Bell, S. G. (2023) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2023.109554 · Cited by 4
Production of highly soluble native human paraoxonase 2 with potential anti-biofilm property
Parween, F., Yadav, P., Singh, K., & Gupta, T. (2022) · Preparative Biochemistry & Biotechnology · doi:10.1080/10826068.2022.2101000 · Cited by 4
Wang, J., & Lee, S. (2025) · Pathogens · doi:10.3390/pathogens14050472 · Cited by 3
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Al-Saadi, A., AL-Khafaji, J. K. T., & Sheriff, N. A. (2013) · Journal of Advances in Medicine and Medical Research · doi:10.9734/bjmmr/2014/6671 · Cited by 2
Metadata
- Authors
- Shiloh, M. U., & DiGiuseppe Champion, P. A.
- Affiliations
- University of California, San Francisco (US)
- ORCID
- Shiloh, Michael U
- Venue
- Current Opinion in Microbiology
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 13
- Issue
- 1
- Pages
- 86-92
- ISSN
- 1369-5274 (ISSN-L)
- PMC
- PMC2876343
- OpenAlex
- W2070413611
- Cited by
- 137
- References
- 50
- Citations by year
- 2026: 4 · 2025: 12 · 2024: 9 · 2023: 11 · 2022: 5 · 2021: 10 · 2020: 11 · 2019: 11 · 2018: 8 · 2017: 8 · 2016: 5 · 2015: 8 · 2014: 6 · 2013: 7 · 2012: 8
- FWCI
- 0.86
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Current Opinion in Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (K08AI076632)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Health Sciences › Medicine › Epidemiology › Mycobacterium research and diagnosis
- Health Sciences › Medicine › Infectious Diseases › Infectious Diseases and Tuberculosis
- Keywords
- Mycobacterium tuberculosis, tuberculosis pathogenesis, Mycobacterium bovis BCG, Mycobacterium marinum, Mycobacterium smegmatis, secretion systems, virulence, latent infection, host response, recombineering, inducible promoters
- MeSH terms
- Humans, Models, Biological, Mycobacterium bovis, Mycobacterium tuberculosis, Tuberculosis, Virulence, Mycobacterium smegmatis, Host-Pathogen Interactions
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