Release of mycobacterial antigens

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 · see citing works

Genes required for mycobacterial growth defined by high density mutagenesis

Sassetti, C. M., Boyd, D. H., & Rubin, E. J. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03425.x · Cited by 2,544 · see citing works

A new evolutionary scenario for the Mycobacterium tuberculosis complex

Brosch, R., Gordon, S. V., Marmiesse, M., Brodin, P. M., Buchrieser, C., Eiglmeier, K., Garnier, T., Gutierrez, C., Hewinson, R. G., Kremer, K., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052548299 · Cited by 1,605 · see citing works

Biological Functions and Biogenesis of Secreted Bacterial Outer Membrane Vesicles

Kulp, A., & Kuehn, M. J. (2010) · Annual Review of Microbiology · doi:10.1146/annurev.micro.091208.073413 · Cited by 1,540 · see citing works

Comparative Genomics of BCG Vaccines by Whole-Genome DNA Microarray

Behr, M. A., Wilson, M. A., Gill, W., Salamon, H., Schoolnik, G. K., Rane, S., & Small, P. M. (1999) · Science · doi:10.1126/science.284.5419.1520 · Cited by 1,527 · see citing works

Genetic requirements for mycobacterial survival during infection

Sassetti, C. M., & Rubin, E. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2134250100 · Cited by 1,327 · see citing works

Pathogenicity Islands and the Evolution of Microbes

Hacker, J. H., & Kaper, J. B. (2000) · Annual Review of Microbiology · doi:10.1146/annurev.micro.54.1.641 · Cited by 1,298 · see citing works

Molecular analysis of genetic differences between Mycobacterium bovis BCG and virulent M. bovis

Mahairas, G. G., Sabo, P. J., Hickey, M. J., Singh, D. C., & Stover, C. K. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.5.1274-1282.1996 · Cited by 1,103 · see citing works

High-Resolution Phenotypic Profiling Defines Genes Essential for Mycobacterial Growth and Cholesterol Catabolism

Griffin, J. E., Gawronski, J. D., DeJesus, M. A., Ioerger, T. R., Akerley, B. J., & Sassetti, C. M. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002251 · Cited by 1,048 · see citing works

RESPONSE OF CULTURED MACROPHAGES TO MYCOBACTERIUM TUBERCULOSIS , WITH OBSERVATIONS ON FUSION OF LYSOSOMES WITH PHAGOSOMES

Armstrong, J. A., & Hart, P. D. (1971) · The Journal of Experimental Medicine · doi:10.1084/jem.134.3.713 · Cited by 991 · see citing works

M. tuberculosis and M. leprae Translocate from the Phagolysosome to the Cytosol in Myeloid Cells

van der Wel, N., Hava, D., Houben, D., Fluitsma, D., van Zon, M., Pierson, J., Brenner, M., & Peters, P. J. (2007) · Cell · doi:10.1016/j.cell.2007.05.059 · Cited by 960 · see citing works

Membrane Vesicle Release in Bacteria, Eukaryotes, and Archaea: a Conserved yet Underappreciated Aspect of Microbial Life

Deatherage, B. L., & Cookson, B. T. (2012) · Infection and Immunity · doi:10.1128/iai.06014-11 · Cited by 765 · see citing works

Type VII secretion — mycobacteria show the way

Abdallah, A. M., Gey van Pittius, N. C., DiGiuseppe Champion, P. A., Cox, J., Luirink, J., Vandenbroucke-Grauls, C. M. J. E., Appelmelk, B. J., & Bitter, W. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1773 · Cited by 763 · see citing works

Host-directed therapy of tuberculosis based on interleukin-1 and type I interferon crosstalk

Mayer-Barber, K. D., Andrade, B. B., Oland, S. D., Amaral, E. P., Barber, D. L., Gonzales, J., Derrick, S. C., Shi, R., Kumar, N. P., Wei, W., et al. (2014) · Nature · doi:10.1038/nature13489 · Cited by 757 · see citing works

Extracellular M. tuberculosis DNA Targets Bacteria for Autophagy by Activating the Host DNA-Sensing Pathway

Watson, R. O., Manzanillo, P. S., & Cox, J. S. (2012) · Cell · doi:10.1016/j.cell.2012.06.040 · Cited by 755 · see citing works

The primary mechanism of attenuation of bacillus Calmette–Guérin is a loss of secreted lytic function required for invasion of lung interstitial tissue

Hsu, T., Hingley-Wilson, S. M., Chen, B., Chen, M., Dai, A. Z., Morin, P. M., Marks, C. B., Padiyar, J., Goulding, C., Gingery, M., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1635213100 · Cited by 731 · see citing works

Loss of RD1 contributed to the attenuation of the live tuberculosis vaccines <i>Mycobacterium bovis</i> BCG and <i>Mycobacterium microti</i>

Pym, A. S., Brodin, P., Brosch, R., Huerre, M., & Cole, S. T. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03237.x · Cited by 729 · see citing works

Human T cell epitopes of Mycobacterium tuberculosis are evolutionarily hyperconserved

Comas, I., Chakravartti, J., Small, P. M., Galagan, J. E., Niemann, S., Kremer, K., Ernst, J., & Gagneux, S. (2010) · Nature Genetics · doi:10.1038/ng.590 · Cited by 711 · see citing works

Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis

Strong, M., Sawaya, M. R., Wang, S., Phillips, M. L., Cascio, D., & Eisenberg, D. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602606103 · Cited by 701 · see citing works

Gram‐positive bacteria produce membrane vesicles: Proteomics‐based characterization of Staphylococcus aureus ‐derived membrane vesicles

Lee, E., Choi, D., Kim, D., Kim, J., Park, J. O., Kim, S., Kim, S., Desiderio, D. M., Kim, Y., Kim, K. P., et al. (2009) · PROTEOMICS · doi:10.1002/pmic.200900338 · Cited by 672 · see citing works

Recombinant BCG exporting ESAT-6 confers enhanced protection against tuberculosis

Pym, A. S., Brodin, P., Majlessi, L., Brosch, R., Demangel, C., Williams, A., Griffiths, K. E., Marchal, G., Leclerc, C., & Cole, S. T. (2003) · Nature Medicine · doi:10.1038/nm859 · Cited by 644 · see citing works

Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature‐tagged transposon mutagenesis

Camacho, L. R., Ensergueix, D., Pérez‐Herrán, E., Gicquel, B., & Guilhot, C. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01593.x · Cited by 616 · see citing works

Pre-Columbian mycobacterial genomes reveal seals as a source of New World human tuberculosis

Bos, K. I., Harkins, K. M., Herbig, A., Coscollá, M., Weber, N., Comas, I., Forrest, S. A., Bryant, J. M., Harris, S. R., Schuenemann, V. J., et al. (2014) · Nature · doi:10.1038/nature13591 · Cited by 608 · see citing works

Disclosure of the mycobacterial outer membrane: Cryo-electron tomography and vitreous sections reveal the lipid bilayer structure

Hoffmann, C., Leis, A., Niederweis, M., Plitzko, J. M., & Engelhardt, H. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709530105 · Cited by 596 · see citing works

Deletion of RD1 from<i>Mycobacterium tuberculosis</i>Mimics Bacille Calmette‐Guérin Attenuation

Lewis, K. N., Liao, R., Guinn, K. M., Hickey, M. J., Smith, S., Behr, M. A., & Sherman, D. R. (2003) · The Journal of Infectious Diseases · doi:10.1086/345862 · Cited by 588 · see citing works

Purification and characterization of a low-molecular-mass T-cell antigen secreted by Mycobacterium tuberculosis

Sørensen, A. L., Nagai, S., Houen, G., Andersen, P., & Andersen, A. B. (1995) · Infection and Immunity · doi:10.1128/iai.63.5.1710-1717.1995 · Cited by 586 · see citing works

The Tat protein export pathway

Berks, B. C., Sargent, F., & Palmer, T. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01719.x · Cited by 578 · see citing works

Insights from the complete genome sequence of <i>Mycobacterium marinum</i> on the evolution of <i>Mycobacterium tuberculosis</i>

Stinear, T. P., Seemann, T., Harrison, P. F., Jenkin, G. A., Davies, J. K., Johnson, P. D. R., Abdellah, Z., Arrowsmith, C., Chillingworth, T., Churcher, C., et al. (2008) · Genome Research · doi:10.1101/gr.075069.107 · Cited by 570 · see citing works

Acute infection and macrophage subversion by Mycobacterium tuberculosis require a specialized secretion system

Stanley, S. A., Raghavan, S., Hwang, W. W., & Cox, J. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2235593100 · Cited by 570 · see citing works

Phagosomal Rupture by Mycobacterium tuberculosis Results in Toxicity and Host Cell Death

Simeone, R., Bobard, A., Lippmann, J., Bitter, W., Majlessi, L., Brosch, R., & Enninga, J. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002507 · Cited by 561 · see citing works

Identification of variable regions in the genomes of tubercle bacilli using bacterial artificial chromosome arrays

Gordon, S. V., Brosch, R., Billault, A., Garnier, T., Eiglmeier, K., & Cole, S. T. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01383.x · Cited by 537 · see citing works

Individual RD1‐region genes are required for export of ESAT‐6/CFP‐10 and for virulence of Mycobacterium tuberculosis

Guinn, K. M., Hickey, M. J., Mathur, S. K., Zakel, K. L., Grotzke, J. E., Lewinsohn, D. M., Smith, S., & Sherman, D. R. (2004) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03844.x · Cited by 508 · see citing works

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 491 · see citing works

A Mycobacterium tuberculosis operon encoding ESAT=6 and a novel low-molecular-mass culture filtrate protein (CFP-10)

Berthet, F., Rasmussen, P. B., Rosenkrands, I., Andersen, P. L., & Gicquel, B. (1998) · Microbiology · doi:10.1099/00221287-144-11-3195 · Cited by 486 · see citing works

Evidence for occurrence of the ESAT-6 protein in Mycobacterium tuberculosis and virulent Mycobacterium bovis and for its absence in Mycobacterium bovis BCG

Harboe, M., Oettinger, T., Wiker, H. G., Rosenkrands, I., & Andersen, P. L. (1996) · Infection and Immunity · doi:10.1128/iai.64.1.16-22.1996 · Cited by 465 · see citing works

Direct Visualization of the Outer Membrane of Mycobacteria and Corynebacteria in Their Native State

Zuber, B., Chami, M., Houssin, C., Dubochet, J., Griffiths, G., & Daffé, M. (2008) · Journal of Bacteriology · doi:10.1128/jb.01919-07 · Cited by 458 · see citing works

Mycobacterium Tuberculosis Activates the DNA-Dependent Cytosolic Surveillance Pathway within Macrophages

Manzanillo, P. S., Shiloh, M. U., Portnoy, D. A., & Cox, J. S. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.03.007 · Cited by 456 · see citing works

The Type I IFN Response to Infection with Mycobacterium tuberculosis Requires ESX-1-Mediated Secretion and Contributes to Pathogenesis

Stanley, S. A., Johndrow, J. E., Manzanillo, P. S., & Cox, J. S. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.5.3143 · Cited by 439 · see citing works

The Mycobacterium tuberculosis regulatory network and hypoxia

Galagan, J. E., Minch, K., Peterson, M., Lyubetskaya, A., Azizi, E., Sweet, L., Gomes, A., Rustad, T., Dolganov, G., Glotova, I., et al. (2013) · Nature · doi:10.1038/nature12337 · Cited by 431 · see citing works

Evasion of innate immunity by Mycobacterium tuberculosis: is death an exit strategy?

Behar, S. M., Divangahi, M., & Remold, H. G. (2010) · Nature Reviews Microbiology · doi:10.1038/nrmicro2387 · Cited by 427 · see citing works

Evolution and expansion of the Mycobacterium tuberculosis PE and PPE multigene families and their association with the duplication of the ESAT-6 (esx) gene cluster regions.

van Pittius, N. C. G., Sampson, S. L., Lee, H., Kim, Y., van Helden, P. D., & Warren, R. M. (2006) · BMC Evolutionary Biology · doi:10.1186/1471-2148-6-95 · Cited by 423 · see citing works

Granuloma-Specific Expression of Mycobacterium Virulence Proteins from the Glycine-Rich PE-PGRS Family

Ramakrishnan, L., Federspiel, N. A., & Falkow, S. (2000) · Science · doi:10.1126/science.288.5470.1436 · Cited by 420 · see citing works

ESX‐1‐mediated translocation to the cytosol controls virulence of mycobacteria

Houben, D., Demangel, C., van Ingen, J., Pérez, J., Baldeón, L., Abdallah, A. M., Caleechurn, L., Bottai, D., van Zon, M., de Punder, K., et al. (2012) · Cellular Microbiology · doi:10.1111/j.1462-5822.2012.01799.x · Cited by 415 · see citing works

Properties and clinical performance of vaccines containing outer membrane vesicles from Neisseria meningitidis

Holst, J., Martin, D., Arnold, R., Huergo, C. C., Oster, P., O’Hallahan, J., & Rosenqvist, E. (2009) · Vaccine · doi:10.1016/j.vaccine.2009.04.071 · Cited by 404 · see citing works

Bacillus anthracis produces membrane-derived vesicles containing biologically active toxins

Rivera, J., Cordero, R. J. B., Nakouzi, A. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008843107 · Cited by 400 · see citing works

Mutually dependent secretion of proteins required for mycobacterial virulence.

Fortune, S. M., Jaeger, A., Sarracino, D. A., Chase, M. R., Sassetti, C. M., Sherman, D. R., Bloom, B. R., & Rubin, E. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504922102 · Cited by 396 · see citing works

A mycobacterial virulence gene cluster extending RD1 is required for cytolysis, bacterial spreading and ESAT‐6 secretion

Gao, L., Guo, S., McLaughlin, B., Morisaki, H., Engel, J. N., & Brown, E. J. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04261.x · Cited by 395 · see citing works

Apoptotic Vesicles Crossprime CD8 T Cells and Protect against Tuberculosis

Winau, F., Weber, S., Sad, S., de Diego, J., Hoops, S. L., Breiden, B., Sandhoff, K., Brinkmann, V., Kaufmann, S. H. E., & Schaible, U. E. (2006) · Immunity · doi:10.1016/j.immuni.2005.12.001 · Cited by 395 · see citing works

The Mycobacterium tuberculosis PhoPR two‐component system regulates genes essential for virulence and complex lipid biosynthesis

Walters, S. B., Dubnau, E., Kolesnikova, I., Laval, F., Daffé, M., & Smith, I. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05102.x · Cited by 385 · see citing works

Pathogenesis of tuberculosis: interaction of Mycobacterium tuberculosis with macrophages

McDonough, K. A., Kress, Y., & Bloom, B. R. (1993) · Infection and Immunity · doi:10.1128/iai.61.7.2763-2773.1993 · Cited by 377 · see citing works

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 · see citing works

Mycobacteria release active membrane vesicles that modulate immune responses in a TLR2-dependent manner in mice

Prados‐Rosales, R., Baena, A., Martinez, L. R., Luque-Garcia, J. L., Kalscheuer, R., Usha, V., Cámara, C., Nosanchuk, J. D., Besra, G. S., Chen, B., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44261 · Cited by 370 · see citing works

The ESAT-6/WXG100 superfamily – and a new Gram-positive secretion system?

Pallen, M. J. (2002) · Trends in Microbiology · doi:10.1016/s0966-842x(02)02345-4 · Cited by 361 · see citing works

Mycobacterium tuberculosis and the environment within the phagosome

Rohde, K. H., Yates, R. M., Purdy, G. E., & Russell, D. G. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00547.x · Cited by 361 · see citing works

Mycobacterium tuberculosis protein ESAT-6 is a potent activator of the NLRP3/ASC inflammasome

Mishra, B. B., Moura‐Alves, P., Sonawane, A., Hacohen, N., Griffiths, G. W., Moita, L. F., & Anes, E. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2010.01450.x · Cited by 353 · see citing works

Conclusive Evidence That the Major T-cell Antigens of theMycobacterium tuberculosis Complex ESAT-6 and CFP-10 Form a Tight, 1:1 Complex and Characterization of the Structural Properties of ESAT-6, CFP-10, and the ESAT-6·CFP-10 Complex

Renshaw, P. S., Panagiotidou, P., Whelan, A. O., Gordon, S. V., Hewinson, R. G., Williamson, R. A., & Carr, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201625200 · Cited by 337 · see citing works

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 329 · see citing works

Structure and function of the complex formed by the tuberculosis virulence factors CFP‐10 and ESAT‐6

Renshaw, P. S., Lightbody, K. L., Veverka, V., Muskett, F. W., Kelly, G. P., Frenkiel, T. A., Gordon, S. V., Hewinson, R. G., Burke, B., Norman, J. C., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600732 · Cited by 329 · see citing works

Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens

Jungblut, P. R., Schaible, U. E., Mollenkopf, H., Zimny‐Arndt, U., Raupach, B., Mattow, J., Halada, P., Lamer, S., Hagens, K., & Kaufmann, S. H. E. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01549.x · Cited by 327 · see citing works

EsxA and EsxB are secreted by an ESAT-6-like system that is required for the pathogenesis of Staphylococcus aureus infections

Burts, M. L., Williams, W. A., DeBord, K. L., & Missiakas, D. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405620102 · Cited by 325 · see citing works

Membrane Vesicles Are Immunogenic Facsimiles of Salmonella typhimurium That Potently Activate Dendritic Cells, Prime B and T Cell Responses, and Stimulate Protective Immunity In Vivo

Alaniz, R. C., Deatherage, B. L., Lara, J. C., & Cookson, B. T. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.11.7692 · Cited by 321 · see citing works

ESAT-6 from Mycobacterium tuberculosis Dissociates from Its Putative Chaperone CFP-10 under Acidic Conditions and Exhibits Membrane-Lysing Activity

de Jonge, M. I., Pehau‐Arnaudet, G., Fretz, M. M., Félix, R., Bottai, D., Brodin, P. M., Honoré, N., Marchal, G., Jiskoot, W., England, P., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.00469-07 · Cited by 316 · see citing works

Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv

Målen, H., Berven, F. S., Fladmark, K. E., & Wiker, H. G. (2007) · PROTEOMICS · doi:10.1002/pmic.200600853 · Cited by 314 · see citing works

ESAT-6 proteins: protective antigens and virulence factors?

Brodin, P., Rosenkrands, I., Andersen, P., Cole, S. T., & Brosch, R. (2004) · Trends in Microbiology · doi:10.1016/j.tim.2004.09.007 · Cited by 312 · see citing works

Dissection of ESAT-6 System 1 of Mycobacterium tuberculosis and Impact on Immunogenicity and Virulence

Brodin, P. M., Majlessi, L., Marsollier, L., de Jonge, M. I., Bottai, D., Demangel, C., Hinds, J., Neyrolles, O., Butcher, P. D., Leclerc, C., et al. (2005) · Infection and Immunity · doi:10.1128/iai.74.1.88-98.2006 · Cited by 312 · see citing works

Analysis of the proteome of Mycobacterium tuberculosis in silico

Tekaia, F., Gordon, S. V., Garnier, T., Brosch, R., Barrell, B. G., & Cole, S. T. (1999) · Tubercle and Lung Disease · doi:10.1054/tuld.1999.0220 · Cited by 311 · see citing works

Systematic Genetic Nomenclature for Type VII Secretion Systems

Bitter, W., Houben, E. N. G., Bottai, D., Brodin, P., Brown, E. J., Cox, J. S., Derbyshire, K., Fortune, S. M., Gao, L.-Y., Liu, J., et al. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000507 · Cited by 307 · see citing works

Mycobacterium tuberculosis CDC1551 Induces a More Vigorous Host Response In Vivo and In Vitro, But Is Not More Virulent Than Other Clinical Isolates

Manca, C., Tsenova, L., Barry, C. E., Bergtold, A., Freeman, S. L., Haslett, P. A. J., Musser, J. M., Freedman, V. H., & Kaplan, G. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.11.6740 · Cited by 306 · see citing works

The Rieske protein from Paracoccus denitrificans is inserted into the cytoplasmic membrane by the twin‐arginine translocase

Bachmann, J., Bauer, B., Zwicker, K., Ludwig, B., & Anderka, O. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05480.x · Cited by 306 · see citing works

Direct Visualization by Cryo-EM of the Mycobacterial Capsular Layer: A Labile Structure Containing ESX-1-Secreted Proteins

Sani, M., Houben, E. N. G., Geurtsen, J., Pierson, J., de Punder, K., van Zon, M., Wever, B., Piersma, S. R., Jiménez, C. R., Daffé, M., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000794 · Cited by 306 · see citing works

Genomic analysis of smooth tubercle bacilli provides insights into ancestry and pathoadaptation of Mycobacterium tuberculosis

Supply, P., Marceau, M., Mangenot, S., Roche, D., Rouanet, C., Khanna, V., Majlessi, L., Criscuolo, A., Tap, J., Pawlik, A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2517 · Cited by 305 · see citing works

Human T Cell Responses to the ESAT‐6 Antigen fromMycobacterium tuberculosis

Ravn, P., Demissie, A., Eguale, T., Wondwosson, H., Lein, D., Amoudy, H. A., Mustafa, A. S., Jensen, A. K., Holm, A., Rosenkrands, I., et al. (1999) · The Journal of Infectious Diseases · doi:10.1086/314640 · Cited by 301 · see citing works

Mycobacterium marinum Escapes from Phagosomes and Is Propelled by Actin-based Motility

Stamm, L. M., Morisaki, J. H., Gao, L., Jeng, R. L., McDonald, K. L., Roth, R. A., Takeshita, S., Heuser, J., Welch, M. D., & Brown, E. J. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20031072 · Cited by 299 · see citing works

Protein secretion systems and adhesins: The molecular armory of Gram-negative pathogens

Gerlach, R. G., & Hensel, M. (2007) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2007.03.017 · Cited by 294 · see citing works

Cholesterol Catabolism by Mycobacterium tuberculosis Requires Transcriptional and Metabolic Adaptations

Griffin, J. E., Pandey, A. K., Gilmore, S. A., Mizrahi, V., McKinney, J. D., Bertozzi, C. R., & Sassetti, C. M. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.12.016 · Cited by 294 · see citing works

Progression to Active Tuberculosis, but Not Transmission, Varies byMycobacterium tuberculosisLineage in The Gambia

de Jong, B. C., Hill, P. C., Aiken, A. M., Awine, T., Antonio, M., Adetifa, I., Jackson-Sillah, D., Fox, A., DeRiemer, K., Gagneux, S., et al. (2008) · The Journal of Infectious Diseases · doi:10.1086/591504 · Cited by 290 · see citing works

Control of M. tuberculosis ESAT-6 Secretion and Specific T Cell Recognition by PhoP

Frigui, W., Bottai, D., Majlessi, L., Monot, M., Josselin, E., Brodin, P. M., Garnier, T., Gicquel, B., Martı́n, C., Leclerc, C., et al. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.0040033 · Cited by 283 · see citing works

Are the PE‐PGRS proteins of Mycobacterium tuberculosis variable surface antigens?

Banu, S., Honoré, N., Saint‐Joanis, B., Philpott, D. J., Prévost, M., & Cole, S. T. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02813.x · Cited by 275 · see citing works

SecA2 functions in the secretion of superoxide dismutase A and in the virulence of <i>Mycobacterium tuberculosis</i>

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Evidence that Mycobacterial PE_PGRS Proteins Are Cell Surface Constituents That Influence Interactions with Other Cells

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