A mycobacterium ESX-1-secreted virulence factor with unique requirements for export.

New use of BCG for recombinant vaccines

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

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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

Identification and Characterization of the New Osteoclast Progenitor with Macrophage Phenotypes Being Able to Differentiate into Mature Osteoclasts

Takeshita, S., Kaji, K., & Kudō, A. (2000) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2000.15.8.1477 · Cited by 602 · 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

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

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

Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcerPreprint

Stinear, T. P., Seemann, T., Pidot, S. J., Frigui, W., Reysset, G., Garnier, T., Meurice, G., Simon, D., Bouchier, C., Ma, L., et al. (2007) · Genome Research · doi:10.1101/gr.5942807 · Cited by 392 · 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

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

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

Tuberculous Granuloma Formation Is Enhanced by a Mycobacterium Virulence Determinant

Volkman, H. E., Clay, H., Beery, D., Chang, J. C., Sherman, D. R., & Ramakrishnan, L. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020367 · Cited by 311 · see citing works

C-Terminal Signal Sequence Promotes Virulence Factor Secretion in Mycobacterium tuberculosis

Champion, P. A. D., Stanley, S. A., Champion, M. M., Brown, E. J., & Cox, J. S. (2006) · Science · doi:10.1126/science.1131167 · Cited by 219 · see citing works

A non‐RD1 gene cluster is required for Snm secretion in <i>Mycobacterium tuberculosis</i>

MacGurn, J. A., Raghavan, S., Stanley, S. A., & Cox, J. S. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04800.x · Cited by 186 · see citing works

A Genetic Screen forMycobacterium tuberculosisMutants Defective for Phagosome Maturation Arrest Identifies Components of the ESX-1 Secretion System

MacGurn, J. A., & Cox, J. S. (2007) · Infection and Immunity · doi:10.1128/iai.01872-06 · Cited by 183 · see citing works

The ESAT-6/CFP-10 secretion system of Mycobacterium marinum modulates phagosome maturation

Tan, T., Lee, W. L., Alexander, D. C., Grinstein, S., & Liu, J. (2006) · Cellular Microbiology · doi:10.1111/j.1462-5822.2006.00721.x · Cited by 172 · see citing works

Evolution of Mycobacterium ulcerans and Other Mycolactone-Producing Mycobacteria from a Common Mycobacterium marinum Progenitor

Yip, M. J., Porter, J. L., Fyfe, J., Lavender, C. J., Portaels, F., Rhodes, M. W., Kator, H. I., Colorni, A., Jenkin, G., & Stinear, T. P. (2006) · Journal of Bacteriology · doi:10.1128/jb.01442-06 · Cited by 169 · see citing works

Comparative proteome analysis of culture supernatant proteins from virulent Mycobacterium tuberculosis H37Rv and attenuated M. bovis BCG Copenhagen

Mattow, J., Schaible, U. E., Schmidt, F., Hagens, K., Siejak, F., Brestrich, G., Haeselbarth, G., Müller, E., Jungblut, P. R., & Kaufmann, S. H. E. (2003) · Electrophoresis · doi:10.1002/elps.200305601 · Cited by 162 · see citing works

A Protein Secretion Pathway Critical for Mycobacterium tuberculosis Virulence Is Conserved and Functional in Mycobacterium smegmatis

Converse, S. E., & Cox, J. S. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.4.1238-1245.2005 · Cited by 154 · see citing works

Ubiquitin-Related Proteins Regulate Interaction of Vimentin Intermediate Filaments with the Plasma Membrane

Wu, A. L., Wang, J., Zheleznyak, A., & Brown, E. J. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80212-9 · Cited by 140 · see citing works

The RD1 virulence locus of Mycobacterium tuberculosis regulates DNA transfer in Mycobacterium smegmatis

Flint, J. L., Kowalski, J. C., Karnati, P. K., & Derbyshire, K. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404892101 · Cited by 134 · see citing works

CFP10 discriminates between nonacetylated and acetylated ESAT‐6 of Mycobacterium tuberculosis by differential interaction

Okkels, L. M., Müller, E., Schmid, M., Rosenkrands, I., Kaufmann, S. H. E., Andersen, P. L., & Jungblut, P. R. (2004) · PROTEOMICS · doi:10.1002/pmic.200400906 · Cited by 100 · see citing works

Transposon Mutagenesis ofMycobacterium marinumIdentifies a Locus Linking Pigmentation and Intracellular Survival

Gao, L., Groger, R. K., Cox, J. S., Beverley, S. M., Lawson, E. H., & Brown, E. J. (2003) · Infection and Immunity · doi:10.1128/iai.71.2.922-929.2003 · Cited by 93 · see citing works

Purification of a mycobacterial adhesin for fibronectin

Ratliff, T. L., McCarthy, R., Telle, W., & Brown, E. J. (1993) · Infection and Immunity · doi:10.1128/iai.61.5.1889-1894.1993 · Cited by 81 · see citing works

Protein-Protein Interactions of Proteins from the ESAT-6 Family of Mycobacterium tuberculosis

Okkels, L. M., & Andersen, P. L. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.8.2487-2491.2004 · Cited by 68 · see citing works

The ubiquitin-related protein PLIC-1 regulates heterotrimeric G protein function through association with Gβγ

N’Diaye, E.-N., & Brown, E. J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200307155 · Cited by 51 · see citing works

In Vivo Interaction between the Polyprenol Phosphate Mannose Synthase Ppm1 and the Integral Membrane Protein Ppm2 from Mycobacterium smegmatis Revealed by a Bacterial Two-hybrid System

Baulard, A. R., Gurcha, S. S., Engohang‐Ndong, J., Gouffi, K., Locht, C., & Besra, G. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207922200 · Cited by 45 · see citing works

Generation of Attenuated Mycobacterium bovis Strains by Signature-Tagged Mutagenesis for Discovery of Novel Vaccine Candidates

Collins, D. M., Skou, B., White, S., Bassett, S. A., Collins, L. J., For, R. J., Hurr, K., Hotter, G. S., & de Lisle, G. W. (2005) · Infection and Immunity · doi:10.1128/iai.73.4.2379-2386.2005 · Cited by 28 · see citing works

Virulence factors of the Mycobacterium tuberculosis complex

Forrellad, M. A., Klepp, L. I., Gioffré, A., y García, J. S., Morbidoni, H. R., Santangelo, M. D. L. P., Cataldi, A. A., & Bigi, F. (2013) · Virulence · doi:10.4161/viru.22329 · Cited by 646 · see citing works

Mycobacterium tuberculosis and the Macrophage: Maintaining a Balance

Pieters, J. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.05.006 · Cited by 498 · see citing works

ESX secretion systems: mycobacterial evolution to counter host immunity

Gröschel, M. I., Sayes, F., Simeone, R., Majlessi, L., & Brosch, R. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.131 · Cited by 382 · see citing works

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 · 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

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

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

Evidence for Pore Formation in Host Cell Membranes by ESX-1-Secreted ESAT-6 and Its Role in Mycobacterium marinum Escape from the Vacuole

Smith, J., Manoranjan, J., Pan, M., Bohsali, A., Xu, J., Liu, J., McDonald, K. L., Szyk, A., LaRonde-LeBlanc, N. A., & Gao, L. (2008) · Infection and Immunity · doi:10.1128/iai.00614-08 · Cited by 291 · see citing works

PPE and PE_PGRS proteins of Mycobacterium marinum are transported via the type VII secretion system ESX‐5

Abdallah, A. M., Verboom, T., Weerdenburg, E. M., van Pittius, N. C. G., Mahasha, P. W., Jiménez, C. R., Parra, M., Cadieux, N., Brennan, M. J., Appelmelk, B. J., et al. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06783.x · Cited by 268 · see citing works

Linking the Transcriptional Profiles and the Physiological States of Mycobacterium tuberculosis during an Extended Intracellular Infection

Rohde, K. H., Veiga, D. F. T., Caldwell, S., Balázsi, G., & Russell, D. G. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002769 · Cited by 269 · see citing works

Genome-Scale Identification of Legionella pneumophila Effectors Using a Machine Learning Approach

Burstein, D. E., Zusman, T., Degtyar, E., Viner, R., Segal, G., & Pupko, T. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000508 · Cited by 259 · see citing works

Dynamic antibody responses to the Mycobacterium tuberculosis proteome

Kunnath-Velayudhan, S., Salamon, H., Wang, H., Davidow, A. L., Molina, D. M., Huynh, V. T., Cirillo, D. M., Michel, G., Talbot, E. A., Perkins, M. D., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009080107 · Cited by 256 · see citing works

Take five — Type VII secretion systems of Mycobacteria

Houben, E. N. G., Korotkov, K. V., & Bitter, W. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.11.003 · Cited by 223 · see citing works

PhoP: A Missing Piece in the Intricate Puzzle of Mycobacterium tuberculosis Virulence

Gonzalo‐Asensio, J., Mostowy, S., Harders-Westerveen, J., Huygen, K., Hernández‐Pando, R., Thole, J. E. R., Behr, M. A., Gicquel, B., & Martı́n, C. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003496 · Cited by 222 · see citing works

Disruption of the ESX‐5 system of <i>Mycobacterium tuberculosis</i> causes loss of PPE protein secretion, reduction of cell wall integrity and strong attenuation

Bottai, D., Di Luca, M., Majlessi, L., Frigui, W., Simeone, R., Sayes, F., Bitter, W., Brennan, M. J., Leclerc, C., Batoni, G., et al. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08001.x · Cited by 210 · see citing works

General secretion signal for the mycobacterial type VII secretion pathway

Daleke, M. H., Ummels, R., Bawono, P., Heringa, J., Vandenbroucke‐Grauls, C. M. J. E., Luirink, J., & Bitter, W. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119453109 · Cited by 192 · see citing works

High Content Phenotypic Cell-Based Visual Screen Identifies Mycobacterium tuberculosis Acyltrehalose-Containing Glycolipids Involved in Phagosome Remodeling

Brodin, P. M., Poquet, Y., Levillain, F., Péguillet, I., Larrouy-Maumus, G. J., Gilleron, M., Ewann, F., Christophe, T., Fenistein, D., Jang, J., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001100 · Cited by 186 · see citing works

Adaptation to Environmental Stimuli within the Host: Two-Component Signal Transduction Systems of Mycobacterium tuberculosis

Bretl, D. J., Demetriadou, C., & Zahrt, T. C. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05004-11 · Cited by 180 · see citing works

Infection of macrophages withMycobacterium tuberculosisinduces global modifications to phagosomal function

Podinovskaia, M., Lee, W., Caldwell, S., & Russell, D. G. (2012) · Cellular Microbiology · doi:10.1111/cmi.12092 · Cited by 171 · see citing works

Composition of the type <scp>VII</scp> secretion system membrane complex

Houben, E. N. G., Bestebroer, J., Ummels, R., Wilson, L., Piersma, S. R., Jiménez, C. R., Ottenhoff, T. H. M., Luirink, J., & Bitter, W. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08206.x · Cited by 168 · see citing works

ESX‐1 secreted virulence factors are recognized by multiple cytosolic AAA ATPases in pathogenic mycobacteria

Champion, P. A. D., Champion, M. M., Manzanillo, P. S., & Cox, J. S. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06821.x · Cited by 149 · see citing works

Mycobacterium tuberculosis MycP1 Protease Plays a Dual Role in Regulation of ESX-1 Secretion and Virulence

Ohol, Y. M., Goetz, D. H., Chan, K., Shiloh, M. U., Craik, C. S., & Cox, J. S. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.02.006 · Cited by 149 · see citing works

Conserved Pro-Glu (PE) and Pro-Pro-Glu (PPE) Protein Domains Target LipY Lipases of Pathogenic Mycobacteria to the Cell Surface via the ESX-5 Pathway

Daleke, M. H., Cascioferro, A., de Punder, K., Ummels, R., Abdallah, A. M., van der Wel, N. N., Peters, P. J., Luirink, J., Manganelli, R., & Bitter, W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.204966 · Cited by 146 · see citing works

The specialized secretory apparatus ESX‐1 is essential for DNA transfer in <i>Mycobacterium smegmatis</i>

Coros, A., Callahan, B., Battaglioli, E., & Derbyshire, K. M. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06299.x · Cited by 137 · see citing works

To catch a killer. What can mycobacterial models teach us about Mycobacterium tuberculosis pathogenesis?

Shiloh, M. U., & DiGiuseppe Champion, P. A. (2010) · Current Opinion in Microbiology · doi:10.1016/j.mib.2009.11.006 · Cited by 137 · see citing works

EsaC substrate for the ESAT‐6 secretion pathway and its role in persistent infections of Staphylococcus aureus

Burts, M. L., DeDent, A. C., & Missiakas, D. M. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06324.x · Cited by 128 · see citing works

Whole genome identification of Mycobacterium tuberculosisvaccine candidates by comprehensive data mining and bioinformatic analyses

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 · see citing works

Capillary Zone Electrophoresis-Electrospray Ionization-Tandem Mass Spectrometry as an Alternative Proteomics Platform to Ultraperformance Liquid Chromatography-Electrospray Ionization-Tandem Mass Spectrometry for Samples of Intermediate Complexity

Li, Y., Champion, M. M., Sun, L., Champion, P. A. D., Wojcik, R., & Dovichi, N. J. (2012) · Analytical Chemistry · doi:10.1021/ac202899p · Cited by 128 · see citing works

Lysosomal Cathepsin Release Is Required for NLRP3-Inflammasome Activation by Mycobacterium tuberculosis in Infected Macrophages

Amaral, E. P., Riteau, N., Moayeri, M., Maier, N. K., Mayer-Barber, K. D., Pereira, R. M., Lage, S. L., Kübler, A., Bishai, W. R., Lima, M. R. D., et al. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01427 · Cited by 119 · see citing works

Polar Localization of Virulence-Related Esx-1 Secretion in Mycobacteria

Carlsson, F., Joshi, S. A., Rangell, L. K., & Brown, E. J. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000285 · Cited by 113 · see citing works

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 108 · see citing works

Mycobacterium tuberculosis Type VII Secretion System Effectors Differentially Impact the ESCRT Endomembrane Damage Response

Mittal, E., Skowyra, M. L., Uwase, G., Tinaztepe, E., Mehra, A., Köster, S., Hanson, P. I., & Philips, J. A. (2018) · mBio · doi:10.1128/mbio.01765-18 · Cited by 110 · see citing works

WXG100 Protein Superfamily Consists of Three Subfamilies and Exhibits an α-Helical C-Terminal Conserved Residue Pattern

Poulsen, C., Panjikar, S., Holton, S. J., Wilmanns, M., & Song, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089313 · Cited by 110 · see citing works

EspA Acts as a Critical Mediator of ESX1-Dependent Virulence in Mycobacterium tuberculosis by Affecting Bacterial Cell Wall Integrity

Garces, A., Atmakuri, K., Chase, M. R., Woodworth, J. S., Krastins, B., Rothchild, A. C., Ramsdell, T. L., Lopez, M. F., Behar, S. M., Sarracino, D. A., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000957 · Cited by 105 · see citing works

Zebrafish embryo screen for mycobacterial genes involved in the initiation of granuloma formation reveals a newly identified ESX-1 component

Stoop, E. J. M., Schipper, T., Huber, S. K. R., Nezhinsky, A. E., Verbeek, F. J., Gurcha, S. S., Besra, G. S., Vandenbroucke‐Grauls, C. M. J. E., Bitter, W., & van der Sar, A. M. (2011) · Disease Models & Mechanisms · doi:10.1242/dmm.006676 · Cited by 104 · see citing works

Type VII secretion systems: structure, functions and transport models

Rivera-Calzada, Á., Famelis, N., Llorca, Ó., & Geibel, S. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-021-00560-5 · Cited by 105 · see citing works

The role of autophagy in host defence against Mycobacterium tuberculosis infection

Songane, M., Kleinnijenhuis, J., Netea, M. G., & van Crevel, R. (2012) · Tuberculosis · doi:10.1016/j.tube.2012.05.004 · Cited by 101 · see citing works

Role of Cathepsins in Mycobacterium tuberculosis Survival in Human Macrophages

Pires, D., Pereira‐Marques, J., Pombo, J. P. N., Carmo, N., Bettencourt, P. J. G., Neyrolles, O., Lugo‐Villarino, G., & Anes, E. (2016) · Scientific Reports · doi:10.1038/srep32247 · Cited by 95 · see citing works

Release of mycobacterial antigens

Majlessi, L., Prados‐Rosales, R., Casadevall, A., & Brosch, R. (2015) · Immunological Reviews · doi:10.1111/imr.12251 · Cited by 93 · see citing works

Solution Structure of the Mycobacterium tuberculosis EsxG·EsxH Complex

Ilghari, D., Lightbody, K. L., Veverka, V., Waters, L. C., Muskett, F. W., Renshaw, P. S., & Carr, M. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.248732 · Cited by 88 · see citing works

Tubercle bacilli rely on a type VII army for pathogenicity

Stoop, E. J. M., Bitter, W., & van der Sar, A. M. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2012.07.001 · Cited by 90 · see citing works

Structure of EspB from the ESX-1 Type VII Secretion System and Insights into its Export Mechanism

Solomonson, M., Setiaputra, D., Makepeace, K. A. T., Lameignère, E., Petrotchenko, E. V., Conrady, D. G., Bergeron, J. R. C., Vuckovic, M., DiMaio, F., Borchers, C. H., et al. (2015) · Structure · doi:10.1016/j.str.2015.01.002 · Cited by 89 · see citing works

Mycobacterial WhiB6 Differentially Regulates ESX-1 and the Dos Regulon to Modulate Granuloma Formation and Virulence in Zebrafish

Chen, Z., Hu, Y., Cumming, B. M., Lu, P., Feng, L., Deng, J., Steyn, A. J. C., & Chen, S. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.080 · Cited by 91 · see citing works

The Mycobacterium marinum ESX-1 system mediates phagosomal permeabilization and type I interferon production via separable mechanisms

Lienard, J., Nobs, E., Lovins, V. M., Movert, E., Valfridsson, C., & Carlsson, F. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911646117 · Cited by 86 · see citing works

Mycobacterial Esx-3 Requires Multiple Components for Iron Acquisition

Siegrist, M. S., Steigedal, M., Ahmad, R., Mehra, A., Dragset, M. S., Schuster, B. M., Philips, J. A., Carr, S. A., & Rubin, E. J. (2014) · mBio · doi:10.1128/mbio.01073-14 · Cited by 87 · see citing works

The ESX-5 System of Pathogenic Mycobacteria Is Involved In Capsule Integrity and Virulence through Its Substrate PPE10

Ates, L. S., van der Woude, A. D., Bestebroer, J., van Stempvoort, G., Musters, R. J. P., García-Vallejo, J. J., Picavet, D. I., van de Weerd, R., Maletta, M., Kuijl, C. P., et al. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005696 · Cited by 86 · see citing works

MprAB Regulates theespAOperon in Mycobacterium tuberculosis and Modulates ESX-1 Function and Host Cytokine Response

Pang, X., Samten, B., Cao, G., Wang, X., Tvinnereim, A., Chen, X.-L., & Howard, S. T. (2012) · Journal of Bacteriology · doi:10.1128/jb.01067-12 · Cited by 80 · see citing works

The ins and outs of Mycobacterium tuberculosis protein export

Ligon, L. S., Hayden, J., & Braunstein, M. (2011) · Tuberculosis · doi:10.1016/j.tube.2011.11.005 · Cited by 83 · see citing works

Specific Chaperones for the Type VII Protein Secretion Pathway

Daleke, M. H., van der Woude, A. D., Parret, A. H. A., Ummels, R., de Groot, A. M., Watson, D., Piersma, S. R., Jiménez, C. R., Luirink, J., Bitter, W., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.397596 · Cited by 81 · see citing works

Mycobacterial manipulation of vacuolar sorting

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ESAT-6-Like Protein Secretion inBacillus anthracis

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