The DOI matches its Crossref record; 79 of the 80 references it cites were found in a registry or an index.
Essential Role of the ESX-5 Secretion System in Outer Membrane Permeability of Pathogenic Mycobacteria
Open accessAbstract
Mycobacteria possess different type VII secretion (T7S) systems to secrete proteins across their unusual cell envelope. One of these systems, ESX-5, is only present in slow-growing mycobacteria and responsible for the secretion of multiple substrates. However, the role of ESX-5 substrates in growth and/or virulence is largely unknown. In this study, we show that esx-5 is essential for growth of both Mycobacterium marinum and Mycobacterium bovis. Remarkably, this essentiality can be rescued by increasing the permeability of the outer membrane, either by altering its lipid composition or by the introduction of the heterologous porin MspA. Mutagenesis of the first nucleotide-binding domain of the membrane ATPase EccC5 prevented both ESX-5-dependent secretion and bacterial growth, but did not affect ESX-5 complex assembly. This suggests that the rescuing effect is not due to pores formed by the ESX-5 membrane complex, but caused by ESX-5 activity. Subsequent proteomic analysis to identify crucial ESX-5 substrates confirmed that all detectable PE and PPE proteins in the cell surface and cell envelope fractions were routed through ESX-5. Additionally, saturated transposon-directed insertion-site sequencing (TraDIS) was applied to both wild-type M. marinum cells and cells expressing mspA to identify genes that are not essential anymore in the presence of MspA. This analysis confirmed the importance of esx-5, but we could not identify essential ESX-5 substrates, indicating that multiple of these substrates are together responsible for the essentiality. Finally, examination of phenotypes on defined carbon sources revealed that an esx-5 mutant is strongly impaired in the uptake and utilization of hydrophobic carbon sources. Based on these data, we propose a model in which the ESX-5 system is responsible for the transport of cell envelope proteins that are required for nutrient uptake. These proteins might in this way compensate for the lack of MspA-like porins in slow-growing mycobacteria.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“ESX-5 was suggested to be crucial for nutrient uptake and for the export of members of the PE and PPE protein families (9,32,33).”
From ESX/Type VII Secretion Systems—An Important Way Out for Mycobacterial Proteins (2019) · cites this paper as [33]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Bergey's Manual of Systematic Bacteriology
(1990) · Annals of Internal Medicine · doi:10.7326/0003-4819-112-5-391_3 · Cited by 15,633
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855
Calamita, E., Schmid, M., Kunz, M., Ndebele-Murisa, M. R., Magadza, C. H. D., Nyambe, I., & Wehrli, B. (2019) · Figshare · doi:10.26181/6153922fe919c · Cited by 4,239
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
A Model for Random Sampling and Estimation of Relative Protein Abundance in Shotgun Proteomics
Liu, H., Sadygov, R. G., & Yates, J. R. (2004) · Analytical Chemistry · doi:10.1021/ac0498563 · Cited by 2,533
Brennan, P. J., & Nikaido, H. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000333 · Cited by 2,045
New use of BCG for recombinant vaccines
Stover, C. K., de la Cruz, V. F., Fuerst, T. R., Burlein, J. E., Benson, L. A., Bennett, L. T., Bansal, G. P., Young, J. F., Lee, M., Hatfull, G. F., et al. (1991) · Nature · doi:10.1038/351456a0 · Cited by 1,492
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
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
Simultaneous assay of every Salmonella Typhi gene using one million transposon mutantsPreprint
Langridge, G. C., Phan, M.-D., Turner, D., Perkins, T. T., Parts, L., Haase, J., Charles, I., Maskell, D. J., Peters, S. E., Dougan, G., et al. (2009) · Genome Research · doi:10.1101/gr.097097.109 · Cited by 641
Flagged first, then by citations
1 of the 80 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–179 of 179
Genome-Wide Transposon Mutagenesis in Mycobacterium tuberculosis and Mycobacterium smegmatis
Majumdar, G., Mbau, R. D., Singh, V., Warner, D. F., Dragset, M. S., & Mukherjee, R. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6472-7_21 · Cited by 14
Burggraaf, M. J., Ates, L. S., Speer, A., van der Kuij, K., Kuijl, C. P., & Bitter, W. (2019) · Microbial Cell Factories · doi:10.1186/s12934-019-1093-1 · Cited by 14
Self-citationCpn60.1 (GroEL1) Contributes to Mycobacterial Crabtree Effect: Implications for Biofilm Formation
Zeng, S., Constant, P., Yang, D. M., Baulard, A. R., Lefèvre, P., Daffé, M., Wattiez, R., & Fontaine, V. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01149 · Cited by 15
Jones, B. S., Hu, D. D., Nicholson, K. R., Cronin, R. M., Weaver, S. D., Champion, M. M., & Champion, P. A. D. (2024) · mSphere · doi:10.1128/msphere.00005-24 · Cited by 13
Elliott, S. R., White, D. W., & Tischler, A. D. (2018) · Infection and Immunity · doi:10.1128/iai.00660-18 · Cited by 14
Type VII Secretion: A Highly Versatile Secretion System
Ates, L. S., Houben, E. N. G., & Bitter, W. (2016) · ASM Press eBooks · doi:10.1128/9781555819286.ch13 · Cited by 13
Self-citationZebrafish Embryo Model for Assessment of Drug Efficacy on Mycobacterial Persisters
Commandeur, S., Iakobachvili, N., Sparrius, M., Nur, M. M., Mukamolova, G. V., & Bitter, W. (2020) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00801-20 · Cited by 12
Self-citationPhosphate responsive regulation provides insights for ESX-5 function in Mycobacterium tuberculosis
Elliott, S. R., & Tischler, A. D. (2016) · Current Genetics · doi:10.1007/s00294-016-0604-4 · Cited by 12
Cantillon, D. M., Wróblewska, J. P., Cooper, I. R., Newport, M. J., & Waddell, S. J. (2021) · npj Biofilms and Microbiomes · doi:10.1038/s41522-021-00186-8 · Cited by 12
A five-antigen Esx-5a fusion delivered as a prime-boost regimen protects against M.tb challenge
Stylianou, E., Pinpathomrat, N., Sampson, O. L., Richard, A., Marcellus, & McShane, H. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1263457 · Cited by 11
Dysregulation of Mycobacterium marinum ESX-5 Secretion by Novel 1,2,4-oxadiazoles
Ho, V. Q. T., Rong, M. K., Habjan, E., Bommer, S. D., Pham, T. V., Piersma, S. R., Bitter, W., Ruijter, E., & Speer, A. (2023) · Biomolecules · doi:10.3390/biom13020211 · Cited by 12
Self-citationMycosins of the Mycobacterial Type VII ESX Secretion System: the Glue That Holds the Party Together
Chen, J. M. (2016) · mBio · doi:10.1128/mbio.02062-16 · Cited by 10
A Bridging Centrality Plugin for GEPHI and a Case Study forMycobacterium TuberculosisH37Rv
Pereira, G. M., Ghosh, P., & dos Santos, A. R. (2021) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2021.3120937 · Cited by 10
The show and tell of cross-presentation
Blander, J. M., Mon, K. J. Y., Jha, A., & Roycroft, D. (2023) · Advances in immunology · doi:10.1016/bs.ai.2023.08.002 · Cited by 9
Modulators targeting protein-protein interactions in Mycobacterium tuberculosis
Luo, G., Ming, T., Yang, L., He, L., Tao, T., & Wang, Y. (2024) · Microbiological Research · doi:10.1016/j.micres.2024.127675 · Cited by 9
Genomic Degeneration and Reduction in the Fish Pathogen Mycobacterium shottsii
Gauthier, D. T., Doss, J. H., LaGatta, M., Gupta, T., Karls, R. K., & Quinn, F. D. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.01158-21 · Cited by 9
Koleske, B. N., Saranathan, R., Schill, C., Lun, S., Vilchèze, C., Das, L., Gupta, M. K., Martinez-Martinez, Y. B., Bishai, W. R., & Jacobs, W. R. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2509997122 · Cited by 8
Small RNA Profiling in Mycobacterium Provides Insights Into Stress Adaptability
Chen, Y., Zhai, W., Zhang, K., Liu, H., Zhu, T., Su, L., Bermudez, L. E., Chen, H., & Guo, A. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.752537 · Cited by 8
Fang, Z., Newton-Foot, M., Sampson, S. L., & van Pittius, N. C. G. (2017) · BMC Research Notes · doi:10.1186/s13104-017-2752-0 · Cited by 8
ESX/Type VII Secretion Systems-An Important Way Out for Mycobacterial Proteins
Vaziri, F., & Brosch, R. (2019) · ASM Press eBooks · doi:10.1128/9781683670285.ch28 · Cited by 8
Park, H.-T., Lee, S., Ko, S., Kim, S., Park, H.-E., Shin, M., Kim, D., & Yoo, H. S. (2022) · Veterinary Research · doi:10.1186/s13567-022-01089-y · Cited by 7
Anand, P. K., Kaur, G., Saini, V., Kaur, J., & Kaur, J. (2023) · Biochimie · doi:10.1016/j.biochi.2023.05.004 · Cited by 7
van Winden, V. J. C., Bunduc, C. M., Ummels, R., Bitter, W., & Houben, E. N. G. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.040 · Cited by 8
Self-citationLuo, C., Hao, X., Wang, X. Q., Liu, M., Chen, S., Wu, C., Li, C., Chen, C., Yang, M., Xu, L., et al. (2025) · mBio · doi:10.1128/mbio.02419-25 · Cited by 6
Modipane, L., Reva, O. N., Magazi, B. T., Antiabong, J. F., Sekyere, J. O., & Mbelle, N. M. (2019) · International Journal of Infectious Diseases · doi:10.1016/j.ijid.2019.08.010 · Cited by 6
Foulon, M., Listian, S. A., Soldati, T., & Barisch, C. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91948-7.00011-7 · Cited by 7
Gkragkopoulou, P., Garrett, S., Shah, P. Y., Grebenc, D. W., Klein, T. A., Kim, Y., & Whitney, J. C. C. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2503581122 · Cited by 5
Block, A. M., Nair, R. R., Meikle, V., Wiegert, P. C., White, D. W., Zhang, L., Niederweis, M., & Tischler, A. D. (2026) · mBio · doi:10.1128/mbio.03500-25 · Cited by 5
Zhou, K., Xie, L., Xu, X., & Sun, J. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.880943 · Cited by 6
Evolution of the PE_PGRS Proteins of Mycobacteria: Are All Equal or Are Some More Equal than Others?
Chen, B., Bajramović, B., Vriesendorp, B., & Spaink, H. P. (2025) · Biology · doi:10.3390/biology14030247 · Cited by 5
Nair, R. R., Meikle, V., Dubey, S., Pavlenok, M., Tischler, A. D., & Niederweis, M. (2025) · Nature Communications · doi:10.1038/s41467-025-65061-y · Cited by 9
Modulating mycobacterial envelope integrity for antibiotic synergy with benzothiazoles
Habjan, E., Lepioshkin, A., Charitou, V., Egorova, A., Kazakova, E., Ho, V. Q. T., Bitter, W., Makarov, V., & Speer, A. (2024) · Life Science Alliance · doi:10.26508/lsa.202302509 · Cited by 5
Self-citationProtein Export into and across the Atypical Diderm Cell Envelope of Mycobacteria
van Winden, V. J. C., Houben, E. N. G., & Braunstein, M. (2019) · ASM Press eBooks · doi:10.1128/9781683670131.ch68 · Cited by 5
Self-citationChekesa, B., Singh, H., González-Juarbe, N., Vashee, S., Wiscovitch-Russo, R. A., Dupont, C. L., Girma, M., Dego, O. K., Gumi, B., & Ameni, G. (2024) · PLoS ONE · doi:10.1371/journal.pone.0304060 · Cited by 4
PE/PPE proteins contribute to Mycobacterium tuberculosis drug resistance
Boradia, V. M., Chen, J., Frando, A., Clark, L. V., & Grundner, C. (2026) · Nature Communications · doi:10.1038/s41467-026-72431-7 · Cited by 4
Marine sponge microbe provides insights into evolution and virulence of the tubercle bacillus
Pidot, S. J., Klatt, S., Ates, L. S., Frigui, W., Sayes, F., Majlessi, L., Izumi, H., Monk, I. R., Porter, J. L., Bennett-Wood, V. R., et al. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012440 · Cited by 4
Self-citationPPE51 modulates membrane integrity in Mycobacterium marinum
Charitou, V., Lafuente, B. I., Habjan, E., Kuijl, C. P., Willemse, J. J., Bitter, W., & Speer, A. (2025) · mBio · doi:10.1128/mbio.01044-25 · Cited by 3
Self-citationDinshaw, K. M., Lien, K. A., Knight, M., Ouonkap, S. V. Y., Liu, H., Savage, D. F., Carlson, H. K., Deutschbauer, A. M., & Stanley, S. A. (2026) · PLoS Biology · doi:10.1371/journal.pbio.3003529 · Cited by 3
Mapping the phylogeny and lineage history of geographically distinct BCG vaccine strains
Elton, L., Kasaragod, S., Donoghue, H. D., Safar, H. A., Amankwah, P. S., Zumla, A. I., Witney, A. A., & McHugh, T. D. (2023) · Microbial Genomics · doi:10.1099/mgen.0.001077 · Cited by 4
Koleske, B. N., Shen, J., Gupta, M., & Bishai, W. R. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1634229 · Cited by 3
Kurniawati, S., Soedarsono, S., Aulanni’am, A., & Mertaniasih, N. M. (2018) · African Journal of Infectious Diseases · doi:10.21010/ajid.v12i2.6 · Cited by 3
Expression and production of soluble Mycobacterium tuberculosis H37Rv mycosin-3
Fang, Z., Schubert, W., & van Pittius, N. C. G. (2016) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2016.02.005 · Cited by 3
Yang, J.-J., Hu, Y., Sun, P.-Y., Wang, L., Xie, X.-J., & Wang, T. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1573643 · Cited by 2
The chamber of secretome in Mycobacterium tuberculosis as a potential therapeutic target
Dwivedi, M., & Bajpai, K. (2022) · Biotechnology and Genetic Engineering Reviews · doi:10.1080/02648725.2022.2076031 · Cited by 2
Sundaram, K., Rathinam, S., Bethunaickan, R., Ranganathan, U. D., Prabhu, V., & Dhanapal, M. (2026) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2026.1797994 · Cited by 2
Tyloxapol inhibits ESX-1 secretion in Mycobacterium marinum
Collars, O. A., Weaver, S. D., Hernandez, R. L., Champion, M. M., & Champion, P. A. D. (2026) · Journal of Bacteriology · doi:10.1128/jb.00136-26 · Cited by 1
Manikoth, A. G., Bisht, M. K., Ghosh, S. K., & Mukhopadhyay, S. (2025) · FEBS Journal · doi:10.1111/febs.70084 · Cited by 1
Advances and Perspectives on Mycobacterial Secretion Systems
Segafreddo, G., Sorze, D., Manganelli, R., & Provvedi, R. (2025) · eMicrobe · doi:10.53941/emicrobe.2026.100003 · Cited by 1
Smith, V., Chandrasekharan, G., Farzand, R., Watkins, K. E., Maset, R. G., Yap, J., Perrier, S., Tchoupa, A. K., & Unnikrishnan, M. (2026) · Journal of Bacteriology · doi:10.1128/jb.00380-25 · Cited by 1
Zhang, Q., Abudukadier, A., Chen, H., Xiong, L., Li, P., Gong, Z., & Xie, J. (2026) · Microbiology Spectrum · doi:10.1128/spectrum.02488-25 · Cited by 2
Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis
Sanyal, P., Jagadeeshwari, U., Sinha, S., Bhat, Y., Khan, S., Rajaram, S. V., Arokiyaraj, E. A., Jhingan, G. D., Agarwal, N., Samal, A., et al. (2026) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2026.101555 · Cited by 1
Blackman, A., Morrison, B., Maruri, F., van der Heijden, Y. F., Nochowicz, C. H., Guo, Y. P., Scholz, M. B., Rustad, T. R., Sherman, D. R., & Sterling, T. R. (2020) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkaa507 · Cited by 1
Farnia, P., Ghanavi, J., Aghajani, J., Ayoubi, S., Besharati, S., Farnia, P., & Velayati, A. A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21712-8.00018-1 · Cited by 1
Staff, T. P. G. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005270 · Cited by 1
Tateishi, Y., Ozeki, Y., Nishiyama, A., Morishige, Y., Minato, Y., Baughn, A. D., & Matsumoto, S. (2024) · eLife · doi:10.7554/elife.99426 · Cited by 1
Trinidad, D., Macdonald, C. B., Rosenberg, O. S., Fraser, J. S., & Coyote‐Maestas, W. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.23.609456 · Cited by 1
Tateishi, Y., Ozeki, Y., Nishiyama, A., Morishige, Y., Minato, Y., Baughn, A. D., & Matsumoto, S. (2025) · eLife · doi:10.7554/elife.99426.2 · Cited by 1
Tateishi, Y., Ozeki, Y., Nishiyama, A., Morishige, Y., Minato, Y., Baughn, A. D., & Matsumoto, S. (2025) · eLife · doi:10.7554/elife.99426.3 · Cited by 1
Structure, proteolysis, and evolution of secreted tuberculosis virulence factors
Solomonson, M. (2015) · cIRcle (University of British Columbia) · doi:10.14288/1.0166602
Berger, C. (2022) · Research Publications (Maastricht University) · doi:10.26481/dis.20221101cb
Tateishi, Y., Ozeki, Y., Nishiyama, A., Morishige, Y., Minato, Y., Baughn, A. D., & Matsumoto, S. (2025) · eLife · doi:10.7554/elife.99426.5
Tateishi, Y., Ozeki, Y., Nishiyama, A., et al. (2024) · eLife · doi:10.7554/elife.99426.1.sa0
Tateishi, Y., Ozeki, Y., Nishiyama, A., et al. (2024) · eLife · doi:10.7554/elife.99426.1.sa2
Functional genomics reveals the mechanism of hypoxic adaptation in nontuberculous mycobacteriaPreprint
Tateishi, Y., Ozeki, Y., Nishiyama, A., Morishige, Y., Minato, Y., Baughn, A. D., & Matsumoto, S. (2024) · eLife · doi:10.7554/elife.99426.1
Tateishi, Y., Ozeki, Y., Nishiyama, A., et al. (2024) · eLife · doi:10.7554/elife.99426.1.sa1
ESX-5 component EccB5 targets GSDMD to drive pyroptosis and promote Mtb dissemination
Shen, Y., He, Y., Liu, X., Chen, A., Geng, L., Liu, X., Gao, Y., Qiu, Y., Zhang, L., Hu, Z., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01895-3
Control of antigen presentation on MHC-I by a bacterial secretion systemPreprint
Leddy, O. K., McGinn, R. A., Allsup, B. L., Leone, M., Timms, P., Gutiérrez-González, M., Fahad, A. S., Milligan, R., García-Beltrán, W. F., DeKosky, B. J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.19.689332 · Cited by 1
Tateishi, Y., Ozeki, Y., Nishiyama, A., Morishige, Y., Minato, Y., Baughn, A. D., & Matsumoto, S. (2025) · eLife · doi:10.7554/elife.99426.4
La Canettose, une maladie infectieuse émergente dans la corne de l'Afrique
Bouzid, F. (2017) · theses.fr (ABES) · doi:10.70675/f51663f2zcc22z4b18z9580z5bf6e0d77024
Functional and structural studies on Type VII Secretion System
Tassinari, M. (2019) · theses.fr (ABES) · doi:10.70675/573aef93zdda2z4ac3za4cczdadb94f07379
Implication des enzymes lipolytiques dans la virulence et la survie mycobactérienne
Santucci, P. (2018) · theses.fr (ABES) · doi:10.70675/b1318398z3b3ez47caza99cz49045a043924
Prophylactic and post-exposure efficacy of a Pichinde virus vector-based tuberculosis vaccine
Cain, M., Block, A. M., Huang, Q., Kirk, N. M., Murphy, H. L., Harris, M. C., Ly, H., Tischler, A. D., & Liang, Y. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1861052
Meijers, A. S., Gallant, J., Speer, A., Maaskant, J. J., Hietamäki, S., Ummels, R., Paulussen, F. M., Grossmann, T. N., Pham, T. V., Piersma, S. R., et al. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113450
Self-citationDey, S., Maurya, V., Pathak, N., & Mukhopadhyay, S. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-27735-1.00009-5
Hart, E. M., de Bruin, D. A., Marando, V. M., Alemany, M. A., Snow, E. D., Schultz, B. J., Kuru, E., Walker, S., Vettiger, A., & Bernhardt, T. G. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2529250123
Kibiloski, A. P., Dechow, S. J., Abdalla, B. J., Murdoch, H. M., Tischler, A. D., & Abramovitch, R. B. (2026) · PLoS Genetics · doi:10.1371/journal.pgen.1012331
Bacterial Surfaces and Barriers: Biogenesis and Pathogen–Host Interactions
Bartholomew-Schoch, J., Finnie, J. K., Gahlmann, A., & Columbus, L. M. (2026) · Chemical Reviews · doi:10.1021/acs.chemrev.5c01068
Metadata
- Authors
- Ates, L. S., Ummels, R., Commandeur, S., van der Weerd, R., Sparrius, M., Weerdenburg, E., Alber, M., Kalscheuer, R., Piersma, S. R., Abdallah, A. M., Abd El Ghany, M., Abdel-Haleem, A. M., Pain, A., Jiménez, C. R., Bitter, W., & Houben, E. N. G.
- Affiliations
- Amsterdam UMC Location Vrije Universiteit Amsterdam (NL)
- Heinrich Heine University Düsseldorf (DE)
- King Abdullah University of Science and Technology (SA)
- Vrije Universiteit Amsterdam (NL)
- Corresponding author
- Houben, Edith N.G.
- ORCID
- Venue
- PLOS Genetics
- Publisher
- Public Library of Science (PLoS)
- Published
- 2015-05-04
- Volume
- 11
- Issue
- 5
- Pages
- e1005190
- ISSN
- 1553-7390 (ISSN-L)
- 1553-7404
- PMC
- PMC4418733
- OpenAlex
- W1508212288
- Cited by
- 185
- References
- 80
- Citations by year
- 2026: 14 · 2025: 19 · 2024: 15 · 2023: 10 · 2022: 21 · 2021: 18 · 2020: 18 · 2019: 18 · 2018: 15 · 2017: 11 · 2016: 19 · 2015: 7
- FWCI
- 13.47
- Type
- journal article
- Language
- en
- Update notices
- correction (2015-05-29)
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS Genetics (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Amsterdam UMC (VU Amsterdam) - Institutional Repository (publishedVersion)
- VU Research Portal (publishedVersion, other-oa)
- Pure Amsterdam UMC (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- King Abdullah University of Science and Technology Repository (King Abdullah University of Science and Technology) (submittedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- Jürgen Manchot Stiftung
- European Federation of Pharmaceutical Industries and Associations (FP7/20072013)
- European Commission (115337, 2007–2013, FP7 2007-2013, FP7/2007)
- Innovative Medicines Initiative (FP7/2007‐2013, 115337)
- 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
- type VII secretion system, Mycobacterium marinum, Mycobacterium bovis, outer membrane permeability, slow-growing mycobacteria, transposon insertion site sequencing
- MeSH terms
- Type VII Secretion Systems, Ampicillin, Bacterial Proteins, Cell Membrane Permeability, Chromatography, Liquid, DNA Transposable Elements, DNA, Bacterial, Mutation, Mycobacterium bovis, Mycobacterium tuberculosis, Gene Expression Regulation, Bacterial, Sequence Analysis, DNA, Mycobacterium marinum, Drug Resistance, Bacterial, Tandem Mass Spectrometry
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