{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T01:02:18Z","timestamp":1781830938423,"version":"3.54.5"},"reference-count":122,"publisher":"Pleiades Publishing Ltd","issue":"S1","license":[{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2025,2,1]],"date-time":"2025-02-01T00:00:00Z","timestamp":1738368000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Biochemistry Moscow"],"published-print":{"date-parts":[[2025,2]]},"DOI":"10.1134\/s0006297924603757","type":"journal-article","created":{"date-parts":[[2025,3,27]],"date-time":"2025-03-27T15:42:37Z","timestamp":1743090157000},"page":"S193-S213","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Biochemistry of Reactivation of Dormant Mycobacteria"],"prefix":"10.1134","volume":"90","author":[{"given":"Margarita O.","family":"Shleeva","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Galina R.","family":"Demina","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arseny S.","family":"Kaprelyants","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"137","published-online":{"date-parts":[[2025,3,27]]},"reference":[{"key":"2814_CR1","doi-asserted-by":"publisher","first-page":"1627","DOI":"10.2174\/1389557519666190625165512","volume":"19","author":"G. Gutti","year":"2019","unstructured":"Gutti, G., Arya, K., and Singh, S. K. (2019) Latent tuberculosis infection (LTBI) and its potential targets: an investigation into dormant phase pathogens, Mini Rev. Med. Chem., 19, 1627-1642, \nhttps:\/\/doi.org\/10.2174\/1389557519666190625165512.","journal-title":"Mini Rev. Med. Chem."},{"key":"2814_CR2","doi-asserted-by":"publisher","first-page":"401","DOI":"10.1086\/338342","volume":"185","author":"T. Lillebaek","year":"2002","unstructured":"Lillebaek, T., Dirksen, A., Baess, I., Strunge, B., Thomsen, V. \u00d8., and Andersen, A.\u00a0B. (2002) Molecular evidence of endogenous reactivation of Mycobacterium tuberculosis after 33 years of latent infection, J.\u00a0Infect. Dis., 185, 401-404, \nhttps:\/\/doi.org\/10.1086\/338342.","journal-title":"J.\u00a0Infect. Dis."},{"key":"2814_CR3","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1007\/s15010-009-8450-7","volume":"37","author":"S. Ehlers","year":"2009","unstructured":"Ehlers, S. (2009) Lazy, dynamic or minimally recrudescent? On the elusive nature and location of the Mycobacterium responsible for latent tuberculosis, Infection, 37, 87-95, \nhttps:\/\/doi.org\/10.1007\/s15010-009-8450-7.","journal-title":"Infection"},{"key":"2814_CR4","doi-asserted-by":"publisher","DOI":"10.1016\/j.cegh.2022.101031","volume":"15","author":"K. Patra","year":"2022","unstructured":"Patra, K., Batabyal, S., Mandal, K., Ghose, D., and Sarkar, J. (2022) Tuberculosis and COVID-19: a combined global threat to human civilization, Clin. Epidemiol. Global Health, 15, 101031, \nhttps:\/\/doi.org\/10.1016\/j.cegh.2022.101031.","journal-title":"Clin. Epidemiol. Global Health"},{"key":"2814_CR5","doi-asserted-by":"publisher","first-page":"S52","DOI":"10.1134\/S0006297923140043","volume":"88","author":"M. O. Shleeva","year":"2023","unstructured":"Shleeva, M. O., and Kaprelyants, A. S. (2023) Hypobiosis of mycobacteria: biochemical aspects, Biochemistry (Moscow), 88, S52-S74, \nhttps:\/\/doi.org\/10.1134\/S0006297923140043.","journal-title":"Biochemistry (Moscow)"},{"key":"2814_CR6","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1016\/S0065-2911(03)47002-1","volume":"47","author":"G. V. Mukamolova","year":"2003","unstructured":"Mukamolova, G. V., Kaprelyants, A. S., Kell, D. B., and Young, M. (2003) Adoption of the transiently non-culturable state\u00a0\u2013 a bacterial survival strategy? Adv. Microb. Physiol., 47, 65-129, \nhttps:\/\/doi.org\/10.1016\/S0065-2911(03)47002-1.","journal-title":"Adv. Microb. Physiol."},{"key":"2814_CR7","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1007\/s002030100314","volume":"176","author":"T. Nystr\u00f6m","year":"2001","unstructured":"Nystr\u00f6m, T. (2001) Not quite dead enough: on bacterial life, culturability, senescence, and death, Arch. Microbiol., 176, 159-164, \nhttps:\/\/doi.org\/10.1007\/s002030100314.","journal-title":"Arch. Microbiol."},{"key":"2814_CR8","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1099\/00221287-70-1-115","volume":"70","author":"P. H. Calcott","year":"1972","unstructured":"Calcott, P. H., Postgate, J. R. (1972) On substrate-accelerated death in Klebsiella aerogenes, J.\u00a0Gen. Microbiol., 70, 115-122, \nhttps:\/\/doi.org\/10.1099\/00221287-70-1-115.","journal-title":"J.\u00a0Gen. Microbiol."},{"key":"2814_CR9","doi-asserted-by":"publisher","first-page":"8916","DOI":"10.1073\/pnas.95.15.8916","volume":"95","author":"G. V. Mukamolova","year":"1998","unstructured":"Mukamolova, G. V., Kaprelyants, A. S., Young, D.\u00a0I., Young, M., and Kell, D.\u00a0B. (1998) A bacterial cytokine, Proc. Natl. Acad. Sci. USA, 95, 8916-8921, \nhttps:\/\/doi.org\/10.1073\/pnas.95.15.8916.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2814_CR10","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1111\/j.1574-695X.2000.tb01528.x","volume":"29","author":"S. F. Biketov","year":"2000","unstructured":"Biketov, S. F., Mukamolova, G.\u00a0V., Potapov, V., Gilenkov, E., Vostroknutova, G. V., Kell, D.\u00a0B., Young, M., and Kaprelyants, A.\u00a0S. (2000) Culturability of Mycobacterium tuberculosis cells isolated from murine macrophages: a bacterial growth factor promotes recovery, FEMS Immunol. Med. Microbiol., 29, 233-240, \nhttps:\/\/doi.org\/10.1111\/j.1574-695X.2000.tb01528.x.","journal-title":"FEMS Immunol. Med. Microbiol."},{"key":"2814_CR11","doi-asserted-by":"publisher","first-page":"1581","DOI":"10.1099\/00221287-148-5-1581","volume":"148","author":"M. O. Shleeva","year":"2002","unstructured":"Shleeva, M. O., Bagramyan, K., Telkov, M. V., Mukamolova, G. V., Young, M., Kell, D.\u00a0B., and Kaprelyants, A.\u00a0S. (2002) Formation and resuscitation of \u201cnon-culturable\u201d cells of Rhodococcus rhodochrous and Mycobacterium tuberculosis in prolonged stationary phase, Microbiology, 148, 1581-1591, \nhttps:\/\/doi.org\/10.1099\/00221287-148-5-1581.","journal-title":"Microbiology"},{"key":"2814_CR12","doi-asserted-by":"publisher","first-page":"169","DOI":"10.1023\/A:1000664013047","volume":"73","author":"D. B. Kell","year":"1998","unstructured":"Kell, D. B., Kaprelyants, A. S., Weichart, D. H., Harwood, C.\u00a0R., and Barer, M.\u00a0R. (1998) Viability and activity in readily culturable bacteria: a review and discussion of the practical issues, Antonie Van Leeuwenhoek, 73, 169-187, \nhttps:\/\/doi.org\/10.1023\/A:1000664013047.","journal-title":"Antonie Van Leeuwenhoek"},{"key":"2814_CR13","doi-asserted-by":"publisher","first-page":"542","DOI":"10.1006\/bbrc.2001.4993","volume":"284","author":"Y. Zhang","year":"2001","unstructured":"Zhang, Y., Yang, Y., Woods, A., Cotter, R.\u00a0J., and Sun, Z. (2001) Resuscitation of dormant Mycobacterium tuberculosis by phospholipids or specific peptides, Biochem. Biophys. Res. Commun., 284, 542-547, \nhttps:\/\/doi.org\/10.1006\/bbrc.2001.4993.","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2814_CR14","doi-asserted-by":"publisher","first-page":"3187","DOI":"10.1128\/aem.59.10.3187-3196.1993","volume":"59","author":"A. Kaprelyants","year":"1993","unstructured":"Kaprelyants, A., and Kell, D. (1993) Dormancy in stationary-phase cultures of Micrococcus luteus: flow cytometric analysis of starvation and resuscitation, Appl. Environ. Microbiol., 59, 3187-3196, \nhttps:\/\/doi.org\/10.1128\/aem.59.10.3187-3196.1993.","journal-title":"Appl. Environ. Microbiol."},{"key":"2814_CR15","doi-asserted-by":"publisher","first-page":"623","DOI":"10.1046\/j.1365-2958.2002.03184.x","volume":"46","author":"G. V. Mukamolova","year":"2002","unstructured":"Mukamolova, G. V., Turapov, O. A., Young, D. I., Kaprelyants, A.\u00a0S., Kell, D.\u00a0B., and Young, M. (2002) A family of autocrine growth factors in Mycobacterium tuberculosis, Mol. Microbiol., 46, 623-635, \nhttps:\/\/doi.org\/10.1046\/j.1365-2958.2002.03184.x.","journal-title":"Mol. Microbiol."},{"key":"2814_CR16","doi-asserted-by":"publisher","DOI":"10.1128\/jb.00337-22","volume":"205","author":"I. L. Sparks","year":"2023","unstructured":"Sparks, I. L., Derbyshire, K. M., Jacobs, W. R., Jr., and Morita, Y.\u00a0S. (2023) Mycobacterium smegmatis: the vanguard of mycobacterial research, J.\u00a0Bacteriol., 205, e0033722, \nhttps:\/\/doi.org\/10.1128\/jb.00337-22.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR17","doi-asserted-by":"publisher","first-page":"672","DOI":"10.1111\/j.1365-2958.2007.06078.x","volume":"67","author":"B. D. Kana","year":"2008","unstructured":"Kana, B. D., Gordhan, B. G., Downing, K. J., Sung, N., Vostroktunova, G., Machowski, E.\u00a0E., Tsenova, L., Young, M., Kaprelyants, A., Kaplan, G., and Mizrahi, V. (2008) The resuscitation-promoting factors of Mycobacterium tuberculosis are required for virulence and resuscitation from dormancy but are collectively dispensable for growth in\u00a0vitro, Mol. Microbiol., 67, 672-684, \nhttps:\/\/doi.org\/10.1111\/j.1365-2958.2007.06078.x.","journal-title":"Mol. Microbiol."},{"key":"2814_CR18","doi-asserted-by":"publisher","first-page":"1121","DOI":"10.1111\/j.1365-2672.2008.03850.x","volume":"105","author":"X. Wu","year":"2008","unstructured":"Wu, X., Yang, Y., Han, Y., Zhang, J., Liang, Y., Li, H., Li, B., and Wang, L. (2008) Effect of recombinant Rv1009 protein on promoting the growth of Mycobacterium tuberculosis, J.\u00a0Appl. Microbiol., 105, 1121-1127, \nhttps:\/\/doi.org\/10.1111\/j.1365-2672.2008.03850.x.","journal-title":"J.\u00a0Appl. Microbiol."},{"key":"2814_CR19","doi-asserted-by":"publisher","first-page":"174","DOI":"10.1164\/rccm.200905-0661OC","volume":"181","author":"G. V. Mukamolova","year":"2010","unstructured":"Mukamolova, G. V., Turapov, O., Malkin, J., Woltmann, G., and Barer, M.\u00a0R. (2010) Resuscitation-promoting factors reveal an occult population of tubercle bacilli in sputum, Am.\u00a0J. Respir. Crit. Care Med., 181, 174-180, \nhttps:\/\/doi.org\/10.1164\/rccm.200905-0661OC.","journal-title":"Am.\u00a0J. Respir. Crit. Care Med."},{"key":"2814_CR20","doi-asserted-by":"publisher","first-page":"2985","DOI":"10.1128\/IAI.74.5.2985-2995.2006","volume":"74","author":"J. M. Tufariello","year":"2006","unstructured":"Tufariello, J. M., Mi, K., Xu, J., Manabe, Y. C., Kesavan, A. K., Drumm, J., Tanaka, K., Jacobs, W. R., Jr., and Chan, J. (2006) Deletion of the Mycobacterium tuberculosis resuscitation-promoting factor Rv1009 gene results in delayed reactivation from chronic tuberculosis, Infect. Immun., 74, 2985-2995, \nhttps:\/\/doi.org\/10.1128\/IAI.74.5.2985-2995.2006.","journal-title":"Infect. Immun."},{"key":"2814_CR21","doi-asserted-by":"publisher","first-page":"4269","DOI":"10.1128\/IAI.01735-07","volume":"76","author":"E. Russell-Goldman","year":"2008","unstructured":"Russell-Goldman, E., Xu, J., Wang, X., Chan, J., and Tufariello, J.\u00a0M. (2008) A Mycobacterium tuberculosis Rpf double-knockout strain exhibits profound defects in reactivation from chronic tuberculosis and innate immunity phenotypes, Infect. Immun., 76, 4269-4281, \nhttps:\/\/doi.org\/10.1128\/IAI.01735-07.","journal-title":"Infect. Immun."},{"key":"2814_CR22","doi-asserted-by":"publisher","first-page":"565","DOI":"10.1007\/s12275-016-6150-4","volume":"54","author":"E. Iona","year":"2016","unstructured":"Iona, E., Pardini, M., Mustazzolu, A., Piccaro, G., Nisini, R., Fattorini, L., and Giannoni, F. (2016) Mycobacterium tuberculosis gene expression at different stages of hypoxia-induced dormancy and upon resuscitation, J.\u00a0Microbiol., 54, 565-572, \nhttps:\/\/doi.org\/10.1007\/s12275-016-6150-4.","journal-title":"J.\u00a0Microbiol."},{"key":"2814_CR23","doi-asserted-by":"publisher","DOI":"10.1098\/rsob.140106","volume":"4","author":"E. G. Salina","year":"2014","unstructured":"Salina, E. G., Waddell, S. J., Hoffmann, N., Rosenkrands, I., Butcher, P. D., and Kaprelyants, A.\u00a0S. (2014) Potassium availability triggers Mycobacterium tuberculosis transition to, and resuscitation from, non-culturable (dormant) states, Open Biol., 4, 140106, \nhttps:\/\/doi.org\/10.1098\/rsob.140106.","journal-title":"Open Biol."},{"key":"2814_CR24","doi-asserted-by":"publisher","first-page":"270","DOI":"10.1038\/nsmb905","volume":"12","author":"M. Cohen-Gonsaud","year":"2005","unstructured":"Cohen-Gonsaud, M., Barthe, P., Bagn\u00e9ris, C., Henderson, B., Ward, J., Roumestand, C., and Keep, N.\u00a0H. (2005) The structure of a resuscitation-promoting factor domain from Mycobacterium tuberculosis shows homology to lysozymes, Nat. Struct. Mol. Biol., 12, 270-273, \nhttps:\/\/doi.org\/10.1038\/nsmb905.","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2814_CR25","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1016\/j.jmb.2008.10.042","volume":"385","author":"A. Ruggiero","year":"2009","unstructured":"Ruggiero, A., Tizzano, B., Pedone, E., Pedone, C., Wilmanns, M., and Berisio, R. (2009) Crystal structure of the resuscitation promoting factor (DeltaDUF)RpfB from M.\u00a0tuberculosis, Mol. Biol., 385, 153-162, \nhttps:\/\/doi.org\/10.1016\/j.jmb.2008.10.042.","journal-title":"Mol. Biol."},{"key":"2814_CR26","doi-asserted-by":"publisher","first-page":"84","DOI":"10.1111\/j.1365-2958.2005.04930.x","volume":"59","author":"G. V. Mukamolova","year":"2006","unstructured":"Mukamolova, G. V., Murzin, A. G., Salina, E. G., Demina, G. R., Kell, D.\u00a0B., Kaprelyants, A.\u00a0S., and Young, M. (2006) Muralytic activity of Micrococcus luteus Rpf and its relationship to physiological activity in promoting bacterial growth and resuscitation, Mol. Microbiol., 59, 84-98, \nhttps:\/\/doi.org\/10.1111\/j.1365-2958.2005.04930.x.","journal-title":"Mol. Microbiol."},{"key":"2814_CR27","doi-asserted-by":"publisher","first-page":"5569","DOI":"10.1128\/JB.00408-09","volume":"191","author":"J. D. Giebel","year":"2009","unstructured":"Giebel, J. D., Carr, K. A., Anderson, E. C., and Hanna, P.\u00a0C. (2009) The germination-specific lytic enzymes SleB, CwlJ1, and CwlJ2 each contribute to Bacillus anthracis spore germination and virulence, J.\u00a0Bacteriol., 191, 5569-5576, \nhttps:\/\/doi.org\/10.1128\/JB.00408-09.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR28","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1128\/JB.01380-09","volume":"192","author":"J. D. Heffron","year":"2010","unstructured":"Heffron, J. D., Lambert, E. A., Sherry, N., and Popham, D.\u00a0L. (2010) Contributions of four cortex lytic enzymes to germination of Bacillus anthracis spores, J.\u00a0Bacteriol., 192, 763-770, \nhttps:\/\/doi.org\/10.1128\/JB.01380-09.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR29","doi-asserted-by":"publisher","first-page":"6501","DOI":"10.1128\/JB.00767-09","volume":"191","author":"H. J. Haiser","year":"2009","unstructured":"Haiser, H. J., Yousef, M. R., and Elliot, M. A. (2009) Cell wall hydrolases affect germination, vegetative growth, and sporulation in Streptomyces coelicolor, J.\u00a0Bacteriol., 191, 6501-6512, \nhttps:\/\/doi.org\/10.1128\/JB.00767-09.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR30","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1134\/S0026261711020123","volume":"80","author":"V. D. Nikitushkin","year":"2011","unstructured":"Nikitushkin, V. D., Demina, G. R., and Kaprelyants, A.\u00a0S. (2011) Effect of secreted Rpf protein on intercellular contacts in Micrococcus luteus and Mycobacterium smegmatis cultures, Microbiology, 80, 155-161, \nhttps:\/\/doi.org\/10.1134\/S0026261711020123.","journal-title":"Microbiology"},{"key":"2814_CR31","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1007\/s10482-012-9784-1","volume":"103","author":"V. D. Nikitushkin","year":"2013","unstructured":"Nikitushkin, V. D., Demina, G. R., Shleeva, M. O., and Kaprelyants, A. S. (2013) Peptidoglycan fragments stimulate resuscitation of \u201cnon-culturable\u201d mycobacteria, Antonie Van Leeuwenhoek, 103, 37-46, \nhttps:\/\/doi.org\/10.1007\/s10482-012-9784-1.","journal-title":"Antonie Van Leeuwenhoek"},{"key":"2814_CR32","doi-asserted-by":"publisher","first-page":"1687","DOI":"10.1099\/mic.0.26893-0","volume":"150","author":"M. O. Shleeva","year":"2004","unstructured":"Shleeva, M. O., Mukamolova, G. V., Young, M., Williams, H.\u00a0D., and Kaprelyants, A. S. (2004) Formation of \u201cnon-culturable\u201d cells of Mycobacterium smegmatis in stationary phase in response to growth under suboptimal conditions and their Rpf-mediated resuscitation, Microbiology, 150, 1687-1697, \nhttps:\/\/doi.org\/10.1099\/mic.0.26893-0.","journal-title":"Microbiology"},{"key":"2814_CR33","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1016\/j.tim.2006.04.003","volume":"14","author":"N. H. Keep","year":"2006","unstructured":"Keep, N. H., Ward, J. M., Cohen-Gonsaud, M., and Henderson, B. (2006) Wake up! Peptidoglycan lysis and bacterial non-growth states, Trends Microbiol., 14, 271-276, \nhttps:\/\/doi.org\/10.1016\/j.tim.2006.04.003.","journal-title":"Trends Microbiol."},{"key":"2814_CR34","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1016\/j.cell.2008.08.039","volume":"135","author":"I. M. Shah","year":"2008","unstructured":"Shah, I. M., Laaberki, M. H., Popham, D. L., and Dworkin, J. (2008) A eukaryotic-like Ser\/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments, Cell, 135, 486-496, \nhttps:\/\/doi.org\/10.1016\/j.cell.2008.08.039.","journal-title":"Cell"},{"key":"2814_CR35","doi-asserted-by":"publisher","first-page":"890","DOI":"10.1038\/nrmicro2453","volume":"8","author":"J. Dworkin","year":"2010","unstructured":"Dworkin, J., and Shah, I. M. (2010) Exit from dormancy in microbial organisms, Nat. Rev. Microbiol., 8, 890-896, \nhttps:\/\/doi.org\/10.1038\/nrmicro2453.","journal-title":"Nat. Rev. Microbiol."},{"key":"2814_CR36","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1111\/j.1574-695X.2009.00606.x","volume":"58","author":"B. D. Kana","year":"2010","unstructured":"Kana, B. D., and Mizrahi, V. (2010) Resuscitation-promoting factors as lytic enzymes for bacterial growth and signaling, FEMS Immunol. Med. Microbiol., 58, 39-50, \nhttps:\/\/doi.org\/10.1111\/j.1574-695X.2009.00606.x.","journal-title":"FEMS Immunol. Med. Microbiol."},{"key":"2814_CR37","doi-asserted-by":"publisher","first-page":"1064","DOI":"10.1111\/j.1365-2958.2009.07041.x","volume":"75","author":"V. Molle","year":"2010","unstructured":"Molle, V., and Kremer, L. (2010) Division and cell envelope regulation by Ser\/Thr phosphorylation: Mycobacterium shows the way, Mol. Microbiol., 75, 1064-1077, \nhttps:\/\/doi.org\/10.1111\/j.1365-2958.2009.07041.x.","journal-title":"Mol. Microbiol."},{"key":"2814_CR38","doi-asserted-by":"publisher","first-page":"7470","DOI":"10.1128\/JB.00800-06","volume":"188","author":"G. Jones","year":"2006","unstructured":"Jones, G., and Dyson, P. (2006) Evolution of transmembrane protein kinases implicated in coordinating remodeling of gram-positive peptidoglycan: inside versus outside, J.\u00a0Bacteriol., 188, 7470-7476, \nhttps:\/\/doi.org\/10.1128\/JB.00800-06.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR39","doi-asserted-by":"publisher","first-page":"725","DOI":"10.1099\/mic.0.2007\/014076-0","volume":"154","author":"C. M. Kang","year":"2008","unstructured":"Kang, C. M., Nyayapathy, S., Lee, J. Y., Suh, J. W., and Husson, R.\u00a0N. (2008) Wag31, a homologue of the cell division protein DivIVA, regulates growth, morphology and polar cell wall synthesis in mycobacteria, Microbiology, 154, 725-735, \nhttps:\/\/doi.org\/10.1099\/mic.0.2007\/014076-0.","journal-title":"Microbiology"},{"key":"2814_CR40","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1002182","volume":"7","author":"M. Mir","year":"2011","unstructured":"Mir, M., Asong, J., Li, X., Cardot, J., Boons, G.\u00a0J., and Husson, R.\u00a0N. (2011) The extracytoplasmic domain of the Mycobacterium tuberculosis Ser\/Thr kinase PknB binds specific muropeptides and is required for PknB localization, PLoS Pathog., 7, e1002182, \nhttps:\/\/doi.org\/10.1371\/journal.ppat.1002182.","journal-title":"PLoS Pathog."},{"key":"2814_CR41","doi-asserted-by":"publisher","first-page":"2525","DOI":"10.1002\/cbic.201000626","volume":"11","author":"M. Lee","year":"2010","unstructured":"Lee, M., Hesek, D., Shah, I. M., Oliver, A. G., Dworkin, J., and Mobashery, S. (2010) Synthetic peptidoglycan motifs for germination of bacterial spores, Eur.\u00a0J. Chem. Biol., 11, 2525-2529, \nhttps:\/\/doi.org\/10.1002\/cbic.201000626.","journal-title":"Eur.\u00a0J. Chem. Biol."},{"key":"2814_CR42","doi-asserted-by":"publisher","first-page":"2295","DOI":"10.1107\/S1399004714013674","volume":"70","author":"F. Squeglia","year":"2014","unstructured":"Squeglia, F., Ruggiero, A., Romano, M., Vitagliano, L., and Berisio, R. (2014) Mutational and structural study of RipA, a key enzyme in Mycobacterium tuberculosis cell division: evidence for the L-to-D inversion of configuration of the catalytic cysteine, Acta Crystallogr. Sect.\u00a0D Biol. Crystallogr., 70, 2295-2300, \nhttps:\/\/doi.org\/10.1107\/S1399004714013674.","journal-title":"Acta Crystallogr. Sect.\u00a0D Biol. Crystallogr."},{"key":"2814_CR43","doi-asserted-by":"publisher","first-page":"70","DOI":"10.2174\/092986610789909557","volume":"17","author":"A. Ruggiero","year":"2010","unstructured":"Ruggiero, A., Squeglia, F., Pirone, L., Correale, S., and Berisio, R. (2010) Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the resuscitation promoting factor interacting protein RipA from M.\u00a0tuberculosis, Acta Crystallogr. Sect.\u00a0F Struct. Biol. Crystall. Commun., 17, 70-73, \nhttps:\/\/doi.org\/10.2174\/092986610789909557.","journal-title":"Acta Crystallogr. Sect.\u00a0F Struct. Biol. Crystall. Commun."},{"key":"2814_CR44","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1000001","volume":"4","author":"E. C. Hett","year":"2008","unstructured":"Hett, E. C., Chao, M. C., Deng, L. L., and Rubin, E.\u00a0J. (2008) A mycobacterial enzyme essential for cell division synergizes with resuscitation-promoting factor, PLoS Pathog., 4, e1000001, \nhttps:\/\/doi.org\/10.1371\/journal.ppat.1000001.","journal-title":"PLoS Pathog."},{"key":"2814_CR45","doi-asserted-by":"publisher","first-page":"658","DOI":"10.1111\/j.1365-2958.2007.05945.x","volume":"66","author":"E. C. Hett","year":"2007","unstructured":"Hett, E. C., Chao, M. C., Steyn, A. J., Fortune, S. M., Deng, L.\u00a0L., and Rubin, E. J. (2007) A partner for the resuscitation-promoting factors of Mycobacterium tuberculosis, Mol. Microbiol., 66, 658-668, \nhttps:\/\/doi.org\/10.1111\/j.1365-2958.2007.05945.x.","journal-title":"Mol. Microbiol."},{"key":"2814_CR46","doi-asserted-by":"publisher","first-page":"2500","DOI":"10.1111\/febs.13292","volume":"282","author":"V. D. Nikitushkin","year":"2015","unstructured":"Nikitushkin, V. D., Demina, G. R., Shleeva, M. O., Guryanova, S.\u00a0V., Ruggiero, A., Berisio, R., and Kaprelyants, A. S. (2015) A product of RpfB and RipA joint enzymatic action promotes the resuscitation of dormant mycobacteria, FEBS\u00a0J., 282, 2500-2511, \nhttps:\/\/doi.org\/10.1111\/febs.13292.","journal-title":"FEBS\u00a0J."},{"key":"2814_CR47","doi-asserted-by":"publisher","first-page":"1067","DOI":"10.1128\/jb.124.3.1067-1076.1975","volume":"124","author":"J. V. Hoeltje","year":"1975","unstructured":"Hoeltje, J. V., Mirelman, D., Sharon, N., and Schwarz, U. (1975) Novel type of murein transglycosylase in Escherichia coli, J.\u00a0Bacteriol., 124, 1067-1076, \nhttps:\/\/doi.org\/10.1128\/jb.124.3.1067-1076.1975.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR48","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0082914","volume":"8","author":"M. Shleeva","year":"2013","unstructured":"Shleeva, M., Goncharenko, A., Kudykina, Y., Young, D., Young, M., and Kaprelyants, A. (2013) Cyclic AMP-dependent resuscitation of dormant mycobacteria by exogenous free fatty acids, PLoS One, 8, e82914, \nhttps:\/\/doi.org\/10.1371\/journal.pone.0082914.","journal-title":"PLoS One"},{"key":"2814_CR49","doi-asserted-by":"publisher","first-page":"5017","DOI":"10.1128\/JB.186.15.5017-5030.2004","volume":"186","author":"J. Daniel","year":"2004","unstructured":"Daniel, J., Deb, C., Dubey, V. S., Sirakova, T. D., Abomoelak, B., Morbidoni, H. R., and Kolattukudy, P.\u00a0E. (2004) Induction of a novel class of diacylglycerol acyltransferases and triacylglycerol accumulation in Mycobacterium tuberculosis as it goes into a dormancy-like state in culture, J.\u00a0Bacteriol., 186, 5017-5030, \nhttps:\/\/doi.org\/10.1128\/JB.186.15.5017-5030.2004.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR50","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1002093","volume":"7","author":"J. Daniel","year":"2011","unstructured":"Daniel, J., Maamar, H., Deb, C., Sirakova, T. D., and Kolattukudy, P.\u00a0E. (2011) Mycobacterium tuberculosis uses host triacylglycerol to accumulate lipid droplets and acquires a dormancy-like phenotype in lipid-loaded macrophages, PLoS Pathog., 7, e1002093, \nhttps:\/\/doi.org\/10.1371\/journal.ppat.1002093.","journal-title":"PLoS Pathog."},{"key":"2814_CR51","doi-asserted-by":"publisher","first-page":"1281","DOI":"10.1007\/s12038-007-0137-6","volume":"32","author":"R. H. Schaloske","year":"2007","unstructured":"Schaloske, R. H., Blaesius, D., Schlatterer, C., and Lusche, D.\u00a0F. (2007) Arachidonic acid is a chemoattractant for Dictyostelium discoideum cells, J.\u00a0Biosci., 32, 1281-1289, \nhttps:\/\/doi.org\/10.1007\/s12038-007-0137-6.","journal-title":"J.\u00a0Biosci."},{"key":"2814_CR52","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1111\/j.1365-2958.1995.tb02290.x","volume":"16","author":"J. Downard","year":"1995","unstructured":"Downard, J., and Toal, D. (1995) Branched-chain fatty acids: the case for a novel form of cell-cell signalling during Myxococcus xanthus development, Mol. Microbiol., 16, 171-175, \nhttps:\/\/doi.org\/10.1111\/j.1365-2958.1995.tb02290.x.","journal-title":"Mol. Microbiol."},{"key":"2814_CR53","doi-asserted-by":"publisher","first-page":"2179","DOI":"10.1099\/00221287-128-9-2179","volume":"128","author":"J. L. Kerwin","year":"1982","unstructured":"Kerwin, J. L. (1982) Chemical control of the germination of asexual spores of Entornophthora culicis, a fungus parasitic on dipterans, J.\u00a0Gen. Microbiol., 128, 2179-2186, \nhttps:\/\/doi.org\/10.1099\/00221287-128-9-2179.","journal-title":"J.\u00a0Gen. Microbiol."},{"key":"2814_CR54","doi-asserted-by":"publisher","first-page":"4219","DOI":"10.1111\/j.1742-4658.2006.05420.x","volume":"273","author":"A. A. Motaal","year":"2006","unstructured":"Motaal, A. A., Tews, I., Schultz, J. E., and Linder, J.\u00a0U. (2006) Fatty acid regulation of adenylyl cyclase Rv2212 from Mycobacterium tuberculosis H37Rv, FEBS\u00a0J., 273, 4219-4228, \nhttps:\/\/doi.org\/10.1111\/j.1742-4658.2006.05420.x.","journal-title":"FEBS\u00a0J."},{"key":"2814_CR55","doi-asserted-by":"publisher","first-page":"2131","DOI":"10.1099\/00221287-144-8-2131","volume":"144","author":"S. Raychaudhuri","year":"1998","unstructured":"Raychaudhuri, S., Basu, M., and Mandal, N. C. (1998) Glutamate and cyclic AMP regulate the expression of galactokinase in Mycobacterium smegmatis, Microbiology, 144, 2131-2140, \nhttps:\/\/doi.org\/10.1099\/00221287-144-8-2131.","journal-title":"Microbiology"},{"key":"2814_CR56","doi-asserted-by":"publisher","first-page":"1883","DOI":"10.1099\/13500872-145-8-1883","volume":"145","author":"K. Virdy","year":"1999","unstructured":"Virdy, K., Sands, T. W., Kopko, S. H., van Es, S., Meima, M., Schaap, P., and Cotter, D.\u00a0A. (1999) High cAMP in spores of Dictyostelium discoideurn: association with spore dormancy and inhibition of germination, Microbiology, 145, 1883-1890, \nhttps:\/\/doi.org\/10.1099\/13500872-145-8-1883.","journal-title":"Microbiology"},{"key":"2814_CR57","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1046\/j.1365-2958.1998.01033.x","volume":"30","author":"U. S\u00fcsstrunk","year":"1998","unstructured":"S\u00fcsstrunk, U., Pidoux, J., Taubert, S., Ullmann, A., and Thompson, C.\u00a0J. (1998) Pleiotropi Streptomyces coelicolor, Mol. Microbiol., 30, 33-46, \nhttps:\/\/doi.org\/10.1046\/j.1365-2958.1998.01033.x.","journal-title":"Mol. Microbiol."},{"key":"2814_CR58","doi-asserted-by":"publisher","DOI":"10.1007\/BF01968222","volume":"35","author":"D. Gersch","year":"1979","unstructured":"Gersch, D., R\u00f6mer, W., and Kr\u00fcgel, H. (1979) Inverse regulation of spore germination and growth by cyclic AMP in Streptomyces hygroscopicus, Experientia, 35, 749, \nhttps:\/\/doi.org\/10.1007\/BF01968222.","journal-title":"Experientia"},{"key":"2814_CR59","doi-asserted-by":"publisher","first-page":"1893","DOI":"10.1128\/JB.186.6.1893-1897.2004","volume":"186","author":"A. Derouaux","year":"2004","unstructured":"Derouaux, A., Halici, S., Nothaft, H., Neutelings, T., Moutzourelis, G., Dusart, J., Titgemeyer, F., and Rigali, S. (2004) Deletion of a cyclic AMP receptor protein homologue diminishes germination and affects morphological development of Streptomyces coelicolor, J.\u00a0Bacteriol., 186, 1893-1897, \nhttps:\/\/doi.org\/10.1128\/JB.186.6.1893-1897.2004.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR60","doi-asserted-by":"publisher","unstructured":"Busby, S., Kolb, A., Buc, H. (1995) The E.\u00a0coli cyclic AMP receptor protein, in Nucleic Acids and Molecular Biology (Eckstein, F., and Lilley, D. M. J., eds) Vol.\u00a09, Springer, Berlin, Heidelberg, \nhttps:\/\/doi.org\/10.1007\/978-3-642-79488-9_9.","DOI":"10.1007\/978-3-642-79488-9_9"},{"key":"2814_CR61","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1111\/j.1462-5822.2010.01562.x","volume":"13","author":"G. Bai","year":"2011","unstructured":"Bai, G., Knapp, G. S., and Mcdonough, K. A. (2011) Cyclic AMP signaling in mycobacteria: redirecting the conversation with a common currency, Cell. Microbiol., 13, 349-358, \nhttps:\/\/doi.org\/10.1111\/j.1462-5822.2010.01562.x.","journal-title":"Cell. Microbiol."},{"key":"2814_CR62","doi-asserted-by":"publisher","first-page":"7795","DOI":"10.1128\/JB.187.22.7795-7804.2005","volume":"187","author":"G. Bai","year":"2005","unstructured":"Bai, G., Mccue, L. A., Mcdonough, K. A. (2005) Characterization of Mycobacterium tuberculosis Rv3676 (CRPMt), a cyclic AMP receptor protein-like DNA binding protein, J.\u00a0Bacteriol., 187, 7795-7804, \nhttps:\/\/doi.org\/10.1128\/JB.187.22.7795-7804.2005.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR63","doi-asserted-by":"publisher","first-page":"1274","DOI":"10.1111\/j.1365-2958.2005.04609.x","volume":"56","author":"L. Rickman","year":"2005","unstructured":"Rickman, L., Scott, C., Hunt, D. M., Hutchinson, T., Men\u00e9ndez, M. C., Whalan, R., Hinds, J., Colston, M.\u00a0J., Green, J., and Buxton, R.\u00a0S. (2005) A member of the cAMP receptor protein family of transcription regulators in Mycobacterium tuberculosis is required for virulence in mice and controls transcription of the rpfA gene coding for a resuscitation promoting factor, Mol. Microbiol., 56, 1274-1286, \nhttps:\/\/doi.org\/10.1111\/j.1365-2958.2005.04609.x.","journal-title":"Mol. Microbiol."},{"key":"2814_CR64","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1007\/s12223-014-0335-1","volume":"60","author":"C. Pedroza-Rold\u00e1n","year":"2015","unstructured":"Pedroza-Rold\u00e1n, C., Aceves-S\u00e1nchez Mde, J., Zaveri, A., Charles-Ni\u00f1o, C., Elizondo-Quiroga, D. E., Hern\u00e1ndez-Guti\u00e9rrez, R., Allen, K., Visweswariah, S. S., and Flores-Valdez, M.\u00a0A. (2015) The adenylyl cyclase Rv2212 modifies the proteome and infectivity of Mycobacterium bovis BCG, Folia Microbiol., 60, 21-31, \nhttps:\/\/doi.org\/10.1007\/s12223-014-0335-1.","journal-title":"Folia Microbiol."},{"key":"2814_CR65","doi-asserted-by":"publisher","first-page":"2841","DOI":"10.1128\/JB.00120-16","volume":"198","author":"A. A. Ganaie","year":"2016","unstructured":"Ganaie, A. A., Trivedi, G., Kaur, A., Jha, S. S., Anand, S., Rana, V., Singh, A., Kumar, S., and Sharma, C. (2016) Interaction of Erp protein of Mycobacterium tuberculosis with Rv2212 enhances intracellular survival of Mycobacterium smegmatis, J.\u00a0Bacteriol., 198, 2841-2852, \nhttps:\/\/doi.org\/10.1128\/JB.00120-16.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR66","doi-asserted-by":"publisher","DOI":"10.3389\/fcimb.2017.00370","volume":"7","author":"M. O. Shleeva","year":"2017","unstructured":"Shleeva, M. O., Kondratieva, T. K., Demina, G. R., Rubakova, E. I., Goncharenko, A. V., Apt, A.\u00a0S., and Kaprelyants, A.\u00a0S. (2017) Overexpression of adenylyl cyclase encoded by the Mycobacterium tuberculosis Rv2212 gene confers improved fitness, accelerated recovery from dormancy and enhanced virulence in mice, Front. Cell. Infect. Microbiol., 7, 370, \nhttps:\/\/doi.org\/10.3389\/fcimb.2017.00370.","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"2814_CR67","doi-asserted-by":"publisher","first-page":"380","DOI":"10.1134\/S0003683819030128","volume":"55","author":"M. O. Shleeva","year":"2019","unstructured":"Shleeva, M. O., Kondratieva, T. K., Goncharenko, A. V., Apt, A. S., and Kaprelyants, A.\u00a0S. (2019) cAMP-dependent transcription factor in Mycobacterium tuberculosis coded by the Rv3676 gene as a possible target for the development of antituberculosis drugs, Appl. Biochem. Microbiol., 55, 380-385, \nhttps:\/\/doi.org\/10.1134\/S0003683819030128.","journal-title":"Appl. Biochem. Microbiol."},{"key":"2814_CR68","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/S0065-2911(08)60166-6","volume":"41","author":"M. R. Barer","year":"1999","unstructured":"Barer, M. R., and Harwood, C. R. (1999) Bacterial viability and culturability, Adv. Microb. Physiol., 41, 93-137, \nhttps:\/\/doi.org\/10.1016\/S0065-2911(08)60166-6.","journal-title":"Adv. Microb. Physiol."},{"key":"2814_CR69","doi-asserted-by":"publisher","first-page":"68","DOI":"10.1111\/j.1574-695X.2008.00500.x","volume":"55","author":"G. Bai","year":"2009","unstructured":"Bai, G., Schaak, D. D., and McDonough, K.\u00a0A. (2009) cAMP levels within Mycobacterium tuberculosis and M.\u00a0bovis BCG increase upon infection of macrophages, FEMS Immunol. Med. Microbiol., 55, 68-73, \nhttps:\/\/doi.org\/10.1111\/j.1574-695X.2008.00500.x.","journal-title":"FEMS Immunol. Med. Microbiol."},{"key":"2814_CR70","doi-asserted-by":"publisher","first-page":"1287","DOI":"10.1016\/j.cell.2007.05.059","volume":"129","author":"N. Van der Wel","year":"2007","unstructured":"Van der Wel, N., Hava, D., Houben, D., Fluitsma, D., van Zon, M., Pierson, J., Brenner, M., and Peters, P.\u00a0J. (2007) M.\u00a0tuberculosis and M.\u00a0leprae translocate from the phagolysosome to the cytosol in myeloid cells, Cell, 129, 1287-1298, \nhttps:\/\/doi.org\/10.1016\/j.cell.2007.05.059.","journal-title":"Cell"},{"key":"2814_CR71","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0086886","volume":"9","author":"A. Rahman","year":"2014","unstructured":"Rahman, A., Sobia, P., Gupta, N., Kaer, L. V., and Das, G. (2014) Mycobacterium tuberculosis subverts the TLR-2\u00a0\u2013 MyD88 pathway to facilitate its translocation into the cytosol, PLoS One, 9, e86886, \nhttps:\/\/doi.org\/10.1371\/journal.pone.0086886.","journal-title":"PLoS One"},{"key":"2814_CR72","doi-asserted-by":"publisher","first-page":"5865","DOI":"10.1128\/JB.00683-09","volume":"191","author":"J. Van Ingen","year":"2009","unstructured":"Van Ingen, J., de Zwaan, R., Dekhuijzen, R., Boeree, M., and van Soolingen, D. (2009) Region of difference 1 in nontuberculous Mycobacterium species adds a phylogenetic and taxonomical character, J.\u00a0Bacteriol., 191, 5865-5867, \nhttps:\/\/doi.org\/10.1128\/JB.00683-09.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR73","doi-asserted-by":"publisher","first-page":"3686","DOI":"10.1242\/jcs.03091","volume":"119","author":"S. A. Kalamidas","year":"2006","unstructured":"Kalamidas, S. A., Kuehnel, M. P., Peyron, P., Rybin, V., Rauch, S., Kotoulas, O. B., Houslay, M., Hemmings, B. A., Gutierrez, M.\u00a0G., Anes, E., and Griffiths, G. (2006) cAMP synthesis and degradation by phagosomes regulate actin assembly and fusion events: consequences for mycobacteria, J.\u00a0Cell Sci., 119, 3686-3694, \nhttps:\/\/doi.org\/10.1242\/jcs.03091.","journal-title":"J.\u00a0Cell Sci."},{"key":"2814_CR74","doi-asserted-by":"publisher","first-page":"98","DOI":"10.1038\/nature08123","volume":"460","author":"N. Agarwal","year":"2009","unstructured":"Agarwal, N., Lamichhane, G., Gupta, R., Nolan, S., and Bishai, W.\u00a0R. (2009) Cyclic AMP intoxication of macrophages by a Mycobacterium tuberculosis adenylate cyclase, Nature, 460, 98-102, \nhttps:\/\/doi.org\/10.1038\/nature08123.","journal-title":"Nature"},{"key":"2814_CR75","doi-asserted-by":"publisher","first-page":"2681","DOI":"10.1128\/JB.187.8.2681-2692.2005","volume":"187","author":"M. A. Gazdik","year":"2005","unstructured":"Gazdik, M. A., and McDonough, K. A. (2005) Identification of cyclic AMP-regulated genes in Mycobacterium tuberculosis complex bacteria under low-oxygen conditions, J.\u00a0Bacteriol., 187, 2681-2692, \nhttps:\/\/doi.org\/10.1128\/JB.187.8.2681-2692.2005.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR76","doi-asserted-by":"publisher","first-page":"5883","DOI":"10.1021\/bi200156t","volume":"50","author":"H. Xu","year":"2011","unstructured":"Xu, H., Hegde, S. S., and Blanchard, J. S. (2011) The reversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMP, Biochemistry, 50, 5883-5892, \nhttps:\/\/doi.org\/10.1021\/bi200156t.","journal-title":"Biochemistry"},{"key":"2814_CR77","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0008174","volume":"4","author":"G. R. Demina","year":"2009","unstructured":"Demina, G. R., Makarov, V. A., Nikitushkin, V. D., Ryabova, O. B., Vostroknutova, G. N., Salina, E. G., Shleeva, M.\u00a0O., Goncharenko, A.\u00a0V., and Kaprelyants, A.\u00a0S. (2009) Finding of the low molecular weight inhibitors of resuscitation promoting factor enzymatic and resuscitation activity, PLoS One, 4, e8174, \nhttps:\/\/doi.org\/10.1371\/journal.pone.0008174.","journal-title":"PLoS One"},{"key":"2814_CR78","doi-asserted-by":"publisher","DOI":"10.1186\/s12941-017-0244-7","volume":"16","author":"G. R. Demina","year":"2017","unstructured":"Demina, G. R., Nikitushkin, V. D., Shleeva, M. O., Riabova, O. B., Lepioshkin, A. Y., Makarov, V. A., and Kaprelyants, A. S. (2017) Benzoylphenyl thiocyanates are new, effective inhibitors of the mycobacterial resuscitation promoting factor B protein, Ann. Clin. Microbiol. Antimicrob., 16, 69, \nhttps:\/\/doi.org\/10.1186\/s12941-017-0244-7.","journal-title":"Ann. Clin. Microbiol. Antimicrob."},{"key":"2814_CR79","doi-asserted-by":"publisher","first-page":"190","DOI":"10.1111\/j.1574-6968.2008.01098.x","volume":"281","author":"B. Jungwirth","year":"2008","unstructured":"Jungwirth, B., Emer, D., Brune, I., Hansmeier, N., P\u00fchler, A., Eikmanns, B.\u00a0J., and Tauch, A. (2008) Triple transcriptional control of the resuscitation promoting factor\u00a02 (rpf2) gene of Corynebacterium glutamicum by the regulators of acetate metabolism RamA and RamB and the cAMP-dependent regulator GlxR, FEMS Microbiol. Lett., 281, 190-197, \nhttps:\/\/doi.org\/10.1111\/j.1574-6968.2008.01098.x.","journal-title":"FEMS Microbiol. Lett."},{"key":"2814_CR80","doi-asserted-by":"publisher","DOI":"10.1007\/s11306-020-1645-8","volume":"16","author":"V. D. Nikitushkin","year":"2020","unstructured":"Nikitushkin, V. D., Trenkamp, S., Demina, G. R., Shleeva, M.\u00a0O., and Kaprelyants, A.\u00a0S. (2020) Metabolic profiling of dormant Mycolicibacterium smegmatis cells\u2019 reactivation reveals a gradual assembly of metabolic processes, Metabolomics, 16, 24, \nhttps:\/\/doi.org\/10.1007\/s11306-020-1645-8.","journal-title":"Metabolomics"},{"key":"2814_CR81","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2017.00524","volume":"8","author":"M. O. Shleeva","year":"2017","unstructured":"Shleeva, M. O., Trutneva, K. A., Demina, G. R., Zinin, A. I., Sorokoumova, G. M., Laptinskaya, P. K., Shumkova, E. S., and Kaprelyants, A. S. (2017) Free trehalose accumulation in dormant Mycobacterium smegmatis cells and its breakdown in early resuscitation phase, Front. Microbiol., 8, 524, \nhttps:\/\/doi.org\/10.3389\/fmicb.2017.00524.","journal-title":"Front. Microbiol."},{"key":"2814_CR82","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2018.02083","volume":"9","author":"K. Trutneva","year":"2018","unstructured":"Trutneva, K., Shleeva, M., Nikitushkin, V., Demina, G., and Kaprelyants, A. (2018) Protein composition of Mycobacterium smegmatis differs significantly between active cells and dormant cells with ovoid morphology, Front. Microbiol., 9, 2083, \nhttps:\/\/doi.org\/10.3389\/fmicb.2018.02083.","journal-title":"Front. Microbiol."},{"key":"2814_CR83","doi-asserted-by":"publisher","DOI":"10.3389\/fcimb.2020.00026","volume":"10","author":"K. A. Trutneva","year":"2020","unstructured":"Trutneva, K. A., Shleeva, M. O., Demina, G. R., Vostroknutova, G.\u00a0N., and Kaprelyans, A.\u00a0S. (2020) One-year old dormant, \u201cnon-culturable\u201d Mycobacterium tuberculosis preserves significantly diverse protein profile, Front. Cell. Infect. Microbiol., 10, 26, \nhttps:\/\/doi.org\/10.3389\/fcimb.2020.00026.","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"2814_CR84","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0269847","volume":"17","author":"V. Nikitushkin","year":"2022","unstructured":"Nikitushkin, V., Shleeva, M., Loginov, D., Dy\u010dka, F.\u00a0F., Sterba, J., and Kaprelyants, A. (2022) Shotgun proteomic profiling of dormant, \u201cnon-culturable\u201d Mycobacterium tuberculosis, PLoS One, 17, e0269847, \nhttps:\/\/doi.org\/10.1371\/journal.pone.0269847.","journal-title":"PLoS One"},{"key":"2814_CR85","doi-asserted-by":"publisher","first-page":"224","DOI":"10.1016\/j.jbiosc.2011.09.018","volume":"113","author":"H. Li","year":"2012","unstructured":"Li, H., Su, H., Kim, S. B., Chang, Y. K., Hong, S. K., Seo, Y. G., and Kim, C.\u00a0J. (2012) Enhanced production of trehalose in Escherichia coli by homologous expression of otsBA in the presence of the trehalase inhibitor, validamycin\u00a0A, at high osmolarity, J.\u00a0Biosci. Bioeng., 113, 224-232, \nhttps:\/\/doi.org\/10.1016\/j.jbiosc.2011.09.018.","journal-title":"J.\u00a0Biosci. Bioeng."},{"key":"2814_CR86","doi-asserted-by":"publisher","first-page":"1084","DOI":"10.1128\/jb.116.2.1084-1085.1973","volume":"116","author":"A. Hey-Ferguson","year":"1973","unstructured":"Hey-Ferguson, A., Mitchell, M., and Elbein, A. D. (1973) Trehalose metabolism in germinating spores of Streptomyces hygroscopicus, J.\u00a0Bacteriol., 116, 1084-1085, \nhttps:\/\/doi.org\/10.1128\/jb.116.2.1084-1085.1973.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR87","doi-asserted-by":"publisher","first-page":"3503","DOI":"10.1073\/pnas.79.11.3503","volume":"79","author":"J. M. Thevelein","year":"1982","unstructured":"Thevelein, J. M., den Hollander, J. A., and Shulman, R.\u00a0G. (1982) Changes in the activity and properties of trehalase during early germination of yeast ascospores: correlation with trehalose breakdown as studied by in\u00a0vivo 13C NMR, Proc. Natl. Acad. Sci. USA, 79, 3503-3507, \nhttps:\/\/doi.org\/10.1073\/pnas.79.11.3503.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2814_CR88","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1111\/j.1432-1033.1983.tb07780.x","volume":"136","author":"J. M. Thevelein","year":"1983","unstructured":"Thevelein, J. M., and Jones, K. A. (1983) Reversibility characteristics of glucose-induced trehalase activation associated with the breaking of dormancy in yeast ascospores, Eur.\u00a0J. Biochem., 136, 583-387, \nhttps:\/\/doi.org\/10.1111\/j.1432-1033.1983.tb07780.x.","journal-title":"Eur.\u00a0J. Biochem."},{"key":"2814_CR89","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1128\/mr.48.1.42-59.1984","volume":"48","author":"J. M. Thevelein","year":"1984","unstructured":"Thevelein, J. M. (1984) Regulation of trehalase mobilization in fungi, Microbiol. Rev., 48, 42-59, \nhttps:\/\/doi.org\/10.1128\/mr.48.1.42-59.1984.","journal-title":"Microbiol. Rev."},{"key":"2814_CR90","doi-asserted-by":"publisher","first-page":"644","DOI":"10.1128\/jb.153.2.644-651.1983","volume":"153","author":"C. H. Ortiz","year":"1983","unstructured":"Ortiz, C. H., Maia, J. C., Tenan, M. N., Braz-Padr\u00e3o, G. R., Mattoon, J.\u00a0R., and Panek, A.\u00a0D. (1983) Regulation of yeast trehalase by a monocyclic, cyclic AMP-dependent phosphorylation-dephosphorylation cascade system, J.\u00a0Bacteriol., 153, 644-651, \nhttps:\/\/doi.org\/10.1128\/jb.153.2.644-651.1983.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR91","doi-asserted-by":"publisher","first-page":"3637","DOI":"10.1128\/jb.172.7.3637-3643.1990","volume":"172","author":"M. J. McBride","year":"1990","unstructured":"McBride, M. J., and Ensign, J. C. (1990) Regulation of trehalose metabolism by Streptomyces griseus spores, J.\u00a0Bacteriol., 172, 3637-3643, \nhttps:\/\/doi.org\/10.1128\/jb.172.7.3637-3643.1990.","journal-title":"J.\u00a0Bacteriol."},{"key":"2814_CR92","doi-asserted-by":"publisher","DOI":"10.1093\/femsle\/fnw206","volume":"363","author":"V. D. Nikitushkin","year":"2016","unstructured":"Nikitushkin, V. D., Shleeva, M. O., Zinin, A. I., Trutneva, K. A., Ostrovsky, D. N., and Kaprelyants, A. S. (2016) The main pigment of the dormant Mycobacterium smegmatis is porphyrin, FEMS Microbiol. Lett., 363, fnw206, \nhttps:\/\/doi.org\/10.1093\/femsle\/fnw206.","journal-title":"FEMS Microbiol. Lett."},{"key":"2814_CR93","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamem.2024.184270","volume":"1866","author":"I. A. Gligonov","year":"2024","unstructured":"Gligonov, I. A., Bagaeva, D. I., Demina, G. R., Vostroknutova, G. N., Vorozhtsov, D. S., Kaprelyants, A. S., Savitsky, A.\u00a0P., and Shleeva, M.\u00a0O. (2024) The accumulation of methylated porphyrins in dormant cells of Mycolicibacterium smegmatis is accompanied by a decrease in membrane fluidity and an impede of the functioning of the respiratory chain, Biochim. Biophys. Acta Biomembr., 1866, 184270, \nhttps:\/\/doi.org\/10.1016\/j.bbamem.2024.184270.","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"2814_CR94","doi-asserted-by":"publisher","first-page":"1186","DOI":"10.1126\/science.aat7925","volume":"362","author":"I. Budin","year":"2018","unstructured":"Budin, I., de Rond, T., Chen, Y., Chan, L. J. G., Petzold, C.\u00a0J., and Keasling, J.\u00a0D. (2018) Viscous control of cellular respiration by membrane lipid composition, Science, 362, 1186-1189, \nhttps:\/\/doi.org\/10.1126\/science.aat7925.","journal-title":"Science"},{"key":"2814_CR95","doi-asserted-by":"publisher","first-page":"60","DOI":"10.1016\/j.pbiomolbio.2007.05.001","volume":"95","author":"N. C. Mykytczuk","year":"2007","unstructured":"Mykytczuk, N. C., Trevors, J. T., Leduc, L. G., and Ferroni, G.\u00a0D. (2007) Fluorescence polarization in studies of bacterial cytoplasmic membrane fluidity under environmental stress, Progress Biophys. Mol. Biol., 95, 60-82, \nhttps:\/\/doi.org\/10.1016\/j.pbiomolbio.2007.05.001.","journal-title":"Progress Biophys. Mol. Biol."},{"key":"2814_CR96","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1146\/annurev.ph.57.030195.000315","volume":"57","author":"J. R. Hazel","year":"1995","unstructured":"Hazel, J. R. (1995) Thermal adaptation in biological membranes: is homeoviscous adaptation the explanation? Annu. Rev. Physiol., 57, 19-42, \nhttps:\/\/doi.org\/10.1146\/annurev.ph.57.030195.000315.","journal-title":"Annu. Rev. Physiol."},{"key":"2814_CR97","doi-asserted-by":"publisher","first-page":"2210","DOI":"10.1073\/pnas.1416285112","volume":"112","author":"H. A. Dailey","year":"2015","unstructured":"Dailey, H. A., Gerdes, S., Dailey, T. A., Burch, J.\u00a0S., and Phillips, J.\u00a0D. (2015) Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin, Proc. Natl. Acad. Sci. USA, 112, 2210-2215, \nhttps:\/\/doi.org\/10.1073\/pnas.1416285112.","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2814_CR98","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fmicb.2021.642487","volume":"12","author":"M. Kundu","year":"2021","unstructured":"Kundu, M., and Basu, J. (2021) Applications of transcriptomics and proteomics for understanding dormancy and resuscitation in Mycobacterium tuberculosis, Front. Microbiol., 12, 1-16, \nhttps:\/\/doi.org\/10.3389\/fmicb.2021.642487.","journal-title":"Front. Microbiol."},{"key":"2814_CR99","doi-asserted-by":"publisher","DOI":"10.1128\/mSystems.00057-17","volume":"2","author":"M. Zimmermann","year":"2017","unstructured":"Zimmermann, M., Kogadeeva, M., Gengenbacher, M., Mcewen, G., Mollenkopf, H.-J., Zamboni, N., Kaufmann, S. H. E., and Sauer, U. (2017) Integration of metabolomics and transcriptomics reveals a complex diet of Mycobacterium tuberculosis during early macrophage infection, mSystems, 2, e00057, \nhttps:\/\/doi.org\/10.1128\/mSystems.00057-17.","journal-title":"mSystems"},{"key":"2814_CR100","doi-asserted-by":"publisher","first-page":"2062","DOI":"10.1128\/iai.64.6.2062-2069.1996","volume":"64","author":"L. G. Wayne","year":"1996","unstructured":"Wayne, L. G., and Hayes, L. G. (1996) An in\u00a0vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence, Infect. Immun., 64, 2062-2069, \nhttps:\/\/doi.org\/10.1128\/iai.64.6.2062-2069.1996.","journal-title":"Infect. Immun."},{"key":"2814_CR101","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1146\/annurev.micro.55.1.139","volume":"55","author":"L. Wayne","year":"2001","unstructured":"Wayne, L., and Sohaskey, C. (2001) Nonreplicating persistence of Mycobacterium tuberculosis, Annu. Rev. Microbiol., 55, 139-163, \nhttps:\/\/doi.org\/10.1146\/annurev.micro.55.1.139.","journal-title":"Annu. Rev. Microbiol."},{"key":"2814_CR102","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0011622","volume":"5","author":"A. M. Sherrid","year":"2010","unstructured":"Sherrid, A. M., Rustad, T. R., Cangelosi, G. A., and Sherman, D.\u00a0R., (2010) Characterization of a Clp protease gene regulator and the reaeration response in Mycobacterium tuberculosis, PLoS One, 5, e11622, \nhttps:\/\/doi.org\/10.1371\/journal.pone.0011622.","journal-title":"PLoS One"},{"key":"2814_CR103","doi-asserted-by":"publisher","DOI":"10.3389\/fcimb.2019.00272","volume":"9","author":"E. G. Salina","year":"2019","unstructured":"Salina, E. G., Grigorov, A. S., Bychenko, O. S., Skvortsova, Y.\u00a0V., Mamedov, I. Z., Azhikina, T.\u00a0L., and Kaprelyants, A.\u00a0S. (2019) Resuscitation of dormant \u201cnon-culturable\u201d Mycobacterium tuberculosis is characterized by immediate transcriptional burst, Front. Cell. Infect. Microbiol., 9, 272, \nhttps:\/\/doi.org\/10.3389\/fcimb.2019.00272.","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"2814_CR104","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1016\/j.chom.2015.06.001","volume":"18","author":"O. T. Schubert","year":"2015","unstructured":"Schubert, O. T., Ludwig, C., Kogadeeva, M., Zimmermann, M., Rosenberger, G., Gengenbacher, M., Gillet, L. C., Collins, B. C., R\u00f6st, H. L., Kaufmann, S. H., Sauer, U., and Aebersold, R. (2015) Absolute proteome composition and dynamics during dormancy and resuscitation of Mycobacterium tuberculosis, Cell Host Microbe, 18, 96-108, \nhttps:\/\/doi.org\/10.1016\/j.chom.2015.06.001.","journal-title":"Cell Host Microbe"},{"key":"2814_CR105","doi-asserted-by":"publisher","first-page":"1876","DOI":"10.1111\/j.1365-2958.2006.05068.x","volume":"59","author":"M. V. Madiraju","year":"2006","unstructured":"Madiraju, M. V., Moomey, M., Neuenschwander, P. F., Muniruzzaman, S., Yamamoto, K., Grimwade, J.\u00a0E., and Rajagopalan, M. (2006) The intrinsic ATPase activity of Mycobacterium tuberculosis DnaA promotes rapid oligomerization of DnaA on oriC, Mol. Microbiol., 59, 1876-1890, \nhttps:\/\/doi.org\/10.1111\/j.1365-2958.2006.05068.x.","journal-title":"Mol. Microbiol."},{"key":"2814_CR106","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1007\/s12013-012-9415-5","volume":"65","author":"W. Hong","year":"2013","unstructured":"Hong, W., Deng, W., and Xie, J. (2013) The structure, function, and regulation of Mycobacterium FtsZ, Cell Biochem. Biophys., 65, 97-105, \nhttps:\/\/doi.org\/10.1007\/s12013-012-9415-5.","journal-title":"Cell Biochem. Biophys."},{"key":"2814_CR107","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2016.01346","volume":"7","author":"P. Du","year":"2016","unstructured":"Du, P., Sohaskey, C. D., and Shi, L. (2016) Transcriptional and physiological changes during Mycobacterium tuberculosis reactivation from non-replicating persistence, Front. Microbiol., 7, 1346, \nhttps:\/\/doi.org\/10.3389\/fmicb.2016.01346.","journal-title":"Front. Microbiol."},{"key":"2814_CR108","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2020.107577","volume":"31","author":"E. J. R. Peterson","year":"2020","unstructured":"Peterson, E. J. R., Abidi, A. A., Arrieta-Ortiz, M. L., Aguilar, B., Yurkovich, J. T., Kaur, A., Pan, M., Srinivas, V., Shmulevich, I., and Baliga, N.\u00a0S. (2020) Intricate genetic programs controlling dormancy in Mycobacterium tuberculosis, Cell Rep., 31, 107577, \nhttps:\/\/doi.org\/10.1016\/j.celrep.2020.107577.","journal-title":"Cell Rep."},{"key":"2814_CR109","doi-asserted-by":"publisher","first-page":"22004","DOI":"10.1074\/jbc.M112.357715","volume":"287","author":"K. L. Smollett","year":"2012","unstructured":"Smollett, K. L., Smith, K. M., Kahramanoglou, C., Arnvig, K. B., Buxton, R. S., and Davis, E.\u00a0O. (2012) Global analysis of the regulon of the transcriptional repressor LexA, a key component of SOS response in Mycobacterium tuberculosis, J.\u00a0Biol. Chem., 287, 22004-22014, \nhttps:\/\/doi.org\/10.1074\/jbc.M112.357715.","journal-title":"J.\u00a0Biol. Chem."},{"key":"2814_CR110","doi-asserted-by":"publisher","first-page":"2160","DOI":"10.1074\/mcp.M115.051151","volume":"14","author":"V. Gopinath","year":"2015","unstructured":"Gopinath, V., Raghunandanan, S., Gomez, R. L., Jose, L., Surendran, A., Ramachandran, R., Pushparajan, A. R., Mundayoor, S., Jaleel, A., and Kumar, R.\u00a0A. (2015) Profiling the proteome of Mycobacterium tuberculosis during dormancy and reactivation, Mol. Cell. Proteomics, 14, 2160-2176, \nhttps:\/\/doi.org\/10.1074\/mcp.M115.051151.","journal-title":"Mol. Cell. Proteomics"},{"key":"2814_CR111","doi-asserted-by":"publisher","first-page":"717","DOI":"10.1046\/j.1365-2958.2002.02779.x","volume":"43","author":"J. C. Betts","year":"2002","unstructured":"Betts, J. C., Lukey, P. T., Robb, L. C., McAdam, R.\u00a0A., and Duncan, K. (2002) Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling, Mol. Microbiol., 43, 717-731, \nhttps:\/\/doi.org\/10.1046\/j.1365-2958.2002.02779.x.","journal-title":"Mol. Microbiol."},{"key":"2814_CR112","doi-asserted-by":"publisher","first-page":"218","DOI":"10.1016\/j.tube.2004.02.003","volume":"84","author":"M. I. Voskuil","year":"2004","unstructured":"Voskuil, M. I., Visconti, K. C., and Schoolnik, G. K. (2004) Mycobacterium tuberculosis gene expression during adaptation to stationary phase and low-oxygen dormancy, Tuberculosis, 84, 218-227, \nhttps:\/\/doi.org\/10.1016\/j.tube.2004.02.003.","journal-title":"Tuberculosis"},{"key":"2814_CR113","doi-asserted-by":"publisher","DOI":"10.1186\/s12864-019-6190-3","volume":"20","author":"M. Nandi","year":"2019","unstructured":"Nandi, M., Sikri, K., Chaudhary, N., Mande, S. C., Sharma, R. D., and Tyagi, J. S. (2019) Multiple transcription factors co-regulate the Mycobacterium tuberculosis adaptation response to vitamin\u00a0C, BioMed Central Genomics, 20, 887, \nhttps:\/\/doi.org\/10.1186\/s12864-019-6190-3.","journal-title":"BioMed Central Genomics"},{"key":"2814_CR114","doi-asserted-by":"publisher","first-page":"2351","DOI":"10.1074\/jbc.M114.615534","volume":"290","author":"A. McGillivray","year":"2015","unstructured":"McGillivray, A., Golden, N. A., and Kaushal, D. (2015) The Mycobacterium tuberculosis Clp gene regulator is required for in\u00a0vitro reactivation from hypoxia-induced dormancy, J.\u00a0Biol. Chem., 290, 2351-2367, \nhttps:\/\/doi.org\/10.1074\/jbc.M114.615534.","journal-title":"J.\u00a0Biol. Chem."},{"key":"2814_CR115","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-019-40051-5","volume":"9","author":"S. Raghunandanan","year":"2019","unstructured":"Raghunandanan, S., Jose, L., Gopinath, V., and Kumar, R.\u00a0A. (2019) Comparative label-free lipidomic analysis of Mycobacterium tuberculosis during dormancy and reactivation, Sci. Rep., 9, 3660, \nhttps:\/\/doi.org\/10.1038\/s41598-019-40051-5.","journal-title":"Sci. Rep."},{"key":"2814_CR116","doi-asserted-by":"publisher","first-page":"28201","DOI":"10.1074\/jbc.M003241200","volume":"275","author":"K. H. Choi","year":"2000","unstructured":"Choi, K. H., Kremer, L., Besra, G. S., and Rock, C.\u00a0O. (2000) Identification and substrate specificity of beta-ketoacyl (acyl carrier protein) synthase\u00a0III (mtFabH) from Mycobacterium tuberculosis, J.\u00a0Biol. Chem., 275, 28201-28207, \nhttps:\/\/doi.org\/10.1074\/jbc.M003241200.","journal-title":"J.\u00a0Biol. Chem."},{"key":"2814_CR117","doi-asserted-by":"publisher","first-page":"178","DOI":"10.1016\/j.chom.2014.12.008","volume":"17","author":"J. Vaubourgeix","year":"2015","unstructured":"Vaubourgeix, J., Lin, G., Dhar, N., Chenouard, N., Jiang, X., Botella, H., Lupoli, T., Mariani, O., Yang, G., Ouerfelli, O., Unser, M., Schnappinger, D., McKinney, J., and Nathan, C. (2015) Stressed mycobacteria use the chaperone ClpB to sequester irreversibly oxidized proteins asymmetrically within and between cells, Cell Host Microbe, 17, 178-190, \nhttps:\/\/doi.org\/10.1016\/j.chom.2014.12.008.","journal-title":"Cell Host Microbe"},{"key":"2814_CR118","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1111\/j.1365-2958.2009.06783.x","volume":"73","author":"A. M. Abdallah","year":"2009","unstructured":"Abdallah, A. M., Verboom, T., Weerdenburg, E. M., Gey van Pittius, N.\u00a0C., Mahasha, P. W., Jim\u00e9nez, C., Parra, M., Cadieux, N., Brennan, M.\u00a0J., Appelmelk, B.\u00a0J., and Bitter, W. (2009) PPE and PE-PGRS proteins of Mycobacterium marinum are transported via the type VII secretion system ESX-5, Mol. Microbiol., 73, 329-340, \nhttps:\/\/doi.org\/10.1111\/j.1365-2958.2009.06783.x.","journal-title":"Mol. Microbiol."},{"key":"2814_CR119","doi-asserted-by":"publisher","DOI":"10.1016\/j.imbio.2022.152321","volume":"228","author":"C. D\u2019Souza","year":"2023","unstructured":"D\u2019Souza, C., Kishore, U., and Tsolaki, A. G. (2023) The PE-PPE family of Mycobacterium tuberculosis: proteins in disguise, Immunobiology, 228, 152321, \nhttps:\/\/doi.org\/10.1016\/j.imbio.2022.152321.","journal-title":"Immunobiology"},{"key":"2814_CR120","doi-asserted-by":"publisher","DOI":"10.3389\/fcimb.2016.00049","volume":"6","author":"S. Shah","year":"2016","unstructured":"Shah, S., and Briken, V. (2016) Modular organization of the ESX-5 secretion system in Mycobacterium tuberculosis, Front. Cell. Infect. Microbiol., 6, 49, \nhttps:\/\/doi.org\/10.3389\/fcimb.2016.00049.","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"2814_CR121","doi-asserted-by":"publisher","first-page":"638","DOI":"10.1134\/S0026261711050080","volume":"80","author":"Y. K. Kudykina","year":"2011","unstructured":"Kudykina, Y. K., Shleeva, M. O., Artsabanov, V. Y., Suzina, N.\u00a0E., and Kaprelyants, A.\u00a0S. (2011) Generation of dormant forms by Mycobacterium smegmatis in the poststationary phase during gradual acidification of the medium, Microbiology, 80, 638-649, \nhttps:\/\/doi.org\/10.1134\/S0026261711050080.","journal-title":"Microbiology"},{"key":"2814_CR122","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1099\/mic.0.000604","volume":"164","author":"S. K. Dolan","year":"2018","unstructured":"Dolan, S. K., Wijaya, A., Geddis, S. M., Spring, D. R., Silva-Rocha, R., and Welch, M. (2018) Loving the poison: the methylcitrate cycle and bacterial pathogenesis, Microbiology, 164, 251-259, \nhttps:\/\/doi.org\/10.1099\/mic.0.000604.","journal-title":"Microbiology"}],"container-title":["Biochemistry (Moscow)"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1134\/S0006297924603757.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1134\/S0006297924603757","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1134\/S0006297924603757.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T00:22:51Z","timestamp":1773620571000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1134\/S0006297924603757"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2]]},"references-count":122,"journal-issue":{"issue":"S1","published-print":{"date-parts":[[2025,2]]}},"alternative-id":["2814"],"URL":"https:\/\/doi.org\/10.1134\/s0006297924603757","relation":{},"ISSN":["0006-2979","1608-3040"],"issn-type":[{"value":"0006-2979","type":"print"},{"value":"1608-3040","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,2]]},"assertion":[{"value":"16 May 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"15 June 2024","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"23 August 2024","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 March 2025","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"Ethics approval and consent to participate.\n                      This work does not contain any studies involving human and animal subjects.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics declarations"}},{"value":"Conflict of interest.\n                      The authors of this work declare that they have no conflicts of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics declarations"}}]}}