{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T18:04:19Z","timestamp":1777572259969,"version":"3.51.4"},"reference-count":202,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2017,3,10]],"date-time":"2017-03-10T00:00:00Z","timestamp":1489104000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Microbiol Spectr"],"published-print":{"date-parts":[[2017,3,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Reversible protein phosphorylation is the most common type of epigenetic posttranslational modification in living cells used as a major regulation mechanism of biological processes. The\n            <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n            genome encodes for 11 serine\/threonine protein kinases that are responsible for sensing environmental signals to coordinate a cellular response to ensure the pathogen\u2019s infectivity, survival, and growth. To overcome killing mechanisms generated within the host during infection,\n            <jats:italic>M. tuberculosis<\/jats:italic>\n            enters a state of nonreplicating persistence that is characterized by arrested growth, limited metabolic activity, and phenotypic resistance to antimycobacterial drugs. In this article we focus our attention on the role of\n            <jats:italic>M. tuberculosis<\/jats:italic>\n            serine\/threonine protein kinases in sensing the host environment to coordinate the bacilli\u2019s physiology, including growth, cell wall components, and central metabolism, to establish a persistent infection.\n          <\/jats:p>","DOI":"10.1128\/microbiolspec.tbtb2-0005-2015","type":"journal-article","created":{"date-parts":[[2017,3,10]],"date-time":"2017-03-10T12:46:04Z","timestamp":1489149964000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":28,"title":["Epigenetic Phosphorylation Control of\n            <i>Mycobacterium tuberculosis<\/i>\n            Infection and Persistence"],"prefix":"10.1128","volume":"5","author":[{"given":"Melissa","family":"Richard-Greenblatt","sequence":"first","affiliation":[{"name":"Division of Infectious Diseases, Department of Medicine, University of British Columbia, Vancouver, BC V6H 3Z6, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yossef","family":"Av-Gay","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Department of Medicine, University of British Columbia, Vancouver, BC V6H 3Z6, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","unstructured":"Wang JY Koshland DE Jr. 1978. Evidence for protein kinase activities in the prokaryote Salmonella typhimurium . J Biol Chem 253: 7605\u20137608. [PubMed]","DOI":"10.1016\/S0021-9258(17)34411-3"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","unstructured":"Garnak M Reeves HC. 1979. Phosphorylation of isocitrate dehydrogenase of Escherichia coli . Science 203: 1111\u20131112. http:\/\/dx.doi.org\/10.1126\/science.34215 [PubMed]","DOI":"10.1126\/science.34215"},{"key":"e_1_3_2_4_2","doi-asserted-by":"crossref","unstructured":"Manai M Cozzone AJ. 1979. Analysis of the protein-kinase activity of Escherichia coli cells. Biochem Biophys Res Commun 91: 819\u2013826. http:\/\/dx.doi.org\/10.1016\/0006-291X(79)91953-3","DOI":"10.1016\/0006-291X(79)91953-3"},{"key":"e_1_3_2_5_2","doi-asserted-by":"crossref","unstructured":"Mizuno T Wurtzel ET Inouye M. 1982. Osmoregulation of gene expression. II. DNA sequence of the envZ gene of the ompB operon of Escherichia coli and characterization of its gene product. J Biol Chem 257: 13692\u201313698. [PubMed]","DOI":"10.1016\/S0021-9258(18)33502-6"},{"key":"e_1_3_2_6_2","doi-asserted-by":"crossref","unstructured":"Tommassen J de Geus P Lugtenberg B Hackett J Reeves P. 1982. Regulation of the pho regulon of Escherichia coli K-12: cloning of the regulatory genes phoB and phoR and identification of their gene products. J Mol Biol 157: 265\u2013274. http:\/\/dx.doi.org\/10.1016\/0022-2836(82)90233-9 [PubMed]","DOI":"10.1016\/0022-2836(82)90233-9"},{"key":"e_1_3_2_7_2","doi-asserted-by":"crossref","unstructured":"Grebe TW Stock JB. 1999. The histidine protein kinase superfamily. Adv Microb Physiol 41: 139\u2013227. http:\/\/dx.doi.org\/10.1016\/S0065-2911(08)60167-8","DOI":"10.1016\/S0065-2911(08)60167-8"},{"key":"e_1_3_2_8_2","doi-asserted-by":"crossref","unstructured":"Kannan N Taylor SS Zhai Y Venter JC Manning G. 2007. Structural and functional diversity of the microbial kinome. PLoS Biol 5: e17. http:\/\/dx.doi.org\/10.1371\/journal.pbio.0050017 [PubMed]","DOI":"10.1371\/journal.pbio.0050017"},{"key":"e_1_3_2_9_2","doi-asserted-by":"crossref","unstructured":"Chao J Wong D Zheng X Poirier V Bach H Hmama Z Av-Gay Y. 2010. Protein kinase and phosphatase signaling in Mycobacterium tuberculosis physiology and pathogenesis. Biochim Biophys Acta 1804: 620\u2013627. http:\/\/dx.doi.org\/10.1016\/j.bbapap.2009.09.008","DOI":"10.1016\/j.bbapap.2009.09.008"},{"key":"e_1_3_2_10_2","doi-asserted-by":"crossref","unstructured":"Wong D Chao JD Av-Gay Y. 2013. Mycobacterium tuberculosis -secreted phosphatases: from pathogenesis to targets for TB drug development. Trends Microbiol 21: 100\u2013109. http:\/\/dx.doi.org\/10.1016\/j.tim.2012.09.002 [PubMed][CrossRef]","DOI":"10.1016\/j.tim.2012.09.002"},{"key":"e_1_3_2_11_2","doi-asserted-by":"crossref","unstructured":"Prisic S Husson RN. 2014. Mycobacterium tuberculosis serine\/threonine protein kinases. Microbiol Spectr 2: 2. http:\/\/dx.doi.org\/10.1128\/microbiolspec.MGM2-0006-2013","DOI":"10.1128\/microbiolspec.MGM2-0006-2013"},{"key":"e_1_3_2_12_2","doi-asserted-by":"crossref","unstructured":"Sickmann A Meyer HE. 2001. Phosphoamino acid analysis. Proteomics 1: 200\u2013206. http:\/\/dx.doi.org\/10.1002\/1615-9861(200102)1:2<200::AID-PROT200>3.0.CO;2-V [PubMed]","DOI":"10.1002\/1615-9861(200102)1:2<200::AID-PROT200>3.0.CO;2-V"},{"key":"e_1_3_2_13_2","doi-asserted-by":"crossref","unstructured":"Av-Gay Y Everett M. 2000. The eukaryotic-like Ser\/Thr protein kinases of Mycobacterium tuberculosis . Trends Microbiol 8: 238\u2013244. http:\/\/dx.doi.org\/10.1016\/S0966-842X(00)01734-0","DOI":"10.1016\/S0966-842X(00)01734-0"},{"key":"e_1_3_2_14_2","doi-asserted-by":"crossref","unstructured":"Alber T. 2009. Signaling mechanisms of the Mycobacterium tuberculosis receptor Ser\/Thr protein kinases. Curr Opin Struct Biol 19: 650\u2013657. http:\/\/dx.doi.org\/10.1016\/j.sbi.2009.10.017","DOI":"10.1016\/j.sbi.2009.10.017"},{"key":"e_1_3_2_15_2","doi-asserted-by":"crossref","unstructured":"Kumar P Kumar D Parikh A Rananaware D Gupta M Singh Y Nandicoori VK. 2009. The Mycobacterium tuberculosis protein kinase K modulates activation of transcription from the promoter of mycobacterial monooxygenase operon through phosphorylation of the transcriptional regulator VirS. J Biol Chem 284: 11090\u201311099. http:\/\/dx.doi.org\/10.1074\/jbc.M808705200","DOI":"10.1074\/jbc.M808705200"},{"key":"e_1_3_2_16_2","doi-asserted-by":"crossref","unstructured":"Koul A Choidas A Treder M Tyagi AK Drlica K Singh Y Ullrich A. 2000. Cloning and characterization of secretory tyrosine phosphatases of Mycobacterium tuberculosis . J Bacteriol 182: 5425\u20135432. http:\/\/dx.doi.org\/10.1128\/JB.182.19.5425-5432.2000 [PubMed]","DOI":"10.1128\/JB.182.19.5425-5432.2000"},{"key":"e_1_3_2_17_2","doi-asserted-by":"crossref","unstructured":"Bach H Papavinasasundaram KG Wong D Hmama Z Av-Gay Y. 2008. Mycobacterium tuberculosis virulence is mediated by PtpA dephosphorylation of human vacuolar protein sorting 33B. Cell Host Microbe 3: 316\u2013322. http:\/\/dx.doi.org\/10.1016\/j.chom.2008.03.008","DOI":"10.1016\/j.chom.2008.03.008"},{"key":"e_1_3_2_18_2","doi-asserted-by":"crossref","unstructured":"Bach H Ko HH Raizman EA Attarian R Cho B Biet F Enns R Bressler B. 2011. Immunogenicity of Mycobacterium avium subsp. paratuberculosis proteins in Crohn\u2019s disease patients. Scand J Gastroenterol 46: 30\u201339. http:\/\/dx.doi.org\/10.3109\/00365521.2010.513061","DOI":"10.3109\/00365521.2010.513061"},{"key":"e_1_3_2_19_2","doi-asserted-by":"crossref","unstructured":"Chow K Ng D Stokes R Johnson P. 1994. Protein tyrosine phosphorylation in Mycobacterium tuberculosis . FEMS Microbiol Lett 124: 203\u2013207. http:\/\/dx.doi.org\/10.1111\/j.1574-6968.1994.tb07285.x","DOI":"10.1111\/j.1574-6968.1994.tb07285.x"},{"key":"e_1_3_2_20_2","doi-asserted-by":"crossref","unstructured":"Bach H Wong D Av-Gay Y. 2009. Mycobacterium tuberculosis PtkA is a novel protein tyrosine kinase whose substrate is PtpA. Biochem J 420: 155\u2013162. http:\/\/dx.doi.org\/10.1042\/BJ20090478","DOI":"10.1042\/BJ20090478"},{"key":"e_1_3_2_21_2","doi-asserted-by":"crossref","unstructured":"Kusebauch U Ortega C Ollodart A Rogers RS Sherman DR Moritz RL Grundner C. 2014. Mycobacterium tuberculosis supports protein tyrosine phosphorylation. Proc Natl Acad Sci USA 111: 9265\u20139270. http:\/\/dx.doi.org\/10.1073\/pnas.1323894111","DOI":"10.1073\/pnas.1323894111"},{"key":"e_1_3_2_22_2","doi-asserted-by":"crossref","unstructured":"Chao KL Gorlatova NV Eisenstein E Herzberg O. 2014. Structural basis for the binding specificity of human Recepteur d\u2019Origine Nantais (RON) receptor tyrosine kinase to macrophage-stimulating protein. J Biol Chem 289: 29948\u201329960. http:\/\/dx.doi.org\/10.1074\/jbc.M114.594341","DOI":"10.1074\/jbc.M114.594341"},{"key":"e_1_3_2_23_2","doi-asserted-by":"crossref","unstructured":"Zhou P Wong D Li W Xie J Av-Gay Y. 2015. Phosphorylation of Mycobacterium tuberculosis protein tyrosine kinase A PtkA by Ser\/Thr protein kinases. Biochem Biophys Res Commun 467: 421\u2013426. http:\/\/dx.doi.org\/10.1016\/j.bbrc.2015.09.124 [PubMed]","DOI":"10.1016\/j.bbrc.2015.09.124"},{"key":"e_1_3_2_24_2","doi-asserted-by":"crossref","unstructured":"Prisic S Dankwa S Schwartz D Chou MF Locasale JW Kang CM Bemis G Church GM Steen H Husson RN. 2010. Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine\/threonine protein kinases. Proc Natl Acad Sci USA 107: 7521\u20137526. http:\/\/dx.doi.org\/10.1073\/pnas.0913482107","DOI":"10.1073\/pnas.0913482107"},{"key":"e_1_3_2_25_2","doi-asserted-by":"crossref","unstructured":"J\u00fcnger MA Aebersold R. 2014. Mass spectrometry-driven phosphoproteomics: patterning the systems biology mosaic. Wiley Interdiscip Rev Dev Biol 3: 83\u2013112. http:\/\/dx.doi.org\/10.1002\/wdev.121","DOI":"10.1002\/wdev.121"},{"key":"e_1_3_2_26_2","doi-asserted-by":"crossref","unstructured":"Sharma K Gupta M Pathak M Gupta N Koul A Sarangi S Baweja R Singh Y. 2006. Transcriptional control of the mycobacterial embCAB operon by PknH through a regulatory protein EmbR in vivo . J Bacteriol 188: 2936\u20132944. http:\/\/dx.doi.org\/10.1128\/JB.188.8.2936-2944.2006","DOI":"10.1128\/JB.188.8.2936-2944.2006"},{"key":"e_1_3_2_27_2","doi-asserted-by":"crossref","unstructured":"Cohen-Gonsaud M Barthe P Canova MJ Stagier-Simon C Kremer L Roumestand C Molle V. 2009. The Mycobacterium tuberculosis Ser\/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation. J Biol Chem 284: 19290\u201319300. http:\/\/dx.doi.org\/10.1074\/jbc.M109.019653 [PubMed]","DOI":"10.1074\/jbc.M109.019653"},{"key":"e_1_3_2_28_2","doi-asserted-by":"crossref","unstructured":"Chao JD Papavinasasundaram KG Zheng X Ch\u00e1vez-Steenbock A Wang X Lee GQ Av-Gay Y. 2010. Convergence of Ser\/Thr and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis . J Biol Chem 285: 29239\u201329246. http:\/\/dx.doi.org\/10.1074\/jbc.M110.132894 [PubMed]","DOI":"10.1074\/jbc.M110.132894"},{"key":"e_1_3_2_29_2","doi-asserted-by":"crossref","unstructured":"Baer CE Iavarone AT Alber T Sassetti CM. 2014. Biochemical and spatial coincidence in the provisional Ser\/Thr protein kinase interaction network of Mycobacterium tuberculosis . J Biol Chem 289: 20422\u201320433. http:\/\/dx.doi.org\/10.1074\/jbc.M114.559054","DOI":"10.1074\/jbc.M114.559054"},{"key":"e_1_3_2_30_2","doi-asserted-by":"crossref","unstructured":"Nagarajan SN Upadhyay S Chawla Y Khan S Naz S Subramanian J Gandotra S Nandicoori VK. 2015. Protein kinase A (PknA) of Mycobacterium tuberculosis is independently activated and is critical for growth in vitro and survival of the pathogen in the host. J Biol Chem 290: 9626\u20139645. http:\/\/dx.doi.org\/10.1074\/jbc.M114.611822","DOI":"10.1074\/jbc.M114.611822"},{"key":"e_1_3_2_31_2","doi-asserted-by":"crossref","unstructured":"Greenstein AE MacGurn JA Baer CE Falick AM Cox JS Alber T. 2007. M. tuberculosis Ser\/Thr protein kinase D phosphorylates an anti-anti-sigma factor homolog. PLoS Pathog 3: e49. http:\/\/dx.doi.org\/10.1371\/journal.ppat.0030049 [PubMed]","DOI":"10.1371\/journal.ppat.0030049"},{"key":"e_1_3_2_32_2","doi-asserted-by":"crossref","unstructured":"Hatzios SK Baer CE Rustad TR Siegrist MS Pang JM Ortega C Alber T Grundner C Sherman DR Bertozzi CR. 2013. Osmosensory signaling in Mycobacterium tuberculosis mediated by a eukaryotic-like Ser\/Thr protein kinase. Proc Natl Acad Sci USA 110: E5069\u2013E5077. http:\/\/dx.doi.org\/10.1073\/pnas.1321205110","DOI":"10.1073\/pnas.1321205110"},{"key":"e_1_3_2_33_2","doi-asserted-by":"crossref","unstructured":"Good MC Greenstein AE Young TA Ng HL Alber T. 2004. Sensor domain of the Mycobacterium tuberculosis receptor Ser\/Thr protein kinase PknD forms a highly symmetric beta propeller. J Mol Biol 339: 459\u2013469. http:\/\/dx.doi.org\/10.1016\/j.jmb.2004.03.063","DOI":"10.1016\/j.jmb.2004.03.063"},{"key":"e_1_3_2_34_2","doi-asserted-by":"crossref","unstructured":"Ortega C Liao R Anderson LN Rustad T Ollodart AR Wright AT Sherman DR Grundner C. 2014. Mycobacterium tuberculosis Ser\/Thr protein kinase B mediates an oxygen-dependent replication switch. PLoS Biol 12: e1001746. http:\/\/dx.doi.org\/10.1371\/journal.pbio.1001746","DOI":"10.1371\/journal.pbio.1001746"},{"key":"e_1_3_2_35_2","doi-asserted-by":"crossref","unstructured":"Armstrong JA Hart PD. 1971. Response of cultured macrophages to Mycobacterium tuberculosis with observations on fusion of lysosomes with phagosomes. J Exp Med 134: 713\u2013740. http:\/\/dx.doi.org\/10.1084\/jem.134.3.713","DOI":"10.1084\/jem.134.3.713"},{"key":"e_1_3_2_36_2","doi-asserted-by":"crossref","unstructured":"Sturgill-Koszycki S Schlesinger PH Chakraborty P Haddix PL Collins HL Fok AK Allen RD Gluck SL Heuser J Russell DG. 1994. Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase. Science 263: 678\u2013681. http:\/\/dx.doi.org\/10.1126\/science.8303277 [PubMed]","DOI":"10.1126\/science.8303277"},{"key":"e_1_3_2_37_2","doi-asserted-by":"crossref","unstructured":"Poirier V Bach H Av-Gay Y. 2014. Mycobacterium tuberculosis promotes anti-apoptotic activity of the macrophage by PtpA protein-dependent dephosphorylation of host GSK3\u03b1. J Biol Chem 289: 29376\u201329385. http:\/\/dx.doi.org\/10.1074\/jbc.M114.582502","DOI":"10.1074\/jbc.M114.582502"},{"key":"e_1_3_2_38_2","doi-asserted-by":"crossref","unstructured":"Wong D Bach H Sun J Hmama Z Av-Gay Y. 2011. Mycobacterium tuberculosis protein tyrosine phosphatase (PtpA) excludes host vacuolar-H+-ATPase to inhibit phagosome acidification. Proc Natl Acad Sci USA 108: 19371\u201319376. http:\/\/dx.doi.org\/10.1073\/pnas.1109201108","DOI":"10.1073\/pnas.1109201108"},{"key":"e_1_3_2_39_2","doi-asserted-by":"crossref","unstructured":"Wang J Li BX Ge PP Li J Wang Q Gao GF Qiu XB Liu CH. 2015. Mycobacterium tuberculosis suppresses innate immunity by coopting the host ubiquitin system. Nat Immunol 16: 237\u2013245. http:\/\/dx.doi.org\/10.1038\/ni.3096 [PubMed]","DOI":"10.1038\/ni.3096"},{"key":"e_1_3_2_40_2","doi-asserted-by":"crossref","unstructured":"Walburger A Koul A Ferrari G Nguyen L Prescianotto-Baschong C Huygen K Klebl B Thompson C Bacher G Pieters J. 2004. Protein kinase G from pathogenic mycobacteria promotes survival within macrophages. Science 304: 1800\u20131804. http:\/\/dx.doi.org\/10.1126\/science.1099384","DOI":"10.1126\/science.1099384"},{"key":"e_1_3_2_41_2","doi-asserted-by":"crossref","unstructured":"O\u2019Hare HM Dur\u00e1n R Cerve\u00f1ansky C Bellinzoni M Wehenkel AM Pritsch O Obal G Baumgartner J Vialaret J Johnsson K Alzari PM. 2008. Regulation of glutamate metabolism by protein kinases in mycobacteria. Mol Microbiol 70: 1408\u20131423. http:\/\/dx.doi.org\/10.1111\/j.1365-2958.2008.06489.x [PubMed]","DOI":"10.1111\/j.1365-2958.2008.06489.x"},{"key":"e_1_3_2_42_2","doi-asserted-by":"crossref","unstructured":"Cowley S Ko M Pick N Chow R Downing KJ Gordhan BG Betts JC Mizrahi V Smith DA Stokes RW Av-Gay Y. 2004. The Mycobacterium tuberculosis protein serine\/threonine kinase PknG is linked to cellular glutamate\/glutamine levels and is important for growth in vivo . Mol Microbiol 52: 1691\u20131702. http:\/\/dx.doi.org\/10.1111\/j.1365-2958.2004.04085.x","DOI":"10.1111\/j.1365-2958.2004.04085.x"},{"key":"e_1_3_2_43_2","doi-asserted-by":"crossref","unstructured":"Keane J Remold HG Kornfeld H. 2000. Virulent Mycobacterium tuberculosis strains evade apoptosis of infected alveolar macrophages. J Immunol 164: 2016\u20132020. http:\/\/dx.doi.org\/10.4049\/jimmunol.164.4.2016","DOI":"10.4049\/jimmunol.164.4.2016"},{"key":"e_1_3_2_44_2","unstructured":"Jayakumar D Jacobs WR Jr Narayanan S. 2008. Protein kinase E of Mycobacterium tuberculosis has a role in the nitric oxide stress response and apoptosis in a human macrophage model of infection. Cell Microbiol 10: 365\u2013374. [PubMed]"},{"key":"e_1_3_2_45_2","doi-asserted-by":"crossref","unstructured":"Papavinasasundaram KG Chan B Chung JH Colston MJ Davis EO Av-Gay Y. 2005. Deletion of the Mycobacterium tuberculosis pknH gene confers a higher bacillary load during the chronic phase of infection in BALB\/c mice. J Bacteriol 187: 5751\u20135760. http:\/\/dx.doi.org\/10.1128\/JB.187.16.5751-5760.2005","DOI":"10.1128\/JB.187.16.5751-5760.2005"},{"key":"e_1_3_2_46_2","doi-asserted-by":"crossref","unstructured":"Li CQ Wogan GN. 2005. Nitric oxide as a modulator of apoptosis. Cancer Lett 226: 1\u201315. http:\/\/dx.doi.org\/10.1016\/j.canlet.2004.10.021","DOI":"10.1016\/j.canlet.2004.10.021"},{"key":"e_1_3_2_47_2","doi-asserted-by":"crossref","unstructured":"Kumar D Narayanan S. 2012. pknE a serine\/threonine kinase of Mycobacterium tuberculosis modulates multiple apoptotic paradigms. Infect Genet Evol 12: 737\u2013747. http:\/\/dx.doi.org\/10.1016\/j.meegid.2011.09.008","DOI":"10.1016\/j.meegid.2011.09.008"},{"key":"e_1_3_2_48_2","doi-asserted-by":"crossref","unstructured":"Parandhaman DK Hanna LE Narayanan S. 2014. PknE a serine\/threonine protein kinase of Mycobacterium tuberculosis initiates survival crosstalk that also impacts HIV coinfection. PLoS One 9: e83541. http:\/\/dx.doi.org\/10.1371\/journal.pone.0083541","DOI":"10.1371\/journal.pone.0083541"},{"key":"e_1_3_2_49_2","doi-asserted-by":"crossref","unstructured":"Sequeira PC Senaratne RH Riley LW. 2014. Inhibition of toll-like receptor 2 (TLR-2)-mediated response in human alveolar epithelial cells by mycolic acids and Mycobacterium tuberculosis mce1 operon mutant. Pathog Dis 70: 132\u2013140. http:\/\/dx.doi.org\/10.1111\/2049-632X.12110","DOI":"10.1111\/2049-632X.12110"},{"key":"e_1_3_2_50_2","doi-asserted-by":"crossref","unstructured":"S\u00e1nchez D Rojas M Hern\u00e1ndez I Radzioch D Garc\u00eda LF Barrera LF. 2010. Role of TLR2- and TLR4-mediated signaling in Mycobacterium tuberculosis -induced macrophage death. Cell Immunol 260: 128\u2013136. http:\/\/dx.doi.org\/10.1016\/j.cellimm.2009.10.007","DOI":"10.1016\/j.cellimm.2009.10.007"},{"key":"e_1_3_2_51_2","doi-asserted-by":"crossref","unstructured":"Nuzzo I Galdiero M Bentivoglio C Galdiero R Romano Carratelli C. 2002. Apoptosis modulation by mycolic acid tuberculostearic acid and trehalose 6 6\u2032-dimycolate. J Infect 44: 229\u2013235. http:\/\/dx.doi.org\/10.1053\/jinf.2002.1001 [PubMed]","DOI":"10.1053\/jinf.2002.1001"},{"key":"e_1_3_2_52_2","doi-asserted-by":"crossref","unstructured":"Zhou P Li W Wong D Xie J Av-Gay Y. 2015. Phosphorylation control of protein tyrosine phosphatase A activity in Mycobacterium tuberculosis . FEBS Lett 589: 326\u2013331. http:\/\/dx.doi.org\/10.1016\/j.febslet.2014.12.015","DOI":"10.1016\/j.febslet.2014.12.015"},{"key":"e_1_3_2_53_2","doi-asserted-by":"crossref","unstructured":"Vishwanath V Meera R Narayanan PR Puvanakrishnan R. 1997. Fate of Mycobacterium tuberculosis inside rat peritoneal macrophages in vitro . Mol Cell Biochem 175: 169\u2013175. http:\/\/dx.doi.org\/10.1023\/A:1006848900722","DOI":"10.1023\/A:1006848900722"},{"key":"e_1_3_2_54_2","doi-asserted-by":"crossref","unstructured":"Sachdeva P Misra R Tyagi AK Singh Y. 2010. The sigma factors of Mycobacterium tuberculosis : regulation of the regulators. FEBS J 277: 605\u2013626. http:\/\/dx.doi.org\/10.1111\/j.1742-4658.2009.07479.x [PubMed]","DOI":"10.1111\/j.1742-4658.2009.07479.x"},{"key":"e_1_3_2_55_2","doi-asserted-by":"crossref","unstructured":"Song T Dove SL Lee KH Husson RN. 2003. RshA an anti-sigma factor that regulates the activity of the mycobacterial stress response sigma factor SigH. Mol Microbiol 50: 949\u2013959. http:\/\/dx.doi.org\/10.1046\/j.1365-2958.2003.03739.x","DOI":"10.1046\/j.1365-2958.2003.03739.x"},{"key":"e_1_3_2_56_2","doi-asserted-by":"crossref","unstructured":"Park ST Kang CM Husson RN. 2008. Regulation of the SigH stress response regulon by an essential protein kinase in Mycobacterium tuberculosis . Proc Natl Acad Sci USA 105: 13105\u201313110. http:\/\/dx.doi.org\/10.1073\/pnas.0801143105 [PubMed]","DOI":"10.1073\/pnas.0801143105"},{"key":"e_1_3_2_57_2","doi-asserted-by":"crossref","unstructured":"Anandan T Han J Baun H Nyayapathy S Brown JT Dial RL Moltalvo JA Kim MS Yang SH Ronning DR Husson RN Suh J Kang CM. 2014. Phosphorylation regulates mycobacterial proteasome. J Microbiol 52: 743\u2013754. http:\/\/dx.doi.org\/10.1007\/s12275-014-4416-2","DOI":"10.1007\/s12275-014-4416-2"},{"key":"e_1_3_2_58_2","doi-asserted-by":"crossref","unstructured":"Festa RA McAllister F Pearce MJ Mintseris J Burns KE Gygi SP Darwin KH. 2010. Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis . PLoS One 5: e8589. http:\/\/dx.doi.org\/10.1371\/journal.pone.0008589","DOI":"10.1371\/journal.pone.0008589"},{"key":"e_1_3_2_59_2","doi-asserted-by":"crossref","unstructured":"Darwin KH Ehrt S Gutierrez-Ramos JC Weich N Nathan CF. 2003. The proteasome of Mycobacterium tuberculosis is required for resistance to nitric oxide. Science 302: 1963\u20131966. http:\/\/dx.doi.org\/10.1126\/science.1091176","DOI":"10.1126\/science.1091176"},{"key":"e_1_3_2_60_2","doi-asserted-by":"crossref","unstructured":"Gandotra S Schnappinger D Monteleone M Hillen W Ehrt S. 2007. In vivo gene silencing identifies the Mycobacterium tuberculosis proteasome as essential for the bacteria to persist in mice. Nat Med 13: 1515\u20131520. http:\/\/dx.doi.org\/10.1038\/nm1683","DOI":"10.1038\/nm1683"},{"key":"e_1_3_2_61_2","doi-asserted-by":"crossref","unstructured":"MacMicking JD North RJ LaCourse R Mudgett JS Shah SK Nathan CF. 1997. Identification of nitric oxide synthase as a protective locus against tuberculosis. Proc Natl Acad Sci USA 94: 5243\u20135248. http:\/\/dx.doi.org\/10.1073\/pnas.94.10.5243","DOI":"10.1073\/pnas.94.10.5243"},{"key":"e_1_3_2_62_2","doi-asserted-by":"crossref","unstructured":"Miller CC Rawat M Johnson T Av-Gay Y. 2007. Innate protection of Mycobacterium smegmatis against the antimicrobial activity of nitric oxide is provided by mycothiol. Antimicrob Agents Chemother 51: 3364\u20133366. http:\/\/dx.doi.org\/10.1128\/AAC.00347-07","DOI":"10.1128\/AAC.00347-07"},{"key":"e_1_3_2_63_2","doi-asserted-by":"crossref","unstructured":"Davis AS Vergne I Master SS Kyei GB Chua J Deretic V. 2007. Mechanism of inducible nitric oxide synthase exclusion from mycobacterial phagosomes. PLoS Pathog 3: e186. http:\/\/dx.doi.org\/10.1371\/journal.ppat.0030186","DOI":"10.1371\/journal.ppat.0030186"},{"key":"e_1_3_2_64_2","doi-asserted-by":"crossref","unstructured":"Aldridge BB Fernandez-Suarez M Heller D Ambravaneswaran V Irimia D Toner M Fortune SM. 2012. Asymmetry and aging of mycobacterial cells lead to variable growth and antibiotic susceptibility. Science 335: 100\u2013104. http:\/\/dx.doi.org\/10.1126\/science.1216166","DOI":"10.1126\/science.1216166"},{"key":"e_1_3_2_65_2","doi-asserted-by":"crossref","unstructured":"Santi I Dhar N Bousbaine D Wakamoto Y McKinney JD. 2013. Single-cell dynamics of the chromosome replication and cell division cycles in mycobacteria. Nat Commun 4: 2470. [PubMed]","DOI":"10.1038\/ncomms3470"},{"key":"e_1_3_2_66_2","doi-asserted-by":"crossref","unstructured":"Kieser KJ Rubin EJ. 2014. How sisters grow apart: mycobacterial growth and division. Nat Rev Microbiol 12: 550\u2013562. http:\/\/dx.doi.org\/10.1038\/nrmicro3299 [PubMed]","DOI":"10.1038\/nrmicro3299"},{"key":"e_1_3_2_67_2","doi-asserted-by":"crossref","unstructured":"Kang CM Abbott DW Park ST Dascher CC Cantley LC Husson RN. 2005. The Mycobacterium tuberculosis serine\/threonine kinases PknA and PknB: substrate identification and regulation of cell shape. Genes Dev 19: 1692\u20131704. http:\/\/dx.doi.org\/10.1101\/gad.1311105","DOI":"10.1101\/gad.1311105"},{"key":"e_1_3_2_68_2","doi-asserted-by":"crossref","unstructured":"Parikh A Verma SK Khan S Prakash B Nandicoori VK. 2009. PknB-mediated phosphorylation of a novel substrate N -acetylglucosamine-1-phosphate uridyltransferase modulates its acetyltransferase activity. J Mol Biol 386: 451\u2013464. http:\/\/dx.doi.org\/10.1016\/j.jmb.2008.12.031","DOI":"10.1016\/j.jmb.2008.12.031"},{"key":"e_1_3_2_69_2","doi-asserted-by":"crossref","unstructured":"Gee CL Papavinasasundaram KG Blair SR Baer CE Falick AM King DS Griffin JE Venghatakrishnan H Zukauskas A Wei JR Dhiman RK Crick DC Rubin EJ Sassetti CM Alber T. 2012. A phosphorylated pseudokinase complex controls cell wall synthesis in mycobacteria. Sci Signal 5: ra7. http:\/\/dx.doi.org\/10.1126\/scisignal.2002525","DOI":"10.1126\/scisignal.2002525"},{"key":"e_1_3_2_70_2","doi-asserted-by":"crossref","unstructured":"Mahapatra S Yagi T Belisle JT Espinosa BJ Hill PJ McNeil MR Brennan PJ Crick DC. 2005. Mycobacterial lipid II is composed of a complex mixture of modified muramyl and peptide moieties linked to decaprenyl phosphate. J Bacteriol 187: 2747\u20132757. http:\/\/dx.doi.org\/10.1128\/JB.187.8.2747-2757.2005 [PubMed]","DOI":"10.1128\/JB.187.8.2747-2757.2005"},{"key":"e_1_3_2_71_2","doi-asserted-by":"crossref","unstructured":"Davis KM Weiser JN. 2011. Modifications to the peptidoglycan backbone help bacteria to establish infection. Infect Immun 79: 562\u2013570. http:\/\/dx.doi.org\/10.1128\/IAI.00651-10 [PubMed]","DOI":"10.1128\/IAI.00651-10"},{"key":"e_1_3_2_72_2","doi-asserted-by":"crossref","unstructured":"Hansen JM Golchin SA Veyrier FJ Domenech P Boneca IG Azad AK Rajaram MV Schlesinger LS Divangahi M Reed MB Behr MA. 2014. N -glycolylated peptidoglycan contributes to the immunogenicity but not pathogenicity of Mycobacterium tuberculosis . J Infect Dis 209: 1045\u20131054. http:\/\/dx.doi.org\/10.1093\/infdis\/jit622","DOI":"10.1093\/infdis\/jit622"},{"key":"e_1_3_2_73_2","doi-asserted-by":"crossref","unstructured":"Coulombe F Divangahi M Veyrier F de L\u00e9s\u00e9leuc L Gleason JL Yang Y Kelliher MA Pandey AK Sassetti CM Reed MB Behr MA. 2009. Increased NOD2-mediated recognition of N -glycolyl muramyl dipeptide. J Exp Med 206: 1709\u20131716. http:\/\/dx.doi.org\/10.1084\/jem.20081779 [PubMed]","DOI":"10.1084\/jem.20081779"},{"key":"e_1_3_2_74_2","doi-asserted-by":"crossref","unstructured":"Munshi T Gupta A Evangelopoulos D Guzman JD Gibbons S Keep NH Bhakta S. 2013. Characterisation of ATP-dependent Mur ligases involved in the biogenesis of cell wall peptidoglycan in Mycobacterium tuberculosis . PLoS One 8: e60143. http:\/\/dx.doi.org\/10.1371\/journal.pone.0060143","DOI":"10.1371\/journal.pone.0060143"},{"key":"e_1_3_2_75_2","doi-asserted-by":"crossref","unstructured":"Thakur M Chakraborti PK. 2008. Ability of PknA a mycobacterial eukaryotic-type serine\/threonine kinase to transphosphorylate MurD a ligase involved in the process of peptidoglycan biosynthesis. Biochem J 415: 27\u201333. http:\/\/dx.doi.org\/10.1042\/BJ20080234","DOI":"10.1042\/BJ20080234"},{"key":"e_1_3_2_76_2","doi-asserted-by":"crossref","unstructured":"Kumar P Arora K Lloyd JR Lee IY Nair V Fischer E Boshoff HI Barry CE III. 2012. Meropenem inhibits D D-carboxypeptidase activity in Mycobacterium tuberculosis . Mol Microbiol 86: 367\u2013381. http:\/\/dx.doi.org\/10.1111\/j.1365-2958.2012.08199.x [PubMed]","DOI":"10.1111\/j.1365-2958.2012.08199.x"},{"key":"e_1_3_2_77_2","doi-asserted-by":"crossref","unstructured":"Lavollay M Arthur M Fourgeaud M Dubost L Marie A Veziris N Blanot D Gutmann L Mainardi JL. 2008. The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L D-transpeptidation. J Bacteriol 190: 4360\u20134366. http:\/\/dx.doi.org\/10.1128\/JB.00239-08","DOI":"10.1128\/JB.00239-08"},{"key":"e_1_3_2_78_2","doi-asserted-by":"crossref","unstructured":"Gupta R Lavollay M Mainardi JL Arthur M Bishai WR Lamichhane G. 2010. The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin. Nat Med 16: 466\u2013469. http:\/\/dx.doi.org\/10.1038\/nm.2120","DOI":"10.1038\/nm.2120"},{"key":"e_1_3_2_79_2","doi-asserted-by":"crossref","unstructured":"Zheng X Papavinasasundaram KG Av-Gay Y. 2007. Novel substrates of Mycobacterium tuberculosis PknH Ser\/Thr kinase. Biochem Biophys Res Commun 355: 162\u2013168. http:\/\/dx.doi.org\/10.1016\/j.bbrc.2007.01.122","DOI":"10.1016\/j.bbrc.2007.01.122"},{"key":"e_1_3_2_80_2","doi-asserted-by":"crossref","unstructured":"Kieser KJ Boutte CC Kester JC Baer CE Barczak AK Meniche X Chao MC Rego EH Sassetti CM Fortune SM Rubin EJ. 2015. Phosphorylation of the peptidoglycan synthase PonA1 governs the rate of polar elongation in mycobacteria. PLoS Pathog 11: e1005010. http:\/\/dx.doi.org\/10.1371\/journal.ppat.1005010","DOI":"10.1371\/journal.ppat.1005010"},{"key":"e_1_3_2_81_2","doi-asserted-by":"crossref","unstructured":"Meniche X Otten R Siegrist MS Baer CE Murphy KC Bertozzi CR Sassetti CM. 2014. Subpolar addition of new cell wall is directed by DivIVA in mycobacteria. Proc Natl Acad Sci USA 111: E3243\u2013E3251. http:\/\/dx.doi.org\/10.1073\/pnas.1402158111 [PubMed]","DOI":"10.1073\/pnas.1402158111"},{"key":"e_1_3_2_82_2","doi-asserted-by":"crossref","unstructured":"Joyce G Williams KJ Robb M Noens E Tizzano B Shahrezaei V Robertson BD. 2012. Cell division site placement and asymmetric growth in mycobacteria. PLoS One 7: e44582. http:\/\/dx.doi.org\/10.1371\/journal.pone.0044582 [PubMed][CrossRef]","DOI":"10.1371\/journal.pone.0044582"},{"key":"e_1_3_2_83_2","doi-asserted-by":"crossref","unstructured":"Singh B Nitharwal RG Ramesh M Pettersson BM Kirsebom LA Dasgupta S. 2013. Asymmetric growth and division in Mycobacterium spp.: compensatory mechanisms for non-medial septa. Mol Microbiol 88: 64\u201376. http:\/\/dx.doi.org\/10.1111\/mmi.12169 [PubMed]","DOI":"10.1111\/mmi.12169"},{"key":"e_1_3_2_84_2","doi-asserted-by":"crossref","unstructured":"Kysela DT Brown PJ Huang KC Brun YV. 2013. Biological consequences and advantages of asymmetric bacterial growth. Annu Rev Microbiol 67: 417\u2013435. http:\/\/dx.doi.org\/10.1146\/annurev-micro-092412-155622","DOI":"10.1146\/annurev-micro-092412-155622"},{"key":"e_1_3_2_85_2","doi-asserted-by":"crossref","unstructured":"Adams DW Errington J. 2009. Bacterial cell division: assembly maintenance and disassembly of the Z ring. Nat Rev Microbiol 7: 642\u2013653. http:\/\/dx.doi.org\/10.1038\/nrmicro2198 [PubMed]","DOI":"10.1038\/nrmicro2198"},{"key":"e_1_3_2_86_2","doi-asserted-by":"crossref","unstructured":"Thakur M Chakraborti PK. 2006. GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser\/Thr kinase PknA. J Biol Chem 281: 40107\u201340113. http:\/\/dx.doi.org\/10.1074\/jbc.M607216200 [PubMed]","DOI":"10.1074\/jbc.M607216200"},{"key":"e_1_3_2_87_2","doi-asserted-by":"crossref","unstructured":"Typas A Banzhaf M Gross CA Vollmer W. 2011. From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat Rev Microbiol 10: 123\u2013136. [PubMed]","DOI":"10.1038\/nrmicro2677"},{"key":"e_1_3_2_88_2","doi-asserted-by":"crossref","unstructured":"Dasgupta A Datta P Kundu M Basu J. 2006. The serine\/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA a penicillin-binding protein required for cell division. Microbiology 152: 493\u2013504. [Retraction doi:10.1099\/mic.0.000110.] http:\/\/dx.doi.org\/10.1099\/mic.0.28630-0","DOI":"10.1099\/mic.0.28630-0"},{"key":"e_1_3_2_89_2","doi-asserted-by":"crossref","unstructured":"Chawla Y Upadhyay S Khan S Nagarajan SN Forti F Nandicoori VK. 2014. Protein kinase B (PknB) of Mycobacterium tuberculosis is essential for growth of the pathogen in vitro as well as for survival within the host. J Biol Chem 289: 13858\u201313875. http:\/\/dx.doi.org\/10.1074\/jbc.M114.563536 [PubMed]","DOI":"10.1074\/jbc.M114.563536"},{"key":"e_1_3_2_90_2","doi-asserted-by":"crossref","unstructured":"Rachman H Strong M Ulrichs T Grode L Schuchhardt J Mollenkopf H Kosmiadi GA Eisenberg D Kaufmann SH. 2006. Unique transcriptome signature of Mycobacterium tuberculosis in pulmonary tuberculosis. Infect Immun 74: 1233\u20131242. http:\/\/dx.doi.org\/10.1128\/IAI.74.2.1233-1242.2006","DOI":"10.1128\/IAI.74.2.1233-1242.2006"},{"key":"e_1_3_2_91_2","doi-asserted-by":"crossref","unstructured":"Griffin JE Pandey AK Gilmore SA Mizrahi V McKinney JD Bertozzi CR Sassetti CM. 2012. Cholesterol catabolism by Mycobacterium tuberculosis requires transcriptional and metabolic adaptations. Chem Biol 19: 218\u2013227. http:\/\/dx.doi.org\/10.1016\/j.chembiol.2011.12.016","DOI":"10.1016\/j.chembiol.2011.12.016"},{"key":"e_1_3_2_92_2","doi-asserted-by":"crossref","unstructured":"Dubnau E Chan J Raynaud C Mohan VP Lan\u00e9elle MA Yu K Qu\u00e9mard A Smith I Daff\u00e9 M. 2000. Oxygenated mycolic acids are necessary for virulence of Mycobacterium tuberculosis in mice. Mol Microbiol 36: 630\u2013637. http:\/\/dx.doi.org\/10.1046\/j.1365-2958.2000.01882.x","DOI":"10.1046\/j.1365-2958.2000.01882.x"},{"key":"e_1_3_2_93_2","doi-asserted-by":"crossref","unstructured":"Vander Beken S Al Dulayymi JR Naessens T Koza G Maza-Iglesias M Rowles R Theunissen C De Medts J Lanckacker E Baird MS Grooten J. 2011. Molecular structure of the Mycobacterium tuberculosis virulence factor mycolic acid determines the elicited inflammatory pattern. Eur J Immunol 41: 450\u2013460. http:\/\/dx.doi.org\/10.1002\/eji.201040719","DOI":"10.1002\/eji.201040719"},{"key":"e_1_3_2_94_2","doi-asserted-by":"crossref","unstructured":"Jain M Petzold CJ Schelle MW Leavell MD Mougous JD Bertozzi CR Leary JA Cox JS. 2007. Lipidomics reveals control of Mycobacterium tuberculosis virulence lipids via metabolic coupling. Proc Natl Acad Sci USA 104: 5133\u20135138. http:\/\/dx.doi.org\/10.1073\/pnas.0610634104","DOI":"10.1073\/pnas.0610634104"},{"key":"e_1_3_2_95_2","doi-asserted-by":"crossref","unstructured":"Bhamidi S Shi L Chatterjee D Belisle JT Crick DC McNeil MR. 2012. A bioanalytical method to determine the cell wall composition of Mycobacterium tuberculosis grown in vivo . Anal Biochem 421: 240\u2013249. http:\/\/dx.doi.org\/10.1016\/j.ab.2011.10.046","DOI":"10.1016\/j.ab.2011.10.046"},{"key":"e_1_3_2_96_2","doi-asserted-by":"crossref","unstructured":"Barry CE III Lee RE Mdluli K Sampson AE Schroeder BG Slayden RA Yuan Y. 1998. Mycolic acids: structure biosynthesis and physiological functions. Prog Lipid Res 37: 143\u2013179. http:\/\/dx.doi.org\/10.1016\/S0163-7827(98)00008-3","DOI":"10.1016\/S0163-7827(98)00008-3"},{"key":"e_1_3_2_97_2","doi-asserted-by":"crossref","unstructured":"Veyron-Churlet R Zanella-Cl\u00e9on I Cohen-Gonsaud M Molle V Kremer L. 2010. Phosphorylation of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein reductase MabA regulates mycolic acid biosynthesis. J Biol Chem 285: 12714\u201312725. http:\/\/dx.doi.org\/10.1074\/jbc.M110.105189","DOI":"10.1074\/jbc.M110.105189"},{"key":"e_1_3_2_98_2","doi-asserted-by":"crossref","unstructured":"Molle V Gulten G Vilch\u00e8ze C Veyron-Churlet R Zanella-Cl\u00e9on I Sacchettini JC Jacobs WR Jr Kremer L. 2010. Phosphorylation of InhA inhibits mycolic acid biosynthesis and growth of Mycobacterium tuberculosis . Mol Microbiol 78: 1591\u20131605. http:\/\/dx.doi.org\/10.1111\/j.1365-2958.2010.07446.x","DOI":"10.1111\/j.1365-2958.2010.07446.x"},{"key":"e_1_3_2_99_2","doi-asserted-by":"crossref","unstructured":"Khan S Nagarajan SN Parikh A Samantaray S Singh A Kumar D Roy RP Bhatt A Nandicoori VK. 2010. Phosphorylation of enoyl-acyl carrier protein reductase InhA impacts mycobacterial growth and survival. J Biol Chem 285: 37860\u201337871. http:\/\/dx.doi.org\/10.1074\/jbc.M110.143131","DOI":"10.1074\/jbc.M110.143131"},{"key":"e_1_3_2_100_2","doi-asserted-by":"crossref","unstructured":"Slama N Leiba J Eynard N Daff\u00e9 M Kremer L Qu\u00e9mard A Molle V. 2011. Negative regulation by Ser\/Thr phosphorylation of HadAB and HadBC dehydratases from Mycobacterium tuberculosis type II fatty acid synthase system. Biochem Biophys Res Commun 412: 401\u2013406. http:\/\/dx.doi.org\/10.1016\/j.bbrc.2011.07.051 [PubMed]","DOI":"10.1016\/j.bbrc.2011.07.051"},{"key":"e_1_3_2_101_2","doi-asserted-by":"crossref","unstructured":"Vilch\u00e8ze C Molle V Carr\u00e8re-Kremer S Leiba J Mourey L Shenai S Baronian G Tufariello J Hartman T Veyron-Churlet R Trivelli X Tiwari S Weinrick B Alland D Gu\u00e9rardel Y Jacobs WR Jr Kremer L. 2014. Phosphorylation of KasB regulates virulence and acid-fastness in Mycobacterium tuberculosis . PLoS Pathog 10: e1004115. http:\/\/dx.doi.org\/10.1371\/journal.ppat.1004115","DOI":"10.1371\/journal.ppat.1004115"},{"key":"e_1_3_2_102_2","doi-asserted-by":"crossref","unstructured":"Molle V Brown AK Besra GS Cozzone AJ Kremer L. 2006. The condensing activities of the Mycobacterium tuberculosis type II fatty acid synthase are differentially regulated by phosphorylation. J Biol Chem 281: 30094\u201330103. http:\/\/dx.doi.org\/10.1074\/jbc.M601691200","DOI":"10.1074\/jbc.M601691200"},{"key":"e_1_3_2_103_2","doi-asserted-by":"crossref","unstructured":"Veyron-Churlet R Molle V Taylor RC Brown AK Besra GS Zanella-Cl\u00e9on I F\u00fctterer K Kremer L. 2009. The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue. J Biol Chem 284: 6414\u20136424. http:\/\/dx.doi.org\/10.1074\/jbc.M806537200","DOI":"10.1074\/jbc.M806537200"},{"key":"e_1_3_2_104_2","doi-asserted-by":"crossref","unstructured":"Bhatt A Fujiwara N Bhatt K Gurcha SS Kremer L Chen B Chan J Porcelli SA Kobayashi K Besra GS Jacobs WR Jr. 2007. Deletion of kasB in Mycobacterium tuberculosis causes loss of acid-fastness and subclinical latent tuberculosis in immunocompetent mice. Proc Natl Acad Sci USA 104: 5157\u20135162. http:\/\/dx.doi.org\/10.1073\/pnas.0608654104","DOI":"10.1073\/pnas.0608654104"},{"key":"e_1_3_2_105_2","doi-asserted-by":"crossref","unstructured":"Gao LY Laval F Lawson EH Groger RK Woodruff A Morisaki JH Cox JS Daffe M Brown EJ. 2003. Requirement for kasB in i mycolic acid biosynthesis cell wall impermeability and intracellular survival: implications for therapy. Mol Microbiol 49: 1547\u20131563. http:\/\/dx.doi.org\/10.1046\/j.1365-2958.2003.03667.x","DOI":"10.1046\/j.1365-2958.2003.03667.x"},{"key":"e_1_3_2_106_2","doi-asserted-by":"crossref","unstructured":"Wilson M DeRisi J Kristensen HH Imboden P Rane S Brown PO Schoolnik GK. 1999. Exploring drug-induced alterations in gene expression in Mycobacterium tuberculosis by microarray hybridization. Proc Natl Acad Sci USA 96: 12833\u201312838. http:\/\/dx.doi.org\/10.1073\/pnas.96.22.12833","DOI":"10.1073\/pnas.96.22.12833"},{"key":"e_1_3_2_107_2","doi-asserted-by":"crossref","unstructured":"Voskuil MI. 2013. Mycobacterium tuberculosis cholesterol catabolism requires a new class of acyl coenzyme A dehydrogenase. J Bacteriol 195: 4319\u20134321. http:\/\/dx.doi.org\/10.1128\/JB.00867-13","DOI":"10.1128\/JB.00867-13"},{"key":"e_1_3_2_108_2","doi-asserted-by":"crossref","unstructured":"Rienksma RA Suarez-Diez M Mollenkopf HJ Dolganov GM Dorhoi A Schoolnik GK Martins Dos Santos VA Kaufmann SH Schaap PJ Gengenbacher M. 2015. Comprehensive insights into transcriptional adaptation of intracellular mycobacteria by microbe-enriched dual RNA sequencing. BMC Genomics 16: 34. http:\/\/dx.doi.org\/10.1186\/s12864-014-1197-2","DOI":"10.1186\/s12864-014-1197-2"},{"key":"e_1_3_2_109_2","doi-asserted-by":"crossref","unstructured":"Asselineau C Asselineau J Lan\u00e9elle G Lan\u00e9elle MA. 2002. The biosynthesis of mycolic acids by mycobacteria: current and alternative hypotheses. Prog Lipid Res 41: 501\u2013523. http:\/\/dx.doi.org\/10.1016\/S0163-7827(02)00008-5 [PubMed]","DOI":"10.1016\/S0163-7827(02)00008-5"},{"key":"e_1_3_2_110_2","doi-asserted-by":"crossref","unstructured":"Singh A Gupta R Vishwakarma RA Narayanan PR Paramasivan CN Ramanathan VD Tyagi AK. 2005. Requirement of the mymA operon for appropriate cell wall ultrastructure and persistence of Mycobacterium tuberculosis in the spleens of guinea pigs. J Bacteriol 187: 4173\u20134186. http:\/\/dx.doi.org\/10.1128\/JB.187.12.4173-4186.2005","DOI":"10.1128\/JB.187.12.4173-4186.2005"},{"key":"e_1_3_2_111_2","doi-asserted-by":"crossref","unstructured":"Singh A Jain S Gupta S Das T Tyagi AK. 2003. mymA operon of Mycobacterium tuberculosis : its regulation and importance in the cell envelope. FEMS Microbiol Lett 227: 53\u201363. http:\/\/dx.doi.org\/10.1016\/S0378-1097(03)00648-7 [PubMed]","DOI":"10.1016\/S0378-1097(03)00648-7"},{"key":"e_1_3_2_112_2","doi-asserted-by":"crossref","unstructured":"Rousseau C Winter N Pivert E Bordat Y Neyrolles O Av\u00e9 P Huerre M Gicquel B Jackson M. 2004. Production of phthiocerol dimycocerosates protects Mycobacterium tuberculosis from the cidal activity of reactive nitrogen intermediates produced by macrophages and modulates the early immune response to infection. Cell Microbiol 6: 277\u2013287. http:\/\/dx.doi.org\/10.1046\/j.1462-5822.2004.00368.x","DOI":"10.1046\/j.1462-5822.2004.00368.x"},{"key":"e_1_3_2_113_2","doi-asserted-by":"crossref","unstructured":"Sharma K Chandra H Gupta PK Pathak M Narayan A Meena LS D\u2019Souza RC Chopra P Ramachandran S Singh Y. 2004. PknH a transmembrane Hank\u2019s type serine\/threonine kinase from Mycobacterium tuberculosis is differentially expressed under stress conditions. FEMS Microbiol Lett 233: 107\u2013113. http:\/\/dx.doi.org\/10.1016\/j.femsle.2004.01.045","DOI":"10.1016\/j.femsle.2004.01.045"},{"key":"e_1_3_2_114_2","doi-asserted-by":"crossref","unstructured":"G\u00f3mez-Velasco A Bach H Rana AK Cox LR Bhatt A Besra GS Av-Gay Y. 2013. Disruption of the serine\/threonine protein kinase H affects phthiocerol dimycocerosates synthesis in Mycobacterium tuberculosis . Microbiology 159: 726\u2013736. http:\/\/dx.doi.org\/10.1099\/mic.0.062067-0","DOI":"10.1099\/mic.0.062067-0"},{"key":"e_1_3_2_115_2","doi-asserted-by":"crossref","unstructured":"P\u00e9rez J Garcia R Bach H de Waard JH Jacobs WR Jr Av-Gay Y Bubis J Takiff HE. 2006. Mycobacterium tuberculosis transporter MmpL7 is a potential substrate for kinase PknD. Biochem Biophys Res Commun 348: 6\u201312. http:\/\/dx.doi.org\/10.1016\/j.bbrc.2006.06.164","DOI":"10.1016\/j.bbrc.2006.06.164"},{"key":"e_1_3_2_116_2","doi-asserted-by":"crossref","unstructured":"Touchette MH Bommineni GR Delle Bovi RJ Gadbery JE Nicora CD Shukla AK Kyle JE Metz TO Martin DW Sampson NS Miller WT Tonge PJ Seeliger JC. 2015. Diacyltransferase activity and chain length specificity of Mycobacterium tuberculosis PapA5 in the synthesis of alkyl \u03b2-diol lipids. Biochemistry 54: 5457\u20135468. http:\/\/dx.doi.org\/10.1021\/acs.biochem.5b00455","DOI":"10.1021\/acs.biochem.5b00455"},{"key":"e_1_3_2_117_2","doi-asserted-by":"crossref","unstructured":"Gupta M Sajid A Arora G Tandon V Singh Y. 2009. Forkhead-associated domain-containing protein Rv0019c and polyketide-associated protein PapA5 from substrates of serine\/threonine protein kinase PknB to interacting proteins of Mycobacterium tuberculosis . J Biol Chem 284: 34723\u201334734. http:\/\/dx.doi.org\/10.1074\/jbc.M109.058834","DOI":"10.1074\/jbc.M109.058834"},{"key":"e_1_3_2_118_2","doi-asserted-by":"crossref","unstructured":"Gilmore SA Schelle MW Holsclaw CM Leigh CD Jain M Cox JS Leary JA Bertozzi CR. 2012. Sulfolipid-1 biosynthesis restricts Mycobacterium tuberculosis growth in human macrophages. ACS Chem Biol 7: 863\u2013870. http:\/\/dx.doi.org\/10.1021\/cb200311s","DOI":"10.1021\/cb200311s"},{"key":"e_1_3_2_119_2","doi-asserted-by":"crossref","unstructured":"Gengenbacher M Kaufmann SH. 2012. Mycobacterium tuberculosis : success through dormancy. FEMS Microbiol Rev 36: 514\u2013532. http:\/\/dx.doi.org\/10.1111\/j.1574-6976.2012.00331.x [PubMed]","DOI":"10.1111\/j.1574-6976.2012.00331.x"},{"key":"e_1_3_2_120_2","unstructured":"Canetti G. 1955. The tubercle bacillus in the pulmonary lesion of man p 111\u2013126. In Dubos RJ McDermott W (ed) Growth of the Tubercle Bacillus in the Tuberculosis Lesion . Springer New York NY."},{"key":"e_1_3_2_121_2","doi-asserted-by":"crossref","unstructured":"Voskuil MI Schnappinger D Visconti KC Harrell MI Dolganov GM Sherman DR Schoolnik GK. 2003. Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program. J Exp Med 198: 705\u2013713. http:\/\/dx.doi.org\/10.1084\/jem.20030205","DOI":"10.1084\/jem.20030205"},{"key":"e_1_3_2_122_2","doi-asserted-by":"crossref","unstructured":"Saini DK Malhotra V Tyagi JS. 2004. Cross talk between DevS sensor kinase homologue Rv2027c and DevR response regulator of Mycobacterium tuberculosis . FEBS Lett 565: 75\u201380. http:\/\/dx.doi.org\/10.1016\/j.febslet.2004.02.092 [PubMed]","DOI":"10.1016\/j.febslet.2004.02.092"},{"key":"e_1_3_2_123_2","doi-asserted-by":"crossref","unstructured":"Kumar A Toledo JC Patel RP Lancaster JR Jr Steyn AJ. 2007. Mycobacterium tuberculosis DosS is a redox sensor and DosT is a hypoxia sensor. Proc Natl Acad Sci USA 104: 11568\u201311573. http:\/\/dx.doi.org\/10.1073\/pnas.0705054104 [PubMed]","DOI":"10.1073\/pnas.0705054104"},{"key":"e_1_3_2_124_2","doi-asserted-by":"crossref","unstructured":"Sherman DR Voskuil M Schnappinger D Liao R Harrell MI Schoolnik GK. 2001. Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha-crystallin. Proc Natl Acad Sci USA 98: 7534\u20137539. [Erratum doi:10.1073\/pnas.98.26.15393-e.] http:\/\/dx.doi.org\/10.1073\/pnas.121172498","DOI":"10.1073\/pnas.121172498"},{"key":"e_1_3_2_125_2","doi-asserted-by":"crossref","unstructured":"Park HD Guinn KM Harrell MI Liao R Voskuil MI Tompa M Schoolnik GK Sherman DR. 2003. Rv3133c\/dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis . Mol Microbiol 48: 833\u2013843. http:\/\/dx.doi.org\/10.1046\/j.1365-2958.2003.03474.x","DOI":"10.1046\/j.1365-2958.2003.03474.x"},{"key":"e_1_3_2_126_2","doi-asserted-by":"crossref","unstructured":"Rosenkrands I Slayden RA Crawford J Aagaard C Barry CE III Andersen P. 2002. Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins. J Bacteriol 184: 3485\u20133491. http:\/\/dx.doi.org\/10.1128\/JB.184.13.3485-3491.2002","DOI":"10.1128\/JB.184.13.3485-3491.2002"},{"key":"e_1_3_2_127_2","doi-asserted-by":"crossref","unstructured":"Kumar A Deshane JS Crossman DK Bolisetty S Yan BS Kramnik I Agarwal A Steyn AJ. 2008. Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium tuberculosis dormancy regulon. J Biol Chem 283: 18032\u201318039. http:\/\/dx.doi.org\/10.1074\/jbc.M802274200","DOI":"10.1074\/jbc.M802274200"},{"key":"e_1_3_2_128_2","doi-asserted-by":"crossref","unstructured":"Shiloh MU Manzanillo P Cox JS. 2008. Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection. Cell Host Microbe 3: 323\u2013330. http:\/\/dx.doi.org\/10.1016\/j.chom.2008.03.007","DOI":"10.1016\/j.chom.2008.03.007"},{"key":"e_1_3_2_129_2","doi-asserted-by":"crossref","unstructured":"Betts JC Lukey PT Robb LC McAdam RA Duncan K. 2002. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Mol Microbiol 43: 717\u2013731. http:\/\/dx.doi.org\/10.1046\/j.1365-2958.2002.02779.x","DOI":"10.1046\/j.1365-2958.2002.02779.x"},{"key":"e_1_3_2_130_2","doi-asserted-by":"crossref","unstructured":"Bacon J Alderwick LJ Allnutt JA Gabasova E Watson R Hatch KA Clark SO Jeeves RE Marriott A Rayner E Tolley H Pearson G Hall G Besra GS Wernisch L Williams A Marsh PD. 2014. Non-replicating Mycobacterium tuberculosis elicits a reduced infectivity profile with corresponding modifications to the cell wall and extracellular matrix. PLoS One 9: e87329. http:\/\/dx.doi.org\/10.1371\/journal.pone.0087329","DOI":"10.1371\/journal.pone.0087329"},{"key":"e_1_3_2_131_2","doi-asserted-by":"crossref","unstructured":"Nyka W. 1974. Studies on the effect of starvation on mycobacteria. Infect Immun 9: 843\u2013850. [PubMed]","DOI":"10.1128\/iai.9.5.843-850.1974"},{"key":"e_1_3_2_132_2","doi-asserted-by":"crossref","unstructured":"Loebel RO Shorr E Richardson HB. 1933. The influence of adverse conditions upon the respiratory metabolism and growth of human tubercle bacilli. J Bacteriol 26: 167\u2013200. [PubMed]","DOI":"10.1128\/jb.26.2.167-200.1933"},{"key":"e_1_3_2_133_2","doi-asserted-by":"crossref","unstructured":"Richard-Greenblatt M Bach H Adamson J Pe\u00f1a-Diaz S Li W Steyn AJ Av-Gay Y. 2015. Regulation of ergothioneine biosynthesis and its effect on Mycobacterium tuberculosis growth and infectivity. J Biol Chem 290: 23064\u201323076. http:\/\/dx.doi.org\/10.1074\/jbc.M115.648642","DOI":"10.1074\/jbc.M115.648642"},{"key":"e_1_3_2_134_2","doi-asserted-by":"crossref","unstructured":"Malhotra V Arteaga-Cort\u00e9s LT Clay G Clark-Curtiss JE. 2010. Mycobacterium tuberculosis protein kinase K confers survival advantage during early infection in mice and regulates growth in culture and during persistent infection: implications for immune modulation. Microbiology 156: 2829\u20132841. http:\/\/dx.doi.org\/10.1099\/mic.0.040675-0","DOI":"10.1099\/mic.0.040675-0"},{"key":"e_1_3_2_135_2","doi-asserted-by":"crossref","unstructured":"Malhotra V Okon BP Clark-Curtiss JE. 2012. Mycobacterium tuberculosis protein kinase K enables growth adaptation through translation control. J Bacteriol 194: 4184\u20134196. http:\/\/dx.doi.org\/10.1128\/JB.00585-12","DOI":"10.1128\/JB.00585-12"},{"key":"e_1_3_2_136_2","doi-asserted-by":"crossref","unstructured":"Gopalaswamy R Narayanan S Chen B Jacobs WR Av-Gay Y. 2009. The serine\/threonine protein kinase PknI controls the growth of Mycobacterium tuberculosis upon infection. FEMS Microbiol Lett 295: 23\u201329. http:\/\/dx.doi.org\/10.1111\/j.1574-6968.2009.01570.x [PubMed]","DOI":"10.1111\/j.1574-6968.2009.01570.x"},{"key":"e_1_3_2_137_2","doi-asserted-by":"crossref","unstructured":"Singh A Singh Y Pine R Shi L Chandra R Drlica K. 2006. Protein kinase I of Mycobacterium tuberculosis : cellular localization and expression during infection of macrophage-like cells. Tuberculosis (Edinb) 86: 28\u201333. http:\/\/dx.doi.org\/10.1016\/j.tube.2005.04.002","DOI":"10.1016\/j.tube.2005.04.002"},{"key":"e_1_3_2_138_2","doi-asserted-by":"crossref","unstructured":"Rittershaus ES Baek SH Sassetti CM. 2013. The normalcy of dormancy: common themes in microbial quiescence. Cell Host Microbe 13: 643\u2013651. http:\/\/dx.doi.org\/10.1016\/j.chom.2013.05.012 [PubMed]","DOI":"10.1016\/j.chom.2013.05.012"},{"key":"e_1_3_2_139_2","doi-asserted-by":"crossref","unstructured":"Cunningham AF Spreadbury CL. 1998. Mycobacterial stationary phase induced by low oxygen tension: cell wall thickening and localization of the 16-kilodalton alpha-crystallin homolog. J Bacteriol 180: 801\u2013808. [PubMed]","DOI":"10.1128\/JB.180.4.801-808.1998"},{"key":"e_1_3_2_140_2","doi-asserted-by":"crossref","unstructured":"Ortalo-Magn\u00e9 A Dupont MA Lemassu A Andersen AB Gounon P Daff\u00e9 M. 1995. Molecular composition of the outermost capsular material of the tubercle bacillus. Microbiology 141: 1609\u20131620. http:\/\/dx.doi.org\/10.1099\/13500872-141-7-1609 [PubMed]","DOI":"10.1099\/13500872-141-7-1609"},{"key":"e_1_3_2_141_2","doi-asserted-by":"crossref","unstructured":"Ortalo-Magn\u00e9 A Lemassu A Lan\u00e9elle MA Bardou F Silve G Gounon P Marchal G Daff\u00e9 M. 1996. Identification of the surface-exposed lipids on the cell envelopes of Mycobacterium tuberculosis and other mycobacterial species. J Bacteriol 178: 456\u2013461. http:\/\/dx.doi.org\/10.1128\/jb.178.2.456-461.1996 [PubMed]","DOI":"10.1128\/jb.178.2.456-461.1996"},{"key":"e_1_3_2_142_2","doi-asserted-by":"crossref","unstructured":"Sambou T Dinadayala P Stadthagen G Barilone N Bordat Y Constant P Levillain F Neyrolles O Gicquel B Lemassu A Daff\u00e9 M Jackson M. 2008. Capsular glucan and intracellular glycogen of Mycobacterium tuberculosis : biosynthesis and impact on the persistence in mice. Mol Microbiol 70: 762\u2013774. http:\/\/dx.doi.org\/10.1111\/j.1365-2958.2008.06445.x","DOI":"10.1111\/j.1365-2958.2008.06445.x"},{"key":"e_1_3_2_143_2","doi-asserted-by":"crossref","unstructured":"Chandra G Chater KF Bornemann S. 2011. Unexpected and widespread connections between bacterial glycogen and trehalose metabolism. Microbiology 157: 1565\u20131572. http:\/\/dx.doi.org\/10.1099\/mic.0.044263-0","DOI":"10.1099\/mic.0.044263-0"},{"key":"e_1_3_2_144_2","doi-asserted-by":"crossref","unstructured":"Leiba J Syson K Baronian G Zanella-Cl\u00e9on I Kalscheuer R Kremer L Bornemann S Molle V. 2013. Mycobacterium tuberculosis maltosyltransferase GlgE a genetically validated antituberculosis target is negatively regulated by Ser\/Thr phosphorylation. J Biol Chem 288: 16546\u201316556. http:\/\/dx.doi.org\/10.1074\/jbc.M112.398503","DOI":"10.1074\/jbc.M112.398503"},{"key":"e_1_3_2_145_2","doi-asserted-by":"crossref","unstructured":"Ojha AK Baughn AD Sambandan D Hsu T Trivelli X Guerardel Y Alahari A Kremer L Jacobs WR Jr Hatfull GF. 2008. Growth of Mycobacterium tuberculosis biofilms containing free mycolic acids and harbouring drug-tolerant bacteria. Mol Microbiol 69: 164\u2013174. http:\/\/dx.doi.org\/10.1111\/j.1365-2958.2008.06274.x [PubMed]","DOI":"10.1111\/j.1365-2958.2008.06274.x"},{"key":"e_1_3_2_146_2","doi-asserted-by":"crossref","unstructured":"Ojha AK Trivelli X Guerardel Y Kremer L Hatfull GF. 2010. Enzymatic hydrolysis of trehalose dimycolate releases free mycolic acids during mycobacterial growth in biofilms. J Biol Chem 285: 17380\u201317389. http:\/\/dx.doi.org\/10.1074\/jbc.M110.112813","DOI":"10.1074\/jbc.M110.112813"},{"key":"e_1_3_2_147_2","doi-asserted-by":"crossref","unstructured":"Kalscheuer R Weinrick B Veeraraghavan U Besra GS Jacobs WR Jr. 2010. Trehalose-recycling ABC transporter LpqY-SugA-SugB-SugC is essential for virulence of Mycobacterium tuberculosis . Proc Natl Acad Sci USA 107: 21761\u201321766. http:\/\/dx.doi.org\/10.1073\/pnas.1014642108 [PubMed]","DOI":"10.1073\/pnas.1014642108"},{"key":"e_1_3_2_148_2","doi-asserted-by":"crossref","unstructured":"Pitarque S Larrouy-Maumus G Payr\u00e9 B Jackson M Puzo G Nigou J. 2008. The immunomodulatory lipoglycans lipoarabinomannan and lipomannan are exposed at the mycobacterial cell surface. Tuberculosis (Edinb) 88: 560\u2013565. http:\/\/dx.doi.org\/10.1016\/j.tube.2008.04.002","DOI":"10.1016\/j.tube.2008.04.002"},{"key":"e_1_3_2_149_2","doi-asserted-by":"crossref","unstructured":"Vignal C Gu\u00e9rardel Y Kremer L Masson M Legrand D Mazurier J Elass E. 2003. Lipomannans but not lipoarabinomannans purified from Mycobacterium chelonae and Mycobacterium kansasii induce TNF-alpha and IL-8 secretion by a CD14-toll-like receptor 2-dependent mechanism. J Immunol 171: 2014\u20132023. http:\/\/dx.doi.org\/10.4049\/jimmunol.171.4.2014 [PubMed][CrossRef]","DOI":"10.4049\/jimmunol.171.4.2014"},{"key":"e_1_3_2_150_2","doi-asserted-by":"crossref","unstructured":"Goude R Amin AG Chatterjee D Parish T. 2008. The critical role of embC in Mycobacterium tuberculosis . J Bacteriol 190: 4335\u20134341. http:\/\/dx.doi.org\/10.1128\/JB.01825-07 [PubMed]","DOI":"10.1128\/JB.01825-07"},{"key":"e_1_3_2_151_2","doi-asserted-by":"crossref","unstructured":"Deb C Lee CM Dubey VS Daniel J Abomoelak B Sirakova TD Pawar S Rogers L Kolattukudy PE. 2009. A novel in vitro multiple-stress dormancy model for Mycobacterium tuberculosis generates a lipid-loaded drug-tolerant dormant pathogen. PLoS One 4: e6077. http:\/\/dx.doi.org\/10.1371\/journal.pone.0006077","DOI":"10.1371\/journal.pone.0006077"},{"key":"e_1_3_2_152_2","doi-asserted-by":"crossref","unstructured":"Gillespie J Barton LL Rypka EW. 1986. Phenotypic changes in mycobacteria grown in oxygen-limited conditions. J Med Microbiol 21: 251\u2013255. http:\/\/dx.doi.org\/10.1099\/00222615-21-3-251 [PubMed]","DOI":"10.1099\/00222615-21-3-251"},{"key":"e_1_3_2_153_2","doi-asserted-by":"crossref","unstructured":"Daniel J Maamar H Deb C Sirakova TD Kolattukudy PE. 2011. Mycobacterium tuberculosis uses host triacylglycerol to accumulate lipid droplets and acquires a dormancy-like phenotype in lipid-loaded macrophages. PLoS Pathog 7: e1002093. http:\/\/dx.doi.org\/10.1371\/journal.ppat.1002093","DOI":"10.1371\/journal.ppat.1002093"},{"key":"e_1_3_2_154_2","doi-asserted-by":"crossref","unstructured":"Corrales RM Molle V Leiba J Mourey L de Chastellier C Kremer L. 2012. Phosphorylation of mycobacterial PcaA inhibits mycolic acid cyclopropanation: consequences for intracellular survival and for phagosome maturation block. J Biol Chem 287: 26187\u201326199. http:\/\/dx.doi.org\/10.1074\/jbc.M112.373209 [PubMed]","DOI":"10.1074\/jbc.M112.373209"},{"key":"e_1_3_2_155_2","doi-asserted-by":"crossref","unstructured":"Rao V Fujiwara N Porcelli SA Glickman MS. 2005. Mycobacterium tuberculosis controls host innate immune activation through cyclopropane modification of a glycolipid effector molecule. J Exp Med 201: 535\u2013543. http:\/\/dx.doi.org\/10.1084\/jem.20041668","DOI":"10.1084\/jem.20041668"},{"key":"e_1_3_2_156_2","doi-asserted-by":"crossref","unstructured":"Glickman MS Cox JS Jacobs WR Jr. 2000. A novel mycolic acid cyclopropane synthetase is required for cording persistence and virulence of Mycobacterium tuberculosis . Mol Cell 5: 717\u2013727. http:\/\/dx.doi.org\/10.1016\/S1097-2765(00)80250-6","DOI":"10.1016\/S1097-2765(00)80250-6"},{"key":"e_1_3_2_157_2","doi-asserted-by":"crossref","unstructured":"Galagan JE Minch K Peterson M Lyubetskaya A Azizi E Sweet L Gomes A Rustad T Dolganov G Glotova I Abeel T Mahwinney C Kennedy AD Allard R Brabant W Krueger A Jaini S Honda B Yu WH Hickey MJ Zucker J Garay C Weiner B Sisk P Stolte C Winkler JK Van de Peer Y Iazzetti P Camacho D Dreyfuss J Liu Y Dorhoi A Mollenkopf HJ Drogaris P Lamontagne J Zhou Y Piquenot J Park ST Raman S Kaufmann SH Mohney RP Chelsky D Moody DB Sherman DR Schoolnik GK. 2013. The Mycobacterium tuberculosis regulatory network and hypoxia. Nature 499: 178\u2013183. http:\/\/dx.doi.org\/10.1038\/nature12337","DOI":"10.1038\/nature12337"},{"key":"e_1_3_2_158_2","doi-asserted-by":"crossref","unstructured":"Barkan D Hedhli D Yan HG Huygen K Glickman MS. 2012. Mycobacterium tuberculosis lacking all mycolic acid cyclopropanation is viable but highly attenuated and hyperinflammatory in mice. Infect Immun 80: 1958\u20131968. http:\/\/dx.doi.org\/10.1128\/IAI.00021-12","DOI":"10.1128\/IAI.00021-12"},{"key":"e_1_3_2_159_2","doi-asserted-by":"crossref","unstructured":"Barkan D Liu Z Sacchettini JC Glickman MS. 2009. Mycolic acid cyclopropanation is essential for viability drug resistance and cell wall integrity of Mycobacterium tuberculosis . Chem Biol 16: 499\u2013509. http:\/\/dx.doi.org\/10.1016\/j.chembiol.2009.04.001 [PubMed]","DOI":"10.1016\/j.chembiol.2009.04.001"},{"key":"e_1_3_2_160_2","doi-asserted-by":"crossref","unstructured":"Bloch H Segal W. 1956. Biochemical differentiation of Mycobacterium tuberculosis grown in vivo and in vitro . J Bacteriol 72: 132\u2013141. [PubMed]","DOI":"10.1128\/jb.72.2.132-141.1956"},{"key":"e_1_3_2_161_2","doi-asserted-by":"crossref","unstructured":"Cole ST Brosch R Parkhill J Garnier T Churcher C Harris D Gordon SV Eiglmeier K Gas S Barry CE III Tekaia F Badcock K Basham D Brown D Chillingworth T Connor R Davies R Devlin K Feltwell T Gentles S Hamlin N Holroyd S Hornsby T Jagels K Krogh A McLean J Moule S Murphy L Oliver K Osborne J Quail MA Rajandream MA Rogers J Rutter S Seeger K Skelton J Squares R Squares S Sulston JE Taylor K Whitehead S Barrell BG. 1998. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393: 537\u2013544. http:\/\/dx.doi.org\/10.1038\/31159","DOI":"10.1038\/31159"},{"key":"e_1_3_2_162_2","doi-asserted-by":"crossref","unstructured":"Marrero J Trujillo C Rhee KY Ehrt S. 2013. Glucose phosphorylation is required for Mycobacterium tuberculosis persistence in mice. PLoS Pathog 9: e1003116. http:\/\/dx.doi.org\/10.1371\/journal.ppat.1003116 [PubMed]","DOI":"10.1371\/journal.ppat.1003116"},{"key":"e_1_3_2_163_2","doi-asserted-by":"crossref","unstructured":"Arora G Sajid A Gupta M Bhaduri A Kumar P Basu-Modak S Singh Y. 2010. Understanding the role of PknJ in Mycobacterium tuberculosis : biochemical characterization and identification of novel substrate pyruvate kinase A. PLoS One 5: e10772. http:\/\/dx.doi.org\/10.1371\/journal.pone.0010772","DOI":"10.1371\/journal.pone.0010772"},{"key":"e_1_3_2_164_2","doi-asserted-by":"crossref","unstructured":"Deol P Vohra R Saini AK Singh A Chandra H Chopra P Das TK Tyagi AK Singh Y. 2005. Role of Mycobacterium tuberculosis Ser\/Thr kinase PknF: implications in glucose transport and cell division. J Bacteriol 187: 3415\u20133420. http:\/\/dx.doi.org\/10.1128\/JB.187.10.3415-3420.2005","DOI":"10.1128\/JB.187.10.3415-3420.2005"},{"key":"e_1_3_2_165_2","doi-asserted-by":"crossref","unstructured":"Molle V Soulat D Jault JM Grangeasse C Cozzone AJ Prost JF. 2004. Two FHA domains on an ABC transporter Rv1747 mediate its phosphorylation by PknF a Ser\/Thr protein kinase from Mycobacterium tuberculosis . FEMS Microbiol Lett 234: 215\u2013223. http:\/\/dx.doi.org\/10.1111\/j.1574-6968.2004.tb09536.x [PubMed]","DOI":"10.1111\/j.1574-6968.2004.tb09536.x"},{"key":"e_1_3_2_166_2","doi-asserted-by":"crossref","unstructured":"Singh DK Singh PK Tiwari S Singh SK Kumari R Tripathi DK Srivastava KK. 2014. Phosphorylation of pyruvate kinase A by protein kinase J leads to the altered growth and differential rate of intracellular survival of mycobacteria. Appl Microbiol Biotechnol 98: 10065\u201310076. http:\/\/dx.doi.org\/10.1007\/s00253-014-5859-4","DOI":"10.1007\/s00253-014-5859-4"},{"key":"e_1_3_2_167_2","doi-asserted-by":"crossref","unstructured":"Marrero J Rhee KY Schnappinger D Pethe K Ehrt S. 2010. Gluconeogenic carbon flow of tricarboxylic acid cycle intermediates is critical for Mycobacterium tuberculosis to establish and maintain infection. Proc Natl Acad Sci USA 107: 9819\u20139824. http:\/\/dx.doi.org\/10.1073\/pnas.1000715107","DOI":"10.1073\/pnas.1000715107"},{"key":"e_1_3_2_168_2","doi-asserted-by":"crossref","unstructured":"Nott TJ Kelly G Stach L Li J Westcott S Patel D Hunt DM Howell S Buxton RS O\u2019Hare HM Smerdon SJ. 2009. An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis . Sci Signal 2: ra12. http:\/\/dx.doi.org\/10.1126\/scisignal.2000212","DOI":"10.1126\/scisignal.2000212"},{"key":"e_1_3_2_169_2","doi-asserted-by":"crossref","unstructured":"Tiwari D Singh RK Goswami K Verma SK Prakash B Nandicoori VK. 2009. Key residues in Mycobacterium tuberculosis protein kinase G play a role in regulating kinase activity and survival in the host. J Biol Chem 284: 27467\u201327479. http:\/\/dx.doi.org\/10.1074\/jbc.M109.036095","DOI":"10.1074\/jbc.M109.036095"},{"key":"e_1_3_2_170_2","doi-asserted-by":"crossref","unstructured":"Chaurasiya SK Srivastava KK. 2009. Downregulation of protein kinase C-alpha enhances intracellular survival of mycobacteria: role of PknG. BMC Microbiol 9: 271. http:\/\/dx.doi.org\/10.1186\/1471-2180-9-271","DOI":"10.1186\/1471-2180-9-271"},{"key":"e_1_3_2_171_2","doi-asserted-by":"crossref","unstructured":"Scherr N M\u00fcller P Perisa D Combaluzier B Jen\u00f6 P Pieters J. 2009. Survival of pathogenic mycobacteria in macrophages is mediated through autophosphorylation of protein kinase G. J Bacteriol 191: 4546\u20134554. http:\/\/dx.doi.org\/10.1128\/JB.00245-09","DOI":"10.1128\/JB.00245-09"},{"key":"e_1_3_2_172_2","doi-asserted-by":"crossref","unstructured":"Kang PB Azad AK Torrelles JB Kaufman TM Beharka A Tibesar E DesJardin LE Schlesinger LS. 2005. The human macrophage mannose receptor directs Mycobacterium tuberculosis lipoarabinomannan-mediated phagosome biogenesis. J Exp Med 202: 987\u2013999. http:\/\/dx.doi.org\/10.1084\/jem.20051239 [PubMed]","DOI":"10.1084\/jem.20051239"},{"key":"e_1_3_2_173_2","doi-asserted-by":"crossref","unstructured":"Wang XM Soetaert K Peirs P Kalai M Fontaine V Dehaye JP Lef\u00e8vre P. 2015. Biochemical analysis of the NAD+-dependent malate dehydrogenase a substrate of several serine\/threonine protein kinases of Mycobacterium tuberculosis . PLoS One 10: e0123327. http:\/\/dx.doi.org\/10.1371\/journal.pone.0123327","DOI":"10.1371\/journal.pone.0123327"},{"key":"e_1_3_2_174_2","doi-asserted-by":"crossref","unstructured":"Be NA Bishai WR Jain SK. 2012. Role of Mycobacterium tuberculosis pknD in the pathogenesis of central nervous system tuberculosis. BMC Microbiol 12: 7. http:\/\/dx.doi.org\/10.1186\/1471-2180-12-7 [PubMed]","DOI":"10.1186\/1471-2180-12-7"},{"key":"e_1_3_2_175_2","doi-asserted-by":"crossref","unstructured":"Wayne LG. 1977. Synchronized replication of Mycobacterium tuberculosis . Infect Immun 17: 528\u2013530. [PubMed]","DOI":"10.1128\/iai.17.3.528-530.1977"},{"key":"e_1_3_2_176_2","unstructured":"Schmitt SK Longworth DL. 2014. Pulmonary infections 505\u2013524. In Kacmarek RM Stoller JK Heuer A (ed) Egan\u2019s Fundamentals of Respiratory Care 10th ed. Elsevier Health Sciences St. Louis MO."},{"key":"e_1_3_2_177_2","doi-asserted-by":"crossref","unstructured":"Tsai MC Chakravarty S Zhu G Xu J Tanaka K Koch C Tufariello J Flynn J Chan J. 2006. Characterization of the tuberculous granuloma in murine and human lungs: cellular composition and relative tissue oxygen tension. Cell Microbiol 8: 218\u2013232. http:\/\/dx.doi.org\/10.1111\/j.1462-5822.2005.00612.x [PubMed]","DOI":"10.1111\/j.1462-5822.2005.00612.x"},{"key":"e_1_3_2_178_2","doi-asserted-by":"crossref","unstructured":"Via LE Lin PL Ray SM Carrillo J Allen SS Eum SY Taylor K Klein E Manjunatha U Gonzales J Lee EG Park SK Raleigh JA Cho SN McMurray DN Flynn JL Barry CE III. 2008. Tuberculous granulomas are hypoxic in guinea pigs rabbits and nonhuman primates. Infect Immun 76: 2333\u20132340. http:\/\/dx.doi.org\/10.1128\/IAI.01515-07","DOI":"10.1128\/IAI.01515-07"},{"key":"e_1_3_2_179_2","doi-asserted-by":"crossref","unstructured":"Barthe P Mukamolova GV Roumestand C Cohen-Gonsaud M. 2010. The structure of PknB extracellular PASTA domain from Mycobacterium tuberculosis suggests a ligand-dependent kinase activation. Structure 18: 606\u2013615. http:\/\/dx.doi.org\/10.1016\/j.str.2010.02.013","DOI":"10.1016\/j.str.2010.02.013"},{"key":"e_1_3_2_180_2","doi-asserted-by":"crossref","unstructured":"Sureka K Hossain T Mukherjee P Chatterjee P Datta P Kundu M Basu J. 2010. Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division. PLoS One 5: e8590. http:\/\/dx.doi.org\/10.1371\/journal.pone.0008590","DOI":"10.1371\/journal.pone.0008590"},{"key":"e_1_3_2_181_2","doi-asserted-by":"crossref","unstructured":"Baronian G Ginda K Berry L Cohen-Gonsaud M Zakrzewska-Czerwi\u0144ska J Jakimowicz D Molle V. 2015. Phosphorylation of Mycobacterium tuberculosis ParB participates in regulating the ParABS chromosome segregation system. PLoS One 10: e0119907. http:\/\/dx.doi.org\/10.1371\/journal.pone.0119907","DOI":"10.1371\/journal.pone.0119907"},{"key":"e_1_3_2_182_2","doi-asserted-by":"crossref","unstructured":"Sharma K Gupta M Krupa A Srinivasan N Singh Y. 2006. EmbR a regulatory protein with ATPase activity is a substrate of multiple serine\/threonine kinases and phosphatase in Mycobacterium tuberculosis . FEBS J 273: 2711\u20132721. http:\/\/dx.doi.org\/10.1111\/j.1742-4658.2006.05289.x","DOI":"10.1111\/j.1742-4658.2006.05289.x"},{"key":"e_1_3_2_183_2","doi-asserted-by":"crossref","unstructured":"Corrales RM Leiba J Cohen-Gonsaud M Molle V Kremer L. 2013. Mycobacterium tuberculosis S-adenosyl-l-homocysteine hydrolase is negatively regulated by Ser\/Thr phosphorylation. Biochem Biophys Res Commun 430: 858\u2013864. http:\/\/dx.doi.org\/10.1016\/j.bbrc.2012.11.038","DOI":"10.1016\/j.bbrc.2012.11.038"},{"key":"e_1_3_2_184_2","doi-asserted-by":"crossref","unstructured":"Sajid A Arora G Gupta M Upadhyay S Nandicoori VK Singh Y. 2011. Phosphorylation of Mycobacterium tuberculosis Ser\/Thr phosphatase by PknA and PknB. PLoS One 6: e17871. http:\/\/dx.doi.org\/10.1371\/journal.pone.0017871 [PubMed]","DOI":"10.1371\/journal.pone.0017871"},{"key":"e_1_3_2_185_2","doi-asserted-by":"crossref","unstructured":"Canova MJ Kremer L Molle V. 2009. The Mycobacterium tuberculosis GroEL1 chaperone is a substrate of Ser\/Thr protein kinases. J Bacteriol 191: 2876\u20132883. http:\/\/dx.doi.org\/10.1128\/JB.01569-08 [PubMed]","DOI":"10.1128\/JB.01569-08"},{"key":"e_1_3_2_186_2","doi-asserted-by":"crossref","unstructured":"Gupta M Sajid A Sharma K Ghosh S Arora G Singh R Nagaraja V Tandon V Singh Y. 2014. HupB a nucleoid-associated protein of Mycobacterium tuberculosis is modified by serine\/threonine protein kinases in vivo . J Bacteriol 196: 2646\u20132657. http:\/\/dx.doi.org\/10.1128\/JB.01625-14","DOI":"10.1128\/JB.01625-14"},{"key":"e_1_3_2_187_2","doi-asserted-by":"crossref","unstructured":"Grundner C Gay LM Alber T. 2005. Mycobacterium tuberculosis serine\/threonine kinases PknB PknD PknE and PknF phosphorylate multiple FHA domains. Protein Sci 14: 1918\u20131921. http:\/\/dx.doi.org\/10.1110\/ps.051413405 [PubMed]","DOI":"10.1110\/ps.051413405"},{"key":"e_1_3_2_188_2","doi-asserted-by":"crossref","unstructured":"Roumestand C Leiba J Galophe N Margeat E Padilla A Bessin Y Barthe P Molle V Cohen-Gonsaud M. 2011. Structural insight into the Mycobacterium tuberculosis Rv0020c protein and its interaction with the PknB kinase. Structure 19: 1525\u20131534. http:\/\/dx.doi.org\/10.1016\/j.str.2011.07.011","DOI":"10.1016\/j.str.2011.07.011"},{"key":"e_1_3_2_189_2","doi-asserted-by":"crossref","unstructured":"Villarino A Duran R Wehenkel A Fernandez P England P Brodin P Cole ST Zimny-Arndt U Jungblut PR Cerve\u00f1ansky C Alzari PM. 2005. Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA a FHA domain-containing protein through activation loop-mediated interactions. J Mol Biol 350: 953\u2013963. http:\/\/dx.doi.org\/10.1016\/j.jmb.2005.05.049","DOI":"10.1016\/j.jmb.2005.05.049"},{"key":"e_1_3_2_190_2","doi-asserted-by":"crossref","unstructured":"Singhal A Arora G Sajid A Maji A Bhat A Virmani R Upadhyay S Nandicoori VK Sengupta S Singh Y. 2013. Regulation of homocysteine metabolism by Mycobacterium tuberculosis S-adenosylhomocysteine hydrolase. Sci Rep 3: 2264. http:\/\/dx.doi.org\/10.1038\/srep02264","DOI":"10.1038\/srep02264"},{"key":"e_1_3_2_191_2","doi-asserted-by":"crossref","unstructured":"Sajid A Arora G Gupta M Singhal A Chakraborty K Nandicoori VK Singh Y. 2011. Interaction of Mycobacterium tuberculosis elongation factor Tu with GTP is regulated by phosphorylation. J Bacteriol 193: 5347\u20135358. http:\/\/dx.doi.org\/10.1128\/JB.05469-11","DOI":"10.1128\/JB.05469-11"},{"key":"e_1_3_2_192_2","doi-asserted-by":"crossref","unstructured":"Corrales RM Molle V Leiba J Mourey L de Chastellier C Kremer L. 2012. Phosphorylation of mycobacterial PcaA inhibits mycolic acid cyclopropanation: consequences for intracellular survival and for phagosome maturation block. J Biol Chem 287: 26187\u201326199. http:\/\/dx.doi.org\/10.1074\/jbc.M112.373209 [PubMed]","DOI":"10.1074\/jbc.M112.373209"},{"key":"e_1_3_2_193_2","doi-asserted-by":"crossref","unstructured":"Molle V Reynolds RC Alderwick LJ Besra GS Cozzone AJ F\u00fctterer K Kremer L. 2008. EmbR2 a structural homologue of EmbR inhibits the Mycobacterium tuberculosis kinase\/substrate pair PknH\/EmbR. Biochem J 410: 309\u2013317. http:\/\/dx.doi.org\/10.1042\/BJ20071384","DOI":"10.1042\/BJ20071384"},{"key":"e_1_3_2_194_2","doi-asserted-by":"crossref","unstructured":"Wolff KA de la Pe\u00f1a AH Nguyen HT Pham TH Amzel LM Gabelli SB Nguyen L. 2015. A redox regulatory system critical for mycobacterial survival in macrophages and biofilm development. PLoS Pathog 11: e1004839. http:\/\/dx.doi.org\/10.1371\/journal.ppat.1004839","DOI":"10.1371\/journal.ppat.1004839"},{"key":"e_1_3_2_195_2","doi-asserted-by":"crossref","unstructured":"Molle V Kremer L Girard-Blanc C Besra GS Cozzone AJ Prost JF. 2003. An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH a Ser\/Thr protein kinase from Mycobacterium tuberculosis . Biochemistry 42: 15300\u201315309. http:\/\/dx.doi.org\/10.1021\/bi035150b [PubMed]","DOI":"10.1021\/bi035150b"},{"key":"e_1_3_2_196_2","doi-asserted-by":"crossref","unstructured":"Jang J Stella A Boudou F Levillain F Darthuy E Vaubourgeix J Wang C Bardou F Puzo G Gilleron M Burlet-Schiltz O Monsarrat B Brodin P Gicquel B Neyrolles O. 2010. Functional characterization of the Mycobacterium tuberculosis serine\/threonine kinase PknJ. Microbiology 156: 1619\u20131631. http:\/\/dx.doi.org\/10.1099\/mic.0.038133-0","DOI":"10.1099\/mic.0.038133-0"},{"key":"e_1_3_2_197_2","doi-asserted-by":"crossref","unstructured":"Kumari R Saxena R Tiwari S Tripathi DK Srivastava KK. 2013. Rv3080c regulates the rate of inhibition of mycobacteria by isoniazid through FabD. Mol Cell Biochem 374: 149\u2013155. http:\/\/dx.doi.org\/10.1007\/s11010-012-1514-5 [PubMed]","DOI":"10.1007\/s11010-012-1514-5"},{"key":"e_1_3_2_198_2","doi-asserted-by":"crossref","unstructured":"Canova MJ Veyron-Churlet R Zanella-Cleon I Cohen-Gonsaud M Cozzone AJ Becchi M Kremer L Molle V. 2008. The Mycobacterium tuberculosis serine\/threonine kinase PknL phosphorylates Rv2175c: mass spectrometric profiling of the activation loop phosphorylation sites and their role in the recruitment of Rv2175c. Proteomics 8: 521\u2013533. http:\/\/dx.doi.org\/10.1002\/pmic.200700442 [PubMed]","DOI":"10.1002\/pmic.200700442"},{"key":"e_1_3_2_199_2","doi-asserted-by":"crossref","unstructured":"Rifat D Bishai WR Karakousis PC. 2009. Phosphate depletion: a novel trigger for Mycobacterium tuberculosis persistence. J Infect Dis 200: 1126\u20131135. http:\/\/dx.doi.org\/10.1086\/605700","DOI":"10.1086\/605700"},{"key":"e_1_3_2_200_2","doi-asserted-by":"crossref","unstructured":"Vanzembergh F Peirs P Lefevre P Celio N Mathys V Content J Kalai M. 2010. Effect of PstS sub-units or PknD deficiency on the survival of Mycobacterium tuberculosis . Tuberculosis (Edinb) 90: 338\u2013345. http:\/\/dx.doi.org\/10.1016\/j.tube.2010.09.004","DOI":"10.1016\/j.tube.2010.09.004"},{"key":"e_1_3_2_201_2","doi-asserted-by":"crossref","unstructured":"Kumar D Palaniyandi K Challu VK Kumar P Narayanan S. 2013. PknE a serine\/threonine protein kinase from Mycobacterium tuberculosis has a role in adaptive responses. Arch Microbiol 195: 75\u201380. http:\/\/dx.doi.org\/10.1007\/s00203-012-0848-4 [PubMed]","DOI":"10.1007\/s00203-012-0848-4"},{"key":"e_1_3_2_202_2","doi-asserted-by":"crossref","unstructured":"Spivey VL Molle V Whalan RH Rodgers A Leiba J Stach L Walker KB Smerdon SJ Buxton RS. 2011. Forkhead-associated (FHA) domain containing ABC transporter Rv1747 is positively regulated by Ser\/Thr phosphorylation in Mycobacterium tuberculosis . J Biol Chem 286: 26198\u201326209. http:\/\/dx.doi.org\/10.1074\/jbc.M111.246132","DOI":"10.1074\/jbc.M111.246132"},{"key":"e_1_3_2_203_2","doi-asserted-by":"crossref","unstructured":"Jani C Eoh H Lee JJ Hamasha K Sahana MB Han JS Nyayapathy S Lee JY Suh JW Lee SH Rehse SJ Crick DC Kang CM. 2010. Regulation of polar peptidoglycan biosynthesis by Wag31 phosphorylation in mycobacteria. BMC Microbiol 10: 327. http:\/\/dx.doi.org\/10.1186\/1471-2180-10-327","DOI":"10.1186\/1471-2180-10-327"}],"container-title":["Microbiology Spectrum"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/microbiolspec.TBTB2-0005-2015","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/microbiolspec.TBTB2-0005-2015","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,8]],"date-time":"2022-03-08T06:53:16Z","timestamp":1646722396000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/microbiolspec.TBTB2-0005-2015"}},"subtitle":[],"editor":[{"given":"William R.","family":"Jacobs Jr.","sequence":"additional","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]},{"given":"Helen","family":"McShane","sequence":"additional","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]},{"given":"Valerie","family":"Mizrahi","sequence":"additional","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]},{"given":"Ian M.","family":"Orme","sequence":"additional","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2017,3,10]]},"references-count":202,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2017,3,10]]}},"alternative-id":["10.1128\/microbiolspec.TBTB2-0005-2015"],"URL":"https:\/\/doi.org\/10.1128\/microbiolspec.tbtb2-0005-2015","relation":{},"ISSN":["2165-0497"],"issn-type":[{"value":"2165-0497","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,3,10]]},"assertion":[{"value":"2015-12-22","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2017-03-10","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"5.2.09"}}