{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T12:43:44Z","timestamp":1792500224635,"version":"4.5.0"},"reference-count":92,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2017,7,1]],"date-time":"2017-07-01T00:00:00Z","timestamp":1498867200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2017,7,1]],"date-time":"2017-07-01T00:00:00Z","timestamp":1498867200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["bmn.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Drug Discovery Today"],"published-print":{"date-parts":[[2017,7]]},"DOI":"10.1016\/j.drudis.2017.04.012","type":"journal-article","created":{"date-parts":[[2017,4,27]],"date-time":"2017-04-27T21:01:10Z","timestamp":1493326870000},"page":"1008-1016","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":56,"title":["Targeting isocitrate lyase for the treatment of latent tuberculosis"],"prefix":"10.1016","volume":"22","author":[{"given":"Ram Prasad","family":"Bhusal","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ghader","family":"Bashiri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6378-9633","authenticated-orcid":false,"given":"Brooke X.C.","family":"Kwai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7288-3939","authenticated-orcid":false,"given":"Jonathan","family":"Sperry","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0633-6771","authenticated-orcid":false,"given":"Ivanhoe K.H.","family":"Leung","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.drudis.2017.04.012_bib0005","doi-asserted-by":"crossref","first-page":"16076","DOI":"10.1038\/nrdp.2016.76","article-title":"Tuberculosis","volume":"27","author":"Pai","year":"2016","journal-title":"Nat. Rev. Dis. Primers"},{"key":"10.1016\/j.drudis.2017.04.012_bib0010","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1056\/NEJMra1200894","article-title":"Tuberculosis","volume":"368","author":"Zumla","year":"2013","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.drudis.2017.04.012_bib0015","doi-asserted-by":"crossref","first-page":"15","DOI":"10.4049\/jimmunol.0903856","article-title":"Understanding latent tuberculosis: a moving target","volume":"185","author":"Lin","year":"2010","journal-title":"J. Immunol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0020","doi-asserted-by":"crossref","first-page":"2127","DOI":"10.1056\/NEJMra1405427","article-title":"Latent Mycobacterium tuberculosis infection","volume":"372","author":"Getahun","year":"2015","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.drudis.2017.04.012_bib0025","doi-asserted-by":"crossref","first-page":"20130437","DOI":"10.1098\/rstb.2013.0437","article-title":"The ongoing challenge of latent tuberculosis","volume":"369","author":"Esmail","year":"2014","journal-title":"Phil. Trans. R. Soc. B"},{"key":"10.1016\/j.drudis.2017.04.012_bib0030","doi-asserted-by":"crossref","first-page":"e1002152","DOI":"10.1371\/journal.pmed.1002152","article-title":"The global burden of latent tuberculosis infection: a re-estimation using mathematical modelling","volume":"13","author":"Houben","year":"2016","journal-title":"PLoS Med."},{"key":"10.1016\/j.drudis.2017.04.012_bib0035","series-title":"Global Tuberculosis Report 2016","author":"World Health Organization","year":"2016"},{"key":"10.1016\/j.drudis.2017.04.012_bib0040","doi-asserted-by":"crossref","first-page":"1563","DOI":"10.1183\/13993003.01245-2015","article-title":"Management of latent Mycobacterium tuberculosis infection: WHO guidelines for low tuberculosis burden countries","volume":"46","author":"Getahun","year":"2015","journal-title":"Eur. Respir. J."},{"key":"10.1016\/j.drudis.2017.04.012_bib0045","doi-asserted-by":"crossref","first-page":"16078","DOI":"10.1038\/npjpcrm.2016.78","article-title":"Recent developments in the diagnosis and management of tuberculosis","volume":"26","author":"Sulis","year":"2016","journal-title":"NPJ Prim. Care Respir. Med"},{"key":"10.1016\/j.drudis.2017.04.012_bib0050","doi-asserted-by":"crossref","first-page":"1814","DOI":"10.1016\/S0140-6736(10)60483-7","article-title":"Tuberculosis control and elimination 2010\u201350: cure, care, and social development","volume":"375","author":"L\u00f6nnroth","year":"2010","journal-title":"Lancet"},{"key":"10.1016\/j.drudis.2017.04.012_bib0055","first-page":"163","article-title":"Current management options for latent tuberculosis: a review","volume":"5","author":"Norton","year":"2012","journal-title":"Infect. Drug Resist"},{"key":"10.1016\/j.drudis.2017.04.012_bib0060","doi-asserted-by":"crossref","first-page":"63","DOI":"10.2147\/IDR.S8994","article-title":"The use of anti-tuberculosis therapy for latent TB infection","volume":"3","author":"Denholm","year":"2010","journal-title":"Infect. Drug Resist"},{"key":"10.1016\/j.drudis.2017.04.012_bib0065","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1164\/rccm.200510-1666ST","article-title":"An official ATS statement: hepatotoxicity of antituberculosis therapy","volume":"174","author":"Saukkonen","year":"2006","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"10.1016\/j.drudis.2017.04.012_bib0070","doi-asserted-by":"crossref","first-page":"7161","DOI":"10.1128\/JB.181.23.7161-7167.1999","article-title":"Characterization of activity and expression of isocitrate lyase in Mycobacterium avium and Mycobacterium tuberculosis","volume":"181","author":"H\u00f6ner zu Bentrup","year":"1999","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0075","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1186\/1745-6150-1-31","article-title":"Evolution of glyoxylate cycle enzymes in Metazoa: evidence of multiple horizontal transfer events and pseudogene formation","volume":"1","author":"Kondrashov","year":"2006","journal-title":"Biol. Direct"},{"key":"10.1016\/j.drudis.2017.04.012_bib0080","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1038\/31159","article-title":"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence","volume":"393","author":"Cole","year":"1998","journal-title":"Nature"},{"key":"10.1016\/j.drudis.2017.04.012_bib0085","doi-asserted-by":"crossref","first-page":"5479","DOI":"10.1128\/JB.184.19.5479-5490.2002","article-title":"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains","volume":"184","author":"Fleischmann","year":"2002","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0090","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1111\/j.1365-2958.2006.05297.x","article-title":"Dual role of isocitrate lyase 1 in the glyoxylate and methylcitrate cycles in Mycobacterium tuberculosis","volume":"61","author":"Gould","year":"2006","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0095","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1038\/nm1252","article-title":"Mycobacterium tuberculosis isocitrate lyases 1 and 2 are jointly required for in vivo growth and virulence","volume":"11","author":"Mu\u00f1oz-El\u00edas","year":"2005","journal-title":"Nat. Med."},{"key":"10.1016\/j.drudis.2017.04.012_bib0100","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1016\/j.tube.2008.01.003","article-title":"Identification of genes of Mycobacterium tuberculosis upregulated during anaerobic persistence by fluorescence and kanamycin resistance selection","volume":"88","author":"Saxena","year":"2008","journal-title":"Tuberculosis"},{"key":"10.1016\/j.drudis.2017.04.012_bib0105","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1111\/j.1365-2958.2010.07399.x","article-title":"Carbon flux rerouting during Mycobacterium tuberculosis growth arrest","volume":"78","author":"Shi","year":"2010","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0110","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1099\/mic.0.033084-0","article-title":"Nutrient-starved, non-replicating Mycobacterium tuberculosis requires respiration, ATP synthase and isocitrate lyase for maintenance of ATP homeostasis and viability","volume":"156","author":"Gengenbacher","year":"2010","journal-title":"Microbiology"},{"key":"10.1016\/j.drudis.2017.04.012_bib0115","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1038\/35021074","article-title":"Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase","volume":"406","author":"McKinney","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.drudis.2017.04.012_bib0120","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1016\/0006-3002(53)90107-3","article-title":"A deviation from the conventional tricarboxylic acid cycle in Pseudomonas aeruginosa","volume":"11","author":"Campbell","year":"1953","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.drudis.2017.04.012_bib0125","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1111\/j.1365-2958.2006.05247.x","article-title":"Revisiting the glyoxylate cycle: alternate pathways for microbial acetate assimilation","volume":"61","author":"Ensign","year":"2006","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0130","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1038\/179988a0","article-title":"Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle","volume":"179","author":"Kornberg","year":"1957","journal-title":"Nature"},{"key":"10.1016\/j.drudis.2017.04.012_bib0135","doi-asserted-by":"crossref","first-page":"9646","DOI":"10.1016\/S0021-9258(17)42750-5","article-title":"Determination of flux through the branch point of two metabolic cycles. The tricarboxylic acid cycle and the glyoxylate shunt","volume":"259","author":"Walsh","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0140","doi-asserted-by":"crossref","first-page":"1122","DOI":"10.1016\/j.chembiol.2010.08.009","article-title":"Metabolomics of Mycobacterium tuberculosis reveals compartmentalized co-catabolism of carbon substrates","volume":"17","author":"de Carvalho","year":"2010","journal-title":"Chem. Biol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0145","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1084\/jem.20030846","article-title":"Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: insights into the phagosomal environment","volume":"198","author":"Schnappinger","year":"2003","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.drudis.2017.04.012_bib0150","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.chom.2010.06.002","article-title":"Mycobacterium tuberculosis wears what it eats","volume":"8","author":"Russell","year":"2010","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.drudis.2017.04.012_bib0155","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1128\/jb.72.2.132-141.1956","article-title":"Biochemical differentiation of Mycobacterium tuberculosis grown in vivo and in vitro","volume":"72","author":"Bloch","year":"1956","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0160","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1111\/j.1462-5822.2005.00648.x","article-title":"Carbon metabolism of intracellular bacteria","volume":"8","author":"Mu\u00f1oz-El\u00edas","year":"2006","journal-title":"Cell Microbiol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0165","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.tube.2013.12.005","article-title":"Role of the Mce1 transporter in the lipid homeostasis of Mycobacterium tuberculosis","volume":"94","author":"Forrellad","year":"2014","journal-title":"Tuberculosis"},{"key":"10.1016\/j.drudis.2017.04.012_bib0170","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1128\/EC.1.5.657-662.2002","article-title":"Life and death in a macrophage: role of the glyoxylate cycle in virulence","volume":"1","author":"Michael","year":"2002","journal-title":"Eukaryot. Cell"},{"key":"10.1016\/j.drudis.2017.04.012_bib0175","doi-asserted-by":"crossref","first-page":"1042","DOI":"10.1128\/iai.37.3.1042-1049.1982","article-title":"Glyoxylate metabolism and adaptation of Mycobacterium tuberculosis to survive under anaerobic conditions","volume":"37","author":"Wayne","year":"1982","journal-title":"Infect. Immun."},{"key":"10.1016\/j.drudis.2017.04.012_bib0180","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1146\/annurev.micro.55.1.139","article-title":"Nonreplicating persistence of Mycobacterium tuberculosis","volume":"55","author":"Wayne","year":"2001","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0185","doi-asserted-by":"crossref","first-page":"6554","DOI":"10.1073\/pnas.1219375110","article-title":"Multifunctional essentiality of succinate metabolism in adaptation to hypoxia in Mycobacterium tuberculosis","volume":"110","author":"Eoh","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.drudis.2017.04.012_bib0190","doi-asserted-by":"crossref","first-page":"e01093","DOI":"10.1128\/mBio.01093-14","article-title":"Essentiality of succinate dehydrogenase in Mycobacterium smegmatis and its role in the generation of the membrane potential under hypoxia","volume":"5","author":"Pecsi","year":"2014","journal-title":"mBio"},{"key":"10.1016\/j.drudis.2017.04.012_bib0195","doi-asserted-by":"crossref","first-page":"6788","DOI":"10.1074\/jbc.M112.445056","article-title":"Intracellular Mycobacterium tuberculosis exploits host-derived fatty acids to limit metabolic stress","volume":"288","author":"Lee","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0200","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1016\/j.plipres.2009.03.003","article-title":"Odd-numbered very-long-chain fatty acids from the microbial, animal and plant kingdoms","volume":"48","author":"\u0158ezanka","year":"2009","journal-title":"Prog. Lipid Res."},{"key":"10.1016\/j.drudis.2017.04.012_bib0205","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/j.chembiol.2011.12.016","article-title":"Cholesterol catabolism by Mycobacterium tuberculosis requires transcriptional and metabolic adaptations","volume":"19","author":"Griffin","year":"2012","journal-title":"Chem. Biol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0210","doi-asserted-by":"crossref","first-page":"3819","DOI":"10.1021\/bi9005418","article-title":"Cholesterol metabolism increases the metabolic pool of propionate in Mycobacterium tuberculosis","volume":"48","author":"Yang","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.drudis.2017.04.012_bib0215","doi-asserted-by":"crossref","first-page":"43668","DOI":"10.1074\/jbc.M111.313643","article-title":"Pathway profiling in Mycobacterium tuberculosis: elucidation of cholesterol-derived catabolite and enzymes that catalyze its metabolism","volume":"286","author":"Thomas","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0220","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1111\/j.1365-2958.2006.05155.x","article-title":"Role of the methylcitrate cycle in Mycobacterium tuberculosis metabolism, intracellular growth, and virulence","volume":"60","author":"Mu\u00f1oz-El\u00edas","year":"2006","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0225","doi-asserted-by":"crossref","first-page":"3886","DOI":"10.1128\/JB.01767-07","article-title":"Functional characterization of a vitamin B12-dependent methylmalonyl pathway in Mycobacterium tuberculosis. Implications for propionate metabolism during growth on fatty acids","volume":"190","author":"Savvi","year":"2008","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0230","doi-asserted-by":"crossref","first-page":"3973","DOI":"10.1099\/mic.0.2007\/011726-0","article-title":"Role of the methylcitrate cycle in propionate metabolism and detoxification in Mycobacterium smegmatis","volume":"153","author":"Upton","year":"2007","journal-title":"Microbiology"},{"key":"10.1016\/j.drudis.2017.04.012_bib0235","doi-asserted-by":"crossref","first-page":"4376","DOI":"10.1073\/pnas.0711159105","article-title":"Mycobacterial persistence requires the utilization of host cholesterol","volume":"105","author":"Pandey","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.drudis.2017.04.012_bib0240","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.tube.2016.12.004","article-title":"Cholesterol plays a larger role during Mycobacterium tuberculosis in vitro dormancy and reactivation than previously suspected","volume":"103","author":"Soto-Ramirez","year":"2017","journal-title":"Tuberculosis"},{"key":"10.1016\/j.drudis.2017.04.012_bib0245","doi-asserted-by":"crossref","first-page":"4976","DOI":"10.1073\/pnas.1400390111","article-title":"Methylcitrate cycle defines the bactericidal essentiality of isocitrate lyase for survival of Mycobacterium tuberculosis on fatty acids","volume":"111","author":"Eoh","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.drudis.2017.04.012_bib0250","doi-asserted-by":"crossref","first-page":"4306","DOI":"10.1038\/ncomms5306","article-title":"Isocitrate lyase mediates broad antibiotic tolerance in Mycobacterium tuberculosis","volume":"5","author":"Nandakuma","year":"2014","journal-title":"Nat. Commun."},{"key":"10.1016\/j.drudis.2017.04.012_bib0255","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1080\/07391102.2016.1169219","article-title":"Lysine succinylation of Mycobacterium tuberculosis isocitrate lyase (ICL) fine-tunes the microbial resistance to antibiotics","volume":"35","author":"Zhou","year":"2017","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.drudis.2017.04.012_bib0260","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1038\/77964","article-title":"Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis","volume":"7","author":"Sharma","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0265","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1021\/bi401432t","article-title":"Cysteine is the general base that serves in catalysis by isocitrate lyase and in mechanism-based inhibition by 3-nitropropionate","volume":"53","author":"Moynihan","year":"2014","journal-title":"Biochemistry"},{"key":"10.1016\/j.drudis.2017.04.012_bib0270","doi-asserted-by":"crossref","first-page":"11473","DOI":"10.1021\/acs.jpcb.5b04732","article-title":"Probing the catalytic mechanism involved in the isocitrate lyase superfamily: hybrid quantum mechanical\/molecular mechanical calculations on 2,3-dimethylmalate lyase","volume":"119","author":"Jongkon","year":"2015","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.drudis.2017.04.012_bib0275","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1007\/s002849900251","article-title":"Cysteine 195 has a critical functional role in catalysis by isocitrate lyase from Escherichia coli","volume":"35","author":"Rehman","year":"1997","journal-title":"Curr. Microbiol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0280","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.biochi.2014.12.016","article-title":"Insight into the structural flexibility and function of Mycobacterium tuberculosis isocitrate lyase","volume":"110","author":"Shukla","year":"2015","journal-title":"Biochimie"},{"key":"10.1016\/j.drudis.2017.04.012_bib0285","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/0014-5793(75)80289-4","article-title":"Reactivation by a bacteria acetate: enzyme ligase of plant glyoxysomal isocitrate lyase","volume":"58","author":"Geissler","year":"1975","journal-title":"FEBS Lett."},{"key":"10.1016\/j.drudis.2017.04.012_bib0290","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1111\/j.1432-1033.1973.tb02988.x","article-title":"Acetyl-CoA-dependent cleavage of citrate on inactivated citrate lyase","volume":"37","author":"Buckel","year":"1973","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0295","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1093\/oxfordjournals.jbchem.a135492","article-title":"Steady-state kinetic analysis of isocitrate lyase from Lupinus seeds: considerations on a possible catalytic mechanism of isocitrate lyase from plants","volume":"99","author":"Vincenzini","year":"1986","journal-title":"J. Biochem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0300","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1074\/mcp.M114.045922","article-title":"Succinylome analysis reveals the involvement of lysine succinylation in metabolism in pathogenic Mycobacterium tuberculosis","volume":"14","author":"Yang","year":"2015","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.drudis.2017.04.012_bib0305","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.biocel.2014.11.010","article-title":"Proteome-wide lysine acetylation profiling of the human pathogen Mycobacterium tuberculosis","volume":"59","author":"Xie","year":"2015","journal-title":"Int. J. Biochem. Cell. Biol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0310","doi-asserted-by":"crossref","first-page":"12527","DOI":"10.1038\/ncomms12527","article-title":"A rheostat mechanism governs the bifurcation of carbon flux in mycobacteria","volume":"7","author":"Murima","year":"2016","journal-title":"Nat. Commun."},{"key":"10.1016\/j.drudis.2017.04.012_bib0315","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1128\/jb.131.1.136-144.1977","article-title":"Itaconate, an isocitrate lyase directed inhibitor in Pseudomonas indigofera","volume":"131","author":"McFadden","year":"1977","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.drudis.2017.04.012_bib0320","doi-asserted-by":"crossref","first-page":"4420","DOI":"10.1021\/bi00261a035","article-title":"Inhibition of isocitrate lyase by 3-nitropropionate, a reaction-intermediate analogue","volume":"21","author":"Schloss","year":"1982","journal-title":"Biochemistry"},{"key":"10.1016\/j.drudis.2017.04.012_bib0325","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1016\/0003-9861(90)90273-2","article-title":"Alkylation of isocitrate lyase from Escherichia coli by 3-bromopyruvate","volume":"278","author":"Ko","year":"1990","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.drudis.2017.04.012_bib0330","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1002\/jps.3030360604","article-title":"Pharmacology of itaconic acid and its sodium, magnesium, and calcium salts","volume":"36","author":"Finkelstein","year":"1947","journal-title":"J. Am. Pharm. Assoc."},{"key":"10.1016\/j.drudis.2017.04.012_bib0335","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1016\/S0021-9258(18)55778-1","article-title":"The inhibitory effects of itaconic acid in vitro and in vivo","volume":"195","author":"Booth","year":"1952","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0340","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1016\/S0306-4522(97)00389-8","article-title":"3-Nitropropionic acid exacerbates N-methyl-d-aspartate toxicity in striatal culture by multiple mechanisms","volume":"84","author":"Greene","year":"1998","journal-title":"Neuroscience"},{"key":"10.1016\/j.drudis.2017.04.012_bib0345","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.bbrc.2004.09.047","article-title":"Advanced cancers: eradication in all cases using 3-bromopyruvate therapy to deplete ATP","volume":"324","author":"Ko","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.drudis.2017.04.012_bib0350","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1007\/s10863-012-9419-2","article-title":"3-bromopyruvate: targets and outcomes","volume":"44","author":"Shoshan","year":"2012","journal-title":"J. Bioenerg. Biomembr."},{"key":"10.1016\/j.drudis.2017.04.012_bib0355","doi-asserted-by":"crossref","first-page":"3767","DOI":"10.1073\/pnas.74.9.3767","article-title":"3-Nitropropionate, the toxic substance of Indigofera, is a suicide inactivator of succinate dehydrogenase","volume":"74","author":"Alston","year":"1977","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.drudis.2017.04.012_bib0360","doi-asserted-by":"crossref","first-page":"7820","DOI":"10.1073\/pnas.1218599110","article-title":"Immune-responsive gene 1 protein links metabolism to immunity by catalyzing itaconic acid production","volume":"110","author":"Michelucci","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.drudis.2017.04.012_bib0365","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1146\/annurev-nutr-071714-034243","article-title":"Itaconic acid: the surprising role of an industrial compound as a mammalian antimicrobial metabolite","volume":"35","author":"Cordes","year":"2015","journal-title":"Annu. Rev. Nutr."},{"key":"10.1016\/j.drudis.2017.04.012_bib0370","doi-asserted-by":"crossref","first-page":"2543","DOI":"10.1007\/s00044-013-0845-4","article-title":"Optimization of phage heptapeptide library-screening process for developing inhibitors of the isocitrate lyase homologue from Mycobacterium tuberculosis","volume":"23","author":"Liu","year":"2014","journal-title":"Med. Chem. Res."},{"key":"10.1016\/j.drudis.2017.04.012_bib0375","doi-asserted-by":"crossref","first-page":"114","DOI":"10.2174\/1872213X11307020003","article-title":"Isocitrate lyase: a potential target for anti-tubercular drugs: recent pat","volume":"7","author":"Sharma","year":"2013","journal-title":"Inflamm. Allergy Drug Discov."},{"key":"10.1016\/j.drudis.2017.04.012_bib0380","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1002\/ddr.20152","article-title":"A high throughput screening approach to identify isocitrate lyase inhibitors from traditional Chinese medicine sources","volume":"67","author":"Bai","year":"2006","journal-title":"Drug Dev. Res."},{"key":"10.1016\/j.drudis.2017.04.012_bib0385","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.tube.2009.05.008","article-title":"High-throughput screening for inhibitors of Mycobacterium tuberculosis H37Rv","volume":"89","author":"Ananthan","year":"2009","journal-title":"Tuberculosis"},{"key":"10.1016\/j.drudis.2017.04.012_bib0390","doi-asserted-by":"crossref","first-page":"376","DOI":"10.7150\/ijbs.7.376","article-title":"Identification of mannich base as a novel inhibitor of Mycobacterium tuberculosis isocitrate by high-throughput screening","volume":"7","author":"Ji","year":"2011","journal-title":"Int. J. Biol. Sci."},{"key":"10.1016\/j.drudis.2017.04.012_bib0395","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.tube.2015.12.003","article-title":"Identification of a novel inhibitor of isocitrate lyase as a potent antitubercular agent against both active and non-replicating Mycobacterium tuberculosis","volume":"97","author":"Liu","year":"2016","journal-title":"Tuberculosis"},{"key":"10.1016\/j.drudis.2017.04.012_bib0400","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.ejmech.2012.08.016","article-title":"Synthesis and in vitro antimycobacterial and isocitrate lyase inhibition properties of novel 2-methoxy-2\u2032-hydroxybenzanilides, their thioxo analogues and benzoxazoles","volume":"56","author":"Kozic","year":"2012","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0405","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/j.ejmech.2012.07.044","article-title":"Synthesis and in vitro antimycobacterial activity of 2-methoxybenzanilides and their thioxo analogues","volume":"56","author":"Kozic","year":"2012","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0410","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/j.tube.2012.06.001","article-title":"Salicylanilide derivatives block Mycobacterium tuberculosis through inhibition of isocitrate lyase and methionine aminopeptidase","volume":"92","author":"Kr\u00e1tk\u00fd","year":"2012","journal-title":"Tuberculosis"},{"key":"10.1016\/j.drudis.2017.04.012_bib0415","doi-asserted-by":"crossref","first-page":"4073","DOI":"10.1016\/j.bmc.2014.05.064","article-title":"Synthesis and biological activity of new salicylanilide NN-disubstituted carbamates and thiocarbamates","volume":"22","author":"Kr\u00e1tk\u00fd","year":"2014","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0420","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ejps.2013.12.001","article-title":"Salicylanilide pyrazinoates inhibit in vitro multidrug-resistant Mycobacterium tuberculosis strains, atypical mycobacteria and isocitrate lyase","volume":"53","author":"Kr\u00e1tk\u00fd","year":"2014","journal-title":"Eur. J. Pharm. Sci."},{"key":"10.1016\/j.drudis.2017.04.012_bib0425","doi-asserted-by":"crossref","first-page":"422","DOI":"10.2174\/157340609789117886","article-title":"Novel pthalazinyl derivatives: synthesis, antimycobacterial activities, and inhibition of Mycobacterium tuberculosis isocitrate lyase enzyme","volume":"5","author":"Sriram","year":"2009","journal-title":"Med. Chem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0430","doi-asserted-by":"crossref","first-page":"765","DOI":"10.3109\/14756360903425221","article-title":"5-Nitro-2,6-dioxohexahydro-4-pyrimidinecarboxamides: synthesis, in vitro antimycobacterial activity, cytotoxicity, and isocitrate lyase inhibition studies","volume":"25","author":"Sriram","year":"2010","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0435","doi-asserted-by":"crossref","first-page":"5149","DOI":"10.1016\/j.bmcl.2011.07.062","article-title":"Synthesis of various 3-nitropropionamides as Mycobacterium tuberculosis isocitrate lyase inhibitor","volume":"21","author":"Sriram","year":"2011","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.drudis.2017.04.012_bib0440","doi-asserted-by":"crossref","first-page":"4313","DOI":"10.1016\/j.bmcl.2010.06.096","article-title":"5-Nitro-2-furoic acid hydrazones: design, synthesis and in vitro antimycobacterial evaluation against log and starved phase cultures","volume":"20","author":"Sriram","year":"2010","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.drudis.2017.04.012_bib0445","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1111\/j.1747-0285.2010.00947.x","article-title":"Synthesis and antimycobacterial evaluation of novel phthalazin-4-ylacetamides against log- and starved phase cultures","volume":"75","author":"Sriram","year":"2010","journal-title":"Chem. Biol. Drug Des."},{"key":"10.1016\/j.drudis.2017.04.012_bib0450","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.ejmech.2010.10.020","article-title":"Novel isatinyl derivatives as potential molecule in the crusade against HIV-TB co-infection","volume":"46","author":"Banerjee","year":"2011","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0455","doi-asserted-by":"crossref","first-page":"6126","DOI":"10.2174\/0929867311209066126","article-title":"Advances in mycobacterial isocitrate lyase targeting and inhibitors","volume":"19","author":"Kr\u00e1tk\u00fd","year":"2012","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.drudis.2017.04.012_bib0460","first-page":"895453","article-title":"Potential inhibitors for isocitrate lyase of Mycobacterium tuberculosis and non-M. tuberculosis: a summary","volume":"2015","author":"Lee","year":"2015","journal-title":"BioMed Res. Int."}],"container-title":["Drug Discovery Today"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1359644617301903?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1359644617301903?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T12:31:49Z","timestamp":1761222709000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1359644617301903"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,7]]},"references-count":92,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2017,7]]}},"alternative-id":["S1359644617301903"],"URL":"https:\/\/doi.org\/10.1016\/j.drudis.2017.04.012","relation":{},"ISSN":["1359-6446"],"issn-type":[{"value":"1359-6446","type":"print"}],"subject":[],"published":{"date-parts":[[2017,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Targeting isocitrate lyase for the treatment of latent tuberculosis","name":"articletitle","label":"Article Title"},{"value":"Drug Discovery Today","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.drudis.2017.04.012","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}