메뉴 건너뛰기




Volumn 18, Issue 3, 2014, Pages 247-256

MmpL3 a potential new target for development of novel anti-tuberculosis drugs

Author keywords

Drug discovery; Drug target; Mycolic acid; Transporters

Indexed keywords

ANIMALS; ANTITUBERCULAR AGENTS; BACTERIAL PROTEINS; DRUG DESIGN; HUMANS; MEMBRANE TRANSPORT PROTEINS; MYCOBACTERIUM TUBERCULOSIS; TUBERCULOSIS;

EID: 84894136887     PISSN: 14728222     EISSN: 17447631     Source Type: Journal    
DOI: 10.1517/14728222.2014.859677     Document Type: Review
Times cited : (39)

References (79)
  • 1
    • 84894215562 scopus 로고    scopus 로고
    • WHO TB Report 2012. Available from: http://www.who.int/tb/country/en/ index. html
    • WHO TB Report 2012
  • 2
    • 77952542701 scopus 로고    scopus 로고
    • Multidrug-resistant and extensively drugresistant tuberculosis: A threat to global control of tuberculosis
    • Gandhi NR, Nunn P, Dheda K, et al. Multidrug-resistant and extensively drugresistant tuberculosis: a threat to global control of tuberculosis. Lancet 2010;375: 1830-43
    • (2010) Lancet , vol.375 , pp. 1830-1843
    • Gandhi, N.R.1    Nunn, P.2    Dheda, K.3
  • 4
    • 84871725540 scopus 로고    scopus 로고
    • Infectious disease: TB's revenge
    • Phillips L. Infectious disease: TB's revenge. Nature 2013;493: 14-16
    • (2013) Nature , vol.493 , pp. 14-16
    • Phillips, L.1
  • 5
    • 84894183756 scopus 로고    scopus 로고
    • Available from: http://www.who.int/tb/features-archive/new-treatment- guidelines-may2010/en/index.html
  • 6
    • 84860380179 scopus 로고    scopus 로고
    • New drugs for the treatment of tuberculosis: Needs, challenges, promise, and prospects for the future
    • Lienhardt C, Raviglione M, Spigelman M, et al. New drugs for the treatment of tuberculosis: needs, challenges, promise, and prospects for the future. J Infect Dis 2010;205:S241-9
    • (2010) J Infect Dis , vol.205
    • Lienhardt, C.1    Raviglione, M.2    Spigelman, M.3
  • 7
    • 84858389346 scopus 로고    scopus 로고
    • Outwitting evolution: Fighting drugresistant TB malaria and HIV
    • Goldberg DE, Siliciano RF, Jacobs WR. Outwitting evolution: fighting drugresistant TB, malaria, and HIV. Cell 2012;148(6): 1271-83
    • (2012) Cell , vol.148 , Issue.6 , pp. 1271-1283
    • Goldberg, D.E.1    Siliciano, R.F.2    Jacobs, W.R.3
  • 9
    • 84860368544 scopus 로고    scopus 로고
    • Drug-resistant tuberculosis - current dilemmas, unanswered questions, challenges, and priority needs
    • Zumla A, Abubakar I, Raviglione M, et al. Drug-resistant tuberculosis - current dilemmas, unanswered questions, challenges, and priority needs. J Infect Dis 2012;205(Suppl 2):S228-40
    • (2012) J Infect Dis , vol.205 , Issue.SUPPL. 2
    • Zumla, A.1    Abubakar, I.2    Raviglione, M.3
  • 10
    • 78449274705 scopus 로고    scopus 로고
    • Drugs in development for tuberculosis
    • Ginsberg AM. Drugs in development for tuberculosis. Drugs 2010;70(17): 2201-14
    • (2010) Drugs , vol.70 , Issue.17 , pp. 2201-2214
    • Ginsberg, A.M.1
  • 11
    • 53249084552 scopus 로고    scopus 로고
    • New antituberculosis drugs with novel mechanisms of action
    • Rivers EC, Mancera RL. New antituberculosis drugs with novel mechanisms of action. Curr Med Chem 2008;15(19): 1956-67
    • (2008) Curr Med Chem , vol.15 , Issue.19 , pp. 1956-1967
    • Rivers, E.C.1    Mancera, R.L.2
  • 12
  • 13
    • 78049452813 scopus 로고    scopus 로고
    • The mechanisms and consequences of the extra-pulmonary dissemination of Mycobacterium tuberculosis
    • Krishnan N, Robertson BD, Thwaites G. The mechanisms and consequences of the extra-pulmonary dissemination of Mycobacterium tuberculosis. Tuberculosis (Edinb) 2010;90(6): 361-6
    • (2010) Tuberculosis (Edinb) , vol.90 , Issue.6 , pp. 361-366
    • Krishnan, N.1    Robertson, B.D.2    Thwaites, G.3
  • 14
    • 84894126674 scopus 로고    scopus 로고
    • WHO TB/HIV Report. Available from: http://www.who.int/tb/challenges/hiv/ factsheets/en/index.html
    • WHO TB/HIV Report
  • 15
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole ST, Brosch R, Parkhill J, et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998;393(6685): 537-44
    • (1998) Nature , vol.393 , Issue.6685 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3
  • 16
    • 40849118255 scopus 로고    scopus 로고
    • Bacterial growth and cell division: A mycobacterial perspective
    • Hett EC, Rubin EJ. Bacterial growth and cell division: a mycobacterial perspective. Microbiol Mol Biol Rev 2008;72(1): 126-56
    • (2008) Microbiol Mol Biol Rev , vol.72 , Issue.1 , pp. 126-156
    • Hett, E.C.1    Rubin, E.J.2
  • 17
    • 84868090447 scopus 로고    scopus 로고
    • Targeting the mycobacterial envelope for tuberculosis drug development
    • Favrot L, Ronning DR. Targeting the mycobacterial envelope for tuberculosis drug development. Expert Rev Anti Infect Ther 2012;10(9): 1023-36
    • (2012) Expert Rev Anti Infect Ther , vol.10 , Issue.9 , pp. 1023-1036
    • Favrot, L.1    Ronning, D.R.2
  • 18
    • 0037844364 scopus 로고    scopus 로고
    • Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis
    • Brennan PJ. Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis. Tuberculosis (Edinburgh) 2003;83: 91-7
    • (2003) Tuberculosis (Edinburgh) , vol.83 , pp. 91-97
    • Brennan, P.J.1
  • 19
    • 12844278679 scopus 로고    scopus 로고
    • Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis
    • Takayama K, Wang C, Besra GS. Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis. Clin Microbiol Rev 2005;18(1): 81-101 • Extensive review of the mycolic acid biosynthesis.
    • (2005) Clin Microbiol Rev , vol.18 , Issue.1 , pp. 81-101
    • Takayama, K.1    Wang, C.2    Besra, G.S.3
  • 20
    • 69249187769 scopus 로고    scopus 로고
    • Biogenesis of the cell wall and other glycoconjugates of Mycobacterium tuberculosis
    • Kaur D, Guerin ME, Škovierová H, et al. Biogenesis of the cell wall and other glycoconjugates of Mycobacterium tuberculosis. Adv Appl Microbiol 2009;69: 23-78
    • (2009) Adv Appl Microbiol , vol.69 , pp. 23-78
    • Kaur, D.1    Guerin, M.E.2    Škovierová, H.3
  • 21
    • 41649116701 scopus 로고    scopus 로고
    • Disclosure of the mycobacterial outer membrane: Cryo-electron tomography and vitreous sections reveal the lipid bilayer structure
    • Hoffmann C, Leis A, Niederweis M, et al. Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure. Proc Natl Acad Sci USA 2008;105(10): 3963-7
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.10 , pp. 3963-3967
    • Hoffmann, C.1    Leis, A.2    Niederweis, M.3
  • 22
    • 84862262996 scopus 로고    scopus 로고
    • Towards understanding the functional diversity of cell wall mycolic acids of Mycobacterium tuberculosis
    • Verschoor JA, Baird MS, Grooten J. Towards understanding the functional diversity of cell wall mycolic acids of Mycobacterium tuberculosis. Prog Lipid Res 2012;51(4): 325-39
    • (2012) Prog Lipid Res , vol.51 , Issue.4 , pp. 325-339
    • Verschoor, J.A.1    Baird, M.S.2    Grooten, J.3
  • 23
    • 84863815961 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis lacking all mycolic acid cyclopropanation is viable but highly attenuated and hyperinflammatory in mice
    • Barkan D, Hedhli D, Yan HG, et al. Mycobacterium tuberculosis lacking all mycolic acid cyclopropanation is viable but highly attenuated and hyperinflammatory in mice. Infect Immun 2012;80(6): 1958-68
    • (2012) Infect Immun , vol.80 , Issue.6 , pp. 1958-1968
    • Barkan, D.1    Hedhli, D.2    Yan, H.G.3
  • 24
    • 78851469937 scopus 로고    scopus 로고
    • Molecular structure of the Mycobacterium tuberculosis virulence factor, mycolic acid, determines the elicited inflammatory pattern
    • Vander Beken S, Al Dulayymi JR, Naessens T, et al. Molecular structure of the Mycobacterium tuberculosis virulence factor, mycolic acid, determines the elicited inflammatory pattern. Eur J Immunol 2011;41(2): 450-60
    • (2011) Eur J Immunol , vol.41 , Issue.2 , pp. 450-460
    • Vander Beken, S.1    Al Dulayymi, J.R.2    Naessens, T.3
  • 25
    • 0031694056 scopus 로고    scopus 로고
    • The effect of oxygenated mycolic acid composition on cell wall function and macrophage growth in Mycobacterium tuberculosis
    • Yuan Y, Zhu Y, Crane DD, Barry CE III. The effect of oxygenated mycolic acid composition on cell wall function and macrophage growth in Mycobacterium tuberculosis. Mol Microbiol 1998;29(6): 1449-58
    • (1998) Mol Microbiol , vol.29 , Issue.6 , pp. 1449-1458
    • Yuan, Y.1    Zhu, Y.2    Crane, D.D.3    Barry III, C.E.4
  • 26
    • 0034073375 scopus 로고    scopus 로고
    • Oxygenated mycolic acids are necessary for virulence of Mycobacterium tuberculosis in mice
    • Dubnau E, Chan J, Raynaud C, et al. Oxygenated mycolic acids are necessary for virulence of Mycobacterium tuberculosis in mice. Mol Microbiol 2000;36(3): 630
    • (2000) Mol Microbiol , vol.36 , Issue.3 , pp. 630
    • Dubnau, E.1    Chan, J.2    Raynaud, C.3
  • 27
    • 4544275674 scopus 로고    scopus 로고
    • Microbial type i fatty acid synthases (FAS): Major players in a network of cellular FAS systems
    • Schweizer E, Hofmann J. Microbial type I fatty acid synthases (FAS): major players in a network of cellular FAS systems. Microbiol Mol Biol Rev 2004;68(3): 501-17
    • (2004) Microbiol Mol Biol Rev , vol.68 , Issue.3 , pp. 501-517
    • Schweizer, E.1    Hofmann, J.2
  • 28
    • 34250198660 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis FAS-II condensing enzymes: Their role in mycolic acid biosynthesis, acid-fastness, pathogenesis and in future drug development
    • Bhatt A, Molle V, Besra GS, et al. The Mycobacterium tuberculosis FAS-II condensing enzymes: their role in mycolic acid biosynthesis, acid-fastness, pathogenesis and in future drug development. Mol Microbiol 2007;64(6): 1442-54
    • (2007) Mol Microbiol , vol.64 , Issue.6 , pp. 1442-1454
    • Bhatt, A.1    Molle, V.2    Besra, G.S.3
  • 29
    • 12344300344 scopus 로고    scopus 로고
    • The reductase steps of the type II fatty acid synthase as antimicrobial targets
    • Zhang YM, Lu YJ, Rock CO. The reductase steps of the type II fatty acid synthase as antimicrobial targets. Lipids 2004;39(11): 1055-60
    • (2004) Lipids , vol.39 , Issue.11 , pp. 1055-1060
    • Zhang, Y.M.1    Lu, Y.J.2    Rock, C.O.3
  • 30
    • 0035861550 scopus 로고    scopus 로고
    • Purification and biochemical characterization of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthases KasA and KasB
    • Schaeffer ML, Agnihotri G, Volker C, et al. Purification and biochemical characterization of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthases KasA and KasB. J Biol Chem 2001;276(50): 47029-37
    • (2001) J Biol Chem , vol.276 , Issue.50 , pp. 47029-47037
    • Schaeffer, M.L.1    Agnihotri, G.2    Volker, C.3
  • 31
    • 35548929836 scopus 로고    scopus 로고
    • The missing piece of the type II fatty acid synthase system from Mycobacterium tuberculosis
    • Sacco E, Covarrubias AS, O'Hare HM, et al. The missing piece of the type II fatty acid synthase system from Mycobacterium tuberculosis. Proc Natl Acad Sci USA 2007;104(37): 14628-33
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.37 , pp. 14628-14633
    • Sacco, E.1    Covarrubias, A.S.2    O'Hare, H.M.3
  • 32
    • 0347719360 scopus 로고    scopus 로고
    • A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms
    • Portevin D, De Sousa-D'Auria C, Houssin C, et al. A polyketide synthase catalyzes the last condensation step of mycolic acid biosynthesis in mycobacteria and related organisms. Proc Natl Acad Sci USA 2004;101(1): 314-19
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.1 , pp. 314-319
    • Portevin, D.1    De Sousa-D'Auria, C.2    Houssin, C.3
  • 33
    • 0036020524 scopus 로고    scopus 로고
    • Drugs that inhibit mycolic acid biosynthesis in Mycobacterium tuberculosis
    • Schroeder EK, de Souza N, Santos DS, et al. Drugs that inhibit mycolic acid biosynthesis in Mycobacterium tuberculosis. Curr Pharm Biotechnol 2002;3(3): 197-225
    • (2002) Curr Pharm Biotechnol , vol.3 , Issue.3 , pp. 197-225
    • Schroeder, E.K.1    De Souza, N.2    Santos, D.S.3
  • 34
    • 0033962136 scopus 로고    scopus 로고
    • InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II
    • Marrakchi H, Lanéelle G, Quémard A. InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II. Microbiology 2000;146(Pt 2): 289-96
    • (2000) Microbiology , vol.146 , Issue.PART 2 , pp. 289-296
    • Marrakchi, H.1    Lanéelle, G.2    Quémard, A.3
  • 35
    • 84869029377 scopus 로고    scopus 로고
    • A common mechanism of inhibition of the Mycobacterium tuberculosis mycolic acid biosynthetic pathway by isoxyl and thiacetazone
    • Grzegorzewicz AE, Korduláková J, Jones V, et al. A common mechanism of inhibition of the Mycobacterium tuberculosis mycolic acid biosynthetic pathway by isoxyl and thiacetazone. J Biol Chem 2012;287(46): 38434-41
    • (2012) J Biol Chem , vol.287 , Issue.46 , pp. 38434-38441
    • Grzegorzewicz, A.E.1    Korduláková, J.2    Jones, V.3
  • 36
    • 84868125770 scopus 로고    scopus 로고
    • Mutations in the essential FAS II betahydroxyacyl ACP dehydratase complex confer resistance to thiacetazone in Mycobacterium tuberculosis and Mycobacterium kansasii
    • Belardinelli JM, Morbidoni HR. Mutations in the essential FAS II betahydroxyacyl ACP dehydratase complex confer resistance to thiacetazone in Mycobacterium tuberculosis and Mycobacterium kansasii. Mol Microbiol 2012;86(3): 568-79
    • (2012) Mol Microbiol , vol.86 , Issue.3 , pp. 568-579
    • Belardinelli, J.M.1    Morbidoni, H.R.2
  • 37
    • 60849124512 scopus 로고    scopus 로고
    • Triclosan derivatives: Towards potent inhibitors of drug-sensitive and drug-resistant Mycobacterium tuberculosis
    • Freundlich JS, Wang F, Vilchèze C, et al. Triclosan derivatives: towards potent inhibitors of drug-sensitive and drug-resistant Mycobacterium tuberculosis. ChemMedChem 2009;4(2): 241-8
    • (2009) Chem Med Chem , vol.4 , Issue.2 , pp. 241-248
    • Freundlich, J.S.1    Wang, F.2    Vilchèze, C.3
  • 38
    • 17644436310 scopus 로고    scopus 로고
    • Inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis, by triclosan and isoniazid
    • Parikh SL, Xiao G, Tonge PJ. Inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis, by triclosan and isoniazid. Biochemistry 2000;39(26): 7645-50
    • (2000) Biochemistry , vol.39 , Issue.26 , pp. 7645-7650
    • Parikh, S.L.1    Xiao, G.2    Tonge, P.J.3
  • 39
    • 0034595879 scopus 로고    scopus 로고
    • Thiolactomycin and related analogues as novel anti-mycobacterial agents targeting KasA and KasB condensing enzymes in Mycobacterium tuberculosis
    • Kremer L, Douglas JD, Baulard AR, et al. Thiolactomycin and related analogues as novel anti-mycobacterial agents targeting KasA and KasB condensing enzymes in Mycobacterium tuberculosis. J Biol Chem 2000;275(22): 16857-64
    • (2000) J Biol Chem , vol.275 , Issue.22 , pp. 16857-16864
    • Kremer, L.1    Douglas, J.D.2    Baulard, A.R.3
  • 40
    • 0041922652 scopus 로고    scopus 로고
    • Signature gene expression profiles discriminate between isoniazid-, thiolactomycin-, and triclosan-treated Mycobacterium tuberculosis
    • Betts JC, McLaren A, Lennon MG, et al. Signature gene expression profiles discriminate between isoniazid-, thiolactomycin-, and triclosan-treated Mycobacterium tuberculosis. Antimicrob Agents Chemother 2003;47(9): 2903-13
    • (2003) Antimicrob Agents Chemother , vol.47 , Issue.9 , pp. 2903-2913
    • Betts, J.C.1    McLaren, A.2    Lennon, M.G.3
  • 41
    • 0031007903 scopus 로고    scopus 로고
    • Role of the major antigen of Mycobacterium tuberculosis in cell wall biogenesis
    • Belisle JT, Vissa VD, Sievert T, et al. Role of the major antigen of Mycobacterium tuberculosis in cell wall biogenesis. Science 1997;276(5317): 1420-2
    • (1997) Science , vol.276 , Issue.5317 , pp. 1420-1422
    • Belisle, J.T.1    Vissa, V.D.2    Sievert, T.3
  • 42
    • 0033960935 scopus 로고    scopus 로고
    • Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines
    • Ronning DR, Klabunde T, Besra GS, et al. Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines. Nat Struct Biol 2000;7(2): 141-6
    • (2000) Nat Struct Biol , vol.7 , Issue.2 , pp. 141-146
    • Ronning, D.R.1    Klabunde, T.2    Besra, G.S.3
  • 43
    • 84858692080 scopus 로고    scopus 로고
    • Antigen 85C inhibition restricts Mycobacterium tuberculosis growth through disruption of cord factor biosynthesis
    • Warrier T, Tropis M, Werngren J, et al. Antigen 85C inhibition restricts Mycobacterium tuberculosis growth through disruption of cord factor biosynthesis. Antimicrob Agents Chemother 2012;56(4): 1735-43
    • (2012) Antimicrob Agents Chemother , vol.56 , Issue.4 , pp. 1735-1743
    • Warrier, T.1    Tropis, M.2    Werngren, J.3
  • 44
    • 84860181497 scopus 로고    scopus 로고
    • MmpL genes are associated with mycolic acid metabolism in mycobacteria and corynebacteria
    • Varela C, Rittmann D, Singh A, et al. MmpL genes are associated with mycolic acid metabolism in mycobacteria and corynebacteria. Chem Biol 2012;19(4): 498-506 • Genetic evidence to suggest MmpL3 as a transporter of mycolic acids.
    • (2012) Chem Biol , vol.19 , Issue.4 , pp. 498-506
    • Varela, C.1    Rittmann, D.2    Singh, A.3
  • 45
  • 46
    • 79956087446 scopus 로고    scopus 로고
    • Switch or funnel: How RNDtype transport systems control periplasmic metal homeostasis
    • Kim EH, Nies DH, McEvoy MM, Rensing C. Switch or funnel: how RNDtype transport systems control periplasmic metal homeostasis. J Bacteriol 2011;193(10): 2381-7
    • (2011) J Bacteriol , vol.193 , Issue.10 , pp. 2381-2387
    • Kim, E.H.1    Nies, D.H.2    McEvoy, M.M.3    Rensing, C.4
  • 47
    • 19744376797 scopus 로고    scopus 로고
    • Contribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistance
    • Domenech P, Reed MB, Barry CE III. Contribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistance. Infect Immun 2005;73(6): 3492-501 • Article demonstrating essentiality of MmpL3 to Mtb.
    • (2005) Infect Immun , vol.73 , Issue.6 , pp. 3492-3501
    • Domenech, P.1    Reed, M.B.2    Barry III, C.E.3
  • 48
    • 0032708648 scopus 로고    scopus 로고
    • Analysis of the proteome of Mycobacterium tuberculosis in silico
    • Tekaia F, Gordon SV, Garnier T, et al. Analysis of the proteome of Mycobacterium tuberculosis in silico. Tuber Lung Dis 1999;79(6): 329-42
    • (1999) Tuber Lung Dis , vol.79 , Issue.6 , pp. 329-342
    • Tekaia, F.1    Gordon, S.V.2    Garnier, T.3
  • 49
    • 0038623770 scopus 로고    scopus 로고
    • MmpL8 is required for sulfolipid-1 biosynthesis and Mycobacterium tuberculosis virulence
    • Converse SE, Mougous JD, Leavell MD, et al. MmpL8 is required for sulfolipid-1 biosynthesis and Mycobacterium tuberculosis virulence. Proc Natl Acad Sci USA 2003;100(10): 6121-6
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.10 , pp. 6121-6126
    • Converse, S.E.1    Mougous, J.D.2    Leavell, M.D.3
  • 50
    • 2442686856 scopus 로고    scopus 로고
    • The role of MmpL8 in sulfatide biogenesis and virulence of Mycobacterium tuberculosis
    • Domenech P, Reed MB, Dowd CS, et al. The role of MmpL8 in sulfatide biogenesis and virulence of Mycobacterium tuberculosis. J Biol Chem 2004;279(20): 21257-65
    • (2004) J Biol Chem , vol.279 , Issue.20 , pp. 21257-21265
    • Domenech, P.1    Reed, M.B.2    Dowd, C.S.3
  • 51
    • 33746680377 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis transporter MmpL7 is a potential substrate for kinase PknD
    • Pérez J, Garcia R, Bach H, et al. Mycobacterium tuberculosis transporter MmpL7 is a potential substrate for kinase PknD. Biochem Biophys Res Commun 2006;348(1): 6-12
    • (2006) Biochem Biophys Res Commun , vol.348 , Issue.1 , pp. 6-12
    • Pérez, J.1    Garcia, R.2    Bach, H.3
  • 52
    • 79953175298 scopus 로고    scopus 로고
    • Discovery and characterization of a unique mycobacterial heme acquisition system
    • Tullius MV, Harmston CA, Owens CP, et al. Discovery and characterization of a unique mycobacterial heme acquisition system. Proc Natl Acad Sci USA 2011;108(12): 5051-6 • Implication of MmpL3 and 11 in heme transport.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.12 , pp. 5051-5056
    • Tullius, M.V.1    Harmston, C.A.2    Owens, C.P.3
  • 53
    • 84881232776 scopus 로고    scopus 로고
    • The mycobacterium tuberculosis secreted protein Rv0203 transfers Heme to membrane proteins MmpL3 and MmpL11
    • Owens CP, Chim N, Graves AB, et al. The mycobacterium tuberculosis secreted protein Rv0203 transfers Heme to membrane proteins MmpL3 and MmpL11. J Biol Chem 2013;288(30): 21714-28 • Evidence for heme binding by MmpL3.
    • (2013) J Biol Chem , vol.288 , Issue.30 , pp. 21714-21728
    • Owens, C.P.1    Chim, N.2    Graves, A.B.3
  • 54
    • 84881498792 scopus 로고    scopus 로고
    • Insights on how the Mycobacterium tuberculosis heme uptake pathway can be used as a drug target
    • Owens CP, Chim N, Goulding CW. Insights on how the Mycobacterium tuberculosis heme uptake pathway can be used as a drug target. Fut Med Chem 2013;5(12): 1391-403
    • (2013) Fut Med Chem , vol.5 , Issue.12 , pp. 1391-1403
    • Owens, C.P.1    Chim, N.2    Goulding, C.W.3
  • 55
    • 84858677107 scopus 로고    scopus 로고
    • Inhibition of mycolic acid transport across the Mycobacterium tuberculosis plasma membrane
    • Grzegorzewicz AE, Pham H, Gundi VA, et al. Inhibition of mycolic acid transport across the Mycobacterium tuberculosis plasma membrane. Nat Chem Biol 2012;8(4): 334-41 • First paper demonstrating involvement of MmpL3 in mycolic acid transport.
    • (2012) Nat Chem Biol , vol.8 , Issue.4 , pp. 334-341
    • Grzegorzewicz, A.E.1    Pham, H.2    Gundi, V.A.3
  • 56
    • 84876129597 scopus 로고    scopus 로고
    • Design synthesis and antituberculosis activity of 1-adamantyl-3- heteroaryl ureas with improved in vitro pharmacokinetic properties
    • North EJ, Scherman MS, Bruhn DF, et al. Design, synthesis and antituberculosis activity of 1-adamantyl-3- heteroaryl ureas with improved in vitro pharmacokinetic properties. Bioorg Med Chem 2013;21(9): 2587-99
    • (2013) Bioorg Med Chem , vol.21 , Issue.9 , pp. 2587-2599
    • North, E.J.1    Scherman, M.S.2    Bruhn, D.F.3
  • 57
    • 0031753303 scopus 로고    scopus 로고
    • Bactericidal activities of the pyrrole derivative BM212 against multidrugresistant and intramacrophagic Mycobacterium tuberculosis strains
    • Deidda D, Lampis G, Fioravanti R, et al. Bactericidal activities of the pyrrole derivative BM212 against multidrugresistant and intramacrophagic Mycobacterium tuberculosis strains. Antimicrob Agents Chemother 1998;42(11): 3035-7
    • (1998) Antimicrob Agents Chemother , vol.42 , Issue.11 , pp. 3035-3037
    • Deidda, D.1    Lampis, G.2    Fioravanti, R.3
  • 58
    • 84455173193 scopus 로고    scopus 로고
    • MmpL3 is the cellular target of the antitubercular pyrrole derivative BM212
    • La Rosa V, Poce G, Canseco JO, et al. MmpL3 is the cellular target of the antitubercular pyrrole derivative BM212. Antimicrob Agents Chemother 2012;56(1): 324-31 • Identification of target for BM212.
    • (2012) Antimicrob Agents Chemother , vol.56 , Issue.1 , pp. 324-331
    • La Rosa, V.1    Poce, G.2    Canseco, J.O.3
  • 59
    • 84874297088 scopus 로고    scopus 로고
    • Improved BM212 MmpL3 inhibitor analogue shows efficacy in acute murine model of tuberculosis infection
    • Poce G, Bates RH, Alfonso S, et al. Improved BM212 MmpL3 inhibitor analogue shows efficacy in acute murine model of tuberculosis infection. PLoS One 2013;8(2):e56980
    • (2013) PLoS One , vol.8 , Issue.2
    • Poce, G.1    Bates, R.H.2    Alfonso, S.3
  • 60
    • 13244283085 scopus 로고    scopus 로고
    • Pharmacodynamics and pharmacokinetics of SQ109, a new diamine-based antitubercular drug
    • Jia L, Tomaszewski JE, Hanrahan C, et al. Pharmacodynamics and pharmacokinetics of SQ109, a new diamine-based antitubercular drug. Br J Pharmacol 2005;144: 80-7
    • (2005) Br J Pharmacol , vol.144 , pp. 80-87
    • Jia, L.1    Tomaszewski, J.E.2    Hanrahan, C.3
  • 61
    • 84863404695 scopus 로고    scopus 로고
    • SQ109 targets MmpL3, a membrane transporter of trehalose monomycolate involved in mycolic acid donation to the cell wall core of Mycobacterium tuberculosis
    • Tahlan K, Wilson R, Kastrinsky DB, et al. SQ109 targets MmpL3, a membrane transporter of trehalose monomycolate involved in mycolic acid donation to the cell wall core of Mycobacterium tuberculosis. Antimicrob Agents Chemother 2012;56(4): 1797-809 • Identification of mechanism of action of SQ109.
    • (2012) Antimicrob Agents Chemother , vol.56 , Issue.4 , pp. 1797-1809
    • Tahlan, K.1    Wilson, R.2    Kastrinsky, D.B.3
  • 62
    • 84865253965 scopus 로고    scopus 로고
    • Identification of novel inhibitors of M. Tuberculosis growth using whole cell based high-throughput screening
    • Stanley SA, Grant SS, Kawate T, et al. Identification of novel inhibitors of M. tuberculosis growth using whole cell based high-throughput screening. ACS Chem Biol 2012;7(8): 1377-84 • Identification of MmpL3 and DprE1 inhibitors from whole cell screening.
    • (2012) ACS Chem Biol , vol.7 , Issue.8 , pp. 1377-1384
    • Stanley, S.A.1    Grant, S.S.2    Kawate, T.3
  • 63
    • 84876272210 scopus 로고    scopus 로고
    • Tetrahydropyrazolo[15-A] Pyrimidine-3-Carboxamide and NBenzyl- 6'7'-Dihydrospiro[ Piperidine- 44'-Thieno[32-c]Pyran] Analogues with Bactericidal Efficacy against Mycobacterium tuberculosis Targeting MmpL3
    • Remuiñán MJ, Pérez-Herrán E, Rullás J, et al. Tetrahydropyrazolo[1,5-a] Pyrimidine-3-Carboxamide and NBenzyl- 6',7'-Dihydrospiro[ Piperidine- 4,4'-Thieno[3,2-c]Pyran] Analogues with Bactericidal Efficacy against Mycobacterium tuberculosis Targeting MmpL3. PLoS One 2013;8(4):e60933 • Two novel inhibitors of MmpL3 showing in vivo efficacy.
    • (2013) PLoS One , vol.8 , Issue.4
    • Remuiñán, M.J.1    Pérez-Herrán, E.2    Rullás, J.3
  • 64
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami S, Nakashima R, Yamashita E, Yamaguchi A. Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 2002;419(6907): 587-93
    • (2002) Nature , vol.419 , Issue.6907 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 65
    • 0036889033 scopus 로고    scopus 로고
    • Substrate specificity of the RND-type multidrug efflux pumps AcrB and AcrD of Escherichia coli is determined predominantly by two large periplasmic loops
    • Elkins CA, Nikaido H. Substrate specificity of the RND-type multidrug efflux pumps AcrB and AcrD of Escherichia coli is determined predominantly by two large periplasmic loops. J Bacteriol 2002;184(23): 6490-8
    • (2002) J Bacteriol , vol.184 , Issue.23 , pp. 6490-6498
    • Elkins, C.A.1    Nikaido, H.2
  • 66
    • 0038670226 scopus 로고    scopus 로고
    • Structural basis of multiple drugbinding capacity of the AcrB multidrug efflux pump
    • Yu EW, McDermott G, Zgurskaya HI, et al. Structural basis of multiple drugbinding capacity of the AcrB multidrug efflux pump. Science 2003;300(5621): 976-80
    • (2003) Science , vol.300 , Issue.5621 , pp. 976-980
    • Yu, E.W.1    McDermott, G.2    Zgurskaya, H.I.3
  • 67
    • 0141615783 scopus 로고    scopus 로고
    • AcrB multidrug efflux pump of Escherichia coli: Composite substrate-binding cavity of exceptional flexibility generates its extremely wide substrate specificity
    • Yu EW, Aires JR, Nikaido H. AcrB multidrug efflux pump of Escherichia coli: composite substrate-binding cavity of exceptional flexibility generates its extremely wide substrate specificity. J Bacteriol 2003;185(19): 5657-64
    • (2003) J Bacteriol , vol.185 , Issue.19 , pp. 5657-5664
    • Yu, E.W.1    Aires, J.R.2    Nikaido, H.3
  • 68
    • 84858626341 scopus 로고    scopus 로고
    • Infectious diseases: Transporter targeted in tuberculosis
    • Cole ST. Infectious diseases: transporter targeted in tuberculosis. Nat Chem Biol 2012;8(4): 326-7
    • (2012) Nat Chem Biol , vol.8 , Issue.4 , pp. 326-327
    • Cole, S.T.1
  • 69
    • 84877267006 scopus 로고    scopus 로고
    • Advances in the development of new tuberculosis drugs and treatment regimens
    • Zumla A, Nahid P, Cole ST. Advances in the development of new tuberculosis drugs and treatment regimens. Nat Rev Drug Discov 2013;12(5): 388-404 • Review article covering novel targets like MmpL3 and DprE1.
    • (2013) Nat Rev Drug Discov , vol.12 , Issue.5 , pp. 388-404
    • Zumla, A.1    Nahid, P.2    Cole, S.T.3
  • 70
    • 33646937005 scopus 로고    scopus 로고
    • Interaction between polyketide synthase and transporter suggests coupled synthesis and export of virulence lipid in M. Tuberculosis
    • Jain M, Cox JS. Interaction between polyketide synthase and transporter suggests coupled synthesis and export of virulence lipid in M. tuberculosis. PLoS Pathog 2005;1(1):e2
    • (2005) PLoS Pathog , vol.1 , Issue.1
    • Jain, M.1    Cox, J.S.2
  • 71
    • 84881309351 scopus 로고    scopus 로고
    • Hitting the tuberculosis wall
    • Harrison C. Hitting the tuberculosis wall. Nat Rev Drug Discov 2013;12: 578-9
    • (2013) Nat Rev Drug Discov , vol.12 , pp. 578-579
    • Harrison, C.1
  • 72
    • 73649143180 scopus 로고    scopus 로고
    • High content screening identifies decaprenyl-phosphoribose 2' epimerase as a target for intracellular antimycobacterial inhibitors
    • Christophe T, Jackson M, Jeon HK, et al. High content screening identifies decaprenyl-phosphoribose 2' epimerase as a target for intracellular antimycobacterial inhibitors. PLoS Pathog 2009;5(10):e1000645
    • (2009) PLoS Pathog , vol.5 , Issue.10
    • Christophe, T.1    Jackson, M.2    Jeon, H.K.3
  • 73
    • 77955626451 scopus 로고    scopus 로고
    • Decaprenylphosphoryl-b-D-ribose 2'- epimerase from Mycobacterium tuberculosis is a magic drug target
    • Manina G, Pasca MR, Buroni S, et al. Decaprenylphosphoryl-b-D-ribose 2'- epimerase from Mycobacterium tuberculosis is a magic drug target. Curr Med Chem 2010;17(27): 3099-108
    • (2010) Curr Med Chem , vol.17 , Issue.27 , pp. 3099-3108
    • Manina, G.1    Pasca, M.R.2    Buroni, S.3
  • 74
    • 78049483746 scopus 로고    scopus 로고
    • Leads for antitubercular compounds from kinase inhibitor library screens
    • Magnet S, Hartkoorn RC, Székely R, et al. Leads for antitubercular compounds from kinase inhibitor library screens. Tuberculosis (Edinb) 2010;90(6): 354-60
    • (2010) Tuberculosis (Edinb) , vol.90 , Issue.6 , pp. 354-360
    • Magnet, S.1    Hartkoorn, R.C.2    Székely, R.3
  • 75
    • 79951566404 scopus 로고    scopus 로고
    • Decaprenylphosphoryl-beta- D-ribose 2'-epimerase the target of benzothiazinones and dinitrobenzamides is an essential enzyme in Mycobacterium smegmatis
    • Crellin PK, Brammananth R, Coppel RL. Decaprenylphosphoryl-beta- D-ribose 2'-epimerase, the target of benzothiazinones and dinitrobenzamides, is an essential enzyme in Mycobacterium smegmatis. PLoS One 2011;6(2):e16869
    • (2011) PLoS One , vol.6 , Issue.2
    • Crellin, P.K.1    Brammananth, R.2    Coppel, R.L.3
  • 76
    • 84863919677 scopus 로고    scopus 로고
    • Structural basis of inhibition of Mycobacterium tuberculosis DprE1 by benzothiazinone inhibitors
    • Batt SM, Jabeen T, Bhowruth V, et al. Structural basis of inhibition of Mycobacterium tuberculosis DprE1 by benzothiazinone inhibitors. Proc Natl Acad Sci USA 2012;109(28): 11354-9
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.28 , pp. 11354-11359
    • Batt, S.M.1    Jabeen, T.2    Bhowruth, V.3
  • 77
    • 84855948516 scopus 로고    scopus 로고
    • Benzothiazinones are suicide inhibitors of mycobacterial decaprenylphosphoryl-beta- D-ribofuranose 2'-oxidase DprE1
    • Trefzer C, Škovierová H, Buroni S, et al. Benzothiazinones are suicide inhibitors of mycobacterial decaprenylphosphoryl-beta- D-ribofuranose 2'-oxidase DprE1. J Am Chem Soc 2012;134(2): 912-15
    • (2012) J Am Chem Soc , vol.134 , Issue.2 , pp. 912-915
    • Trefzer, C.1    Škovierová, H.2    Buroni, S.3
  • 78
    • 84879707160 scopus 로고    scopus 로고
    • Identification of a small molecule with activity against drug-resistant and persistent tuberculosis
    • Wang F, Sambandan D, Halder R, et al. Identification of a small molecule with activity against drug-resistant and persistent tuberculosis. Proc Natl Acad Sci USA 2013;110(27):E2510-17
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.27
    • Wang, F.1    Sambandan, D.2    Halder, R.3
  • 79
    • 65649096556 scopus 로고    scopus 로고
    • Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis
    • Makarov V, Manina G, Mikusova K, et al. Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis. Science 2009;324(5928): 801-4
    • (2009) Science , vol.324 , Issue.5928 , pp. 801-804
    • Makarov, V.1    Manina, G.2    Mikusova, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.