메뉴 건너뛰기




Volumn 7, Issue 5, 2007, Pages 489-498

Development of modern InhA inhibitors to combat drug resistant strains of Mycobacterium tuberculosis

Author keywords

Cell wall; Diphenyl ether; Enoyl reductase; Fatty acid biosynthesis; InhA; Isoniazid; Mycobacterium; Mycolic acid; Triclosan

Indexed keywords

5 BUTYL 2 PHENOXYPHENOL; 5 ETHYL 2 PHENOXYPHENOL; 5 HEXYL 2 PHENOXYPHENOL; 5 OCTYL 2 PHENOXYPHENOL; 5 PENTYL 2 PHENOXYPHENOL; 5 TETRADECYL 2 PHENOXYPHENOL; ANTIINFECTIVE AGENT; CERULENIN; DIPHENYL ETHER; ENOYL REDUCTASE INHIBITOR; ENZYME INHIBITOR; ETHAMBUTOL; FATTY ACID; ISONIAZID; PIPERAZINE DERIVATIVE; THIENODIAZABORINE; THIOLACTOMYCIN; TRICLOSAN; TUBERCULOSTATIC AGENT; UNCLASSIFIED DRUG;

EID: 33947651030     PISSN: 15680266     EISSN: None     Source Type: Journal    
DOI: 10.2174/156802607780059781     Document Type: Review
Times cited : (45)

References (78)
  • 1
    • 0026026102 scopus 로고
    • The global tuberculosis situation and the new control strategy of the World Health Organization
    • Kochi, A. The global tuberculosis situation and the new control strategy of the World Health Organization. Tubercle 1991, 72 (1), 1-6.
    • (1991) Tubercle , vol.72 , Issue.1 , pp. 1-6
    • Kochi, A.1
  • 2
    • 0026686943 scopus 로고
    • Tuberculosis: Commentary on a reemergent killer
    • Bloom, B. R.; Murray, C. J. Tuberculosis: commentary on a reemergent killer. Science 1992, 257 (5073), 1055-64.
    • (1992) Science , vol.257 , Issue.5073 , pp. 1055-1064
    • Bloom, B.R.1    Murray, C.J.2
  • 3
    • 0031254565 scopus 로고    scopus 로고
    • Susceptibility to levofloxacin of Mycobacterium tuberculosis isolates from patients with HIV-related tuberculosis and characterization of a strain with levofloxacin monoresistance
    • Perlman, D. C.; ElSadr, W. M.; Heifets, L. B.; Nelson, E. T.; Matts, J. P.; Chirgwin, K.; Salomon, N.; Telzak, E. E.; Klein, O.; Kreiswirth, B. N.; Musser, J. M.; Hafner, R. Susceptibility to levofloxacin of Mycobacterium tuberculosis isolates from patients with HIV-related tuberculosis and characterization of a strain with levofloxacin monoresistance. Aids 1997, 11 (12), 1473-1478.
    • (1997) Aids , vol.11 , Issue.12 , pp. 1473-1478
    • Perlman, D.C.1    ElSadr, W.M.2    Heifets, L.B.3    Nelson, E.T.4    Matts, J.P.5    Chirgwin, K.6    Salomon, N.7    Telzak, E.E.8    Klein, O.9    Kreiswirth, B.N.10    Musser, J.M.11    Hafner, R.12
  • 4
    • 0031862229 scopus 로고    scopus 로고
    • Multidrug-resistant Mycobacterium tuberculosis: Molecular perspectives
    • Rattan, A.; Kalia, A.; Ahmad, N. Multidrug-resistant Mycobacterium tuberculosis: molecular perspectives. Emerg. Infect. Dis. 1998, 4 (2), 195-209.
    • (1998) Emerg. Infect. Dis. , vol.4 , Issue.2 , pp. 195-209
    • Rattan, A.1    Kalia, A.2    Ahmad, N.3
  • 6
    • 3042817281 scopus 로고    scopus 로고
    • Tuberculosis as a major global health problem in the 21st century: A WHO perspective
    • Gupta, R.; Espinal, M. A.; Raviglione, M. C. Tuberculosis as a major global health problem in the 21st century: a WHO perspective. Semin. Respir. Crit. Care Med. 2004, 25 (3), 245-53.
    • (2004) Semin. Respir. Crit. Care Med. , vol.25 , Issue.3 , pp. 245-253
    • Gupta, R.1    Espinal, M.A.2    Raviglione, M.C.3
  • 9
    • 0036322591 scopus 로고    scopus 로고
    • Mycobacterium and the coat of many lipids
    • Russell, D. G.; Mwandumba, H. C.; Rhoades, E. E. Mycobacterium and the coat of many lipids. J. Cell. Biol. 2002, 158 (3), 421-6.
    • (2002) J. Cell. Biol. , vol.158 , Issue.3 , pp. 421-426
    • Russell, D.G.1    Mwandumba, H.C.2    Rhoades, E.E.3
  • 10
    • 0026705772 scopus 로고
    • The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis
    • Zhang, Y.; Heym, B.; Allen, B.; Young, D.; Cole, S. The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature 1992, 358 (6387), 591-3.
    • (1992) Nature , vol.358 , Issue.6387 , pp. 591-593
    • Zhang, Y.1    Heym, B.2    Allen, B.3    Young, D.4    Cole, S.5
  • 12
    • 0027993499 scopus 로고
    • Mechanistic Studies of the Oxidation of Isoniazid by the Catalase Peroxidase from Mycobacterium tuberculosis
    • Johnsson, K.; Schultz, P. G. Mechanistic Studies of the Oxidation of Isoniazid by the Catalase Peroxidase from Mycobacterium tuberculosis. J. Am. Chem. Soc. 1994, 116, 7425-7426.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 7425-7426
    • Johnsson, K.1    Schultz, P.G.2
  • 13
    • 0029042636 scopus 로고
    • Studies on the Mechanism of Action of Isoniazid and Ethionamide in the Chemotherapy of Tuberculosis
    • Johnsson, K.; King, D. S.; Schultz, P. G. Studies on the Mechanism of Action of Isoniazid and Ethionamide in the Chemotherapy of Tuberculosis. J. Am. Chem. Soc. 1995, 117, 5009-5010.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5009-5010
    • Johnsson, K.1    King, D.S.2    Schultz, P.G.3
  • 14
    • 0029860774 scopus 로고    scopus 로고
    • Kinetics of inactivation of WT and C243S mutant of Mycobacterium tuberculosis enoyl reductase by activated isoniazid
    • Basso, L. A.; Zheng, R. J.; Blanchard, J. S. Kinetics of inactivation of WT and C243S mutant of Mycobacterium tuberculosis enoyl reductase by activated isoniazid. J. Am. Chem. Soc. 1996, 118 (45), 11301-11302.
    • (1996) J. Am. Chem. Soc. , vol.118 , Issue.45 , pp. 11301-11302
    • Basso, L.A.1    Zheng, R.J.2    Blanchard, J.S.3
  • 15
    • 0028988237 scopus 로고
    • Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis
    • Dessen, A.; Quemard, A.; Blanchard, J. S.; Jacobs WR, J. r.; Sacchettini, J. C. Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis. Science 1995, 267 (5204), 1638-41.
    • (1995) Science , vol.267 , Issue.5204 , pp. 1638-1641
    • Dessen, A.1    Quemard, A.2    Blanchard, J.S.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 17
    • 0038492810 scopus 로고    scopus 로고
    • Binding of Catalase-Peroxidase-Activated Isoniazid to Wild-Type and Mutant Mycobacterium tuberculosis Enoyl - ACP Reductases
    • Quemard, A.; Dessen, A.; Sugantino, M.; Jacobs, W. R. Jr.; Sacchettini, J. C.; Blanchard, J. S. Binding of Catalase-Peroxidase-Activated Isoniazid to Wild-Type and Mutant Mycobacterium tuberculosis Enoyl - ACP Reductases. J. Am. Chem. Soc. 1996, 118 (6), 1561-1562.
    • (1996) J. Am. Chem. Soc. , vol.118 , Issue.6 , pp. 1561-1562
    • Quemard, A.1    Dessen, A.2    Sugantino, M.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5    Blanchard, J.S.6
  • 18
    • 0032472224 scopus 로고    scopus 로고
    • Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis
    • Rozwarski, D. A.; Grant, G. A.; Barton, D. H. R.; Jacobs WR, J. r.; Sacchettini, J. C. Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis. Science 1998, 279 (5347), 98-102.
    • (1998) Science , vol.279 , Issue.5347 , pp. 98-102
    • Rozwarski, D.A.1    Grant, G.A.2    Barton, D.H.R.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 19
    • 0027282748 scopus 로고
    • Catalase-peroxidase gene sequences in isoniazid-sensitive and - Resistant strains of Mycobacterium tuberculosis from New York City
    • Stoeckle, M. Y.; Guan, L.; Riegler, N.; Weitzman, I.; Kreiswirth, B.; Kornblum, J.; Laraque, F.; Riley, L. W. Catalase-peroxidase gene sequences in isoniazid-sensitive and - resistant strains of Mycobacterium tuberculosis from New York City. J. Infect. Dis. 1993, 168 (4), 1063-1065.
    • (1993) J. Infect. Dis. , vol.168 , Issue.4 , pp. 1063-1065
    • Stoeckle, M.Y.1    Guan, L.2    Riegler, N.3    Weitzman, I.4    Kreiswirth, B.5    Kornblum, J.6    Laraque, F.7    Riley, L.W.8
  • 21
    • 0030042509 scopus 로고    scopus 로고
    • Characterization of the catalase-peroxidase gene (katG) and inhA locus in isoniazid-resistant and - Susceptible strains of Mycobacterium tuberculosis by automated DNA sequencing: Restricted array of mutations associated with drug resistance
    • Musser, J. M.; Kapur, V.; Williams, D. L.; Kreiswirth, B. N.; van Soolingen, D.; van Embden, J. D. Characterization of the catalase-peroxidase gene (katG) and inhA locus in isoniazid-resistant and - susceptible strains of Mycobacterium tuberculosis by automated DNA sequencing: restricted array of mutations associated with drug resistance. J. Infect. Dis. 1996, 173 (1), 196-202.
    • (1996) J. Infect. Dis. , vol.173 , Issue.1 , pp. 196-202
    • Musser, J.M.1    Kapur, V.2    Williams, D.L.3    Kreiswirth, B.N.4    van Soolingen, D.5    van Embden, J.D.6
  • 23
    • 0345133299 scopus 로고    scopus 로고
    • The Isoniazid-NAD Adduct is a Slow, Tight-Binding Inhibitor of InhA, the Mycobacterium Tuberculosis Enoyl Reductase; Adduct Affinity and Drug Resistance
    • Rawat, R.; Whitty, A.; Tonge, P. J. The Isoniazid-NAD Adduct is a Slow, Tight-Binding Inhibitor of InhA, the Mycobacterium Tuberculosis Enoyl Reductase; Adduct Affinity and Drug Resistance. Proc. Nat. Acad. Sci. U.S.A. 2003, 100, 13881-13886.
    • (2003) Proc. Nat. Acad. Sci. U.S.A. , vol.100 , pp. 13881-13886
    • Rawat, R.1    Whitty, A.2    Tonge, P.J.3
  • 24
    • 0033709606 scopus 로고    scopus 로고
    • Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis
    • Slayden, R. A.; Lee, R. E.; Barry, C. E. 3rd, Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis. Mol. Microbiol. 2000, 38 (3), 514-25.
    • (2000) Mol. Microbiol. , vol.38 , Issue.3 , pp. 514-525
    • Slayden, R.A.1    Lee, R.E.2    Barry III, C.E.3
  • 25
    • 0034084624 scopus 로고    scopus 로고
    • The genetics and biochemistry of isoniazid resistance in Mycobacterium tuberculosis
    • Slayden, R. A.; Barry, C. E. 3rd, The genetics and biochemistry of isoniazid resistance in Mycobacterium tuberculosis. Microbes Infect. 2000, 2 (6), 659-69.
    • (2000) Microbes Infect. , vol.2 , Issue.6 , pp. 659-669
    • Slayden, R.A.1    Barry III, C.E.2
  • 26
    • 0038410325 scopus 로고    scopus 로고
    • Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis
    • Vilcheze, C.; Morbidoni, H. R.; Weisbrod, T. R.; Iwamoto, H.; Kuo, M.; Sacchettini, J. C.; Jacobs, W. R. Jr. Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis. J. Bacteriol. 2000, 182 (14), 4059-67.
    • (2000) J. Bacteriol. , vol.182 , Issue.14 , pp. 4059-4067
    • Vilcheze, C.1    Morbidoni, H.R.2    Weisbrod, T.R.3    Iwamoto, H.4    Kuo, M.5    Sacchettini, J.C.6    Jacobs Jr., W.R.7
  • 28
    • 33947706952 scopus 로고    scopus 로고
    • The role of KasA and KasB in the biosynthesis of meromycolic acids and isoniazid resistance in Mycobacterium tuberculosis
    • Slayden, R. A.; Barry CE, r. The role of KasA and KasB in the biosynthesis of meromycolic acids and isoniazid resistance in Mycobacterium tuberculosis. Tuberculosis 2002, 81 (1), 1-12.
    • (2002) Tuberculosis , vol.81 , Issue.1 , pp. 1-12
    • Slayden, R.A.1    Barry, C.E.R.2
  • 30
    • 0034804919 scopus 로고    scopus 로고
    • Lipid biosynthesis as a target for antibacterial agents
    • Heath, R. J.; White, S. W.; Rock, C. O. Lipid biosynthesis as a target for antibacterial agents. Prog. Lipid Res. 2001, 40 (6), 467-97.
    • (2001) Prog. Lipid Res. , vol.40 , Issue.6 , pp. 467-497
    • Heath, R.J.1    White, S.W.2    Rock, C.O.3
  • 31
    • 0034780806 scopus 로고    scopus 로고
    • Bacterial fatty acid biosynthesis: Targets for antibacterial drug discovery
    • Campbell, J. W.; Cronan, J. E. Jr. Bacterial fatty acid biosynthesis: targets for antibacterial drug discovery. Annu. Rev. Microbiol. 2001, 55, 305-32.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 305-332
    • Campbell, J.W.1    Cronan Jr., J.E.2
  • 32
    • 0036247948 scopus 로고    scopus 로고
    • Inhibitors of fatty acid synthesis as antimicrobial chemotherapeutics
    • Heath, R. J.; White, S. W.; Rock, C. O. Inhibitors of fatty acid synthesis as antimicrobial chemotherapeutics. Appl. Microbiol. Biotechnol. 2002, 58 (6), 695-703.
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , Issue.6 , pp. 695-703
    • Heath, R.J.1    White, S.W.2    Rock, C.O.3
  • 33
    • 0015340462 scopus 로고
    • The action mechanism of cerulenin. I. Effect of cerulenin on sterol and fatty acid biosynthesis in yeast
    • Nomura, S.; Horiuchi, T.; Omura, S.; Hata, T. The action mechanism of cerulenin. I. Effect of cerulenin on sterol and fatty acid biosynthesis in yeast. J. Biochem. 1972, 71 (5), 783-96.
    • (1972) J. Biochem. , vol.71 , Issue.5 , pp. 783-796
    • Nomura, S.1    Horiuchi, T.2    Omura, S.3    Hata, T.4
  • 34
    • 0019977450 scopus 로고
    • Thiolactomycin, a new antibiotic. III. In vitro antibacterial activity
    • Noto, T.; Miyakawa, S.; Oishi, H.; Endo, H.; Okazaki, H. Thiolactomycin, a new antibiotic. III. In vitro antibacterial activity. J. Antibiot. 1982, 35 (4), 401-10.
    • (1982) J. Antibiot. , vol.35 , Issue.4 , pp. 401-410
    • Noto, T.1    Miyakawa, S.2    Oishi, H.3    Endo, H.4    Okazaki, H.5
  • 35
    • 0026544037 scopus 로고
    • Overproduction of beta-ketoacyl-acyl carrier protein synthase I imparts thiolactomycin resistance to Escherichia coli K-12
    • Tsay, J. T.; Rock, C. O.; Jackowski, S. Overproduction of beta-ketoacyl-acyl carrier protein synthase I imparts thiolactomycin resistance to Escherichia coli K-12. J. Bacteriol. 1992, 174 (2), 508-13.
    • (1992) J. Bacteriol. , vol.174 , Issue.2 , pp. 508-513
    • Tsay, J.T.1    Rock, C.O.2    Jackowski, S.3
  • 36
    • 0030911594 scopus 로고    scopus 로고
    • In vivo and in vitro effects of thiolactomycin on fatty acid biosynthesis in Streptomyces collinus
    • Wallace, K. K.; Lobo, S.; Han, L.; McArthur, H. A.; Reynolds, K. A. In vivo and in vitro effects of thiolactomycin on fatty acid biosynthesis in Streptomyces collinus. J. Bacteriol. 1997, 179 (12), 3884-91.
    • (1997) J. Bacteriol. , vol.179 , Issue.12 , pp. 3884-3891
    • Wallace, K.K.1    Lobo, S.2    Han, L.3    McArthur, H.A.4    Reynolds, K.A.5
  • 37
    • 0031918573 scopus 로고    scopus 로고
    • Intrinsic resistance to inhibitors of fatty acid biosynthesis in Pseudomonas aeruginosa is due to efflux: Application of a novel technique for generation of unmarked chromosomal mutations for the study of efflux systems
    • Schweizer, H. P. Intrinsic resistance to inhibitors of fatty acid biosynthesis in Pseudomonas aeruginosa is due to efflux: application of a novel technique for generation of unmarked chromosomal mutations for the study of efflux systems. Antimicrob. Agents Chemother. 1998, 42 (2), 394-8.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , Issue.2 , pp. 394-398
    • Schweizer, H.P.1
  • 38
    • 0034623067 scopus 로고    scopus 로고
    • Identification and substrate specificity of beta -ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis
    • Choi, K. H.; Kremer, L.; Besra, G. S.; Rock, C. O. Identification and substrate specificity of beta -ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis. J. Biol. Chem. 2000, 275 (36), 28201-7.
    • (2000) J. Biol. Chem. , vol.275 , Issue.36 , pp. 28201-28207
    • Choi, K.H.1    Kremer, L.2    Besra, G.S.3    Rock, C.O.4
  • 40
    • 0035794127 scopus 로고    scopus 로고
    • Inhibition of beta-ketoacyl-acyl carrier protein synthases by thiolactomycin and cerulenin. Structure and mechanism
    • Price, A. C.; Choi, K. H.; Heath, R. J.; Li, Z.; White, S. W.; Rock, C. O. Inhibition of beta-ketoacyl-acyl carrier protein synthases by thiolactomycin and cerulenin. Structure and mechanism. J. Biol. Chem. 2001, 276 (9), 6551-9.
    • (2001) J. Biol. Chem. , vol.276 , Issue.9 , pp. 6551-6559
    • Price, A.C.1    Choi, K.H.2    Heath, R.J.3    Li, Z.4    White, S.W.5    Rock, C.O.6
  • 41
    • 0035861550 scopus 로고    scopus 로고
    • Purification and biochemical characterization of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthases KasA and KasB
    • Schaeffer, M. L.; Agnihotri, G.; Volker, C.; Kallender, H.; Brennan, P. J.; Lonsdale, J. T. 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    Kallender, H.4    Brennan, P.J.5    Lonsdale, J.T.6
  • 43
    • 0036233536 scopus 로고    scopus 로고
    • A missense mutation in the fabB (beta-ketoacyl-acyl carrier protein synthase I) gene confers thiolactomycin resistance to Escherichia coli. Antimicrob
    • Jackowski, S.; Zhang, Y. M.; Price, A. C.; White, S. W.; Rock, C. O. A missense mutation in the fabB (beta-ketoacyl-acyl carrier protein synthase I) gene confers thiolactomycin resistance to Escherichia coli. Antimicrob. Agents Chemother. 2002, 46 (5), 1246-52.
    • (2002) Agents Chemother. , vol.46 , Issue.5 , pp. 1246-1252
    • Jackowski, S.1    Zhang, Y.M.2    Price, A.C.3    White, S.W.4    Rock, C.O.5
  • 45
    • 0024331888 scopus 로고
    • envM genes of Salmonella typhimurium and Escherichia coli
    • Turnowsky, F.; Fuchs, K.; Jeschek, C.; Hogenauer, G. envM genes of Salmonella typhimurium and Escherichia coli. J. Bacteriol. 1989, 171 (12), 6555-65.
    • (1989) J. Bacteriol. , vol.171 , Issue.12 , pp. 6555-6565
    • Turnowsky, F.1    Fuchs, K.2    Jeschek, C.3    Hogenauer, G.4
  • 48
    • 0032515066 scopus 로고    scopus 로고
    • Broad spectrum antimicrobial biocides target the FabI component of fatty acid synthesis
    • Heath, R. J.; Yu, Y. T.; Shapiro, M. A.; Olson, E.; Rock, C. O. Broad spectrum antimicrobial biocides target the FabI component of fatty acid synthesis. J. Biol. Chem. 1998, 273 (46), 30316-20.
    • (1998) J. Biol. Chem. , vol.273 , Issue.46 , pp. 30316-30320
    • Heath, R.J.1    Yu, Y.T.2    Shapiro, M.A.3    Olson, E.4    Rock, C.O.5
  • 49
    • 0032490937 scopus 로고    scopus 로고
    • Triclosan targets lipid synthesis
    • McMurry, L. M.; Oethinger, M.; Levy, S. B. Triclosan targets lipid synthesis. Nature 1998, 394 (6693), 531-2.
    • (1998) Nature , vol.394 , Issue.6693 , pp. 531-532
    • McMurry, L.M.1    Oethinger, M.2    Levy, S.B.3
  • 50
    • 0033574422 scopus 로고    scopus 로고
    • Mechanism of triclosan inhibition of bacterial fatty acid synthesis
    • Heath, R. J.; Rubin, J. R.; Holland, D. R.; Zhang, E.; Snow, M. E.; Rock, C. O. Mechanism of triclosan inhibition of bacterial fatty acid synthesis. J. Biol. Chem. 1999, 274 (16), 11110-4.
    • (1999) J. Biol. Chem. , vol.274 , Issue.16 , pp. 11110-11114
    • Heath, R.J.1    Rubin, J.R.2    Holland, D.R.3    Zhang, E.4    Snow, M.E.5    Rock, C.O.6
  • 52
    • 0033055847 scopus 로고    scopus 로고
    • Genetic evidence that InhA of Mycobacterium smegmatis is a target for triclosan
    • McMurry, L. M.; McDermott, P. F.; Levy, S. B. Genetic evidence that InhA of Mycobacterium smegmatis is a target for triclosan. Antimicrob. Agents Chemother. 1999, 43 (3), 711-3.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , Issue.3 , pp. 711-713
    • McMurry, L.M.1    McDermott, P.F.2    Levy, S.B.3
  • 53
    • 0032721424 scopus 로고    scopus 로고
    • Molecular basis for triclosan activity involves a flipping loop in the active site
    • Qiu, X. Y.; Janson, C. A.; Court, R. I.; Smyth, M. G.; Payne, D. J.; Abdel-Meguid, S. S. Molecular basis for triclosan activity involves a flipping loop in the active site. Protein Sci. 1999, 8 (11), 2529-2532.
    • (1999) Protein Sci. , vol.8 , Issue.11 , pp. 2529-2532
    • Qiu, X.Y.1    Janson, C.A.2    Court, R.I.3    Smyth, M.G.4    Payne, D.J.5    Abdel-Meguid, S.S.6
  • 55
    • 0032775211 scopus 로고    scopus 로고
    • Structural basis and mechanism of enoyl reductase inhibition by triclosan
    • Stewart, M. J.; Parikh, S.; Xiao, G.; Tonge, P. J.; Kisker, C. Structural basis and mechanism of enoyl reductase inhibition by triclosan. J. Mol. Biol. 1999, 290, 859-865.
    • (1999) J. Mol. Biol. , vol.290 , pp. 859-865
    • Stewart, M.J.1    Parikh, S.2    Xiao, G.3    Tonge, P.J.4    Kisker, C.5
  • 57
    • 17644436310 scopus 로고    scopus 로고
    • Inhibition of InhA, the enoyl-reductase from Mycobacterium tuberculosis, by triclosan and isoniazid
    • Parikh, S. L.; Xiao, G.; Tonge, P. J. Inhibition of InhA, the enoyl-reductase from Mycobacterium tuberculosis, by triclosan and isoniazid. Biochemistry 2000, 39 (26), 7645-7650.
    • (2000) Biochemistry , vol.39 , Issue.26 , pp. 7645-7650
    • Parikh, S.L.1    Xiao, G.2    Tonge, P.J.3
  • 58
    • 26844550453 scopus 로고    scopus 로고
    • Identification of inhibitors of bacterial enoyl-acyl carrier protein reductase
    • Moir, D. T. Identification of inhibitors of bacterial enoyl-acyl carrier protein reductase. Curr. Drug Targets Infect. Disord. 2005, 5 (3), 297-305.
    • (2005) Curr. Drug Targets Infect. Disord. , vol.5 , Issue.3 , pp. 297-305
    • Moir, D.T.1
  • 63
    • 12844282019 scopus 로고    scopus 로고
    • Anti-protozoal and plasmodial FabI enzyme inhibiting metabolites of Scrophularia lepidota roots
    • Tasdemir, D.; Guner, N. D.; Perozzo, R.; Brun, R.; Donmez, A. A.; Calis, I.; Ruedi, P. Anti-protozoal and plasmodial FabI enzyme inhibiting metabolites of Scrophularia lepidota roots. Phytochemistry 2005, 66 (3), 355-62.
    • (2005) Phytochemistry , vol.66 , Issue.3 , pp. 355-362
    • Tasdemir, D.1    Guner, N.D.2    Perozzo, R.3    Brun, R.4    Donmez, A.A.5    Calis, I.6    Ruedi, P.7
  • 65
    • 4444261960 scopus 로고    scopus 로고
    • Inhibiting activities of the secondary metabolites of Phlomis brunneogaleata against parasitic protozoa and plasmodial enoyl-ACP Reductase, a crucial enzyme in fatty acid biosynthesis
    • Kirmizibekmez, H.; Calis, I.; Perozzo, R.; Brun, R.; Donmez, A. A.; Linden, A.; Ruedi, P.; Tasdemir, D. Inhibiting activities of the secondary metabolites of Phlomis brunneogaleata against parasitic protozoa and plasmodial enoyl-ACP Reductase, a crucial enzyme in fatty acid biosynthesis. Planta. Med. 2004, 70 (8), 711-7.
    • (2004) Planta. Med. , vol.70 , Issue.8 , pp. 711-717
    • Kirmizibekmez, H.1    Calis, I.2    Perozzo, R.3    Brun, R.4    Donmez, A.A.5    Linden, A.6    Ruedi, P.7    Tasdemir, D.8
  • 67
    • 0037066782 scopus 로고    scopus 로고
    • Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase
    • Perozzo, R.; Kuo, M.; Sidhu, A. S.; Valiyaveettil, J. T.; Bittman, R.; Jacobs, W. R. Jr.; Fidock, D. A.; Sacchettini, J. C. Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase. J. Biol. Chem. 2002, 277 (15), 13106-14.
    • (2002) J. Biol. Chem. , vol.277 , Issue.15 , pp. 13106-13114
    • Perozzo, R.1    Kuo, M.2    Sidhu, A.S.3    Valiyaveettil, J.T.4    Bittman, R.5    Jacobs Jr., W.R.6    Fidock, D.A.7    Sacchettini, J.C.8
  • 68
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    • Surolia, N.; Surolia, A. Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum. Nat. Med. 2001, 7 (2), 167-73.
    • (2001) Nat. Med. , vol.7 , Issue.2 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 69
    • 1642540581 scopus 로고    scopus 로고
    • Inhibition of the Bacterial Enoyl Reductase FabI by Triclosan: A Structure-Reactivity Analysis of FabI Inhibition by Triclosan Analogs
    • Sivaraman, S.; Sullivan, T. J.; Johnson, F.; Novichenok, P.; Cui, G.; Simmerling, C.; Tonge, P. J. Inhibition of the Bacterial Enoyl Reductase FabI by Triclosan: A Structure-Reactivity Analysis of FabI Inhibition by Triclosan Analogs. J. Med Chem. 2004, 47, 509-518.
    • (2004) J. Med Chem. , vol.47 , pp. 509-518
    • Sivaraman, S.1    Sullivan, T.J.2    Johnson, F.3    Novichenok, P.4    Cui, G.5    Simmerling, C.6    Tonge, P.J.7
  • 70
    • 0037461276 scopus 로고    scopus 로고
    • Structure-Activity Studies of the Inhibition of FabI, the Enoyl Reductase from Escherichia coli, by Triclosan: Kinetic Analysis of Mutant FabIs
    • Sivaraman, S.; Zwahlen, J.; Bell, A. F.; Hedstrom, L.; Tonge, P. J. Structure-Activity Studies of the Inhibition of FabI, the Enoyl Reductase from Escherichia coli, by Triclosan: Kinetic Analysis of Mutant FabIs. Biochemistry 2003, 42 (15), 4406-4413.
    • (2003) Biochemistry , vol.42 , Issue.15 , pp. 4406-4413
    • Sivaraman, S.1    Zwahlen, J.2    Bell, A.F.3    Hedstrom, L.4    Tonge, P.J.5
  • 72
    • 0040017633 scopus 로고    scopus 로고
    • Crystal Structure of the Mycobacterium tuberculosis Enoyl-ACP Reductase, InhA, in Complex with NAD+ and a C16 Fatty Acyl Substrate
    • Rozwarski, D. A.; Vilcheze, C.; Sugantino, M.; Bittman, R.; Sacchettini, J. C. Crystal Structure of the Mycobacterium tuberculosis Enoyl-ACP Reductase, InhA, in Complex with NAD+ and a C16 Fatty Acyl Substrate. J. Biol. Chem. 1999, 274, 15582-15589.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15582-15589
    • Rozwarski, D.A.1    Vilcheze, C.2    Sugantino, M.3    Bittman, R.4    Sacchettini, J.C.5
  • 73
    • 0034812321 scopus 로고    scopus 로고
    • The first general method for palladium-catalyzed Negishi cross-coupling of aryl and vinyl chlorides: Use of commercially available Pd(P(t-BU)(3))(2) as a catalyst
    • Dai, C. Y.; Fu, G. C. The first general method for palladium-catalyzed Negishi cross-coupling of aryl and vinyl chlorides: Use of commercially available Pd(P(t-BU)(3))(2) as a catalyst. J. Am. Chem. Soc. 2001, 123 (12), 2719-2724.
    • (2001) J. Am. Chem. Soc. , vol.123 , Issue.12 , pp. 2719-2724
    • Dai, C.Y.1    Fu, G.C.2
  • 74
    • 0025020985 scopus 로고
    • Development of a High-Affinity and Stereoselective Photoaffinity Label for the D-1 Dopamine Receptor - Synthesis and Resolution of 7-(I-125) Iodo-8-Hydroxy-3-Methyl-1-(4′-Azidophenyl)-2,3,4,5-Tetrahydro-1h-3- Benzazepine
    • Neumeyer, J. L.; Baindur, N.; Yuan, J.; Booth, G.; Seeman, P.; Niznik, H. B. Development of a High-Affinity and Stereoselective Photoaffinity Label for the D-1 Dopamine Receptor - Synthesis and Resolution of 7-(I-125)Iodo-8-Hydroxy-3-Methyl-1-(4′-Azidophenyl)-2,3,4,5- Tetrahydro-1h-3-Benzazepine. J. Med. Chem. 1990, 33 (2), 521-526.
    • (1990) J. Med. Chem. , vol.33 , Issue.2 , pp. 521-526
    • Neumeyer, J.L.1    Baindur, N.2    Yuan, J.3    Booth, G.4    Seeman, P.5    Niznik, H.B.6
  • 75
    • 0030700314 scopus 로고    scopus 로고
    • A general copper-catalyzed synthesis of diaryl ethers
    • Marcoux, J. F.; Doye, S.; Buchwald, S. L. A general copper-catalyzed synthesis of diaryl ethers. J. Am. Chem. Soc. 1997, 119 (43), 10539-10540.
    • (1997) J. Am. Chem. Soc. , vol.119 , Issue.43 , pp. 10539-10540
    • Marcoux, J.F.1    Doye, S.2    Buchwald, S.L.3
  • 76
    • 0041922652 scopus 로고    scopus 로고
    • Signature gene expression profiles discriminate between isoniazid-, thiolactomycin-, and triclosan-treated Mycobacterium tuberculosis
    • Betts, J. C.; McLaren, A.; Lennon, M. G.; Kelly, F. M.; Lukey, P. T.; Blakemore, S. J.; Duncan, K. 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    Kelly, F.M.4    Lukey, P.T.5    Blakemore, S.J.6    Duncan, K.7
  • 77
  • 78
    • 0033966884 scopus 로고    scopus 로고
    • Another brick in the wall
    • Tonge, P. J. Another brick in the wall. Nat. Struct. Biol. 2000, 7 (2), 94-96.
    • (2000) Nat. Struct. Biol. , vol.7 , Issue.2 , pp. 94-96
    • Tonge, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.