메뉴 건너뛰기




Volumn 7, Issue 4, 2012, Pages 327-339

Bacterial DNA replication enzymes as targets for antibacterial drug discovery

Author keywords

antibacterial agents; antibiotics; bacterial DNA synthesis; bacterial targets; DNA gyrase; DNA helicase; DNA ligase; DNA polymerase; DNA primase; topoisomerase

Indexed keywords

ANTIINFECTIVE AGENT; BACTERIAL DNA; BACTERIAL ENZYME; DNA DIRECTED DNA POLYMERASE GAMMA; DNA PRIMASE; DNA TOPOISOMERASE (ATP HYDROLYSING); GSK 299423; GYRASE INHIBITOR; HELICASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; UNCLASSIFIED DRUG;

EID: 84859364840     PISSN: 17460441     EISSN: 1746045X     Source Type: Journal    
DOI: 10.1517/17460441.2012.660478     Document Type: Review
Times cited : (66)

References (117)
  • 2
    • 77953710831 scopus 로고    scopus 로고
    • SnapShot: The replisome
    • Yao NY, O'Donnell M. SnapShot: the replisome. Cell 2010;141:1088
    • (2010) Cell , vol.141 , pp. 1088
    • Yao, N.Y.1    O'Donnell, M.2
  • 3
    • 38849201038 scopus 로고    scopus 로고
    • Understanding how the replisome works
    • DOI 10.1038/nsmb0208-125, PII NSMB0208125
    • Marians KJ. Understanding how the replisome works. Nat Struct Mol Biol 2008;15:125-7 (Pubitemid 351207523)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.2 , pp. 125-127
    • Marians, K.J.1
  • 4
    • 0003890119 scopus 로고    scopus 로고
    • 2nd edition. University Science Books; Sausalito, CA
    • Kornberg A, Baker TA. DNA replication. 2nd edition. University Science Books; Sausalito, CA: 2005
    • (2005) DNA Replication
    • Kornberg, A.1    Baker, T.A.2
  • 5
    • 34047149973 scopus 로고    scopus 로고
    • Replisome mechanics: insights into a twin DNA polymerase machine
    • DOI 10.1016/j.tim.2007.02.007, PII S0966842X0700042X
    • Pomerantz RT, O'Donnell M. Replisome mechanics: insights into a twin DNA polymerase machine. Trends Microbiol 2007;15:156-64 A review of replisome function. (Pubitemid 46528254)
    • (2007) Trends in Microbiology , vol.15 , Issue.4 , pp. 156-164
    • Pomerantz, R.T.1    O'Donnell, M.2
  • 6
    • 17044371192 scopus 로고    scopus 로고
    • Solution structure of the helicase-interaction domain of the primase DnaG: A model for helicase activation
    • Syson K, Thirlway J, Hounslow AM, et al. Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation. Structure 2005;13:609-16
    • (2005) Structure , vol.13 , pp. 609-616
    • Syson, K.1    Thirlway, J.2    Hounslow, A.M.3
  • 7
    • 14844347928 scopus 로고    scopus 로고
    • Bacterial topoisomerase inhibitors: Quinolone and pyridone antibacterial agents
    • DOI 10.1021/cr030101q
    • Mitscher LA. Bacterial topoisomerase inhibitors: quinolone and pyridone antibacterial agents. Chem Rev 2005;105:559-92 (Pubitemid 40351634)
    • (2005) Chemical Reviews , vol.105 , Issue.2 , pp. 559-592
    • Mitscher, L.A.1
  • 8
    • 0012684806 scopus 로고    scopus 로고
    • The ATP-binding site of type II topoisomerases as a target for antibacterial drugs
    • Maxwell A, Lawson DM. The ATP-binding site of type II topoisomerases as a target for antibacterial drugs. Curr Top Med Chem 2003;3:283-303
    • (2003) Curr Top Med Chem , vol.3 , pp. 283-303
    • Maxwell, A.1    Lawson, D.M.2
  • 10
    • 0031105464 scopus 로고    scopus 로고
    • DNA gyrase as a drug target
    • DOI 10.1016/S0966-842X(96)10085-8, PII S0966842X96100858
    • Maxwell A. DNA gyrase as a drug target. Trends Microbiol 1997;5:102-9 (Pubitemid 27139470)
    • (1997) Trends in Microbiology , vol.5 , Issue.3 , pp. 102-109
    • Maxwell, A.1
  • 11
    • 0024444020 scopus 로고
    • Inhibitory effects of quinolones on DNA gyrase of Escherichia coli and topoisomerase II of fetal calf thymus
    • Hoshino K, Sato K, Une T, et al. Inhibitory effects of quinolones on DNA gyrase of Escherichia coli and topoisomerase II of fetal calf thymus. Antimicrob Agents Chemother 1989;33:1816-18 (Pubitemid 19239181)
    • (1989) Antimicrobial Agents and Chemotherapy , vol.33 , Issue.10 , pp. 1816-1818
    • Hoshino, K.1    Sato, K.2    Une, T.3    Osada, Y.4
  • 14
    • 0028334718 scopus 로고
    • DNA transport by a type II DNA topoisomerase: Evidence in favor of a two-gate mechanism
    • Along with reference 15, proposes the two gate mechanism of DNA gyrase
    • Roca J, Wang JC. DNA transport by a type II DNA topoisomerase: evidence in favor of a two-gate mechanism. Cell 1994;77:609-16 Along with reference 15, proposes the two gate mechanism of DNA gyrase.
    • (1994) Cell , vol.77 , pp. 609-616
    • Roca, J.1    Wang, J.C.2
  • 15
    • 0026448670 scopus 로고
    • The capture of a DNA double helix by an ATP-dependent protein clamp: A key step in DNA transport by type II DNA topoisomerases
    • Along with reference 14, proposes the two gate mechanism of DNA gyrase
    • Roca J, Wang JC. The capture of a DNA double helix by an ATP-dependent protein clamp: a key step in DNA transport by type II DNA topoisomerases. Cell 1992;71:833-40 Along with reference 14, proposes the two gate mechanism of DNA gyrase.
    • (1992) Cell , vol.71 , pp. 833-840
    • Roca, J.1    Wang, J.C.2
  • 16
    • 77953237570 scopus 로고    scopus 로고
    • The role of ATP in the reactions of type II DNA topoisomerases
    • Bates AD, Maxwell A. The role of ATP in the reactions of type II DNA topoisomerases. Biochem Soc Trans 2010;38:438-42
    • (2010) Biochem Soc Trans , vol.38 , pp. 438-442
    • Bates, A.D.1    Maxwell, A.2
  • 17
    • 34447323073 scopus 로고    scopus 로고
    • Energy coupling in type II topoisomerases: Why do they hydrolyze ATP?
    • DOI 10.1021/bi700789g
    • Bates AD, Maxwell A. Energy coupling in type II topoisomerases: why do they hydrolyze ATP? Biochemistry (NY) 2007;46:7929-41 (Pubitemid 47053858)
    • (2007) Biochemistry , vol.46 , Issue.27 , pp. 7929-7941
    • Bates, A.D.1    Maxwell, A.2
  • 18
    • 28844493513 scopus 로고    scopus 로고
    • Coupling ATP hydrolysis to DNA strand passage in type IIA DNA topoisomerases
    • DOI 10.1042/BST20051460
    • Maxwell A, Costenaro L, Mitelheiser S, et al. Coupling ATP hydrolysis to DNA strand passage in type IIA DNA topoisomerases. Biochem Soc Trans 2005;33:1460-4 (Pubitemid 41779715)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.6 , pp. 1460-1464
    • Maxwell, A.1    Costenaro, L.2    Mitelheiser, S.3    Bates, A.D.4
  • 20
    • 33646584802 scopus 로고    scopus 로고
    • Structural features of new quinolones and relationship to antibacterial activity against gram-positive bacteria
    • Emami S, Shafiee A, Foroumadi A. Structural features of new quinolones and relationship to antibacterial activity against gram-positive bacteria. Mini Rev Med Chem 2006;6:375-86
    • (2006) Mini Rev Med Chem , vol.6 , pp. 375-386
    • Emami, S.1    Shafiee, A.2    Foroumadi, A.3
  • 21
    • 80255135542 scopus 로고    scopus 로고
    • New antimicrobial agents on the horizon
    • Recent review of the antibacterial drug discovery pipeline
    • Bush K, Pucci MJ. New antimicrobial agents on the horizon. Biochem Pharmacol 2011;82:1528-39 Recent review of the antibacterial drug discovery pipeline.
    • (2011) Biochem Pharmacol , vol.82 , pp. 1528-1539
    • Bush, K.1    Pucci, M.J.2
  • 22
    • 82355173219 scopus 로고    scopus 로고
    • Exploiting bacterial DNA gyrase as a drug target: Current state and perspectives
    • Recent review of DNA gyrase and selected inhibitors
    • Collin F, Karkare S, Maxwell A. Exploiting bacterial DNA gyrase as a drug target: current state and perspectives. Appl Microbiol Biotechnol 2011;92:479-97 Recent review of DNA gyrase and selected inhibitors.
    • (2011) Appl Microbiol Biotechnol , vol.92 , pp. 479-497
    • Collin, F.1    Karkare, S.2    Maxwell, A.3
  • 23
    • 0035180501 scopus 로고    scopus 로고
    • Target preference of 15 quinolones against Staphylococcus aureus, based on antibacterial activities and target inhibition
    • DOI 10.1128/AAC.45.12.3544-3547.2001
    • Takei M, Fukuda H, Kishii R, et al. Target preference of 15 quinolones against Staphylococcus aureus, based on antibacterial activities and target inhibition. Antimicrob Agents Chemother 2001;45:3544-7 (Pubitemid 33107875)
    • (2001) Antimicrobial Agents and Chemotherapy , vol.45 , Issue.12 , pp. 3544-3547
    • Takei, M.1    Fukuda, H.2    Kishii, R.3    Hosaka, M.4
  • 24
    • 80051684987 scopus 로고    scopus 로고
    • Inhibition of DNA gyrase and DNA topoisomerase IV of Staphylococcus aureus and e by aminocoumarin antibiotics
    • Alt S, Mitchenall LA, Maxwell A, et al. Inhibition of DNA gyrase and DNA topoisomerase IV of Staphylococcus aureus and E by aminocoumarin antibiotics. J Antimicrob Chemother 2011;66:2061-9
    • (2011) J Antimicrob Chemother , vol.66 , pp. 2061-2069
    • Alt, S.1    Mitchenall, L.A.2    Maxwell, A.3
  • 26
    • 34548628774 scopus 로고    scopus 로고
    • Discovery and development of ATPase inhibitors of DNA gyrase as antibacterial agents
    • DOI 10.2174/092986707781368414
    • Oblak M, Kotnik M, Solmajer T. Discovery and development of ATPase inhibitors of DNA gyrase as antibacterial agents. Curr Med Chem 2007;14:2033-47 (Pubitemid 47578161)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.19 , pp. 2033-2047
    • Oblak, M.1    Kotnik, M.2    Solmajer, T.3
  • 27
    • 84863393500 scopus 로고    scopus 로고
    • Pyrrolamide DNA gyrase inhibitors: Fragment-based NMR screening to antibacterial agents
    • In press Describes the application of NMR and structure-based design in fragment-based lead generation
    • Eakin AE, Green O, Hales N, et al. Pyrrolamide DNA gyrase inhibitors: Fragment-based NMR screening to antibacterial agents. Antimicrob Agents Chemother 2012; In press Describes the application of NMR and structure-based design in fragment-based lead generation.
    • (2012) Antimicrob Agents Chemother
    • Eakin, A.E.1    Green, O.2    Hales, N.3
  • 28
    • 84859373439 scopus 로고    scopus 로고
    • Novel DNA gyrase inhibitors: The effect of pyrrolamide variations at site 1 and site 2 upon potency
    • abstract F1-2027
    • Hull K, Green O, Singh A, et al. Novel DNA gyrase inhibitors: the effect of pyrrolamide variations at site 1 and site 2 upon potency [abstract F1-2027]. 48th Intersci. Conf. Antimicrob Agents Chemother; 2008
    • 48th Intersci. Conf. Antimicrob Agents Chemother; 2008
    • Hull, K.1    Green, O.2    Singh, A.3
  • 30
    • 0030893658 scopus 로고    scopus 로고
    • The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin
    • Tsai FT, Singh OM, Skarzynski T, et al. The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin. Proteins 1997;28:41-52
    • (1997) Proteins , vol.28 , pp. 41-52
    • Tsai, F.T.1    Singh, O.M.2    Skarzynski, T.3
  • 31
    • 33947476615 scopus 로고
    • 1,8-naphthyridine derivatives. A new class of chemotherapeutic agents
    • Lesher GY, Froelich EJ, Gruett MD, et al. 1,8-naphthyridine derivatives. A new class of chemotherapeutic agents. J Med Pharm Chem 1962;91:1063-5
    • (1962) J Med Pharm Chem , vol.91 , pp. 1063-1065
    • Lesher, G.Y.1    Froelich, E.J.2    Gruett, M.D.3
  • 32
    • 1642543137 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis DNA Gyrase: Interaction with Quinolones and Correlation with Antimycobacterial Drug Activity
    • DOI 10.1128/AAC.48.4.1281-1288.2004
    • Aubry A, Pan XS, Fisher LM, et al. Mycobacterium tuberculosis DNA gyrase: interaction with quinolones and correlation with antimycobacterial drug activity. Antimicrob Agents Chemother 2004;48:1281-8 (Pubitemid 38405482)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.4 , pp. 1281-1288
    • Aubry, A.1    Pan, X.-S.2    Fisher, L.M.3    Jarlier, V.4    Cambau, E.5
  • 34
    • 0029991326 scopus 로고    scopus 로고
    • DNA gyrase and topoisomerase IV on the bacterial chromosome: Quinolone-induced DNA cleavage
    • DOI 10.1006/jmbi.1996.0274
    • Chen CR, Malik M, Snyder M, et al. DNA gyrase and topoisomerase IV on the bacterial chromosome: quinolone-induced DNA cleavage. J Mol Biol 1996;258:627-37 (Pubitemid 26145906)
    • (1996) Journal of Molecular Biology , vol.258 , Issue.4 , pp. 627-637
    • Chen, C.-R.1    Malik, M.2    Snyder, M.3    Drlica, K.4
  • 35
    • 38649088911 scopus 로고    scopus 로고
    • Quinolone-mediated bacterial death
    • DOI 10.1128/AAC.01617-06
    • Drlica K, Malik M, Kerns RJ, et al. Quinolone-mediated bacterial death. Antimicrob Agents Chemother 2008;52:385-92 Interesting paper on how quinolones kill bacteria. (Pubitemid 351170804)
    • (2008) Antimicrobial Agents and Chemotherapy , vol.52 , Issue.2 , pp. 385-392
    • Drlica, K.1    Malik, M.2    Kerns, R.J.3    Zhao, X.4
  • 36
    • 33947247352 scopus 로고    scopus 로고
    • Gyrase inhibitors induce an oxidative damage cellular death pathway in Escherichia coli
    • Dwyer DJ, Kohanski MA, Hayete B, et al. Gyrase inhibitors induce an oxidative damage cellular death pathway in Escherichia coli. Mol Syst Biol 2007;3:91
    • (2007) Mol Syst Biol , vol.3 , pp. 91
    • Dwyer, D.J.1    Kohanski, M.A.2    Hayete, B.3
  • 37
    • 77952884274 scopus 로고    scopus 로고
    • How antibiotics kill bacteria: From targets to networks
    • Kohanski MA, Dwyer DJ, Collins JJ. How antibiotics kill bacteria: from targets to networks. Nat Rev Microbiol 2010;8:423-35
    • (2010) Nat Rev Microbiol , vol.8 , pp. 423-435
    • Kohanski, M.A.1    Dwyer, D.J.2    Collins, J.J.3
  • 38
    • 0017697662 scopus 로고
    • Repair of DNA double strand breaks in Escherichia coli, which requires recA function and the presence of a duplicate genome
    • DOI 10.1016/0022-2836(77)90120-6
    • Krasin F, Hutchinson F. Repair of DNA double-strand breaks in Escherichia coli, which requires recA function and the presence of a duplicate genome. J Mol Biol 1977;116:81-98 (Pubitemid 8205769)
    • (1977) Journal of Molecular Biology , vol.116 , Issue.1 , pp. 81-98
    • Krasin, F.1    Hutchinson, F.2
  • 39
    • 0025930861 scopus 로고
    • Quinolone resistance-determining region in the DNA gyrase gyrB gene of Escherichia coli
    • Yoshida H, Bogaki M, Nakamura M, et al. Quinolone resistance-determining region in the DNA gyrase gyrB gene of Escherichia coli. Antimicrob Agents Chemother 1991;35:1647-50
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 1647-1650
    • Yoshida, H.1    Bogaki, M.2    Nakamura, M.3
  • 40
    • 0036093581 scopus 로고    scopus 로고
    • Quinolone-binding pocket of DNA gyrase: Role of GyrB
    • DOI 10.1128/AAC.46.6.1805-1815.2002
    • Heddle J, Maxwell A. Quinolone-binding pocket of DNA gyrase: role of GyrB. Antimicrob Agents Chemother 2002;46:1805-15 (Pubitemid 34535201)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.6 , pp. 1805-1815
    • Heddle, J.1    Maxwell, A.2
  • 41
    • 0029904283 scopus 로고    scopus 로고
    • DNA cleavage is not required for the binding of quinolone drugs to the DNA gyrase-DNA complex
    • NY
    • Critchlow SE, Maxwell A. DNA cleavage is not required for the binding of quinolone drugs to the DNA gyrase-DNA complex. Biochemistry (NY) 1996;35:7387-93
    • (1996) Biochemistry , vol.35 , pp. 7387-7393
    • Critchlow, S.E.1    Maxwell, A.2
  • 42
    • 0030962482 scopus 로고    scopus 로고
    • Mechanism of quinolone action. A drug-induced structural perturbation of the DNA precedes strand cleavage by topoisomerase IV
    • DOI 10.1074/jbc.272.14.9401
    • Marians KJ, Hiasa H. Mechanism of quinolone action. A drug-induced structural perturbation of the DNA precedes strand cleavage by topoisomerase IV. J Biol Chem 1997;272:9401-9 (Pubitemid 27154954)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 9401-9409
    • Marians, K.J.1    Hiasa, H.2
  • 43
    • 0032575668 scopus 로고    scopus 로고
    • The DNA gyrase-quinolone complex. ATP hydrolysis and the mechanism of DNA cleavage
    • DOI 10.1074/jbc.273.35.22615
    • Kampranis SC, Maxwell A. The DNA gyrase-quinolone complex. ATP hydrolysis and the mechanism of DNA cleavage. J Biol Chem 1998;273:22615-26 (Pubitemid 28399831)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.35 , pp. 22615-22626
    • Kampranis, S.C.1    Maxwell, A.2
  • 44
    • 0027210004 scopus 로고
    • Function of the SOS process in repair of DNA damage induced by modern 4-quinolones
    • Howard BM, Pinney RJ, Smith JT. Function of the SOS process in repair of DNA damage induced by modern 4-quinolones. J Pharm Pharmacol 1993;45:658-62 (Pubitemid 23226761)
    • (1993) Journal of Pharmacy and Pharmacology , vol.45 , Issue.7 , pp. 658-662
    • Howard, B.M.A.1    Pinney, R.J.2    Smith, J.T.3
  • 45
    • 34548213103 scopus 로고    scopus 로고
    • A Common Mechanism of Cellular Death Induced by Bactericidal Antibiotics
    • DOI 10.1016/j.cell.2007.06.049, PII S0092867407008999
    • Kohanski MA, Dwyer DJ, Hayete B, et al. A common mechanism of cellular death induced by bactericidal antibiotics. Cell 2007;130:797-810 (Pubitemid 47332566)
    • (2007) Cell , vol.130 , Issue.5 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 46
    • 77950325093 scopus 로고    scopus 로고
    • Contribution of reactive oxygen species to pathways of quinolone-mediated bacterial cell death
    • Wang X, Zhao X, Malik M, et al. Contribution of reactive oxygen species to pathways of quinolone-mediated bacterial cell death. J Antimicrob Chemother 2010;65:520-4
    • (2010) J Antimicrob Chemother , vol.65 , pp. 520-524
    • Wang, X.1    Zhao, X.2    Malik, M.3
  • 47
    • 77955917935 scopus 로고    scopus 로고
    • Type IIA topoisomerase inhibition by a new class of antibacterial agents
    • Reports crystal structure of a DNA gyrase construct bound to novel quinolines
    • Bax BD, Chan PF, Eggleston DS, et al. Type IIA topoisomerase inhibition by a new class of antibacterial agents. Nature 2010;466:935-40 Reports crystal structure of a DNA gyrase construct bound to novel quinolines.
    • (2010) Nature , vol.466 , pp. 935-940
    • Bax, B.D.1    Chan, P.F.2    Eggleston, D.S.3
  • 48
    • 77956343814 scopus 로고    scopus 로고
    • Structural basis of quinolone inhibition of type IIA topoisomerases and target-mediated resistance
    • Wohlkonig A, Chan PF, Fosberry AP, et al. Structural basis of quinolone inhibition of type IIA topoisomerases and target-mediated resistance. Nat Struct Mol Biol 2010;17:1152-3
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1152-1153
    • Wohlkonig, A.1    Chan, P.F.2    Fosberry, A.P.3
  • 49
    • 67349272340 scopus 로고    scopus 로고
    • Structural insight into the quinolone-DNA cleavage complex of type IIA topoisomerases
    • Laponogov I, Sohi MK, Veselkov DA, et al. Structural insight into the quinolone-DNA cleavage complex of type IIA topoisomerases. Nat Struct Mol Biol 2009;16:667-9
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 667-669
    • Laponogov, I.1    Sohi, M.K.2    Veselkov, D.A.3
  • 50
    • 77955334540 scopus 로고    scopus 로고
    • Structural basis of gate-DNA breakage and resealing by type II topoisomerases
    • Electronic Resource
    • Laponogov I, Pan XS, Veselkov DA, et al. Structural basis of gate-DNA breakage and resealing by type II topoisomerases. [Electronic Resource]. PLoS ONE 2010;5:e11338
    • (2010) PLoS ONE , vol.5
    • Laponogov, I.1    Pan, X.S.2    Veselkov, D.A.3
  • 51
    • 35548999431 scopus 로고    scopus 로고
    • Breakage-reunion domain of streptococcus pneumoniae topoisomerase IV: Crystal structure of a gram-positive quinolone target
    • Electronic Resource
    • Laponogov I, Veselkov DA, Sohi MK, et al. Breakage-reunion domain of streptococcus pneumoniae topoisomerase IV: crystal structure of a gram-positive quinolone target [Electronic Resource]. PLoS ONE 2007;2:e301
    • (2007) PLoS ONE , vol.2
    • Laponogov, I.1    Veselkov, D.A.2    Sohi, M.K.3
  • 52
    • 54849420897 scopus 로고    scopus 로고
    • Recent advances in bacterial topoisomerase inhibitors
    • Key review of bacterial topoisomerase type II inhibitors, especially quinolones
    • Bradbury BJ, Pucci MJ. Recent advances in bacterial topoisomerase inhibitors. Curr Opin Pharmacol 2008;8:574-81 Key review of bacterial topoisomerase type II inhibitors, especially quinolones.
    • (2008) Curr Opin Pharmacol , vol.8 , pp. 574-581
    • Bradbury, B.J.1    Pucci, M.J.2
  • 53
    • 33947701471 scopus 로고    scopus 로고
    • Exploring DNA topoisomerases as targets of novel therapeutic agents in the treatment of infectious diseases
    • Tse-Dinh YC. Exploring DNA topoisomerases as targets of novel therapeutic agents in the treatment of infectious diseases. Infect Disord Drug Targets 2007;7:3-9
    • (2007) Infect Disord Drug Targets , vol.7 , pp. 3-9
    • Tse-Dinh, Y.C.1
  • 55
    • 33645791657 scopus 로고    scopus 로고
    • In vitro characterization of the antibacterial spectrum of novel bacterial type II topoisomerase inhibitors of the aminobenzimidazole class
    • Mani N, Gross CH, Parsons JD, et al. In vitro characterization of the antibacterial spectrum of novel bacterial type II topoisomerase inhibitors of the aminobenzimidazole class. Antimicrob Agents Chemother 2006;50:1228-37
    • (2006) Antimicrob Agents Chemother , vol.50 , pp. 1228-1237
    • Mani, N.1    Gross, C.H.2    Parsons, J.D.3
  • 57
    • 50949110901 scopus 로고    scopus 로고
    • Mechanism of action of the antibiotic NXL101, a novel nonfluoroquinolone inhibitor of bacterial type II topoisomerases
    • Black MT, Stachyra T, Platel D, et al. Mechanism of action of the antibiotic NXL101, a novel nonfluoroquinolone inhibitor of bacterial type II topoisomerases. Antimicrob Agents Chemother 2008;52:3339-49
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 3339-3349
    • Black, M.T.1    Stachyra, T.2    Platel, D.3
  • 58
    • 84859313941 scopus 로고    scopus 로고
    • Gyrase inhibiting antibacterial agents: Structure-activity relationships for four isomeric tetrahydronaphthyridine spirocyclic pyrimidinetrionesimidinetriones
    • abstract F1-1839.
    • Basarab GS, Beaudoin M-, Brassil P, et al. Gyrase inhibiting antibacterial agents: Structure-activity relationships for four isomeric tetrahydronaphthyridine spirocyclic pyrimidinetrionesimidinetriones [abstract F1-1839]. 51st Intersci. Conf. Antimicrob Agents Chemother; 2011
    • 51st Intersci. Conf. Antimicrob Agents Chemother; 2011
    • Basarab, G.S.1    Beaudoin, M.2    Brassil, P.3
  • 59
    • 48749117988 scopus 로고    scopus 로고
    • Discovery and characterization of QPT-1, the progenitor of a new class of bacterial topoisomerase inhibitors
    • Miller AA, Bundy GL, Mott JE, et al. Discovery and characterization of QPT-1, the progenitor of a new class of bacterial topoisomerase inhibitors. Antimicrob Agents Chemother 2008;52:2806-12
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 2806-2812
    • Miller, A.A.1    Bundy, G.L.2    Mott, J.E.3
  • 60
    • 81555223850 scopus 로고    scopus 로고
    • Novel N-linked aminopiperidine inhibitors of bacterial topoisomerase type II: Broad-spectrum antibacterial agents with reduced hERG activity
    • Reck F, Alm R, Brassil P, et al. Novel N-linked aminopiperidine inhibitors of bacterial topoisomerase type II: broad-spectrum antibacterial agents with reduced hERG activity. J Med Chem 2011;54:7834-47
    • (2011) J Med Chem , vol.54 , pp. 7834-7847
    • Reck, F.1    Alm, R.2    Brassil, P.3
  • 63
    • 81255157631 scopus 로고    scopus 로고
    • Novel cyclohexyl-amides as potent antibacterials targeting bacterial type IIA topoisomerases
    • Miles TJ, Barfoot C, Brooks G, et al. Novel cyclohexyl-amides as potent antibacterials targeting bacterial type IIA topoisomerases. Bioorg Med Chem Lett 2011;21:7483-8
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 7483-7488
    • Miles, T.J.1    Barfoot, C.2    Brooks, G.3
  • 64
    • 81255208413 scopus 로고    scopus 로고
    • Novel amino-piperidines as potent antibacterials targeting bacterial type IIA topoisomerases
    • Miles TJ, Axten JM, Barfoot C, et al. Novel amino-piperidines as potent antibacterials targeting bacterial type IIA topoisomerases. Bioorg Med Chem Lett 2011;21:7489-95
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 7489-7495
    • Miles, T.J.1    Axten, J.M.2    Barfoot, C.3
  • 65
    • 80051932934 scopus 로고    scopus 로고
    • Exploring left-hand-side substitutions in the benzoxazinone series of 4-amino-piperidine bacterial type IIa topoisomerase inhibitors
    • Geng B, Comita-Prevoir J, Eyermann CJ, et al. Exploring left-hand-side substitutions in the benzoxazinone series of 4-amino-piperidine bacterial type IIa topoisomerase inhibitors. Bioorg Med Chem Lett 2011;21:5432-5
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 5432-5435
    • Geng, B.1    Comita-Prevoir, J.2    Eyermann, C.J.3
  • 69
    • 34147112254 scopus 로고    scopus 로고
    • Concise synthesis of the bacterial DNA primase inhibitor (+) -sch 642305
    • Wilson EM, Trauner D. Concise synthesis of the bacterial DNA primase inhibitor (+) -sch 642305. Org Lett 2007;9:1327-9
    • (2007) Org Lett , vol.9 , pp. 1327-1329
    • Wilson, E.M.1    Trauner, D.2
  • 70
    • 35348948949 scopus 로고    scopus 로고
    • Stereoselective synthesis of the bacterial DNA primase inhibitor Sch 642305 and its C-4 epimer
    • DOI 10.1016/j.tet.2007.09.080, PII S0040402007016705
    • Garcia-Fortanet J, Carda M, Marco JA. Stereoselective synthesis of the bacterial DNA primase inhibitor sch 642305 and its C-4 epimer. Tetrahedron 2007;63:12131-7 (Pubitemid 47600291)
    • (2007) Tetrahedron , vol.63 , Issue.49 , pp. 12131-12137
    • Garcia-Fortanet, J.1    Carda, M.2    Alberto, M.J.3
  • 72
    • 44249097571 scopus 로고    scopus 로고
    • Staphylococcus aureus primase has higher initiation specificity, interacts with single-stranded DNA stronger, but is less stimulated by its helicase than Escherichia coli primase
    • DOI 10.1111/j.1365-2958.2008.06255.x
    • Koepsell SA, Larson MA, Frey CA, et al. Staphylococcus aureus primase has higher initiation specificity, interacts with single-stranded DNA stronger, but is less stimulated by its helicase than Escherichia coli primase. Mol Microbiol 2008;68:1570-82 (Pubitemid 351725266)
    • (2008) Molecular Microbiology , vol.68 , Issue.6 , pp. 1570-1582
    • Koepsell, S.A.1    Larson, M.A.2    Frey, C.A.3    Hinrichs, S.H.4    Griep, M.A.5
  • 73
    • 0002250965 scopus 로고    scopus 로고
    • DNA helicases
    • ML DePamphilis. editor. Cold Spring Harbor Laboratory Press; NY
    • Borowiec JA. DNA helicases. In: ML DePamphilis. editor. DNA Replication in Eukaryotic Cells. Cold Spring Harbor Laboratory Press; NY: 1996. p. 545-74
    • (1996) DNA Replication in Eukaryotic Cells , pp. 545-574
    • Borowiec, J.A.1
  • 74
    • 84859332566 scopus 로고    scopus 로고
    • Protein-protein interactions in the bacterial replisome
    • Schaeffer P, Headlam M, Dixon N. Protein-protein interactions in the bacterial replisome. Aust Biochem 2004;35:9-12
    • (2004) Aust Biochem , vol.35 , pp. 9-12
    • Schaeffer, P.1    Headlam, M.2    Dixon, N.3
  • 75
    • 51249093024 scopus 로고    scopus 로고
    • Insights into the replisome from the structure of a ternary complex of the DNA polymerase III alpha-subunit
    • Wing RA, Bailey S, Steitz TA. Insights into the replisome from the structure of a ternary complex of the DNA polymerase III alpha-subunit. J Mol Biol 2008;382:859-69
    • (2008) J Mol Biol , vol.382 , pp. 859-869
    • Wing, R.A.1    Bailey, S.2    Steitz, T.A.3
  • 76
    • 35348979683 scopus 로고    scopus 로고
    • Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
    • DOI 10.1126/science.1147353
    • Bailey S, Eliason WK, Steitz TA. Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science 2007;318:459-63 (Pubitemid 47614533)
    • (2007) Science , vol.318 , Issue.5849 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 77
    • 66449129371 scopus 로고    scopus 로고
    • Discovery, characterization and comparison of inhibitors of Bacillus anthracis and Staphylococcus aureus replicative DNA helicases
    • Aiello D, Barnes MH, Biswas EE, et al. Discovery, characterization and comparison of inhibitors of Bacillus anthracis and Staphylococcus aureus replicative DNA helicases. Bioorg Med Chem 2009;17:4466-76
    • (2009) Bioorg Med Chem , vol.17 , pp. 4466-4476
    • Aiello, D.1    Barnes, M.H.2    Biswas, E.E.3
  • 78
    • 84859363846 scopus 로고    scopus 로고
    • Optimization of coumarin-based inhibitors of Staphylococcus aureus and Bacillus anthracis replicative DNA helicases
    • abstract. F1-1838
    • Moir DT, Li B, Pai R, et al. Optimization of coumarin-based inhibitors of Staphylococcus aureus and Bacillus anthracis replicative DNA helicases [abstract. F1-1838]. 51st Intersci. Conf. Antimicrob Agents Chemother; 2011
    • 51st Intersci. Conf. Antimicrob Agents Chemother; 2011
    • Moir, D.T.1    Li, B.2    Pai, R.3
  • 79
    • 0035213509 scopus 로고    scopus 로고
    • Genetic identification of two distinct DNA polymerases, DnaE and PolC, that are essential for chromosomal dna replication in staphylococcus aureus
    • DOI 10.1007/s004380100564
    • Inoue R, Kaito C, Tanabe M, et al. Genetic identification of two distinct DNA polymerases, DnaE and PolC, that are essential for chromosomal DNA replication in Staphylococcus aureus. Molecular Genet Genomics 2001;266:564-71 (Pubitemid 33145118)
    • (2001) Molecular Genetics and Genomics , vol.266 , Issue.4 , pp. 564-571
    • Inoue, R.1    Kaito, C.2    Tanabe, M.3    Kamura, K.4    Akimitsu, N.5    Sekimizu, K.6
  • 80
    • 0032867111 scopus 로고    scopus 로고
    • Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria
    • Tarantino PM Jr, Zhi C, Wright GE, et al. Inhibitors of DNA polymerase III as novel antimicrobial agents against gram-positive eubacteria. Antimicrob Agents Chemother 1999;43:1982-7 Original report of aniline uracil DNA polymerase inhibitors. (Pubitemid 29395196)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.8 , pp. 1982-1987
    • Tarantino Jr., P.M.1    Zhi, C.2    Wright, G.E.3    Brown, N.C.4
  • 81
    • 0033915251 scopus 로고    scopus 로고
    • In vitro antimicrobial activities of novel anilinouracils which selectively inhibit DNA polymerase III of gram-positive bacteria
    • DOI 10.1128/AAC.44.8.2217-2221.2000
    • Daly JS, Giehl TJ, Brown NC, et al. In vitro antimicrobial activities of novel anilinouracils which selectively inhibit DNA polymerase III of gram-positive bacteria. Antimicrob Agents & Chemother 2000;44:2217-21 (Pubitemid 30484459)
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.8 , pp. 2217-2221
    • Daly, J.S.1    Giehl, T.J.2    Brown, N.C.3    Zhi, C.4    Wright, G.E.5    Ellison III, R.T.6
  • 82
    • 0032403213 scopus 로고    scopus 로고
    • The hyperthermophilic bacterium Thermotoga maritima has two different classes of family C DNA polymerases: Evolutionary implications
    • Huang YP, Ito J. The hyperthermophilic bacterium thermotoga maritima has two different classes of family C DNA polymerases: evolutionary implications. Nucleic Acids Res 1998;26:5300-9 (Pubitemid 28542728)
    • (1998) Nucleic Acids Research , vol.26 , Issue.23 , pp. 5300-5309
    • Huang, Y.-P.1    Ito, J.2
  • 83
    • 33845903833 scopus 로고    scopus 로고
    • Drugs for bad bugs: Confronting the challenges of antibacterial discovery
    • DOI 10.1038/nrd2201, PII NRD2201
    • Payne DJ, Gwynn MN, Holmes DJ, et al. Drugs for bad bugs: confronting the challenges of antibacterial discovery. Nat Rev Drug Discov 2007;6:29-40 Interesting review on the challenges of antibiotic discovery. (Pubitemid 46020284)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.1 , pp. 29-40
    • Payne, D.J.1    Gwynn, M.N.2    Holmes, D.J.3    Pompliano, D.L.4
  • 85
    • 54849417792 scopus 로고    scopus 로고
    • New DNA polymerase IIIC inhibitors: 3-subtituted anilinouracils with potent antibacterial activity in vitro and in vivo
    • Svenstrup N, Ehlert K, Ladel C, et al. New DNA polymerase IIIC inhibitors: 3-subtituted anilinouracils with potent antibacterial activity in vitro and in vivo. ChemMedChem 2008;3:1604-15
    • (2008) ChemMedChem , vol.3 , pp. 1604-1615
    • Svenstrup, N.1    Ehlert, K.2    Ladel, C.3
  • 86
    • 31344436112 scopus 로고    scopus 로고
    • +-dependent DNA ligase is selectively inhibited by glycosylamines compared with human DNA ligase I
    • DOI 10.1093/nar/gki1006
    • Srivastava SK, Dube D, Tewari N, et al. Mycobacterium tuberculosis NAD+- dependent DNA ligase is selectively inhibited by glycosylamines compared with human DNA ligase I. Nucleic Acids Res 2005;33:7090-101 (Pubitemid 43135685)
    • (2005) Nucleic Acids Research , vol.33 , Issue.22 , pp. 7090-7101
    • Srivastava, S.K.1    Dube, D.2    Tewari, N.3    Dwivedi, N.4    Tripathi, R.P.5    Ramachandran, R.6
  • 87
    • 34247279304 scopus 로고    scopus 로고
    • Last Stop on the Road to Repair: Structure of E. coli DNA Ligase Bound to Nicked DNA-Adenylate
    • DOI 10.1016/j.molcel.2007.02.026, PII S109727650700144X
    • Nandakumar J, Nair PA, Shuman S. Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-adenylate. Mol Cell 2007;26:257-71 (Pubitemid 46617333)
    • (2007) Molecular Cell , vol.26 , Issue.2 , pp. 257-271
    • Nandakumar, J.1    Nair, P.A.2    Shuman, S.3
  • 88
    • 0033634655 scopus 로고    scopus 로고
    • Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining
    • Odell M, Sriskanda V, Shuman S, et al. Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining. Mol Cell 2000;6:1183-93
    • (2000) Mol Cell , vol.6 , pp. 1183-1193
    • Odell, M.1    Sriskanda, V.2    Shuman, S.3
  • 89
    • 0034944736 scopus 로고    scopus 로고
    • Bacterial DNA ligases
    • DOI 10.1046/j.1365-2958.2001.02479.x
    • Wilkinson A, Day J, Bowater R. Bacterial DNA ligases. Mol Microbiol 2001;40:1241-8 (Pubitemid 32635295)
    • (2001) Molecular Microbiology , vol.40 , Issue.6 , pp. 1241-1248
    • Wilkinson, A.1    Day, J.2    Bowater, R.3
  • 90
    • 67650538051 scopus 로고    scopus 로고
    • DNA ligases: Progress and prospects
    • A good overview of DNA ligases
    • Shuman S. DNA ligases: progress and prospects. J Biol Chem 2009;284:17365-9 A good overview of DNA ligases.
    • (2009) J Biol Chem , vol.284 , pp. 17365-17369
    • Shuman, S.1
  • 91
    • 39149142191 scopus 로고    scopus 로고
    • DNA and RNA ligases: Structural variations and shared mechanisms
    • Pascal JM. DNA and RNA ligases: structural variations and shared mechanisms. Curr Opin Struct Biol 2008;18:96-105
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 96-105
    • Pascal, J.M.1
  • 93
    • 84858659396 scopus 로고    scopus 로고
    • Structure guided understanding of NAD+ recognition in bacterial DNA ligases
    • In press
    • Lahiri SD, Gu R, Gao N, et al. Structure guided understanding of NAD+ recognition in bacterial DNA ligases. Chem Biol 2012; In press
    • (2012) Chem Biol
    • Lahiri, S.D.1    Gu, R.2    Gao, N.3
  • 94
    • 16844373913 scopus 로고    scopus 로고
    • Structure-guided mutational analysis of the nucleotidyltransferase domain of Escherichia coli NAD+-dependent DNA ligase (LigA)
    • Zhu H, Shuman S. Structure-guided mutational analysis of the nucleotidyltransferase domain of Escherichia coli NAD+-dependent DNA ligase (LigA). J Biol Chem 2005;280:12137-44
    • (2005) J Biol Chem , vol.280 , pp. 12137-12144
    • Zhu, H.1    Shuman, S.2
  • 95
    • 73449135113 scopus 로고    scopus 로고
    • Structure of the adenylation domain of NAD(+)-dependent DNA ligase from Staphylococcus aureus
    • Han S, Chang JS, Griffor M. Structure of the adenylation domain of NAD(+)-dependent DNA ligase from Staphylococcus aureus. Acta Crystallograph Sect F Struct Biol Cryst Commun 2009;65:1078-82
    • (2009) Acta Crystallograph Sect F Struct Biol Cryst Commun , vol.65 , pp. 1078-1082
    • Han, S.1    Chang, J.S.2    Griffor, M.3
  • 97
    • 84859363848 scopus 로고    scopus 로고
    • Crystal structures of DNA ligase from pathogenic bacteria reveal extensive structural conservation and provide critical insight into protein-ligand interaction
    • Pinko C, Chu S, Su Y, et al. Crystal structures of DNA ligase from pathogenic bacteria reveal extensive structural conservation and provide critical insight into protein-ligand interaction. 43rd Interscience Conference on Antimicrobial Agents and Chemotherapy; 2003
    • 43rd Interscience Conference on Antimicrobial Agents and Chemotherapy; 2003
    • Pinko, C.1    Chu, S.2    Su, Y.3
  • 98
    • 4143117765 scopus 로고    scopus 로고
    • + synthesis within a bacterial DNA ligase crystal
    • DOI 10.1016/j.str.2004.05.017, PII S0969212604002357
    • Gajiwala KS, Pinko C. Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal. Structure 2004;12:1449-59 (Pubitemid 39092089)
    • (2004) Structure , vol.12 , Issue.8 , pp. 1449-1459
    • Gajiwala, K.S.1    Pinko, C.2
  • 99
    • 53849127859 scopus 로고    scopus 로고
    • Identification and characterization of an inhibitor specific to bacterial NAD+-dependent DNA ligases
    • Meier TI, Yan D, Peery RB, et al. Identification and characterization of an inhibitor specific to bacterial NAD+-dependent DNA ligases. FEBS J 2008;275:5258-71
    • (2008) FEBS J , vol.275 , pp. 5258-5271
    • Meier, T.I.1    Yan, D.2    Peery, R.B.3
  • 100
    • 79952353538 scopus 로고    scopus 로고
    • Novel bacterial NAD+-dependent DNA ligase inhibitors with broad-spectrum activity and antibacterial efficacy in vivo
    • Biochemical and structural analysis of a novel DNA ligase inhibitors, leading to efficacy in a murine infection model
    • Mills SD, Eakin AE, Buurman ET, et al. Novel bacterial NAD+-dependent DNA ligase inhibitors with broad-spectrum activity and antibacterial efficacy in vivo. Antimicrob Agents Chemother 2011;55:1088-96 Biochemical and structural analysis of a novel DNA ligase inhibitors, leading to efficacy in a murine infection model.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 1088-1096
    • Mills, S.D.1    Eakin, A.E.2    Buurman, E.T.3
  • 101
    • 79960374372 scopus 로고    scopus 로고
    • Discovery of bacterial NAD+-dependent DNA ligase inhibitors: Optimization of antibacterial activity
    • Stokes SS, Huynh H, Gowravaram M, et al. Discovery of bacterial NAD+-dependent DNA ligase inhibitors: optimization of antibacterial activity. Bioorg Med Chem Lett 2011;21:4556-60
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 4556-4560
    • Stokes, S.S.1    Huynh, H.2    Gowravaram, M.3
  • 105
    • 0035945275 scopus 로고    scopus 로고
    • +-dependent DNA ligase (LigB) in Escherichia coli
    • Sriskanda V, Shuman S. A second NAD(+)-dependent DNA ligase (LigB) in Escherichia coli. Nucleic Acids Res 2001;29:4930-4 (Pubitemid 34065406)
    • (2001) Nucleic Acids Research , vol.29 , Issue.24 , pp. 4930-4934
    • Sriskanda, V.1    Shuman, S.2
  • 106
    • 51849112827 scopus 로고    scopus 로고
    • Novel dual-targeting benzimidazole urea inhibitors of DNA gyrase and topoisomerase IV possessing potent antibacterial activity: Intelligent design and evolution through the judicious use of structure-guided design and structure-activity relationships
    • Charifson PS, Grillot AL, Grossman TH, et al. Novel dual-targeting benzimidazole urea inhibitors of DNA gyrase and topoisomerase IV possessing potent antibacterial activity: intelligent design and evolution through the judicious use of structure-guided design and structure-activity relationships. J Med Chem 2008;51:5243-63
    • (2008) J Med Chem , vol.51 , pp. 5243-5263
    • Charifson, P.S.1    Grillot, A.L.2    Grossman, T.H.3
  • 107
    • 37849024100 scopus 로고    scopus 로고
    • The structure of a DnaB-family replicative helicase and its interactions with primase
    • Wang G, Klein MG, Tokonzaba E, et al. The structure of a DnaB-family replicative helicase and its interactions with primase. Nat Struct Mol Biol 2008;15:94-100
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 94-100
    • Wang, G.1    Klein, M.G.2    Tokonzaba, E.3
  • 109
    • 77955982439 scopus 로고    scopus 로고
    • Structural biology in fragment-based drug design
    • Murray CW, Blundell TL. Structural biology in fragment-based drug design. Curr Opin Struct Biol 2010;20:497-507
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 497-507
    • Murray, C.W.1    Blundell, T.L.2
  • 113
    • 51349104146 scopus 로고    scopus 로고
    • Synthesis and antibacterial activity of the C-7 side chain of 3-aminoquinazolinediones
    • Hutchings KM, Tran TP, Ellsworth EL, et al. Synthesis and antibacterial activity of the C-7 side chain of 3-aminoquinazolinediones. Bioorg Med Chem Lett 2008;18:5087-90
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 5087-5090
    • Hutchings, K.M.1    Tran, T.P.2    Ellsworth, E.L.3
  • 115
    • 34447294228 scopus 로고    scopus 로고
    • Design, synthesis, and structure-activity relationship studies of new phenolic DNA gyrase inhibitors
    • DOI 10.1016/j.bmcl.2006.12.065, PII S0960894X06014703
    • Lubbers T, Angehrn P, Gmunder H, et al. Design, synthesis, and structure-activity relationship studies of new phenolic DNA gyrase inhibitors. Bioorg Med Chem Lett 2007;17:4708-14 (Pubitemid 47058923)
    • (2007) Bioorganic and Medicinal Chemistry Letters , vol.17 , Issue.16 , pp. 4708-4714
    • Lubbers, T.1    Angehrn, P.2    Gmunder, H.3    Herzig, S.4
  • 116
    • 79953768958 scopus 로고    scopus 로고
    • A new DNA gyrase inhibitor subclass of the cyclothialidine family based on a bicyclic dilactam-lactone scaffold. synthesis and antibacterial properties
    • Angehrn P, Goetschi E, Gmuender H, et al. A new DNA gyrase inhibitor subclass of the cyclothialidine family based on a bicyclic dilactam-lactone scaffold. synthesis and antibacterial properties. J Med Chem 2011;54:2207-24
    • (2011) J Med Chem , vol.54 , pp. 2207-2224
    • Angehrn, P.1    Goetschi, E.2    Gmuender, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.