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Volumn 2, Issue 8, 2007, Pages 1085-1101

Structural biology approaches to antibacterial drug discovery

Author keywords

Antibacterial agent; Drug target; Eubacteria; Fragment based screening; High throughput screening; Structural genomics; Structure based design

Indexed keywords

3 OXOACYL ACYL CARRIER PROTEIN SYNTHASE 2 INHIBITOR; 3 OXOACYL ACYL CARRIER PROTEIN SYNTHASE 3 INHIBITOR; AMINOGLYCOSIDE ANTIBIOTIC AGENT; ANTIBIOTIC AGENT; BACTERIAL PROTEIN; BAMBERMYCIN; BBT 78484; BL 11B3; CEPHALOSPORIN; CHIR 090; CIPROFLOXACIN; DIHYDROFOLATE REDUCTASE INHIBITOR; ENZYME INHIBITOR; GYRASE INHIBITOR; ICLAPRIM; INDOLINONE; MEMBRANE PROTEIN; MJ 0577; NEAMINE ANALOG 1; NOVOBIOCIN; OXAZOLIDINONE DERIVATIVE; PENICILLIN BINDING PROTEIN; PENICILLIN G; PEPTIDE DEFORMYLASE INHIBITOR; PLATENSIMYCIN; QUINOLINE DERIVED ANTIINFECTIVE AGENT; RX A 8; TRIMETHOPRIM; UNCLASSIFIED DRUG; UNINDEXED DRUG; URIDINE DIPHOSPHATE 3 O (3 HYDROXYMYRISTOYL) N ACETYLGLUCOSAMINE DEACETYLASE INHIBITOR; VRT 752586;

EID: 34548439949     PISSN: 17460441     EISSN: None     Source Type: Journal    
DOI: 10.1517/17460441.2.8.1085     Document Type: Review
Times cited : (6)

References (99)
  • 2
    • 33644517894 scopus 로고    scopus 로고
    • Unmet medical needs in antibacterial therapy
    • RICE LB: Unmet medical needs in antibacterial therapy. Biochem. Pharmacol. (2006) 71:991-995.
    • (2006) Biochem. Pharmacol , vol.71 , pp. 991-995
    • RICE, L.B.1
  • 3
    • 33144473431 scopus 로고    scopus 로고
    • Bad bugs need drugs: An update on the development pipeline from the antimicrobial availability task force of the infectious diseases society of America
    • TALBOT GH, BRADLEY J, EDWARDS JE et al.: Bad bugs need drugs: an update on the development pipeline from the antimicrobial availability task force of the infectious diseases society of America. Clin. Infect. Dis. (2006) 42:657-668.
    • (2006) Clin. Infect. Dis , vol.42 , pp. 657-668
    • TALBOT, G.H.1    BRADLEY, J.2    EDWARDS, J.E.3
  • 4
    • 15544382241 scopus 로고    scopus 로고
    • Innovative antibacterial drugs: Nothing ventured, nothing gained
    • STEIN J: Innovative antibacterial drugs: nothing ventured, nothing gained. Expert Opin. Investig. Drugs (2005) 14(2):107-109.
    • (2005) Expert Opin. Investig. Drugs , vol.14 , Issue.2 , pp. 107-109
    • STEIN, J.1
  • 6
    • 33845894155 scopus 로고    scopus 로고
    • Multi-targeting by monotherapeutic antibacterials
    • SILVER LL: Multi-targeting by monotherapeutic antibacterials. Nat. Rev. Drug Discov. (2007) 6:41-55.
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 41-55
    • SILVER, L.L.1
  • 7
    • 12844274375 scopus 로고    scopus 로고
    • Antibiotics: Where did we go wrong?
    • OVERBYE KM, BARRETT JF: Antibiotics: where did we go wrong? Drug Discov. Today (2005) 10(1):45-52.
    • (2005) Drug Discov. Today , vol.10 , Issue.1 , pp. 45-52
    • OVERBYE, K.M.1    BARRETT, J.F.2
  • 8
    • 33748430340 scopus 로고    scopus 로고
    • Peptide deformylase as an antibacterial target: A critical assessment
    • LEEDS JA, DEAN CR: Peptide deformylase as an antibacterial target: a critical assessment. Curr. Opin. Pharmacol. (2006) 6:445-452.
    • (2006) Curr. Opin. Pharmacol , vol.6 , pp. 445-452
    • LEEDS, J.A.1    DEAN, C.R.2
  • 9
    • 0038779250 scopus 로고    scopus 로고
    • Variable sensitivity to bacterial methionyl-tRNA synthetase inhibitors reveals subpopulations of Streptococcus pneumoniae with two distinct methionly-tRNA synthetase genes
    • GENTRY DR, INGRAHAM KA, STANHOPE MJ et al.: Variable sensitivity to bacterial methionyl-tRNA synthetase inhibitors reveals subpopulations of Streptococcus pneumoniae with two distinct methionly-tRNA synthetase genes. Antimicrob. Agents Chemother. (2003) 47(6):1784-1789.
    • (2003) Antimicrob. Agents Chemother , vol.47 , Issue.6 , pp. 1784-1789
    • GENTRY, D.R.1    INGRAHAM, K.A.2    STANHOPE, M.J.3
  • 10
    • 0034644010 scopus 로고    scopus 로고
    • A triclosan-resistant bacterial enzyme
    • HEATH RJ, ROCK CO: A triclosan-resistant bacterial enzyme. Nature (2000) 406:145.
    • (2000) Nature , vol.406 , pp. 145
    • HEATH, R.J.1    ROCK, C.O.2
  • 12
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • LIPINSKI CA, LOMBARDO F, DOMINY BW, FEENY PJ: Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. (1997) 23:3-25.
    • (1997) Adv. Drug Deliv. Rev , vol.23 , pp. 3-25
    • LIPINSKI, C.A.1    LOMBARDO, F.2    DOMINY, B.W.3    FEENY, P.J.4
  • 13
    • 0036589827 scopus 로고    scopus 로고
    • Knowledge-based approaches in the design and selection of compound libraries for drug discovery
    • VISWANADHAN VN, BALAN C, HULME C, CHEETHAM JC, SUN Y: Knowledge-based approaches in the design and selection of compound libraries for drug discovery. Curr. Opin. Drug Disc. Devel. (2002) 5(3):400-406.
    • (2002) Curr. Opin. Drug Disc. Devel , vol.5 , Issue.3 , pp. 400-406
    • VISWANADHAN, V.N.1    BALAN, C.2    HULME, C.3    CHEETHAM, J.C.4    SUN, Y.5
  • 15
    • 33646112903 scopus 로고    scopus 로고
    • Antibacterial drug discovery and structure-based design
    • BARKER JJ: Antibacterial drug discovery and structure-based design. Drug Discov. Today (2006) 11(9/10):391-404.
    • (2006) Drug Discov. Today , vol.11 , Issue.9-10 , pp. 391-404
    • BARKER, J.J.1
  • 16
    • 33644503872 scopus 로고    scopus 로고
    • Crystallizing new approaches for antimicrobial drug discovery
    • SCHMID MB: Crystallizing new approaches for antimicrobial drug discovery. Biochem. Pharmacol. (2006) 71:1048-1056.
    • (2006) Biochem. Pharmacol , vol.71 , pp. 1048-1056
    • SCHMID, M.B.1
  • 17
    • 0031566958 scopus 로고    scopus 로고
    • A single amino acid substitution in Staphylococcus aureus dihydrofolate reductase determines trimethoprim resistance
    • DALE GE, BROGER C, D'ARCY A et al.: A single amino acid substitution in Staphylococcus aureus dihydrofolate reductase determines trimethoprim resistance, J. Mol. Biol. (1997) 266:23-30.
    • (1997) J. Mol. Biol , vol.266 , pp. 23-30
    • DALE, G.E.1    BROGER, C.2    D'ARCY, A.3
  • 19
    • 33644508373 scopus 로고    scopus 로고
    • Dihydrofolate reductase inhibitors as antibacterial agents
    • HAUSER S, LOCIURO S, ISLAM K: Dihydrofolate reductase inhibitors as antibacterial agents. Biochem. Pharmacol. (2006) 71:941-948.
    • (2006) Biochem. Pharmacol , vol.71 , pp. 941-948
    • HAUSER, S.1    LOCIURO, S.2    ISLAM, K.3
  • 20
    • 0035805213 scopus 로고    scopus 로고
    • Crystal structure of the ribosome at 5.5 Å resolution
    • YUSUPOV MM, YUSUPOVA GZ, BAUCOM A et al.: Crystal structure of the ribosome at 5.5 Å resolution. Science (2001) 292:883-896.
    • (2001) Science , vol.292 , pp. 883-896
    • YUSUPOV, M.M.1    YUSUPOVA, G.Z.2    BAUCOM, A.3
  • 21
    • 0034268836 scopus 로고    scopus 로고
    • Structure of functionally activated small ribosomal subunit at 3.3 A resolution
    • SCHLUENZEN F, TOCIJ A, ZAIRVACH R et al.: Structure of functionally activated small ribosomal subunit at 3.3 A resolution. Cell (2000) 102(5):615-623.
    • (2000) Cell , vol.102 , Issue.5 , pp. 615-623
    • SCHLUENZEN, F.1    TOCIJ, A.2    ZAIRVACH, R.3
  • 23
    • 0035977093 scopus 로고    scopus 로고
    • High resolution structure of the large ribosomal subunit from a mesophilic eubacterium
    • HARMS J, SCHLUENZEN F, ZARIVACH R et al.: High resolution structure of the large ribosomal subunit from a mesophilic eubacterium. Cell (2001) 107(5):679-688.
    • (2001) Cell , vol.107 , Issue.5 , pp. 679-688
    • HARMS, J.1    SCHLUENZEN, F.2    ZARIVACH, R.3
  • 24
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • BAN N, NISSEN P, HANSEN J, MOORE PB, STEITZ TA: The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science (2000) 289:905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • BAN, N.1    NISSEN, P.2    HANSEN, J.3    MOORE, P.B.4    STEITZ, T.A.5
  • 25
    • 33847310868 scopus 로고    scopus 로고
    • Post-translational modifications in the small subunit ribosomal RNA from Thermotoga maritima, including presence of a novel modified cytidine
    • GUYMON R, POMERANTZ SC, ISON JN, CRAIN PF, MCCLOSKEY JA: Post-translational modifications in the small subunit ribosomal RNA from Thermotoga maritima, including presence of a novel modified cytidine. RNA (2007) 13:396-403.
    • (2007) RNA , vol.13 , pp. 396-403
    • GUYMON, R.1    POMERANTZ, S.C.2    ISON, J.N.3    CRAIN, P.F.4    MCCLOSKEY, J.A.5
  • 27
    • 33644610182 scopus 로고    scopus 로고
    • Structure-based drug design meets the ribosome
    • FRANCESCHI F, DUFFY EM: Structure-based drug design meets the ribosome. Biochem. Pharmacol. (2006) 71:1016-1025.
    • (2006) Biochem. Pharmacol , vol.71 , pp. 1016-1025
    • FRANCESCHI, F.1    DUFFY, E.M.2
  • 28
    • 32844459761 scopus 로고    scopus 로고
    • Interactions of designer antibiotics and the ribosomal aminoacyl-tRNA site
    • MURRAY JB, MEROUEH SO, RUSSELL RJM et al.: Interactions of designer antibiotics and the ribosomal aminoacyl-tRNA site. Chem. Biol. (2006) 13:129-138.
    • (2006) Chem. Biol , vol.13 , pp. 129-138
    • MURRAY, J.B.1    MEROUEH, S.O.2    RUSSELL, R.J.M.3
  • 29
    • 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
  • 30
    • 0030758672 scopus 로고    scopus 로고
    • The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant gyrase: A thermodynamic and crystallographic study
    • HOLDGATE GA, TUNNICLIFFE A, WARD WH et al.: The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant gyrase: a thermodynamic and crystallographic study. Biochemistry (1997) 36:9663-9673.
    • (1997) Biochemistry , vol.36 , pp. 9663-9673
    • HOLDGATE, G.A.1    TUNNICLIFFE, A.2    WARD, W.H.3
  • 31
    • 2142814314 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli topoisomerase IV par E subunit (24 and 43 kilodaltons): A single residue dictates differences in novobiocin potency against topoisomerase IV and DNA gyrase
    • BELLON S, PARSONS JD, WEI Y et al.: Crystal structures of Escherichia coli topoisomerase IV par E subunit (24 and 43 kilodaltons): a single residue dictates differences in novobiocin potency against topoisomerase IV and DNA gyrase. Antimicrob. Agents Chemother. (2004) 48(5):1856-1864.
    • (2004) Antimicrob. Agents Chemother , vol.48 , Issue.5 , pp. 1856-1864
    • BELLON, S.1    PARSONS, J.D.2    WEI, Y.3
  • 32
    • 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(4):1228-1237.
    • (2006) Antimicrob. Agents Chemother , vol.50 , Issue.4 , pp. 1228-1237
    • MANI, N.1    GROSS, C.H.2    PARSONS, J.D.3
  • 33
    • 33846582343 scopus 로고    scopus 로고
    • GROSSMANTH, BARTELS DJ, MULLIN S et al.: Dual targeting of GyrB and Par E by a novel aminobenzimidazole class of antibacterial compounds. Antimicrob. Agents Chemother. (2007) 51(2):657-666.
    • GROSSMANTH, BARTELS DJ, MULLIN S et al.: Dual targeting of GyrB and Par E by a novel aminobenzimidazole class of antibacterial compounds. Antimicrob. Agents Chemother. (2007) 51(2):657-666.
  • 35
    • 0026604214 scopus 로고
    • The lipid A biosynthesis mutation lpxA2 of Escherichia coli results in drastic antibiotic supersusceptibility
    • VUORIO R, VAARA M: The lipid A biosynthesis mutation lpxA2 of Escherichia coli results in drastic antibiotic supersusceptibility. Antimicrob. Agents Chemother. (1992) 36:826-829.
    • (1992) Antimicrob. Agents Chemother , vol.36 , pp. 826-829
    • VUORIO, R.1    VAARA, M.2
  • 37
    • 13444287735 scopus 로고    scopus 로고
    • Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: Insights into the mechanism and inhibitor design
    • COGGINS BE, MCCLERREN AL, JIANG L et al.: Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: insights into the mechanism and inhibitor design. Biochemistry (2005) 44:1114-1126.
    • (2005) Biochemistry , vol.44 , pp. 1114-1126
    • COGGINS, B.E.1    MCCLERREN, A.L.2    JIANG, L.3
  • 38
    • 33745602267 scopus 로고    scopus 로고
    • Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase
    • GENNADIOS HA, WHITTINGTON DA, LI X, FIERKE CA, CHRISTIANSON DW: Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase. Biochemistry (2006) 45:7940-7948.
    • (2006) Biochemistry , vol.45 , pp. 7940-7948
    • GENNADIOS, H.A.1    WHITTINGTON, D.A.2    LI, X.3    FIERKE, C.A.4    CHRISTIANSON, D.W.5
  • 39
    • 0034646694 scopus 로고    scopus 로고
    • Antibacterial agents that target lipid A biosynthesis in Gram-negative bacteria
    • JACKMAN JE, FIERKE CA, TUMEY LN et al.: Antibacterial agents that target lipid A biosynthesis in Gram-negative bacteria. J. Biol. Chem. (2000) 275(15):11002-11009.
    • (2000) J. Biol. Chem , vol.275 , Issue.15 , pp. 11002-11009
    • JACKMAN, J.E.1    FIERKE, C.A.2    TUMEY, L.N.3
  • 40
    • 33845951202 scopus 로고    scopus 로고
    • Binding of uridine 5′-diphosphate in the "basic parch" of the zinc-dependent deactylase LpxC and implications for substrate binding
    • GENNADIOS HA, CHRISTIANSON DW: Binding of uridine 5′-diphosphate in the "basic parch" of the zinc-dependent deactylase LpxC and implications for substrate binding. Biochemistry (2006) 45:15216-15223.
    • (2006) Biochemistry , vol.45 , pp. 15216-15223
    • GENNADIOS, H.A.1    CHRISTIANSON, D.W.2
  • 41
    • 10544252685 scopus 로고    scopus 로고
    • ONISHI HR, PELAK BA, GERKENS LS et al.: Antibacterial agents that inhibit lipid A biosynthesis. Science (1996) 274:980-982.
    • ONISHI HR, PELAK BA, GERKENS LS et al.: Antibacterial agents that inhibit lipid A biosynthesis. Science (1996) 274:980-982.
  • 42
    • 0036096165 scopus 로고    scopus 로고
    • Antibacterial activities and characterization of novel inhibitors of Lpx C
    • CLEMENTS JM, COIGNARD F, JOHNSON I et al.: Antibacterial activities and characterization of novel inhibitors of Lpx C. Antimicrob. Agents Chemother. (2002) 46(6):1793-1799.
    • (2002) Antimicrob. Agents Chemother , vol.46 , Issue.6 , pp. 1793-1799
    • CLEMENTS, J.M.1    COIGNARD, F.2    JOHNSON, I.3
  • 43
    • 0037019270 scopus 로고    scopus 로고
    • Potent, novel in vitro inhibitors of the Pseudomonas aeruginosa deacetylase LpxC
    • KLINE T, ANDERSEN NH, HARWOOD EA et al.: Potent, novel in vitro inhibitors of the Pseudomonas aeruginosa deacetylase LpxC. J. Med. Chem. (2002) 45(14):3112-3129.
    • (2002) J. Med. Chem , vol.45 , Issue.14 , pp. 3112-3129
    • KLINE, T.1    ANDERSEN, N.H.2    HARWOOD, E.A.3
  • 44
    • 0037068502 scopus 로고    scopus 로고
    • Inhibition of the antibacterial target UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC): Isoxazoline zinc amidase inhibitors bearing diverse metal binding groups
    • PIRRUNG MC, TUMEY LN, RAETZ CRH et al.: Inhibition of the antibacterial target UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC): isoxazoline zinc amidase inhibitors bearing diverse metal binding groups. J. Med Chem. (2002) 45(19):4359-4370.
    • (2002) J. Med Chem , vol.45 , Issue.19 , pp. 4359-4370
    • PIRRUNG, M.C.1    TUMEY, L.N.2    RAETZ, C.R.H.3
  • 45
    • 33947676835 scopus 로고    scopus 로고
    • Inhibition of lipid A biosynthesis as the primary mechanism of CHIR-090 antibiotic activity in Escherichia coli
    • BARB AW, MCCLERREN AL, SNEHELATHA K et al.: Inhibition of lipid A biosynthesis as the primary mechanism of CHIR-090 antibiotic activity in Escherichia coli. Biochemistry (2007) 46(12):3793-3802.
    • (2007) Biochemistry , vol.46 , Issue.12 , pp. 3793-3802
    • BARB, A.W.1    MCCLERREN, A.L.2    SNEHELATHA, K.3
  • 46
    • 0034780806 scopus 로고    scopus 로고
    • Bacterial fatty acid biosynthesis: Targets for antibacterial drug discovery
    • CAMPBELL JW, CRONAN JE: Bacterial fatty acid biosynthesis: targets for antibacterial drug discovery. Annu. Rev. Microbiol. (2001) 55:305-332.
    • (2001) Annu. Rev. Microbiol , vol.55 , pp. 305-332
    • CAMPBELL, J.W.1    CRONAN, J.E.2
  • 47
    • 0034651317 scopus 로고    scopus 로고
    • The 1.8 Å crystal structure and active-site architecture of β-ketoacyl-acyl carrier protein synthase III (FabH) from Escherichia coli
    • DAVIES C, HEATH RJ, WHITE SW, ROCK CO: The 1.8 Å crystal structure and active-site architecture of β-ketoacyl-acyl carrier protein synthase III (FabH) from Escherichia coli. Structure (2000) 8:185-195.
    • (2000) Structure , vol.8 , pp. 185-195
    • DAVIES, C.1    HEATH, R.J.2    WHITE, S.W.3    ROCK, C.O.4
  • 48
    • 0035896021 scopus 로고    scopus 로고
    • Refined structures of β-ketoacyl-acyl carrier protein synthase III
    • QUI X, JANSON CA, SMITH WW et al.: Refined structures of β-ketoacyl-acyl carrier protein synthase III. J. Mol. Biol. (2001) 307:341-356.
    • (2001) J. Mol. Biol , vol.307 , pp. 341-356
    • QUI, X.1    JANSON, C.A.2    SMITH, W.W.3
  • 49
    • 23644436692 scopus 로고    scopus 로고
    • Crystal structure and substrate specificity of the β-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus
    • QIU X, CHOUDHRY AE, JANSON CA et al.: Crystal structure and substrate specificity of the β-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus. Protein Sci. (2005) 14:2087-2094.
    • (2005) Protein Sci , vol.14 , pp. 2087-2094
    • QIU, X.1    CHOUDHRY, A.E.2    JANSON, C.A.3
  • 50
    • 13844296950 scopus 로고    scopus 로고
    • Crystal structure of a substrate complex of Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A
    • MUSAYEV F, SACHDEVA S, SCARSDALE JN, REYNOLDS KA, WRIGHT HT: Crystal structure of a substrate complex of Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A. J. Mol. Biol. (2005) 346:1313-1321.
    • (2005) J. Mol. Biol , vol.346 , pp. 1313-1321
    • MUSAYEV, F.1    SACHDEVA, S.2    SCARSDALE, J.N.3    REYNOLDS, K.A.4    WRIGHT, H.T.5
  • 51
    • 0037413576 scopus 로고    scopus 로고
    • First X-ray co-crystal structure of a bacterial FabH condensing enzyme and a small molecule inhibitor achieved using rational design and homology modeling
    • DAINES RA, PENDRAK I, SHAM K et al.: First X-ray co-crystal structure of a bacterial FabH condensing enzyme and a small molecule inhibitor achieved using rational design and homology modeling. J. Med Chem. (2003) 46(1):5-8.
    • (2003) J. Med Chem , vol.46 , Issue.1 , pp. 5-8
    • DAINES, R.A.1    PENDRAK, I.2    SHAM, K.3
  • 52
    • 33744994317 scopus 로고    scopus 로고
    • Platensimycin is a selective FabF inhibitor with potent antibiotic properties
    • WANG J, SOISSON SM, YOUNG K et al.: Platensimycin is a selective FabF inhibitor with potent antibiotic properties. Nature (2006) 441:358-361.
    • (2006) Nature , vol.441 , pp. 358-361
    • WANG, J.1    SOISSON, S.M.2    YOUNG, K.3
  • 53
    • 20144370577 scopus 로고    scopus 로고
    • Structure-based design, synthesis and study of potent inhibitors of β-ketoacyl-acyl carrier protein synthase III as potential antimicrobial agents
    • NIE Z, PERRETTA C, LU J et al.: Structure-based design, synthesis and study of potent inhibitors of β-ketoacyl-acyl carrier protein synthase III as potential antimicrobial agents. J. Med. Chem. (2005) 48:1596-1609.
    • (2005) J. Med. Chem , vol.48 , pp. 1596-1609
    • NIE, Z.1    PERRETTA, C.2    LU, J.3
  • 54
    • 31944450795 scopus 로고    scopus 로고
    • Discovery of FabF/FabH inhibitors from natural products
    • YOUNG K, JAYASURIYA H, ONDEYKA JG et al.: Discovery of FabF/FabH inhibitors from natural products. Antimicrob. Agents Chemother. (2006) 50(2):519-526.
    • (2006) Antimicrob. Agents Chemother , vol.50 , Issue.2 , pp. 519-526
    • YOUNG, K.1    JAYASURIYA, H.2    ONDEYKA, J.G.3
  • 55
    • 0035856021 scopus 로고    scopus 로고
    • Helicobacter pylori infection and the development of gastric cancer
    • UEMURA N, OKAMATO S, YAMAMOTO S et al.: Helicobacter pylori infection and the development of gastric cancer. N. Engl. J. Med. (2001) 345(11):784-789.
    • (2001) N. Engl. J. Med , vol.345 , Issue.11 , pp. 784-789
    • UEMURA, N.1    OKAMATO, S.2    YAMAMOTO, S.3
  • 56
    • 27644453362 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in Bacillus subtilis glutamate racemase and their implications for drug discovery
    • RUZHEINIKOV SN, TAAL MA, SEDELNIKOVA SE, BAKER PJ, RICE DW: Substrate-induced conformational changes in Bacillus subtilis glutamate racemase and their implications for drug discovery. Structure (2005) 13:1707-1713.
    • (2005) Structure , vol.13 , pp. 1707-1713
    • RUZHEINIKOV, S.N.1    TAAL, M.A.2    SEDELNIKOVA, S.E.3    BAKER, P.J.4    RICE, D.W.5
  • 57
    • 34548437000 scopus 로고    scopus 로고
    • Identification and biochemical characterization of agents selective for Helicobacter pylori glutamate racemase
    • Washington, DC, USA
    • FISHER SL, KERN G, NEWTON T et al.: Identification and biochemical characterization of agents selective for Helicobacter pylori glutamate racemase. In: Interscience Conference on Antimicrobial Agents and Chemotherapy. Washington, DC, USA (2005).
    • (2005) Interscience Conference on Antimicrobial Agents and Chemotherapy
    • FISHER, S.L.1    KERN, G.2    NEWTON, T.3
  • 58
    • 34548453620 scopus 로고    scopus 로고
    • Design and synthesis of potent and selective inhibitors of Helicobacter pylori glutamate racemase (MurI) Poster F-1877
    • Washington, DC, USA
    • GOWRAVRAM M, BASARAB G, EYERMANN C et al.: Design and synthesis of potent and selective inhibitors of Helicobacter pylori glutamate racemase (MurI) Poster F-1877. In: Interscience Conference on Antimicrobial Agents and Chemotherapy. Washington, DC, USA (2005).
    • (2005) Interscience Conference on Antimicrobial Agents and Chemotherapy
    • GOWRAVRAM, M.1    BASARAB, G.2    EYERMANN, C.3
  • 59
    • 34248400401 scopus 로고    scopus 로고
    • Crystal ctructure of a peptidoglycan glycosyltransferase suggests a model of processive glycan chain synthesis
    • YUAN Y, BARRETT D, ZHANG Y et al.: Crystal ctructure of a peptidoglycan glycosyltransferase suggests a model of processive glycan chain synthesis. Proc. Natl. Acad. Sci. USA (2007) 104:5348-5353.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 5348-5353
    • YUAN, Y.1    BARRETT, D.2    ZHANG, Y.3
  • 60
    • 33947132188 scopus 로고    scopus 로고
    • Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis
    • LOVERING AL, CASTRO LHD, LIM D, STRYNADKA NCJ: Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis. Science (2007) 315:1402-1405.
    • (2007) Science , vol.315 , pp. 1402-1405
    • LOVERING, A.L.1    CASTRO, L.H.D.2    LIM, D.3    STRYNADKA, N.C.J.4
  • 61
    • 33644499476 scopus 로고    scopus 로고
    • Practical applications and feasibility of efflux pump inhibitors in the clinic - a vision for applied use
    • LOMOVSKAYA O, BOSTIAN KA: Practical applications and feasibility of efflux pump inhibitors in the clinic - a vision for applied use. Biochem. Pharmacol. (2006) 71:910-918.
    • (2006) Biochem. Pharmacol , vol.71 , pp. 910-918
    • LOMOVSKAYA, O.1    BOSTIAN, K.A.2
  • 63
    • 23244458270 scopus 로고    scopus 로고
    • SILVER LL: A retrospective on the failures and successes of antibacterial drug discovery. IDrugsi (2005) 8(8):651-655.
    • SILVER LL: A retrospective on the failures and successes of antibacterial drug discovery. IDrugsi (2005) 8(8):651-655.
  • 64
    • 21544464022 scopus 로고    scopus 로고
    • Functional genomics in antibacterial drug discovery
    • FREIBERG C, BROTZ-OESTERHELT H: Functional genomics in antibacterial drug discovery. Drug Discov. Today (2005) 10(13):927-935.
    • (2005) Drug Discov. Today , vol.10 , Issue.13 , pp. 927-935
    • FREIBERG, C.1    BROTZ-OESTERHELT, H.2
  • 65
    • 0032905858 scopus 로고    scopus 로고
    • A brighter future for protein structure prediction
    • KOEHL P, LEVITT M: A brighter future for protein structure prediction. Nat. Struct. Biol. (1999) 6(2):108-111.
    • (1999) Nat. Struct. Biol , vol.6 , Issue.2 , pp. 108-111
    • KOEHL, P.1    LEVITT, M.2
  • 66
    • 1042264059 scopus 로고    scopus 로고
    • Searching for functional sites in protein structures
    • JONES S, THORNTON JM: Searching for functional sites in protein structures. Curr. Opin. Chem. Biol. (2004) 8(1):3-7.
    • (2004) Curr. Opin. Chem. Biol , vol.8 , Issue.1 , pp. 3-7
    • JONES, S.1    THORNTON, J.M.2
  • 68
    • 1442336002 scopus 로고    scopus 로고
    • PSI-Phase I and beyond
    • KONFORTI B: PSI-Phase I and beyond. Nat. Struct. Mol. Biol. (2004) 11(3):201.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , Issue.3 , pp. 201
    • KONFORTI, B.1
  • 69
    • 4344592748 scopus 로고    scopus 로고
    • The impact of structural genomics on the protein data bank
    • BERMAN HM, WESTBROOK JD: The impact of structural genomics on the protein data bank. Am. J. Pharmacogenomics (2004) 4(4):247-252.
    • (2004) Am. J. Pharmacogenomics , vol.4 , Issue.4 , pp. 247-252
    • BERMAN, H.M.1    WESTBROOK, J.D.2
  • 70
    • 31144467558 scopus 로고    scopus 로고
    • The impact of structural genomics: Expectations and outcomes
    • CHANDONIA JM, BRENNER SE: The impact of structural genomics: expectations and outcomes. Science (2006) 311(5759):347-351.
    • (2006) Science , vol.311 , Issue.5759 , pp. 347-351
    • CHANDONIA, J.M.1    BRENNER, S.E.2
  • 71
    • 4243139636 scopus 로고    scopus 로고
    • Structural genomics on membrane proteins: Mini review
    • LUNDSTROM K: Structural genomics on membrane proteins: mini review. Comb. Chem. High Throughput Screen. (2004) 7(5):431-439.
    • (2004) Comb. Chem. High Throughput Screen , vol.7 , Issue.5 , pp. 431-439
    • LUNDSTROM, K.1
  • 72
    • 4444295503 scopus 로고    scopus 로고
    • Seeing is believing: The impact of structural genomics on antimicrobial drug discovery
    • SCHMID MB: Seeing is believing: the impact of structural genomics on antimicrobial drug discovery. Nat. Rev. Microbiol. (2004) 2(9):739-746.
    • (2004) Nat. Rev. Microbiol , vol.2 , Issue.9 , pp. 739-746
    • SCHMID, M.B.1
  • 73
    • 33745076219 scopus 로고    scopus 로고
    • Advances in homology protein structure modeling
    • XIANG Z: Advances in homology protein structure modeling. Curr. Protein Pept. Sci. (2006) 7(3):217-227.
    • (2006) Curr. Protein Pept. Sci , vol.7 , Issue.3 , pp. 217-227
    • XIANG, Z.1
  • 74
    • 30344459116 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction (CASP) - round 6
    • MOULT J, FIDELIS K, ROST B, HUBBARD T, TRAMONTANO A: Critical assessment of methods of protein structure prediction (CASP) - round 6. Proteins (2005) 61(Suppl. 7):3-7.
    • (2005) Proteins , vol.61 , Issue.SUPPL. 7 , pp. 3-7
    • MOULT, J.1    FIDELIS, K.2    ROST, B.3    HUBBARD, T.4    TRAMONTANO, A.5
  • 75
    • 33646365635 scopus 로고    scopus 로고
    • Rigorous performance evaluation in protein structure modeling and implications for computational biology
    • MOULT J: Rigorous performance evaluation in protein structure modeling and implications for computational biology. Philos. Trans. R. Soc. Lond. B Biol. Sci. (2006) 361(1467):453-458.
    • (2006) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.361 , Issue.1467 , pp. 453-458
    • MOULT, J.1
  • 76
    • 19944431737 scopus 로고    scopus 로고
    • Cell size and nucleoid organization of engineered Escherichia coli cells with a reduced genome
    • HASHIMOTO M, ICHIMURA T, MIZOGUCHI H et al.: Cell size and nucleoid organization of engineered Escherichia coli cells with a reduced genome. Mol. Microbiol. (2005) 55(1):137-149.
    • (2005) Mol. Microbiol , vol.55 , Issue.1 , pp. 137-149
    • HASHIMOTO, M.1    ICHIMURA, T.2    MIZOGUCHI, H.3
  • 77
    • 0141504252 scopus 로고    scopus 로고
    • Experimental determination and system level analysis of essential genes in Escherichia coli MG1655
    • GERDES SY, SCHOLLE MD, CAMPBELL JW et al.: Experimental determination and system level analysis of essential genes in Escherichia coli MG1655. J. Bacteriol. (2003) 185(19):5673-5684.
    • (2003) J. Bacteriol , vol.185 , Issue.19 , pp. 5673-5684
    • GERDES, S.Y.1    SCHOLLE, M.D.2    CAMPBELL, J.W.3
  • 80
    • 12144291286 scopus 로고    scopus 로고
    • A global approach to identify novel broad-spectrum antibacterial targets among proteins of unknown function
    • ZALACAIN M, BISWAS S, INGRAHAM KA et al.: A global approach to identify novel broad-spectrum antibacterial targets among proteins of unknown function. J. Mol. Microbiol. Biotechnol. (2003) 6(2):109-126.
    • (2003) J. Mol. Microbiol. Biotechnol , vol.6 , Issue.2 , pp. 109-126
    • ZALACAIN, M.1    BISWAS, S.2    INGRAHAM, K.A.3
  • 81
    • 0033961632 scopus 로고    scopus 로고
    • Finding function through structural genomics
    • SHAPIRO L, HARRIS T: Finding function through structural genomics. Curr. Opin. Biotechnol. (2000) 11(1):31-35.
    • (2000) Curr. Opin. Biotechnol , vol.11 , Issue.1 , pp. 31-35
    • SHAPIRO, L.1    HARRIS, T.2
  • 82
    • 33947433660 scopus 로고    scopus 로고
    • The crystal structure of Rv0813c from Mycobacterium tuberculosis reveals a new family of fatty acid-binding protein-like proteins in bacteria
    • SHEPARD W, HAOUZ A, GRANA M et al.: The crystal structure of Rv0813c from Mycobacterium tuberculosis reveals a new family of fatty acid-binding protein-like proteins in bacteria. J. Bacteriol. (2007) 189(5):1899-1904.
    • (2007) J. Bacteriol , vol.189 , Issue.5 , pp. 1899-1904
    • SHEPARD, W.1    HAOUZ, A.2    GRANA, M.3
  • 83
    • 0037300533 scopus 로고    scopus 로고
    • Functional annotation of putative aminoglycoside antibiotic modifying proteins in Mycobacterium tuberculosis H37Rv
    • DRAKER KA, BOEHR DD, ELOWE NH, NOGA TJ, WRIGHT GD: Functional annotation of putative aminoglycoside antibiotic modifying proteins in Mycobacterium tuberculosis H37Rv. J. Antibiot. (Tokyo) (2003) 56(2):135-142.
    • (2003) J. Antibiot. (Tokyo) , vol.56 , Issue.2 , pp. 135-142
    • DRAKER, K.A.1    BOEHR, D.D.2    ELOWE, N.H.3    NOGA, T.J.4    WRIGHT, G.D.5
  • 84
    • 17144408302 scopus 로고    scopus 로고
    • The crystal structure of Rv1347c, a putative antibiotic resistance protein from Mycobacterium tuberculosis, reveals a GCN5-related fold and suggests an alternative function in siderophore biosynthesis
    • CARD GL, PETERSON NA, SMITH CA et al.: The crystal structure of Rv1347c, a putative antibiotic resistance protein from Mycobacterium tuberculosis, reveals a GCN5-related fold and suggests an alternative function in siderophore biosynthesis. J. Biol. Chem. (2005) 280(14):13978-13986.
    • (2005) J. Biol. Chem , vol.280 , Issue.14 , pp. 13978-13986
    • CARD, G.L.1    PETERSON, N.A.2    SMITH, C.A.3
  • 86
    • 4444285829 scopus 로고    scopus 로고
    • Crystal structure of YjeQ from Thermotoga maritima contains a circularly permuted GTPase domain
    • SHIN DH, LOU Y, JANCARIK J et al.: Crystal structure of YjeQ from Thermotoga maritima contains a circularly permuted GTPase domain. Proc. Natl. Acad. Sci. USA (2004) 101(36):13198-13203.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.36 , pp. 13198-13203
    • SHIN, D.H.1    LOU, Y.2    JANCARIK, J.3
  • 87
    • 0037125960 scopus 로고    scopus 로고
    • YjeQ, an essential, conserved, uncharacterized protein from Escherichia coli, is an unusual GTPase with circularly permuted G-motifs and marked burst kinetics
    • DAIGLE DM, ROSSI L, BERGHUIS AM et al.: YjeQ, an essential, conserved, uncharacterized protein from Escherichia coli, is an unusual GTPase with circularly permuted G-motifs and marked burst kinetics. Biochemistry (2002) 41(37):11109-11117.
    • (2002) Biochemistry , vol.41 , Issue.37 , pp. 11109-11117
    • DAIGLE, D.M.1    ROSSI, L.2    BERGHUIS, A.M.3
  • 88
    • 0032431024 scopus 로고    scopus 로고
    • Structure-based assignment of the biochemical function of a hypothetical protein: A rest case of structural genomics
    • ZAREMBINSKI TI, HUNG LW, MUELLER-DIECKMANN HJ et al.: Structure-based assignment of the biochemical function of a hypothetical protein: a rest case of structural genomics. Proc. Natl. Acad. Sci. USA (1998) 95(26):15189-15193.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.26 , pp. 15189-15193
    • ZAREMBINSKI, T.I.1    HUNG, L.W.2    MUELLER-DIECKMANN, H.J.3
  • 89
    • 33845458652 scopus 로고    scopus 로고
    • Predicting substrates by docking high-energy intermediates to enzyme structures
    • HERMANN JC, GHANEM E, LI Y et al.: Predicting substrates by docking high-energy intermediates to enzyme structures. J. Am. Chem. Soc. (2006) 128(49):15882-15891.
    • (2006) J. Am. Chem. Soc , vol.128 , Issue.49 , pp. 15882-15891
    • HERMANN, J.C.1    GHANEM, E.2    LI, Y.3
  • 90
    • 34548448070 scopus 로고    scopus 로고
    • Assume that the bacterium is a right rectangular cylinder of 2 μm in height and 0.5 μm in radius capped on each end by a hemisphere of radius 0.5 μm
    • Assume that the bacterium is a right rectangular cylinder of 2 μm in height and 0.5 μm in radius capped on each end by a hemisphere of radius 0.5 μm.
  • 91
    • 31344479308 scopus 로고    scopus 로고
    • Advances in understanding bacterial outer-membrane biogenesis
    • RUIZ N, KAHNE D, SILHAVY TJ: Advances in understanding bacterial outer-membrane biogenesis. Nat. Rev. Microbiol. (2006) 4:57-66.
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 57-66
    • RUIZ, N.1    KAHNE, D.2    SILHAVY, T.J.3
  • 92
    • 1542437307 scopus 로고    scopus 로고
    • Crystallography of membrane proteins
    • WOUTERS J: Crystallography of membrane proteins. Mini Rev. Med. Chem. (2003) 3:439-448.
    • (2003) Mini Rev. Med. Chem , vol.3 , pp. 439-448
    • WOUTERS, J.1
  • 93
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: Strategic advances and lessons learned
    • HAJDUK PJ, GREER J: A decade of fragment-based drug design: strategic advances and lessons learned. Nat. Rev. Drug Disc. (2007) 6:211-219.
    • (2007) Nat. Rev. Drug Disc , vol.6 , pp. 211-219
    • HAJDUK, P.J.1    GREER, J.2
  • 95
    • 22144478634 scopus 로고    scopus 로고
    • Efficient synthetic inhibitors of anthrax lethal factor
    • FIORINO M, JOHNSON S, WQONG TY et al.: Efficient synthetic inhibitors of anthrax lethal factor. Proc. Natl. Acad. Sci. USA (2005) 102(27):9499-9504.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.27 , pp. 9499-9504
    • FIORINO, M.1    JOHNSON, S.2    WQONG, T.Y.3
  • 96
    • 33750067690 scopus 로고    scopus 로고
    • Discovery of novel inhibitors of the ZipA/FtsZ complex by NMR fragment screening coupled with structure-based design
    • TSAO DHH, SUTHERLAND AG, JENNINGS LD et al.: Discovery of novel inhibitors of the ZipA/FtsZ complex by NMR fragment screening coupled with structure-based design. Bioorg. Med. Chem. (2006) 14:7953-7961.
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 7953-7961
    • TSAO, D.H.H.1    SUTHERLAND, A.G.2    JENNINGS, L.D.3
  • 97
    • 14944348527 scopus 로고    scopus 로고
    • A shape-based 3-D scaffold hopping method and its application to a bacterial protein-protein interaction
    • RUSH TSI, GRANT JA, MOSYAK L, NICHOLS A: A shape-based 3-D scaffold hopping method and its application to a bacterial protein-protein interaction. J. Med. Chem. (2005) 48:1489-1495.
    • (2005) J. Med. Chem , vol.48 , pp. 1489-1495
    • RUSH, T.S.I.1    GRANT, J.A.2    MOSYAK, L.3    NICHOLS, A.4
  • 98
    • 1642288258 scopus 로고    scopus 로고
    • Novel inhibitors of DNA gyrase: 3D structure based biased needle screening, hit validation by biophysical methods, and 3-D guided optimization. A promising alternative to random screening
    • BOEHM H-J, BOEHRINGER M, BUR D et al.: Novel inhibitors of DNA gyrase: 3D structure based biased needle screening, hit validation by biophysical methods, and 3-D guided optimization. A promising alternative to random screening. J. Med. Chem. (2000) 43:2664-2674.
    • (2000) J. Med. Chem , vol.43 , pp. 2664-2674
    • BOEHM, H.-J.1    BOEHRINGER, M.2    BUR, D.3
  • 99
    • 33748925426 scopus 로고    scopus 로고
    • Biophysical characterization of an indolinone inhibitor in the ATP-binding site of DNA gyrase
    • OBLAK M, GRDADOLNIK SG, KOTNIK M et al.: Biophysical characterization of an indolinone inhibitor in the ATP-binding site of DNA gyrase. Biochem. Biophys. Res. Commun. (2006) 349(4):1206-1213.
    • (2006) Biochem. Biophys. Res. Commun , vol.349 , Issue.4 , pp. 1206-1213
    • OBLAK, M.1    GRDADOLNIK, S.G.2    KOTNIK, M.3


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