메뉴 건너뛰기




Volumn 3, Issue 9, 2007, Pages 541-548

Targeting virulence: A new paradigm for antimicrobial therapy

Author keywords

[No Author keywords available]

Indexed keywords

2 [(4 FLUORO 3 METHYLPHENYL)SULFONYLAMINO] N HYDROXY 2 (TETRAHYDRO 2H PYRAN 4 YL)ACETAMIDE; ANTIINFECTIVE AGENT; ARGININE; BACTERIAL TOXIN; CIPROFLOXACIN; CISPLATIN; CLOSTRIDIUM TOXIN; FURANONE DERIVATIVE; INP 0400; PILICIDE; PILIN; PYRIDONE DERIVATIVE; TOBRAMYCIN; UNCLASSIFIED DRUG; VIRSTATIN; VIRULENCE FACTOR;

EID: 34548108138     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.2007.24     Document Type: Review
Times cited : (1099)

References (62)
  • 1
    • 0035823272 scopus 로고    scopus 로고
    • Humans as the world's greatest evolutionary force
    • Palumbi, S.R. Humans as the world's greatest evolutionary force. Science 293, 1786-1790 (2001).
    • (2001) Science , vol.293 , pp. 1786-1790
    • Palumbi, S.R.1
  • 2
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: Receptor-binding, internalization, pore formation, and translocation
    • Young, J.A. & Collier, R.J. Anthrax toxin: receptor-binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 76, 243-265 (2007).
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2
  • 3
    • 31744441475 scopus 로고    scopus 로고
    • Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
    • Boyden, E.D. & Dietrich, W.F. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat. Genet. 38, 240-244 (2006).
    • (2006) Nat. Genet , vol.38 , pp. 240-244
    • Boyden, E.D.1    Dietrich, W.F.2
  • 4
    • 18244414803 scopus 로고    scopus 로고
    • Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor
    • Duesbery, N.S. et al. Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. Science 280, 734-737 (1998).
    • (1998) Science , vol.280 , pp. 734-737
    • Duesbery, N.S.1
  • 5
    • 0032581369 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages
    • Vitale, G. et al. Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages. Biochem. Biophys. Res. Commun. 248, 706-711 (1998).
    • (1998) Biochem. Biophys. Res. Commun , vol.248 , pp. 706-711
    • Vitale, G.1
  • 6
    • 33947247554 scopus 로고    scopus 로고
    • Chemical genetic screening identifies critical pathways in anthrax lethal toxin-induced pathogenesis
    • Panchal, R.G. et al. Chemical genetic screening identifies critical pathways in anthrax lethal toxin-induced pathogenesis. Chem. Biol. 14, 245-255 (2007).
    • (2007) Chem. Biol , vol.14 , pp. 245-255
    • Panchal, R.G.1
  • 7
    • 34247643279 scopus 로고    scopus 로고
    • Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation
    • During, R.L. et al. Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation. EMBO J. 26, 2240-2250 (2007).
    • (2007) EMBO J , vol.26 , pp. 2240-2250
    • During, R.L.1
  • 8
    • 4444317796 scopus 로고    scopus 로고
    • Antitoxins: Novel strategies to target agents of bioterrorism
    • Rainey, G.J. & Young, J.A. Antitoxins: novel strategies to target agents of bioterrorism. Nat. Rev. Microbiol. 2, 721-726 (2004).
    • (2004) Nat. Rev. Microbiol , vol.2 , pp. 721-726
    • Rainey, G.J.1    Young, J.A.2
  • 9
    • 20344391159 scopus 로고    scopus 로고
    • Anthrax lethal factor inhibition
    • Shoop, W.L. et al. Anthrax lethal factor inhibition. Proc. Natl. Acad. Sci. USA 102, 7958-7963 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7958-7963
    • Shoop, W.L.1
  • 10
    • 0347192782 scopus 로고    scopus 로고
    • The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor
    • Turk, B.E. et al. The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor. Nat. Struct. Mol. Biol. 11, 60-66 (2004).
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 60-66
    • Turk, B.E.1
  • 11
    • 23044508996 scopus 로고    scopus 로고
    • A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore
    • Krantz, B.A. et al. A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore. Science 309, 777-781 (2005).
    • (2005) Science , vol.309 , pp. 777-781
    • Krantz, B.A.1
  • 12
    • 6944243965 scopus 로고    scopus 로고
    • Artenstein, A.W. et al. Chloroquine enhances survival in Bacillus anthracis intoxication. J. Infect. Dis. 190, 1655-1660 (2004).
    • Artenstein, A.W. et al. Chloroquine enhances survival in Bacillus anthracis intoxication. J. Infect. Dis. 190, 1655-1660 (2004).
  • 13
    • 34447277103 scopus 로고    scopus 로고
    • Amiodarone and bepridil inhibit anthrax toxin entry into host cells
    • Sanchez, A.M. et al. Amiodarone and bepridil inhibit anthrax toxin entry into host cells. Antimicrob. Agents Chemother 51, 2403-2411 (2007).
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 2403-2411
    • Sanchez, A.M.1
  • 15
    • 0036896008 scopus 로고    scopus 로고
    • Thiazolidinone CFTR inhibitor identified by high-throughput screening blocks cholera toxin-induced intestinal fluid secretion
    • Ma, T. et al. Thiazolidinone CFTR inhibitor identified by high-throughput screening blocks cholera toxin-induced intestinal fluid secretion. J. Clin. Invest. 110, 1651-1658 (2002).
    • (2002) J. Clin. Invest , vol.110 , pp. 1651-1658
    • Ma, T.1
  • 16
    • 0019423603 scopus 로고
    • Analysis of the in vitro interaction between vancomycin and cholestyramine
    • King, C.Y. & Barriere, S.L. Analysis of the in vitro interaction between vancomycin and cholestyramine. Antimicrob. Agents Chemother. 19, 326-327 (1981).
    • (1981) Antimicrob. Agents Chemother , vol.19 , pp. 326-327
    • King, C.Y.1    Barriere, S.L.2
  • 17
    • 33845249292 scopus 로고    scopus 로고
    • Protein delivery into eukaryotic cells by type III secretion machines
    • Galan, J.E. & Wolf-Watz, H. Protein delivery into eukaryotic cells by type III secretion machines. Nature 444, 567-573 (2006).
    • (2006) Nature , vol.444 , pp. 567-573
    • Galan, J.E.1    Wolf-Watz, H.2
  • 18
    • 0037350267 scopus 로고    scopus 로고
    • Targeting bacterial virulence: Inhibitors of type III secretion in Yersinia
    • Kauppi, A.M., Nordfelth, R., Uvell, H., Wolf-Watz, H. & Elofsson, M. Targeting bacterial virulence: inhibitors of type III secretion in Yersinia. Chem. Biol. 10, 241-249 (2003).
    • (2003) Chem. Biol , vol.10 , pp. 241-249
    • Kauppi, A.M.1    Nordfelth, R.2    Uvell, H.3    Wolf-Watz, H.4    Elofsson, M.5
  • 20
    • 33749259792 scopus 로고    scopus 로고
    • A small-molecule inhibitor of type III secretion inhibits different stages of the infectious cycle of Chlamydia trachomatis
    • Muschiol, S. et al. A small-molecule inhibitor of type III secretion inhibits different stages of the infectious cycle of Chlamydia trachomatis. Proc. Natl. Acad. Sci. USA 103, 14566-14571 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 14566-14571
    • Muschiol, S.1
  • 21
    • 33846878999 scopus 로고    scopus 로고
    • Small molecule inhibitors of type III secretion in Yersinia block the Chlamydia pneumoniae infection cycle
    • Bailey, L. et al. Small molecule inhibitors of type III secretion in Yersinia block the Chlamydia pneumoniae infection cycle. FEBS Lett. 581, 587-595 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 587-595
    • Bailey, L.1
  • 22
    • 34447273555 scopus 로고    scopus 로고
    • Inhibition of type III secretion in Salmonella enterica serovar Typhimurium by small-molecule inhibitors
    • Hudson, D.L. et al. Inhibition of type III secretion in Salmonella enterica serovar Typhimurium by small-molecule inhibitors. Antimicrob. Agents Chemother 51, 2631-2635 (2007).
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 2631-2635
    • Hudson, D.L.1
  • 23
    • 0023786989 scopus 로고
    • The Eagle effect revisited: Efficacy of clindamycin, erythromycin, and penicillin in the treatment of streptococcal myositis
    • Stevens, D.L., Gibbons, A.E., Bergstrom, R. & Winn, V. The Eagle effect revisited: efficacy of clindamycin, erythromycin, and penicillin in the treatment of streptococcal myositis. J. Infect. Dis. 158, 23-28 (1988).
    • (1988) J. Infect. Dis , vol.158 , pp. 23-28
    • Stevens, D.L.1    Gibbons, A.E.2    Bergstrom, R.3    Winn, V.4
  • 26
    • 0034724191 scopus 로고    scopus 로고
    • AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora
    • Dong, Y.H., Xu, J.L., Li, X.Z. & Zhang, L.H. AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora. Proc. Natl. Acad. Sci. USA 97, 3526-3531 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3526-3531
    • Dong, Y.H.1    Xu, J.L.2    Li, X.Z.3    Zhang, L.H.4
  • 27
    • 0035859128 scopus 로고    scopus 로고
    • Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase
    • Dong, Y.H. et al. Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase. Nature 411, 813-817 (2001).
    • (2001) Nature , vol.411 , pp. 813-817
    • Dong, Y.H.1
  • 28
    • 21244473275 scopus 로고    scopus 로고
    • Quorum quenching enzyme activity is widely conserved in the sera of mammalian species
    • Yang, F. et al. Quorum quenching enzyme activity is widely conserved in the sera of mammalian species. FEBS Lett. 579, 3713-3717 (2005).
    • (2005) FEBS Lett , vol.579 , pp. 3713-3717
    • Yang, F.1
  • 29
    • 21244491480 scopus 로고    scopus 로고
    • Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities
    • Draganov, D.I. et al. Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J. Lipid Res. 46, 1239-1247 (2005).
    • (2005) J. Lipid Res , vol.46 , pp. 1239-1247
    • Draganov, D.I.1
  • 30
    • 33750582503 scopus 로고    scopus 로고
    • Novel Pseudomonas aeruginosa quorum-sensing inhibitors identified in an ultra-high-throughput screen
    • Muh, U. et al. Novel Pseudomonas aeruginosa quorum-sensing inhibitors identified in an ultra-high-throughput screen. Antimicrob. Agents Chemother. 50, 3674-3679 (2006).
    • (2006) Antimicrob. Agents Chemother , vol.50 , pp. 3674-3679
    • Muh, U.1
  • 31
    • 25144448174 scopus 로고    scopus 로고
    • Small molecule inhibitors of bacterial quorum sensing and biofilm formation
    • Geske, G.D., Wezeman, R.J., Siegel, A.P. & Blackwell, H.E. Small molecule inhibitors of bacterial quorum sensing and biofilm formation. J. Am. Chem. Soc. 127, 12762-12763 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 12762-12763
    • Geske, G.D.1    Wezeman, R.J.2    Siegel, A.P.3    Blackwell, H.E.4
  • 32
    • 0037256665 scopus 로고    scopus 로고
    • Induction and inhibition of Pseudomonas aeruginosa quorum sensing by synthtic autoinducer analogs
    • Smith, K.M., Bu, Y. & Suga, H. Induction and inhibition of Pseudomonas aeruginosa quorum sensing by synthtic autoinducer analogs. Chem. Biol. 10, 81-89 (2003).
    • (2003) Chem. Biol , vol.10 , pp. 81-89
    • Smith, K.M.1    Bu, Y.2    Suga, H.3
  • 33
    • 0029854171 scopus 로고    scopus 로고
    • Eukaryotic interference with homoserine lactone-mediated prokaryotic signalling
    • Givskov, M. et al. Eukaryotic interference with homoserine lactone-mediated prokaryotic signalling. J. Bacteriol. 178, 6618-6622 (1996).
    • (1996) J. Bacteriol , vol.178 , pp. 6618-6622
    • Givskov, M.1
  • 34
    • 0036229278 scopus 로고    scopus 로고
    • Halogenated furanones inhibit quorum sensing through accelerated LuxR turnover
    • Manefield, M. et al. Halogenated furanones inhibit quorum sensing through accelerated LuxR turnover. Microbiology 148, 1119-1127 (2002).
    • (2002) Microbiology , vol.148 , pp. 1119-1127
    • Manefield, M.1
  • 35
    • 0035960709 scopus 로고    scopus 로고
    • Halogenated furanones from the red alga, Delisea pulchra, inhibit carbapenem antibiotic synthesis and exoenzyme virulence factor production in the phytopathogen Erwinia carotovora
    • Manefield, M., Welch, M., Givskov, M., Salmond, G.P. & Kjelleberg, S. Halogenated furanones from the red alga, Delisea pulchra, inhibit carbapenem antibiotic synthesis and exoenzyme virulence factor production in the phytopathogen Erwinia carotovora. FEMS Microbiol. Lett. 205, 131-138 (2001).
    • (2001) FEMS Microbiol. Lett , vol.205 , pp. 131-138
    • Manefield, M.1    Welch, M.2    Givskov, M.3    Salmond, G.P.4    Kjelleberg, S.5
  • 36
    • 0036148647 scopus 로고    scopus 로고
    • Inhibition of quorum sensing in Pseudomonas aeruginosa biofilm bacteria by a halogenated furanone compound
    • Hentzer, M. et al. Inhibition of quorum sensing in Pseudomonas aeruginosa biofilm bacteria by a halogenated furanone compound. Microbiology 148, 87-102 (2002).
    • (2002) Microbiology , vol.148 , pp. 87-102
    • Hentzer, M.1
  • 37
    • 0041989633 scopus 로고    scopus 로고
    • Attenuation of Pseudomonas aeruginosa virulence by quorum sensing inhibitors
    • Hentzer, M. et al. Attenuation of Pseudomonas aeruginosa virulence by quorum sensing inhibitors. EMBO J. 22, 3803-3815 (2003).
    • (2003) EMBO J , vol.22 , pp. 3803-3815
    • Hentzer, M.1
  • 38
    • 3042597309 scopus 로고    scopus 로고
    • Synthetic furanones inhibit quorum-sensing and enhance bacterial clearance in Pseudomonas aeruginosa lung infection in mice
    • Wu, H. et al. Synthetic furanones inhibit quorum-sensing and enhance bacterial clearance in Pseudomonas aeruginosa lung infection in mice. J. Antimicrob. Chemother. 53, 1054-1061 (2004).
    • (2004) J. Antimicrob. Chemother , vol.53 , pp. 1054-1061
    • Wu, H.1
  • 39
    • 0036785621 scopus 로고    scopus 로고
    • N-acylhomoserine lactones undergo lactonolysis in a pH-, temperature-, and acyl chain length-dependent manner during growth of Yersinia pseudotuberculosis and Pseudomonas aeruginosa
    • Yates, E.A. et al. N-acylhomoserine lactones undergo lactonolysis in a pH-, temperature-, and acyl chain length-dependent manner during growth of Yersinia pseudotuberculosis and Pseudomonas aeruginosa. Infect. Immun. 70, 5635-5646 (2002).
    • (2002) Infect. Immun , vol.70 , pp. 5635-5646
    • Yates, E.A.1
  • 40
    • 33750961249 scopus 로고    scopus 로고
    • A structurally unrelated mimic of a Pseudomonas aeruginosa acyl-homoserine lactone quorum-sensing signal
    • Muh, U. et al. A structurally unrelated mimic of a Pseudomonas aeruginosa acyl-homoserine lactone quorum-sensing signal. Proc. Natl. Acad. Sci. USA 103, 16948-16952 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16948-16952
    • Muh, U.1
  • 41
    • 0037155217 scopus 로고    scopus 로고
    • Reversible and specific extracellular antagonism of receptor-histidine kinase signaling
    • Lyon, G.J., Wright, J.S., Christopoulos, A., Novick, R.P. & Muir, T.W. Reversible and specific extracellular antagonism of receptor-histidine kinase signaling. J. Biol. Chem. 277, 6247-6253 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 6247-6253
    • Lyon, G.J.1    Wright, J.S.2    Christopoulos, A.3    Novick, R.P.4    Muir, T.W.5
  • 42
    • 0033574039 scopus 로고    scopus 로고
    • Structure-activity analysis of synthetic autoinducing thiolactone peptides from Staphylococcus aureus responsible for virulence
    • Mayville, P. et al. Structure-activity analysis of synthetic autoinducing thiolactone peptides from Staphylococcus aureus responsible for virulence. Proc. Natl. Acad. Sci. USA 96, 1218-1223 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1218-1223
    • Mayville, P.1
  • 43
    • 13444309093 scopus 로고    scopus 로고
    • Transient interference with staphylococcal quorum sensing blocks abscess formation
    • Wright, J.S. III, Jin, R. & Novick, R.P. Transient interference with staphylococcal quorum sensing blocks abscess formation. Proc. Natl. Acad. Sci. USA 102, 1691-1696 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1691-1696
    • Wright III, J.S.1    Jin, R.2    Novick, R.P.3
  • 44
    • 27344443267 scopus 로고    scopus 로고
    • Small-molecule inhibitor of Vibrio cholerae virulence and intestinal colonization
    • Hung, D.T., Shakhnovich, E.A., Pierson, E. & Mekalanos, J.J. Small-molecule inhibitor of Vibrio cholerae virulence and intestinal colonization. Science 310, 670-674 (2005).
    • (2005) Science , vol.310 , pp. 670-674
    • Hung, D.T.1    Shakhnovich, E.A.2    Pierson, E.3    Mekalanos, J.J.4
  • 45
    • 25844524137 scopus 로고    scopus 로고
    • Transcriptional inhibitor of virulence factors in enteropathogenic Escherichia coli
    • Gauthier, A. et al. Transcriptional inhibitor of virulence factors in enteropathogenic Escherichia coli. Antimicrob. Agents Chemother. 49, 4101-4109 (2005).
    • (2005) Antimicrob. Agents Chemother , vol.49 , pp. 4101-4109
    • Gauthier, A.1
  • 46
    • 0033794322 scopus 로고    scopus 로고
    • Chaperone-assisted pilus assembly and bacterial attachment
    • Sauer, F.G. et al. Chaperone-assisted pilus assembly and bacterial attachment. Curr. Opin. Struct. Biol. 10, 548-556 (2000).
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 548-556
    • Sauer, F.G.1
  • 47
    • 0035804157 scopus 로고    scopus 로고
    • Design and evaluation of pilicides: Potential novel antibacterial agents directed against uropathogenic Escherichia coli
    • Svensson, A. et al. Design and evaluation of pilicides: potential novel antibacterial agents directed against uropathogenic Escherichia coli. ChemBioChem 2, 915-918 (2001).
    • (2001) ChemBioChem , vol.2 , pp. 915-918
    • Svensson, A.1
  • 48
    • 33845228423 scopus 로고    scopus 로고
    • Rationally designed small compounds inhibit pilus biogenesis in uropathogenic bacteria
    • Pinkner, J.S. et al. Rationally designed small compounds inhibit pilus biogenesis in uropathogenic bacteria. Proc. Natl. Acad. Sci. USA 103, 17897-17902 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 17897-17902
    • Pinkner, J.S.1
  • 49
    • 0141646503 scopus 로고    scopus 로고
    • Targeting virulence for antimicrobial chemotherapy
    • Lee, Y.M., Almqvist, F. & Hultgren, S.J. Targeting virulence for antimicrobial chemotherapy. Curr. Opin. Pharmacol. 3, 513-519 (2003).
    • (2003) Curr. Opin. Pharmacol , vol.3 , pp. 513-519
    • Lee, Y.M.1    Almqvist, F.2    Hultgren, S.J.3
  • 50
    • 0242268400 scopus 로고    scopus 로고
    • Genetic requirements for mycobacterial survival during infection
    • Sassetti, C.M. & Rubin, E.J. Genetic requirements for mycobacterial survival during infection. Proc. Natl. Acad. Sci. USA 100, 12989-12994 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12989-12994
    • Sassetti, C.M.1    Rubin, E.J.2
  • 51
    • 0142167588 scopus 로고    scopus 로고
    • Zebrafish-based small molecule discovery
    • MacRae, C.A. & Peterson, R.T. Zebrafish-based small molecule discovery. Chem. Biol. 10, 901-908 (2003).
    • (2003) Chem. Biol , vol.10 , pp. 901-908
    • MacRae, C.A.1    Peterson, R.T.2
  • 52
    • 2342454415 scopus 로고    scopus 로고
    • Chemical suppression of a genetic mutation in a zebrafish model of aortic coarctation
    • Peterson, R.T. et al. Chemical suppression of a genetic mutation in a zebrafish model of aortic coarctation. Nat. Biotechnol. 22, 595-599 (2004).
    • (2004) Nat. Biotechnol , vol.22 , pp. 595-599
    • Peterson, R.T.1
  • 53
    • 33644788489 scopus 로고    scopus 로고
    • Small molecules that delay S phase suppress a zebrafish bmyb mutant
    • Stern, H.M. et al. Small molecules that delay S phase suppress a zebrafish bmyb mutant. Nat. Chem. Biol. 1, 366-370 (2005).
    • (2005) Nat. Chem. Biol , vol.1 , pp. 366-370
    • Stern, H.M.1
  • 54
    • 18744363879 scopus 로고    scopus 로고
    • Real-time visualization of Mycobacterium-macrophage interactions leading to initiation of granuloma formation in zebrafish embryos
    • Davis, J.M. et al. Real-time visualization of Mycobacterium-macrophage interactions leading to initiation of granuloma formation in zebrafish embryos. Immunity 17, 693-702 (2002).
    • (2002) Immunity , vol.17 , pp. 693-702
    • Davis, J.M.1
  • 55
    • 0036081383 scopus 로고    scopus 로고
    • Streptococcus-zebrafish model of bacterial pathogenesis
    • Neely, M.N., Pfeifer, J.D. & Caparon, M. Streptococcus-zebrafish model of bacterial pathogenesis. Infect. Immun. 70, 3904-3914 (2002).
    • (2002) Infect. Immun , vol.70 , pp. 3904-3914
    • Neely, M.N.1    Pfeifer, J.D.2    Caparon, M.3
  • 56
    • 0042829260 scopus 로고    scopus 로고
    • Zebrafish embryos as a model host for the real time analysis of Salmonella typhimurium infections
    • van der Sar, A.M. et al. Zebrafish embryos as a model host for the real time analysis of Salmonella typhimurium infections. Cell. Microbiol. 5, 601-611 (2003).
    • (2003) Cell. Microbiol , vol.5 , pp. 601-611
    • van der Sar, A.M.1
  • 58
    • 33745912507 scopus 로고    scopus 로고
    • Identification of novel antimicrobials using a live-animal infection model
    • Moy, T.I. et al. Identification of novel antimicrobials using a live-animal infection model. Proc. Natl. Acad. Sci. USA 103, 10414-10419 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10414-10419
    • Moy, T.I.1
  • 59
    • 33845903833 scopus 로고    scopus 로고
    • Drugs for bad bugs: Confronting the challenges of antibacterial discovery
    • Payne, D.J., Gwynn, M.N., Holmes, D.J. & Pompliano, D.L. Drugs for bad bugs: confronting the challenges of antibacterial discovery. Nat. Rev. Drug Discov. 6, 29-40 (2007).
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 29-40
    • Payne, D.J.1    Gwynn, M.N.2    Holmes, D.J.3    Pompliano, D.L.4
  • 60
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski, C.A., Lombardo, F., Dominy, B.W. & Feeney, P.J. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. 46, 3-26 (2001).
    • (2001) Adv. Drug Deliv. Rev , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 61
    • 0034678033 scopus 로고    scopus 로고
    • Target-oriented and diversity-oriented organic synthesis in drug discovery
    • Schreiber, S.L. Target-oriented and diversity-oriented organic synthesis in drug discovery. Science 287, 1964-1969 (2000).
    • (2000) Science , vol.287 , pp. 1964-1969
    • Schreiber, S.L.1
  • 62
    • 0346881395 scopus 로고    scopus 로고
    • Protection against anthrax toxemia by hexa-D-arginine in vitro and in vivo
    • Sarac, M.S., Peinado, J.R., Leppla, S.H. & Lindberg, I. Protection against anthrax toxemia by hexa-D-arginine in vitro and in vivo. Infect. Immun. 72, 602-605 (2004).
    • (2004) Infect. Immun , vol.72 , pp. 602-605
    • Sarac, M.S.1    Peinado, J.R.2    Leppla, S.H.3    Lindberg, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.