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Volumn 22, Issue 3, 1997, Pages 271-284

Current approaches to overcome bacterial resistance

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; BOXAZOMYCIN; EPEREZOLID; GE 2270A; GE 37468A; LANTABIOTIC; LINEZOLID; LIPOSIDOMYCIN; MERSACIDIN; MUREIDOMYCIN A; PRISTINAMYCIN; PSEUDOMONIC ACID; RAMOPLANIN; TUNICAMYCIN; UNCLASSIFIED DRUG;

EID: 0030923633     PISSN: 03778282     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (31)

References (162)
  • 1
    • 0026760182 scopus 로고
    • The crisis of antibiotic resistance
    • Neu, H.C. The crisis of antibiotic resistance. Science 1992, 257: 1064-72.
    • (1992) Science , vol.257 , pp. 1064-1072
    • Neu, H.C.1
  • 2
    • 0026705492 scopus 로고
    • Epidemiology of drug resistance: Implications for a post-antimicrobial era
    • Cohen, M.L. Epidemiology of drug resistance: Implications for a post-antimicrobial era. Science 1992, 257: 1050-5.
    • (1992) Science , vol.257 , pp. 1050-1055
    • Cohen, M.L.1
  • 3
    • 0028951636 scopus 로고
    • The world-wide prevalence of methicillin-resistant S. aureus
    • Voss, A., Doebbeling, B. The world-wide prevalence of methicillin-resistant S. aureus. Int J Antimicrob Agents 1995, 5: 101-6.
    • (1995) Int J Antimicrob Agents , vol.5 , pp. 101-106
    • Voss, A.1    Doebbeling, B.2
  • 4
    • 0029025750 scopus 로고
    • Trends in antimicrobial resistant Streptococcus pneumoniae in Japan
    • Yoshida, R., Kaku, M., Kohno, S. et al. Trends in antimicrobial resistant Streptococcus pneumoniae in Japan. Antimicrob Agents Chemother 1995, 39: 1196-8.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 1196-1198
    • Yoshida, R.1    Kaku, M.2    Kohno, S.3
  • 5
    • 0027118906 scopus 로고
    • Back to frightening future
    • (a) Bloom, B. Back to frightening future. Nature 1992, 358: 538-9.
    • (1992) Nature , vol.358 , pp. 538-539
    • Bloom, B.1
  • 6
    • 0026559854 scopus 로고
    • Drug-resistant TB may bring epidemic
    • (b) Culliton, B. Drug-resistant TB may bring epidemic. Nature 1992, 356: 473.
    • (1992) Nature , vol.356 , pp. 473
    • Culliton, B.1
  • 7
    • 0023808730 scopus 로고
    • Plasmid mediated resistance to vancomycin-teicoplanin in Enterococcus faecium
    • (a) Leclerq, R., Derlot, E., Duval, J., Courvalin, P. Plasmid mediated resistance to vancomycin-teicoplanin in Enterococcus faecium. New Engl J Med 1988, 319: 157-61.
    • (1988) New Engl J Med , vol.319 , pp. 157-161
    • Leclerq, R.1    Derlot, E.2    Duval, J.3    Courvalin, P.4
  • 9
    • 0023933144 scopus 로고
    • Guidelines for improving the use of antimicrobial agents in hospitals: A statement by the Infectious Disease Society of America
    • Marr, J.J., Moffet, H.L., Kunin, C.M. Guidelines for improving the use of antimicrobial agents in hospitals: A statement by the Infectious Disease Society of America. J Infect Dis 1988, 157: 869-76.
    • (1988) J Infect Dis , vol.157 , pp. 869-876
    • Marr, J.J.1    Moffet, H.L.2    Kunin, C.M.3
  • 10
    • 0030031423 scopus 로고    scopus 로고
    • Strategies to prevent and control the emergence and spread of antimicrobial-resistant microorganisms in hospitals
    • Goldman, D.A., Weinstein, R.A., Wenzel, R.P. et al. Strategies to prevent and control the emergence and spread of antimicrobial-resistant microorganisms in hospitals. JAMA 1996, 275: 234-40.
    • (1996) JAMA , vol.275 , pp. 234-240
    • Goldman, D.A.1    Weinstein, R.A.2    Wenzel, R.P.3
  • 11
    • 0030067151 scopus 로고    scopus 로고
    • New approaches to the control of infections caused by antibiotic-resistant bacteria
    • Chopra, I., Hodgson, J., Metcalf, B., Poste, G. New approaches to the control of infections caused by antibiotic-resistant bacteria. JAMA 1996, 275: 401-3.
    • (1996) JAMA , vol.275 , pp. 401-403
    • Chopra, I.1    Hodgson, J.2    Metcalf, B.3    Poste, G.4
  • 12
    • 0037505244 scopus 로고
    • Strategies in discovering drugs from natural sources
    • Souza, N.J., Ganguli, B.N., Reden, J. Strategies in discovering drugs from natural sources. Annu Rep Med Chem 1982, 17: 301-10.
    • (1982) Annu Rep Med Chem , vol.17 , pp. 301-310
    • Souza, N.J.1    Ganguli, B.N.2    Reden, J.3
  • 13
    • 0025156911 scopus 로고
    • Discovery and development of new antimicrobial agents
    • Gootz, T.D. Discovery and development of new antimicrobial agents. Clin Microbiol Rev 1990, 3: 13-31.
    • (1990) Clin Microbiol Rev , vol.3 , pp. 13-31
    • Gootz, T.D.1
  • 14
    • 0024577485 scopus 로고
    • Drug discovery and development through the genetic engineering of antibiotic-producing microorganisms
    • Hutchinson, C.R., Borell, C.W., Otten, S.L., Stutzman-Engwall, K.J., Wang, Y. Drug discovery and development through the genetic engineering of antibiotic-producing microorganisms. J Med Chem 1989, 32: 929-37.
    • (1989) J Med Chem , vol.32 , pp. 929-937
    • Hutchinson, C.R.1    Borell, C.W.2    Otten, S.L.3    Stutzman-Engwall, K.J.4    Wang, Y.5
  • 15
    • 0346080764 scopus 로고
    • Biosynthesis of penicillins. IV. New crystalline biosynthetic penicillins
    • Behrens, O.K., Corse, J., Edwards, J.P. et al. Biosynthesis of penicillins. IV. New crystalline biosynthetic penicillins. J Biol Chem 1948, 175: 793.
    • (1948) J Biol Chem , vol.175 , pp. 793
    • Behrens, O.K.1    Corse, J.2    Edwards, J.P.3
  • 16
    • 0023690604 scopus 로고
    • Prospect for the discovery of new (hybrid) antibiotics by genetic engineering of antibiotic-producing bacteria
    • Hutchinson, C.R. Prospect for the discovery of new (hybrid) antibiotics by genetic engineering of antibiotic-producing bacteria. Med Res Rev 1988, 8: 557-67.
    • (1988) Med Res Rev , vol.8 , pp. 557-567
    • Hutchinson, C.R.1
  • 19
    • 0029867221 scopus 로고    scopus 로고
    • Synthetic combinatorial libraries: Novel discovery strategy for identification of antimicrobial agents
    • and references therein
    • (a) Blondelle, S.E., Pérez-Payá, E., Houghten, R.A. Synthetic combinatorial libraries: Novel discovery strategy for identification of antimicrobial agents. Antimicrob Agents Chemother 1996, 40: 1067-71, and references therein.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1067-1071
    • Blondelle, S.E.1    Pérez-Payá, E.2    Houghten, R.A.3
  • 20
    • 2842605870 scopus 로고    scopus 로고
    • Discovery of sequence-selective peptide binding by synthetic receptors using encoded combinatorial libraries
    • and references therein
    • (b) Still, W.C. Discovery of sequence-selective peptide binding by synthetic receptors using encoded combinatorial libraries. Acc Chem Res 1996, 29: 155-63, and references therein.
    • (1996) Acc Chem Res , vol.29 , pp. 155-163
    • Still, W.C.1
  • 21
    • 0029815534 scopus 로고    scopus 로고
    • Combination antimicrobial therapy for bacterial infections, guidelines for the clinician
    • Rybak, M.J., McGrath, B.J. Combination antimicrobial therapy for bacterial infections, guidelines for the clinician. Drugs 1996, 52 (3): 390-405.
    • (1996) Drugs , vol.52 , Issue.3 , pp. 390-405
    • Rybak, M.J.1    McGrath, B.J.2
  • 22
    • 0027445867 scopus 로고
    • Cytokines as antimicrobial therapy for the T cell-deficient patient: Prospect for treatment of nonviral opportunistic infections
    • and references therein
    • (a) Murray, H.W. Cytokines as antimicrobial therapy for the T cell-deficient patient: Prospect for treatment of nonviral opportunistic infections. Clin Infect Dis 1993, 17 (Suppl. 2): s407-13, and references therein.
    • (1993) Clin Infect Dis , vol.17 , Issue.2 SUPPL.
    • Murray, H.W.1
  • 23
    • 0025689946 scopus 로고
    • Gamma interferon, cytokine-induced macrophage activation and antimicrobial host defense: In vitro, in animal models, and in humans
    • (b) Murray, H.W. Gamma interferon, cytokine-induced macrophage activation and antimicrobial host defense: In vitro, in animal models, and in humans. Diagn Microbiol Infect Dis 1990, 13: 411-21.
    • (1990) Diagn Microbiol Infect Dis , vol.13 , pp. 411-421
    • Murray, H.W.1
  • 24
    • 0027986554 scopus 로고
    • Randomized phase I/II trial of a macrophage-specific-immunomodulator (PGG-glucan) in high-risk surgical patients
    • and references therein
    • (c) Babineau, T.J., Marcello, P., Forse, R.A. Randomized phase I/II trial of a macrophage-specific-immunomodulator (PGG-glucan) in high-risk surgical patients. Ann Surg 1994, 220: 601-9, and references therein.
    • (1994) Ann Surg , vol.220 , pp. 601-609
    • Babineau, T.J.1    Marcello, P.2    Forse, R.A.3
  • 25
    • 1842367162 scopus 로고
    • Strategies to overcome bacterial virulence mechanisms: An overview
    • Roth, J.A. (Ed.). ASM Press: Washington, DC
    • a) Corbeil, B.L. Strategies to overcome bacterial virulence mechanisms: An overview. In: Virulence Mechanisms of Bacterial Pathogens. Roth, J.A. (Ed.). ASM Press: Washington, DC 1988, 301-10.
    • (1988) Virulence Mechanisms of Bacterial Pathogens , pp. 301-310
    • Corbeil, B.L.1
  • 26
    • 0029900553 scopus 로고    scopus 로고
    • The value of influenza and pneumococcal vaccines in the elderly
    • (b) Monto, A.S., Terpenning, M.S. The value of influenza and pneumococcal vaccines in the elderly. Drugs Aging 1996, 8: 445-51.
    • (1996) Drugs Aging , vol.8 , pp. 445-451
    • Monto, A.S.1    Terpenning, M.S.2
  • 27
    • 0029897605 scopus 로고    scopus 로고
    • The contribution of the case-control approach to vaccine evaluation: Pneumococcal and Haemophilus influenzae type B PRP vaccines
    • (c) Mills, O.F., Rhoads, G.G. The contribution of the case-control approach to vaccine evaluation: Pneumococcal and Haemophilus influenzae type B PRP vaccines. J Clin Epidemiol 1996, 49: 631-6.
    • (1996) J Clin Epidemiol , vol.49 , pp. 631-636
    • Mills, O.F.1    Rhoads, G.G.2
  • 28
    • 23444440823 scopus 로고
    • Inactivation of antibiotics and the dissemination of resistance genes
    • (a) Davies, J. Inactivation of antibiotics and the dissemination of resistance genes. Science 1994, 264: 375-81.
    • (1994) Science , vol.264 , pp. 375-381
    • Davies, J.1
  • 29
    • 0001916347 scopus 로고
    • Mechanism of antibiotic resistance
    • Mandell, G.L., Douglas, R.G. Jr., Bennett, J.E. (Eds.). Churchill Livingstone: New York
    • (b) Mayer, K.H., Opal, S.M., Madeiros, A.A. Mechanism of antibiotic resistance. In: Principles and Practice of Infectious Diseases, 3rd Ed. Mandell, G.L., Douglas, R.G. Jr., Bennett, J.E. (Eds.). Churchill Livingstone: New York 1990, 218-26.
    • (1990) Principles and Practice of Infectious Diseases, 3rd Ed. , pp. 218-226
    • Mayer, K.H.1    Opal, S.M.2    Madeiros, A.A.3
  • 30
    • 0242711908 scopus 로고
    • Aminoglycoside antibiotic-inactivating enzymes in actinomycetes similar to those present in clinical isolates of antibiotic-resistant bacteria
    • (a) Benveniste, R., Davies, J. Aminoglycoside antibiotic-inactivating enzymes in actinomycetes similar to those present in clinical isolates of antibiotic-resistant bacteria. Proc Natl Acad Sci USA 1973, 70: 2276-80.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 2276-2280
    • Benveniste, R.1    Davies, J.2
  • 31
    • 0017794318 scopus 로고
    • Plasmidresistance to antimicrobial agents
    • (b) Davies, J., Smith, D.I. Plasmidresistance to antimicrobial agents. Ann Rev Microbiol 1978, 32: 469-518.
    • (1978) Ann Rev Microbiol , vol.32 , pp. 469-518
    • Davies, J.1    Smith, D.I.2
  • 32
    • 0028420272 scopus 로고
    • Resistance to antibiotic mediated by target alterations
    • Spratt, B. Resistance to antibiotic mediated by target alterations. Science 1994, 264: 388-93.
    • (1994) Science , vol.264 , pp. 388-393
    • Spratt, B.1
  • 33
    • 0001930562 scopus 로고
    • Mode of action: Interaction with the penicillin binding proteins
    • Page, M.I. (Ed.). Blackie Academic and Professional: New York
    • Frère, J.M., Nguyen-Distèche, M., Coyette, J., Joris, B. Mode of action: Interaction with the penicillin binding proteins. In: The Chemistry of β-Lactams. Page, M.I. (Ed.). Blackie Academic and Professional: New York 1992, 148-97.
    • (1992) The Chemistry of β-Lactams , pp. 148-197
    • Frère, J.M.1    Nguyen-Distèche, M.2    Coyette, J.3    Joris, B.4
  • 34
    • 0001817705 scopus 로고
    • Beta-lactamases: Mechanism of action
    • Page, M.I. (Ed.). Blackie Academic and Professional: New York
    • (a) Waley, S.G. Beta-lactamases: Mechanism of action. In: The Chemistry of β-lactams. Page, M.I. (Ed.). Blackie Academic and Professional: New York 1992, 198-228.
    • (1992) The Chemistry of β-lactams , pp. 198-228
    • Waley, S.G.1
  • 35
    • 0028313131 scopus 로고
    • β-Lactamases: Targets for drug design
    • Ellis, G.P., Luscombe, D.K. (Eds.). Elsevier Science Amsterdam
    • (b) Coulton, S.,. François, I. β-Lactamases: Targets for drug design. In: Progressin Medicinal Chemistry. Ellis, G.P., Luscombe, D.K. (Eds.). Elsevier Science Amsterdam 1994, 31: 297-349.
    • (1994) Progressin Medicinal Chemistry , vol.31 , pp. 297-349
    • Coulton, S.1    François, I.2
  • 36
    • 0017074284 scopus 로고
    • Naturally-occurring β-lactamase inhibitor with antibacterial activity
    • Brown, A.G., Butterworth, D., Cole, M. et al. Naturally-occurring β-lactamase inhibitor with antibacterial activity. J Antibiot 1976, 29: 668-9
    • (1976) J Antibiot , vol.29 , pp. 668-669
    • Brown, A.G.1    Butterworth, D.2    Cole, M.3
  • 37
    • 0017727925 scopus 로고
    • Clavulanic acid: Aβ-lactamase-inhibiting β-lactam from Streptomyces clavuligerus
    • Reading, C., Cole, M. Clavulanic acid: Aβ-lactamase-inhibiting β-lactam from Streptomyces clavuligerus. Antimicrob Agents Chemother 1977, 11: 852-7.
    • (1977) Antimicrob Agents Chemother , vol.11 , pp. 852-857
    • Reading, C.1    Cole, M.2
  • 38
    • 0018143694 scopus 로고
    • CP-45,899, a β-lactamase inhibitor that extends the antibacterial spectrum of β-lactams: Initial bacteriological characterization
    • English, A.R., Retsema, J.A., Girard, A.E., Lynch, J.E., Barth, W.E. CP-45,899, a β-lactamase inhibitor that extends the antibacterial spectrum of β-lactams: Initial bacteriological characterization. Antimicrob Agents Chemother 1978, 14: 414-9.
    • (1978) Antimicrob Agents Chemother , vol.14 , pp. 414-419
    • English, A.R.1    Retsema, J.A.2    Girard, A.E.3    Lynch, J.E.4    Barth, W.E.5
  • 39
    • 0023278943 scopus 로고
    • Synthesis and β-lactamase inhibitory properties of 2β-[(1,2,3-triazol-1-yl)methyl]-2α-methylpenam-3α-carboxilic acid 1,1-dioxide and related triazolyl derivatives
    • (a) Micetich, R.G., Maiti, S.N., Spevak, P. et al. Synthesis and β-lactamase inhibitory properties of 2β-[(1,2,3-triazol-1-yl)methyl]-2α-methylpenam-3α-carboxilic acid 1,1-dioxide and related triazolyl derivatives. J Med Chem 1987, 30: 1469-74.
    • (1987) J Med Chem , vol.30 , pp. 1469-1474
    • Micetich, R.G.1    Maiti, S.N.2    Spevak, P.3
  • 40
    • 0022491880 scopus 로고
    • Comparative activities of the β-lactamase inhibitor YTR 830, clavulanate and sulbactam combined with extended-spectrum penicillins against ticarcillin-resistant Enterobacteriaceae and Pseudomonas
    • (b) Aronoff, S.C., Jacobs, M.R., Johenning, S., Yarrabe, S. Comparative activities of the β-lactamase inhibitor YTR 830, clavulanate and sulbactam combined with extended-spectrum penicillins against ticarcillin-resistant Enterobacteriaceae and Pseudomonas. J Antimicrob Chemother 1986, 18: 177-84.
    • (1986) J Antimicrob Chemother , vol.18 , pp. 177-184
    • Aronoff, S.C.1    Jacobs, M.R.2    Johenning, S.3    Yarrabe, S.4
  • 41
    • 0000893032 scopus 로고
    • The tetracyclines
    • Hlavaka, J.J., Boothe, J.H. (Eds.). Springer-Verlag: Berlin
    • (a) Chopra, I. The tetracyclines. In: Handbook of Experimental Pharmacology. Hlavaka, J.J., Boothe, J.H. (Eds.). Springer-Verlag: Berlin 1985, 317-91.
    • (1985) Handbook of Experimental Pharmacology , pp. 317-391
    • Chopra, I.1
  • 42
    • 0030163126 scopus 로고    scopus 로고
    • Tetracyclines: Antibiotic action, uptake and resistance mechanisms
    • (b) Schnappinger, D., Hillen, W. Tetracyclines: Antibiotic action, uptake and resistance mechanisms. Arch Microbiol 1996, 165: 359-69.
    • (1996) Arch Microbiol , vol.165 , pp. 359-369
    • Schnappinger, D.1    Hillen, W.2
  • 43
    • 0027958117 scopus 로고
    • Glycylcyclines. 1. a new generation of potent antibacterial agents through modification of 9-aminotetracyclines
    • (a) Sum, P.-E, Lee, V.J., Testa, R.T. et al. Glycylcyclines. 1. A new generation of potent antibacterial agents through modification of 9-aminotetracyclines. J Med Chem 1994, 37: 184-8.
    • (1994) J Med Chem , vol.37 , pp. 184-188
    • Sum, P.-E.1    Lee, V.J.2    Testa, R.T.3
  • 45
    • 0027358590 scopus 로고
    • In vitro and in vivo antibacterial activity of glycylcyclines, a new class of semisynthetic tetracyclines
    • Testa, R.T., Petersen, P.J. et al. In vitro and in vivo antibacterial activity of glycylcyclines, a new class of semisynthetic tetracyclines. Antimicrob Agents Chemother 1993, 37: 2270-7.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 2270-2277
    • Testa, R.T.1    Petersen, P.J.2
  • 46
    • 0027400746 scopus 로고
    • Inhibition of the tetracycline efflux antiport protein by 13-thio-substituted 5-hydroxy-6-deoxy tetracyclines
    • Nelson, M.L., Park, B.H., Andrews, J.S., Georgian, V.A., Thomas, R.C., Levy, S.B. Inhibition of the tetracycline efflux antiport protein by 13-thio-substituted 5-hydroxy-6-deoxy tetracyclines. J Med Chem 1993, 36: 370-7.
    • (1993) J Med Chem , vol.36 , pp. 370-377
    • Nelson, M.L.1    Park, B.H.2    Andrews, J.S.3    Georgian, V.A.4    Thomas, R.C.5    Levy, S.B.6
  • 47
    • 0018117795 scopus 로고
    • Biological activity of SCH 21420, the 1-N-α-hydroxy-13-aminopropionyl derivative of gentamicin
    • Miller, G.H., Chiu, P.J.S., Waitz, J.A. Biological activity of SCH 21420, the 1-N-α-hydroxy-13-aminopropionyl derivative of gentamicin. J Antibiot 1978, 31: 688-96.
    • (1978) J Antibiot , vol.31 , pp. 688-696
    • Miller, G.H.1    Chiu, P.J.S.2    Waitz, J.A.3
  • 48
    • 0028832552 scopus 로고
    • Isepamicin(SCH21420, 1-N-HAPA gentamicin B): Microbiological characteristics including antimicrobial potency and spectrum of activity
    • Jones, R.N. Isepamicin(SCH21420, 1-N-HAPA gentamicin B): Microbiological characteristics including antimicrobial potency and spectrum of activity. J Chemother 1995, 7 (Suppl. 2): 7-16.
    • (1995) J Chemother , vol.7 , Issue.2 SUPPL. , pp. 7-16
    • Jones, R.N.1
  • 49
    • 0025906723 scopus 로고
    • Mechanism of bacterial resistance to antibiotics
    • and references therein
    • Dever, L.A., Dermody, T.S. Mechanism of bacterial resistance to antibiotics. Arch Intern Med 1991, 151: 886-95, and references therein.
    • (1991) Arch Intern Med , vol.151 , pp. 886-895
    • Dever, L.A.1    Dermody, T.S.2
  • 50
    • 0027421676 scopus 로고
    • Characterization of Acinetobacter haemolyticus AAC(6′)-lg gene encoding an aminoglycoside 6″-N-acetyltransferase which modifies amikacin
    • Lambert, T., Gerbaud, G., Galimand, M. Courvalin, P. Characterization of Acinetobacter haemolyticus AAC(6′)-lg gene encoding an aminoglycoside 6″-N-acetyltransferase which modifies amikacin. Antimicrob Agents Chemother 1993, 37: 2093-100.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 2093-2100
    • Lambert, T.1    Gerbaud, G.2    Galimand, M.3    Courvalin, P.4
  • 51
    • 0028849715 scopus 로고
    • The changing nature of aminoglycoside resistance mechanisms and the role of isepamicin - A new broad-spectrum aminoglycoside
    • Miller, G.H., Sabatelli, F.J., Naples, L., Hare, R.S., Shaw, K.J. The changing nature of aminoglycoside resistance mechanisms and the role of isepamicin - A new broad-spectrum aminoglycoside. J Chemother 1995, 7 (Suppl. 2): 31-44.
    • (1995) J Chemother , vol.7 , Issue.2 SUPPL. , pp. 31-44
    • Miller, G.H.1    Sabatelli, F.J.2    Naples, L.3    Hare, R.S.4    Shaw, K.J.5
  • 52
    • 0015698884 scopus 로고
    • Synthesis of 1-N-{(S)-4-amino-2-hydroxybutyryl-kanamycin B and -3′,4′-dideoxykanamycin B active against kanamycin-resistant bacteria
    • Kondo, S., Iinuma, K. Yamamoto, H., Maeda, K., Umezawa, H. Synthesis of 1-N-{(S)-4-amino-2-hydroxybutyryl)-kanamycin B and -3′,4′-dideoxykanamycin B active against kanamycin-resistant bacteria. J Antibiot 1973, 26: 412-5.
    • (1973) J Antibiot , vol.26 , pp. 412-415
    • Kondo, S.1    Iinuma, K.2    Yamamoto, H.3    Maeda, K.4    Umezawa, H.5
  • 53
    • 0029889142 scopus 로고    scopus 로고
    • Enzymatic 2′-N-acetylation of arbekacin and antibiotic activity of its product
    • Hotta, K., Zhu, C.B., Ogata, T. et al. Enzymatic 2′-N-acetylation of arbekacin and antibiotic activity of its product. J Antibiot 1996, 49: 458-64.
    • (1996) J Antibiot , vol.49 , pp. 458-464
    • Hotta, K.1    Zhu, C.B.2    Ogata, T.3
  • 54
    • 0021154432 scopus 로고
    • The structure and mode of action of glycopeptide antibiotics of the vancomycin group
    • (a) Barna, J.C.J., Williams, D.H. The structure and mode of action of glycopeptide antibiotics of the vancomycin group. Annu Rev Microbiol 1984, 38: 339-57.
    • (1984) Annu Rev Microbiol , vol.38 , pp. 339-357
    • Barna, J.C.J.1    Williams, D.H.2
  • 55
    • 0024355483 scopus 로고
    • Structure, biochemistry and mechanism of action of glycopeptide antibiotics
    • (b) Reynolds, P.E. Structure, biochemistry and mechanism of action of glycopeptide antibiotics. Eur J Clin Microbiol Infect Dis 1989, 8: 943-50.
    • (1989) Eur J Clin Microbiol Infect Dis , vol.8 , pp. 943-950
    • Reynolds, P.E.1
  • 56
    • 0026658231 scopus 로고
    • The cytoplasmic peptidoglycan precursor of vancomycin-resistant Enterococcus faecalis terminates in lactate
    • (a) Handwerger, S., Pucci, M.J., Volk, K.J., Liu, J., Lee, M.S. The cytoplasmic peptidoglycan precursor of vancomycin-resistant Enterococcus faecalis terminates in lactate. J Bacteriol 1992, 174: 5982-4.
    • (1992) J Bacteriol , vol.174 , pp. 5982-5984
    • Handwerger, S.1    Pucci, M.J.2    Volk, K.J.3    Liu, J.4    Lee, M.S.5
  • 57
    • 0026892270 scopus 로고
    • Modified peptidoglycan precursors produced by glycopeptide-resistant enterococci
    • (b) Messer, J., Reynolds, P.E. Modified peptidoglycan precursors produced by glycopeptide-resistant enterococci. FEMS Microbiol Lett 1992, 94: 195-200.
    • (1992) FEMS Microbiol Lett , vol.94 , pp. 195-200
    • Messer, J.1    Reynolds, P.E.2
  • 58
    • 0029797308 scopus 로고    scopus 로고
    • Inhibition of peptidoglycan biosynthesis in vancomycin-susceptible and -resistant bacteria by a semisynthetic glycopeptide antibiotic
    • Allen, N.E., Hobbs, J.N. Jr., Nicas, T.I. Inhibition of peptidoglycan biosynthesis in vancomycin-susceptible and -resistant bacteria by a semisynthetic glycopeptide antibiotic. Antimicrob Agents Chemother 1996, 40: 2356-62.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 2356-2362
    • Allen, N.E.1    Hobbs Jr., J.N.2    Nicas, T.I.3
  • 59
    • 9544220776 scopus 로고    scopus 로고
    • Semisynthetic glycopeptide antibiotics derived from LY264826 active against vancomycin-resistant enterococci
    • Nicas, T.I., Mullen, D.L., Flokowitsch, J.E. et al. Semisynthetic glycopeptide antibiotics derived from LY264826 active against vancomycin-resistant enterococci. Antimicrob Agents Chemother 1996, 40: 2194-9.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 2194-2199
    • Nicas, T.I.1    Mullen, D.L.2    Flokowitsch, J.E.3
  • 60
    • 0024467106 scopus 로고
    • Outer membrane barrier as a mechanism of antimicrobial resistance
    • (a) Nikaido, H. Outer membrane barrier as a mechanism of antimicrobial resistance. Antimicrob Agents Chemother 1989, 33: 1831-6.
    • (1989) Antimicrob Agents Chemother , vol.33 , pp. 1831-1836
    • Nikaido, H.1
  • 61
    • 0023639252 scopus 로고
    • Penetration of β-lactam through Pseudomonas aeruginosa porin channels
    • (b) Godfrey, A.J., Bryan, L.E. Penetration of β-lactam through Pseudomonas aeruginosa porin channels. Antimicrob Agents Chemother 1987, 31: 1216-21.
    • (1987) Antimicrob Agents Chemother , vol.31 , pp. 1216-1221
    • Godfrey, A.J.1    Bryan, L.E.2
  • 62
    • 0024042262 scopus 로고
    • Roles of porin and β-lactamase in β-lactam resistance of Pseudomonas aeruginosa
    • (c) Hancock, R.E.W., Woodruff, W.A. Roles of porin and β-lactamase in β-lactam resistance of Pseudomonas aeruginosa. Rev Infect Dis 1988, 10: 770-5.
    • (1988) Rev Infect Dis , vol.10 , pp. 770-775
    • Hancock, R.E.W.1    Woodruff, W.A.2
  • 63
    • 23444456920 scopus 로고
    • Prevention of drug access to bacterial targets: Role of permeability barriers and active efflux
    • Nikaido, H. Prevention of drug access to bacterial targets: Role of permeability barriers and active efflux. Science 1994, 264: 382-9.
    • (1994) Science , vol.264 , pp. 382-389
    • Nikaido, H.1
  • 64
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H., Vaara, M. Molecular basis of bacterial outer membrane permeability. Microbiol Rev 1985, 45: 1-32.
    • (1985) Microbiol Rev , vol.45 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 65
    • 0027528537 scopus 로고
    • Activity of the carbapenem panipenem and role of the OprD (D2) protein in its diffusion through the Pseudomonas aeruginosa outer membrane
    • (a) Fukuoka, T., Ohya, S., Narita, T. et al. Activity of the carbapenem panipenem and role of the OprD (D2) protein in its diffusion through the Pseudomonas aeruginosa outer membrane. Antimicrob Agents Chemother 1993, 37: 322-7.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 322-327
    • Fukuoka, T.1    Ohya, S.2    Narita, T.3
  • 66
    • 0028878343 scopus 로고
    • Structure-activity relationship of carbapenems that determine their dependence on porin protein D2 for activity against Pseudomonas aeruginosa
    • (b) Fung-Tomc, J.C., Huczko, E., Banville, J. et al. Structure-activity relationship of carbapenems that determine their dependence on porin protein D2 for activity against Pseudomonas aeruginosa. Antimicrob Agents Chemother 1995, 39: 394-9.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 394-399
    • Fung-Tomc, J.C.1    Huczko, E.2    Banville, J.3
  • 67
    • 0028873156 scopus 로고
    • Activity of carbapenem BMS-181139 against Pseudomonas aeruginosa is not dependent on porin protein D2
    • (c) Fung-Tomc, J.C., Gradelski, E., Kolek, B. et al. Activity of carbapenem BMS-181139 against Pseudomonas aeruginosa is not dependent on porin protein D2. Antimicrob Agents Chemother 1995, 39: 386-93.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 386-393
    • Fung-Tomc, J.C.1    Gradelski, E.2    Kolek, B.3
  • 68
    • 0025186624 scopus 로고
    • Outer membrane protein D2 catalyzes facilitated diffusion of carbapenems and penems through the outer membrane of Pseudomonas aeruginosa
    • (a) Trias, J., Nikaido, H. Outer membrane protein D2 catalyzes facilitated diffusion of carbapenems and penems through the outer membrane of Pseudomonas aeruginosa. Antimicrob Agents Chemother 1990, 34: 52-7.
    • (1990) Antimicrob Agents Chemother , vol.34 , pp. 52-57
    • Trias, J.1    Nikaido, H.2
  • 69
    • 0027490864 scopus 로고
    • The effect of 1β-methyl and imidoyl substituents on the antipseudomonal activity of carbapenems
    • (b) Sumita, Y., Eguchi, Y., Fukasawa, M. et al. The effect of 1β-methyl and imidoyl substituents on the antipseudomonal activity of carbapenems. J Antibiot 1993, 46: 1629-32.
    • (1993) J Antibiot , vol.46 , pp. 1629-1632
    • Sumita, Y.1    Eguchi, Y.2    Fukasawa, M.3
  • 70
    • 10344230917 scopus 로고    scopus 로고
    • Species selectivity of new siderophore-drug conjugates that use specific iron uptake for entry into bacteria
    • (a) Diarra, M.S., Lavoie, M.C., Jacques, M. et al. Species selectivity of new siderophore-drug conjugates that use specific iron uptake for entry into bacteria. Antimicrob Agents Chemother 1996, 40: 2610-7.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 2610-2617
    • Diarra, M.S.1    Lavoie, M.C.2    Jacques, M.3
  • 71
    • 0025872964 scopus 로고
    • 5-hydroxy-L-ornithine-derived siderophore-β-lactam conjugates: Iron transport-mediated drug delivery
    • 5-hydroxy-L-ornithine-derived siderophore-β-lactam conjugates: Iron transport-mediated drug delivery. J Med Chem 1991, 34: 968-78.
    • (1991) J Med Chem , vol.34 , pp. 968-978
    • Dolence, E.K.1    Minnick, A.A.2    Lin, C.3    Miller, M.J.4
  • 72
    • 0001653464 scopus 로고
    • Microbial iron chelators as drug delivery agents: The rational design and synthesis of siderophore-drug conjugates
    • (c) Miller, M.J., Malouin, F. Microbial iron chelators as drug delivery agents: The rational design and synthesis of siderophore-drug conjugates. Acc Chem Res 1993, 26: 241-9.
    • (1993) Acc Chem Res , vol.26 , pp. 241-249
    • Miller, M.J.1    Malouin, F.2
  • 74
    • 0025666854 scopus 로고
    • TonB and the Gram-negative dilemma
    • Postle, K. TonB and the Gram-negative dilemma. Mol Microbiol 1990, 4: 2019-25.
    • (1990) Mol Microbiol , vol.4 , pp. 2019-2025
    • Postle, K.1
  • 75
    • 0026728122 scopus 로고
    • Mode of action and inhibitory activities of new siderophore-β-lactam conjugates that use specific iron uptake pathways for entry into bacteria
    • (a) Brochu, A., Brochu, N., Nicas, T.I. et al. Mode of action and inhibitory activities of new siderophore-β-lactam conjugates that use specific iron uptake pathways for entry into bacteria. Antimicrob Agents Chemother 1992, 36: 2166-75.
    • (1992) Antimicrob Agents Chemother , vol.36 , pp. 2166-2175
    • Brochu, A.1    Brochu, N.2    Nicas, T.I.3
  • 76
    • 0026535375 scopus 로고
    • Iron transport-mediated antibacterial activity of and development of resistance to hydroxamate and catechol siderophore-carbacephalosporin conjugates
    • (b) Minnick, A.A., McKee, J.A., Dolence, K.E., Miller, M.J. Iron transport-mediated antibacterial activity of and development of resistance to hydroxamate and catechol siderophore-carbacephalosporin conjugates. Antimicrob Agents Chemother 1992, 36: 840-50.
    • (1992) Antimicrob Agents Chemother , vol.36 , pp. 840-850
    • Minnick, A.A.1    McKee, J.A.2    Dolence, K.E.3    Miller, M.J.4
  • 77
    • 0025219010 scopus 로고
    • Cir and Fiu proteins in the outer membrane of Escherichia coli catalyze transport of monomeric catechol: Study with β-lactam antibiotic containing catechol and analogous groups
    • (a) Nikaido, H., Rosenberg, E.Y. Cir and Fiu proteins in the outer membrane of Escherichia coli catalyze transport of monomeric catechol: Study with β-lactam antibiotic containing catechol and analogous groups. J Bacteriol 1990, 172: 1361-7.
    • (1990) J Bacteriol , vol.172 , pp. 1361-1367
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 78
    • 0028955845 scopus 로고
    • Mechanism of tonB-dependent transport of KP-736, a 1,5-dihydroxy-4-pyridone-substituted cephalosporin, into Escherichia coli K-12 cells
    • (b) Tatsumi, Y., Maejima, T., Mitsuhashi, S. Mechanism of tonB-dependent transport of KP-736, a 1,5-dihydroxy-4-pyridone-substituted cephalosporin, into Escherichia coli K-12 cells. Antimicrob Agents Chemother 1995, 39: 613-9.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 613-619
    • Tatsumi, Y.1    Maejima, T.2    Mitsuhashi, S.3
  • 79
    • 0025075685 scopus 로고
    • Mode of action of GR69153, a novel catechol-substituted cephalosporin, and its interaction with the tonB-dependent iron transport system
    • (c) Silley, P., Griffiths, J.W., Monsey, D., Harris, A.M. Mode of action of GR69153, a novel catechol-substituted cephalosporin, and its interaction with the tonB-dependent iron transport system. Antimicrob Agents Chemother 1990, 34: 1806-8.
    • (1990) Antimicrob Agents Chemother , vol.34 , pp. 1806-1808
    • Silley, P.1    Griffiths, J.W.2    Monsey, D.3    Harris, A.M.4
  • 80
    • 0027402458 scopus 로고
    • In vitro and in vivo antibacterial activities of E1077, a novel parenteral cephalosporin
    • (d) Toyosawa, T., Miyazaki, S., Tsuji, A., Yamaguchi, K., Goto, S. In vitro and in vivo antibacterial activities of E1077, a novel parenteral cephalosporin. Antimicrob Agents Chemother 1993, 37: 60-6.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 60-66
    • Toyosawa, T.1    Miyazaki, S.2    Tsuji, A.3    Yamaguchi, K.4    Goto, S.5
  • 81
    • 0029949956 scopus 로고    scopus 로고
    • Synthesis and antibacterial activities of novel C(7)-catechol-substituted cephalosporins (II)
    • (e) Kim, Y.-Z., Lim, J.-C, Yeo, J.-H. et al. Synthesis and antibacterial activities of novel C(7)-catechol-substituted cephalosporins (II). J Antibiot 1996, 49: 499-501.
    • (1996) J Antibiot , vol.49 , pp. 499-501
    • Kim, Y.-Z.1    Lim, J.-C.2    Yeo, J.-H.3
  • 82
    • 0028139998 scopus 로고
    • Antibacterial synergism of polymyxin B nonapeptide and hydrophobic antibiotics in experimental Gram-negative infections in mice
    • Ofek, I., Cohen, S., Rahmani, R. et al. Antibacterial synergism of polymyxin B nonapeptide and hydrophobic antibiotics in experimental Gram-negative infections in mice. Antimicrob Agents Chemother 1994, 38: 374-7.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 374-377
    • Ofek, I.1    Cohen, S.2    Rahmani, R.3
  • 83
    • 0027535455 scopus 로고
    • Discovery and development of new antibiotics: The problem of antibiotic resistance
    • Silver, L.L., Bostian, K.A. Discovery and development of new antibiotics: The problem of antibiotic resistance. Antimicrob Agents Chemother 1993, 37: 377-83.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 377-383
    • Silver, L.L.1    Bostian, K.A.2
  • 84
    • 0029837992 scopus 로고    scopus 로고
    • Modern drug design and lead discovery: An overview
    • Setti, E.L., Micetich, R.G. Modern drug design and lead discovery: An overview. Curr Med Chem 1996, 3: 317-24.
    • (1996) Curr Med Chem , vol.3 , pp. 317-324
    • Setti, E.L.1    Micetich, R.G.2
  • 85
    • 0025903443 scopus 로고
    • Activity of mersacidin, a novel peptide, compared with that of vancomycin, teicoplanin, and daptomycin
    • (a) Niu, W.W., Neu, H.C. Activity of mersacidin, a novel peptide, compared with that of vancomycin, teicoplanin, and daptomycin. Antimicrob Agents Chemother 1991, 35: 998-1000.
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 998-1000
    • Niu, W.W.1    Neu, H.C.2
  • 86
    • 0028952641 scopus 로고
    • Mode of action of the antibiotic mersacidin: Inhibition of peptidoglycan biosynthesis via a novel mechanism?
    • (b) Brötz, H., Bierbaum, G., Markus, A. Molitor, E., Sahl, H.G. Mode of action of the antibiotic mersacidin: Inhibition of peptidoglycan biosynthesis via a novel mechanism? Antimicrob Agents Chemother 1995, 39: 714-9.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 714-719
    • Brötz, H.1    Bierbaum, G.2    Markus, A.3    Molitor, E.4    Sahl, H.G.5
  • 87
    • 0026648308 scopus 로고
    • Mersacidin, a new antibiotic from Bacillus, in vitro and in vivo antibacterial activity
    • (c) Chatterjee, S., Chatterjee, D.K., Jani, R.H. et al. Mersacidin, a new antibiotic from Bacillus, in vitro and in vivo antibacterial activity. J Antibiot 1992, 45: 839-45.
    • (1992) J Antibiot , vol.45 , pp. 839-845
    • Chatterjee, S.1    Chatterjee, D.K.2    Jani, R.H.3
  • 89
    • 0025093558 scopus 로고
    • Inhibition of peptidoglycan biosynthesis by ramoplanin
    • (a) Somner, E.A., Reynolds, P.E. Inhibition of peptidoglycan biosynthesis by ramoplanin. Antimicrob Agents Chemother 1990, 34: 413-9.
    • (1990) Antimicrob Agents Chemother , vol.34 , pp. 413-419
    • Somner, E.A.1    Reynolds, P.E.2
  • 90
    • 0024459180 scopus 로고
    • In vitro evaluation of ramoplanin (a 16686 or MDL 62198), a new depsipeptide complex for potential topical use
    • (b) Jones, R.N., Barry, A. In vitro evaluation of ramoplanin (A 16686 or MDL 62198), a new depsipeptide complex for potential topical use. Diagn Microbiol Infect Dis 1989, 12: 279-82.
    • (1989) Diagn Microbiol Infect Dis , vol.12 , pp. 279-282
    • Jones, R.N.1    Barry, A.2
  • 91
    • 0029902635 scopus 로고    scopus 로고
    • Mode of action of tunicamycin, liposidomycin B, and mureidomycin A: Inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli
    • Brandish, P.E., Kimura, K.I., Inukai, M., Southgate, R., Lonsdale, J.T., Bugg, T.D.H. Mode of action of tunicamycin, liposidomycin B, and mureidomycin A: Inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli. Antimicrob Agents Chemother 1996, 40: 1640-4.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1640-1644
    • Brandish, P.E.1    Kimura, K.I.2    Inukai, M.3    Southgate, R.4    Lonsdale, J.T.5    Bugg, T.D.H.6
  • 92
    • 0030004930 scopus 로고    scopus 로고
    • Slow-binding inhibition of phospho-N-acetylmuramyl-pentapeptide translocase (Escherichia coli) by mureidomycin A
    • (a) Brandish, P.E., Burnham, M.K., Lonsdale, J.T. Southgate, R., Inukai, M. Bugg, T.D.H. Slow-binding inhibition of phospho-N-acetylmuramyl-pentapeptide translocase (Escherichia coli) by mureidomycin A. J Biol Chem 1996, 271, 7609-14.
    • (1996) J Biol Chem , vol.271 , pp. 7609-7614
    • Brandish, P.E.1    Burnham, M.K.2    Lonsdale, J.T.3    Southgate, R.4    Inukai, M.5    Bugg, T.D.H.6
  • 93
    • 0026081814 scopus 로고
    • Mureidomycin A, a new inhibitor of bacterial peptidoglycan synthesis
    • (b) Isono, F., Inukai, M. Mureidomycin A, a new inhibitor of bacterial peptidoglycan synthesis. Antimicrob Agents Chemother 1991, 35: 234-6.
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 234-236
    • Isono, F.1    Inukai, M.2
  • 94
    • 0027233035 scopus 로고
    • Selective inhibition of the bacterial translocase reaction in peptidoglycan synthesis by mureidomycins
    • (c) Inukai, M. Isono, F., Takatsuki, A. Selective inhibition of the bacterial translocase reaction in peptidoglycan synthesis by mureidomycins. Antimicrob Agents Chemother 1993, 37: 980-3.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 980-983
    • Inukai, M.1    Isono, F.2    Takatsuki, A.3
  • 95
    • 0023619963 scopus 로고
    • Oxazolidinones, a new class of synthetic antibacterial agents: In vitro and in vivo activities of DuP 105 and DuP 721
    • (a) Slee, A.M., Wuonola, M.A., McRipley, R.J. et al. Oxazolidinones, a new class of synthetic antibacterial agents: In vitro and in vivo activities of DuP 105 and DuP 721. Antimicrob Agents Chemother 1987, 31: 1791-7.
    • (1987) Antimicrob Agents Chemother , vol.31 , pp. 1791-1797
    • Slee, A.M.1    Wuonola, M.A.2    McRipley, R.J.3
  • 96
    • 0023748768 scopus 로고
    • Mechanism of action of DuP 721: Inhibition of an early event in protein synthesis
    • (b) Eustice, D., Feldman, P.A., Zajac, I., Slee, A.M. Mechanism of action of DuP 721: Inhibition of an early event in protein synthesis. Antimicrob Agents Chemother 1988, 32: 1218-22.
    • (1988) Antimicrob Agents Chemother , vol.32 , pp. 1218-1222
    • Eustice, D.1    Feldman, P.A.2    Zajac, I.3    Slee, A.M.4
  • 97
    • 0029922958 scopus 로고    scopus 로고
    • In vitro activities of oxazolidinones U-100592 and U-100766 against penicillin-resistant and cephalosporin-resistant strains of Streptococcus pneumoniae
    • (a) Mason, E.G. Jr., Lamberth, L.B. Kaplan, S.L. In vitro activities of oxazolidinones U-100592 and U-100766 against penicillin-resistant and cephalosporin-resistant strains of Streptococcus pneumoniae. Antimicrob Agents Chemother 1996, 40: 1039-40.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1039-1040
    • Mason Jr., E.G.1    Lamberth, L.B.2    Kaplan, S.L.3
  • 98
    • 0029976183 scopus 로고    scopus 로고
    • In vitro activities of oxazolidinone compounds U100592 and U100766 against Staphylococcus aureus and Staphylococcus epidermis
    • (b) Kaatz, G.W., Seo, S.M. In vitro activities of oxazolidinone compounds U100592 and U100766 against Staphylococcus aureus and Staphylococcus epidermis. Antimicrob Agents Chemother 1996, 40, 799-801.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 799-801
    • Kaatz, G.W.1    Seo, S.M.2
  • 99
    • 0029940428 scopus 로고    scopus 로고
    • In vivo activities of U-100592 and U-100766, novel oxazolidinone antibacterial agents, against experimental bacterial infections
    • (c) Ford, C.W., Hamel, J.C., Wilson, D.M. et al. In vivo activities of U-100592 and U-100766, novel oxazolidinone antibacterial agents, against experimental bacterial infections. Antimicrob Agents Chemother 1996, 40: 1508-13.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1508-1513
    • Ford, C.W.1    Hamel, J.C.2    Wilson, D.M.3
  • 100
    • 0029942573 scopus 로고    scopus 로고
    • In vitro activities of U-100592 and U-100766. novel oxazolidinone antibacterial agents
    • (d) Zurenko, G.E., Yagi, B.H., Schaadt, R.D. et al. In vitro activities of U-100592 and U-100766. novel oxazolidinone antibacterial agents. Antimicrob Agents Chemother 1996, 40: 839-45.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 839-845
    • Zurenko, G.E.1    Yagi, B.H.2    Schaadt, R.D.3
  • 101
    • 1842300288 scopus 로고
    • Lapristinamycin (7293 RP) antibiotique antistaphylococcique. Etude comparative in-vitro, première expérience clinique
    • (a) Janbon, N., Brunei, D., Bertrand, A., Michel-Briand. Lapristinamycin (7293 RP) antibiotique antistaphylococcique. Etude comparative in-vitro, première expérience clinique. Sem Thèr 1962, 38: 25-33.
    • (1962) Sem Thèr , vol.38 , pp. 25-33
    • Janbon, N.1    Brunei, D.2    Bertrand, A.3    Michel-Briand4
  • 102
    • 0029994714 scopus 로고    scopus 로고
    • Mechanism of action of streptogramin and macrolides
    • (b) Vannuffel, P., Cocito, C. Mechanism of action of streptogramin and macrolides. Drugs 1996, 51 (Suppl. 1): 20-30.
    • (1996) Drugs , vol.51 , Issue.1 SUPPL. , pp. 20-30
    • Vannuffel, P.1    Cocito, C.2
  • 103
    • 0026773160 scopus 로고
    • In-vitro activity of RP 59500, a new semisynthetic streptogramin antibiotic, against Gram-positive bacteria
    • Brumfitt, W., Hamilton-Miller, J.M.T., Shah, S. In-vitro activity of RP 59500, a new semisynthetic streptogramin antibiotic, against Gram-positive bacteria. J Antimicrob Chemother 1992, 30 (Suppl. A): 29-37.
    • (1992) J Antimicrob Chemother , vol.30 , Issue.SUPPL. A , pp. 29-37
    • Brumfitt, W.1    Hamilton-Miller, J.M.T.2    Shah, S.3
  • 104
    • 0026659517 scopus 로고
    • The in-vitro activity of RP 59500 against Gram-positive cocci
    • (a) Goto, S., Miyazaki, S., Kaneko, Y. The in-vitro activity of RP 59500 against Gram-positive cocci. J Antimicrob Chemother 1992, 30 (Suppl. A): 25-8.
    • (1992) J Antimicrob Chemother , vol.30 , Issue.SUPPL. A , pp. 25-28
    • Goto, S.1    Miyazaki, S.2    Kaneko, Y.3
  • 105
    • 0026769025 scopus 로고
    • Comparative in-vitro activity of RP 59500
    • (b) Verhaegen, J., Verbist, L. Comparative in-vitro activity of RP 59500. J Antimicrob Chemother 1992, 30 (Suppl. A): 39-44.
    • (1992) J Antimicrob Chemother , vol.30 , Issue.SUPPL. A , pp. 39-44
    • Verhaegen, J.1    Verbist, L.2
  • 106
    • 0026771397 scopus 로고
    • In-vitro antibacterial activity of RP 59500, a semisynthetic streptogramin, against Streptococcus pneumoniae
    • (c) Fremaux, A., Sissia, R., Cohen, R., Geslin, P. In-vitro antibacterial activity of RP 59500, a semisynthetic streptogramin, against Streptococcus pneumoniae. J Antimicrob Chemother 1992, 30 (Suppl. A): 19-23.
    • (1992) J Antimicrob Chemother , vol.30 , Issue.SUPPL. A , pp. 19-23
    • Fremaux, A.1    Sissia, R.2    Cohen, R.3    Geslin, P.4
  • 107
    • 0030004654 scopus 로고    scopus 로고
    • Antibacterial activity of quinupristin/dalfopristin
    • (d) Finch, R.G. Antibacterial activity of quinupristin/dalfopristin. Drugs 1996, 51 (Suppl. 1): 31-7.
    • (1996) Drugs , vol.51 , Issue.1 SUPPL. , pp. 31-37
    • Finch, R.G.1
  • 108
    • 1842295555 scopus 로고    scopus 로고
    • Activity of the oral streptogramin antibiotic RP106972 against Haemophilus influenzae
    • Sept 15-18. New Orleans Abst F229
    • (a) Jorgensen, J.H., McElmeel, M.L., Trippy, C.W. Activity of the oral streptogramin antibiotic RP106972 against Haemophilus influenzae. 36th Intersci Conf Antimicrob Agents Chemother (Sept 15-18. New Orleans) 1996, Abst F229.
    • (1996) 36th Intersci Conf Antimicrob Agents Chemother
    • Jorgensen, J.H.1    McElmeel, M.L.2    Trippy, C.W.3
  • 110
    • 0025779043 scopus 로고
    • Antibiotic GE2270A: A novel inhibitor of bacterial protein synthesis
    • Selva, E., Beretta, G., Montanini, N. et al. Antibiotic GE2270A: A novel inhibitor of bacterial protein synthesis. J Antibiot 1991, 44: 693-701.
    • (1991) J Antibiot , vol.44 , pp. 693-701
    • Selva, E.1    Beretta, G.2    Montanini, N.3
  • 112
    • 0027405295 scopus 로고
    • In vitro activity of MDL 62,879 (GE2270A) against aerobic Gram-positive and anaerobic bacteria
    • (b) King, A., Bethune, L., Phillips, I. In vitro activity of MDL 62,879 (GE2270A) against aerobic Gram-positive and anaerobic bacteria. Antimicrob Agents Chemother 1993, 37: 746-9.
    • (1993) Antimicrob Agents Chemother , vol.37 , pp. 746-749
    • King, A.1    Bethune, L.2    Phillips, I.3
  • 113
    • 0028805475 scopus 로고
    • Antibiotic GE37468A: A novel inhibitor of bacterial protein synthesis. II. Structure elucidation
    • (a) Ferrari, P., Colombo, L. Stella, S., Selva, E., Zerilli, L.F. Antibiotic GE37468A: A novel inhibitor of bacterial protein synthesis. II. Structure elucidation. J Antibiot 1995, 48: 1304-11.
    • (1995) J Antibiot , vol.48 , pp. 1304-1311
    • Ferrari, P.1    Colombo, L.2    Stella, S.3    Selva, E.4    Zerilli, L.F.5
  • 114
    • 0029127329 scopus 로고
    • Antibiotic GE37468A: A new inhibitor of bacterial protein synthesis. I. Isolation and characterization
    • (b) Stella, S., Montanini, N., LeMonnier, F. et al. Antibiotic GE37468A: A new inhibitor of bacterial protein synthesis. I. Isolation and characterization. J Antibiot 1995, 48: 780-6.
    • (1995) J Antibiot , vol.48 , pp. 780-786
    • Stella, S.1    Montanini, N.2    LeMonnier, F.3
  • 115
    • 0019164866 scopus 로고
    • Interaction of pseudomonic acid A with Escherichia coli B isoleucyl-tRNa synthetase
    • Hughes, J., Mellows, G. Interaction of pseudomonic acid A with Escherichia coli B isoleucyl-tRNA synthetase. Biochem J 1978, 191: 209-19.
    • (1978) Biochem J , vol.191 , pp. 209-219
    • Hughes, J.1    Mellows, G.2
  • 116
    • 1842377888 scopus 로고
    • Bactobran
    • Dobson, R.L., Leyden, J.J., Noble, W.C., Price, J.D. (Eds.). Elsevier: Amsterdam
    • Bactobran. Proceedings of an International Symposium. Dobson, R.L., Leyden, J.J., Noble, W.C., Price, J.D. (Eds.). Elsevier: Amsterdam 1985.
    • (1985) Proceedings of An International Symposium
  • 117
    • 0029820014 scopus 로고    scopus 로고
    • The chemistry of pseudomonic acid. 17. Dual-action C-1 oxazole derivatives of pseudomonic acid having an extended spectrum of antibacterial activity
    • (a) Broom, N.J.P., Cassels, R., Cheng, H.Y. et al. The chemistry of pseudomonic acid. 17. Dual-action C-1 oxazole derivatives of pseudomonic acid having an extended spectrum of antibacterial activity. J Med Chem 1996, 39: 3596-600.
    • (1996) J Med Chem , vol.39 , pp. 3596-3600
    • Broom, N.J.P.1    Cassels, R.2    Cheng, H.Y.3
  • 118
    • 0028805477 scopus 로고
    • The chemistry of pseudomonic acid part 14. Synthesis and in vivo biological activity of heterocyclic substituted oxazole derivatives
    • (b) Broom, N.J.P., Elder, J.S., Hannan, P.C.T. et al. The chemistry of pseudomonic acid part 14. Synthesis and in vivo biological activity of heterocyclic substituted oxazole derivatives. J Antibiot 1995, 48: 1336-44.
    • (1995) J Antibiot , vol.48 , pp. 1336-1344
    • Broom, N.J.P.1    Elder, J.S.2    Hannan, P.C.T.3
  • 119
    • 1842365342 scopus 로고
    • Synthesis and antibacterial activity of new boxazomycin derivatives: The structure-activity relationship of the A ring
    • Sept 17-20, San Francisco Abst F21
    • (a) Stier, M.A., Domagala, J.M., Gogliotti, R.D. et al. Synthesis and antibacterial activity of new boxazomycin derivatives: The structure-activity relationship of the A ring. 35th Intersci Conf Antimicrob Agents Chemother (Sept 17-20, San Francisco) 1995, Abst F21.
    • (1995) 35th Intersci Conf Antimicrob Agents Chemother
    • Stier, M.A.1    Domagala, J.M.2    Gogliotti, R.D.3
  • 120
    • 1842337294 scopus 로고
    • Boxazomycin analogues as new antibacterial agents: Synthesis and structure-activity relationship
    • Sept 17-20, San Francisco Abst F22.
    • (b) Song, Y., Domagala, J.M., Turner, W.R. et al. Boxazomycin analogues as new antibacterial agents: Synthesis and structure-activity relationship. 35th Intersci Conf Antimicrob Agents Chemother (Sept 17-20, San Francisco) 1995, Abst F22.
    • (1995) 35th Intersci Conf Antimicrob Agents Chemother
    • Song, Y.1    Domagala, J.M.2    Turner, W.R.3
  • 121
    • 1842287842 scopus 로고
    • Determination of the mechanism of action of boxazomycin B, a Gram-positive specific antibacterial agent
    • Sept 17-20, San Francisco Abst F23
    • (c) Miller, P.F., Johnson, G., Gracheck, S.J. et al. Determination of the mechanism of action of boxazomycin B, a Gram-positive specific antibacterial agent. 35th Intersci Conf Antimicrob Agents Chemother (Sept 17-20, San Francisco) 1995, Abst F23.
    • (1995) 35th Intersci Conf Antimicrob Agents Chemother
    • Miller, P.F.1    Johnson, G.2    Gracheck, S.J.3
  • 122
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptide from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • (a) Zasloff, M. Magainins, a class of antimicrobial peptide from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci USA 1987, 84: 5449-53.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 123
    • 0023854883 scopus 로고
    • Antimicrobial activity of synthetic magainin peptides and several analogues
    • (b) Zasloff, M., Martin, B., Chen, H.-C. Antimicrobial activity of synthetic magainin peptides and several analogues. Proc Natl Acad Sci USA 1988, 85: 910-3.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 910-913
    • Zasloff, M.1    Martin, B.2    Chen, H.-C.3
  • 124
    • 0025160241 scopus 로고
    • Magainin analogs effective against pathogenic protozoa
    • (c) Huang, C.M., Chen, H.C., Zierdt, C.H. Magainin analogs effective against pathogenic protozoa. Antimicrob Agents Chemother 1990, 34: 1824-6.
    • (1990) Antimicrob Agents Chemother , vol.34 , pp. 1824-1826
    • Huang, C.M.1    Chen, H.C.2    Zierdt, C.H.3
  • 125
    • 0025757215 scopus 로고
    • β-Lactam antibiotics potentiate magainin 2 antimicrobial activity in vitro and in vivo
    • Darveau, R.P., Cunningham, M.D., Seachord, C.L. et al. β-Lactam antibiotics potentiate magainin 2 antimicrobial activity in vitro and in vivo. Antimicrob Agents Chemother 1991, 35: 1153-9.
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 1153-1159
    • Darveau, R.P.1    Cunningham, M.D.2    Seachord, C.L.3
  • 126
    • 0018820115 scopus 로고
    • Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • Hultmark, D., Steiner, H., Rasmuson, T., Boman, H.G. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia. Eur J Biochem 1980, 106: 7-16.
    • (1980) Eur J Biochem , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 127
    • 0029916112 scopus 로고    scopus 로고
    • Cationic antimicrobial proteins
    • (a) Larrick, J.W., Wright, S.C. Cationic antimicrobial proteins. Drugs Fut 1996, 21: 41-8.
    • (1996) Drugs Fut , vol.21 , pp. 41-48
    • Larrick, J.W.1    Wright, S.C.2
  • 129
    • 0027474382 scopus 로고
    • Defensins: Antimicrobial and cytotoxic peptide of mammalian cells
    • Lehrer, R.I., Lichtenstein, A.K., Ganz, T. Defensins: Antimicrobial and cytotoxic peptide of mammalian cells. Ann Rev Immunol 1993, 11: 105-28.
    • (1993) Ann Rev Immunol , vol.11 , pp. 105-128
    • Lehrer, R.I.1    Lichtenstein, A.K.2    Ganz, T.3
  • 131
    • 1842407643 scopus 로고    scopus 로고
    • Protegrins protect mice from systemic infection by antibiotic resistant pathogens
    • Sept 15-18, New Orleans Abst F244
    • (b) Kung, A.H.C., Fiddes, J.C., Loury, D.J., Ho, J.F., Cheng, F.-C. Protegrins protect mice from systemic infection by antibiotic resistant pathogens. 36th Intersci Conf Antimicrob Agents (Sept 15-18, New Orleans) 1996, Abst F244.
    • (1996) 36th Intersci Conf Antimicrob Agents
    • Kung, A.H.C.1    Fiddes, J.C.2    Loury, D.J.3    Ho, J.F.4    Cheng, F.-C.5
  • 133
    • 0007943587 scopus 로고    scopus 로고
    • Antimicrobial peptides: Broadspectrum antibiotics from nature
    • (a) Hancock, R.E.W., Falla, T.J. Antimicrobial peptides: Broadspectrum antibiotics from nature. Clin Microbiol Infect 1996, 1: 226-9.
    • (1996) Clin Microbiol Infect , vol.1 , pp. 226-229
    • Hancock, R.E.W.1    Falla, T.J.2
  • 134
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • (b) Christensen, B., Fink, J., Merrifield, R.B., Mauzerall, D. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc Natl Acad Sci USA 1988, 85: 5072-6.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 136
    • 0343304554 scopus 로고
    • SCH 27899 (EVE), an everninomicin active against multiply-resistant (R) enterococci and staphylococci
    • Oct 17-20, New Orleans Abst 460
    • (b) Shlaes, D.M., Shlaes, J.H., Etter, L., Hare, R.S., Miller, G.H. SCH 27899 (EVE), an everninomicin active against multiply-resistant (R) enterococci and staphylococci. 33rd Intersci Conf Antimicrob Agents Chemother (Oct 17-20, New Orleans) 1993, Abst 460.
    • (1993) 33rd Intersci Conf Antimicrob Agents Chemother
    • Shlaes, D.M.1    Shlaes, J.H.2    Etter, L.3    Hare, R.S.4    Miller, G.H.5
  • 137
    • 0029871090 scopus 로고    scopus 로고
    • Antibacterial activity of hydroxychalcone against methicillin-resistant Staphylococcus aureus
    • Sato, M., Tsuchiya, H., Miyazaki, T. et al. Antibacterial activity of hydroxychalcone against methicillin-resistant Staphylococcus aureus. Int J Antimicrob Agents 1996, 6: 227-31.
    • (1996) Int J Antimicrob Agents , vol.6 , pp. 227-231
    • Sato, M.1    Tsuchiya, H.2    Miyazaki, T.3
  • 138
    • 0027962689 scopus 로고
    • Flavanones with potent antibacterial activity against methicillin-resistant Staphylococcus aureus
    • Iinuma, M., Tsuchiya, H., Sato, M. et al. Flavanones with potent antibacterial activity against methicillin-resistant Staphylococcus aureus. J Pharm Pharmacol 1994, 46: 892-5.
    • (1994) J Pharm Pharmacol , vol.46 , pp. 892-895
    • Iinuma, M.1    Tsuchiya, H.2    Sato, M.3
  • 139
    • 0030474049 scopus 로고    scopus 로고
    • What can we learn from molecular recognition in protein-ligand complexes for the design of new drugs?
    • and references therein
    • For a recent review about structure-based drug design see Böhm, H.-J., Klebe, G. What can we learn from molecular recognition in protein-ligand complexes for the design of new drugs? Angew Chem Int Ed Engl 1996, 35: 2588-614, and references therein.
    • (1996) Angew Chem Int Ed Engl , vol.35 , pp. 2588-2614
    • Böhm, H.-J.1    Klebe, G.2
  • 140
    • 0028006393 scopus 로고
    • (6S)-6-Fluoroshikimic acid, an antibacterial agent acting on the aromatic biosynthetic pathway
    • (a) Davies, G.M., Barrett-Bee, K.J., Jude, D.A. et al. (6S)-6-Fluoroshikimic acid, an antibacterial agent acting on the aromatic biosynthetic pathway. Antimicrob Agents Chemother 1994, 38: 403-6.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 403-406
    • Davies, G.M.1    Barrett-Bee, K.J.2    Jude, D.A.3
  • 142
    • 3743149783 scopus 로고    scopus 로고
    • Synthesis and activity of a new class of antibacterial agents which target isoleucyl t-RNA synthetase
    • Sept 15-18, New Orleans Abst F235
    • Hill, J.M., Yu, G., Shue, Y.-K., McCarthy, P., Wendler, P.A., Li, T. Synthesis and activity of a new class of antibacterial agents which target isoleucyl t-RNA synthetase. 36th Intersci Conf Antimicrob Agents Chemother (Sept 15-18, New Orleans) 1996, Abst F235.
    • (1996) 36th Intersci Conf Antimicrob Agents Chemother
    • Hill, J.M.1    Yu, G.2    Shue, Y.-K.3    McCarthy, P.4    Wendler, P.A.5    Li, T.6
  • 143
    • 11944267365 scopus 로고
    • Antisense oligonucleotides: A new therapeutic principle
    • (a) Uhlmann, E., Peyman, A. Antisense oligonucleotides: A new therapeutic principle. Chem Rev 1990, 90: 543-84.
    • (1990) Chem Rev , vol.90 , pp. 543-584
    • Uhlmann, E.1    Peyman, A.2
  • 144
    • 0027228277 scopus 로고
    • Current concepts in antisense drug design
    • (b) Milligan, B.F., Matteucci, M.D., Martin, J.C. Current concepts in antisense drug design. J Med Chem 1993, 36: 1923-37.
    • (1993) J Med Chem , vol.36 , pp. 1923-1937
    • Milligan, B.F.1    Matteucci, M.D.2    Martin, J.C.3
  • 145
    • 0029986009 scopus 로고    scopus 로고
    • Peptide nucleic acids (PNA): Synthesis, properties and potential applications
    • (c) Hyrup, B., Nielsen, P.E. Peptide nucleic acids (PNA): Synthesis, properties and potential applications. Bioorg Med Chem 1996, 4: 5-23.
    • (1996) Bioorg Med Chem , vol.4 , pp. 5-23
    • Hyrup, B.1    Nielsen, P.E.2
  • 147
    • 0018412567 scopus 로고
    • Prevention of colonization of the urinary tract of mice with Escherichia coli by blocking of bacterial adherence with methyl-α-D-mannopyranoside
    • Aronson, M., Medalia, O., Schori, L., Mirelman, D., Sharon, N., Ofek, I. Prevention of colonization of the urinary tract of mice with Escherichia coli by blocking of bacterial adherence with methyl-α-D-mannopyranoside. J Infect Dis 1979, 139: 329-32.
    • (1979) J Infect Dis , vol.139 , pp. 329-332
    • Aronson, M.1    Medalia, O.2    Schori, L.3    Mirelman, D.4    Sharon, N.5    Ofek, I.6
  • 148
    • 0027339137 scopus 로고
    • Carbohydrates in cell recognition
    • Sharon, N., Lis, H., Carbohydrates in cell recognition. Sci Am Jan. 1993, 82-9.
    • (1993) Sci Am Jan. , pp. 82-89
    • Sharon, N.1    Lis, H.2
  • 149
    • 0029990596 scopus 로고    scopus 로고
    • Thes tereospecific synthesis of methyl-α-C-mannobioside: A potential inhibitor of M. tuberculosis binding to human macrophages
    • Jarreton, O., Skrydstrup, T., Beau, J.-M. Thes tereospecific synthesis of methyl-α-C-mannobioside: A potential inhibitor of M. tuberculosis binding to human macrophages. Chem Commun 1996, 1661-2.
    • (1996) Chem Commun , pp. 1661-1662
    • Jarreton, O.1    Skrydstrup, T.2    Beau, J.-M.3
  • 150
    • 0028842451 scopus 로고
    • Synthesis of a functionalized hexasaccharide precursor of a glycoconjugate vaccine against cholera
    • (a) Ogawa, Y., Lei, P.-S., Kovác, P. Synthesis of a functionalized hexasaccharide precursor of a glycoconjugate vaccine against cholera. Bioorg Med Chem Lett 1995, 5: 2283-6.
    • (1995) Bioorg Med Chem Lett , vol.5 , pp. 2283-2286
    • Ogawa, Y.1    Lei, P.-S.2    Kovác, P.3
  • 151
    • 0040180603 scopus 로고
    • Synthesis of terminal disaccharides corresponding to Owaga and Inaba antigenic determinant from Vibrio cholerae
    • (b) Arencibia-Mohar, A., Madrazo-Alonso, O., Ariosa-Alvarez, A. et al. Synthesis of terminal disaccharides corresponding to Owaga and Inaba antigenic determinant from Vibrio cholerae. Carbohydr Lett 1995, 1: 173-8.
    • (1995) Carbohydr Lett , vol.1 , pp. 173-178
    • Arencibia-Mohar, A.1    Madrazo-Alonso, O.2    Ariosa-Alvarez, A.3
  • 152
    • 1842367161 scopus 로고
    • The recognition of carbohydrate antigens by antibody at atomic resolution
    • Bundle, D.R. The recognition of carbohydrate antigens by antibody at atomic resolution. Carbohydr Eur 1994, 22-30.
    • (1994) Carbohydr Eur , pp. 22-30
    • Bundle, D.R.1
  • 153
    • 0030591866 scopus 로고    scopus 로고
    • Novel inhibitors of influenza sialidases related to GC167. Structure-activity, crystallographic and molecular dynamics studies with 4H-pyran-2-carboxylic acid 6-carboxamides
    • (a) Smith, P.W., Sollis, S.L., Howes, P.D. et al. Novel inhibitors of influenza sialidases related to GC167. Structure-activity, crystallographic and molecular dynamics studies with 4H-pyran-2-carboxylic acid 6-carboxamides. Bioorg Med Chem Lett 1996, 6: 2931-6.
    • (1996) Bioorg Med Chem Lett , vol.6 , pp. 2931-2936
    • Smith, P.W.1    Sollis, S.L.2    Howes, P.D.3
  • 154
    • 37049080529 scopus 로고
    • Synthesis of 6-, 7- and 8-carbon sugar analogues of potent anti-influenza 2,3-didehydro-2,3-dideoxy- N-acetylneuraminic acid derivatives
    • (b) Bamford, M.J., Castro Pichel, J., Husman, W., Patel, B., Storer, R., Weir, N.G. Synthesis of 6-, 7-and 8-carbon sugar analogues of potent anti-influenza 2,3-didehydro-2,3-dideoxy-N-acetylneuraminic acid derivatives. J Chem Soc Perkin Trans I 1995, 1181-7.
    • (1995) J Chem Soc Perkin Trans I , pp. 1181-1187
    • Bamford, M.J.1    Castro Pichel, J.2    Husman, W.3    Patel, B.4    Storer, R.5    Weir, N.G.6
  • 155
    • 37049089589 scopus 로고
    • Approaches to carbocyclic analogues of the potent neuraminidase inhibitor 4-guanidino-Neu5Ac2en. X-ray molecular structure of N-[(1S,2S,6R)-2-azido-6-benzyloxymethyl-4-formylcyclo-hex-3-enyl]acetamide
    • Chandler, M., Conroy, R., Cooper, A.W.J. et al. Approaches to carbocyclic analogues of the potent neuraminidase inhibitor 4-guanidino-Neu5Ac2en. X-ray molecular structure of N-[(1S,2S,6R)-2-azido-6-benzyloxymethyl-4-formylcyclo-hex-3-enyl]acetamide. J Chem Soc Perkin Trans I 1995, 1189-91.
    • (1995) J Chem Soc Perkin Trans I , pp. 1189-1191
    • Chandler, M.1    Conroy, R.2    Cooper, A.W.J.3
  • 156
    • 0027287506 scopus 로고
    • Rational design of potent sialidase-based inhibitors of influenza virus replication
    • (a) von Itzstein, M., Wu, W.-Y, Kok, G.B. et al. Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature 1993, 363: 418-23.
    • (1993) Nature , vol.363 , pp. 418-423
    • Von Itzstein, M.1    Wu, W.-Y.2    Kok, G.B.3
  • 157
    • 37049084551 scopus 로고
    • Synthesis of the potent influenza neuraminidase inhibitor 4-guanidino Neu5Ac2en. X-ray molecular structure of 5-acetamido-4-amino-2,6-anhydro-3,4,5-trideoxy-D-erythro-L-gluconononic acid
    • (b) Chandler, M., Bamford, M.J., Conroy, R. et al. Synthesis of the potent influenza neuraminidase inhibitor 4-guanidino Neu5Ac2en. X-ray molecular structure of 5-acetamido-4-amino-2,6-anhydro-3,4,5-trideoxy-D-erythro-L-gluconononic acid. J Chem Soc Perkin Trans I 1995, 1173-80.
    • (1995) J Chem Soc Perkin Trans I , pp. 1173-1180
    • Chandler, M.1    Bamford, M.J.2    Conroy, R.3
  • 158
    • 0026326503 scopus 로고
    • Arresting tissue invasion of a parasite by protease inhibitors chosen with the aid of computer modeling
    • Cohen, F.E., Gregoret, L.M., Amiri, P., Aldape, K., Railey, J., McKerrow, J.H. Arresting tissue invasion of a parasite by protease inhibitors chosen with the aid of computer modeling. Biochemistry 1991, 30: 11221-9.
    • (1991) Biochemistry , vol.30 , pp. 11221-11229
    • Cohen, F.E.1    Gregoret, L.M.2    Amiri, P.3    Aldape, K.4    Railey, J.5    McKerrow, J.H.6
  • 159
    • 0027439498 scopus 로고
    • Inhibitors of two component signal transduction systems: Inhibition of alignate gene activation in Pseudomonas aeruginosa
    • Roychoudhury, S., Zeilinski, N.A., Ninfa, A.J. et al. Inhibitors of two component signal transduction systems: Inhibition of alignate gene activation in Pseudomonas aeruginosa. Proc Natl Acad Sci USA 1993, 90: 965-9.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 965-969
    • Roychoudhury, S.1    Zeilinski, N.A.2    Ninfa, A.J.3
  • 160
    • 0024843712 scopus 로고
    • Genetic regulation of bacterial virulence
    • (a) DiRita, V.J., Mekalanos, J.J. Genetic regulation of bacterial virulence. Annu Rev Genet 1989, 23: 455-82.
    • (1989) Annu Rev Genet , vol.23 , pp. 455-482
    • DiRita, V.J.1    Mekalanos, J.J.2
  • 161
    • 0002946893 scopus 로고
    • Structural and functional conservation in response regulators
    • Hoch, J.A., Silhavy, T.J. (Eds.). ASM Press: Washington, DC
    • (b) Volz, K. Structural and functional conservation in response regulators In: Two-Component Signal Transduction. Hoch, J.A., Silhavy, T.J. (Eds.). ASM Press: Washington, DC 1995, 53-64.
    • (1995) Two-Component Signal Transduction , pp. 53-64
    • Volz, K.1
  • 162
    • 0002685487 scopus 로고
    • Two-component signal transduction and its role in the expression of bacterial virulence factors
    • Hoch, J.A., Silhavy, T.J. (Eds.). ASM Press: Washington, DC
    • Dziejman, M., Mekalanos, J.J. Two-component signal transduction and its role in the expression of bacterial virulence factors. In: Two-Component Signal Transduction, Hoch, J.A., Silhavy, T.J. (Eds.). ASM Press: Washington, DC 1995, 305-17.
    • (1995) Two-Component Signal Transduction , pp. 305-317
    • Dziejman, M.1    Mekalanos, J.J.2


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