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Volumn 48, Issue 16, 2005, Pages 5349-5359

Designer antibacterial peptides kill fluoroquinolone-resistant clinical isolates

Author keywords

[No Author keywords available]

Indexed keywords

ARGINYLPROLYLASPARTYLLYSYLPROLYLARGINYLPROLYLTYROSYLLEUCYLPROLYLTHREONYLPRO LYLPROLYLPROLYLARGINYLPROLYLVALYLTYROSYLASPARAGINYLARGININE; CIPROFLOXACIN; PEPTIDE DERIVATIVE; PROLINE; PROTEIN DNAK; QUINOLINE DERIVED ANTIINFECTIVE AGENT; UNCLASSIFIED DRUG;

EID: 23644459481     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm050347i     Document Type: Article
Times cited : (82)

References (60)
  • 2
    • 10944272743 scopus 로고    scopus 로고
    • Antibacterial resistance worldwide: Causes, challenges and responses
    • Levy, S. B.; Marshall, B. Antibacterial resistance worldwide: causes, challenges and responses. Nat. Med. 2004, 10, S122-129.
    • (2004) Nat. Med. , vol.10
    • Levy, S.B.1    Marshall, B.2
  • 3
    • 1842832773 scopus 로고    scopus 로고
    • The use of fluoroquinolones in gonorrhea: The increasing problem of resistance
    • Dan, M. The use of fluoroquinolones in gonorrhea: the increasing problem of resistance. Expert Opin. Pharmacother. 2004, 5, 829-854.
    • (2004) Expert Opin. Pharmacother. , vol.5 , pp. 829-854
    • Dan, M.1
  • 4
    • 14844339904 scopus 로고    scopus 로고
    • Antibiotic resistance of Escherichia coli from community-acquired urinary tract infections in relation to demographic and clinical data
    • Alos, J. I.; Serrano, M. G.; Gomez-Garces, J. L.; Perianes, J. Antibiotic resistance of Escherichia coli from community-acquired urinary tract infections in relation to demographic and clinical data. Clin. Microbiol. Infect. 2005, 11, 199-203.
    • (2005) Clin. Microbiol. Infect. , vol.11 , pp. 199-203
    • Alos, J.I.1    Serrano, M.G.2    Gomez-Garces, J.L.3    Perianes, J.4
  • 5
    • 3042793159 scopus 로고    scopus 로고
    • Acute uncomplicated cystitis in an era of increasing antibiotic resistance: A proposed approach to empirical therapy
    • Hooton, T. M.; Besser, R.; Foxman, B.; Fritsche, T. R.; Nicolle, L. E. Acute uncomplicated cystitis in an era of increasing antibiotic resistance: a proposed approach to empirical therapy. Clin. Infect. Dis. 2004, 39, 75-80.
    • (2004) Clin. Infect. Dis. , vol.39 , pp. 75-80
    • Hooton, T.M.1    Besser, R.2    Foxman, B.3    Fritsche, T.R.4    Nicolle, L.E.5
  • 6
  • 7
    • 4644303468 scopus 로고    scopus 로고
    • Taking inventory: Antibacterial agents currently at or beyond Phase I
    • Bush, K.; Macielag, M.; Weidner-Wells, M. Taking inventory: antibacterial agents currently at or beyond Phase I. Curr. Opin. Microbiol. 2004, 7, 466-476.
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 466-476
    • Bush, K.1    Macielag, M.2    Weidner-Wells, M.3
  • 9
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • Hancock, R. E. W.; Scott, M. G. The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 8856-8861.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8856-8861
    • Hancock, R.E.W.1    Scott, M.G.2
  • 10
    • 15244342412 scopus 로고    scopus 로고
    • Walking the fine line between intracellular and membrane activities of antibacterial peptides
    • Bower, M. A.; Cudic, M.; Campbell, W.; Wade, J. D.; Otvos, L., Jr. Walking the fine line between intracellular and membrane activities of antibacterial peptides. Lett. Pept. Sci. 2003, 10, 463-473.
    • (2003) Lett. Pept. Sci. , vol.10 , pp. 463-473
    • Bower, M.A.1    Cudic, M.2    Campbell, W.3    Wade, J.D.4    Otvos Jr., L.5
  • 11
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen, Y.; Mant, C. T.; Farmer, S. W.; Hancock, R. E.; Vasil, M. L.; Hodges, R. S. Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J. Biol. Chem. 2005, 280, 12316-12329.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 12
    • 0036158878 scopus 로고    scopus 로고
    • Peptides as drugs: Is there a market?
    • Loffet, A. Peptides as drugs: is there a market? J. Pept. Sci. 2002, 8, 1-7.
    • (2002) J. Pept. Sci. , vol.8 , pp. 1-7
    • Loffet, A.1
  • 13
    • 0036214967 scopus 로고    scopus 로고
    • Intracellular targets of antibacterial peptides
    • Cudic, M.; Otvos, L., Jr. Intracellular targets of antibacterial peptides. Curr. Drug Targets 2002, 3, 101-106.
    • (2002) Curr. Drug Targets , vol.3 , pp. 101-106
    • Cudic, M.1    Otvos Jr., L.2
  • 14
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • Park, C. B.; Kim, H. S.; Kim, S. C. Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem. Biophys. Res. Commun. 1998, 244, 253-257.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 15
    • 0035853022 scopus 로고    scopus 로고
    • The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding
    • Kragol, G.; Lovas, S.; Varadi, G.; Condie, B. A.; Hoffmann, R.; Otvos, L., Jr. The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding. Biochemistry 2001, 40, 3016-3026.
    • (2001) Biochemistry , vol.40 , pp. 3016-3026
    • Kragol, G.1    Lovas, S.2    Varadi, G.3    Condie, B.A.4    Hoffmann, R.5    Otvos Jr., L.6
  • 17
    • 0036327627 scopus 로고    scopus 로고
    • The efficacy of the antibacterial peptide, pyrrhocoricin, is finely regulated by its amino acid residues and active domains
    • Bencivengo, A.-M.; Cudic, M.; Hoffmann, R.; Otvos, L., Jr. The efficacy of the antibacterial peptide, pyrrhocoricin, is finely regulated by its amino acid residues and active domains. Lett. Pept. Sci. 2001, 8, 201-209.
    • (2001) Lett. Pept. Sci. , vol.8 , pp. 201-209
    • Bencivengo, A.-M.1    Cudic, M.2    Hoffmann, R.3    Otvos Jr., L.4
  • 18
    • 0027973437 scopus 로고
    • Biodiversity of apidaecin-type peptide antibiotics. Prospects of manipulating the antibacterial spectrum and combating acquired resistance
    • Casteels, P.; Romagnolo, J.; Castle, M.; Casteels-Josson, K.; Erdjument-Bromage, H.; Tempst, P. Biodiversity of apidaecin-type peptide antibiotics. Prospects of manipulating the antibacterial spectrum and combating acquired resistance. J. Biol. Chem. 1994, 269, 26107-26115.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26107-26115
    • Casteels, P.1    Romagnolo, J.2    Castle, M.3    Casteels-Josson, K.4    Erdjument-Bromage, H.5    Tempst, P.6
  • 20
  • 21
    • 0042430615 scopus 로고    scopus 로고
    • In vitro and in vivo activity of a designed antibacterial peptide analogue against uropathogens
    • Cudic, M.; Lockatell, C. V.; Johnson, D. E.; Otvos, L., Jr. In vitro and in vivo activity of a designed antibacterial peptide analogue against uropathogens. Peptides 2003, 24, 807-820.
    • (2003) Peptides , vol.24 , pp. 807-820
    • Cudic, M.1    Lockatell, C.V.2    Johnson, D.E.3    Otvos Jr., L.4
  • 23
    • 0036633301 scopus 로고    scopus 로고
    • The short, proline-rich antibacterial peptide family
    • Otvos, L. The short, proline-rich antibacterial peptide family. Cell. Mol. Life Sci. 2002, 59, 1138-1150.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1138-1150
    • Otvos, L.1
  • 24
    • 0028304808 scopus 로고
    • Novel inducible antibacterial peptides from a hemipteran insect, the sap sucking-bug Pyrrhocoris apterus
    • Cociancich, S.; Dupont, A.; Hegy, G.; Lanot, R.; Holder, F.; Hetru, C.; Hoffmann, J. A.; Bulet, P. Novel inducible antibacterial peptides from a hemipteran insect, the sap sucking-bug Pyrrhocoris apterus. Biochem. J. 1994, 300, 567-575.
    • (1994) Biochem. J. , vol.300 , pp. 567-575
    • Cociancich, S.1    Dupont, A.2    Hegy, G.3    Lanot, R.4    Holder, F.5    Hetru, C.6    Hoffmann, J.A.7    Bulet, P.8
  • 26
    • 0024454751 scopus 로고
    • Apidaecins: Antibacterial peptides from honeybees
    • Casteels, P.; Ampe, C.; Jacobs, F.; Vaeck, M.; Tempst, P. Apidaecins: antibacterial peptides from honeybees. EMBO J. 1989, 8, 2387-2391.
    • (1989) EMBO J. , vol.8 , pp. 2387-2391
    • Casteels, P.1    Ampe, C.2    Jacobs, F.3    Vaeck, M.4    Tempst, P.5
  • 27
    • 0029929079 scopus 로고    scopus 로고
    • Enlarged scale chemical synthesis and range of activity of drosocin, an O-glycosylated antibacterial peptide from Drosophila
    • Bulet, P.; Urge, L.; Ohresser, S.; Hetru, C.; Otvos, L., Jr. Enlarged scale chemical synthesis and range of activity of drosocin, an O-glycosylated antibacterial peptide from Drosophila. Eur. J. Biochem. 1996, 238, 64-69.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 64-69
    • Bulet, P.1    Urge, L.2    Ohresser, S.3    Hetru, C.4    Otvos Jr., L.5
  • 28
    • 0032992923 scopus 로고    scopus 로고
    • Range of activity and metabolic stability of synthetic antibacterial glycopeptides from insects
    • Hoffmann, R.; Bulet, P.; Urge, L.; Otvos, L., Jr. Range of activity and metabolic stability of synthetic antibacterial glycopeptides from insects. Biochim. Biophys. Acta 1999, 1426, 459-467.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 459-467
    • Hoffmann, R.1    Bulet, P.2    Urge, L.3    Otvos Jr., L.4
  • 29
    • 0019333890 scopus 로고
    • Structural significance of the amino-terminal residues of sperm whale myoglobin
    • DiMarchi, R. D.; Neireiter, G. W.; Heath, W. F.; Gurd, F. R. Structural significance of the amino-terminal residues of sperm whale myoglobin. Biochemistry 1980, 19, 2454-2465.
    • (1980) Biochemistry , vol.19 , pp. 2454-2465
    • Dimarchi, R.D.1    Neireiter, G.W.2    Heath, W.F.3    Gurd, F.R.4
  • 30
    • 0027070864 scopus 로고
    • Peptide stability in drug development: A comparison of peptide reactivity in different biological media
    • Powell, M. F.; Grey, H.; Gaeta, F.; Sette, A.; Colon, S. Peptide stability in drug development: a comparison of peptide reactivity in different biological media. J. Pharm. Sci. 1992, 81, 731-735.
    • (1992) J. Pharm. Sci. , vol.81 , pp. 731-735
    • Powell, M.F.1    Grey, H.2    Gaeta, F.3    Sette, A.4    Colon, S.5
  • 31
    • 0035814260 scopus 로고    scopus 로고
    • Liquid chromatography-mass spectrometry assay of a thiadiazole derivative in mice: Application to pharmacokinetic studies
    • Wong, H; Jia, L.; Camden, J. B.; Weitman, S. D. Liquid chromatography-mass spectrometry assay of a thiadiazole derivative in mice: application to pharmacokinetic studies. J. Chromatogr. 2001, 765, 55-62.
    • (2001) J. Chromatogr. , vol.765 , pp. 55-62
    • Wong, H.1    Jia, L.2    Camden, J.B.3    Weitman, S.D.4
  • 32
    • 0035877121 scopus 로고    scopus 로고
    • Pharmacokinetic differences between a T cell-tolerizing and a T cell-activating peptide
    • Weijzen, S.; Meredith, S. C.; Velders, M. P.; Elmishad, A. G.; Schreiber, H.; Kast, W. M. Pharmacokinetic differences between a T cell-tolerizing and a T cell-activating peptide. J. Immunol. 2001, 166, 7151-7157.
    • (2001) J. Immunol. , vol.166 , pp. 7151-7157
    • Weijzen, S.1    Meredith, S.C.2    Velders, M.P.3    Elmishad, A.G.4    Schreiber, H.5    Kast, W.M.6
  • 33
    • 0033485701 scopus 로고    scopus 로고
    • Chemical synthesis, antibacterial activity and conformation of diptericin, an 82-mer peptide originally isolated from insects
    • Cudic, M.; Bulet, P.; Hoffmann, R.; Craik, D. J.; Otvos, L. Jr. Chemical synthesis, antibacterial activity and conformation of diptericin, an 82-mer peptide originally isolated from insects. Eur. J. Biochem. 2002, 266, 549-558.
    • (2002) Eur. J. Biochem. , vol.266 , pp. 549-558
    • Cudic, M.1    Bulet, P.2    Hoffmann, R.3    Craik, D.J.4    Otvos Jr., L.5
  • 34
    • 0031813836 scopus 로고    scopus 로고
    • Comparison of Escherichia coli strains recovered from human cystitis and pyelonephritis infections in transurethrally challenged mice
    • Johnson, D. E.; Lockatell, C. V.; Russell, R. G.; Hebel, J. R.; Island, M. D.; Stapleton, A.; Stamm, W. E.; Warren, J. W. Comparison of Escherichia coli strains recovered from human cystitis and pyelonephritis infections in transurethrally challenged mice. Infect. Immun. 1998, 66, 3059-3065.
    • (1998) Infect. Immun. , vol.66 , pp. 3059-3065
    • Johnson, D.E.1    Lockatell, C.V.2    Russell, R.G.3    Hebel, J.R.4    Island, M.D.5    Stapleton, A.6    Stamm, W.E.7    Warren, J.W.8
  • 36
    • 0001994881 scopus 로고    scopus 로고
    • Susceptibility testing of antimicrobials in liquid media
    • Loman, V., Ed; Williams and Wilkins: Philadelphia
    • Amsterdam, D. Susceptibility testing of antimicrobials in liquid media. In Antibiotics in Laboratory Medicine; Loman, V., Ed; Williams and Wilkins: Philadelphia, 1996; pp 52-111.
    • (1996) Antibiotics in Laboratory Medicine , pp. 52-111
    • Amsterdam, D.1
  • 37
    • 0342699767 scopus 로고    scopus 로고
    • Antimicrobial peptides derived from heme-containing proteins: Hemocidins
    • Mak, P.; Wojcik, K.; Silberring, J.; Dubin, A. Antimicrobial peptides derived from heme-containing proteins: hemocidins. Antonie Van Leeuwenhoek 2000, 77, 197-207.
    • (2000) Antonie Van Leeuwenhoek , vol.77 , pp. 197-207
    • Mak, P.1    Wojcik, K.2    Silberring, J.3    Dubin, A.4
  • 38
    • 0036785559 scopus 로고    scopus 로고
    • The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses
    • Scott, M. G.; Davidson, D. J.; Gold, M. R.; Bowdish, D.; Hancock, R. E. The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses. J. Immunol. 2002, 169, 3883-3891.
    • (2002) J. Immunol. , vol.169 , pp. 3883-3891
    • Scott, M.G.1    Davidson, D.J.2    Gold, M.R.3    Bowdish, D.4    Hancock, R.E.5
  • 41
    • 0036765438 scopus 로고    scopus 로고
    • The combined effects of antibacterial peptide cecropin a and anti-cancer agents on leukemia cells
    • Hui, L.; Leung, K.; Chen, H. M. The combined effects of antibacterial peptide cecropin A and anti-cancer agents on leukemia cells. Anticancer Res. 2002, 22, 2811-2816.
    • (2002) Anticancer Res. , vol.22 , pp. 2811-2816
    • Hui, L.1    Leung, K.2    Chen, H.M.3
  • 42
    • 0035896429 scopus 로고    scopus 로고
    • Ancient system gets new respect
    • Gura, T. Ancient system gets new respect. Science 2001, 291, 2068-2071.
    • (2001) Science , vol.291 , pp. 2068-2071
    • Gura, T.1
  • 47
    • 0037103242 scopus 로고    scopus 로고
    • Arginine-rich molecular transporters for drug delivery: Role of backbone spacing in cellular uptake
    • Rothbard, J. B.; Kreider, E.; VanDeusen, C. L.; Wright, L.; Wylie, B. L.; Wender, P. A. Arginine-rich molecular transporters for drug delivery: role of backbone spacing in cellular uptake. J. Med. Chem. 2002, 45, 3612-3618.
    • (2002) J. Med. Chem. , vol.45 , pp. 3612-3618
    • Rothbard, J.B.1    Kreider, E.2    Vandeusen, C.L.3    Wright, L.4    Wylie, B.L.5    Wender, P.A.6
  • 48
    • 3142774800 scopus 로고    scopus 로고
    • Potential peptide carriers: Amphipathic proline-rich peptides derived from the N-terminal domain of γ-zein
    • Fernandez-Carneado, J.; Kogan, M. J.; Castel, S.; Giralt, E. Potential peptide carriers: amphipathic proline-rich peptides derived from the N-terminal domain of γ-zein. Angew. Chem., Int. Ed. 2004, 43, 1811-1814.
    • (2004) Angew. Chem., Int. Ed. , vol.43 , pp. 1811-1814
    • Fernandez-Carneado, J.1    Kogan, M.J.2    Castel, S.3    Giralt, E.4
  • 51
    • 0037179619 scopus 로고    scopus 로고
    • Antimicrobial peptides: Synthesis and antibacterial activity of linear and cyclic drosocin and apidaecin Ib analogues
    • Gobbo, M.; Biondi, L.; Filira, F.; Gennaro, R.; Benincasa, M.; Scolaro, B.; Rocchi, R. Antimicrobial peptides: synthesis and antibacterial activity of linear and cyclic drosocin and apidaecin Ib analogues. J. Med. Chem. 2002, 45, 4494-4504.
    • (2002) J. Med. Chem. , vol.45 , pp. 4494-4504
    • Gobbo, M.1    Biondi, L.2    Filira, F.3    Gennaro, R.4    Benincasa, M.5    Scolaro, B.6    Rocchi, R.7
  • 52
    • 0033547753 scopus 로고    scopus 로고
    • Conformational studies by NMR of the antimicrobial peptide, drosocin, and its non-glycosylated derivative: Effects of glycosylation on solution conformation
    • McManus, A. M.; Otvos, L. Jr.; Hoffmann, R.; Craik, D. J. Conformational studies by NMR of the antimicrobial peptide, drosocin, and its non-glycosylated derivative: effects of glycosylation on solution conformation. Biochemistry 1999, 38, 705-714.
    • (1999) Biochemistry , vol.38 , pp. 705-714
    • McManus, A.M.1    Otvos Jr., L.2    Hoffmann, R.3    Craik, D.J.4
  • 53
    • 2442538316 scopus 로고    scopus 로고
    • Primary structure and in vitro antibacterial properties of the Drosophila melanogaster attacin C Pro-domain
    • Rabel, D.; Charlet, M.; Ehret-Sabatier, L.; Cavicchioli, L.; Cudic, M.; Otvos, L., Jr.; Bulet P. Primary structure and in vitro antibacterial properties of the Drosophila melanogaster attacin C Pro-domain. J. Biol. Chem. 2004, 279, 14853-14859.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14853-14859
    • Rabel, D.1    Charlet, M.2    Ehret-Sabatier, L.3    Cavicchioli, L.4    Cudic, M.5    Otvos Jr., L.6    Bulet, P.7
  • 54
    • 0033801238 scopus 로고    scopus 로고
    • Human lactoferricin and peptides derived from a surface-exposed helical region reduce experimental Escherichia coli urinary tract infection in mice
    • Haversen, L. A.; Engberg, I.; Baltzer, L.; Dolphin, G.; Hanson, L. A.; Mattsby-Baltzer, I. Human lactoferricin and peptides derived from a surface-exposed helical region reduce experimental Escherichia coli urinary tract infection in mice. Infect. Immun. 2000, 68, 5816-5823.
    • (2000) Infect. Immun. , vol.68 , pp. 5816-5823
    • Haversen, L.A.1    Engberg, I.2    Baltzer, L.3    Dolphin, G.4    Hanson, L.A.5    Mattsby-Baltzer, I.6
  • 55
    • 0036931775 scopus 로고    scopus 로고
    • Comparison of once-daily extended-release ciprofloxacin and conventional twice-daily ciprofloxacin for the treatment of uncomplicated urinary tract infection in women
    • Henry, D. C., Jr.; Bettis, R. B.; Riffer, E.; Haverstock, D. C.; Kowalsky, S. F.; Manning, K.; Hamed, K. A.; Church, D. A. Comparison of once-daily extended-release ciprofloxacin and conventional twice-daily ciprofloxacin for the treatment of uncomplicated urinary tract infection in women. Clin. Ther. 2002, 24, 2088-2104.
    • (2002) Clin. Ther. , vol.24 , pp. 2088-2104
    • Henry Jr., D.C.1    Bettis, R.B.2    Riffer, E.3    Haverstock, D.C.4    Kowalsky, S.F.5    Manning, K.6    Hamed, K.A.7    Church, D.A.8
  • 57
    • 0018719070 scopus 로고
    • Gentamicin for treatment of resistant urinary tract infections in dogs
    • Ling, G. V.; Ruby, A. L. Gentamicin for treatment of resistant urinary tract infections in dogs. J. Am. Vet. Med. Assoc. 1979, 175, 480-481.
    • (1979) J. Am. Vet. Med. Assoc. , vol.175 , pp. 480-481
    • Ling, G.V.1    Ruby, A.L.2
  • 58
    • 0041382380 scopus 로고    scopus 로고
    • Trends in fluoroquinolone resistance of bacteria isolated from canine urinary tracts
    • Cohn, L. A.; Gary, A. T.; Fales, W. H.; Madsen, R. W. Trends in fluoroquinolone resistance of bacteria isolated from canine urinary tracts. J. Vet. Diagn. Invest. 2003, 15, 338-343.
    • (2003) J. Vet. Diagn. Invest. , vol.15 , pp. 338-343
    • Cohn, L.A.1    Gary, A.T.2    Fales, W.H.3    Madsen, R.W.4
  • 59
    • 0037080164 scopus 로고    scopus 로고
    • Enrofloxacin resistance in Escherichia coli isolated from dogs with urinary tract infections
    • Cooke, C. L.; Singer R. S.; Jang, S. S.; Hirsh, D. C. Enrofloxacin resistance in Escherichia coli isolated from dogs with urinary tract infections. J. Am. Vet. Med. Assoc. 2002, 220, 190-192.
    • (2002) J. Am. Vet. Med. Assoc. , vol.220 , pp. 190-192
    • Cooke, C.L.1    Singer, R.S.2    Jang, S.S.3    Hirsh, D.C.4
  • 60
    • 0025232814 scopus 로고
    • Solid-phase peptide synthesis using 9-fluorenylmethoxycarbonyl amino acids
    • Fields, G. B.; Noble, R. L. Solid-phase peptide synthesis using 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 1990, 35, 161-214.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2


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