메뉴 건너뛰기




Volumn 41, Issue 4, 1997, Pages 866-868

Sensitivity of Aeromonas hydrophila carbapenemase to δ3-cephems: Comparative study with other metallo-β-lactamases

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE; BETA LACTAMASE INHIBITOR; CEFOXITIN; CEFTRIAXONE; CEPHALOSPORIN C; CEPHALOSPORIN C GAMMA LACTONE; CEPHALOSPORIN DERIVATIVE; CILASTATIN; LORACARBEF; PANIPENEM; RO 09 1428; TAZOBACTAM; UNCLASSIFIED DRUG;

EID: 0030933875     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.41.4.866     Document Type: Article
Times cited : (10)

References (10)
  • 2
    • 0027515959 scopus 로고
    • Kinetic interactions of tazobactam with β-lactamases from all major structural classes
    • Bush, K., C. Macalintal, B. A. Rasmussen, V. J. Lee, and Y. Yang. 1993. Kinetic interactions of tazobactam with β-lactamases from all major structural classes. Antimicrob. Agents Chemother. 37:851-858.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 851-858
    • Bush, K.1    Macalintal, C.2    Rasmussen, B.A.3    Lee, V.J.4    Yang, Y.5
  • 3
    • 0028810769 scopus 로고
    • The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold
    • Carfi, A., S. Pares, E. Duée, M. Galleni, C. Duez, J.-M. Frère, and O. Dideberg. 1995. The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14:4914-4921.
    • (1995) EMBO J. , vol.14 , pp. 4914-4921
    • Carfi, A.1    Pares, S.2    Duée, E.3    Galleni, M.4    Duez, C.5    Frère, J.-M.6    Dideberg, O.7
  • 4
    • 0030586055 scopus 로고    scopus 로고
    • Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis
    • Concha, N. O., B. A. Rasmussen, K. Bush, and O. Herzberg. 1996. Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis. Structure 4:823-836.
    • (1996) Structure , vol.4 , pp. 823-836
    • Concha, N.O.1    Rasmussen, B.A.2    Bush, K.3    Herzberg, O.4
  • 7
    • 0028837277 scopus 로고
    • Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo-β-lactamases
    • Felici, A., and G. Amicosante. 1995. Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo-β-lactamases. Antimicrob. Agents Chemother. 39:192-199.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 192-199
    • Felici, A.1    Amicosante, G.2
  • 8
    • 0029031384 scopus 로고
    • The renal membrane dipeptidase (dehydropeptidase I) inhibitor, cilastatin, inhibits the bacterial metallo-β-lactamase enzyme CphA
    • Keynan, S., N. M. Hooper, A. Felici, G. Amicosante, and A. J. Turner. 1995. The renal membrane dipeptidase (dehydropeptidase I) inhibitor, cilastatin, inhibits the bacterial metallo-β-lactamase enzyme CphA. Antimicrob. Agents Chemother. 39:1629-1631.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1629-1631
    • Keynan, S.1    Hooper, N.M.2    Felici, A.3    Amicosante, G.4    Turner, A.J.5
  • 9
    • 0027284501 scopus 로고
    • Metallo-β-lactamases - A new therapeutic challenge
    • Payne, D. J. 1993. Metallo-β-lactamases - a new therapeutic challenge. J. Med. Microbiol. 39:93-99.
    • (1993) J. Med. Microbiol. , vol.39 , pp. 93-99
    • Payne, D.J.1
  • 10
    • 0023650377 scopus 로고
    • The importance of the negative charge of β-lactam compounds for the inactivation of the active site serine dipeptidase of Streptomyces R61
    • Varetto, L., J.-M. Frère, and J.-M. Ghuysen. 1987. The importance of the negative charge of β-lactam compounds for the inactivation of the active site serine dipeptidase of Streptomyces R61. FEBS Lett. 225:218-222.
    • (1987) FEBS Lett. , vol.225 , pp. 218-222
    • Varetto, L.1    Frère, J.-M.2    Ghuysen, J.-M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.