메뉴 건너뛰기




Volumn 148, Issue 1, 1997, Pages 59-62

Tazobactam is a potent inactivator of selected inhibitor-resistant class A β-lactamases

Author keywords

inhibitor resistant lactamase; piperacillin; tazobactam

Indexed keywords

AMPICILLIN; BETA LACTAMASE; CLAVULANIC ACID; PIPERACILLIN; SULBACTAM; TAZOBACTAM; TICARCILLIN;

EID: 0031105398     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(97)00013-X     Document Type: Article
Times cited : (40)

References (14)
  • 1
    • 0027370236 scopus 로고
    • Characteristics of a new TEM-type β-lactamase resistant to clavulanate, sulbactam, and tazobactam in a clinical isolate or Escherichia coli
    • Blazquez, J., Baquero, M.R., Canton, R., Alos, I., and Baquero, F. (1993) Characteristics of a new TEM-type β-lactamase resistant to clavulanate, sulbactam, and tazobactam in a clinical isolate or Escherichia coli. Antimicrob. Agents Chemother. 37, 2059-2063.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 2059-2063
    • Blazquez, J.1    Baquero, M.R.2    Canton, R.3    Alos, I.4    Baquero, F.5
  • 2
    • 0028798040 scopus 로고
    • Molecular characterization of nine different types of mutants among 107 inhibitor-resistant TEM β-lactamases from clinical isolates of Escherichia coli
    • Henquell, C., Chanal, C., Sirot, D., Labia, R., and Sirot, J. (1995) Molecular characterization of nine different types of mutants among 107 inhibitor-resistant TEM β-lactamases from clinical isolates of Escherichia coli. Antimicrob. Agents Chemother. 39, 427-437.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 427-437
    • Henquell, C.1    Chanal, C.2    Sirot, D.3    Labia, R.4    Sirot, J.5
  • 5
    • 0028302091 scopus 로고
    • Emergence of clinical isolates of Esterichia coli producing TEM-1 derivatives or an OXA-1 β-lactamase conferring resistnce to β-lactamase inhibitors
    • Zhou, X.Y., Bordon, F., Sirot, D., Kitzis, M.-D., Gutmann, L. (1994) Emergence of clinical isolates of Esterichia coli producing TEM-1 derivatives or an OXA-1 β-lactamase conferring resistnce to β-lactamase inhibitors. Antimicrob. Agents Chemother. 38, 1085-1089.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1085-1089
    • Zhou, X.Y.1    Bordon, F.2    Sirot, D.3    Kitzis, M.-D.4    Gutmann, L.5
  • 7
    • 0029120340 scopus 로고    scopus 로고
    • The asparagine to aspartic acid substitution at position 276 of TEM-35 and TEM-36 is involved in β-lactamase resistance to clavulanic acid
    • (19??)
    • Saves, I., Burlet-Schultz, O., Swaren, P., Lefevre, F., Masson, J.M., Prome, J.C., and Samama, J.P. (19??) The asparagine to aspartic acid substitution at position 276 of TEM-35 and TEM-36 is involved in β-lactamase resistance to clavulanic acid. J. Biol. Chem. 270, 18240-18245.
    • J. Biol. Chem. , vol.270 , pp. 18240-18245
    • Saves, I.1    Burlet-Schultz, O.2    Swaren, P.3    Lefevre, F.4    Masson, J.M.5    Prome, J.C.6    Samama, J.P.7
  • 8
    • 0026846814 scopus 로고
    • OHIO-1 beta-lactamase resistant to mechanism-based inactivators
    • Bonomo, R.A., Currie-McCumber, C., and Shlaes, D.M. (1992) OHIO-1 beta-lactamase resistant to mechanism-based inactivators. FEMS Microbiol. Lett. 92, 79-82.
    • (1992) FEMS Microbiol. Lett. , vol.92 , pp. 79-82
    • Bonomo, R.A.1    Currie-McCumber, C.2    Shlaes, D.M.3
  • 9
    • 0028985358 scopus 로고
    • β-lactamase mutation far from the active site influence inhibitor binding
    • Bonomo, R.A., Dawes, C.G., Knox, J.R., and Shlaes, D.M. (1995) β-lactamase mutation far from the active site influence inhibitor binding. Biochim. Biophys. Acta 1247, 121-125.
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 121-125
    • Bonomo, R.A.1    Dawes, C.G.2    Knox, J.R.3    Shlaes, D.M.4
  • 10
    • 0028954421 scopus 로고
    • Complementary role of positions 69 and 242 in β-lactam binding in OHIO-1 a class A β-lactamase
    • Bonomo, R.A., Dawes, C.G., Knox, J.R., and Shlaes, D.M. (1995) Complementary role of positions 69 and 242 in β-lactam binding in OHIO-1 a class A β-lactamase. Biochim. Biophys. Acta 1247, 113-120.
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 113-120
    • Bonomo, R.A.1    Dawes, C.G.2    Knox, J.R.3    Shlaes, D.M.4
  • 12
    • 0027479143 scopus 로고
    • Determinants of the activity of β-lactamase inhibitor combinations
    • Livermore, D.M. (1993) Determinants of the activity of β-lactamase inhibitor combinations. J. Antimicrob. Chemother. 31, Suppl. A, 9-21.
    • (1993) J. Antimicrob. Chemother. , vol.31 , Issue.SUPPL. A , pp. 9-21
    • Livermore, D.M.1
  • 13
    • 0026654218 scopus 로고
    • Elucidation fo the role of arginine-244 in the turnover processes of class A β-lactamases
    • Zafarella, G., Manavathu, E.K., Lerner, S.A., and Mobashery, S. (1992) Elucidation fo the role of arginine-244 in the turnover processes of class A β-lactamases. Biochemistry 31, 3847-3852.
    • (1992) Biochemistry , vol.31 , pp. 3847-3852
    • Zafarella, G.1    Manavathu, E.K.2    Lerner, S.A.3    Mobashery, S.4
  • 14
    • 0028219728 scopus 로고
    • Comparative activities of clavulanic acid, sulbactam and tazobactam against clinically important β-lactamases
    • Payne, D.J., Cramp, R., Winstanley, D.J., and Knowles, D.J. (1994) Comparative activities of clavulanic acid, sulbactam and tazobactam against clinically important β-lactamases. Antimicrob. Agents Chemother. 38, 767-772.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 767-772
    • Payne, D.J.1    Cramp, R.2    Winstanley, D.J.3    Knowles, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.