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Volumn 17, Issue 7, 2006, Pages 1000-1004

Studies on Ternary Metallo-β Lactamase-Inhibitor Complexes Using Electrospray Ionization Mass Spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

IONIZATION MASS SPECTROMETRY; LACTAMASE-INHIBITOR COMPLEXES; METALLO-Β-LACTAMASES (MBL); OPTIMAL METAL STOICHIOMETRIES;

EID: 33745255068     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2006.03.010     Document Type: Article
Times cited : (21)

References (20)
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    • Metallo-β-lactamases. Two binding sites for one catalytic metal ion?
    • Heinz U., and Adolph H.W. Metallo-β-lactamases. Two binding sites for one catalytic metal ion?. Cell. Mol. Life. Sci. 61 (2004) 2827-2839
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    • Heinz, U.1    Adolph, H.W.2
  • 8
    • 0042707576 scopus 로고    scopus 로고
    • The inhibitor thiomandelic acid binds to both metal ions in metallo-β-lactamase and induces positive cooperativity in metal binding
    • Damblon C., Jensen M., Ababou A., Barsukov I., Papamicael C., Schofield C.J., Olsen L., Bauer R., and Roberts G.C. The inhibitor thiomandelic acid binds to both metal ions in metallo-β-lactamase and induces positive cooperativity in metal binding. J. Biol. Chem. 278 (2003) 29240-29251
    • (2003) J. Biol. Chem. , vol.278 , pp. 29240-29251
    • Damblon, C.1    Jensen, M.2    Ababou, A.3    Barsukov, I.4    Papamicael, C.5    Schofield, C.J.6    Olsen, L.7    Bauer, R.8    Roberts, G.C.9
  • 9
    • 0034681922 scopus 로고    scopus 로고
    • Crystal structure of the IMP-1 metallo β-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor. Binding determinants of a potent, broad-spectrum inhibitor
    • Concha N.O., Janson C.A., Rowling P., Pearson S., Cheever C.A., Clarke B.P., Lewis C., Galleni M., Frère J.M., Payne D.J., Bateson J.H., and Abdel-Meguid S.S. Crystal structure of the IMP-1 metallo β-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor. Binding determinants of a potent, broad-spectrum inhibitor. Biochemistry 39 (2000) 4288-4298
    • (2000) Biochemistry , vol.39 , pp. 4288-4298
    • Concha, N.O.1    Janson, C.A.2    Rowling, P.3    Pearson, S.4    Cheever, C.A.5    Clarke, B.P.6    Lewis, C.7    Galleni, M.8    Frère, J.M.9    Payne, D.J.10    Bateson, J.H.11    Abdel-Meguid, S.S.12
  • 13
    • 11744250060 scopus 로고
    • Study of noncovalent enzyme-inhibitor complexes and metal binding stoichiometry of matrilysin by electrospray ionization mass spectrometry
    • Feng R., Castelhano A.L., Biuedeau R., and Yuan Z. Study of noncovalent enzyme-inhibitor complexes and metal binding stoichiometry of matrilysin by electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 6 (1995) 1105-1111
    • (1995) J. Am. Soc. Mass Spectrom. , vol.6 , pp. 1105-1111
    • Feng, R.1    Castelhano, A.L.2    Biuedeau, R.3    Yuan, Z.4
  • 18
    • 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., Pares S., Duee E., Galleni M., Duez C., Frère J.M., and Dideberg O. The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14 (1995) 4914-4921
    • (1995) EMBO J. , vol.14 , pp. 4914-4921
    • Carfi, A.1    Pares, S.2    Duee, E.3    Galleni, M.4    Duez, C.5    Frère, J.M.6    Dideberg, O.7
  • 19
    • 0038338887 scopus 로고    scopus 로고
    • Quantitative determination of noncovalent binding interactions using automated nanoelectrospray mass spectrometry
    • Zhang S., Van Pelt C.K., and Wilson D.B. Quantitative determination of noncovalent binding interactions using automated nanoelectrospray mass spectrometry. Anal. Chem. 75 (2003) 3010-3018
    • (2003) Anal. Chem. , vol.75 , pp. 3010-3018
    • Zhang, S.1    Van Pelt, C.K.2    Wilson, D.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.