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Journal Abstract Search

298 related items for PubMed ID: 17915249

  • 1. The Zn2 position in metallo-beta-lactamases is critical for activity: a study on chimeric metal sites on a conserved protein scaffold.
    González JM, Medrano Martín FJ, Costello AL, Tierney DL, Vila AJ.
    J Mol Biol; 2007 Nov 09; 373(5):1141-56. PubMed ID: 17915249
    [Abstract] [Full Text] [Related]

  • 2. Metal content and localization during turnover in B. cereus metallo-beta-lactamase.
    Llarrull LI, Tioni MF, Vila AJ.
    J Am Chem Soc; 2008 Nov 26; 130(47):15842-51. PubMed ID: 18980306
    [Abstract] [Full Text] [Related]

  • 3. Evidence of adaptability in metal coordination geometry and active-site loop conformation among B1 metallo-beta-lactamases .
    González JM, Buschiazzo A, Vila AJ.
    Biochemistry; 2010 Sep 14; 49(36):7930-8. PubMed ID: 20677753
    [Abstract] [Full Text] [Related]

  • 4. Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo-beta-lactamases.
    Murphy TA, Catto LE, Halford SE, Hadfield AT, Minor W, Walsh TR, Spencer J.
    J Mol Biol; 2006 Mar 31; 357(3):890-903. PubMed ID: 16460758
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  • 5. Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism.
    Davies AM, Rasia RM, Vila AJ, Sutton BJ, Fabiane SM.
    Biochemistry; 2005 Mar 29; 44(12):4841-9. PubMed ID: 15779910
    [Abstract] [Full Text] [Related]

  • 6. The variation of catalytic efficiency of Bacillus cereus metallo-beta-lactamase with different active site metal ions.
    Badarau A, Page MI.
    Biochemistry; 2006 Sep 05; 45(35):10654-66. PubMed ID: 16939217
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  • 7. Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme.
    Fabiane SM, Sohi MK, Wan T, Payne DJ, Bateson JH, Mitchell T, Sutton BJ.
    Biochemistry; 1998 Sep 08; 37(36):12404-11. PubMed ID: 9730812
    [Abstract] [Full Text] [Related]

  • 8. Positively cooperative binding of zinc ions to Bacillus cereus 569/H/9 beta-lactamase II suggests that the binuclear enzyme is the only relevant form for catalysis.
    Jacquin O, Balbeur D, Damblon C, Marchot P, De Pauw E, Roberts GC, Frère JM, Matagne A.
    J Mol Biol; 2009 Oct 09; 392(5):1278-91. PubMed ID: 19665032
    [Abstract] [Full Text] [Related]

  • 9. Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily.
    Bebrone C.
    Biochem Pharmacol; 2007 Dec 15; 74(12):1686-701. PubMed ID: 17597585
    [Abstract] [Full Text] [Related]

  • 10. Enzyme deactivation due to metal-ion dissociation during turnover of the cobalt-beta-lactamase catalyzed hydrolysis of beta-lactams.
    Badarau A, Page MI.
    Biochemistry; 2006 Sep 12; 45(36):11012-20. PubMed ID: 16953588
    [Abstract] [Full Text] [Related]

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  • 12. Evidence for a dinuclear active site in the metallo-beta-lactamase BcII with substoichiometric Co(II). A new model for metal uptake.
    Llarrull LI, Tioni MF, Kowalski J, Bennett B, Vila AJ.
    J Biol Chem; 2007 Oct 19; 282(42):30586-95. PubMed ID: 17715135
    [Abstract] [Full Text] [Related]

  • 13. Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase.
    Chantalat L, Duée E, Galleni M, Frère JM, Dideberg O.
    Protein Sci; 2000 Jul 19; 9(7):1402-6. PubMed ID: 10933508
    [Abstract] [Full Text] [Related]

  • 14. Thiols as classical and slow-binding inhibitors of IMP-1 and other binuclear metallo-beta-lactamases.
    Siemann S, Clarke AJ, Viswanatha T, Dmitrienko GI.
    Biochemistry; 2003 Feb 18; 42(6):1673-83. PubMed ID: 12578382
    [Abstract] [Full Text] [Related]

  • 15. Mimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations.
    Tomatis PE, Rasia RM, Segovia L, Vila AJ.
    Proc Natl Acad Sci U S A; 2005 Sep 27; 102(39):13761-6. PubMed ID: 16172409
    [Abstract] [Full Text] [Related]

  • 16. Engineered mononuclear variants in Bacillus cereus metallo-beta-lactamase BcII are inactive.
    Abriata LA, González LJ, Llarrull LI, Tomatis PE, Myers WK, Costello AL, Tierney DL, Vila AJ.
    Biochemistry; 2008 Aug 19; 47(33):8590-9. PubMed ID: 18652482
    [Abstract] [Full Text] [Related]

  • 17. Asp120Asn mutation impairs the catalytic activity of NDM-1 metallo-β-lactamase: experimental and computational study.
    Chen J, Chen H, Zhu T, Zhou D, Zhang F, Lao X, Zheng H.
    Phys Chem Chem Phys; 2014 Apr 14; 16(14):6709-16. PubMed ID: 24584846
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  • 19. Zn(II) dependence of the Aeromonas hydrophila AE036 metallo-beta-lactamase activity and stability.
    Hernandez Valladares M, Felici A, Weber G, Adolph HW, Zeppezauer M, Rossolini GM, Amicosante G, Frère JM, Galleni M.
    Biochemistry; 1997 Sep 23; 36(38):11534-41. PubMed ID: 9298974
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