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154 related items for PubMed ID: 17715946

  • 1. Structural basis for the role of Asp-120 in metallo-beta-lactamases.
    Crisp J, Conners R, Garrity JD, Carenbauer AL, Crowder MW, Spencer J.
    Biochemistry; 2007 Sep 18; 46(37):10664-74. PubMed ID: 17715946
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  • 2. The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution.
    Ullah JH, Walsh TR, Taylor IA, Emery DC, Verma CS, Gamblin SJ, Spencer J.
    J Mol Biol; 1998 Nov 20; 284(1):125-36. PubMed ID: 9811546
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  • 4. Structural consequences of the active site substitution Cys181 ==> Ser in metallo-beta-lactamase from Bacteroides fragilis.
    Li Z, Rasmussen BA, Herzberg O.
    Protein Sci; 1999 Jan 20; 8(1):249-52. PubMed ID: 10210203
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  • 5. 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
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  • 7. Antibiotic recognition by binuclear metallo-beta-lactamases revealed by X-ray crystallography.
    Spencer J, Read J, Sessions RB, Howell S, Blackburn GM, Gamblin SJ.
    J Am Chem Soc; 2005 Oct 19; 127(41):14439-44. PubMed ID: 16218639
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  • 10. Antibiotic deactivation by a dizinc beta-lactamase: mechanistic insights from QM/MM and DFT studies.
    Xu D, Guo H, Cui Q.
    J Am Chem Soc; 2007 Sep 05; 129(35):10814-22. PubMed ID: 17691780
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  • 11. Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis.
    Concha NO, Rasmussen BA, Bush K, Herzberg O.
    Protein Sci; 1997 Dec 05; 6(12):2671-6. PubMed ID: 9416622
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  • 12. 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
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  • 13. Metal binding Asp-120 in metallo-beta-lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis.
    Garrity JD, Carenbauer AL, Herron LR, Crowder MW.
    J Biol Chem; 2004 Jan 09; 279(2):920-7. PubMed ID: 14573595
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  • 18. Antibiotic binding to dizinc beta-lactamase L1 from Stenotrophomonas maltophilia: SCC-DFTB/CHARMM and DFT studies.
    Xu D, Guo H, Cui Q.
    J Phys Chem A; 2007 Jul 05; 111(26):5630-6. PubMed ID: 17388313
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  • 20. Structural and biochemical analysis of the metallo-β-lactamase L1 from emerging pathogen Stenotrophomonas maltophilia revealed the subtle but distinct di-metal scaffold for catalytic activity.
    Kim Y, Maltseva N, Wilamowski M, Tesar C, Endres M, Joachimiak A.
    Protein Sci; 2020 Mar 05; 29(3):723-743. PubMed ID: 31846104
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