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154 related items for PubMed ID: 17715946

  • 1.
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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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  • 3. 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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  • 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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  • 6. 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
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  • 8. 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
    [Abstract] [Full Text] [Related]

  • 9. Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia.
    Nauton L, Kahn R, Garau G, Hernandez JF, Dideberg O.
    J Mol Biol; 2008 Jan 04; 375(1):257-69. PubMed ID: 17999929
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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 04; 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
    [Abstract] [Full Text] [Related]

  • 14. A specific peptide inhibitor of the class B metallo-beta-lactamase L-1 from Stenotrophomonas maltophilia identified using phage display.
    Sanschagrin F, Levesque RC.
    J Antimicrob Chemother; 2005 Feb 09; 55(2):252-5. PubMed ID: 15659541
    [Abstract] [Full Text] [Related]

  • 15. Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli.
    Martí-Arbona R, Fresquet V, Thoden JB, Davis ML, Holden HM, Raushel FM.
    Biochemistry; 2005 May 17; 44(19):7115-24. PubMed ID: 15882050
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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
    [Abstract] [Full Text] [Related]


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