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Journal Abstract Search


421 related items for PubMed ID: 26369960

  • 1. Elucidating the Role of Residue 67 in IMP-Type Metallo-β-Lactamase Evolution.
    LaCuran AE, Pegg KM, Liu EM, Bethel CR, Ai N, Welsh WJ, Bonomo RA, Oelschlaeger P.
    Antimicrob Agents Chemother; 2015 Dec; 59(12):7299-307. PubMed ID: 26369960
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  • 4. Impact of remote mutations on metallo-beta-lactamase substrate specificity: implications for the evolution of antibiotic resistance.
    Oelschlaeger P, Mayo SL, Pleiss J.
    Protein Sci; 2005 Mar; 14(3):765-74. PubMed ID: 15722450
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  • 10. Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site.
    Morán-Barrio J, Lisa MN, Larrieux N, Drusin SI, Viale AM, Moreno DM, Buschiazzo A, Vila AJ.
    Antimicrob Agents Chemother; 2016 Oct; 60(10):6013-22. PubMed ID: 27458232
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  • 11. E152A substitution drastically affects NDM-5 activity.
    Kumar G, Issa B, Kar D, Biswal S, Ghosh AS.
    FEMS Microbiol Lett; 2017 Feb 01; 364(3):. PubMed ID: 28087620
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  • 12. Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism.
    Zhang H, Hao Q.
    FASEB J; 2011 Aug 01; 25(8):2574-82. PubMed ID: 21507902
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  • 14. Role of Non-Active-Site Residue Trp-93 in the Function and Stability of New Delhi Metallo-β-Lactamase 1.
    Khan AU, Rehman MT.
    Antimicrob Agents Chemother; 2016 Jan 01; 60(1):356-60. PubMed ID: 26525789
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  • 18. Potency of IMP-10 metallo-beta-lactamase in hydrolysing various antipseudomonal beta-lactams.
    Zhao WH, Hu ZQ, Shimamura T.
    J Med Microbiol; 2008 Aug 01; 57(Pt 8):974-979. PubMed ID: 18628498
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  • 20. Modeling domino effects in enzymes: molecular basis of the substrate specificity of the bacterial metallo-beta-lactamases IMP-1 and IMP-6.
    Oelschlaeger P, Schmid RD, Pleiss J.
    Biochemistry; 2003 Aug 05; 42(30):8945-56. PubMed ID: 12885227
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