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Journal Abstract Search

855 related items for PubMed ID: 10757977

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  • 23. New Delhi metallo-β-lactamase: structural insights into β-lactam recognition and inhibition.
    King DT, Worrall LJ, Gruninger R, Strynadka NC.
    J Am Chem Soc; 2012 Jul 18; 134(28):11362-5. PubMed ID: 22713171
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  • 25. Crystal structure of the mobile metallo-β-lactamase AIM-1 from Pseudomonas aeruginosa: insights into antibiotic binding and the role of Gln157.
    Leiros HK, Borra PS, Brandsdal BO, Edvardsen KS, Spencer J, Walsh TR, Samuelsen O.
    Antimicrob Agents Chemother; 2012 Aug 18; 56(8):4341-53. PubMed ID: 22664968
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  • 27. X-ray crystallographic analysis of IMP-1 metallo-β-lactamase complexed with a 3-aminophthalic acid derivative, structure-based drug design, and synthesis of 3,6-disubstituted phthalic acid derivative inhibitors.
    Hiraiwa Y, Saito J, Watanabe T, Yamada M, Morinaka A, Fukushima T, Kudo T.
    Bioorg Med Chem Lett; 2014 Oct 15; 24(20):4891-4. PubMed ID: 25246278
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  • 30. Mutagenesis of zinc ligand residue Cys221 reveals plasticity in the IMP-1 metallo-β-lactamase active site.
    Horton LB, Shanker S, Mikulski R, Brown NG, Phillips KJ, Lykissa E, Venkataram Prasad BV, Palzkill T.
    Antimicrob Agents Chemother; 2012 Nov 15; 56(11):5667-77. PubMed ID: 22908171
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  • 34. Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis.
    Concha NO, Rasmussen BA, Bush K, Herzberg O.
    Structure; 1996 Jul 15; 4(7):823-36. PubMed ID: 8805566
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  • 36. Synthesis and kinetic testing of new inhibitors for a metallo-β-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa.
    Mohamed MS, Hussein WM, McGeary RP, Vella P, Schenk G, Abd El-Hameed RH.
    Eur J Med Chem; 2011 Dec 15; 46(12):6075-82. PubMed ID: 22051063
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  • 37. 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 15; 8(1):249-52. PubMed ID: 10210203
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  • 38. Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic studies, and X-ray crystallography.
    Yamaguchi Y, Kuroki T, Yasuzawa H, Higashi T, Jin W, Kawanami A, Yamagata Y, Arakawa Y, Goto M, Kurosaki H.
    J Biol Chem; 2005 May 27; 280(21):20824-32. PubMed ID: 15788415
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  • 40. 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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