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Journal Abstract Search

190 related items for PubMed ID: 32146530

  • 21. Structure, Function of Serine and Metallo-β-lactamases and their Inhibitors.
    Salahuddin P, Kumar A, Khan AU.
    Curr Protein Pept Sci; 2018; 19(2):130-144. PubMed ID: 28745223
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  • 23. Crystallography and QM/MM Simulations Identify Preferential Binding of Hydrolyzed Carbapenem and Penem Antibiotics to the L1 Metallo-β-Lactamase in the Imine Form.
    Twidale RM, Hinchliffe P, Spencer J, Mulholland AJ.
    J Chem Inf Model; 2021 Dec 27; 61(12):5988-5999. PubMed ID: 34637298
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  • 27. 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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  • 30. The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site.
    Morán-Barrio J, González JM, Lisa MN, Costello AL, Peraro MD, Carloni P, Bennett B, Tierney DL, Limansky AS, Viale AM, Vila AJ.
    J Biol Chem; 2007 Jun 22; 282(25):18286-18293. PubMed ID: 17403673
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  • 31. 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
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  • 32. 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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  • 33. The Reaction Mechanism of Metallo-β-Lactamases Is Tuned by the Conformation of an Active-Site Mobile Loop.
    Palacios AR, Mojica MF, Giannini E, Taracila MA, Bethel CR, Alzari PM, Otero LH, Klinke S, Llarrull LI, Bonomo RA, Vila AJ.
    Antimicrob Agents Chemother; 2019 Jan 20; 63(1):. PubMed ID: 30348667
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  • 36. Substrate binding and catalytic mechanism of class B beta-lactamases: a molecular modelling study.
    Prosperi-Meys C, Wouters J, Galleni M, Lamotte-Brasseur J.
    Cell Mol Life Sci; 2001 Dec 20; 58(14):2136-43. PubMed ID: 11814063
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  • 37. Structural and Kinetic Studies of the Potent Inhibition of Metallo-β-lactamases by 6-Phosphonomethylpyridine-2-carboxylates.
    Hinchliffe P, Tanner CA, Krismanich AP, Labbé G, Goodfellow VJ, Marrone L, Desoky AY, Calvopiña K, Whittle EE, Zeng F, Avison MB, Bols NC, Siemann S, Spencer J, Dmitrienko GI.
    Biochemistry; 2018 Mar 27; 57(12):1880-1892. PubMed ID: 29485857
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  • 38. Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor.
    Concha NO, Janson CA, Rowling P, Pearson S, Cheever CA, Clarke BP, Lewis C, Galleni M, Frère JM, Payne DJ, Bateson JH, Abdel-Meguid SS.
    Biochemistry; 2000 Apr 18; 39(15):4288-98. PubMed ID: 10757977
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  • 39. Binding of β-lactam antibiotics to a bioinspired dizinc complex reminiscent of the active site of metallo-β-lactamases.
    Wöckel S, Galezowska J, Dechert S, Meyer F.
    Inorg Chem; 2012 Feb 20; 51(4):2486-93. PubMed ID: 22296309
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