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Kinetic Studies on CphA Mutants Reveal the Role of the P158-P172 Loop in Activity versus Carbapenems.
Antimicrob Agents Chemother. 2016 Apr 22;60(5):3123-6. doi: 10.1128/AAC.01703-15. Print 2016 May.
3
Dramatic broadening of the substrate profile of the Aeromonas hydrophila CphA metallo-beta-lactamase by site-directed mutagenesis.
J Biol Chem. 2005 Aug 5;280(31):28195-202. doi: 10.1074/jbc.M414052200. Epub 2005 Apr 30.
5
The structure of the dizinc subclass B2 metallo-beta-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site.
Antimicrob Agents Chemother. 2009 Oct;53(10):4464-71. doi: 10.1128/AAC.00288-09. Epub 2009 Aug 3.
7
Common mechanistic features among metallo-beta-lactamases: a computational study of Aeromonas hydrophila CphA enzyme.
J Biol Chem. 2009 Oct 9;284(41):28164-28171. doi: 10.1074/jbc.M109.049502. Epub 2009 Aug 11.
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Probing the specificity of the subclass B3 FEZ-1 metallo-beta-lactamase by site-directed mutagenesis.
J Biol Chem. 2004 Aug 6;279(32):33630-8. doi: 10.1074/jbc.M403671200. Epub 2004 May 24.
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Expanded Substrate Activity of OXA-24/40 in Carbapenem-Resistant Acinetobacter baumannii Involves Enhanced Binding Loop Flexibility.
Biochemistry. 2016 Nov 29;55(47):6535-6544. doi: 10.1021/acs.biochem.6b00806. Epub 2016 Nov 11.
10
Monitoring the zinc affinity of the metallo-beta-lactamase CphA by automated nanoESI-MS.
J Am Soc Mass Spectrom. 2006 Feb;17(2):180-8. doi: 10.1016/j.jasms.2005.10.007. Epub 2006 Jan 10.

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Enzyme graphene oxide interaction: the case system of β-lactamases.
RSC Adv. 2025 Jun 23;15(26):21199-21211. doi: 10.1039/d5ra01697e. eCollection 2025 Jun 16.
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Mutations in cause hyperproduction of AmpC and CmcB β-lactamases and high resistance to β-lactam antibiotics in .
Microbiol Spectr. 2025 Aug 5;13(8):e0091625. doi: 10.1128/spectrum.00916-25. Epub 2025 Jun 12.
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Camel-Derived Nanobodies as Potent Inhibitors of New Delhi Metallo-β-Lactamase-1 Enzyme.
Molecules. 2024 Mar 22;29(7):1431. doi: 10.3390/molecules29071431.
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Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.
Chem Rev. 2021 Jul 14;121(13):7957-8094. doi: 10.1021/acs.chemrev.1c00138. Epub 2021 Jun 15.
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Shaping Substrate Selectivity in a Broad-Spectrum Metallo-β-Lactamase.
Antimicrob Agents Chemother. 2018 Mar 27;62(4). doi: 10.1128/AAC.02079-17. Print 2018 Apr.

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Biochemical characterization of Sfh-I, a subclass B2 metallo-beta-lactamase from Serratia fonticola UTAD54.
Antimicrob Agents Chemother. 2011 Nov;55(11):5392-5. doi: 10.1128/AAC.00429-11. Epub 2011 Aug 29.
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Crystal structure of Serratia fonticola Sfh-I: activation of the nucleophile in mono-zinc metallo-β-lactamases.
J Mol Biol. 2011 Sep 2;411(5):951-9. doi: 10.1016/j.jmb.2011.06.043. Epub 2011 Jul 6.
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The structure of the dizinc subclass B2 metallo-beta-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site.
Antimicrob Agents Chemother. 2009 Oct;53(10):4464-71. doi: 10.1128/AAC.00288-09. Epub 2009 Aug 3.
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Update of the standard numbering scheme for class B beta-lactamases.
Antimicrob Agents Chemother. 2004 Jul;48(7):2347-9. doi: 10.1128/AAC.48.7.2347-2349.2004.
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Zn(II) dependence of the Aeromonas hydrophila AE036 metallo-beta-lactamase activity and stability.
Biochemistry. 1997 Sep 23;36(38):11534-41. doi: 10.1021/bi971056h.
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The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold.
EMBO J. 1995 Oct 16;14(20):4914-21. doi: 10.1002/j.1460-2075.1995.tb00174.x.

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