"Unusual metallo-β-lactamases may constitute a new subgroup in this family of enzymes"
written by Chun-Feng D. Hou, Emer K. Phelan, Manfredi Miraula, David L. Ollis, Gerhard Schenk, Nataša Mitić,
published by American Journal of Molecular Biology, Vol.4 No.1, 2014
has been cited by the following article(s):
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[4] Structure-activity relationship study and optimisation of 2-aminopyrrole-1-benzyl-4, 5-diphenyl-1H-pyrrole-3-carbonitrile as a broad spectrum metallo-β-lactamase …
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[5] Progress toward inhibitors of metallo-β-lactamases
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[6] Characterization of a highly efficient antibiotic-degrading metallo-β-lactamase obtained from an uncultured member of a permafrost community
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[7] Captopril analogues as metallo-β-lactamase inhibitors
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[8] Enhanced hydrogen production in microbial electrolysis cell with 3D self-assembly nickel foam-graphene cathode
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[9] Design, synthesis, and in vitro and biological evaluation of potent amino acid-derived thiol inhibitors of the metallo-β-lactamase IMP-1
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[10] The applications of binuclear metallohydrolases in medicine: Recent advances in the design and development of novel drug leads for purple acid phosphatases, metallo-β-lactamases and arginases
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[11] 3-Catalytic Mechanisms of Metallohydrolases Containing Two Metal Ions
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[12] Metallo-β-Lactamases: A Major Threat to Human Health
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[13] Metallo‐β‐lactamases and Their Biomimetic Complexes
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[14] Characterisation and directed evolution of novel metallo-β-lactamases-spr-1 and aim-1
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[15] The applications of binuclear metallohydrolases in medicine: recent advances in the design and development of novel drug leads for purple acid phosphatases …
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[16] Catalytic mechanisms of metallohydrolases containing two metal ions
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