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Elucidating the Role of Residue 67 in IMP-Type Metallo-β-Lactamase Evolution.
Antimicrob Agents Chemother. 2015 Dec;59(12):7299-307. doi: 10.1128/AAC.01651-15. Epub 2015 Sep 14.
Antimicrob Agents Chemother. 2015.
PMID: 26369960
Free PMC article.
The sequence-activity relationship between metallo-β-lactamases IMP-1, IMP-6, and IMP-25 suggests an evolutionary adaptation to meropenem exposure.
Liu EM, Pegg KM, Oelschlaeger P.
Liu EM, et al. Among authors: pegg km.
Antimicrob Agents Chemother. 2012 Dec;56(12):6403-6. doi: 10.1128/AAC.01440-12. Epub 2012 Sep 24.
Antimicrob Agents Chemother. 2012.
PMID: 23006757
Free PMC article.
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Biochemical characterization of IMP-30, a metallo-β-lactamase with enhanced activity toward ceftazidime.
Pegg KM, Liu EM, Lacuran AE, Oelschlaeger P.
Pegg KM, et al.
Antimicrob Agents Chemother. 2013 Oct;57(10):5122-6. doi: 10.1128/AAC.02341-12. Epub 2013 Jul 8.
Antimicrob Agents Chemother. 2013.
PMID: 23836186
Free PMC article.
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Understanding the determinants of substrate specificity in IMP family metallo-β-lactamases: the importance of residue 262.
Pegg KM, Liu EM, George AC, LaCuran AE, Bethel CR, Bonomo RA, Oelschlaeger P.
Pegg KM, et al.
Protein Sci. 2014 Oct;23(10):1451-60. doi: 10.1002/pro.2530. Epub 2014 Aug 20.
Protein Sci. 2014.
PMID: 25131397
Free PMC article.
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