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Items: 6

1.

Elucidating the Role of Residue 67 in IMP-Type Metallo-β-Lactamase Evolution.

LaCuran AE, Pegg KM, Liu EM, Bethel CR, Ai N, Welsh WJ, Bonomo RA, Oelschlaeger P.

Antimicrob Agents Chemother. 2015 Dec;59(12):7299-307. doi: 10.1128/AAC.01651-15. Epub 2015 Sep 14.

2.

Uncovering Molecular Bases Underlying Bone Morphogenetic Protein Receptor Inhibitor Selectivity.

Alsamarah A, LaCuran AE, Oelschlaeger P, Hao J, Luo Y.

PLoS One. 2015 Jul 2;10(7):e0132221. doi: 10.1371/journal.pone.0132221. eCollection 2015.

3.

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.

Protein Sci. 2014 Oct;23(10):1451-60. doi: 10.1002/pro.2530. Epub 2014 Aug 20.

4.

Diaryl-substituted azolylthioacetamides: Inhibitor discovery of New Delhi metallo-β-lactamase-1 (NDM-1).

Zhang YL, Yang KW, Zhou YJ, LaCuran AE, Oelschlaeger P, Crowder MW.

ChemMedChem. 2014 Nov;9(11):2445-8. doi: 10.1002/cmdc.201402249. Epub 2014 Jul 22.

PMID:
25048031
5.

New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamases.

Yang KW, Feng L, Yang SK, Aitha M, LaCuran AE, Oelschlaeger P, Crowder MW.

Bioorg Med Chem Lett. 2013 Nov 1;23(21):5855-9. doi: 10.1016/j.bmcl.2013.08.098. Epub 2013 Sep 8.

6.

Biochemical characterization of IMP-30, a metallo-β-lactamase with enhanced activity toward ceftazidime.

Pegg KM, Liu EM, Lacuran AE, Oelschlaeger P.

Antimicrob Agents Chemother. 2013 Oct;57(10):5122-6. doi: 10.1128/AAC.02341-12. Epub 2013 Jul 8.

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