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Crystal Structures of Substrate and Inhibitor Complexes with AmpC β-Lactamase: Possible Implications for Substrate-Assisted Catalysis
Group I β-lactamases are major resistance determinants to β-lactam antibiotics. Despite intense study, the identity of the catalytic base, the direction of hydrolytic attack, and the functionalExpand
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Functional analyses of AmpC β‐lactamase through differential stability
Despite decades of intense study, the complementarity of β‐lactams for β‐lactamases and penicillin binding proteins is poorly understood. For most of these enzymes, β‐lactam binding involves rapidExpand
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Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Putidaredoxin (Pdx) is a 106-residue Fe2S2 ferredoxin which acts as the physiological reductant and effector of cytochrome P-450cam. Pdx has two accessible oxidation states, Fe+3-Fe+3 (oxidized) andExpand
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Functional analyses of AmpC beta-lactamase through differential stability.
Despite decades of intense study, the complementarity of beta-lactams for beta-lactamases and penicillin binding proteins is poorly understood. For most of these enzymes, beta-lactam binding involvesExpand
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Solution structure and dynamics of a serpin reactive site loop using interleukin 1β as a presentation scaffold
Human interleukin-1b (IL1b) was used as a presentation scaffold for the characterization of the reactive site loop (RSL) of the serpin a1-antitrypsin (A1AT), the physiological inhibitor of leukocyteExpand
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Carnitine in Relation to Feeding Infants
The importance of carnitine in facilitating long chain fatty acid oxidation and the importance of long chain fatty acid oxidation in energy metabolism of the infant are both well documented (1).Expand
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Solution structure and dynamics of a serpin reactive site loop using interleukin 1beta as a presentation scaffold.
Human interleukin-1beta (IL1beta) was used as a presentation scaffold for the characterization of the reactive site loop (RSL) of the serpin alpha1-antitrypsin (A1AT), the physiological inhibitor ofExpand
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