|Graduate School||University of Michigan-Ann Arbor (2000)|
- Identification of the physiological functions of paraoxonases (PONs), a family of calcium dependent esterases. Investigation of PONs’ protective functions as they relate to atherosclerosis, bacterial pathogenesis and organophosphate toxicity.
- Paraoxonase 2 is down-regulated by the Pseudomonas aeruginosa quorumsensing signal N-(3-oxododecanoyl)-L-homoserine lactone and attenuates oxidative stress induced by pyocyanin.
- Horke S, Witte I, Altenhöfer S, Wilgenbus P, Goldeck M, Förstermann U, Xiao J, Kramer GL, Haines DC, Chowdhary PK, Haley RW, Teiber JF Biochem. J. 2010 Feb 426 1 73-83
- Dominant Role of Paraoxonases in Inactivation of the Pseudomonas aeruginosa Quorum-Sensing Signal N-(3-Oxododecanoyl)-L-Homoserine Lactone
- John F. Teiber, Sven Horke, Donovan C. Haines, Puneet K. Chowdhary, Junhui Xiao, Gerald L. Kramer, Robert W. Haley, and Dragomir I. Draganov Infection and Immunity June 2008 76 2512-2519
- Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities.
- Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN. J. Lipid Res. June 2005 46 1239-1247
- Purified human serum PON1 does not protect LDL against oxidation in the in vitro assays initiated with copper or AAPH.
- Teiber JF, Draganov DI, La Du BN. J. Lipid Res. December 2004 45 2260-2268