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Molecular and Cellular Biosciences at Wake Forest University

Wake Forest University Graduate School » Molecular and Cellular Biosciences

William Todd Lowther, Ph.D.

William Todd Lowther, Ph.D.
Associate Professor, Biochemistry
Education & Training
  BS Stetson University 1989
  PhD University of Florida 1994
Molecular Biology University of Florida College of Medicine 2002
American Chemical Society
American Crystallographic Association
American Society of Biochem & Molecular Biology


Chen H, Gu Z, Zhang H, Wang M, Chen W, Lowther WT, Chen YQ. Expression and purification of integral membrane fatty acid desaturases. PLoS One. 2013;8(3):e58139.


Jiang J, Johnson LC, Knight J, Callahan MF, Riedel TJ, Holmes RP, Lowther WT.Metabolism of [13C5]hydroxyproline in vitro and in vivo: implications for primary hyperoxaluria. Am J Physiol Gastrointest Liver Physiol. 2012;302(6):G637-G643.


Lema Tome CM, Palma E, Ferlaga S, Lowther WT, Hantgan R, Wykosky J, Debinski W. Structural and functional characterization of monomeric EphrinA1 binding site to EphA2 receptor. J Biol Chem. 2012;287(17):14012-22.


Riedel TJ, Knight J, Murray MS, Milliner DS, Holmes RP, Lowther WT. 4-Hydroxy-2-oxoglutarate aldolase inactivity in primary hyperoxaluria type 3 and glyoxylate reductase inhibition. Biochim Biophys Acta. 2012;1822(10):1544-1552.


Lowther WT, Haynes AC. Reduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin. Antioxid Redox Signal. 2011;15(1):99-109.


Riedel TJ, Johnson LC, Knight J, Hantgan RR, Holmes RP, Lowther WT. Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria. PLoS ONE. 2011;6(10):e26021.


Klomsiri C, Nelson KJ, Bechtold E, Soito L, Johnson LC, Lowther WT, Ryu S-E, King SB, Furdui CM, Poole LB. Use of dimedone-based chemical probes for sulfenic acid detection evaluation of conditions affecting probe incorporation into redox-sensitive proteins. Methods Enzymol. 2010;473():77-94.


Cox AG, Pearson AG, Pullar JM, Jonsson TJ, Lowther WT, Winterbourn CC, Hampton MB. Mitochondrial peroxiredoxin 3 is more resilient to hyperoxidation than cytoplasmic peroxiredoxins. Biochem J. 2009;421(1):51-58.



Jonsson TJ, Johnson LC, Lowther WT. Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace. Nature. 2008;451(7174):98-101.





Brunell DJ, Lowther T, Sagher D, Brot N, Weissbach H. A disulfide intermediate is required for the reduction of methionine sulfoxide reductase by thioredoxin [abstract]. FASEB J. 2007;21(5):A275.


Lin Z, Johnson LC, Weissbach H, Brot N, Lively MO, Lowther WT. Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function. Proc Natl Acad Sci U S A. 2007;104(23):9597-9602.


Pemble CW IV, Johnson LC, Kridel SJ, Lowther WT. Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat. Nat Struct Mol Biol. 2007;14(8):704-709.


Kridel SJ, Lowther WT, Pemble CW IV. Fatty acid synthase inhibitors: new directions for oncology. Expert Opin Investig Drugs. 2007;16(11):1817-1829.


Jonsson TJ, Lowther WT. The peroxiredoxin repair proteins. Subcell Biochem. 2007;44():115-141.


Jonsson TJ, Johnson LC, Lowther WT. Structure of the sulfiredoxin-peroxiredoxin complex reveals basis for cysteine sulfinic acid repair [abstract]. Free Radic Biol Med. 2007;43(Suppl 1):S110.


The overall focus of several ongoing projects in my laboratory is to understand the molecular basis for enzyme catalysis and substrate/inhibitor/ligand specificity.  In these endeavors we utilize a variety of molecular biology, biochemical and X-ray crystallographic methods. Current projects in the lab include: (1) an analysis of the molecular basis for the repair or retro-reduction of hyperoxidized peroxiredoxins by an enzyme called surfiredoxin, (2) the characterization of enzymes involved in glyoxylate metabolism and kidney stone formation, (3) the study of the thioesterase domain of human fatty acid synthase and its inhibition by the anti-cancer compound Orlistat, and (4) the study of methionine sulfoxide reductases.