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William T. Lowther, Ph.D.

William T. Lowther, Ph.D.

Associate Professor, Biochemistry
Comprehensive Cancer Center
Contact Information
Office:
336-716-7230
Email: tlowther@wakehealth.edu
Education & Training
  BSStetson University1989
  PhDUniversity of Florida1994
FellowshipMolecular BiologyUniversity of Florida College of Medicine2002
Memberships
American Chemical Society
American Crystallographic Association
American Society of Biochem & Molecular Biology
William T. Lowther, Ph.D.

William T. Lowther, Ph.D.

Associate Professor, Biochemistry
Comprehensive Cancer Center
Contact Information
Office:
336-716-7230
Email: tlowther@wakehealth.edu
Research Interests
biotechnology , cancer/oncogenesis , drugs/therapeutic agents pharm , instrument development , structural biology
Recent Publications
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. Protein engineering of the quaternary sulfiredoxin.peroxiredoxin enzyme.substrate complex reveals the molecular basis for cysteine sulfinic acid phosphorylation. J Biol Chem. 2009; 284(48):33305-10.


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


Murray MS, Holmes RP, Lowther WT. Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design. Biochemistry. 2008; 47(8):2439-2449.


Jonsson TJ, Tsang AW, Lowther WT, Furdui CM. Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin. J Biol Chem. 2008; 283(34):22890-94.


Jonsson TJ, Murray MS, Johnson LC, Lowther WT. Reduction of cysteine sulfinic acid in peroxiredoxin by sulfiredoxin proceeds directly through a sulfinic phosphoryl ester intermediate. J Biol Chem. 2008; 283(35):23846-51.


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.


Brot N, Collet J-F, Johnson LC, Jonsson TJ, Weissbach H, Lowther WT. The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases. J Biol Chem. 2006; 281(43):32668-75.
All Publications

For a listing of recent publications, refer to PubMed, a service provided by the National Library of Medicine.

For a list of earlier publications, visit the Carpenter Library Publication Search.

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Last Updated 1/4/2012
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