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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

James L. Thomas

Division of Basic Medical Sciences

Mercer University School of Medicine

1550 College St


United States


Name/email consistency: high



  • Division of Basic Medical Sciences, Mercer University School of Medicine, 1550 College St, Macon, United States. 2002 - 2010
  • Mercer University School of Medicine, Macon, GA 31207, USA. 2002


  1. The functions of key residues in the inhibitor, substrate and cofactor sites of human 3beta-hydroxysteroid dehydrogenase type 1 are validated by mutagenesis. Thomas, J.L., Mack, V.L., Sun, J., Terrell, J.R., Bucholtz, K.M. J. Steroid Biochem. Mol. Biol. (2010) [Pubmed]
  2. Structure/function of human type 1 3beta-hydroxysteroid dehydrogenase: An intrasubunit disulfide bond in the Rossmann-fold domain and a Cys residue in the active site are critical for substrate and coenzyme utilization. Thomas, J.L., Huether, R., Mack, V.L., Scaccia, L.A., Stoner, R.C., Duax, W.L. J. Steroid Biochem. Mol. Biol. (2007) [Pubmed]
  3. Identification of key amino acids responsible for the substantially higher affinities of human type 1 3beta-hydroxysteroid dehydrogenase/isomerase (3beta-HSD1) for substrates, coenzymes, and inhibitors relative to human 3beta-HSD2. Thomas, J.L., Boswell, E.L., Scaccia, L.A., Pletnev, V., Umland, T.C. J. Biol. Chem. (2005) [Pubmed]
  4. Serine 124 completes the Tyr, Lys and Ser triad responsible for the catalysis of human type 1 3beta-hydroxysteroid dehydrogenase. Thomas, J.L., Duax, W.L., Addlagatta, A., Scaccia, L.A., Frizzell, K.A., Carloni, S.B. J. Mol. Endocrinol. (2004) [Pubmed]
  5. Structure/function relationships responsible for coenzyme specificity and the isomerase activity of human type 1 3 beta-hydroxysteroid dehydrogenase/isomerase. Thomas, J.L., Duax, W.L., Addlagatta, A., Brandt, S., Fuller, R.R., Norris, W. J. Biol. Chem. (2003) [Pubmed]
  6. Structure/function relationships responsible for the kinetic differences between human type 1 and type 2 3beta-hydroxysteroid dehydrogenase and for the catalysis of the type 1 activity. Thomas, J.L., Mason, J.I., Brandt, S., Spencer, B.R., Norris, W. J. Biol. Chem. (2002) [Pubmed]
  7. Differences in substrate and inhibitor kinetics of human type 1 and type 2 3beta-hydroxysteroid dehydrogenase are explained by the type 1 mutant, H156Y. Thomas, J.L., Mason, J.I., Brandt, S., Norris, W. Endocr. Res. (2002) [Pubmed]
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