L. A. Scaccia

Agonist-induced endocytosis of lysophosphatidic acid-coupled LPA1/EDG-2 receptors via a dynamin2- and Rab5-dependent pathway

Mandi M. Murph, H. Radhakrishna, L. Volpicelli, 2003, Journal of Cell Science.

Identification of Key Amino Acids Responsible for the Substantially Higher Affinities of Human Type 1 3β-Hydroxysteroid Dehydrogenase/Isomerase (3β-HSD1) for Substrates, Coenzymes, and Inhibitors Relative to Human 3β-HSD2*

V. Pletnev, T. Umland, James L. Thomas, 2005, Journal of Biological Chemistry.

Structure/function of human type 1 3β-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

R. Huether, W. Duax, James L. Thomas, 2007, The Journal of Steroid Biochemistry and Molecular Biology.

Serine 124 completes the Tyr, Lys and Ser triad responsible for the catalysis of human type 1 3beta-hydroxysteroid dehydrogenase.

W. Duax, A. Addlagatta, S. Carloni, 2004, Journal of molecular endocrinology.

The Higher Affinity of Human Type 1 3β‐Hydroxysteroid Dehydrogenase (3β‐HSD1) for Substrate and Inhibitor Steroids Relative to Human 3β‐HSD2 is Validated in MCF‐7 Tumor Cells and Related to Subunit Interactions

T. Umland, B. Kacsoh, James L. Thomas, 2004, Endocrine research.

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.

V. Pletnev, T. Umland, James L. Thomas, 2005, Journal of Biological Chemistry.