James L. Thomas

发表

Inner Mitochondrial Translocase Tim50 Interacts with 3β-Hydroxysteroid Dehydrogenase Type 2 to Regulate Adrenal and Gonadal Steroidogenesis*

H. Bose, R. Whittal, M. Prasad, 2011, The Journal of Biological Chemistry.

The functions of key residues in the inhibitor, substrate and cofactor sites of human 3β-hydroxysteroid dehydrogenase type 1 are validated by mutagenesis

James L. Thomas, Vance L. Mack, Jingping Sun, 2010, The Journal of Steroid Biochemistry and Molecular Biology.

Endoplasmic Reticulum Stress Enhances Mitochondrial Metabolic Activity in Mammalian Adrenals and Gonads

A. Pandey, H. Bose, R. Whittal, 2016, Molecular and Cellular Biology.

Regulation of Human 3β-Hydroxysteroid Dehydrogenase Type 2 by Adrenal Corticosteroids and Product-Feedback by Androstenedione in Human Adrenarche

H. Bose, J. Majzoub, M. Rajapaksha, 2015, The Journal of Pharmacology and Experimental Therapeutics.

Analysis of coenzyme binding by human placental 3β-hydroxy-5-ene-steroid dehydrogenase and steroid 5→4-ene-isomerase using 5′-[p-(fluorosulfonyl)benzoyl]adenosine, an affinity labeling cofactor analog

R. Strickler, James L. Thomas, R. Myers, 1991, The Journal of Steroid Biochemistry and Molecular Biology.

The affinity alkylators, 11α-bromoacetoxyprogesterone and estrone 3-bromoacetate, modify a common histidyl residue in the active site of human placental 17β,20α-hydroxysteroid dehydrogenase

R. Strickler, E. Asibey-Berko, James L. Thomas, 1986 .

Lipid-mediated unfolding of 3β-hydroxysteroid dehydrogenase 2 is essential for steroidogenic activity.

J. D. Bell, H. Bose, R. Whittal, 2011, Biochemistry.

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.

Structural basis for the selective inhibition of human 3β-hydroxysteroid dehydrogenase 1 in human breast tumor MCF-7 cells

B. Kacsoh, James L. Thomas, Vance L. Mack, 2009, Molecular and Cellular Endocrinology.

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.

Structure/function aspects of human 3β-hydroxysteroid dehydrogenase

W. Duax, B. Kacsoh, A. Addlagatta, 2004, Molecular and Cellular Endocrinology.

3β-Hydroxysteroid dehydrogenase in human placental microsomes and mitochondria: Co-solubilization of androstene and pregnene activities

R. Strickler, E. Asibey-Berko, James L. Thomas, 1986, Steroids.

Reactivation of human placental 17β, 20α-hydroxysteroid dehydrogenase: Affirmation of affinity labeling principles

R. Strickler, James L. Thomas, M. C. LaRochelle, 1984, Steroids.

Site-directed mutagenesis identifies amino acid residues associated with the dehydrogenase and isomerase activities of human type I (placental) 3β-hydroxysteroid dehydrogenase/Isomerase 1 Supported by NIH Grant HD20055 (JLT). 1

W. Nash, K. Isenberg, R. Strickler, 1998, The Journal of Steroid Biochemistry and Molecular Biology.

3β-hydroxysteroid dehydrogenase activity in tissues of the human fetus determined with 5α-androstane-3β,17β-diol and dehydroepiandrosterone as substrates

J. Mason, B. Carr, C. Blomquist, 1993, The Journal of Steroid Biochemistry and Molecular Biology.

Full Length cDNA Structure and Deduced Amino Acid Sequence of Human β-Hydroxy-5-Ene Steroid Dehydrogenase

Y. Lachance, C. Labrie, R. Strickler, 1989 .

A modified digitonin-precipitation radioassay for 3β-hydroxy-Δ5-steroid dehydrogenase☆

James L. Thomas, Ebenezer A. Berko, Ronald C. Strickler, 1987 .

Structure/Function Relationships Responsible for the Kinetic Differences between Human Type 1 and Type 2 3β-Hydroxysteroid Dehydrogenase and for the Catalysis of the Type 1 Activity*

J. Mason, James L. Thomas, Stacey Brandt, 2002, The Journal of Biological Chemistry.

Over-expression of human type I (placental) 3β-hydroxy-5-ene-steroid dehydrogenase/isomerase in insect cells infected with recombinant baculovirus

W. Nash, R. Strickler, J. Mason, 1994, The Journal of Steroid Biochemistry and Molecular Biology.

STRUCTURE/FUNCTION RELATIONSHIPS FOR A NOVEL INHIBITOR OF HUMAN 3β- HYDROXYSTEROID DEHYDROGENASE 1 by JENNY

H. Pham, James L. Thomas, 2017 .

Structure/function of the inhibition of human 3β-hydroxysteroid dehydrogenase type 1 and type 2 by trilostane

James L. Thomas, Vance L. Mack, J. Terrell, 2008, The Journal of Steroid Biochemistry and Molecular Biology.

Costs and Consequences of Cellular Compartmentalization and Substrate Competition among Human Enzymes Involved in Androgen and Estrogen Synthesis

N. Gee, B. Lasley, C. Corbin, 2012, Biology of reproduction.

Selective inhibition of human 3β-hydroxysteroid dehydrogenase type 1 as a potential treatment for breast cancer

B. Kacsoh, James L. Thomas, Kevin M. Bucholtz, 2011, The Journal of Steroid Biochemistry and Molecular Biology.

Regulation of human 3-beta-hydroxysteroid dehydrogenase type-2 (3βHSD2) by molecular chaperones and the mitochondrial environment affects steroidogenesis

H. Bose, James L. Thomas, 2015, The Journal of Steroid Biochemistry and Molecular Biology.

Structure-function relationships for the selective inhibition of human 3β-hydroxysteroid dehydrogenase type 1 by a novel androgen analog

James L. Thomas, Vance L. Mack, Kevin M. Bucholtz, 2017, The Journal of Steroid Biochemistry and Molecular Biology.

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.

Structure/Function Relationships Responsible for Coenzyme Specificity and the Isomerase Activity of Human Type 1 3β-Hydroxysteroid Dehydrogenase/Isomerase*

W. Duax, R. R. Fuller, William L Duax, 2003, Journal of Biological Chemistry.

DIFFERENCES IN SUBSTRATE AND INHIBITOR KINETICS OF HUMAN TYPE 1 AND TYPE 2 3β-HYDROXYSTEROID DEHYDROGENASE ARE EXPLAINED BY THE TYPE 1 MUTANT, H156Y

J. Mason, James L. Thomas, Stacey Brandt, 2002, Endocrine research.

Affinity Labeling in the Presence of the Reduced Diphosphopyridine Nucleotide NADH Identifies Peptides Associated With the Activities of Human Placental 3β-Hydroxy-Δ5- Steroid Dehydrogenase/Isomerase

W. Nash, R. Strickler, M. Crankshaw, 1994, The Journal of the Society for Gynecologic Investigation: JSGI.

Chaperones rejuvenate folding and activity of 3-β hydroxysteroid dehydrogenase 2.

H. Bose, R. Whittal, M. Prasad, 2013, ACS chemical biology.

Mitochondrial 3β-Hydroxysteroid Dehydrogenase Enzyme Activity Requires Reversible pH-dependent Conformational Change at the Intermembrane Space*

H. Bose, R. Whittal, M. Prasad, 2012, The Journal of Biological Chemistry.

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.

Human placental 3 beta-hydroxy-5-ene-steroid dehydrogenase and steroid 5----4-ene-isomerase: purification from mitochondria and kinetic profiles, biophysical characterization of the purified mitochondrial and microsomal enzymes.

R. P. Myers, R. Strickler, J. Thomas, 1989, Journal of steroid biochemistry.

Regulation of Human 3β-Hydroxysteroid Dehydrogenase Type 2 by Adrenal Corticosteroids and Product-Feedback by Androstenedione in Human Adrenarche

H. Bose, J. Majzoub, M. Rajapaksha, 2015, The Journal of Pharmacology and Experimental Therapeutics.

Creation of a fully active, cytosolic form of human type I 3beta-hydroxysteroid dehydrogenase/isomerase by the deletion of a membrane-spanning domain.

James L. Thomas, B. W. Evans, G. Blanco, 1999, Journal of molecular endocrinology.

Structure-function relationships for the selective inhibition of human 3β-hydroxysteroid dehydrogenase type 1 by a novel androgen analog

James L. Thomas, Vance L. Mack, Kevin M. Bucholtz, 2017, The Journal of Steroid Biochemistry and Molecular Biology.

Physiological 3β-hydroxy-5-ene steroid substrates bind to 3β-hydroxysteroid dehydrogenase without the prior binding of cofactor

W. Nash, R. Strickler, James L. Thomas, 1996, The Journal of Steroid Biochemistry and Molecular Biology.