Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1–AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones
暂无分享,去创建一个
Michael E. Burczynski | Trevor M. Penning | Joseph M. Jez | Haiching Ma | N. Palackal | J. Jez | T. Penning | M. Burczynski | Chien-Fu Hung | Hseuh-Kung Lin | Haiching Ma | Margaret Moore | Nisha T. Palackal | Kapila Ratnam | C. Hung | K. Ratnam | Hseuh-Kung Lin | M. Moore | T. Penning
[1] N. Palackal,et al. Polycyclic Aromatic Hydrocarbon Trans-Dihydrodiol Specificity of four Recombinant Human Dihydrodiol Dehydrogenase Isoforms , 2000 .
[2] R. de Waal Malefyt,et al. Expression cloning and characterization of a human IL-10 receptor. , 1994, Journal of immunology.
[3] P. Soucy,et al. Characteristics of a Highly Labile Human Type 5 17β-Hydroxysteroid Dehydrogenase1. , 1999, Endocrinology.
[4] D. Peehl,et al. Expression and Characterization of Recombinant Type 2 3α-Hydroxysteroid Dehydrogenase (HSD) from Human Prostate: Demonstration of Bifunctional 3α/17β-HSD Activity and Cellular Distribution , 1997 .
[5] T. Flynn,et al. A new nomenclature for the aldo-keto reductase superfamily. , 1997, Biochemical pharmacology.
[6] M. Nakanishi,et al. Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. , 1994, The Biochemical journal.
[7] J. Sjövall,et al. Bile acid metabolism. , 1975, Annual review of biochemistry.
[8] Jean D. Wilson,et al. The Formation of 5α-Androstane-3α,17β-diol by Dog Prostate , 1976 .
[9] M. Majewska,et al. Neurosteroids: Endogenous bimodal modulators of the GABAA receptor mechanism of action and physiological significance , 1992, Progress in Neurobiology.
[10] Tomkins Gm. Enzymatic mechanisms of hormone metabolism. I. Oxidation-reduction of the steroid nucleus. , 1956 .
[11] G. N. Wilkinson. Statistical estimations in enzyme kinetics. , 1961, The Biochemical journal.
[12] J. A. Peters,et al. Neurosteroids and GABAA receptor function. , 1995, Trends in pharmacological sciences.
[13] H. Takikawa,et al. cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family. , 1993, The Journal of biological chemistry.
[14] H. Takikawa,et al. cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family. , 1993, The Journal of biological chemistry.
[15] M. J. Bennett,et al. Steroid recognition and regulation of hormone action: crystal structure of testosterone and NADP+ bound to 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase. , 1997, Structure.
[16] D. Russell,et al. Expression Cloning and Characterization of Oxidative 17β- and 3α-Hydroxysteroid Dehydrogenases from Rat and Human Prostate* , 1997, The Journal of Biological Chemistry.
[17] T. Penning,et al. Members of the nuclear factor 1 transcription factor family regulate rat 3alpha-hydroxysteroid/dihydrodiol dehydrogenase (3alpha-HSD/DD AKR1C9) gene expression: a member of the aldo-keto reductase superfamily. , 1999, Molecular endocrinology.
[18] F. Labrie,et al. Molecular Cloning of Human Type 3 3α-Hydroxysteroid Dehydrogenase That Differs from 20α-Hydroxysteroid Dehydrogenase by Seven Amino Acids , 1996 .
[19] S. Liao,et al. Steroid structure and androgenic activity. Specificities involved in the receptor binding and nuclear retention of various androgens. , 1973, The Journal of biological chemistry.
[20] J. A. Peters,et al. Neurosteroids and GABA, receptor function , 1995 .
[21] Ronald J. Moore,et al. Characterization of the 3α-hydroxysteroid dehydrogenase of dog prostate , 1977 .
[22] Y. Sasaguri,et al. Close kinship of human 20α‐hydroxysteroid dehydrogenase gene with three aldo‐keto reductase genes , 2000, Genes to cells : devoted to molecular & cellular mechanisms.
[23] A. Morrow,et al. Effects of progesterone or neuroactive steroid? , 1998, Nature.
[24] J. Wilson,et al. Partial characterization of the cytosol 3 alpha-hydroxysteroid: NAD(P)+oxidoreductase of rat ventral prostate. , 1975, Biochemistry.
[25] Fernand Labrie,et al. The key role of 17β-hydroxysteroid dehydrogenases in sex steroid biology , 1997, Steroids.
[26] D. Russell,et al. The parturition defect in steroid 5alpha-reductase type 1 knockout mice is due to impaired cervical ripening. , 1999, Molecular endocrinology.
[27] T. Smithgall,et al. Rat liver 3α-hydroxysteroid dehydrogenase , 1986, Steroids.
[28] M. Lewis,et al. Comparative anatomy of the aldo-keto reductase superfamily. , 1997, The Biochemical journal.
[29] K. Sato,et al. Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells. , 1996, The Biochemical journal.
[30] S. Mellon,et al. Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[31] K. Cheng,et al. Substrate Specificity, Gene Structure, and Tissue-specific Distribution of Multiple Human 3α-Hydroxysteroid Dehydrogenases (*) , 1995, The Journal of Biological Chemistry.
[32] M. J. Bennett,et al. Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+. , 1996, Biochemistry.
[33] J. Pawlowski,et al. Overexpression and mutagenesis of the cDNA for rat liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase. Role of cysteines and tyrosines in catalysis. , 1994, The Journal of biological chemistry.
[34] D. Russell,et al. 5 alpha-reduced androgens play a key role in murine parturition. , 1996, Molecular endocrinology.
[35] S. Paul,et al. Steroid hormone metabolites are barbiturate-like modulators of the GABA receptor. , 1986, Science.
[36] T. Penning,et al. Expression and characterization of four recombinant human dihydrodiol dehydrogenase isoforms: oxidation of trans-7, 8-dihydroxy-7,8-dihydrobenzo[a]pyrene to the activated o-quinone metabolite benzo[a]pyrene-7,8-dione. , 1998, Biochemistry.
[37] Haiching Ma,et al. Conversion of mammalian 3alpha-hydroxysteroid dehydrogenase to 20alpha-hydroxysteroid dehydrogenase using loop chimeras: changing specificity from androgens to progestins. , 1999, Proceedings of the National Academy of Sciences of the United States of America.