메뉴 건너뛰기




Volumn 94, Issue 1-3 SPEC. ISS., 2005, Pages 173-179

Cloning and characterization of human form 2 type 7 17β-hydroxysteroid dehydrogenase, a primarily 3β-keto reductase and estrogen activating and androgen inactivating enzyme

Author keywords

17 Hydroxysteroid dehydrogenase; Androgens; Cloning; Estrogens

Indexed keywords

17BETA HYDROXYSTEROID DEHYDROGENASE TYPE 7 FORM 2; 3BETA ANDROSTANEDIOL; ANDROSTANOLONE; COMPLEMENTARY DNA; ESTRADIOL; ESTRONE; ISOENZYME; TESTOSTERONE 17BETA DEHYDROGENASE; UNCLASSIFIED DRUG; VIRUS VECTOR;

EID: 18144386878     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2005.01.023     Document Type: Article
Times cited : (23)

References (14)
  • 1
    • 0035931115 scopus 로고    scopus 로고
    • A guide to 17beta-hydroxysteroid dehydrogenases
    • J. Adamski, and F.J. Jakob A guide to 17beta-hydroxysteroid dehydrogenases Mol. Cell Endocrinol. 171 2001 1 4
    • (2001) Mol. Cell Endocrinol. , vol.171 , pp. 1-4
    • Adamski, J.1    Jakob, F.J.2
  • 2
    • 0030013632 scopus 로고    scopus 로고
    • Cloning and characterization of an ovarian-specific protein that associates with the short form of the prolactin receptor
    • W.R. Duan, D.I. Linzer, and G. Gibori Cloning and characterization of an ovarian-specific protein that associates with the short form of the prolactin receptor J. Biol. Chem. 271 1996 15602 15607
    • (1996) J. Biol. Chem. , vol.271 , pp. 15602-15607
    • Duan, W.R.1    Linzer, D.I.2    Gibori, G.3
  • 3
    • 0001429526 scopus 로고    scopus 로고
    • Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase
    • I. Dufort, P. Rheault, X.F. Huang, P. Soucy, and V. Luu-The Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase Endocrinology 140 1999 568 574
    • (1999) Endocrinology , vol.140 , pp. 568-574
    • Dufort, I.1    Rheault, P.2    Huang, X.F.3    Soucy, P.4    Luu-The, V.5
  • 4
    • 0026667606 scopus 로고
    • High-resolution mapping of mammalian genes by in situ hybridization to free chromatin
    • H.H. Heng, J. Squire, and L.C. Tsui High-resolution mapping of mammalian genes by in situ hybridization to free chromatin Proc. Natl. Acad. Sci. U.S.A. 89 1992 9509 9513
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 9509-9513
    • Heng, H.H.1    Squire, J.2    Tsui, L.C.3
  • 5
    • 0032727093 scopus 로고    scopus 로고
    • Determination of cDNA, gene structure and chromosomal localization of the novel human 17beta-hydroxysteroid dehydrogenase type 7(1)
    • A. Krazeisen, R. Breitling, K. Imai, S. Fritz, G. Moller, and J. Adamski Determination of cDNA, gene structure and chromosomal localization of the novel human 17beta-hydroxysteroid dehydrogenase type 7(1) FEBS Lett. 460 1999 373 379
    • (1999) FEBS Lett. , vol.460 , pp. 373-379
    • Krazeisen, A.1    Breitling, R.2    Imai, K.3    Fritz, S.4    Moller, G.5    Adamski, J.6
  • 6
    • 0035931122 scopus 로고    scopus 로고
    • Expression and regulation of 17beta-hydroxysteroid dehydrogenase 7 in the rabbit
    • C.A. Krusche, G. Moller, H.M. Beier, and J. Adamski Expression and regulation of 17beta-hydroxysteroid dehydrogenase 7 in the rabbit Mol. Cell Endocrinol. 171 2001 169 177
    • (2001) Mol. Cell Endocrinol. , vol.171 , pp. 169-177
    • Krusche, C.A.1    Moller, G.2    Beier, H.M.3    Adamski, J.4
  • 7
    • 0034993363 scopus 로고    scopus 로고
    • Analysis and characteristics of multiple types of human 17beta-hydroxysteroid dehydrogenase
    • V. Luu-The Analysis and characteristics of multiple types of human 17beta-hydroxysteroid dehydrogenase J. Steroid Biochem. Mol. Biol. 76 2001 143 151
    • (2001) J. Steroid Biochem. Mol. Biol. , vol.76 , pp. 143-151
    • Luu-The, V.1
  • 9
    • 0029593494 scopus 로고
    • Characteristics of human types 1, 2 and 3 17 beta-hydroxysteroid dehydrogenase activities: Oxidation/reduction and inhibition
    • V. Luu-The, Y. Zhang, D. Poirier, and F. Labrie Characteristics of human types 1, 2 and 3 17 beta-hydroxysteroid dehydrogenase activities: oxidation/reduction and inhibition J. Steroid Biochem. Mol. Biol. 55 1995 581 587
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.55 , pp. 581-587
    • Luu-The, V.1    Zhang, Y.2    Poirier, D.3    Labrie, F.4
  • 10
    • 0041833725 scopus 로고    scopus 로고
    • Closing the gap: Identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis
    • Z. Marijanovic, D. Laubner, G. Moller, C. Gege, B. Husen, J. Adamski, and R. Breitling Closing the gap: identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis Mol. Endocrinol. 17 2003 1715 1725
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1715-1725
    • Marijanovic, Z.1    Laubner, D.2    Moller, G.3    Gege, C.4    Husen, B.5    Adamski, J.6    Breitling, R.7
  • 11
    • 0032230308 scopus 로고    scopus 로고
    • Expression cloning of a novel estrogenic mouse 17 beta-hydroxysteroid dehydrogenase/17-ketosteroid reductase (m17HSD7), previously described as a prolactin receptor-associated protein (PRAP) in rat
    • P. Nokelainen, H. Peltoketo, R. Vihko, and P. Vihko Expression cloning of a novel estrogenic mouse 17 beta-hydroxysteroid dehydrogenase/17-ketosteroid reductase (m17HSD7), previously described as a prolactin receptor-associated protein (PRAP) in rat Mol. Endocrinol. 12 1998 1048 1059
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1048-1059
    • Nokelainen, P.1    Peltoketo, H.2    Vihko, R.3    Vihko, P.4
  • 13
    • 0035931459 scopus 로고    scopus 로고
    • Expression of the estradiol-synthesizing 17beta-hydroxysteroid dehydrogenases type 1 and type 7 in the nonhuman primate Callithrix jacchus
    • I. Schwabe, B. Husen, and A. Einspanier Expression of the estradiol-synthesizing 17beta-hydroxysteroid dehydrogenases type 1 and type 7 in the nonhuman primate Callithrix jacchus Mol. Cell Endocrinol. 171 2001 187 192
    • (2001) Mol. Cell Endocrinol. , vol.171 , pp. 187-192
    • Schwabe, I.1    Husen, B.2    Einspanier, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.