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Volumn 125, Issue 1-2, 2011, Pages 83-94

Contribution to the development of inhibitors of 17β-hydroxysteroid dehydrogenase types 1 and 7: Key tools for studying and treating estrogen-dependent diseases

Author keywords

17 HSD; Cancer; Enzyme; Estrogen; Hydroxysteroid dehydrogenase; Inhibitor; Steroid

Indexed keywords

17BETA (N,N DIETHYLCARBAMOYL) 4 METHYL 4 AZA 5ALPHA ANDROSTAN 3 ONE; AROMATASE INHIBITOR; PRASTERONE; TESTOSTERONE 17BETA DEHYDROGENASE;

EID: 79957737745     PISSN: 09600760     EISSN: 18791220     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2010.12.007     Document Type: Review
Times cited : (37)

References (95)
  • 1
    • 10644266103 scopus 로고    scopus 로고
    • Overview of steroidogenic enzymes in the pathway from cholesterol to active steroid hormones
    • DOI 10.1210/er.2003-0030
    • A.H. Payne, and D.B. Hales Overview of steroidogenic enzymes in the pathway from cholesterol to active steroid hormones Endocr. Rev. 25 2004 947 970 (Pubitemid 39657774)
    • (2004) Endocrine Reviews , vol.25 , Issue.6 , pp. 947-970
    • Payne, A.H.1    Hales, D.B.2
  • 2
    • 0030925341 scopus 로고    scopus 로고
    • Molecular endocrinology of hydroxysteroid dehydrogenases
    • DOI 10.1210/er.18.3.281
    • T.M. Penning Molecular endocrinology of hydroxysteroid dehydrogenases Endocr. Rev. 18 1997 281 305 (Pubitemid 27246879)
    • (1997) Endocrine Reviews , vol.18 , Issue.3 , pp. 281-305
    • Penning, T.M.1
  • 3
    • 0025741147 scopus 로고
    • Mechanism based inhibition of hydroxysteroid dehydrogenases
    • T.M. Penning, and J.W. Ricigliano Mechanism based inhibition of hydroxysteroid dehydrogenases J. Enzyme Inhib. 5 1991 165 198
    • (1991) J. Enzyme Inhib. , vol.5 , pp. 165-198
    • Penning, T.M.1    Ricigliano, J.W.2
  • 4
    • 0033673885 scopus 로고    scopus 로고
    • Role of 17β-hydroxysteroid dehydrogenases in sex steroid formation in peripheral intracrine tissues
    • F. Labrie, V. Luu-The, S.X. Lin, J. Simard, and C. Labrie Role of 17β-hydroxysteroid dehydrogenases in sex steroid formation in peripheral intracrine tissues Trends Endocr. Metab. 11 2000 421 427
    • (2000) Trends Endocr. Metab. , vol.11 , pp. 421-427
    • Labrie, F.1    Luu-The, V.2    Lin, S.X.3    Simard, J.4    Labrie, C.5
  • 5
    • 0031023049 scopus 로고    scopus 로고
    • The key role of 17β-hydroxysteroid dehydrogenases in sex steroid biology
    • DOI 10.1016/S0039-128X(96)00174-2, PII S0039128X96001747
    • F. Labrie, V. Luu-The, S.X. Lin, C. Labrie, J. Simard, R. Breton, and A. Bélanger The key role of 17β-hydroxysteroid dehydrogenases in sex steroid biology Steroids 62 1997 148 158 (Pubitemid 27066999)
    • (1997) Steroids , vol.62 , Issue.1 , pp. 148-158
    • Labrie, F.1    Luu-The, V.2    Lin, S.-X.3    Labrie, C.4    Simard, J.5    Breton, R.6    Belanger, A.7
  • 6
    • 77955507711 scopus 로고    scopus 로고
    • The intracrine sex steroid biosynthesis pathways
    • V. Luu-The, and F. Labrie The intracrine sex steroid biosynthesis pathways L. Martini, Progress in Brain Research vol. 181 2010 Elsevier 177 192 (Chapter 10)
    • (2010) Progress in Brain Research , vol.181 , pp. 177-192
    • Luu-The, V.1    Labrie, F.2
  • 7
    • 60249089957 scopus 로고    scopus 로고
    • Integrated view on 17beta-hydroxysteroid dehydrogenases
    • G. Moeller, and J. Adamski Integrated view on 17beta-hydroxysteroid dehydrogenases Mol. Cell. Endocrinol. 301 2009 7 19
    • (2009) Mol. Cell. Endocrinol. , vol.301 , pp. 7-19
    • Moeller, G.1    Adamski, J.2
  • 8
    • 33644894458 scopus 로고    scopus 로고
    • Multifunctionality of human 17β-hydroxysteroid dehydrogenases
    • G. Moeller, and J. Adamski Multifunctionality of human 17β-hydroxysteroid dehydrogenases Mol. Cell. Endocrinol. 248 2006 47 55
    • (2006) Mol. Cell. Endocrinol. , vol.248 , pp. 47-55
    • Moeller, G.1    Adamski, J.2
  • 9
    • 33644989471 scopus 로고    scopus 로고
    • Structure and function of human 17β-hydroxysteroid dehydrogenases
    • P. Lukacik, K.L. Kavanagh, and U. Oppermann Structure and function of human 17β-hydroxysteroid dehydrogenases Mol. Cell. Endocrinol. 248 2006 61 71
    • (2006) Mol. Cell. Endocrinol. , vol.248 , pp. 61-71
    • Lukacik, P.1    Kavanagh, K.L.2    Oppermann, U.3
  • 10
    • 0034993363 scopus 로고    scopus 로고
    • Analysis and characteristics of multiple types of human 17β-hydroxysteroid dehydrogenase
    • DOI 10.1016/S0960-0760(00)00155-2, PII S0960076000001552
    • V. Luu-The Analysis and characteristics of multiple types of human 17β-hydroxysteroid dehydrogenase J. Steroid Biochem. Mol. Biol. 76 2001 143 151 (Pubitemid 32510676)
    • (2001) Journal of Steroid Biochemistry and Molecular Biology , vol.76 , Issue.1-5 , pp. 143-151
    • Luu-The, V.1
  • 11
    • 0001385935 scopus 로고
    • The interconversion of estrone and estradiol by human tissue slices
    • K.J. Ryan, and L.L. Engel The interconversion of estrone and estradiol by human tissue slices Endocrinology 52 1953 287 291
    • (1953) Endocrinology , vol.52 , pp. 287-291
    • Ryan, K.J.1    Engel, L.L.2
  • 12
    • 77955836270 scopus 로고    scopus 로고
    • Inhibitors of 17β-hydroxysteroid dehydrogenase: A patent review
    • D. Poirier Inhibitors of 17β-hydroxysteroid dehydrogenase: a patent review Expert Opin. Ther. Patents 20 2010 1123 1145
    • (2010) Expert Opin. Ther. Patents , vol.20 , pp. 1123-1145
    • Poirier, D.1
  • 13
    • 70349150178 scopus 로고    scopus 로고
    • Advances in development of inhibitors of 17β-hydroxysteroid dehydrogenases
    • D. Poirier Advances in development of inhibitors of 17β- hydroxysteroid dehydrogenases Anti-Cancer Agents Med. Chem. 9 2009 642 660
    • (2009) Anti-Cancer Agents Med. Chem. , vol.9 , pp. 642-660
    • Poirier, D.1
  • 15
    • 61649096847 scopus 로고    scopus 로고
    • Perspectives in understanding the role of human 17β-hydroxysteroid dehydrogenases in health and disease
    • M. Meier, G. Möller, and J. Adamski Perspectives in understanding the role of human 17β-hydroxysteroid dehydrogenases in health and disease Ann. N. Y. Acad. Sci. 1155 2009 15 24
    • (2009) Ann. N. Y. Acad. Sci. , vol.1155 , pp. 15-24
    • Meier, M.1    Möller, G.2    Adamski, J.3
  • 16
    • 39049103081 scopus 로고    scopus 로고
    • Inhibitors of 17beta-hydroxysteroid dehydrogenase type 1
    • P. Brozic, T. Lanisnik-Risner, and S. Gobec Inhibitors of 17beta-hydroxysteroid dehydrogenase type 1 Curr. Med. Chem. 15 2008 137 150
    • (2008) Curr. Med. Chem. , vol.15 , pp. 137-150
    • Brozic, P.1    Lanisnik-Risner, T.2    Gobec, S.3
  • 17
    • 53849119147 scopus 로고    scopus 로고
    • Design and validation of specific inhibitors of 17β-hydroxysteroid dehydrogenases for therapeutic application in breast and prostate cancer, and in endometriosis
    • J.M. Day, H.J. Tutill, A. Purohit, and M.J. Reed Design and validation of specific inhibitors of 17β-hydroxysteroid dehydrogenases for therapeutic application in breast and prostate cancer, and in endometriosis Endocr. Relat. Cancer 15 2008 665 692
    • (2008) Endocr. Relat. Cancer , vol.15 , pp. 665-692
    • Day, J.M.1    Tutill, H.J.2    Purohit, A.3    Reed, M.J.4
  • 18
    • 57749091994 scopus 로고    scopus 로고
    • Hydroxysteroid dehydrogenase (17β-HSD3, 17β-HSD5 and 3α-HSD3) inhibitors: Extragonadal regulation of intracellular sex steroid hormone levels
    • M.L. Mohler, R. Narayanan, Y. He, D.D. Miler, and J.T. Dalton Hydroxysteroid dehydrogenase (17β-HSD3, 17β-HSD5 and 3α-HSD3) inhibitors: extragonadal regulation of intracellular sex steroid hormone levels Recent Pat. Endocr. Metab. Immune Drug Discov. 1 2007 103 108
    • (2007) Recent Pat. Endocr. Metab. Immune Drug Discov. , vol.1 , pp. 103-108
    • Mohler, M.L.1    Narayanan, R.2    He, Y.3    Miler, D.D.4    Dalton, J.T.5
  • 19
    • 2542492928 scopus 로고    scopus 로고
    • The selective estrogen enzyme modulators in breast cancer: A review
    • DOI 10.1016/j.bbcan.2004.03.001, PII S0304419X04000186
    • J.R. Pasqualini The selective estrogen enzyme modulators in breast cancer: a review Biochim. Biophys. Acta 1654 2004 123 143 (Pubitemid 38681205)
    • (2004) Biochimica et Biophysica Acta - Reviews on Cancer , vol.1654 , Issue.2 , pp. 123-143
    • Pasqualini, J.R.1
  • 20
    • 0037277521 scopus 로고    scopus 로고
    • Inhibitors of 17β-hydroxysteroid dehydrogenases
    • D. Poirier Inhibitors of 17β-hydroxysteroid dehydrogenases Curr. Med. Chem. 10 2003 453 477
    • (2003) Curr. Med. Chem. , vol.10 , pp. 453-477
    • Poirier, D.1
  • 24
    • 0037396439 scopus 로고    scopus 로고
    • Endocrine and intracrine sources of androgens in women: Inhibition of breast cancer and other roles of androgens and their precursor dehydroepiandrosterone
    • DOI 10.1210/er.2001-0031
    • F. Labrie, V. Luu-The, C. Labrie, A. Bélanger, J. Simard, S.X. Lin, and G. Pelletier Endocrine and intracrine sources of androgens in women: inhibition of breast cancer and other roles of androgens and their precursor dehydroepiandrosterone Endocr. Rev. 24 2003 152 182 (Pubitemid 36515283)
    • (2003) Endocrine Reviews , vol.24 , Issue.2 , pp. 152-182
    • Labrie, F.1    Luu-The, V.2    Labrie, C.3    Belanger, A.4    Simard, J.5    Lin, S.-X.6    Pelletier, G.7
  • 25
    • 0035019952 scopus 로고    scopus 로고
    • Inhibitors of steroidogenesis as agents for the treatment of hormone-dependent cancers
    • DOI 10.1517/13543776.11.5.789
    • H.J. Smith, P.J. Nicholls, C. Simons, and R. Le Lain Inhibitors of steroidogenesis as agents for the treatment of hormone-dependent cancers Exp. Opin. Ther. Patents 11 2001 789 824 (Pubitemid 32427704)
    • (2001) Expert Opinion on Therapeutic Patents , vol.11 , Issue.5 , pp. 789-824
    • Smith, H.J.1    Nicholls, P.J.2    Simons, C.3    Le Lain, R.4
  • 26
    • 0031971764 scopus 로고    scopus 로고
    • Molecular mechanisms of steroid hormone action
    • DOI 10.1677/erc.0.0050001
    • R. White, and M.G. Parker Molecular mechanisms of steroid hormone action Endocr. Relat. Cancer 5 1998 1 14 (Pubitemid 28168185)
    • (1998) Endocrine-Related Cancer , vol.5 , Issue.1 , pp. 1-14
    • White, R.1    Parker, M.G.2
  • 27
    • 0031059270 scopus 로고    scopus 로고
    • The estradiol pharmacophore: Ligand structure-estrogen receptor binding affinity relationships and a model for the receptor binding site
    • DOI 10.1016/S0039-128X(96)00242-5, PII S0039128X96002425
    • G.M. Anstead, K.E. Carlson, and J.A. Katzenellenbogen The estradiol pharmacophore: ligand structure-estrogen receptor binding affinity relationships and a model for the receptor binding site Steroids 62 1997 268 303 (Pubitemid 27114399)
    • (1997) Steroids , vol.62 , Issue.3 , pp. 268-303
    • Anstead, G.M.1    Carlson, K.E.2    Katzenellenbogen, J.A.3
  • 28
    • 0013283803 scopus 로고
    • The estrogen receptor as a target for rational drug design
    • R.G. Landes Company Austin, TX
    • E. von Angerer The estrogen receptor as a target for rational drug design Molecular Biology Intelligence Unit 1995 R.G. Landes Company Austin, TX
    • (1995) Molecular Biology Intelligence Unit
    • Von Angerer, E.1
  • 29
    • 57749106633 scopus 로고    scopus 로고
    • New cancer drugs targeting the biosynthesis of estrogens and androgens
    • D. Poirier New cancer drugs targeting the biosynthesis of estrogens and androgens Drug Devel. Res. 69 2008 304 318
    • (2008) Drug Devel. Res. , vol.69 , pp. 304-318
    • Poirier, D.1
  • 30
    • 0023865466 scopus 로고
    • 5 adrenal steroids in rat pituitary lactrotrophs and somatotrophs
    • J. Simard, A. Vincent, R. Duchesne, and F. Labrie Full oestrogenic activity of C19-delta 5 adrenal steroids in rat pituitary lactotrophs and somatotrophs Mol. Cell. Endocrinol. 55 1988 233 242 (Pubitemid 18055213)
    • (1988) Molecular and Cellular Endocrinology , vol.55 , Issue.2-3 , pp. 233-242
    • Simard, J.1    Vincent, A.2    Duchesne, R.3    Labrie, F.4
  • 31
    • 0029005016 scopus 로고
    • Synthesis and biological activities of thioether derivatives related to the antiestrogens tamoxifen and ICI 164384
    • S. Auger, Y. Mérand, J.D. Pelletier, D. Poirier, and F. Labrie Synthesis and biological activities of thioether derivatives related to the antiestrogens tamoxifen and ICI 164384 J. Steroid Biochem. Mol. Biol. 52 1995 547 565
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.52 , pp. 547-565
    • Auger, S.1    Mérand, Y.2    Pelletier, J.D.3    Poirier, D.4    Labrie, F.5
  • 32
    • 0031596753 scopus 로고    scopus 로고
    • A 6β-(thiaheptanamide) derivative of estradiol as inhibitor of 17β-hydroxysteroid dehydrogenase type 1
    • DOI 10.1016/S0960-0760(97)00136-2, PII S0960076097001362
    • D. Poirier, P. Dionne, and S. Auger A 6β-(thiaheptanamide) derivative of estradiol as inhibitor of 17β-hydroxysteroid dehydrogenase type 1 J. Steroid Biochem. Mol. Biol. 64 1998 83 90 (Pubitemid 28132850)
    • (1998) Journal of Steroid Biochemistry and Molecular Biology , vol.64 , Issue.1-2 , pp. 83-90
    • Poirier, D.1    Dionne, P.2    Auger, S.3
  • 33
    • 18444369971 scopus 로고    scopus 로고
    • Inhibitors of type 1 17β-hydroxysteroid dehydrogenase with reduced estrogenic activity: Modifications of the positions 3 and 6 of estradiol
    • DOI 10.1080/14756360500043307
    • M.R. Tremblay, R.P. Boivin, V. Luu-The, and D. Poirier Inhibitors of type 1 17β-hydroxysteroid dehydrogenase with reduced estrogenic activity: modifications of the positions 3 and 6 of estradiol J. Enzyme Inhib. Med. Chem. 20 2005 153 163 (Pubitemid 40645506)
    • (2005) Journal of Enzyme Inhibition and Medicinal Chemistry , vol.20 , Issue.2 , pp. 153-163
    • Tremblay, M.R.1    Boivin, R.P.2    Luu-The, V.3    Poirier, D.4
  • 34
    • 33845336541 scopus 로고    scopus 로고
    • C6-(N,N-butyl-methyl-heptanamide) derivatives of estrone and estradiol as inhibitors of type 1 17β-hydroxysteroid dehydrogenase: Chemical synthesis and biological evaluation
    • DOI 10.1016/j.bmc.2006.10.055, PII S096808960600887X
    • C. Cadot, Y. Laplante, F. Kamal, V. Luu-The, and D. Poirier C6-(NN-butyl-methyl-heptanamide) derivatives of estrone and estradiol as inhibitors of type 1 17β-hydroxysteroid dehydrogenase: chemical synthesis and biological evaluation Bioorg. Med. Chem. 15 2007 714 726 (Pubitemid 44880729)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.2 , pp. 714-726
    • Cadot, C.1    Laplante, Y.2    Kamal, F.3    Luu-The, V.4    Poirier, D.5
  • 35
    • 0028027142 scopus 로고
    • 16α-propyl derivatives of estradiol as inhibitors of 17β-hydroxysteroid dehydrogenase type 1
    • DOI 10.1016/S0960-894X(01)80115-3
    • K.M. Sam, R.P. Boivin, S. Auger, and D. Poirier 16α-Propyl derivatives of estradiol as inhibitors of 17β-hydroxysteroid dehydrogenase type 1 Bioorg. Med. Chem. Lett. 4 1994 2129 2132 (Pubitemid 24283139)
    • (1994) Bioorganic and Medicinal Chemistry Letters , vol.4 , Issue.17 , pp. 2129-2132
    • Sam, K.M.1    Boivin, R.P.2    Auger, S.3    Poirier, D.4
  • 36
    • 0031841053 scopus 로고    scopus 로고
    • C16 and C17 derivatives of estradiol as inhibitors of 17β-hydroxysteroid dehydrogenase type 1: Chemical synthesis and structure-activity relationships
    • K.M. Sam, R.P. Boivin, M.R. Tremblay, S. Auger, and D. Poirier C16 and C17 derivatives of estradiol as inhibitors of 17β-hydroxysteroid dehydrogenase type 1: chemical synthesis and structure-activity relationships Drug Des. Discov. 15 1998 157 180 (Pubitemid 28301999)
    • (1998) Drug Design and Discovery , vol.15 , Issue.3 , pp. 157-180
    • Sam, K.-M.1    Boivin, R.P.2    Tremblay, M.R.3    Auger, S.4    Poirier, D.5
  • 37
    • 0029593494 scopus 로고
    • Characteristics of human types 1, 2 and 3 17β-hydroxysteroid dehydrogenase activities: Oxidation/reduction and inhibition
    • DOI 10.1016/0960-0760(95)00209-X
    • V. Luu-The, Y. Zhang, D. Poirier, and F. Labrie Characteristics of human types 1, 2, and 3 17β-hydroxysteroid dehydrogenase activities: oxidation/reduction and inhibition J. Steroid Biochem. Mol. Biol. 55 1995 581 587 (Pubitemid 26019342)
    • (1995) Journal of Steroid Biochemistry and Molecular Biology , vol.55 , Issue.5-6 , pp. 581-587
    • Luu-The, V.1    Zhang, Y.2    Poirier, D.3    Labrie, F.4
  • 38
    • 0030925164 scopus 로고    scopus 로고
    • Intracellular regulation of 17β-hydroxysteroid dehydrogenase type 2 catalytic activity in A431 cells
    • C.H. Blomquist, B.S. Leung, C. Beaudoin, D. Poirier, and Y. Tremblay Intracellular regulation of 17β-hydroxysteroid dehydrogenase type 2 catalytic activity in A431 cells J. Endocrinol. 153 1997 453 464 (Pubitemid 27261256)
    • (1997) Journal of Endocrinology , vol.153 , Issue.3 , pp. 453-464
    • Blomquist, C.H.1    Leung, B.S.2    Beaudoin, C.3    Poirier, D.4    Tremblay, Y.5
  • 39
    • 0029011261 scopus 로고
    • Synthesis of 16α-(bromoalkyl)-estradiols having inhibitory effect on human placental estradiol 17β-hydroxysteroid dehydrogenase (17β-HSD type 1)
    • M.R. Tremblay, S. Auger, and D. Poirier Synthesis of 16α- (bromoalkyl)-estradiols having inhibitory effect on human placental estradiol 17β-hydroxysteroid dehydrogenase (17β-HSD type 1) Bioorg. Med. Chem. 3 1995 505 523
    • (1995) Bioorg. Med. Chem. , vol.3 , pp. 505-523
    • Tremblay, M.R.1    Auger, S.2    Poirier, D.3
  • 40
    • 0031713373 scopus 로고    scopus 로고
    • Overview of a rational approach to design type I 17β-hydroxysteroid dehydrogenase inhibitors without estrogenic activity: Chemical synthesis and biological evaluation
    • DOI 10.1016/S0960-0760(98)00043-0, PII S0960076098000430
    • M.R. Tremblay, and D. Poirier Overview of a rational approach to design type I 17β-hydroxysteroid dehydrogenase inhibitors without estrogenic activity: chemical synthesis and biological evaluation J. Steroid Biochem. Mol. Biol. 66 1998 179 191 (Pubitemid 28401692)
    • (1998) Journal of Steroid Biochemistry and Molecular Biology , vol.66 , Issue.4 , pp. 179-191
    • Tremblay, M.R.1    Poirier, D.2
  • 41
    • 0029038902 scopus 로고
    • A convenient synthetic method for alpha-alkylation of steroidal 17-ketone: Preparation of 16β-(THPO-heptyl)-estradiol
    • M.R. Tremblay, S. Auger, and D. Poirier A convenient synthetic method for alpha-alkylation of steroidal 17-ketone: preparation of 16β-(THPO-heptyl)- estradiol Synth. Commun. 25 1995 2483 2495
    • (1995) Synth. Commun. , vol.25 , pp. 2483-2495
    • Tremblay, M.R.1    Auger, S.2    Poirier, D.3
  • 42
    • 0028059981 scopus 로고
    • N-butyl, N-methyl 11-[3′,17'β-(dihydroxy)-1′,3′, 5′(10′)-estratrien-16′α-yl]-9(R/S)-bromo undecanamide: Synthesis and 17β-HSD inhibiting, estrogenic and antiestrogenic activities
    • J.D. Pelletier, F. Labrie, and D. Poirier N-butyl, N-methyl 11-[3′,17'β-(dihydroxy)-1′,3′,5′(10′) -estratrien-16′α-yl]-9(R/S)-bromo undecanamide: synthesis and 17β-HSD inhibiting, estrogenic and antiestrogenic activities Steroids 59 1994 536 547
    • (1994) Steroids , vol.59 , pp. 536-547
    • Pelletier, J.D.1    Labrie, F.2    Poirier, D.3
  • 43
    • 0030272290 scopus 로고    scopus 로고
    • Synthesis and evaluation of estradiol derivatives with 16α-(bromoalkylamide), 16α-(bromoalkyl) or 16α-(Bromoalkynyl) side chain as inhibitors of 17β-hydroxysteroid dehydrogenase type 1 without estrogenic activity
    • DOI 10.1016/0968-0896(96)00154-X, PII S096808969600154X
    • J.D. Pelletier, and D. Poirier Synthesis and evaluation of estradiol derivatives with 16α-(bromoalkylamide), 16α-(bromoalkyl) or 16α-(bromoalkynyl) side chain as inhibitors of 17β-hydroxysteroid dehydrogenase type 1 without estrogenic activity Bioorg. Med. Chem. 4 1996 1617 1628 (Pubitemid 26361866)
    • (1996) Bioorganic and Medicinal Chemistry , vol.4 , Issue.10 , pp. 1617-1628
    • Pelletier, J.D.1    Poirier, D.2
  • 44
    • 0002085765 scopus 로고    scopus 로고
    • Synthesis of 16-[carbamoyl (bromomethyl)alkyl]-estradiol: A potential dual-action inhibitor designed to blockade estrogen action and biosynthesis
    • M.R. Tremblay, and D. Poirier Synthesis of 16-[carbamoyl (bromomethyl)alkyl]-estradiol: a potential dual-action inhibitor designed to blockade estrogen action and biosynthesis J. Chem. Soc. Perkin Trans. I 1996 2765 2771
    • (1996) J. Chem. Soc. Perkin Trans. i , pp. 2765-2771
    • Tremblay, M.R.1    Poirier, D.2
  • 45
    • 79957685616 scopus 로고    scopus 로고
    • Chemical synthesis, 17β-hydroxysteroid dehydrogenase inhibitory activity and assessment of in vitro and in vivo estrogenic activities of estradiol derivatives
    • F. Rouillard, J. Lefebvre, M.A. Fournier, and D. Poirier Chemical synthesis, 17β-hydroxysteroid dehydrogenase inhibitory activity and assessment of in vitro and in vivo estrogenic activities of estradiol derivatives Open Enzyme Inhib. J. 1 2008 61 71
    • (2008) Open Enzyme Inhib. J. , vol.1 , pp. 61-71
    • Rouillard, F.1    Lefebvre, J.2    Fournier, M.A.3    Poirier, D.4
  • 46
    • 0020709715 scopus 로고
    • Fast kinetic study of yeast phenylalanyl-tRNA synthetase: An efficient discrimination between tyrosine and phenylalanine at the level of the aminoacyladenylate-enzyme complex
    • S.X. Lin, M. Baltzinger, and P. Remy Fast kinetic study of yeast phenylalanyl-tRNA synthetase: an efficient discrimination between tyrosine and phenylalanine at the level of the aminoacyladenylate-enzyme complex Biochemistry 22 1983 681 689
    • (1983) Biochemistry , vol.22 , pp. 681-689
    • Lin, S.X.1    Baltzinger, M.2    Remy, P.3
  • 49
    • 0029761692 scopus 로고    scopus 로고
    • Crystal structure of human estrogenic 17β-hydroxysteroid dehydrogenase complexed with 17β-estradiol
    • DOI 10.1038/nsb0896-665
    • A. Azzi, P. Rehse, D.W. Zhu, R.L. Campbell, F. Labrie, and S.X. Lin Crystal structure of human estrogenic 17β-hydroxysteroid dehydrogenase complexed with 17β-estradiol Nat. Struct. Biol. 3 1996 665 668 (Pubitemid 26260054)
    • (1996) Nature Structural Biology , vol.3 , Issue.8 , pp. 665-668
    • Azzi, A.1    Rehse, P.H.2    Zhu, D.-W.3    Campbell, R.L.4    Labrie, F.5    Lin, S.-X.6
  • 50
    • 0042835739 scopus 로고    scopus 로고
    • Synthesis of a first estradiol-adenosine hybrid compound
    • DOI 10.1081/SCC-120023440
    • D. Poirier, R.P. Boivin, M. Bérubé, and S.X. Lin Synthesis of a first estradiol-adenosine hybrid compound Synth. Commun. 33 2003 3183 3192 (Pubitemid 37093354)
    • (2003) Synthetic Communications , vol.33 , Issue.18 , pp. 3183-3192
    • Poirier, D.1    Boivin, R.P.2    Berube, M.3    Lin, S.-X.4
  • 51
    • 29744458970 scopus 로고    scopus 로고
    • Estradiol-adenosine hybrid compounds designed to inhibit type 1 17β-hydroxysteroid dehydrogenase
    • DOI 10.1021/jm058235e
    • D. Poirier, R.P. Boivin, M.R. Tremblay, M. Bérubé, W. Qiu, and S.X. Lin Estradiol-adenosine hybrid compounds designed to inhibit type 1 17β-hydroxysteroid dehydrogenase J. Med. Chem. 48 2005 8134 8147 (Pubitemid 43032522)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.26 , pp. 8134-8147
    • Poirier, D.1    Boivin, R.P.2    Tremblay, M.R.3    Berube, M.4    Qiu, W.5    Lin, S.-X.6
  • 52
    • 0036831679 scopus 로고    scopus 로고
    • A concerted, rational design of type 1 17β-hydroxysteroid dehydrogenase inhibitors: Estradiol-adenosine hybrids with high affinity
    • W. Qiu, R.L. Campbell, A. Gangloff, P. Dupuis, R.P. Boivin, M.R. Tremblay, D. Poirier, and S.X. Lin A concerted, rational design of type 1 17β-hydroxysteroid dehydrogenase inhibitors: estradiol-adenosine hybrids with high affinity Faseb J. 16 2002 1829 1831
    • (2002) Faseb J. , vol.16 , pp. 1829-1831
    • Qiu, W.1    Campbell, R.L.2    Gangloff, A.3    Dupuis, P.4    Boivin, R.P.5    Tremblay, M.R.6    Poirier, D.7    Lin, S.X.8
  • 53
    • 70749099419 scopus 로고    scopus 로고
    • Improved synthesis of EM-1745, preparation of its C17-ketone analogue and comparison of their inhibitory potency on 17β-hydroxysteroid dehydrogenase type 1
    • M. Bérubé, and D.D. Poirier Improved synthesis of EM-1745, preparation of its C17-ketone analogue and comparison of their inhibitory potency on 17β-hydroxysteroid dehydrogenase type 1 J. Enzyme Inhib. Med. Chem. 24 2009 832 843
    • (2009) J. Enzyme Inhib. Med. Chem. , vol.24 , pp. 832-843
    • Bérubé, M.1    Poirier, D.D.2
  • 54
    • 54049116349 scopus 로고    scopus 로고
    • Design and synthesis of bisubstrate inhibitors of type 1 17β-hydroxysteroid dehydrogenase: Overview and perspectives
    • D. Fournier, D. Poirier, M. Mazumdar, and S.X. Lin Design and synthesis of bisubstrate inhibitors of type 1 17β-hydroxysteroid dehydrogenase: overview and perspectives Eur. J. Med. Chem. 43 2008 2298 2306
    • (2008) Eur. J. Med. Chem. , vol.43 , pp. 2298-2306
    • Fournier, D.1    Poirier, D.2    Mazumdar, M.3    Lin, S.X.4
  • 55
    • 4544388288 scopus 로고    scopus 로고
    • Synthesis of simplified hybrid inhibitors of type 1 17β- hydroxysteroid dehydrogenase via cross-metathesis and Sonogashira coupling reactions
    • DOI 10.1021/ol048820u
    • M. Bérubé, and D. Poirier Synthesis of simplified hybrid inhibitors of type 1 17β-hydroxysteroid dehydrogenase via the cross-methathesis and the Sonogashira coupling reactions Org. Lett. 6 2004 3127 3130 (Pubitemid 39233136)
    • (2004) Organic Letters , vol.6 , Issue.18 , pp. 3127-3130
    • Berube, M.1    Poirier, D.2
  • 56
    • 69149084099 scopus 로고    scopus 로고
    • Design, chemical synthesis and in vitro biological evaluation of simplified estradiol-adenosine hybrids as inhibitors of 17β-hydroxysteroid dehydrogenase type 1
    • M. Bérubé, and D. Poirier Design, chemical synthesis and in vitro biological evaluation of simplified estradiol-adenosine hybrids as inhibitors of 17β-hydroxysteroid dehydrogenase type 1 Can. J. Chem. 87 2009 1180 1199
    • (2009) Can. J. Chem. , vol.87 , pp. 1180-1199
    • Bérubé, M.1    Poirier, D.2
  • 57
    • 0034741614 scopus 로고    scopus 로고
    • Chemical synthesis of 16β-propylaminoacyl derivatives of estradiol and their inhibitory potency on type 1 17β-hydroxysteroid dehydrogenase and binding affinity on steroid receptors
    • DOI 10.1016/S0039-128X(01)00116-7, PII S0039128X01001167
    • M.R. Tremblay, S.X. Lin, and D. Poirier Chemical synthesis of 16β-propylaminoacyl derivatives of estradiol and their inhibitory potency on type 1 17β-hydroxysteroid dehydrogenase and binding affinity on steroid receptors Steroids 66 2001 821 831 (Pubitemid 32884309)
    • (2001) Steroids , vol.66 , Issue.11 , pp. 821-831
    • Tremblay, M.R.1    Lin, S.-X.2    Poirier, D.3
  • 58
    • 0033651549 scopus 로고    scopus 로고
    • Solid-phase synthesis of phenolic steroids: From optimization studies to a convenient procedure for combinatorial synthesis of biologically relevant estradiol derivatives
    • M.R. Tremblay, and D. Poirier Solid-phase synthesis of phenolic steroids: from optimization studies to a convenient procedure for combinatorial synthesis of biologically relevant estradiol derivatives J. Comb. Chem. 2 2000 48 65
    • (2000) J. Comb. Chem. , vol.2 , pp. 48-65
    • Tremblay, M.R.1    Poirier, D.2
  • 59
    • 0034320360 scopus 로고    scopus 로고
    • Solid-phase synthesis of hydroxysteroid derivatives using the diethylsilyloxy linker
    • R. Maltais, M.R. Tremblay, and D. Poirier Solid-phase synthesis of hydroxysteroid derivatives using the diethylsilyloxy linker J. Comb. Chem. 2 2000 604 614
    • (2000) J. Comb. Chem. , vol.2 , pp. 604-614
    • Maltais, R.1    Tremblay, M.R.2    Poirier, D.3
  • 60
    • 0001526459 scopus 로고    scopus 로고
    • The sulfamate functional group as a new anchor for solid-phase organic synthesis
    • L.C. Ciobanu, R. Maltais, and D. Poirier The sulfamate functional group as a new anchor for solid-phase organic synthesis Org. Lett. 2 2000 445 448
    • (2000) Org. Lett. , vol.2 , pp. 445-448
    • Ciobanu, L.C.1    Maltais, R.2    Poirier, D.3
  • 61
    • 55249099842 scopus 로고    scopus 로고
    • Recent developments of steroid sulfatase inhibitors as anti-cancer agents
    • P.A. Foster, M.J. Reed, and A. Purohit Recent developments of steroid sulfatase inhibitors as anti-cancer agents Anti-Cancer Agents Med. Chem. 8 2008 732 738
    • (2008) Anti-Cancer Agents Med. Chem. , vol.8 , pp. 732-738
    • Foster, P.A.1    Reed, M.J.2    Purohit, A.3
  • 64
    • 33644906407 scopus 로고    scopus 로고
    • Solid-phase organic synthesis (SPOS) of modulators of estrogenic and androgenic action
    • D. Poirier, and R. Maltais Solid-phase organic synthesis (SPOS) of modulators of estrogenic and androgenic action Mini-Rev. Med. Chem. 6 2006 37 52
    • (2006) Mini-Rev. Med. Chem. , vol.6 , pp. 37-52
    • Poirier, D.1    Maltais, R.2
  • 65
    • 0037152452 scopus 로고    scopus 로고
    • A multidetachable sulfamate linker successfully used in a solid-Phase strategy to generate libraries of sulfamate and phenol derivatives
    • DOI 10.1016/S0960-894X(02)00637-6, PII S0960894X02006376
    • D. Poirier, L.C. Ciobanu, and M. Bérubé A multidetachable sulfamate linker and solid-phase strategy used to generate libraries of sulfamate and phenol derivatives Bioorg. Med. Chem. Lett. 12 2002 2833 2838 (Pubitemid 35266744)
    • (2002) Bioorganic and Medicinal Chemistry Letters , vol.12 , Issue.20 , pp. 2833-2838
    • Poirier, D.1    Ciobanu, L.C.2    Berube, M.3
  • 67
    • 66349089930 scopus 로고    scopus 로고
    • Synthesis of aryl sulfamate and phenol small peptide derivatives using a multidetachable sulfamate linker strategy
    • D. Fournier, P.A. Breuil, and D. Poirier Synthesis of aryl sulfamate and phenol small peptide derivatives using a multidetachable sulfamate linker strategy Adv. Exp. Med. Biol. 611 2009 219 220
    • (2009) Adv. Exp. Med. Biol. , vol.611 , pp. 219-220
    • Fournier, D.1    Breuil, P.A.2    Poirier, D.3
  • 68
    • 33751247648 scopus 로고    scopus 로고
    • Synthesis of libraries of 16β-aminopropyl estradiol derivatives for targeting two key steroidogenic enzymes
    • DOI 10.1002/cmdc.200600071
    • L.C. Ciobanu, and D. Poirier Synthesis of libraries of 16β-aminopropyl estradiol derivatives for targeting two key steroidogenic enzymes ChemMedChem 1 2006 1249 1259 (Pubitemid 44786931)
    • (2006) ChemMedChem , vol.1 , Issue.11 , pp. 1249-1259
    • Ciobanu, L.C.1    Poirier, D.2
  • 69
    • 77950356448 scopus 로고    scopus 로고
    • Preparation of libraries of 16β-estradiol derivatives as bisubstrate inhibitors of type 1 17β-hydroxysteroid dehydrogenase using the multidetachable sulfamate linker
    • M. Bérubé, F. Delagoutte, and D. Poirier Preparation of libraries of 16β-estradiol derivatives as bisubstrate inhibitors of type 1 17β-hydroxysteroid dehydrogenase using the multidetachable sulfamate linker Molecules 15 2010 1590 1631
    • (2010) Molecules , vol.15 , pp. 1590-1631
    • Bérubé, M.1    Delagoutte, F.2    Poirier, D.3
  • 70
    • 33644887991 scopus 로고    scopus 로고
    • Estrone and estradiol C-16 derivatives as inhibitors of type 1 17β-hydroxysteroid dehydrogenase
    • D. Poirier, H.J. Chang, A. Azzi, R.P. Boivin, and S.X. Lin Estrone and estradiol C-16 derivatives as inhibitors of type 1 17β-hydroxysteroid dehydrogenase Mol. Cell. Endocrinol. 248 2006 236 238
    • (2006) Mol. Cell. Endocrinol. , vol.248 , pp. 236-238
    • Poirier, D.1    Chang, H.J.2    Azzi, A.3    Boivin, R.P.4    Lin, S.X.5
  • 75
    • 73149097897 scopus 로고    scopus 로고
    • Binary and ternary crystal structure analyses of a novel inhibitor with 17β-HSD type 1: A lead compound for breast cancer therapy
    • M. Mazumdar, D. Fournier, D.W. Zhu, C. Cadot, D. Poirier, and S.X. Lin Binary and ternary crystal structure analyses of a novel inhibitor with 17β-HSD type 1: a lead compound for breast cancer therapy Biochem. J. 424 2009 357 366
    • (2009) Biochem. J. , vol.424 , pp. 357-366
    • Mazumdar, M.1    Fournier, D.2    Zhu, D.W.3    Cadot, C.4    Poirier, D.5    Lin, S.X.6
  • 76
    • 0033532388 scopus 로고    scopus 로고
    • Human estrogenic 17β-hydroxysteroidehydrogenase: Predominance of estrone reduction and its induction by NADPH
    • J.Z. Jin, and S.X.S.X. Lin Human estrogenic 17β- hydroxysteroidehydrogenase: predominance of estrone reduction and its induction by NADPH Biochem. Biophys. Res. Commun. 259 1999 489 493
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 489-493
    • Jin, J.Z.1    Lin, S.X.S.X.2
  • 77
    • 0032727093 scopus 로고    scopus 로고
    • Determination of cDNA, gene structure and chromosomal localization of the novel human 17β-hydroxysteroid dehydrogenase type 7
    • DOI 10.1016/S0014-5793(99)01366-6, PII S0014579399013666
    • A. Krazeisen, R. Breitling, K. Imai, S. Fritz, G. Möller, and J. Adamski Determination of cDNA, gene structure and chromosomal localization of the novel human 17β-hydroxysteroid dehydrogenase type 7 FEBS Lett. 460 1999 373 379 (Pubitemid 29495972)
    • (1999) FEBS Letters , vol.460 , Issue.2 , pp. 373-379
    • Krazeisen, A.1    Breitling, R.2    Imai, K.3    Fritz, S.4    Moller, G.5    Adamski, J.6
  • 78
    • 0035931123 scopus 로고    scopus 로고
    • 17β-hydroxysteroid dehydrogenase type 7 - An ancient 3-ketosteroid reductase of cholesterogenesis
    • DOI 10.1016/S0303-7207(00)00416-0, PII S0303720700004160
    • R. Breitling, A. Krazeisen, G. Möller, and J. Adamski 17β-Hydroxysteroid dehydrogenase type 7 - an ancient 3-ketosteroid reductase of cholesterogenesis Mol. Cell. Endocrinol. 171 2001 199 204 (Pubitemid 32098215)
    • (2001) Molecular and Cellular Endocrinology , vol.171 , Issue.1-2 , pp. 199-204
    • Breitling, R.1    Krazeisen, A.2    Moller, G.3    Adamski, J.4
  • 81
    • 33750414318 scopus 로고    scopus 로고
    • Effects of 3-beta-diol, an androgen metabolite with intrinsic estrogen-like effects, in modulating the aquaporin-9 expression in the rat efferent ductules
    • P. Picciarelli-Lima, A.G. Oliveira, A.M. Reis, E. Kalapothakis, G.A.B. Mahecha, R.A. Hess, and C. Oliveira Effects of 3-beta-diol, an androgen metabolite with intrinsic estrogen-like effects, in modulating the aquaporin-9 expression in the rat efferent ductules Reprod. Biol. Endocrinol. 4 2006 51
    • (2006) Reprod. Biol. Endocrinol. , vol.4 , pp. 51
    • Picciarelli-Lima, P.1    Oliveira, A.G.2    Reis, A.M.3    Kalapothakis, E.4    Mahecha, G.A.B.5    Hess, R.A.6    Oliveira, C.7
  • 82
    • 0041833725 scopus 로고    scopus 로고
    • Closing the gap: Identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis
    • DOI 10.1210/me.2002-0436
    • 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 (Pubitemid 37072289)
    • (2003) Molecular Endocrinology , vol.17 , Issue.9 , pp. 1715-1725
    • Marijanovic, Z.1    Laubner, D.2    Moller, G.3    Gege, C.4    Husen, B.5    Adamski, J.6    Breitling, R.7
  • 83
    • 18144384374 scopus 로고    scopus 로고
    • Promoter analyses of human and mouse 17beta-hydroxysteroid dehydrogenase type 7
    • DOI 10.1016/j.jsbmb.2005.01.012
    • T. Ohnesorg, and J. Adamski Promoter analyses of human and mouse 17beta-hydroxysteroid dehydrogenase type 7 J. Steroid Biochem. Mol. Biol. 94 2005 259 261 (Pubitemid 40614539)
    • (2005) Journal of Steroid Biochemistry and Molecular Biology , vol.94 , Issue.SPEC. ISSUE , pp. 259-261
    • Ohnesorg, T.1    Adamski, J.2
  • 84
    • 33747876939 scopus 로고    scopus 로고
    • Transcriptional regulation of human and murine 17β-hydroxysteroid dehydrogenase type-7 confers its participation in cholesterol biosynthesis
    • DOI 10.1677/jme.1.02043
    • T. Ohnesorg, B. Keller, M. Hrabé de Angelis, and J. Adamski Transcriptional regulation of human and murine 17β-hydroxysteroid dehydrogenase type-7 confers its participation in cholesterol biosynthesis J. Mol. Endocrinol. 37 2006 185 197 (Pubitemid 44288616)
    • (2006) Journal of Molecular Endocrinology , vol.37 , Issue.1 , pp. 185-197
    • Ohnesorg, T.1    Keller, B.2    De Angelis, M.H.3    Adamski, J.4
  • 85
    • 33644886821 scopus 로고    scopus 로고
    • First inhibitors of the steroidogenic enzyme type 7 17β- hydroxysteroid dehydrogenase
    • E. Bellavance, V. Luu-The, and D. Poirier First inhibitors of the steroidogenic enzyme type 7 17β-hydroxysteroid dehydrogenase Lett. Drug Design Discov. 1 2004 194 197
    • (2004) Lett. Drug Design Discov. , vol.1 , pp. 194-197
    • Bellavance, E.1    Luu-The, V.2    Poirier, D.3
  • 86
    • 72249090207 scopus 로고    scopus 로고
    • Potent and selective inhibitors of 17β-hydroxysteroid dehydrogenase type 7, an enzyme that catalyzes the reduction of the key hormones estrone and dihydrotestosterone
    • E. Bellavance, V. Luu-The, and D. Poirier Potent and selective inhibitors of 17β-hydroxysteroid dehydrogenase type 7, an enzyme that catalyzes the reduction of the key hormones estrone and dihydrotestosterone J. Med. Chem. 52 2009 7488 7502
    • (2009) J. Med. Chem. , vol.52 , pp. 7488-7502
    • Bellavance, E.1    Luu-The, V.2    Poirier, D.3
  • 87
    • 60149084693 scopus 로고    scopus 로고
    • Steroidal lactones as inhibitors of 17β-hydroxysteroid dehydrogenase type 5: Chemical synthesis, enzyme inhibitory activity, and assessment of estrogenic and androgenic activities
    • P. Bydal, V. Luu-The, F. Labrie, and D. Poirier Steroidal lactones as inhibitors of 17β-hydroxysteroid dehydrogenase type 5: chemical synthesis, enzyme inhibitory activity, and assessment of estrogenic and androgenic activities Eur. J. Med. Chem. 44 2009 632 644
    • (2009) Eur. J. Med. Chem. , vol.44 , pp. 632-644
    • Bydal, P.1    Luu-The, V.2    Labrie, F.3    Poirier, D.4
  • 89
    • 60249090183 scopus 로고    scopus 로고
    • Relative involvement of three 17β-hydroxysteroid dehydrogenases (types 1, 7 and 12) in the formation of estradiol in various breast cancer cell lines using selective inhibitors
    • Y. Laplante, C. Rancourt, and D. Poirier Relative involvement of three 17β-hydroxysteroid dehydrogenases (types 1, 7 and 12) in the formation of estradiol in various breast cancer cell lines using selective inhibitors Mol. Cell. Endocrinol. 301 2009 146 153
    • (2009) Mol. Cell. Endocrinol. , vol.301 , pp. 146-153
    • Laplante, Y.1    Rancourt, C.2    Poirier, D.3
  • 91
    • 67650649396 scopus 로고    scopus 로고
    • Specific estradiol biosynthesis pathway in choriocarcinoma (JEG-3) cell line
    • M. Samson, F. Labrie, and V. Luu-The Specific estradiol biosynthesis pathway in choriocarcinoma (JEG-3) cell line J. Steroid Biochem. Mol. Biol. 116 2009 154 159
    • (2009) J. Steroid Biochem. Mol. Biol. , vol.116 , pp. 154-159
    • Samson, M.1    Labrie, F.2    Luu-The, V.3
  • 92
    • 60249090902 scopus 로고    scopus 로고
    • Estrogen formation in endometrial and cervix cancer cell lines: Involvement of aromatase, steroid sulfatase and 17β-hydroxysteroid dehydrogenases (types 1, 5, 7 and 12)
    • M.A. Fournier, and D. Poirier Estrogen formation in endometrial and cervix cancer cell lines: involvement of aromatase, steroid sulfatase and 17β-hydroxysteroid dehydrogenases (types 1, 5, 7 and 12) Mol. Cell. Endocrinol. 301 2009 142 145
    • (2009) Mol. Cell. Endocrinol. , vol.301 , pp. 142-145
    • Fournier, M.A.1    Poirier, D.2
  • 93
    • 21744450737 scopus 로고    scopus 로고
    • Estrogen-induced loss of progesterone receptor expression in normal and malignant ovarian surface epithelial cells
    • DOI 10.1038/sj.onc.1208623
    • K. Mukherjee, V. Syed, and S.M. Ho Estrogen-induced loss of progesterone receptor expression in normal and malignant ovarian surface epithelial cells Oncogene 24 2005 4388 4400 (Pubitemid 40961762)
    • (2005) Oncogene , vol.24 , Issue.27 , pp. 4388-4400
    • Mukherjee, K.1    Syed, V.2    Ho, S.-M.3
  • 94
    • 77950421854 scopus 로고    scopus 로고
    • 17β-Hydroxysteroid dehydrogenase type 1 stimulates breast cancer by dihydrotestosterone inactivation in addition to estradiol production
    • J. Aka, M. Mazumdar, C.Q. Chen, D. Poirier, and S.X. Lin 17β-Hydroxysteroid dehydrogenase type 1 stimulates breast cancer by dihydrotestosterone inactivation in addition to estradiol production Mol. Endocrinol. 24 2010 832 845
    • (2010) Mol. Endocrinol. , vol.24 , pp. 832-845
    • Aka, J.1    Mazumdar, M.2    Chen, C.Q.3    Poirier, D.4    Lin, S.X.5
  • 95
    • 41849117998 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of (hydroxyphenyl) naphthalene and -quinoline derivatives: Potent and selective nonsteroidal inhibitors of 17β-hydroxysteroid dehydrogenase type 1 (17β-HSD1) for the treatment of estrogen-dependent diseases
    • DOI 10.1021/jm701447v
    • M. Frotscher, E. Ziegler, S. Marchais-Oberwinkler, P. Kruchten, A. Neugebauer, L. Fetzer, C. Scherer, U. Muller-Vieira, J. Messinger, H. Thole, and R.W. Hartmann Design, synthesis, and biological evaluation of (hydroxyphenyl)naphthalene and quinoline derivatives: potent and selective nonsteroidal inhibitors of 17β-hydroxysteroid dehydrogenase type 1 (17β-HSD1) for the treatment of estrogen-dependent diseases J. Med. Chem. 51 2008 2158 2169 (Pubitemid 351503271)
    • (2008) Journal of Medicinal Chemistry , vol.51 , Issue.7 , pp. 2158-2169
    • Frotscher, M.1    Ziegler, E.2    Marchais-Oberwinkler, S.3    Kruchten, P.4    Neugebauer, A.5    Fetzer, L.6    Scherer, C.7    Muller-Vieira, U.8    Messinger, J.9    Thole, H.10    Hartmann, R.W.11


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