메뉴 건너뛰기




Volumn 125, Issue 1-2, 2011, Pages 105-111

Inhibitors of human 20α-hydroxysteroid dehydrogenase (AKR1C1)

Author keywords

20 Hydroxysteroid dehydrogenase; 3 Hydroxysteroid dehydrogenase; Aldo keto reductase; Cancer; Drug design

Indexed keywords

2 (2',3 DICHLORO N METHYLBIPHENYL 4 YL CARBOXAMIDO)BENZOIC ACID; 2 (4 CHLOROBENZYLIDENE) CYCLOPENTANONE; 20ALPHA HYDROXYSTEROID DEHYDROGENASE; 3 BROMO 5 PHENYLSALICYLIC ACID; 3,7 DIHYDROXYFLAVONE; 3ALPHA HYDROXY 5ALPHA PREGNAN 20 ONE; 7 HYDROXYFLAVONE; ANTHRANILIC ACID DERIVATIVE; CYCLOPENTANE DERIVATIVE; EFENAMIC ACID; FLAVONE DERIVATIVE; LITHOCHOLIC ACID; MEDAZEPAM; N BENZYL 2 (2 (4 METHOXYBENZYL) 6 OXO 1,6 DIHYDROPYRIMIDIN 4 YL)ACETAMIDE; NARINGENIN; PYRIMIDINE DERIVATIVE; UNCLASSIFIED DRUG; XENYSALATE;

EID: 79957723874     PISSN: 09600760     EISSN: 18791220     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2010.10.006     Document Type: Article
Times cited : (35)

References (54)
  • 1
    • 13544273915 scopus 로고    scopus 로고
    • Regulation of progesterone levels during pregnancy and parturition by signal transducer and activator of transcription 5 and 20α-hydroxysteroid dehydrogenase
    • DOI 10.1210/me.2004-0302
    • R.P. Piekorz, S. Gingras, A. Hoffmeyer, J.N. Ihle, and Y. Weinstein Regulation of progesterone levels during pregnancy and parturition by signal transducer and activator of transcription 5 and 20α-hydroxysteroid dehydrogenase Mol. Endocrinol. 19 2 2005 431 440 (Pubitemid 40223467)
    • (2005) Molecular Endocrinology , vol.19 , Issue.2 , pp. 431-440
    • Piekorz, R.P.1    Gingras, S.2    Hoffmeyer, A.3    Ihle, J.N.4    Weinstein, Y.5
  • 2
    • 58049218988 scopus 로고    scopus 로고
    • Non-genomic progesterone actions in female reproduction
    • B. Gellersen, M.S. Fernandes, and J.J. Brosens Non-genomic progesterone actions in female reproduction Hum. Reprod. Update 15 1 2009 119 138
    • (2009) Hum. Reprod. Update , vol.15 , Issue.1 , pp. 119-138
    • Gellersen, B.1    Fernandes, M.S.2    Brosens, J.J.3
  • 3
    • 40749153470 scopus 로고    scopus 로고
    • Progesterone exerts neuroprotective effects after brain injury
    • DOI 10.1016/j.brainresrev.2007.06.012, PII S0165017307001129
    • D.G. Stein Progesterone exerts neuroprotective effects after brain injury Brain Res. Rev. 57 2 2008 386 397 (Pubitemid 351381771)
    • (2008) Brain Research Reviews , vol.57 , Issue.2 , pp. 386-397
    • Stein, D.G.1
  • 4
    • 43249131666 scopus 로고    scopus 로고
    • Improved outcomes from the administration of progesterone for patients with acute severe traumatic brain injury: A randomized controlled trial
    • G. Xiao, J. Wei, W. Yan, W. Wang, and Z. Lu Improved outcomes from the administration of progesterone for patients with acute severe traumatic brain injury: a randomized controlled trial Crit. Care 12 2 2008 R61
    • (2008) Crit. Care , vol.12 , Issue.2 , pp. 61
    • Xiao, G.1    Wei, J.2    Yan, W.3    Wang, W.4    Lu, Z.5
  • 6
    • 33846287960 scopus 로고    scopus 로고
    • Progesterone and its derivatives are neuroprotective agents in experimental diabetic neuropathy: A multimodal analysis
    • DOI 10.1016/j.neuroscience.2006.11.014, PII S0306452206015326
    • E. Leonelli, R. Bianchi, G. Cavaletti, D. Caruso, D. Crippa, L.M. Garcia-Segura, G. Lauria, V. Magnaghi, I. Roglio, and R.C. Melcangi Progesterone and its derivatives are neuroprotective agents in experimental diabetic neuropathy: a multimodal analysis Neuroscience 144 4 2007 1293 1304 (Pubitemid 46123820)
    • (2007) Neuroscience , vol.144 , Issue.4 , pp. 1293-1304
    • Leonelli, E.1    Bianchi, R.2    Cavaletti, G.3    Caruso, D.4    Crippa, D.5    Garcia-Segura, L.M.6    Lauria, G.7    Magnaghi, V.8    Roglio, I.9    Melcangi, R.C.10
  • 7
    • 0034287545 scopus 로고    scopus 로고
    • 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
    • T.M. Penning, M.E. Burczynski, J.M. Jez, C.F. Hung, H.K. Lin, H. Ma, M. Moore, N. Palackal, and K. Ratnam 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 Biochem. J. 351 Pt 1 2000 67 77
    • (2000) Biochem. J. , vol.351 , Issue.PART 1 , pp. 67-77
    • Penning, T.M.1    Burczynski, M.E.2    Jez, J.M.3    Hung, C.F.4    Lin, H.K.5    Ma, H.6    Moore, M.7    Palackal, N.8    Ratnam, K.9
  • 10
    • 66949164462 scopus 로고    scopus 로고
    • Aldo-keto reductase 1C subfamily genes in skin are UV-inducible: Possible role in keratinocytes survival
    • Y.E. Marín, M. Seiberg, and C.B. Lin Aldo-keto reductase 1C subfamily genes in skin are UV-inducible: possible role in keratinocytes survival Exp. Dermatol. 18 7 2009 611 618
    • (2009) Exp. Dermatol. , vol.18 , Issue.7 , pp. 611-618
    • Marín, Y.E.1    Seiberg, M.2    Lin, C.B.3
  • 11
    • 54049138429 scopus 로고    scopus 로고
    • Progesterone is extensively metabolized in osteoblasts: Implications for progesterone action on bone
    • M. Quinkler, K. Kaur, M. Hewison, P.M. Stewart, and M.S. Cooper Progesterone is extensively metabolized in osteoblasts: implications for progesterone action on bone Horm. Metab. Res. 40 10 2008 679 684
    • (2008) Horm. Metab. Res. , vol.40 , Issue.10 , pp. 679-684
    • Quinkler, M.1    Kaur, K.2    Hewison, M.3    Stewart, P.M.4    Cooper, M.S.5
  • 12
    • 33846818874 scopus 로고    scopus 로고
    • 4-Hydroxynonenal, a product of oxidative stress, leads to an antioxidant response in optic nerve head astrocytes
    • DOI 10.1016/j.exer.2006.10.020, PII S0014483506004234
    • P.E. Malone, and M.R. Hernandez 4-Hydroxynonenal, a product of oxidative stress, leads to an antioxidant response in optic nerve head astrocytes Exp. Eye Res. 84 3 2007 444 454 (Pubitemid 46210058)
    • (2007) Experimental Eye Research , vol.84 , Issue.3 , pp. 444-454
    • Malone, P.E.1    Hernandez, M.R.2
  • 13
    • 0037324845 scopus 로고    scopus 로고
    • Selective and potent inhibitors of human 20α-hydroxysteroid dehydrogenase (AKR1C1) that metabolizes neurosteroids derived from progesterone
    • DOI 10.1016/S0009-2797(02)00206-5, PII S0009279702002065
    • Y. Higaki, N. Usami, S. Shintani, S. Ishikura, O. El-Kabbani, and A. Hara Selective and potent inhibitors of human 20α-hydroxysteroid dehydrogenase (AKR1C1) that metabolizes neurosteroids derived from progesterone Chem. Biol. Interact. 143-144 2003 503 513 (Pubitemid 36253599)
    • (2003) Chemico-Biological Interactions , vol.143-144 , pp. 503-513
    • Higaki, Y.1    Usami, N.2    Shintani, S.3    Ishikura, S.4    El-Kabbani, O.5    Hara, A.6
  • 14
    • 12344300599 scopus 로고    scopus 로고
    • The roles of Aldo-Keto reductases in steroid hormone action
    • DOI 10.1358/dnp.2004.17.9.872570
    • D.R. Bauman, S. Steckelbroeck, and T.M. Penning The roles of aldo-keto reductases in steroid hormone action Drug News Perspect. 17 9 2004 563 578 (Pubitemid 40136607)
    • (2004) Drug News and Perspectives , vol.17 , Issue.9 , pp. 563-578
    • Bauman, D.R.1    Steckelbroeck, S.2    Penning, T.M.3
  • 15
    • 54549110136 scopus 로고    scopus 로고
    • The aldo-keto reductase superfamily and its role in drug metabolism and detoxification
    • O.A. Barski, S.M. Tipparaju, and A. Bhatnagar The aldo-keto reductase superfamily and its role in drug metabolism and detoxification Drug Metab. Rev. 40 4 2008 553 624
    • (2008) Drug Metab. Rev. , vol.40 , Issue.4 , pp. 553-624
    • Barski, O.A.1    Tipparaju, S.M.2    Bhatnagar, A.3
  • 16
    • 33847021147 scopus 로고    scopus 로고
    • Aldo-keto reductases and bioactivation/detoxication
    • Y. Jin, and T.M. Penning Aldo-keto reductases and bioactivation/ detoxication Annu. Rev. Pharmacol. Toxicol. 47 2007 263 292
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 263-292
    • Jin, Y.1    Penning, T.M.2
  • 19
    • 0035951825 scopus 로고    scopus 로고
    • The reactive oxygen species- and Michael acceptor-inducible human aldo-keto reductase AKR1C1 reduces the α,β-unsaturated aldehyde 4-hydroxy-2-nonenal to 1,4-dihydroxy-2-nonene
    • M.E. Burczynski, G.R. Sridhar, N.T. Palackal, and T.M. Penning The reactive oxygen species- and Michael acceptor-inducible human aldo-keto reductase AKR1C1 reduces the α,β-unsaturated aldehyde 4-hydroxy-2-nonenal to 1,4-dihydroxy-2-nonene J. Biol. Chem. 276 4 2001 2890 2897
    • (2001) J. Biol. Chem. , vol.276 , Issue.4 , pp. 2890-2897
    • Burczynski, M.E.1    Sridhar, G.R.2    Palackal, N.T.3    Penning, T.M.4
  • 20
    • 0033837032 scopus 로고    scopus 로고
    • Characterization of 4-oxo-2-nonenal as a novel product of lipid peroxidation
    • DOI 10.1021/tx000101a
    • S.H. Lee, and I.A. Blair Characterization of 4-oxo-2-nonenal as a novel product of lipid peroxidation Chem. Res. Toxicol. 13 8 2000 698 702 (Pubitemid 30663446)
    • (2000) Chemical Research in Toxicology , vol.13 , Issue.8 , pp. 698-702
    • Hwa Lee, S.1    Blair, I.A.2
  • 21
    • 0344874622 scopus 로고    scopus 로고
    • Aldose Reductase Catalyzes Reduction of the Lipid Peroxidation Product 4-Oxonon-2-enal
    • DOI 10.1021/tx0300378
    • J.A. Doorn, S.K. Srivastava, and D.R. Petersen Aldose reductase catalyzes reduction of the lipid peroxidation product 4-oxonon-2-enal Chem. Res. Toxicol. 16 11 2003 1418 1423 (Pubitemid 37474091)
    • (2003) Chemical Research in Toxicology , vol.16 , Issue.11 , pp. 1418-1423
    • Doorn, J.A.1    Srivastava, S.K.2    Petersen, D.R.3
  • 22
    • 0035866794 scopus 로고    scopus 로고
    • Overexpression of dihydrodiol dehydrogenase as a prognostic marker of non-small cell lung cancer
    • N.Y. Hsu, H.C. Ho, K.C. Chow, T.Y. Lin, C.S. Shih, L.S. Wang, and C.M. Tsai Overexpression of dihydrodiol dehydrogenase as a prognostic marker of non-small cell lung cancer Cancer Res. 61 6 2001 2727 2731
    • (2001) Cancer Res. , vol.61 , Issue.6 , pp. 2727-2731
    • Hsu, N.Y.1    Ho, H.C.2    Chow, K.C.3    Lin, T.Y.4    Shih, C.S.5    Wang, L.S.6    Tsai, C.M.7
  • 23
    • 0036582569 scopus 로고    scopus 로고
    • Expression of dihydrodiol dehydrogenase in the resected stage i non-small cell lung cancer
    • C.Y. Chen, C.P. Hsu, N.Y. Hsu, C.S. Shih, T.Y. Lin, and K.C. Chow Expression of dihydrodiol dehydrogenase in the resected stage I non-small cell lung cancer Oncol. Rep. 9 3 2002 515 519
    • (2002) Oncol. Rep. , vol.9 , Issue.3 , pp. 515-519
    • Chen, C.Y.1    Hsu, C.P.2    Hsu, N.Y.3    Shih, C.S.4    Lin, T.Y.5    Chow, K.C.6
  • 24
    • 33644909044 scopus 로고    scopus 로고
    • AKR1C1 and AKR1C3 may determine progesterone and estrogen ratios in endometrial cancer
    • T.L. Rizner, T. Smuc, R. Rupreht, J. Sinkovec, and T.M. Penning AKR1C1 and AKR1C3 may determine progesterone and estrogen ratios in endometrial cancer Mol. Cell. Endocrinol. 248 1-2 2006 126 135
    • (2006) Mol. Cell. Endocrinol. , vol.248 , Issue.12 , pp. 126-135
    • Rizner, T.L.1    Smuc, T.2    Rupreht, R.3    Sinkovec, J.4    Penning, T.M.5
  • 25
    • 60249103491 scopus 로고    scopus 로고
    • Aberrant pre-receptor regulation of estrogen and progesterone action in endometrial cancer
    • T. Smuc, and T.L. Rizner Aberrant pre-receptor regulation of estrogen and progesterone action in endometrial cancer Mol. Cell. Endocrinol. 301 1-2 2009 74 82
    • (2009) Mol. Cell. Endocrinol. , vol.301 , Issue.12 , pp. 74-82
    • Smuc, T.1    Rizner, T.L.2
  • 26
    • 15544379141 scopus 로고    scopus 로고
    • Overexpression of dihydrodiol dehydrogenase is associated with cisplatin-based chemotherapy resistance in ovarian cancer patients
    • Y.J. Chen, C.C. Yuan, K.C. Chow, P.H. Wang, C.R. Lai, M.S. Yen, and L.S. Wang Overexpression of dihydrodiol dehydrogenase is associated with cisplatin-based chemotherapy resistance in ovarian cancer patients Gynecol. Oncol. 97 1 2005 110 117
    • (2005) Gynecol. Oncol. , vol.97 , Issue.1 , pp. 110-117
    • Chen, Y.J.1    Yuan, C.C.2    Chow, K.C.3    Wang, P.H.4    Lai, C.R.5    Yen, M.S.6    Wang, L.S.7
  • 28
    • 59449102794 scopus 로고    scopus 로고
    • Overexpression of dihydrodiol dehydrogenase as a prognostic marker in resected gastric cancer patients
    • H.C. Chang, Y.L. Chen, C.P. Chan, K.T. Yeh, S.J. Kuo, C.J. Ko, and H.Y. Fang Overexpression of dihydrodiol dehydrogenase as a prognostic marker in resected gastric cancer patients Dig. Dis. Sci. 54 2 2009 342 347
    • (2009) Dig. Dis. Sci. , vol.54 , Issue.2 , pp. 342-347
    • Chang, H.C.1    Chen, Y.L.2    Chan, C.P.3    Yeh, K.T.4    Kuo, S.J.5    Ko, C.J.6    Fang, H.Y.7
  • 29
    • 32644460836 scopus 로고    scopus 로고
    • Expression of dihydrodiol dehydrogenase plays important roles in apoptosis- and drug-resistance of A431 squamous cell carcinoma
    • K.C. Chow, M.P. Lu, and M.T. Wu Expression of dihydrodiol dehydrogenase plays important roles in apoptosis- and drug-resistance of A431 squamous cell carcinoma J. Dermatol. Sci. 41 3 2006 205 212
    • (2006) J. Dermatol. Sci. , vol.41 , Issue.3 , pp. 205-212
    • Chow, K.C.1    Lu, M.P.2    Wu, M.T.3
  • 31
    • 33947427509 scopus 로고    scopus 로고
    • Characterization of side population in thyroid cancer cell lines: Cancer stem-like cells are enriched partly but not exclusively
    • DOI 10.1210/en.2006-1553
    • N. Mitsutake, A. Iwao, K. Nagai, H. Namba, A. Ohtsuru, V. Saenko, and S. Yamashita Characterization of side population in thyroid cancer cell lines: cancer stem-like cells are enriched partly but not exclusively Endocrinology 148 4 2007 1797 1803 (Pubitemid 46457095)
    • (2007) Endocrinology , vol.148 , Issue.4 , pp. 1797-1803
    • Mitsutake, N.1    Iwao, A.2    Nagai, K.3    Namba, H.4    Ohtsuru, A.5    Saenko, V.6    Yamashita, S.7
  • 32
    • 70349991888 scopus 로고    scopus 로고
    • Induction of neoplastic transformation by ectopic expression of human aldo-keto reductase 1C isoforms in NIH3T3 cells
    • C.W. Chien, I.C. Ho, and T.C. Lee Induction of neoplastic transformation by ectopic expression of human aldo-keto reductase 1C isoforms in NIH3T3 cells Carcinogenesis 30 10 2009 1813 1820
    • (2009) Carcinogenesis , vol.30 , Issue.10 , pp. 1813-1820
    • Chien, C.W.1    Ho, I.C.2    Lee, T.C.3
  • 33
    • 4644249735 scopus 로고    scopus 로고
    • Ubiquitous induction of resistance to platinum drugs in human ovarian, cervical, germ-cell and lung carcinoma tumor cells overexpressing isoforms 1 and 2 of dihydrodiol dehydrogenase
    • DOI 10.1007/s00280-004-0815-0
    • H.B. Deng, M. Adikari, H.K. Parekh, and H. Simpkins Ubiquitous induction of resistance to platinum drugs in human ovarian, cervical, germ-cell and lung carcinoma tumor cells overexpressing isoforms 1 and 2 of dihydrodiol dehydrogenase Cancer Chemother. Pharmacol. 54 4 2004 301 307 (Pubitemid 39304424)
    • (2004) Cancer Chemotherapy and Pharmacology , vol.54 , Issue.4 , pp. 301-307
    • Deng, H.B.1    Adikari, M.2    Parekh, H.K.3    Simpkins, H.4
  • 34
    • 33947256988 scopus 로고    scopus 로고
    • Reversal of inflammation-associated dihydrodiol dehydrogenases (AKR1C1 and AKR1C2) overexpression and drug resistance in nonsmall cell lung cancer cells by wogonin and chrysin
    • H.W. Wang, C.P. Lin, J.H. Chiu, K.C. Chow, K.T. Kuo, C.S. Lin, and L.S. Wang Reversal of inflammation-associated dihydrodiol dehydrogenases (AKR1C1 and AKR1C2) overexpression and drug resistance in nonsmall cell lung cancer cells by wogonin and chrysin Int. J. Cancer 120 9 2007 2019 2027
    • (2007) Int. J. Cancer , vol.120 , Issue.9 , pp. 2019-2027
    • Wang, H.W.1    Lin, C.P.2    Chiu, J.H.3    Chow, K.C.4    Kuo, K.T.5    Lin, C.S.6    Wang, L.S.7
  • 35
    • 41049113672 scopus 로고    scopus 로고
    • Dihydrodiol dehydrogenases regulate the generation of reactive oxygen species and the development of cisplatin resistance in human ovarian carcinoma cells
    • DOI 10.1007/s00280-007-0554-0
    • J. Chen, M. Adikari, R. Pallai, H.K. Parekh, and H. Simpkins Dihydrodiol dehydrogenases regulate the generation of reactive oxygen species and the development of cisplatin resistance in human ovarian carcinoma cells Cancer Chemother. Pharmacol. 61 6 2008 979 987 (Pubitemid 351423125)
    • (2008) Cancer Chemotherapy and Pharmacology , vol.61 , Issue.6 , pp. 979-987
    • Chen, J.1    Adikari, M.2    Pallai, R.3    Parekh, H.K.4    Simpkins, H.5
  • 36
    • 33745902254 scopus 로고    scopus 로고
    • Infection of human papillomavirus and overexpression of dihydrodiol dehydrogenase in uterine cervical cancer
    • DOI 10.1016/j.ygyno.2005.12.009, PII S0090825805010619
    • M. Ueda, Y.C. Hung, J.T. Chen, S.H. Chiou, H.H. Huang, T.Y. Lin, Y. Terai, and K.C. Chow Infection of human papillomavirus and overexpression of dihydrodiol dehydrogenase in uterine cervical cancer Gynecol. Oncol. 102 2 2006 173 181 (Pubitemid 44041634)
    • (2006) Gynecologic Oncology , vol.102 , Issue.2 , pp. 173-181
    • Ueda, M.1    Hung, Y.-C.2    Chen, J.-T.3    Chiou, S.-H.4    Huang, H.-H.5    Lin, T.-Y.6    Terai, Y.7    Chow, K.-C.8
  • 37
    • 37349121900 scopus 로고    scopus 로고
    • Transcriptional regulation of aldo-keto reductase 1C1 in HT29 human colon cancer cells resistant to methotrexate: Role in the cell cycle and apoptosis
    • DOI 10.1016/j.bcp.2007.08.034, PII S0006295207005953
    • E. Selga, V. Noé, and C.J. Ciudad Transcriptional regulation of aldo-keto reductase 1C1 in HT29 human colon cancer cells resistant to methotrexate: role in the cell cycle and apoptosis Biochem. Pharmacol. 75 2 2008 414 426 (Pubitemid 350298467)
    • (2008) Biochemical Pharmacology , vol.75 , Issue.2 , pp. 414-426
    • Selga, E.1    Noe, V.2    Ciudad, C.J.3
  • 38
    • 34547692874 scopus 로고    scopus 로고
    • Human aldo-keto reductases: Function, gene regulation, and single nucleotide polymorphisms
    • DOI 10.1016/j.abb.2007.04.024, PII S0003986107002226
    • T.M. Penning, and J.E. Drury Human aldo-keto reductases: function, gene regulation, and single nucleotide polymorphisms Arch. Biochem. Biophys. 464 2 2007 241 250 (Pubitemid 47214569)
    • (2007) Archives of Biochemistry and Biophysics , vol.464 , Issue.2 , pp. 241-250
    • Penning, T.M.1    Drury, J.E.2
  • 39
    • 70249138697 scopus 로고    scopus 로고
    • Characterization of the cancer chemopreventive NRF2-dependent gene battery in human keratinocytes: Demonstration that the KEAP1-NRF2 pathway, and not the BACH1-NRF2 pathway, controls cytoprotection against electrophiles as well as redox-cycling compounds
    • A.K. MacLeod, M. McMahon, S.M. Plummer, L.G. Higgins, T.M. Penning, K. Igarashi, and J.D. Hayes Characterization of the cancer chemopreventive NRF2-dependent gene battery in human keratinocytes: demonstration that the KEAP1-NRF2 pathway, and not the BACH1-NRF2 pathway, controls cytoprotection against electrophiles as well as redox-cycling compounds Carcinogenesis 30 9 2009 1571 1580
    • (2009) Carcinogenesis , vol.30 , Issue.9 , pp. 1571-1580
    • MacLeod, A.K.1    McMahon, M.2    Plummer, S.M.3    Higgins, L.G.4    Penning, T.M.5    Igarashi, K.6    Hayes, J.D.7
  • 40
    • 0043095539 scopus 로고    scopus 로고
    • Human 20α-hydroxysteroid dehydrogenase: Crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids
    • DOI 10.1016/S0022-2836(03)00762-9
    • J.F. Couture, P. Legrand, L. Cantin, V. Luu-The, F. Labrie, and R. Breton Human 20α-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids J. Mol. Biol. 331 3 2003 593 604 (Pubitemid 36937148)
    • (2003) Journal of Molecular Biology , vol.331 , Issue.3 , pp. 593-604
    • Couture, J.-F.1    Legrand, P.2    Cantin, L.3    Luu-The, V.4    Labrie, F.5    Breton, R.6
  • 41
    • 49449097049 scopus 로고    scopus 로고
    • Selectivity determinants of inhibitor binding to human 20α-hydroxysteroid dehydrogenase: Crystal structure of the enzyme in ternary complex with coenzyme and the potent inhibitor 3,5-dichlorosalicylic acid
    • U. Dhagat, S. Endo, R. Sumii, A. Hara, and O. El-Kabbani Selectivity determinants of inhibitor binding to human 20α-hydroxysteroid dehydrogenase: crystal structure of the enzyme in ternary complex with coenzyme and the potent inhibitor 3,5-dichlorosalicylic acid J. Med. Chem. 51 15 2008 4844 4848
    • (2008) J. Med. Chem. , vol.51 , Issue.15 , pp. 4844-4848
    • Dhagat, U.1    Endo, S.2    Sumii, R.3    Hara, A.4    El-Kabbani, O.5
  • 42
    • 0036547847 scopus 로고    scopus 로고
    • Substrate specificity of human 3(20)α-hydroxysteroid dehydrogenase for neurosteroids and its inhibition by benzodiazepines
    • DOI 10.1248/bpb.25.441
    • N. Usami, T. Yamamoto, S. Shintani, S. Ishikura, Y. Higaki, Y. Katagiri, and A. Hara Substrate specificity of human 3(20)α-hydroxysteroid dehydrogenase for neurosteroids and its inhibition by benzodiazepines Biol. Pharm. Bull. 25 4 2002 441 445 (Pubitemid 40044660)
    • (2002) Biological and Pharmaceutical Bulletin , vol.25 , Issue.4 , pp. 441-445
    • Usami, N.1    Yamamoto, T.2    Shintani, S.3    Higaki, Y.4    Ishikura, S.5    Katagiri, Y.6    Hara, A.7
  • 44
    • 11244348953 scopus 로고    scopus 로고
    • Development of nonsteroidal anti-inflammatory drug analogs and steroid carboxylates selective for human aldo-keto reductase isoforms: Potential antineoplastic agents that work independently of cyclooxygenase isozymes
    • DOI 10.1124/mol.104.006569
    • D.R. Bauman, S.I. Rudnick, L.M. Szewczuk, Y. Jin, S. Gopishetty, and T.M. Penning Development of nonsteroidal anti-inflammatory drug analogs and steroid carboxylates selective for human aldo-keto reductase isoforms: potential antineoplastic agents that work independently of cyclooxygenase isozymes Mol. Pharmacol. 67 1 2005 60 68 (Pubitemid 40069966)
    • (2005) Molecular Pharmacology , vol.67 , Issue.1 , pp. 60-68
    • Bauman, D.R.1    Rudnick, S.I.2    Szewczuk, L.M.3    Jin, Y.4    Gopishetty, S.5    Penning, T.M.6
  • 45
    • 33748848304 scopus 로고    scopus 로고
    • Phytoestrogens as inhibitors of the human progesterone metabolizing enzyme AKR1C1
    • DOI 10.1016/j.mce.2006.08.001, PII S0303720706003807
    • P. Brozic, T. Smuc, S. Gobec, and T.L. Rizner Phytoestrogens as inhibitors of the human progesterone metabolizing enzyme AKR1C1 Mol. Cell. Endocrinol. 259 1-2 2006 30 42 (Pubitemid 44419585)
    • (2006) Molecular and Cellular Endocrinology , vol.259 , Issue.1-2 , pp. 30-42
    • Brozic, P.1    Smuc, T.2    Gobec, S.3    Rizner, T.L.4
  • 46
    • 64249160631 scopus 로고    scopus 로고
    • New cyclopentane derivatives as inhibitors of steroid metabolizing enzymes AKR1C1 and AKR1C3
    • B. Stefane, P. Brozic, M. Vehovc, T.L. Rizner, and S. Gobec New cyclopentane derivatives as inhibitors of steroid metabolizing enzymes AKR1C1 and AKR1C3 Eur. J. Med. Chem. 44 6 2009 2563 2571
    • (2009) Eur. J. Med. Chem. , vol.44 , Issue.6 , pp. 2563-2571
    • Stefane, B.1    Brozic, P.2    Vehovc, M.3    Rizner, T.L.4    Gobec, S.5
  • 47
    • 60249087561 scopus 로고    scopus 로고
    • Discovery of new inhibitors of aldo-keto reductase 1C1 by structure-based virtual screening
    • P. Brozic, S. Turk, T. Lanisnik Rizner, and S. Gobec Discovery of new inhibitors of aldo-keto reductase 1C1 by structure-based virtual screening Mol. Cell. Endocrinol. 301 1-2 2009 245 250
    • (2009) Mol. Cell. Endocrinol. , vol.301 , Issue.12 , pp. 245-250
    • Brozic, P.1    Turk, S.2    Lanisnik Rizner, T.3    Gobec, S.4
  • 48
    • 37349053079 scopus 로고    scopus 로고
    • A salicylic acid-based analogue discovered from virtual screening as a potent inhibitor of human 20α-hydroxysteroid dehydrogenase
    • DOI 10.2174/157340607782360399
    • U. Dhagat, V. Carbone, R.P. Chung, T. Matsunaga, S. Endo, A. Hara, and O. El-Kabbani A salicylic acid-based analogue discovered from virtual screening as a potent inhibitor of human 20α-hydroxysteroid dehydrogenase Med. Chem. 3 6 2007 546 550 (Pubitemid 350303069)
    • (2007) Medicinal Chemistry , vol.3 , Issue.6 , pp. 546-550
    • Dhagat, U.1    Carbone, V.2    Chung, R.P.T.3    Matsunaga, T.4    Endo, S.5    Hara, A.6    El-Kabbani, O.7
  • 49
    • 34447642375 scopus 로고    scopus 로고
    • Selectivity determinants of the aldose and aldehyde reductase inhibitor-binding sites
    • DOI 10.1007/s00018-007-6514-3
    • O. El-Kabbani, and A. Podjarny Selectivity determinants of the aldose and aldehyde reductase inhibitor-binding sites Cell. Mol. Life Sci. 64 15 2007 1970 1978 (Pubitemid 47094426)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.15 , pp. 1970-1978
    • El-Kabbani, O.1    Podjarny, A.2
  • 50
    • 23944478339 scopus 로고    scopus 로고
    • Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat: Implications for inhibitor binding and selectivity
    • DOI 10.1021/jm050412o
    • O. El-Kabbani, V. Carbone, C. Darmanin, M. Oka, A. Mitschler, A. Podjarny, C. Schulze-Briese, and R.P. Chung Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity J. Med. Chem. 48 17 2005 5536 5542 (Pubitemid 41209251)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.17 , pp. 5536-5542
    • El-Kabbani, O.1    Carbone, V.2    Darmanin, C.3    Oka, M.4    Mitschler, A.5    Podjarny, A.6    Schulze-Briese, C.7    Chung, R.P.-T.8
  • 51
    • 24744457100 scopus 로고    scopus 로고
    • Factorizing selectivity determinants of inhibitor binding toward aldose and aldehyde reductases: Structural and thermodynamic properties of the aldose reductase mutant Leu300Pro-fidarestat complex
    • DOI 10.1021/jm050424+
    • T. Petrova, H. Steuber, I. Hazemann, A. Cousido-Siah, A. Mitschler, R. Chung, M. Oka, G. Klebe, O. El-Kabbani, A. Joachimiak, and A. Podjarny Factorizing selectivity determinants of inhibitor binding toward aldose and aldehyde reductases: structural and thermodynamic properties of the aldose reductase mutant Leu300Pro-Fidarestat complex J. Med. Chem. 48 18 2005 5659 5665 (Pubitemid 41298340)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.18 , pp. 5659-5665
    • Petrova, T.1    Steuber, H.2    Hazemann, I.3    Cousido-Siah, A.4    Mitschler, A.5    Chung, R.6    Oka, M.7    Klebe, G.8    El-Kabbani, O.9    Joachimiak, A.10    Podjarny, A.11
  • 52
    • 66249105304 scopus 로고    scopus 로고
    • Structure-guided design, synthesis, and evaluation of salicylic acid-based inhibitors targeting a selectivity pocket in the active site of human 20α-hydroxysteroid dehydrogenase (AKR1C1)
    • O. El-Kabbani, P.J. Scammells, J. Gosling, U. Dhagat, S. Endo, T. Matsunaga, M. Soda, and A. Hara Structure-guided design, synthesis, and evaluation of salicylic acid-based inhibitors targeting a selectivity pocket in the active site of human 20α-hydroxysteroid dehydrogenase (AKR1C1) J. Med. Chem. 52 10 2009 3259 3264
    • (2009) J. Med. Chem. , vol.52 , Issue.10 , pp. 3259-3264
    • El-Kabbani, O.1    Scammells, P.J.2    Gosling, J.3    Dhagat, U.4    Endo, S.5    Matsunaga, T.6    Soda, M.7    Hara, A.8
  • 53
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • DOI 10.1021/jm00145a002
    • P.J. Goodford A computational procedure for determining energetically favorable binding sites on biologically important macromolecules J. Med. Chem. 28 7 1985 849 857 (Pubitemid 15012490)
    • (1985) Journal of Medicinal Chemistry , vol.28 , Issue.7 , pp. 849-857
    • Goodford, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.