메뉴 건너뛰기




Volumn 301, Issue 1-2, 2009, Pages 245-250

Discovery of new inhibitors of aldo-keto reductase 1C1 by structure-based virtual screening

Author keywords

AKR1C1 inhibitors; eHiTS; NCI "Diversity Set"; Virtual high throughput screening

Indexed keywords

ALDO KETO REDUCTASE 1C1 INHIBITOR; ENZYME INHIBITOR; NSC 1012; NSC 10460; NSC 116702; NSC 128609; NSC 13987; NSC 18877; NSC 23583; NSC 28136; NSC 282027; NSC 28311; NSC 292213; NSC 31698; NSC 327705; NSC 328087; NSC 33052; NSC 34352; NSC 35489; NSC 36369; NSC 371684; NSC 371876; NSC 371884; NSC 372046; NSC 41550; NSC 41663; NSC 42384; NSC 47932; NSC 48168; NSC 48708; NSC 5844; NSC 67690; NSC 74702; NSC 7510; NSC 7810; NSC371884; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 60249087561     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2008.08.002     Document Type: Article
Times cited : (10)

References (19)
  • 1
    • 11244348953 scopus 로고    scopus 로고
    • Development of non-steroidal anti-inflammatory drug (NSAID) analogs and steroid carboxylates selective for human aldo-keto reductase isoforms: potential antineoplastic agents that work independently of cyclooxygenase isozymes
    • Bauman D.R., Rudnick S., Szewczuk L.M., Jin Y., Gopishetty S., and Penning T.M. Development of non-steroidal anti-inflammatory drug (NSAID) analogs and steroid carboxylates selective for human aldo-keto reductase isoforms: potential antineoplastic agents that work independently of cyclooxygenase isozymes. Mol. Pharmacol. 67 (2005) 60-68
    • (2005) Mol. Pharmacol. , vol.67 , pp. 60-68
    • Bauman, D.R.1    Rudnick, S.2    Szewczuk, L.M.3    Jin, Y.4    Gopishetty, S.5    Penning, T.M.6
  • 2
    • 33748848304 scopus 로고    scopus 로고
    • Phytoestrogens as inhibitors of the human progesterone metabolizing enzyme AKR1C1
    • Brožič P., Šmuc T., Gobec S., and Lanišnik Rižner T. Phytoestrogens as inhibitors of the human progesterone metabolizing enzyme AKR1C1. Mol. Cell. Endocrinol. 259 (2006) 30-42
    • (2006) Mol. Cell. Endocrinol. , vol.259 , pp. 30-42
    • Brožič, P.1    Šmuc, T.2    Gobec, S.3    Lanišnik Rižner, T.4
  • 3
    • 0036006774 scopus 로고    scopus 로고
    • Expression, crystallization and preliminary X-ray analysis of human and rabbit 20α-hydroxysteroid dehydrogenases in complex with NADP(H) and various steroid substrates
    • Couture J.F., Cantin L., Legrand P., Luu-The V., Labrie F., and Breton R. Expression, crystallization and preliminary X-ray analysis of human and rabbit 20α-hydroxysteroid dehydrogenases in complex with NADP(H) and various steroid substrates. Acta Crystallogr. D 58 (2002) 135-139
    • (2002) Acta Crystallogr. D , vol.58 , pp. 135-139
    • Couture, J.F.1    Cantin, L.2    Legrand, P.3    Luu-The, V.4    Labrie, F.5    Breton, R.6
  • 4
    • 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
    • Couture J.-F., Legrand P., Cantin L., Luu-The V., Labrie F., and Breton R. 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 (2003) 593-604
    • (2003) J. Mol. Biol. , vol.331 , pp. 593-604
    • Couture, J.-F.1    Legrand, P.2    Cantin, L.3    Luu-The, V.4    Labrie, F.5    Breton, R.6
  • 5
    • 37349053079 scopus 로고    scopus 로고
    • A salicylic acid-based analogue discovered from virtual screening as a potent inhibitor of human 20α-hydroxysteroid dehydrogenase
    • Dhagat U., Carbone V., Chung R.P.-T., Matsunaga T., Endo S., Hara A., and El-Kabbani O. A salicylic acid-based analogue discovered from virtual screening as a potent inhibitor of human 20α-hydroxysteroid dehydrogenase. Med. Chem. 3 (2007) 546-550
    • (2007) Med. Chem. , vol.3 , 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
  • 6
    • 0035093784 scopus 로고    scopus 로고
    • Human types 1 and 3 3α-hydroxysteroid dehydrogenases: differential lability and tissue distribution
    • Dufort I., Labrie F., and Luu V. Human types 1 and 3 3α-hydroxysteroid dehydrogenases: differential lability and tissue distribution. J. Clin. Endocrinol. Metab. 86 (2001) 841-846
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 841-846
    • Dufort, I.1    Labrie, F.2    Luu, V.3
  • 7
    • 0001429526 scopus 로고    scopus 로고
    • Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase
    • Dufort I., Rheault P., Huang X.F., Soucy P., and Luu V. 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, V.5
  • 8
    • 0033539661 scopus 로고    scopus 로고
    • Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes
    • Griffin L.D., and Mellon S.H. Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 13512-13517
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13512-13517
    • Griffin, L.D.1    Mellon, S.H.2
  • 9
    • 39049094335 scopus 로고    scopus 로고
    • Virtual screening and its integration with modern drug design technologies
    • Guido R.V.C., Oliva G., and Andricopul A.D. Virtual screening and its integration with modern drug design technologies. Curr. Med. Chem. 15 (2008) 37-46
    • (2008) Curr. Med. Chem. , vol.15 , pp. 37-46
    • Guido, R.V.C.1    Oliva, G.2    Andricopul, A.D.3
  • 10
    • 0037324845 scopus 로고    scopus 로고
    • Selective and potent inhibitors of human 20α-hydroxysteroid dehydrogenase (AKR1C1) that metabolizes neurosteroids derived from progesterone
    • Higaki Y., Usami N., Shintani S., Ishikura S., El-Kabbani O., and Hara O. Selective and potent inhibitors of human 20α-hydroxysteroid dehydrogenase (AKR1C1) that metabolizes neurosteroids derived from progesterone. Chem. Biol. Interact. 143-144 (2003) 503-514
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 503-514
    • Higaki, Y.1    Usami, N.2    Shintani, S.3    Ishikura, S.4    El-Kabbani, O.5    Hara, O.6
  • 13
    • 0034836548 scopus 로고    scopus 로고
    • Metabolic conversion as a pre-receptor control mechanism for lipophilic hormones
    • Nobel S., Abrahamsen L., and Oppermann U. Metabolic conversion as a pre-receptor control mechanism for lipophilic hormones. Eur. J. Biochem. 268 (2001) 4113-4125
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4113-4125
    • Nobel, S.1    Abrahamsen, L.2    Oppermann, U.3
  • 14
    • 0034287545 scopus 로고    scopus 로고
    • Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of sex hormones
    • Penning T.M., Burczynski M.E., Jez J.M., Lin H.K., Ma H., Moore M., Palackal N., and Ratnam K. Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of sex hormones. Biochem. J. 351 (2000) 67-77
    • (2000) Biochem. J. , vol.351 , pp. 67-77
    • Penning, T.M.1    Burczynski, M.E.2    Jez, J.M.3    Lin, H.K.4    Ma, H.5    Moore, M.6    Palackal, N.7    Ratnam, K.8
  • 15
    • 0038013585 scopus 로고    scopus 로고
    • Hydroxysteroid dehydrogenases and pre-receptor regulation of steroid hormone action
    • Penning T.M. Hydroxysteroid dehydrogenases and pre-receptor regulation of steroid hormone action. Hum. Reprod. Update 9 (2003) 193-205
    • (2003) Hum. Reprod. Update , vol.9 , pp. 193-205
    • Penning, T.M.1
  • 16
    • 0025883535 scopus 로고
    • Characteristics of short-chain alcohol dehydrogenases and related enzymes
    • Persson B., Krook M., and Jornvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 200 (1991) 537-543
    • (1991) Eur. J. Biochem. , vol.200 , pp. 537-543
    • Persson, B.1    Krook, M.2    Jornvall, H.3
  • 17
    • 0036547847 scopus 로고    scopus 로고
    • Substrate specificity of human 3(20)alpha-hydroxysteroid dehydrogenase for neurosteroids and its inhibition by benzodiazepines
    • Usami N., Yamamoto T., Shintani S., Higaki Y., Ishikura S., Katagiri Y., and Hara A. Substrate specificity of human 3(20)alpha-hydroxysteroid dehydrogenase for neurosteroids and its inhibition by benzodiazepines. Biol. Pharm. Bull. 25 (2002) 441-445
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 441-445
    • Usami, N.1    Yamamoto, T.2    Shintani, S.3    Higaki, Y.4    Ishikura, S.5    Katagiri, Y.6    Hara, A.7
  • 19
    • 33749521613 scopus 로고    scopus 로고
    • eHiTS: an innovative approach to the docking and scoring function problems
    • Zsoldos Z., Simon A., Reid D., Sadjad B., and Johnson A.P. eHiTS: an innovative approach to the docking and scoring function problems. Curr. Prot. Pept. Sci. 7 (2006) 421-435
    • (2006) Curr. Prot. Pept. Sci. , vol.7 , pp. 421-435
    • Zsoldos, Z.1    Simon, A.2    Reid, D.3    Sadjad, B.4    Johnson, A.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.