메뉴 건너뛰기




Volumn 191, Issue 1-3, 2011, Pages 261-268

Roles of rat and human aldo-keto reductases in metabolism of farnesol and geranylgeraniol

Author keywords

AKR1C15; AKR1C3; Alcohol dehydrogenase; Aldehyde dehydrogenase; Farnesol; Geranylgeraniol

Indexed keywords

ALDEHYDE DEHYDROGENASE; ALDO KETO REDUCTASE; ALDO KETO STEROID REDUCTASE 1B10; ALDO KETO STEROID REDUCTASE 1C15; ALDO KETO STEROID REDUCTASE 1C3; BETAMETHASONE; CARBOXYLIC ACID; FARNESOL; FLURBIPROFEN; GERANYLGERANIOL; INDOMETACIN; MECLOFENAMIC ACID; MEDROXYPROGESTERONE; MEFENAMIC ACID; STEROID REDUCTASE; TOLFENAMIC ACID; UNCLASSIFIED DRUG;

EID: 79957566848     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.12.017     Document Type: Conference Paper
Times cited : (51)

References (50)
  • 1
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • J.L. Goldstein, M.S. Brown, Regulation of the mevalonate pathway, Nature 343 (1990) 425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 2
    • 0032851111 scopus 로고    scopus 로고
    • Sterols and isoprenoids: Signaling molecules derived from the cholesterol biosynthetic pathway
    • DOI 10.1146/annurev.biochem.68.1.157
    • P.A. Edwards, J. Ericsson, Sterols and isoprenoids: signaling molecules derived from the cholesterol biosynthetic pathway, Annu. Rev. Biochem. 68 (1999) 157-185. (Pubitemid 29449190)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 157-185
    • Edwards, P.A.1    Ericsson, J.2
  • 3
    • 23044507603 scopus 로고    scopus 로고
    • Role of the isoprenoid pathway in ras transforming activity, cytoskeleton organization, cell proliferation and apoptosis
    • M. Bifulco, Role of the isoprenoid pathway in ras transforming activity, cytoskeleton organization, cell proliferation and apoptosis, Life Sci. 77 (2005) 1740-1749.
    • (2005) Life Sci. , vol.77 , pp. 1740-1749
    • Bifulco, M.1
  • 4
    • 0028035383 scopus 로고
    • Characterization of two distinct allyl pyrophosphatase activities from rat liver microsomes
    • V.S Bansal, S. Vaidya, Characterization of two distinct allyl pyrophosphatase activities from rat liver microsomes, Arch. Biochem. Biophys. 315 (1994) 393-399.
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 393-399
    • Bansal, V.S.1    Vaidya, S.2
  • 5
    • 0242331163 scopus 로고    scopus 로고
    • Isoprenoid alcohols restore protein isoprenylation in a time-dependent manner independent of protein synthesis
    • S.E. Ownby, R.J. Hohl, Isoprenoid alcohols restore protein isoprenylation in a time-dependent manner independent of protein synthesis, Lipids 38 (2003) 751-759.
    • (2003) Lipids , vol.38 , pp. 751-759
    • Ownby, S.E.1    Hohl, R.J.2
  • 7
    • 0036840528 scopus 로고    scopus 로고
    • Squalestatin 1-inducible expression of rat CYP2B: Evidence that an endogenous isoprenoid is an activator of the constitutive androstane receptor
    • T.A. Kocarek, N.A. Mercer-Haines, Squalestatin 1-inducible expression of rat CYP2B: evidence that an endogenous isoprenoid is an activator of the constitutive androstane receptor, Mol. Pharmacol. 62 (2002) 1177-1186.
    • (2002) Mol. Pharmacol. , vol.62 , pp. 1177-1186
    • Kocarek, T.A.1    Mercer-Haines, N.A.2
  • 8
    • 18344374193 scopus 로고    scopus 로고
    • Dual action of isoprenols from herbal medicines on both PPARγ and PPARα in 3T3-L1 adipocytes and HepG2 hepatocytes
    • DOI 10.1016/S0014-5793(02)02390-6, PII S0014579302023906
    • N. Takahashi, T. Kawada, T. Goto, T. Yamamoto, A. Taimatsu, N. Matsui, K. Kimura, M. Saito, M. Hosokawa, K. Miyashita, T. Fushiki, Dual action of isoprenols from herbal medicines on both PPARγ and PPARα in 3T3-L1 adipocytes and HepG2 hepatocytes, FEBS Lett. 514 (2002) 315-322. (Pubitemid 34273961)
    • (2002) FEBS Letters , vol.514 , Issue.2-3 , pp. 315-322
    • Takahashi, N.1    Kawada, T.2    Goto, T.3    Yamamoto, T.4    Taimatsu, A.5    Matsui, N.6    Kimura, K.7    Saito, M.8    Hosokawa, M.9    Miyashita, K.10    Fushiki, T.11
  • 9
    • 0030885520 scopus 로고    scopus 로고
    • The orphan nuclear receptor LXRα is positively and negatively regulated by distinct products of mevalonate metabolism
    • B.M. Forman, B. Ruan, J. Chen, G.J. Schroepfer Jr., R.M. Evans, The orphan nuclear receptor LXRα is positively and negatively regulated by distinct products of mevalonate metabolism, Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 10588-10593.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10588-10593
    • Forman, B.M.1    Ruan, B.2    Chen, J.3    Schroepfer Jr., G.J.4    Evans, R.M.5
  • 11
    • 0021051936 scopus 로고
    • Schroepfer metabolism of mevalonic acid in cell-free homogenates of bovine retinas. Formation of novel isoprenoid acids
    • S.J. Fliesler G.J.Jr., Schroepfer metabolism of mevalonic acid in cell-free homogenates of bovine retinas. Formation of novel isoprenoid acids, J. Biol. Chem. 258 (1983) 15062-15070.
    • (1983) J. Biol. Chem. , vol.258 , pp. 15062-15070
    • Fliesler, S.J.1    J Jr., G.2
  • 12
    • 0023874006 scopus 로고
    • Isopentenoid synthesis in isolated embryonic Drosophila cells. Farnesol catabolism and -oxidation
    • D. Gonzalez-Pacanowska, B. Arison, C.M. Havel, J.A. Watson, Isopentenoid synthesis in isolated embryonic Drosophila cells. Farnesol catabolism and - oxidation, J. Biol. Chem. 263 (1988) 1301-1306. (Pubitemid 18039931)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.3 , pp. 1301-1306
    • Gonzalez-Pacanowska, D.1    Arison, B.2    Havel, C.M.3    Watson, J.A.4
  • 13
    • 0013853867 scopus 로고
    • Dehydrogenation of trans-trans farnesol by horse liver alcohol dehydrogenase
    • G.R. Waller, Dehydrogenation of trans-trans farnesol by horse liver alcohol dehydrogenase, Nature 207 (1965) 1389-1390.
    • (1965) Nature , vol.207 , pp. 1389-1390
    • Waller, G.R.1
  • 14
    • 0025974055 scopus 로고
    • Human liver alcohol dehydrogenases catalyze the oxidation of the intermediary alcohols of the shunt pathway of mevalonate metabolism
    • W.M. Keung, Human liver alcohol dehydrogenases catalyze the oxidation of the intermediary alcohols of the shunt pathway of mevalonate metabolism, Biochem. Biophys. Res. Commun. 174 (1991) 701-707.
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 701-707
    • Keung, W.M.1
  • 15
    • 0036684886 scopus 로고    scopus 로고
    • Formation of (R)-2,3-dihydrogeranylgeranoic acid from geranylgeraniol in rat thymocytes
    • Y. Kodaira, K. Usui, I. Kon, H. Sagami, Formation of (R)-2,3- dihydrogeranylgeranoic acid from geranylgeraniol in rat thymocytes, J. Biochem. 132 (2002) 327-334. (Pubitemid 34947897)
    • (2002) Journal of Biochemistry , vol.132 , Issue.2 , pp. 327-334
    • Kodaira, Y.1    Usui, K.2    Kon, I.3    Sagami, H.4
  • 16
    • 0031550232 scopus 로고    scopus 로고
    • Rapid loss in the mitochondrial membrane potential during geranylgeranoic acid-induced apoptosis
    • DOI 10.1006/bbrc.1996.5883
    • Y. Shidoji, N. Nakamura, H. Moriwaki, Y. Muto, Rapid loss in the mitochondrial membrane potential during geranylgeranoic acid-induced apoptosis, Biochem. Biophys. Res. Commun. 230 (1997) 58-63. (Pubitemid 27210242)
    • (1997) Biochemical and Biophysical Research Communications , vol.230 , Issue.1 , pp. 58-63
    • Shidoji, Y.1    Nakamura, N.2    Moriwaki, H.3    Muto, Y.4
  • 19
    • 0030801368 scopus 로고    scopus 로고
    • Isolation and characterization of a prenylcysteine lyase from bovine brain
    • L. Zhang, W.R. Tschantz, P.J. Casey, Isolation and characterization of a prenylcysteine lyase from bovine brain, J. Biol. Chem. 272 (1997) 23354-23359.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23354-23359
    • Zhang, L.1    Tschantz, W.R.2    Casey, P.J.3
  • 20
    • 33746075254 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. Lysosomal metabolism of lipid-modified proteins
    • J.Y. Lu, S.L. Hofmann, Thematic review series: lipid posttranslational modifications. Lysosomal metabolism of lipid-modified proteins, J. Lipid Res. 47 (2006) 1352-1357.
    • (2006) J. Lipid Res. , vol.47 , pp. 1352-1357
    • Lu, J.Y.1    Hofmann, S.L.2
  • 21
    • 34548020351 scopus 로고    scopus 로고
    • Enzymatic characteristics of an aldo-keto reductase family protein (AKR1C15) and its localization in rat tissues
    • DOI 10.1016/j.abb.2007.05.008, PII S0003986107002536
    • S. Endo, T. Matsunaga, K. Horie, K. Tajima, Y. Bunai, V. Carbone, O. El-Kabbani, A. Hara, Enzymatic characteristics of an aldo-keto reductase family protein (AKR1C15) and its localization in rat tissues, Arch. Biochem. Biophys. 465 (2007) 136-147. (Pubitemid 47283988)
    • (2007) Archives of Biochemistry and Biophysics , vol.465 , Issue.1 , pp. 136-147
    • Endo, S.1    Matsunaga, T.2    Horie, K.3    Tajima, K.4    Bunai, Y.5    Carbone, V.6    El-Kabbani, O.7    Hara, A.8
  • 22
    • 3242787113 scopus 로고    scopus 로고
    • Attempted synthesis of casbene by intramolecular cyclopropanation
    • M.P. Doyle, M. Yan, Attempted synthesis of casbene by intramolecular cyclopropanation, ARKIVOC 2002 (2002) Part viii 180-185. (Pubitemid 38977528)
    • (2002) Arkivoc , vol.2002 , Issue.8 , pp. 180-185
    • Doyle, M.P.1    Yan, M.2
  • 23
    • 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, 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 (2009) 3259-3264.
    • (2009) J. Med. Chem. , vol.52 , 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
  • 25
    • 0035830422 scopus 로고    scopus 로고
    • Enzymatic characteristics and subcellular distribution of a short-chain dehydrogenase/ reductase family protein, P26h, in hamster testis and epididymis
    • S. Ishikura, N. Usami, K. Kitahara, T. Isaji, K. Oda, J. Nakagawa, A. Hara, Enzymatic characteristics and subcellular distribution of a short-chain dehydrogenase/ reductase family protein, P26h, in hamster testis and epididymis, Biochemistry 40 (2001) 214-224.
    • (2001) Biochemistry , vol.40 , pp. 214-224
    • Ishikura, S.1    Usami, N.2    Kitahara, K.3    Isaji, T.4    Oda, K.5    Nakagawa, J.6    Hara, A.7
  • 27
    • 34447639776 scopus 로고    scopus 로고
    • +-dependent 3α-hydroxysteroid dehydrogenase (AKR1C17): A member of the aldo-keto reductase family highly expressed in kidney cytosol
    • DOI 10.1016/j.abb.2007.04.003, PII S0003986107001828
    • M. Sanai, S. Endo, T. Matsunaga, S. Ishikura, K. Tajima, O. El-Kabbani, A. Hara, Rat NAD+-dependent 3α-hydroxysteroid dehydrogenase (AKR1C17): a member of the aldo - keto reductase family highly expressed in kidney cytosol, Arch. Biochem. Biophys. 464 (2007) 122-129. (Pubitemid 47088362)
    • (2007) Archives of Biochemistry and Biophysics , vol.464 , Issue.1 , pp. 122-129
    • Sanai, M.1    Endo, S.2    Matsunaga, T.3    Ishikura, S.4    Tajima, K.5    El-Kabbani, O.6    Hara, A.7
  • 28
    • 0042125492 scopus 로고    scopus 로고
    • Tetrahydrobiopterin is synthesized from 6-pyruvoyl-tetrahydropterin by the human aldo-keto reductase AKR1 family members
    • DOI 10.1016/S0003-9861(03)00295-9
    • T. Iino, M. Tabata, S. Takikawa, H. Sawada, H. Shintaku, S. Ishikura, A. Hara, Tetrahydrobiopterin is synthesized from 6-pyruvoyl-tetrahydropterin by the human aldo - keto reductase AKR1 family members, Arch. Biochem. Biophys. 416 (2003) 180-187. (Pubitemid 36957843)
    • (2003) Archives of Biochemistry and Biophysics , vol.416 , Issue.2 , pp. 180-187
    • Iino, T.1    Tabata, M.2    Takikawa, S.-I.3    Sawada, H.4    Shintaku, H.5    Ishikura, S.6    Hara, A.7
  • 29
    • 0032400498 scopus 로고    scopus 로고
    • Roles of the C-terminal domains of human dihydrodiol dehydrogenase isoforms in the binding of substrates and modulators: Probing with chimaeric enzymes
    • K. Matsuura, A. Hara, Y. Deyashiki, H. Iwasa, T. Kume, S. Ishikura, H. Shiraishi, Y. Katagiri, Roles of the C-terminal domains of human dihydrodiol dehydrogenase isoforms in the binding of substrates and modulators: probing with chimaeric enzymes, Biochem. J. 336 (1998) 429-436. (Pubitemid 28564401)
    • (1998) Biochemical Journal , vol.336 , Issue.2 , pp. 429-436
    • Matsuura, K.1    Hara, A.2    Deyashiki, Y.3    Iwasa, H.4    Kume, T.5    Ishikura, S.6    Shiraishi, H.7    Katagiri, Y.8
  • 30
    • 0032168199 scopus 로고    scopus 로고
    • Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA
    • H. Shiraishi, S. Ishikura, K. Matsuura, Y. Deyashiki, M. Ninomiya, S. Sakai, A. Hara, Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA, Biochem. J. 334 (1998) 399-405. (Pubitemid 28448583)
    • (1998) Biochemical Journal , vol.334 , Issue.2 , pp. 399-405
    • Shiraishi, H.1    Ishikura, S.2    Matsuura, K.3    Deyashiki, Y.4    Ninomiya, M.5    Sakai, S.6    Hara, A.7
  • 33
    • 79957552424 scopus 로고    scopus 로고
    • Protective effect of rat aldo-keto reductase (AKR1C15) on endothelial cell damage elicited by 4-hydroxy-2-nonenal
    • T. Matsunaga, Y. Shinoda, Y. Inoue, S. Endo, O. El-Kabbani, A. Hara, Protective effect of rat aldo-keto reductase (AKR1C15) on endothelial cell damage elicited by 4-hydroxy-2-nonenal, Chem. Biol. Interact. 191 (2011) 364-370.
    • (2011) Chem. Biol. Interact. , vol.191 , pp. 364-370
    • Matsunaga, T.1    Shinoda, Y.2    Inoue, Y.3    Endo, S.4    El-Kabbani, O.5    Hara, A.6
  • 34
    • 0021162297 scopus 로고
    • Rat liver aldehyde dehydrogenase. I. Isolation and characterization of four high Km normal liver isozymes
    • R. Lindahl, S. Evces, Rat liver aldehyde dehydrogenase. I. Isolation and characterization of four high Km normal liver isozymes, J. Biol. Chem. 259 (1984) 11986-11990.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11986-11990
    • Lindahl, R.1    Evces, S.2
  • 35
    • 0030936743 scopus 로고    scopus 로고
    • Human liver fatty aldehyde dehydrogenase: Microsomal localization, purification, and biochemical characterization
    • DOI 10.1016/S0304-4165(96)00126-2, PII S0304416596001262
    • T.L. Kelson, J.R. Secor McVoy, W.B. Rizzo, Human liver fatty aldehyde dehydrogenase: microsomal localization, purification, and biochemical characterization, Biochim. Biophys. Acta 1335 (1997) 99-110. (Pubitemid 27174510)
    • (1997) Biochimica et Biophysica Acta - General Subjects , vol.1335 , Issue.1-2 , pp. 99-110
    • Kelson, T.L.1    Secor, M.V.J.R.2    Rizzo, W.B.3
  • 36
    • 0024503296 scopus 로고
    • Oxidation of aldehydic products of lipid peroxidation by rat liver microsomal aldehyde dehydrogenase
    • DOI 10.1016/0003-9861(89)90081-7
    • D.Y. Mitchell, D.R. Petersen, Oxidation of aldehydic products of lipid peroxidation by rat liver microsomal aldehyde dehydrogenase, Arch. Biochem. Biophys. 269 (1989) 11-17. (Pubitemid 19052284)
    • (1989) Archives of Biochemistry and Biophysics , vol.269 , Issue.1 , pp. 11-17
    • Mitchell, D.Y.1    Petersen, D.R.2
  • 37
    • 0025935386 scopus 로고
    • Molecular cloning, sequencing, and expression of cDNA for rat liver microsomal aldehyde dehydrogenase
    • K. Miyauchi, R. Masaki, S. Taketani, A. Yamamoto, M. Akayama, Y. Tashiro, Molecular cloning, sequencing, and expression of cDNA for rat liver microsomal aldehyde dehydrogenase, J. Biol. Chem. 266 (1991) 19536-19542. (Pubitemid 21908263)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.29 , pp. 19536-19542
    • Miyauchi, K.1    Masaki, R.2    Taketani, S.3    Yamamoto, A.4    Akayama, M.5    Tashiro, Y.6
  • 38
    • 0023093115 scopus 로고
    • Characterization of three isoenzymes of rat alcohol dehydrogenase. Tissue distribution and physical and enzymatic properties
    • P. Julià, J. Farrés, X. Parés, Characterization of three isoenzymes of rat alcohol dehydrogenase. Tissue distribution and physical and enzymatic properties, Eur. J. Biochem. 162 (1987) 179-189.
    • (1987) Eur. J. Biochem. , vol.162 , pp. 179-189
    • Julià, P.1    Farrés, J.2    Parés, X.3
  • 40
    • 0027428440 scopus 로고
    • Physiological substrates for rat alcohol dehydrogenase classes: Aldehydes of lipid peroxidation, -hydroxyfatty acids, and retinoids
    • M.D Boleda, N. Saubi, J. Farrés, X. Parés, Physiological substrates for rat alcohol dehydrogenase classes: aldehydes of lipid peroxidation, -hydroxyfatty acids, and retinoids, Arch. Biochem. Biophys. 307 (1993) 85-90.
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 85-90
    • Boleda, M.D.1    Saubi, N.2    Farrés, J.3    Parés, X.4
  • 41
    • 0019989182 scopus 로고
    • Effects in vitro of medroxyprogesterone acetate on steroid metabolizing enzymes in the rat: Selective inhibition of 3α-hydroxysteroid oxidoreductase activity
    • DOI 10.1016/0022-4731(82)90122-4
    • A. Sunde, P.A. Rosness, K.B. Eik-Nes, Effects in vitro of medroxyprogesterone acetate on steroid metabolizing enzymes in the rat: selective inhibition of 3α-hydroxysteroid oxidoreductase activity, J. Steroid Biochem. 17 (1982) 197-203. (Pubitemid 12064469)
    • (1982) Journal of Steroid Biochemistry , vol.17 , Issue.2 , pp. 197-203
    • Sunde, A.1    Rosness, P.A.2    Eik-Nes, K.B.3
  • 42
    • 0021167976 scopus 로고
    • Purification and properties of a 3α-hydroxysteroid dehydrogenase of rat liver cytosol and its inhibition by anti-inflammatory drugs
    • T.M. Penning, I. Mukharji, S. Barrows, P. Talalay, Purification and properties of a 3α-hydroxysteroid dehydrogenase of rat liver cytosol and its inhibition by anti-inflammatory drugs, Biochem. J. 222 (1984) 601-611. (Pubitemid 14007827)
    • (1984) Biochemical Journal , vol.222 , Issue.3 , pp. 601-611
    • Penning, T.M.1    Mukharji, I.2    Barrows, S.3    Talalay, P.4
  • 43
    • 0021981334 scopus 로고
    • Indomethacin-sensitive 3α-hydroxysteroid dehydrogenase in rat tissues
    • T.E. Smithgall, T.M. Penning, Indomethacin-sensitive 3α- hydroxysteroid dehydrogenase in rat tissues, Biochem. Pharmacol. 34 (1985) 831-835.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 831-835
    • Smithgall, T.E.1    Penning, T.M.2
  • 44
    • 33645963469 scopus 로고    scopus 로고
    • Multiplicity of mammalian reductases for xenobiotic carbonyl compounds
    • T. Matsunaga, S. Shintani, A. Hara, Multiplicity of mammalian reductases for xenobiotic carbonyl compounds, Drug Metab. Pharmacokinet. 21 (2006) 1-18.
    • (2006) Drug Metab. Pharmacokinet. , vol.21 , pp. 1-18
    • Matsunaga, T.1    Shintani, S.2    Hara, A.3
  • 45
    • 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
    • D.R. Bauman, S.I. Rudnick, L.M. Szewczuk, Y. Jin, S. Gopishetty, 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 (2005) 60-68.
    • (2005) Mol. Pharmacol. , vol.67 , 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
  • 46
    • 26844480987 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs and their analogues as inhibitors of aldo-keto reductase AKR1C3: New lead compounds for the development of anticancer agents
    • DOI 10.1016/j.bmcl.2005.08.063, PII S0960894X05010917
    • S. Gobec, P. Brozic, T.L. Rizner, Nonsteroidal anti-inflammatory drugs and their analogues as inhibitors of aldo - keto reductase AKR1C3: new lead compounds for the development of anticancer agents, Bioorg. Med. Chem. Lett. 15 (2005) 5170-5175. (Pubitemid 41463641)
    • (2005) Bioorganic and Medicinal Chemistry Letters , vol.15 , Issue.23 , pp. 5170-5175
    • Gobec, S.1    Brozic, P.2    Rizner, T.L.3
  • 47
    • 77950037964 scopus 로고    scopus 로고
    • Chromene-3-carboxamide derivatives discovered from virtual screening as potent inhibitors of the tumour maker, AKR1B10
    • S. Endo, T. Matsunaga, K. Kuwata, H.T. Zhao, O. El-Kabbani, Y. Kitade, A. Hara, Chromene-3-carboxamide derivatives discovered from virtual screening as potent inhibitors of the tumour maker, AKR1B10, Bioorg. Med. Chem. 18 (2010) 2485-2490.
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 2485-2490
    • Endo, S.1    Matsunaga, T.2    Kuwata, K.3    Zhao, H.T.4    El-Kabbani, O.5    Kitade, Y.6    Hara, A.7
  • 48
    • 77952414106 scopus 로고    scopus 로고
    • Selective inhibition of the tumor marker AKR1B10 by antiinflammatory N-phenylanthranilic acids and glycyrrhetic acid
    • S. Endo, T. Matsunaga, M. Soda, K. Tajima, H.T. Zhao, O. El-Kabbani, A. Hara, Selective inhibition of the tumor marker AKR1B10 by antiinflammatory N-phenylanthranilic acids and glycyrrhetic acid, Biol. Pharm. Bull. 33 (2010) 886-890.
    • (2010) Biol. Pharm. Bull. , vol.33 , pp. 886-890
    • Endo, S.1    Matsunaga, T.2    Soda, M.3    Tajima, K.4    Zhao, H.T.5    El-Kabbani, O.6    Hara, A.7
  • 49
    • 61649103983 scopus 로고    scopus 로고
    • Steroid hormone transforming aldo - Keto reductases and cancer
    • T.M. Penning, M.C. Byrns, Steroid hormone transforming aldo - keto reductases and cancer, Ann. N.Y. Acad. Sci. 1155 (2009) 33-42.
    • (2009) Ann. N.Y. Acad. Sci. , vol.1155 , pp. 33-42
    • Penning, T.M.1    Byrns, M.C.2
  • 50
    • 70350778508 scopus 로고    scopus 로고
    • Aldo - Keto reductase family 1 member B1 inhibitors: Old drugs with new perspectives
    • J. Liu, G. Wen, D. Cao, Aldo - keto reductase family 1 member B1 inhibitors: old drugs with new perspectives, Recent Pat. Anticancer Drug Discov. 4 (2009) 246-253.
    • (2009) Recent Pat. Anticancer Drug Discov. , vol.4 , pp. 246-253
    • Liu, J.1    Wen, G.2    Cao, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.