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Volumn 46, Issue 13, 2003, Pages 2580-2588

Inhibition of Cdc25 phosphatases by indolyldihydroxyquinones

Author keywords

[No Author keywords available]

Indexed keywords

2,5 DIHYDROXY 3 (1H INDOL 3 YL)[1,4]BENZOQUINONE; 2,5 DIHYDROXY 3 (4,6 DICHLORO 7 FARNESYL 1H INDOL 3 YL)[1,4]BENZOQUINONE; 2,5 DIHYDROXY 3 (7 FARNESYL 1H INDOL 3 YL)[1,4]BENZOQUINONE; 3 [4,6 DICHLORO 7 (3 METHYLBUT 2 ENYL) 1H INDOL 3 YL] 2,5 DIHYDROXY [1,4]BENZOQUINONE; 3 [6 CHLORO 7 (3 METHYLBUT 2 ENYL) 1H INDOL 3 YL] 2,5 DIHYDROXY [1,4]BENZOQUINONE; COMPOUND 5; ENZYME INHIBITOR; INDOLYLDIHYDROXYQUINONE; ISOENZYME; NSC 668394; NSC 95397; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE A; PROTEIN TYROSINE PHOSPHATASE B; PROTEIN TYROSINE PHOSPHATASE C; QUINONE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0037777745     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm0300835     Document Type: Article
Times cited : (68)

References (53)
  • 1
    • 0029317904 scopus 로고
    • Cyclin-dependent protein kinases: Key regulators of the eukaryotic cell cycle
    • Nigg, E. A. Cyclin-Dependent Protein Kinases: Key Regulators of the Eukaryotic Cell Cycle. BioEssays 1995, 17, 471-480.
    • (1995) BioEssays , vol.17 , pp. 471-480
    • Nigg, E.A.1
  • 2
    • 0033629383 scopus 로고    scopus 로고
    • Cell cycle regulation by the Cdc25 phosphatase family
    • Nilsson, I.; Hoffman, I. Cell cycle regulation by the Cdc25 phosphatase family. Prog. Cell Cycle Res. 2000, 4, 107-114.
    • (2000) Prog. Cell Cycle Res. , vol.4 , pp. 107-114
    • Nilsson, I.1    Hoffman, I.2
  • 4
    • 0029779280 scopus 로고    scopus 로고
    • Cdc25 cell-cycle phosphatase as a target of c-myc
    • Galaktionov, K.; Chen, X.; Beach, D. Cdc25 cell-cycle phosphatase as a target of c-myc. Nature 1996, 382, 511-517.
    • (1996) Nature , vol.382 , pp. 511-517
    • Galaktionov, K.1    Chen, X.2    Beach, D.3
  • 6
    • 0030681035 scopus 로고    scopus 로고
    • Overexpression of cyclin-dependent kinase-activating CDC25B phosphatase in human gastric carcinomas
    • Kudo, Y.; Yasui, W.; Ue, T.; Yamamoto, S.; Yokozaki, H.; Nikai, H.; Tahara, E. Overexpression of cyclin-dependent kinase-activating CDC25B phosphatase in human gastric carcinomas. Jpn. J. Cancer Res. 1997, 88, 9947-952.
    • (1997) Jpn. J. Cancer Res. , vol.88 , pp. 9947-9952
    • Kudo, Y.1    Yasui, W.2    Ue, T.3    Yamamoto, S.4    Yokozaki, H.5    Nikai, H.6    Tahara, E.7
  • 7
    • 0031853064 scopus 로고    scopus 로고
    • Elevated expression of the cdc25A protein phosphatase in colon cancer
    • Dixon, D.; Moyana, T.; King, M. J. Elevated expression of the cdc25A protein phosphatase in colon cancer. Exp. Cell Res. 1998, 240, 236-243.
    • (1998) Exp. Cell Res. , vol.240 , pp. 236-243
    • Dixon, D.1    Moyana, T.2    King, M.J.3
  • 9
    • 0032530140 scopus 로고    scopus 로고
    • Over-expression of cdc25A and cdc25B is frequent in primary nonsmall cell lung cancer but is not associated with overexpression of c-myc
    • Wu, W. G.; Fan, Y. H.; Kemp, B. L.; Walsh, G.; Mao, L. Over-expression of cdc25A and cdc25B is frequent in primary nonsmall cell lung cancer but is not associated with overexpression of c-myc. Cancer Res. 1998, 58, 4082-4085.
    • (1998) Cancer Res. , vol.58 , pp. 4082-4085
    • Wu, W.G.1    Fan, Y.H.2    Kemp, B.L.3    Walsh, G.4    Mao, L.5
  • 11
    • 0033549866 scopus 로고    scopus 로고
    • Induction of mammary gland hyperplasia in transgenic mice overexpressing human Cdc25B
    • Ma, Z.-Q.; Chua, S. S.; DeMayo, F. J.; Tsai, S. Y. Induction of mammary gland hyperplasia in transgenic mice overexpressing human Cdc25B. Oncogene 1999, 18, 4564-4576.
    • (1999) Oncogene , vol.18 , pp. 4564-4576
    • Ma, Z.-Q.1    Chua, S.S.2    DeMayo, F.J.3    Tsai, S.Y.4
  • 13
    • 0033181209 scopus 로고    scopus 로고
    • Vitamin K3 induces cell cycle arrest and cell death by inhibiting cdc25 phosphatase
    • Wu, F. Y.-H.; Sun, T. P. Vitamin K3 induces cell cycle arrest and cell death by inhibiting cdc25 phosphatase. Eur. J. Cancer 1999, 35, 1388-1393.
    • (1999) Eur. J. Cancer , vol.35 , pp. 1388-1393
    • Wu, F.Y.-H.1    Sun, T.P.2
  • 14
    • 0033604449 scopus 로고    scopus 로고
    • Dual G1 and G2/M phase inhibition by SC-9, a combinatorially derived Cdc25 phosphatase inhibitor
    • Tamura, K.; Rice, R. L.; Wipf, P.; Lazo, J. S. Dual G1 and G2/M phase inhibition by SC-9, a combinatorially derived Cdc25 phosphatase inhibitor. Oncogene 1999, 18, 6989-6996.
    • (1999) Oncogene , vol.18 , pp. 6989-6996
    • Tamura, K.1    Rice, R.L.2    Wipf, P.3    Lazo, J.S.4
  • 15
    • 0034163387 scopus 로고    scopus 로고
    • Cdc25 inhibition and cell cycle arrest by a synthetic thioalkyl vitamin K analogue
    • Tamura, K.; Southwick, E. C.; Kerns, J.; Rosi, K.; Carr, B. I.; Wilcox, C.; Lazo, J. S. Cdc25 inhibition and cell cycle arrest by a synthetic thioalkyl vitamin K analogue. Cancer Res. 2000, 60, 1317-1325.
    • (2000) Cancer Res. , vol.60 , pp. 1317-1325
    • Tamura, K.1    Southwick, E.C.2    Kerns, J.3    Rosi, K.4    Carr, B.I.5    Wilcox, C.6    Lazo, J.S.7
  • 17
    • 0032547896 scopus 로고    scopus 로고
    • Novel Cdc25A phosphatase inhibitors from pyrolysis of 3-alpha-azido-B-homo-6-oxa-4-cholesten-7-one on silica gel
    • Peng, H.; Zalkow, L. H.; Abraham, R. T.; Powis, G. Novel Cdc25A phosphatase inhibitors from pyrolysis of 3-alpha-azido-B-homo-6-oxa-4-cholesten-7-one on silica gel. J. Med. Chem. 1998, 41, 4677-4680.
    • (1998) J. Med. Chem. , vol.41 , pp. 4677-4680
    • Peng, H.1    Zalkow, L.H.2    Abraham, R.T.3    Powis, G.4
  • 18
    • 0037100740 scopus 로고    scopus 로고
    • Targeting the cell cycle for cancer therapy
    • Carnero, A. Targeting the cell cycle for cancer therapy. Br. J. Cancer 2002, 87, 129-133.
    • (2002) Br. J. Cancer , vol.87 , pp. 129-133
    • Carnero, A.1
  • 19
    • 0036884693 scopus 로고    scopus 로고
    • Dual-specificity phosphatases as targets for antineoplastic agents
    • Lyon, M. A.; Ducruet, A. P.; Wipf, P.; Lazo, J. S. Dual-specificity phosphatases as targets for antineoplastic agents. Nat. Rev. Drug Discovery 2002, 1, 961-976.
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 961-976
    • Lyon, M.A.1    Ducruet, A.P.2    Wipf, P.3    Lazo, J.S.4
  • 20
    • 0029816291 scopus 로고    scopus 로고
    • Dysidiolide: A novel protein phosphatase inhibitor from Caribbean Spongs Diysidea ehterria de Laubenfels
    • Gunasekera, S. P.; McCarthy, P. J.; Kelly-Broger, M.; Lobkovsky, E.; Clardy, J. Dysidiolide: A novel protein phosphatase inhibitor from Caribbean Spongs Diysidea ehterria de Laubenfels. J. Am. Chem. Soc. 1996, 118, 8759-8760.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8759-8760
    • Gunasekera, S.P.1    McCarthy, P.J.2    Kelly-Broger, M.3    Lobkovsky, E.4    Clardy, J.5
  • 21
    • 0033530145 scopus 로고    scopus 로고
    • Dysidiolide and related γ-hydroxy butenolide compounds as inhibitors of the protein tyrosine phosphatase, Cdc25
    • Blanchard, J. L.; Epstein, D. M.; Boisclair, M. D.; Rudolph, J.; Pal, K. Dysidiolide and Related γ-Hydroxy Butenolide Compounds as Inhibitors of the Protein Tyrosine Phosphatase, Cdc25. Bioorg. Med. Chem. Lett. 1999, 9, 2537-2538.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 2537-2538
    • Blanchard, J.L.1    Epstein, D.M.2    Boisclair, M.D.3    Rudolph, J.4    Pal, K.5
  • 23
    • 0027337571 scopus 로고
    • Vitamin K3 inhibits growth of human hepatoma HepG2 cells by decreasing activities of both p34cdc2 kinase and phosphatase
    • Juan, C. C.; Wu, F. Y. Vitamin K3 inhibits growth of human hepatoma HepG2 cells by decreasing activities of both p34cdc2 kinase and phosphatase. Biochem. Biophys. Res. Comm. 1993, 190, 907-913.
    • (1993) Biochem. Biophys. Res. Comm. , vol.190 , pp. 907-913
    • Juan, C.C.1    Wu, F.Y.2
  • 24
    • 0031471026 scopus 로고    scopus 로고
    • A targeted library of small-molecule, tyrosine, and dual-specificity phosphatase inhibitors derived from a rational core design and random side chain variations
    • Rice, R. L.; Rusnak, J. M.; Yokokawa, F.; Messner, D. J.; Boynton, A. L.; Wipf, P.; Lazo, J. S. A targeted library of small-molecule, tyrosine, and dual-specificity phosphatase inhibitors derived from a rational core design and random side chain variations. Biochem. 1997, 36, 15965-15974.
    • (1997) Biochem. , vol.36 , pp. 15965-15974
    • Rice, R.L.1    Rusnak, J.M.2    Yokokawa, F.3    Messner, D.J.4    Boynton, A.L.5    Wipf, P.6    Lazo, J.S.7
  • 25
    • 0033523644 scopus 로고    scopus 로고
    • Generation of an Ugi library of phosphate mimic-containing compounds and identification of novel dual specificity phosphatase inhibitors
    • Bergnes, G.; Gilliam, C. L.; Boisclair, M. D.; Blanchard, J. L.; Blake, K. V.; Epstein, D. M.; Pal, K. Generation of an Ugi library of phosphate mimic-containing compounds and identification of novel dual specificity phosphatase inhibitors. Bioorg. Med. Chem. Lett. 1999, 9, 2849-2854.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 2849-2854
    • Bergnes, G.1    Gilliam, C.L.2    Boisclair, M.D.3    Blanchard, J.L.4    Blake, K.V.5    Epstein, D.M.6    Pal, K.7
  • 27
    • 0035935711 scopus 로고    scopus 로고
    • Discovery and biological evaluation of a new family of potent inhibitors of the dual specificity protein phosphatase Cdc25
    • Lazo, J. S.; Aslan, D. C.; Southwick, E. C.; Cooley, K. A.; Ducruet, A. P.; Joo, B.; Vogt, A.; Wipf, P. Discovery and biological evaluation of a new family of potent inhibitors of the dual specificity protein phosphatase Cdc25. J. Med. Chem. 2001, 44, 4042-4049.
    • (2001) J. Med. Chem. , vol.44 , pp. 4042-4049
    • Lazo, J.S.1    Aslan, D.C.2    Southwick, E.C.3    Cooley, K.A.4    Ducruet, A.P.5    Joo, B.6    Vogt, A.7    Wipf, P.8
  • 29
    • 0037032557 scopus 로고    scopus 로고
    • Dual G1 and G2 phase inhibition by a novel, selective Cdc25 inhibitor 7-chloro-6-(2-morpholin-4-ylethylamino)-quinoline-5,8-dione
    • Pu, L.; Amoscato, A. A.; Bier, M. E.; Lazo, J. S. Dual G1 and G2 Phase Inhibition by a Novel, Selective Cdc25 Inhibitor 7-Chloro-6-(2-morpholin-4-ylethylamino)-quinoline-5,8-dione. J. Biol. Chem. 2002, 277, 46877-46885.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46877-46885
    • Pu, L.1    Amoscato, A.A.2    Bier, M.E.3    Lazo, J.S.4
  • 30
    • 0037058883 scopus 로고    scopus 로고
    • The catalytic mechanism of Cdc25
    • Rudolph, J. The Catalytic Mechanism of Cdc25. Biochem. 2002, 41, 14613-14623.
    • (2002) Biochem. , vol.41 , pp. 14613-14623
    • Rudolph, J.1
  • 31
    • 0037036460 scopus 로고    scopus 로고
    • Redox regulation of Cdc25C
    • Savitsky, P. A.; Finkel, T. Redox regulation of Cdc25C. J. Biol. Chem. 2002, 277, 20535-20540.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20535-20540
    • Savitsky, P.A.1    Finkel, T.2
  • 33
    • 0032738102 scopus 로고    scopus 로고
    • Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of the cell cycle
    • Reynolds, R. A.; Yem, A. W.; Wolfe, C. L.; Deibel, M. R. J.; Chidester, C. G.; Watenpaugh, K. D. Crystal Structure of the Catalytic Subunit of Cdc25B Required for G2/M Phase Transition of the Cell Cycle. J. Mol. Biol. 1999, 293, 559-568.
    • (1999) J. Mol. Biol. , vol.293 , pp. 559-568
    • Reynolds, R.A.1    Yem, A.W.2    Wolfe, C.L.3    Deibel, M.R.J.4    Chidester, C.G.5    Watenpaugh, K.D.6
  • 34
    • 0035253383 scopus 로고    scopus 로고
    • Specificity of natural and artifical substrates for human Cdc25A
    • Rudolph, J.; Epstein, D.; Parker, L.; Eckstein, J. Specificity of natural and artifical substrates for human Cdc25A. Anal. Biochem. 2001, 289, 43-51.
    • (2001) Anal. Biochem. , vol.289 , pp. 43-51
    • Rudolph, J.1    Epstein, D.2    Parker, L.3    Eckstein, J.4
  • 35
    • 0037195656 scopus 로고    scopus 로고
    • Synthesis of 2,5-dihydroxy-3-(indol-3yl)benzoquinones by acid-catalyzed condensation of indoles with 2, 5 dichlorobenzoquinone
    • Pirrung, M. C.; Deng, L.; Li, Z.; Park, K. Synthesis of 2,5-dihydroxy-3-(indol-3yl)benzoquinones by acid-catalyzed condensation of indoles with 2, 5 dichlorobenzoquinone. J. Org. Chem. 2002.
    • (2002) J. Org. Chem.
    • Pirrung, M.C.1    Deng, L.2    Li, Z.3    Park, K.4
  • 36
    • 0041005418 scopus 로고    scopus 로고
    • Nitroarylamines via the vicarious nucleophilic substitution of hydrogen: Amination, alkylamination, and arylamination of nitroarenes with sulfenamides
    • Makosza, M.; Bjaleki, M. Nitroarylamines via the Vicarious Nucleophilic Substitution of Hydrogen: Amination, Alkylamination, and Arylamination of Nitroarenes with Sulfenamides. J. Org. Chem. 1998, 63, 4878-4888.
    • (1998) J. Org. Chem. , vol.63 , pp. 4878-4888
    • Makosza, M.1    Bjaleki, M.2
  • 37
    • 0038251538 scopus 로고
    • Copper(I) catalyzed replacement of iodine by chloride ion in halonitrobenzenes
    • Liedholm, B. Copper(I) catalyzed replacement of iodine by chloride ion in halonitrobenzenes. Acta Chem. Scand. 1971, 25, 113-117.
    • (1971) Acta Chem. Scand. , vol.25 , pp. 113-117
    • Liedholm, B.1
  • 38
    • 0033838318 scopus 로고    scopus 로고
    • Straightforward synthesis of new tetrahydroquinoline derivatives
    • DiFabrio, R.; Alvaro, G.; Bertani, B.; Giacobbe, S. Straightforward synthesis of new tetrahydroquinoline derivatives. Can. J. Chem. 2000, 78, 809-815.
    • (2000) Can. J. Chem. , vol.78 , pp. 809-815
    • DiFabrio, R.1    Alvaro, G.2    Bertani, B.3    Giacobbe, S.4
  • 39
    • 0034609567 scopus 로고    scopus 로고
    • Dual-specific Cdc25B phosphatase: In search of the catalytic acid
    • Chen, W.; Wilborn, M.; Rudolph, J. Dual-specific Cdc25B phosphatase: in search of the catalytic acid. Biochemistry 2000, 39, 10781-10789.
    • (2000) Biochemistry , vol.39 , pp. 10781-10789
    • Chen, W.1    Wilborn, M.2    Rudolph, J.3
  • 40
    • 0035960635 scopus 로고    scopus 로고
    • The C-terminal tail of the dual-specificity Cdc25B phosphatase mediates modular substrate recognition
    • Wilborn, M.; Free, S.; Ban, A.; Rudolph, J. The C-Terminal Tail of the Dual-Specificity Cdc25B Phosphatase Mediates Modular Substrate Recognition. Biochemistry 2001, 40, 14200-14206.
    • (2001) Biochemistry , vol.40 , pp. 14200-14206
    • Wilborn, M.1    Free, S.2    Ban, A.3    Rudolph, J.4
  • 41
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W. W. Statistical analysis of enzyme kinetic data. Methods Enzymol. 1979, 63, 103-138.
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 42
    • 0020600551 scopus 로고
    • Regulation of human histone gene expression: Kinetics of accumulation and changes in the rate of synthesis and in the half-lives of individual histone mRNAs during the HeLa cell cycle
    • Heintz, N.; Sive, H. L.; Roeder, R. G. Regulation of human histone gene expression: kinetics of accumulation and changes in the rate of synthesis and in the half-lives of individual histone mRNAs during the HeLa cell cycle. Mol. Cell. Biol. 1983, 3, 539-550.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 539-550
    • Heintz, N.1    Sive, H.L.2    Roeder, R.G.3
  • 44
    • 0029914039 scopus 로고    scopus 로고
    • Kinetic analysis of the catalytic domain of human Cdc25B
    • Gottlin, E.; Epstein, D. M.; Eckstein, J.; Dixon, J. Kinetic analysis of the catalytic domain of human Cdc25B. J. Biol. Chem. 1996, 272, 27445-27449.
    • (1996) J. Biol. Chem. , vol.272 , pp. 27445-27449
    • Gottlin, E.1    Epstein, D.M.2    Eckstein, J.3    Dixon, J.4
  • 45
    • 0023944408 scopus 로고
    • Redox cycling and sulphydryl arylation; their relative importance in the mechanism of quinone cytotoxicity to isolated hepatocytes
    • Gant, T. W.; Rao, D. N.; Mason, R. P.; Cohen, G. M. Redox cycling and sulphydryl arylation; their relative importance in the mechanism of quinone cytotoxicity to isolated hepatocytes. Chem. Biol. Interact. 1988, 65, 157-173.
    • (1988) Chem. Biol. Interact. , vol.65 , pp. 157-173
    • Gant, T.W.1    Rao, D.N.2    Mason, R.P.3    Cohen, G.M.4
  • 49
    • 0345534590 scopus 로고    scopus 로고
    • Hydrogen bonding and molecular vibrations of 2,5-dihydroxy-1,4-benzoquinone
    • Szabó, Z.; Kovács, A. Hydrogen bonding and molecular vibrations of 2,5-dihydroxy-1,4-benzoquinone. J. Mol. Struct. 1999, 510, 215-225.
    • (1999) J. Mol. Struct. , vol.510 , pp. 215-225
    • Szabó, Z.1    Kovács, A.2
  • 50
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of haemoglobin on its biochemical and other systems
    • Hill, A. V. The possible effects of the aggregation of the molecules of haemoglobin on its biochemical and other systems. J. Physiol. (London) 1910, 40, iv-vii.
    • (1910) J. Physiol. (London) , vol.40
    • Hill, A.V.1
  • 51
    • 0001314221 scopus 로고
    • The hemoglobin system. VI. The oxygen dissociation curve of hemoglobin
    • Adair, G. S. The hemoglobin system. VI. The oxygen dissociation curve of hemoglobin. Chemistry 1925, 63, 529-545.
    • (1925) Chemistry , vol.63 , pp. 529-545
    • Adair, G.S.1
  • 52
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual high-throughput screening
    • McGovern, S. L.; Caselli, E.; Grigorieff, N.; Shoichet, B. K. A Common Mechanism Underlying Promiscuous Inhibitors from Virtual and High-Throughput Screening. J. Med. Chem. 2002, 1712-1722.
    • (2002) J. Med. Chem. , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4


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