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Volumn 47, Issue 12, 2004, Pages 2984-2994

Antiproliferative and phenotype-transforming antitumor agents derived from cysteine

Author keywords

[No Author keywords available]

Indexed keywords

4 BUTANOYL HYDROXAMATE; ANTINEOPLASTIC AGENT; BENZYLAMINE; CARBOXYLIC ACID; CYSTEINE; HYDROXAMIC ACID; PROTEIN P21; UNCLASSIFIED DRUG;

EID: 2542643987     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm030222i     Document Type: Article
Times cited : (36)

References (42)
  • 1
    • 0028116705 scopus 로고
    • Inducing differentiation of transformed cells with hybrid polar compounds: A cell cycle-dependent process
    • Marks, P. A.; Richon, V. M.; Kiyokawa, H.; Rifkind, R. A. Inducing differentiation of transformed cells with hybrid polar compounds: a cell cycle-dependent process. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 10251-10254.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 10251-10254
    • Marks, P.A.1    Richon, V.M.2    Kiyokawa, H.3    Rifkind, R.A.4
  • 2
    • 0029927535 scopus 로고    scopus 로고
    • Induced differentiation, the cell cycle and the treatment of cancer
    • Rifkind, R. A.; Richon, V. M.; Marks, P. A. Induced differentiation, the cell cycle and the treatment of cancer. Pharmacol. Ther. 1996, 69, 97-102.
    • (1996) Pharmacol. Ther. , vol.69 , pp. 97-102
    • Rifkind, R.A.1    Richon, V.M.2    Marks, P.A.3
  • 3
    • 0034816040 scopus 로고    scopus 로고
    • Differentiation therapy of human cancer: Basic science and clinical implications
    • Leszczyniecka, M.; Roberts, T.; Dent, P.; Grant, S.; Fisher P. B. Differentiation therapy of human cancer: basic science and clinical implications. Pharmacol. Ther. 2001, 90, 105-156.
    • (2001) Pharmacol. Ther. , vol.90 , pp. 105-156
    • Leszczyniecka, M.1    Roberts, T.2    Dent, P.3    Grant, S.4    Fisher, P.B.5
  • 4
    • 0036176617 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer treatment
    • Vigushin, D. M.; Coombes, R. C. Histone deacetylase inhibitors in cancer treatment. Anti-Cancer Drugs. 2002, 13, 1-13.
    • (2002) Anti-Cancer Drugs , vol.13 , pp. 1-13
    • Vigushin, D.M.1    Coombes, R.C.2
  • 8
    • 0034124166 scopus 로고    scopus 로고
    • A novel histone deacetylase inhibitor identified by high-troughput transcriptional screening of a compound library
    • Su, G. H.; Sohn, T. A.; Ryu, B.; Kern, S. E. A Novel Histone Deacetylase Inhibitor Identified by High-Troughput Transcriptional Screening of a Compound Library. Cancer Res. 2000, 60, 3137-3142.
    • (2000) Cancer Res. , vol.60 , pp. 3137-3142
    • Su, G.H.1    Sohn, T.A.2    Ryu, B.3    Kern, S.E.4
  • 9
  • 11
    • 0024996768 scopus 로고
    • Potent and specifik inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida, M.; Kijima, M.; Akita, M.; Beppu, T. Potent and specifik Inhibition of Mammalian Histone Deacetylase Both in Vivo and in Vitro by Trichostatin A. J. Biol. Chem. 1990, 265, 17174-17179.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 12
    • 0027378351 scopus 로고
    • Trapoxin, an antitumor cyclic tetrapeptide, is an irreverible inhibitor of mammalian histone deacetylase
    • Kijima, M.; Yoshida, M.; Sugita, K.; Horinouchi, S.; Beppu, T. Trapoxin, an Antitumor Cyclic Tetrapeptide, Is an Irreverible Inhibitor of Mammalian Histone Deacetylase. J. Biol. Chem. 1993, 268, 22429-22435.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22429-22435
    • Kijima, M.1    Yoshida, M.2    Sugita, K.3    Horinouchi, S.4    Beppu, T.5
  • 15
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin
    • Furumai, R.; Komatsu, Y.; Nishino, N.; Khochbin, S.; Yoshida, M.; Horinouchi, S. Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc. Nat. Acad. Sci. U.S.A. 2001, 98, 87-92.
    • (2001) Proc. Nat. Acad. Sci. U.S.A. , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 17
    • 0029795991 scopus 로고    scopus 로고
    • Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function
    • Taunton, J.; Collins, J. L.; Schreiber, S. L. Synthesis of Natural and Modified Trapoxins, Useful Reagents for Exploring Histone Deacetylase Function. J. Am. Chem. Soc. 1996, 118, 10412-10422.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10412-10422
    • Taunton, J.1    Collins, J.L.2    Schreiber, S.L.3
  • 19
    • 0035500502 scopus 로고    scopus 로고
    • Emerging roles for chromatin remodelling in cancer biology
    • Cairns B. R. Emerging roles for chromatin remodelling in cancer biology. Trends Cell Biol. 2001, 11, S15-S21.
    • (2001) Trends Cell Biol. , vol.11
    • Cairns, B.R.1
  • 20
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylase, transcriptional control, and cancer
    • Cress, W. D.; Seto, E. Histone Deacetylase, Transcriptional Control, and Cancer. J. Cell. Physiol. 2000, 184, 1-16.
    • (2000) J. Cell. Physiol. , vol.184 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 21
    • 0028201770 scopus 로고
    • Gene expression within a chromatin domain: The role of core histone hyperacetylation
    • Schlake, T.; Klehr-Wirth, D.; Yoshida, M.; Beppu, T.; Bode, J. Gene expression within a chromatin domain: the role of core histone hyperacetylation. Biochemistry 1994, 33, 4197-4206.
    • (1994) Biochemistry , vol.33 , pp. 4197-4206
    • Schlake, T.1    Klehr-Wirth, D.2    Yoshida, M.3    Beppu, T.4    Bode, J.5
  • 23
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • Grozinger, C. M.; Schreiber, S. L. Deacetylase Enzymes: Biological Functions and the Use of Small-Molecule Inhibitors. Chem. Biol. 2002, 9, 3-16.
    • (2002) Chem. Biol. , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 24
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • Johnstone, R. W. Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer. Nature Rev. 2002, 1, 287-299.
    • (2002) Nature Rev. , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 26
    • 0035662888 scopus 로고    scopus 로고
    • Structure of histone deacetylases: Insights into substrate recognition and catalysis
    • Marmorstein, R. Structure of Histone Deacetylases: Insights into Substrate Recognition and Catalysis. Structure 2001, 9, 1127-1133.
    • (2001) Structure , vol.9 , pp. 1127-1133
    • Marmorstein, R.1
  • 27
    • 0034086168 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors trigger a G2 checkpoint in normal cells that is defective in tumor cells
    • Qiu, L.; Burgess, A.; Fairlie, D. P.; Leonard, H.; Parsons, P. G.; Gabrielli, B. G. Histone deacetylase inhibitors trigger a G2 checkpoint in normal cells that is defective in tumor cells. Mol. Biol. Cell. 2000, 11, 2069-2083.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 2069-2083
    • Qiu, L.1    Burgess, A.2    Fairlie, D.P.3    Leonard, H.4    Parsons, P.G.5    Gabrielli, B.G.6
  • 29
    • 0025995325 scopus 로고
    • Flow cytometric and biochemical analysis of dose-dependent effects of sodium butyrate on human endometrial adenocarcinoma cells
    • Saito, S.; Crissman, H. A.; Nishijima, M.; Kagabu, T.; Nishiya, I.; Cram, L. S. Flow cytometric and biochemical analysis of dose-dependent effects of sodium butyrate on human endometrial adenocarcinoma cells. Cytometry 1991, 12, 757-764.
    • (1991) Cytometry , vol.12 , pp. 757-764
    • Saito, S.1    Crissman, H.A.2    Nishijima, M.3    Kagabu, T.4    Nishiya, I.5    Cram, L.S.6
  • 30
    • 0032989027 scopus 로고    scopus 로고
    • Anti-tumour activity in vitro and in vivo of selective differentiating agents containing hydroxamate
    • Qiu, L.; Kelso, M. J.; Hansen, C.; West, M. L.; Fairlie, D. P.; Parsons, P. G. Anti-tumour activity in vitro and in vivo of selective differentiating agents containing hydroxamate. Br. J. Cancer 1999, 80, 1252-1258.
    • (1999) Br. J. Cancer , vol.80 , pp. 1252-1258
    • Qiu, L.1    Kelso, M.J.2    Hansen, C.3    West, M.L.4    Fairlie, D.P.5    Parsons, P.G.6
  • 32
    • 0035325163 scopus 로고    scopus 로고
    • Histone acetylation and chromatin remodeling
    • Gregory, P. D.; Wagner, K.; Horz, W. Histone acetylation and chromatin remodeling. Exp. Cell. Res. 2001, 265, 195-202.
    • (2001) Exp. Cell. Res. , vol.265 , pp. 195-202
    • Gregory, P.D.1    Wagner, K.2    Horz, W.3
  • 33
    • 0029693220 scopus 로고    scopus 로고
    • Expression of a small fraction of cellular genes is changed in response to histone acetylation
    • Van-Lint, C.; Emiliani, S.; Verdin, E. Expression of a small fraction of cellular genes is changed in response to histone acetylation. Gene Express. 1996, 5, 245-253.
    • (1996) Gene Express , vol.5 , pp. 245-253
    • Van-Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 34
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon, V. M.; Sandhoff, T. W.; Rifkind, R. A.; Marks, P. A. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 10014-10019.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 37
    • 0023003386 scopus 로고
    • Selective toxicity of deoxyadenosine analogues in human melanoma cell lines
    • Parsons, P. G.; Bowman, E. P. W.; Blakely, R. L. Selective toxicity of deoxyadenosine analogues in human melanoma cell lines. Biochem. Pharmacol. 1986, 35, 4025-4029.
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 4025-4029
    • Parsons, P.G.1    Bowman, E.P.W.2    Blakely, R.L.3
  • 38
    • 0013543749 scopus 로고
    • Transforming growth factors produced by certain human tumour cells: Polypeptides that interact with epidermal growth factor receptors
    • Todaro, G. J.; Fryling, C.; De Larco, J. E. Transforming growth factors produced by certain human tumour cells: polypeptides that interact with epidermal growth factor receptors. Proc. Natl. Acad. Sci. U.S.A. 1980, 77, 5258-5262.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 5258-5262
    • Todaro, G.J.1    Fryling, C.2    De Larco, J.E.3
  • 39
    • 0033127758 scopus 로고    scopus 로고
    • Cell cycle delay, mitochondrial stress and uptake of hydrophobic cat-ions induced by sunscreens in cultured human cells
    • Xu, C.; Parsons, P. G. Cell cycle delay, mitochondrial stress and uptake of hydrophobic cat-ions induced by sunscreens in cultured human cells. Photochem. Photobiol. 1999, 69, 611-616.
    • (1999) Photochem. Photobiol. , vol.69 , pp. 611-616
    • Xu, C.1    Parsons, P.G.2
  • 40
    • 0017346890 scopus 로고
    • In situ detection of mycoplasma contamination in cell cultures by fluorescent Hoechst 33258 stain
    • Chen, T. R. In situ detection of mycoplasma contamination in cell cultures by fluorescent Hoechst 33258 stain. Exp. Cell. Res. 1977, 104, 255-262.
    • (1977) Exp. Cell. Res. , vol.104 , pp. 255-262
    • Chen, T.R.1
  • 42
    • 0025367455 scopus 로고
    • Comparison of in vitro anticancer-drug-screening data generated with a tetrazolium assay versus a protein assay against a diverse panel of human tumor cell lines
    • Rubinstein, L. V.; Shoemaker, R. H.; Paull, K. D.; Simon, R. M.; Tosini, S.; Skehan, P.; Scudiero, D. A.; Monks, A.; Boyd, M. R. Comparison of in vitro anticancer-drug-screening data generated with a tetrazolium assay versus a protein assay against a diverse panel of human tumor cell lines. J. Natl. Cancer Inst. 1990, 82, 1113-1118.
    • (1990) J. Natl. Cancer Inst. , vol.82 , pp. 1113-1118
    • Rubinstein, L.V.1    Shoemaker, R.H.2    Paull, K.D.3    Simon, R.M.4    Tosini, S.5    Skehan, P.6    Scudiero, D.A.7    Monks, A.8    Boyd, M.R.9


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