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Volumn 2, Issue 4, 2003, Pages 401-408

Modulation of histone acetylation by [4-(acetylamino)-N-(2-amino-phenyl) benzamide] in HCT-8 colon carcinoma

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLDINALINE; ANTINEOPLASTIC AGENT; ENZYME INHIBITOR; HISTONE; HISTONE DEACETYLASE; PHENYLENEDIAMINE DERIVATIVE;

EID: 0141996376     PISSN: 15357163     EISSN: 15388514     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (62)

References (54)
  • 1
    • 0004050816 scopus 로고    scopus 로고
    • Ed. 3. Academic Press, Inc.: San Diego
    • Wolffe, A. P. Chromatin (Ed. 3). Academic Press, Inc.: San Diego, 1998.
    • (1998) Chromatin
    • Wolffe, A.P.1
  • 2
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung, P., Allis, C. D., and Sassone-Corsi, P. Signaling to chromatin through histone modifications. Cell, 103: 263-271, 2000.
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 3
    • 0033080794 scopus 로고    scopus 로고
    • Chromatin disruption and modification
    • DOI 10.1093/nar/27.3.711
    • Wolffe, A. P., and Hayes, J. J. Chromatin disruption and modification. Nucleic Acids Res., 27: 711-720, 1999. (Pubitemid 29209356)
    • (1999) Nucleic Acids Research , vol.27 , Issue.3 , pp. 711-720
    • Wolffe, A.P.1    Hayes, J.J.2
  • 4
    • 0033257094 scopus 로고    scopus 로고
    • Control of histone modifications
    • Davie, J. R, and Spencer, V. A. Control of histone modifications. J. Cell. Biochem. Supp., 32/33: 141-148, 1999. (Pubitemid 30041820)
    • (1999) Journal of Cellular Biochemistry , vol.76 , Issue.SUPPL. 32 AND 33 , pp. 141-148
    • Davie, J.R.1    Spencer, V.A.2
  • 5
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukaemia
    • DOI 10.1038/35895
    • Lin, R. J., Nagy, L., Inoue, S., Shao, W., Miller, W. H., Jr., and Evans, R. M. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature (Lond.), 391: 811-814, 1998. (Pubitemid 28099682)
    • (1998) Nature , vol.391 , Issue.6669 , pp. 811-814
    • Lin, R.J.1    Nagy, L.2    Inoue, S.3    Shao, W.4    Miller Jr., W.H.5    Evans, R.M.6
  • 9
    • 0031964479 scopus 로고    scopus 로고
    • Linking histone acetylation to transcriptional regulation
    • Mizzen, C. A., and Allis, C. D. Linking histone acetylation to transcriptional regulation. Cell. Mol. Life Sci., 54: 6-20, 1996.
    • (1996) Cell. Mol. Life Sci. , vol.54 , pp. 6-20
    • Mizzen, C.A.1    Allis, C.D.2
  • 10
    • 0034717183 scopus 로고    scopus 로고
    • Structure and function of a human TAF(II)250 double bromodomain module
    • DOI 10.1126/science.288.5470.1422
    • Jacobson, R. H., Ladurner, A. G., King, D. S., and Tjian, R. Structure and function of a human TAFII250 double bromodomain module. Science (Wash. DC), 288: 1422-1425, 2000. (Pubitemid 30366328)
    • (2000) Science , vol.288 , Issue.5470 , pp. 1422-1425
    • Jacobson, R.H.1    Ladurner, A.G.2    King, D.S.3    Tjian, R.4
  • 11
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • DOI 10.1038/20974
    • Dhalluin, C., Carlson, J. E., Zeng, L., He, C., Aggarwal, A. K., and Zhou, M. M. Structure and ligand of a histone acetyltransferase bromodomain. Nature (Lond.), 399: 491-496, 1999. (Pubitemid 29258857)
    • (1999) Nature , vol.399 , Issue.6735 , pp. 491-496
    • Dhalluin, C.1    Carlson, J.E.2    Zeng, L.3    He, C.4    Aggarwal, A.K.5    Zhou, M.-M.6
  • 12
    • 0032965152 scopus 로고    scopus 로고
    • Esa1p is an essential histone acetyltransferase required for cell cycle progression
    • Clarke, A. S., Lowell, J. E., Jacobson, S. J., and Pillus, L. Esa1p is an essential histone acetyltransferase required for cell cycle progression. Mol. Cell. Biol., 19: 2515-2526, 1999. (Pubitemid 29144495)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.4 , pp. 2515-2526
    • Clarke, A.S.1    Lowell, J.E.2    Jacobson, S.J.3    Pillus, L.4
  • 14
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylases, transcriptional control, and cancer
    • DOI 10.1002/(SICI)1097-4652(200007)184:1<1::AID-JC
    • Cress, W. D., and Seto, E. Histone deacetylases, transcriptional control, and cancer. J. Cell. Physiol., 184: 1-16, 2000. (Pubitemid 30349623)
    • (2000) Journal of Cellular Physiology , vol.184 , Issue.1 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 15
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C. A., and Schreiber, S. L. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science (Wash. DC), 272: 408-411, 1996. (Pubitemid 26138177)
    • (1996) Science , vol.272 , Issue.5260 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 16
    • 0029974613 scopus 로고    scopus 로고
    • Modulation of growth and differentiation of human colon carcinoma cells by histone deacetylase inhibitory trichostatins
    • Li, X., Yoshida, M., Beppu, T., and Lotan, R. Modulation of growth and differentiation of human colon carcinoma cell by histone deacetylase inhibitory trichostatins. Int. J. Oncol., 8: 431-437, 1996. (Pubitemid 26083101)
    • (1996) International Journal of Oncology , vol.8 , Issue.3 , pp. 431-437
    • Li, X.1    Yoshida, M.2    Beppu, T.3    Lotan, R.4
  • 17
    • 0029294663 scopus 로고
    • TSA and trapoxin: Novel chemical probes for the role of histone acetylation in chromatin structures and function
    • Yoshida, M., Horinouchi, S., and Beppu, T. TSA and trapoxin: novel chemical probes for the role of histone acetylation in chromatin structures and function. Bioessays, 17: 423-430, 1995.
    • (1995) Bioessays , vol.17 , pp. 423-430
    • Yoshida, M.1    Horinouchi, S.2    Beppu, T.3
  • 18
    • 0029795991 scopus 로고    scopus 로고
    • Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function
    • DOI 10.1021/ja9615841
    • Taunton, J., Collins, J. L., and Schreiber, S. Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function. J. Am. Chem. Soc., 118: 10412-10422, 1996. (Pubitemid 26381223)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.43 , pp. 10412-10422
    • Taunton, J.1    Collins, J.L.2    Schreiber, S.L.3
  • 20
    • 0033303876 scopus 로고    scopus 로고
    • Hybrid polar inducers of transformed cell differentiation/apoptosis. From the cell to the clinic
    • Paris
    • Marks, P. A., Richon, V. M., Breslow, R., and Rifkind, R. A. Hybrid polar inducers of transformed cell differentiation/apoptosis. From the cell to the clinic. C. R. Acad. Sci. (Paris), 322: 161-165, 1999.
    • (1999) C. R. Acad. Sci. , vol.322 , pp. 161-165
    • Marks, P.A.1    Richon, V.M.2    Breslow, R.3    Rifkind, R.A.4
  • 23
    • 0033523895 scopus 로고    scopus 로고
    • Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation
    • DOI 10.1021/jm991091h
    • Jung, M., Brosch, G., Kölle, D., Scherf, H., Gerhäuser, C., and Loidl, P. Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation. J. Med. Chem., 42: 4669-4679, 1999. (Pubitemid 29530020)
    • (1999) Journal of Medicinal Chemistry , vol.42 , Issue.22 , pp. 4669-4679
    • Jung, M.1    Brosch, G.2    Kolle, D.3    Scherf, H.4    Gerhauser, C.5    Loidl, P.6
  • 24
    • 0034596309 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Inducers of differentiation or apoptosis of transformed cells
    • Marks, P. A., Richon, V. M., and Rifkind, R. A. Histone deacetylase inhibitors: inducers of differentiation or apoptosis of transformed cells. J. Natl. Cancer Inst. (Bethesda), 92: 1210-1216, 2000. (Pubitemid 30627729)
    • (2000) Journal of the National Cancer Institute , vol.92 , Issue.15 , pp. 1210-1216
    • Marks, P.A.1    Richon, V.M.2    Rifkind, R.A.3
  • 25
    • 0012107820 scopus 로고    scopus 로고
    • Phase II trial of CI-994 in patients (pts) with advanced nonsmall cell lung cancer (NSCLC)
    • Wozniak, A., O'Shaughnessy, J., Fiorica, J., and Grove, W. Phase II trial of CI-994 in patients (pts) with advanced nonsmall cell lung cancer (NSCLC). Proc. Am. Soc. Clin. Oncol., 18: 487a, 1999.
    • (1999) Proc. Am. Soc. Clin. Oncol. , vol.18
    • Wozniak, A.1    O'Shaughnessy, J.2    Fiorica, J.3    Grove, W.4
  • 29
    • 0029099455 scopus 로고
    • Role of a small molecular weight phosphoprotein in the mechanism of action of CI-994 (N-acetyldinaline)
    • Rummel, S. A., Kraker, A. J., Steinkampf, R. W., Hook, K. E., and Klohs, W. D., Role of a small molecular weight phosphoprotein in the mechanism of action of CI-994 (N-acetyldinaline). Int. J. Cancer, 62: 636-642, 1995.
    • (1995) Int. J. Cancer , vol.62 , pp. 636-642
    • Rummel, S.A.1    Kraker, A.J.2    Steinkampf, R.W.3    Hook, K.E.4    Klohs, W.D.5
  • 31
    • 0021111818 scopus 로고
    • Histone deacetylase
    • Hay, C. W., and Candido, E. P. M. Histone deacetylase. J. Biol. Chem., 256: 3726-3734, 1983.
    • (1983) J. Biol. Chem. , vol.256 , pp. 3726-3734
    • Hay, C.W.1    Candido, E.P.M.2
  • 32
    • 0033529706 scopus 로고    scopus 로고
    • Requirement of Rsk-2 for epidermal growth factor-activated phosphorylation of histone H3
    • DOI 10.1126/science.285.5429.886
    • Sassone-Corsi, P., Mizzen, C. A., Cheung, P., Crosio, C., Monaco, L., Jacquot, S., Hanauer, A., and Allis, C. D. Requirement of Rsk-2 for epidermal growth factor-activated phosphorylation of histone H3. Science (Wash. DC), 285: 886-891, 1999. (Pubitemid 29381988)
    • (1999) Science , vol.285 , Issue.5429 , pp. 886-891
    • Sassone-Corsi, P.1    Mizzen, C.A.2    Cheung, P.3    Crosio, C.4    Monaco, L.5    Jacquot, S.6    Hanauer, A.7    Allis, C.D.8
  • 33
    • 0031036154 scopus 로고    scopus 로고
    • Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation
    • Wang, L., Mizzen, C., Ying, C., Candau, R., Barlev, N., Brownell, J., Allis, C. D., and Berger, S. L. Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation. Mol. Cell. Biol., 17: 519-527, 1997. (Pubitemid 26425641)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.1 , pp. 519-527
    • Wang, L.1    Mizzen, C.2    Ying, C.3    Candau, R.4    Barlev, N.5    Brownell, J.6    Allis, C.D.7    Berger, S.L.8
  • 34
    • 0033031978 scopus 로고    scopus 로고
    • Histone acetyltransferases: Preparation of substrates and assay procedures
    • DOI 10.1016/S0076-6879(99)04041-0
    • Mizzen, C. A., Brownell, J. E., and Allis, C. D. Histone acetyltransferases: preparation of substrates and assay procedures. Methods Enzymol., 304: 675-696, 1999. (Pubitemid 29268912)
    • (1999) Methods in Enzymology , vol.304 , pp. 675-696
    • Mizzen, C.A.1    Brownell, J.E.2    Cook, R.G.3    Allis, C.D.4
  • 35
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida, M., Kijima, M., Akita, M., and Beppu, T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J. Biol. Chem., 265: 17174-17179, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 36
    • 0033561497 scopus 로고    scopus 로고
    • Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase
    • DOI 10.1038/sj.onc.1202564
    • Kim, Y. B., Lee, K-H., Sugita, K., Yoshida, M., and Horinouchi, S. Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase. Oncogene, 18: 2461-2470, 1999. (Pubitemid 29206159)
    • (1999) Oncogene , vol.18 , Issue.15 , pp. 2461-2470
    • Kim, Y.B.1    Lee, K.-H.2    Sugita, K.3    Yoshida, M.4    Horinouchi, S.5
  • 38
    • 0035870122 scopus 로고    scopus 로고
    • dSIR2 and dHDAC6: Two novel, inhibitor-resistant deacetylases in Drosophila melanogaster
    • DOI 10.1006/excr.2001.5162
    • Barlow, A. L., van Drunen, C. M., Johnson, C. A., Tweedie, S., Bird, A., and Turner, B. M. dSIR2 and dHDAC6: two novel, inhibitor-resistant deacetylases in Drosophila melanogaster. Exp. Cell Res., 265: 90-103, 2001. (Pubitemid 32989067)
    • (2001) Experimental Cell Research , vol.265 , Issue.1 , pp. 90-103
    • Barlow, A.L.1    Van Drunen, C.M.2    Johnson, C.A.3    Tweedie, S.4    Bird, A.5    Turner, B.M.6
  • 40
    • 0344431240 scopus 로고    scopus 로고
    • FR901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor
    • DOI 10.1006/excr.1998.4027
    • Nakajima, H., Kim, Y. B., Terano, H., Yoshida, M., and Horinouchi, S. FR901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor. Exp. Cell Res., 241: 126-133, 1998. (Pubitemid 28366586)
    • (1998) Experimental Cell Research , vol.241 , Issue.1 , pp. 126-133
    • Nakajima, H.1    Kim, Y.B.2    Terano, H.3    Yoshida, M.4    Horinouchi, S.5
  • 41
    • 0030723231 scopus 로고    scopus 로고
    • Preclinical pharmacokinetic, antitumor and toxicity studies with CL-994 (N-acetyldinaline)
    • DOI 10.1023/A:1005846026398
    • Foster, B. J., Jones, L., Wiegand, R., LoRusso, P. M., and Corbett, T. H. Preclinical pharmacokinetic, antitumor and toxicity studies with CI-994 (N-acetyldinaline). Investig. New Drugs, 15: 187-194, 1997. (Pubitemid 27453873)
    • (1997) Investigational New Drugs , vol.15 , Issue.3 , pp. 187-194
    • Foster, B.J.1    Jones, L.2    Wiegand, R.3    LoRusso, P.M.4    Corbett, T.H.5
  • 42
    • 0030271680 scopus 로고    scopus 로고
    • Efficacy of dinaline and its methyl and acetyl derivatives against colorectal cancer in vivo and in vitro
    • DOI 10.1016/0959-8049(96)00217-1, PII S0959804996002171
    • Seelig, M. H., and Berger, M. R. Efficacy of Dinaline and its methyl and acetyl derivatives against colorectal cancer in vivo and in vitro. Eur. J. Cancer, 32A: 1968-1976, 1996. (Pubitemid 26361693)
    • (1996) European Journal of Cancer Part A , vol.32 , Issue.11 , pp. 1968-1976
    • Seelig, M.H.1    Berger, M.R.2
  • 43
    • 0033520944 scopus 로고    scopus 로고
    • Histone deacetylase inhibition selectively alters the activity and expression of cell cycle proteins leading to specific chromatin acetylation and antiproliferative effects
    • Sambucetti, L. C., Fischer, D. D., Zabludoff, S., Kwon, P. O., Chamberlin, H., Trogani, N., Xu, H., and Cohen, D. Histone deacetylase inhibition selectively alters the activity and expression of cell cycle proteins leading to specific chromatin acetylation and antiproliferative effects. J. Biol. Chem., 274: 34940-34947, 1999. (Pubitemid 129509542)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.49 , pp. 34940-34947
    • Sambucetti, L.C.1    Fischer, D.D.2    Zabludoff, S.3    Kwon, P.O.4    Chamberlin, H.5    Trogani, N.6    Xu, H.7    Cohen, D.8
  • 44
    • 0036737592 scopus 로고    scopus 로고
    • Current patent status of histone deacetylase inhibitors
    • Curtin, M. L., Current patent status of histone deacetylase inhibitors. Exp. Opin. Ther. Patents, 12: 1375-1383, 2002.
    • (2002) Exp. Opin. Ther. Patents , vol.12 , pp. 1375-1383
    • Curtin, M.L.1
  • 45
    • 0036651788 scopus 로고    scopus 로고
    • Recent advances in the discovery of small molecule histone deacetylase inhibitors
    • Remiszewski, S. W., Recent advances in the discovery of small molecule histone deacetylase inhibitors. Curr. Opin. Drug Disc. Dev., 5: 487-499, 2002. (Pubitemid 36748979)
    • (2002) Current Opinion in Drug Discovery and Development , vol.5 , Issue.4 , pp. 487-499
    • Remiszewski, S.W.1
  • 46
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacetylases associated with the mSin3 corepressor mediate Mad transcriptional repression
    • DOI 10.1016/S0092-8674(00)80215-9
    • Laherty, C. D., Yang, W. M., Sun, J. M., Davie, J. R., Seto, E., and Eisenman, R. N. Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell, 89: 349-356, 1997. (Pubitemid 27220879)
    • (1997) Cell , vol.89 , Issue.3 , pp. 349-356
    • Laherty, C.D.1    Yang, W.-M.2    Jian-Min, S.3    Davie, J.R.4    Seto, E.5    Eisenman, R.N.6
  • 47
    • 0030916729 scopus 로고    scopus 로고
    • Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex
    • DOI 10.1016/S0092-8674(00)80216-0
    • Zhang, Y., Iratni, R., Erdjument-Bromage, H., Tempst, P., and Reinberg, D. Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Cell, 89: 357-364, 1997. (Pubitemid 27220880)
    • (1997) Cell , vol.89 , Issue.3 , pp. 357-364
    • Zhang, Y.1    Iratni, R.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 48
    • 0032538293 scopus 로고    scopus 로고
    • The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities
    • DOI 10.1016/S0092-8674(00)81758-4
    • Zhang, Y., LeRoy, G., Seelig, H. P., Lane, W. S., and Reinberg, D. The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell, 95: 279-289, 1998. (Pubitemid 28473788)
    • (1998) Cell , vol.95 , Issue.2 , pp. 279-289
    • Zhang, Y.1    LeRoy, G.2    Seelig, H.-P.3    Lane, W.S.4    Reinberg, D.5
  • 49
    • 0037205476 scopus 로고    scopus 로고
    • Phosphatase inhibition leads to histone deacetylases 1 and 2 phosphorylation and disruption of corepressor interactions
    • DOI 10.1074/jbc.M201174200
    • Galasinski, S. C., Resing, K. A., Goodrich, J. A., and Ahn, N. G. Phosphatase inhibition leads to histone deacetylases 1 and 2 phosphorylation and disruption of corepressor interactions. J. Biol. Chem., 277: 19618-19626, 2002. (Pubitemid 34967475)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.22 , pp. 19618-19626
    • Galasinski, S.C.1    Resing, K.A.2    Goodrich, J.A.3    Ahn, N.G.4
  • 50
    • 0035794163 scopus 로고    scopus 로고
    • Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1
    • Humphrey, G. W., Wang, Y., Russanova, V. R., Hirai, T., Qin, J., Nakatani, Y., and Howard, B. H. Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1. J. Biol. Chem., 276: 6817-6824, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6817-6824
    • Humphrey, G.W.1    Wang, Y.2    Russanova, V.R.3    Hirai, T.4    Qin, J.5    Nakatani, Y.6    Howard, B.H.7
  • 52
    • 0033199896 scopus 로고    scopus 로고
    • Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/CD95 ligand expression in human neuroblastoma
    • Glick, R. D., Swendeman, S. L., Coffey, D. C., Rifkind, R. A., Marks, P. A., Richon, V. M., and La Quaglia, M. P. Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/CD95 ligand expression in human neuroblastoma. Cancer Res., 59: 4392-4399, 1999. (Pubitemid 29418759)
    • (1999) Cancer Research , vol.59 , Issue.17 , pp. 4392-4399
    • Glick, R.D.1    Swendeman, S.L.2    Coffey, D.C.3    Rifkind, R.A.4    Marks, P.A.5    Richon, V.M.6    La, Q.M.P.7
  • 53
    • 84880158529 scopus 로고    scopus 로고
    • In vivo antitumor activity of CI-994 (N-acetyldinaline, GOE5549) alone and in combination with Adriamycin against mammary adenocarcinoma 16C
    • Howard, C. T., Guisbert, E. A., Dykes, D. J., and Merriman, R. L. In vivo antitumor activity of CI-994 (N-acetyldinaline, GOE5549) alone and in combination with Adriamycin against mammary adenocarcinoma 16C. Proc. Am. Assoc. Cancer Res., 39: 311, 1998.
    • (1998) Proc. Am. Assoc. Cancer Res. , vol.39 , pp. 311
    • Howard, C.T.1    Guisbert, E.A.2    Dykes, D.J.3    Merriman, R.L.4
  • 54
    • 0011748844 scopus 로고    scopus 로고
    • In vivo antitumor activity of CI-994 (N-acetyldinaline, GOE 5549) alone and in combination with gemcitabine against LC12 squamous cell lung carcinoma
    • Howard, C. T., Guisbert, E. A., Schaefer, J. S., and Merriman, R. L. In vivo antitumor activity of CI-994 (N-acetyldinaline, GOE 5549) alone and in combination with gemcitabine against LC12 squamous cell lung carcinoma. Proc. Am. Assoc. Cancer Res., 40: 590, 1999.
    • (1999) Proc. Am. Assoc. Cancer Res. , vol.40 , pp. 590
    • Howard, C.T.1    Guisbert, E.A.2    Schaefer, J.S.3    Merriman, R.L.4


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