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Volumn 59, Issue 21, 1999, Pages 5586-5595

The apoptotic effects and synergistic interaction of sodium butyrate and MG132 in human retinoblastoma Y79 cells

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BUTYRIC ACID; CASPASE 3; CYTOCHROME C; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LAMIN B; PROTEIN BAX; PROTEIN BCL 2; PROTEIN P53; REGULATOR PROTEIN;

EID: 0033230594     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (95)

References (61)
  • 1
    • 0345090929 scopus 로고
    • Short chain fatty acids in the human colon
    • Cummings, J. H. Short chain fatty acids in the human colon. Gut, 28: 3-13, 1981.
    • (1981) Gut , vol.28 , pp. 3-13
    • Cummings, J.H.1
  • 2
    • 0027617675 scopus 로고
    • Butyrate rapidly induces growth inhibition and differentiation in HT-29 cells
    • Barnard, J. A., and Warwick, G. Butyrate rapidly induces growth inhibition and differentiation in HT-29 cells. Cell Growth Differ., 4: 495-501, 1993.
    • (1993) Cell Growth Differ. , vol.4 , pp. 495-501
    • Barnard, J.A.1    Warwick, G.2
  • 3
    • 0027485599 scopus 로고
    • Sodium butyrate induces apoptosis in human colonic tumour cell lines in a p53-independent pathway: Implications for the possible role of dietary fibre in the prevention of large-bowel cancer
    • Hague, A., Manning, A. M., Hanlon, K. A., Huschtscha, L. I., Hart, D., and Paraskeva, C. Sodium butyrate induces apoptosis in human colonic tumour cell lines in a p53-independent pathway: implications for the possible role of dietary fibre in the prevention of large-bowel cancer. Int. J. Cancer, 55: 498-505, 1993.
    • (1993) Int. J. Cancer , vol.55 , pp. 498-505
    • Hague, A.1    Manning, A.M.2    Hanlon, K.A.3    Huschtscha, L.I.4    Hart, D.5    Paraskeva, C.6
  • 4
    • 0030796349 scopus 로고    scopus 로고
    • Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): Dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway
    • Medina, V., Edmonds, B., Young, G. P., James, R., Appleton, S., and Zalewski, P. D. Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway. Cancer Res., 57: 3697-3707, 1997.
    • (1997) Cancer Res. , vol.57 , pp. 3697-3707
    • Medina, V.1    Edmonds, B.2    Young, G.P.3    James, R.4    Appleton, S.5    Zalewski, P.D.6
  • 5
    • 0030881282 scopus 로고    scopus 로고
    • Butyrate modulates DNA-damage-induced p53 response by induction of p53-independent differentiation and apoptosis
    • Janson, W., Brandner, G., and Siegel, J. Butyrate modulates DNA-damage-induced p53 response by induction of p53-independent differentiation and apoptosis. Oncogene, 15: 1395-1406, 1997.
    • (1997) Oncogene , vol.15 , pp. 1395-1406
    • Janson, W.1    Brandner, G.2    Siegel, J.3
  • 7
    • 0029092238 scopus 로고
    • Stimulation of tissue type plasminogen activator gene expression by sodium butyrate and TSA in human endothelial cells involves histone acetylation
    • Arts, J., Lansink, M., Grimbergen, J., Toet, K. H., and Kooistra, T. Stimulation of tissue type plasminogen activator gene expression by sodium butyrate and TSA in human endothelial cells involves histone acetylation. Biochem. J., 310: 171-176, 1995.
    • (1995) Biochem. J. , vol.310 , pp. 171-176
    • Arts, J.1    Lansink, M.2    Grimbergen, J.3    Toet, K.H.4    Kooistra, T.5
  • 9
    • 0027184401 scopus 로고
    • Abnormalities of retinoblastoma gene structure in human lung tumors
    • Linardopoulo, S., Gonos, E. S., and Spandidos, D. A. Abnormalities of retinoblastoma gene structure in human lung tumors. Cancer Lett., 71: 67-74, 1993.
    • (1993) Cancer Lett. , vol.71 , pp. 67-74
    • Linardopoulo, S.1    Gonos, E.S.2    Spandidos, D.A.3
  • 10
    • 0031935648 scopus 로고    scopus 로고
    • Control of pRB phosphorylation
    • Mittnacht, S. Control of pRB phosphorylation. Curr. Opin. Genet. Dev., 8: 21-27, 1998.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 21-27
    • Mittnacht, S.1
  • 11
    • 0030991235 scopus 로고    scopus 로고
    • The retinoblastoma protein: A master regulator of cell cycle differentiation and apoptosis
    • Herwig, S., and Strauss, M. The retinoblastoma protein: a master regulator of cell cycle differentiation and apoptosis. Eur. J. Biochem., 246: 581-601, 1997.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 581-601
    • Herwig, S.1    Strauss, M.2
  • 12
    • 0031817711 scopus 로고    scopus 로고
    • pRb and the Cdks in apoptosis and the cell cycle
    • Kasten, M. M., and Giordano, A. pRb and the Cdks in apoptosis and the cell cycle. Cell Death Differ., 5: 132-140, 1998.
    • (1998) Cell Death Differ. , vol.5 , pp. 132-140
    • Kasten, M.M.1    Giordano, A.2
  • 14
    • 0030850752 scopus 로고    scopus 로고
    • E2F1-induced apoptosis required DNA binding but not transactivation and is inhibited by the retinoblastoma protein through direct interaction
    • Hsieh, J-K., Fredersdorf, S., Kouzarides, T., Martin, K., and Lu, X. E2F1-induced apoptosis required DNA binding but not transactivation and is inhibited by the retinoblastoma protein through direct interaction. Genes Dev., 11: 1840-1852, 1997.
    • (1997) Genes Dev. , vol.11 , pp. 1840-1852
    • Hsieh, J.-K.1    Fredersdorf, S.2    Kouzarides, T.3    Martin, K.4    Lu, X.5
  • 15
    • 0021205549 scopus 로고
    • Effects of butyrate, retinol, and retinoic acid on human Y-79 retinoblastoma cells growing in monolayer cultures
    • Kyritsis, T., Joseph, G., and Chader, G. J. Effects of butyrate, retinol, and retinoic acid on human Y-79 retinoblastoma cells growing in monolayer cultures. J. Natl. Cancer Inst., 73: 649-654, 1984.
    • (1984) J. Natl. Cancer Inst. , vol.73 , pp. 649-654
    • Kyritsis, T.1    Joseph, G.2    Chader, G.J.3
  • 16
    • 0028809535 scopus 로고
    • Induction of apoptosis by sodium butyrate in the human Y-79 retinoblastoma cell line
    • Conway, R. M., Madigan. M. C., Penfold, P. L., and Billson, F. A. Induction of apoptosis by sodium butyrate in the human Y-79 retinoblastoma cell line. Oncol. Res., 7: 289-297, 1995.
    • (1995) Oncol. Res. , vol.7 , pp. 289-297
    • Conway, R.M.1    Madigan, M.C.2    Penfold, P.L.3    Billson, F.A.4
  • 17
    • 0031927472 scopus 로고    scopus 로고
    • Apoptotic effects of different drugs on cultured retinoblastoma Y79 cells
    • Lauricella, M., Giuliano, M., Emanuele, S., Vento, R., and Tesoriere, G. Apoptotic effects of different drugs on cultured retinoblastoma Y79 cells. Tumour Biol., 19: 356-363, 1998.
    • (1998) Tumour Biol. , vol.19 , pp. 356-363
    • Lauricella, M.1    Giuliano, M.2    Emanuele, S.3    Vento, R.4    Tesoriere, G.5
  • 21
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application and cytotoxicity assay
    • Mosmann, T. Rapid colorimetric assay for cellular growth and survival: application and cytotoxicity assay. J. Immunol. Methods, 65: 55-63, 1983.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 23
    • 0032254614 scopus 로고    scopus 로고
    • Dexamethasone-induced cytotoxic activity and drug resistance effects in androgen-independent prostate tumor PC-3 cells are mediated by Lipocortin I
    • Carollo, M., Parente, L., and D'Alessandro, N. Dexamethasone-induced cytotoxic activity and drug resistance effects in androgen-independent prostate tumor PC-3 cells are mediated by Lipocortin I. Oncol. Res., 10: 245-254, 1998.
    • (1998) Oncol. Res. , vol.10 , pp. 245-254
    • Carollo, M.1    Parente, L.2    D'Alessandro, N.3
  • 25
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Washington DC
    • Yang, J., Liu, X., Bhalla, K., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T., Jones, D. P., and Wang, X. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science (Washington DC), 275: 1129-1132, 1997.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3    Kim, C.N.4    Ibrado, A.M.5    Cai, J.6    Peng, T.7    Jones, D.P.8    Wang, X.9
  • 26
    • 0032103504 scopus 로고    scopus 로고
    • Proteasome activities decrease during dexamethasone-induced apoptosis of thymocytes
    • Beyette, J., Mason, G. G. F., Murray, R. Z., Cohen, G. M., and Rivett, A. J. Proteasome activities decrease during dexamethasone-induced apoptosis of thymocytes. Biochem. J., 332: 315-320, 1998.
    • (1998) Biochem. J. , vol.332 , pp. 315-320
    • Beyette, J.1    Mason, G.G.F.2    Murray, R.Z.3    Cohen, G.M.4    Rivett, A.J.5
  • 27
    • 0028673206 scopus 로고
    • Multicatalytic endopeptidase complex: Proteasome
    • Rivett, A. J., Savory, P. J., and Djaballah, H. Multicatalytic endopeptidase complex: proteasome. Methods Enzymol., 244: 331-350, 1994.
    • (1994) Methods Enzymol. , vol.244 , pp. 331-350
    • Rivett, A.J.1    Savory, P.J.2    Djaballah, H.3
  • 28
    • 0031817144 scopus 로고    scopus 로고
    • Apoptosis: Unmasking the executioner
    • Wilson, M. R. Apoptosis: unmasking the executioner. Cell Death Differ., 5: 646-652, 1998.
    • (1998) Cell Death Differ. , vol.5 , pp. 646-652
    • Wilson, M.R.1
  • 29
    • 0032579414 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate inhibits activation of caspases that cleave poly(ADP-ribose) polymerase and lamins during Fas- and ceramide-mediated apoptosis in Jurkat T lymphocytes
    • Cuvillier, O., Rosenthal, D. S., Smulson, M. E., and Spiegel, S. Sphingosine 1-phosphate inhibits activation of caspases that cleave poly(ADP-ribose) polymerase and lamins during Fas- and ceramide-mediated apoptosis in Jurkat T lymphocytes. J. Biol. Chem., 273: 2910-2916, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2910-2916
    • Cuvillier, O.1    Rosenthal, D.S.2    Smulson, M.E.3    Spiegel, S.4
  • 30
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • Hilt, W., and Wolf, D. H. Proteasomes: destruction as a programme. Trends Biochem. Sci., 21: 96-101, 1996.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 96-101
    • Hilt, W.1    Wolf, D.H.2
  • 31
    • 0028607435 scopus 로고
    • Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53
    • Scheffner, M., Huibregtse, J., and Howley, P. Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53. Proc. Natl. Acad. Sci. USA, 91: 8797-8801, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8797-8801
    • Scheffner, M.1    Huibregtse, J.2    Howley, P.3
  • 34
    • 0021241701 scopus 로고
    • Expression and amplification of the N-myc gene in primary retinoblastoma
    • Lond.
    • Lee, W. H., Murphree, A. L., and Benedict, W. F. Expression and amplification of the N-myc gene in primary retinoblastoma. Nature (Lond.), 309: 458-460, 1984.
    • (1984) Nature , vol.309 , pp. 458-460
    • Lee, W.H.1    Murphree, A.L.2    Benedict, W.F.3
  • 35
    • 0031577480 scopus 로고    scopus 로고
    • Sodium butyrate induces NIH3T3 cells to senescence-like state and enhances promoter activity of p21/WAFI in p53-independent manner. Biochem
    • Xiao, H., Hasegawa, T., Miyaishi, O., Ohkusu, K., and Isobe, K. Sodium butyrate induces NIH3T3 cells to senescence-like state and enhances promoter activity of p21/WAFI in p53-independent manner. Biochem. Biophys. Res. Commun., 237: 457-460, 1997.
    • (1997) Biophys. Res. Commun. , vol.237 , pp. 457-460
    • Xiao, H.1    Hasegawa, T.2    Miyaishi, O.3    Ohkusu, K.4    Isobe, K.5
  • 36
    • 0030903750 scopus 로고    scopus 로고
    • Regulation of E2F through ubiquitin-proteasome-dependent degradation: Stabilization by the pRB tumor suppressor protein
    • Campanero, M. R., and Flemington, E. K. Regulation of E2F through ubiquitin-proteasome-dependent degradation: stabilization by the pRB tumor suppressor protein. Proc. Natl. Acad. Sci. USA, 94: 2221-2226, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2221-2226
    • Campanero, M.R.1    Flemington, E.K.2
  • 37
    • 0023724778 scopus 로고
    • IκB: A specific inhibitor of the NF-κB transcription factor
    • Washington DC
    • Baeuerle, P. A., and Baltimore, D. IκB: a specific inhibitor of the NF-κB transcription factor. Science (Washington DC), 242: 540-546, 1988.
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.A.1    Baltimore, D.2
  • 38
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Washington DC
    • Green, D. R., and Reed, J. C. Mitochondria and apoptosis. Science (Washington DC), 281: 1309-1312, 1998.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 40
    • 0031825739 scopus 로고    scopus 로고
    • Butyrate-induced differentiation of Caco-2 cells is associated with apoptosis and early induction of p21/Waf1 and p27Kip I
    • Litvak, D. A., Evers, B. M., Hwang, K. O., Hellmich, M. R., Ko, T. C., and Townsend, C. M., Jr. Butyrate-induced differentiation of Caco-2 cells is associated with apoptosis and early induction of p21/Waf1 and p27Kip I. Surgery, 124: 161-170, 1998.
    • (1998) Surgery , vol.124 , pp. 161-170
    • Litvak, D.A.1    Evers, B.M.2    Hwang, K.O.3    Hellmich, M.R.4    Ko, T.C.5    Townsend C.M., Jr.6
  • 42
    • 0028673348 scopus 로고
    • Inhibition of cell cycle progression by sodium butyrate in normal rat kidney fibroblasts is altered by expression of the adenovirus 5 early 1A gene
    • Joensuu, T., and Mester, J. Inhibition of cell cycle progression by sodium butyrate in normal rat kidney fibroblasts is altered by expression of the adenovirus 5 early 1A gene. Biosci. Rep., 14: 291-300, 1994.
    • (1994) Biosci. Rep. , vol.14 , pp. 291-300
    • Joensuu, T.1    Mester, J.2
  • 43
    • 0029024015 scopus 로고
    • Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
    • Washington DC
    • Pagano, M., Tam, S. W., Theodoras, A. M., Romero-Beer, P., Del Sal, G., Chau, V., Yew, R., Draetta, G., and Rolfe, M. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science (Washington DC), 269: 682-685, 1995.
    • (1995) Science , vol.269 , pp. 682-685
    • Pagano, M.1    Tam, S.W.2    Theodoras, A.M.3    Romero-Beer, P.4    Del Sal, G.5    Chau, V.6    Yew, R.7    Draetta, G.8    Rolfe, M.9
  • 45
    • 0028970734 scopus 로고
    • Stimulation-dependent IκBα phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway
    • Alkalay, K., Yaron, A., Hatzubai, A., Orian, A., Ciechanover, A., and Ben-Neriah, Y. Stimulation-dependent IκBα phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway. Proc. Natl. Acad. Sci. USA, 92: 10599-10603, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10599-10603
    • Alkalay, K.1    Yaron, A.2    Hatzubai, A.3    Orian, A.4    Ciechanover, A.5    Ben-Neriah, Y.6
  • 46
    • 0030156633 scopus 로고    scopus 로고
    • Protein degradation: De-ubiquitinate to decide your fate
    • Kalderon, D. Protein degradation: de-ubiquitinate to decide your fate. Curr. Biol., 6: 662-665, 1996.
    • (1996) Curr. Biol. , vol.6 , pp. 662-665
    • Kalderon, D.1
  • 48
    • 0027368034 scopus 로고
    • Kinetic mechanism of activation by cardiolipin (diphosphatidylglycerol) of the rat liver multicatalytic proteinase
    • Ruiz de Mena, I., Mahillo, E., Arribas, J., and Castano, J. G. Kinetic mechanism of activation by cardiolipin (diphosphatidylglycerol) of the rat liver multicatalytic proteinase. Biochem. J., 296: 93-97, 1993.
    • (1993) Biochem. J. , vol.296 , pp. 93-97
    • Ruiz De Mena, I.1    Mahillo, E.2    Arribas, J.3    Castano, J.G.4
  • 49
    • 0031991819 scopus 로고    scopus 로고
    • Irreversible potent activation and reversible inhibition of trypsin-like activity of 20S proteasome purified from Xenopus oocytes by fatty acids
    • Yamada, S., Yamada, J., Sato, K., Tokumoto, T., Yasutomi, M., and Ishikawa, K. Irreversible potent activation and reversible inhibition of trypsin-like activity of 20S proteasome purified from Xenopus oocytes by fatty acids. Zool. Sci., 15: 43-49, 1998.
    • (1998) Zool. Sci. , vol.15 , pp. 43-49
    • Yamada, S.1    Yamada, J.2    Sato, K.3    Tokumoto, T.4    Yasutomi, M.5    Ishikawa, K.6
  • 50
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee, D. H., and Goldberg, A. L. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol., 8: 397-403, 1998.
    • (1998) Trends Cell Biol. , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 52
    • 0031034762 scopus 로고    scopus 로고
    • p53 status affects the rate of the onset but rot the overall extent of doxorubicin-induced cell death in rat-1 fibroblasts constitutively expressing c-Myc
    • Han, J. W., Dionne, C. A., Kedersha, N. L., and Goldmacher, V. S. p53 status affects the rate of the onset but rot the overall extent of doxorubicin-induced cell death in rat-1 fibroblasts constitutively expressing c-Myc. Cancer Res., 57: 176-182, 1997.
    • (1997) Cancer Res. , vol.57 , pp. 176-182
    • Han, J.W.1    Dionne, C.A.2    Kedersha, N.L.3    Goldmacher, V.S.4
  • 54
    • 0032508414 scopus 로고    scopus 로고
    • NF-κB antiapoptosis: Induction of TRAF1 and TRAF2 c-IAP1 and C-IAP2 to suppress caspase-8 activation
    • Washington DC
    • Wang, C. Y., Mayo, M. W., Korneluk, R. G., Goeddel, D. V., and Baldwin, A. S., Jr. NF-κB antiapoptosis: induction of TRAF1 and TRAF2 c-IAP1 and C-IAP2 to suppress caspase-8 activation. Science (Washington DC), 281: 1680-1683, 1998.
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin A.S., Jr.5
  • 55
    • 0031906567 scopus 로고    scopus 로고
    • The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-α-initiated apoptosis
    • Delic, J., Masdehors, P., Omura, S., Cosset, J. M., Dumont, J., Binet, J. L., and Magdelenat, H. The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-α-initiated apoptosis. Br. J. Cancer, 77: 1103-1107, 1998.
    • (1998) Br. J. Cancer , vol.77 , pp. 1103-1107
    • Delic, J.1    Masdehors, P.2    Omura, S.3    Cosset, J.M.4    Dumont, J.5    Binet, J.L.6    Magdelenat, H.7
  • 56
    • 0030962262 scopus 로고    scopus 로고
    • p53-dependent induction of apoptosis by proteasome inhibitors
    • Lopez, U. G., Erhardt, P., Yao, R., and Cooper, G. M. p53-dependent induction of apoptosis by proteasome inhibitors. J. Biol. Chem., 272: 12893-12896, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12893-12896
    • Lopez, U.G.1    Erhardt, P.2    Yao, R.3    Cooper, G.M.4
  • 57
    • 0029753773 scopus 로고    scopus 로고
    • The role of c-Jun N-terminal kinase (JNK) in apoptosis induced by ultraviolet C and γ radiation
    • Chen, Y. R., Wang, X., Templeton, D., Davis, R. J., and Tan, T. H. The role of c-Jun N-terminal kinase (JNK) in apoptosis induced by ultraviolet C and γ radiation. J. Biol. Chem., 271: 31929-31936, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31929-31936
    • Chen, Y.R.1    Wang, X.2    Templeton, D.3    Davis, R.J.4    Tan, T.H.5
  • 58
    • 0028222124 scopus 로고
    • p53 and E2F1 cooperate to mediate apoptosis
    • Wu, X. W., and Levine, A. J. p53 and E2F1 cooperate to mediate apoptosis. Proc. Natl. Acad. Sci. USA, 91: 3602-3606, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3602-3606
    • Wu, X.W.1    Levine, A.J.2
  • 59
    • 0025353691 scopus 로고
    • Cellular pharmacology of cisplatin: Perspectives on mechanisms of acquired resistance
    • Andrews, P. A., and Howell, S. B. Cellular pharmacology of cisplatin: perspectives on mechanisms of acquired resistance. Cancer Cells, 2: 35-43, 1990.
    • (1990) Cancer Cells , vol.2 , pp. 35-43
    • Andrews, P.A.1    Howell, S.B.2
  • 60
    • 0023515476 scopus 로고
    • Clinical pharmacology of sodium butyrate in patients with acute leukemia
    • Miller, A. A., Kurschel, E., Osieka, R., and Schmidt, C. G. Clinical pharmacology of sodium butyrate in patients with acute leukemia. Eur. J. Cancer Clin. Oncol., 23: 1283-1287, 1987.
    • (1987) Eur. J. Cancer Clin. Oncol. , vol.23 , pp. 1283-1287
    • Miller, A.A.1    Kurschel, E.2    Osieka, R.3    Schmidt, C.G.4


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