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Volumn 11, Issue 10, 2012, Pages 2116-2126

The inhibitor of histone deacetylases sodium butyrate enhances the cytotoxicity of mitomycin C

Author keywords

[No Author keywords available]

Indexed keywords

BUTYRIC ACID; MITOMYCIN C; REACTIVE OXYGEN METABOLITE;

EID: 84867424244     PISSN: 15357163     EISSN: 15388514     Source Type: Journal    
DOI: 10.1158/1535-7163.MCT-12-0193     Document Type: Article
Times cited : (8)

References (50)
  • 1
    • 79952262759 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitors in recent clinical trials for cancer therapy
    • Wagner JM, Hackanson B, Lubbert M, Jung M. Histone deacetylase (HDAC) inhibitors in recent clinical trials for cancer therapy. Clin Epigenetics 2010;1:117-36.
    • (2010) Clin Epigenetics , vol.1 , pp. 117-136
    • Wagner, J.M.1    Hackanson, B.2    Lubbert, M.3    Jung, M.4
  • 2
    • 77950860448 scopus 로고    scopus 로고
    • Inside HDAC with HDAC inhibitors
    • Bertrand P. Inside HDAC with HDAC inhibitors. Eur J Med Chem 2010;45:2095-116.
    • (2010) Eur J Med Chem , vol.45 , pp. 2095-2116
    • Bertrand, P.1
  • 3
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • DOI 10.1038/nrc1779
    • Minucci S, Pelicci PG. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 2006;6:38-51. (Pubitemid 43054973)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.1 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 4
    • 0031596491 scopus 로고    scopus 로고
    • 1 arrest results from p21-independent disruption of retinoblastoma protein-mediated signals
    • Vaziri C, Stice L, Faller DV. Butyrate-induced G1 arrest results from p21-independent disruption of retinoblastoma protein-mediated signals. Cell Growth Differ 1998;9:465-74. (Pubitemid 28345871)
    • (1998) Cell Growth and Differentiation , vol.9 , Issue.6 , pp. 465-474
    • Vaziri, C.1    Stice, L.2    Faller, D.V.3
  • 5
    • 0141570734 scopus 로고    scopus 로고
    • Functional interplay between modulation of histone deacetylase activity and its regulatory role in G2-M transition
    • DOI 10.1016/j.bbrc.2003.09.013
    • Noh EJ, Lee JS. Functional interplay between modulation of histone deacetylase activity and its regulatory role in G2-M transition. Biochem Biophys Res Commun 2003;310:267-73. (Pubitemid 37163659)
    • (2003) Biochemical and Biophysical Research Communications , vol.310 , Issue.2 , pp. 267-273
    • Noh, E.J.1    Lee, J.-S.2
  • 6
    • 0032499756 scopus 로고    scopus 로고
    • p21(WAF1) is required for butyrate-mediated growth inhibition of human colon cancer cells
    • Archer SY, Meng S, Shei A, Hodin RA. p21(WAF1) is required for butyrate-mediated growth inhibition of human colon cancer cells. Proc Natl Acad Sci U S A 1998;95:6791-6.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6791-6796
    • Archer, S.Y.1    Meng, S.2    Shei, A.3    Hodin, R.A.4
  • 8
    • 80051818192 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor sodium butyrate enhances cellular radiosensitivity by inhibiting both DNA nonhomologous end joining and homologous recombination
    • Amst
    • Koprinarova M, Botev P, Russev G. Histone deacetylase inhibitor sodium butyrate enhances cellular radiosensitivity by inhibiting both DNA nonhomologous end joining and homologous recombination. DNA Repair (Amst) 2011;10:970-7.
    • (2011) DNA Repair , vol.10 , pp. 970-977
    • Koprinarova, M.1    Botev, P.2    Russev, G.3
  • 9
    • 77956341931 scopus 로고    scopus 로고
    • Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining
    • Miller KM, Tjeertes JV, Coates J, Legube G, Polo SE, Britton S, et al. Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining. Nat Struct Mol Biol 2010;17:1144-51.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1144-1151
    • Miller, K.M.1    Tjeertes, J.V.2    Coates, J.3    Legube, G.4    Polo, S.E.5    Britton, S.6
  • 11
    • 65949105730 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor sodium butyrate enhances the cell killing effect of psoralen plus UVA by attenuating nucleotide excision repair
    • Toyooka T, Ibuki Y. Histone deacetylase inhibitor sodium butyrate enhances the cell killing effect of psoralen plus UVA by attenuating nucleotide excision repair. Cancer Res 2009;69:3492-500.
    • (2009) Cancer Res , vol.69 , pp. 3492-3500
    • Toyooka, T.1    Ibuki, Y.2
  • 14
    • 0038079767 scopus 로고    scopus 로고
    • CIP1/WAF1
    • Rosato RR, Almenara JA, Grant S. The histone deacetylase inhibitor MS-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21CIP1/WAF1 1. Cancer Res 2003;63:3637-45. (Pubitemid 36793047)
    • (2003) Cancer Research , vol.63 , Issue.13 , pp. 3637-3645
    • Rosato, R.R.1    Almenara, J.A.2    Grant, S.3
  • 15
    • 55749113687 scopus 로고    scopus 로고
    • Role of histone deacetylase inhibitor-induced reactive oxygen species and DNA damage in LAQ-824/fludarabine antileukemic interactions
    • Rosato RR, Almenara JA, Maggio SC, Coe S, Atadja P, Dent P, et al. Role of histone deacetylase inhibitor-induced reactive oxygen species and DNA damage in LAQ-824/fludarabine antileukemic interactions. Mol Cancer Ther 2008;7:3285-97.
    • (2008) Mol Cancer Ther , vol.7 , pp. 3285-3297
    • Rosato, R.R.1    Almenara, J.A.2    Maggio, S.C.3    Coe, S.4    Atadja, P.5    Dent, P.6
  • 16
    • 70349564782 scopus 로고    scopus 로고
    • Role of reactive oxygen species in proapoptotic ability of oncogenic H-Ras to increase human bladder cancer cell susceptibility to histone deacetylase inhibitor for caspase induction
    • Choudhary S, Wang HC. Role of reactive oxygen species in proapoptotic ability of oncogenic H-Ras to increase human bladder cancer cell susceptibility to histone deacetylase inhibitor for caspase induction. J Cancer Res Clin Oncol 2009;135:1601-13.
    • (2009) J Cancer Res Clin Oncol , vol.135 , pp. 1601-1613
    • Choudhary, S.1    Wang, H.C.2
  • 17
    • 77951241720 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors activate NF-kappaB in human leukemia cells through an ATM/NEMO-related pathway
    • Rosato RR, Kolla SS, Hock SK, Almenara JA, Patel A, Amin S, et al. Histone deacetylase inhibitors activate NF-kappaB in human leukemia cells through an ATM/NEMO-related pathway. J Biol Chem 2010;285:10064-77.
    • (2010) J Biol Chem , vol.285 , pp. 10064-10077
    • Rosato, R.R.1    Kolla, S.S.2    Hock, S.K.3    Almenara, J.A.4    Patel, A.5    Amin, S.6
  • 19
    • 25144513926 scopus 로고    scopus 로고
    • Mitotic spindle checkpoint inactivation by trichostatin A defines a mechanism for increasing cancer cell killing by microtubule-disrupting agents
    • Dowling M, Voong KR, Kim M, Keutmann MK, Harris E, Kao GD. Mitotic spindle checkpoint inactivation by trichostatin a defines a mechanism for increasing cancer cell killing by microtubule-disrupting agents. Cancer Biol Ther 2005;4:197-206. (Pubitemid 41351319)
    • (2005) Cancer Biology and Therapy , vol.4 , Issue.2 , pp. 197-206
    • Dowling, M.1    Voong, K.R.2    Kim, M.3    Keutmann, M.K.4    Harris, E.5    Kao, G.D.6
  • 20
    • 77954852413 scopus 로고    scopus 로고
    • Sodium butyrate enhances the cytotoxic effect of cisplatin by abrogating the cisplatin imposed cell cycle arrest
    • Koprinarova M, Markovska P, Iliev I, Anachkova B, Russev G. Sodium butyrate enhances the cytotoxic effect of cisplatin by abrogating the cisplatin imposed cell cycle arrest. BMC Mol Biol 2010;11:49.
    • (2010) BMC Mol Biol , vol.11 , pp. 49
    • Koprinarova, M.1    Markovska, P.2    Iliev, I.3    Anachkova, B.4    Russev, G.5
  • 21
    • 0035807079 scopus 로고    scopus 로고
    • Repair of DNA interstrand cross-links
    • DOI 10.1016/S0921-8777(01)00092-1, PII S0921877701000921
    • Dronkert ML, Kanaar R. Repair of DNA interstrand cross-links. Mutat Res 2001;486:217-47. (Pubitemid 32763210)
    • (2001) Mutation Research - DNA Repair , vol.486 , Issue.4 , pp. 217-247
    • Dronkert, M.L.G.1    Kanaar, R.2
  • 22
    • 34147201571 scopus 로고    scopus 로고
    • Activation of the S phase DNA damage checkpoint by mitomycin C
    • DOI 10.1002/jcp.20957
    • Mladenov E, Tsaneva I, Anachkova B. Activation of the S phase DNA damage checkpoint by mitomycin C. J Cell Physiol 2007;211:468-76. (Pubitemid 46580100)
    • (2007) Journal of Cellular Physiology , vol.211 , Issue.2 , pp. 468-476
    • Mladenov, E.1    Tsaneva, I.2    Anachkova, B.3
  • 23
    • 77955876503 scopus 로고    scopus 로고
    • Mammalian nucleotide excision repair proteins and interstrand crosslink repair
    • Wood RD. Mammalian nucleotide excision repair proteins and interstrand crosslink repair. Environ Mol Mutagen 2010;51:520-6.
    • (2010) Environ Mol Mutagen , vol.51 , pp. 520-526
    • Wood, R.D.1
  • 24
    • 77955910902 scopus 로고    scopus 로고
    • Role of homologous recombination in DNA interstrand crosslink repair
    • Hinz JM. Role of homologous recombination in DNA interstrand crosslink repair. Environ Mol Mutagen 2010;51:582-603.
    • (2010) Environ Mol Mutagen , vol.51 , pp. 582-603
    • Hinz, J.M.1
  • 25
    • 30344444484 scopus 로고    scopus 로고
    • Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks
    • DOI 10.1038/ncb1343, PII N1343
    • Murr R, Loizou JI, Yang Y-G, Cuenin C, Li H, Wang Z-Q, et al. Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks. Nat Cell Biol 2006;8:91-9. (Pubitemid 43064802)
    • (2006) Nature Cell Biology , vol.8 , Issue.1 , pp. 91-99
    • Murr, R.1    Loizou, J.I.2    Yang, Y.-G.3    Cuenin, C.4    Li, H.5    Wang, Z.-Q.6    Herceg, Z.7
  • 26
    • 0037225019 scopus 로고    scopus 로고
    • Relationship between DNA repair capacity and resistance to genotoxins in four human cell lines
    • DOI 10.1016/S0361-090X(02)00175-7, PII S0361090X02001757
    • Atanassov BS, Ninova PD, Anachkova BB, Russev GC. Relationship between DNA repair capacity and resistance to genotoxins in four human cell lines. Cancer Detect Prev 2003;27:24-9. (Pubitemid 36339415)
    • (2003) Cancer Detection and Prevention , vol.27 , Issue.1 , pp. 24-29
    • Atanassov, B.S.1    Ninova, P.D.2    Anachkova, B.B.3    Russev, G.C.4
  • 27
    • 0034697177 scopus 로고    scopus 로고
    • Formation of the main UV-induced thymine dimeric lesions within isolated and cellular DNA as measured by high performance liquid chromatography-tandem mass spectrometry
    • DOI 10.1074/jbc.275.16.11678
    • Douki T, Court M, Sauvaigo S, Odin F, Cadet J. Formation of the main UV-induced thymine dimeric lesions within isolated and cellular DNA as measured by high performance liquid chromatography-tandem mass spectrometry. J Biol Chem 2000;275:11678-85. (Pubitemid 30237729)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.16 , pp. 11678-11685
    • Douki, T.1    Court, M.2    Sauvaigo, S.3    Odin, F.4    Cadet, J.5
  • 28
    • 0037446478 scopus 로고    scopus 로고
    • Determination of DNA repair capacity of protein extracts by restoration of the transformation efficiency of damaged plasmids
    • DOI 10.1016/S0003-2697(03)00006-X
    • Gospodinov A, Russev G, Anachkova B. Determination of DNA repair capacity of protein extracts by restoration of the transformation efficiency of damaged plasmids. Anal Biochem 2003;315:285-8. (Pubitemid 36407505)
    • (2003) Analytical Biochemistry , vol.315 , Issue.2 , pp. 285-288
    • Gospodinov, A.1    Russev, G.2    Anachkova, B.3
  • 29
    • 0033569684 scopus 로고    scopus 로고
    • XRCC3 promotes homology-directed repair of DNA damage in mammalian cells
    • DOI 10.1101/gad.13.20.2633
    • Pierce AJ, Johnson RD, Thompson LH, Jasin M. XRCC3 promotes homology-directed repair of DNA damage in mammalian cells. Genes Dev 1999;13:2633-8. (Pubitemid 29508550)
    • (1999) Genes and Development , vol.13 , Issue.20 , pp. 2633-2638
    • Pierce, A.J.1    Johnson, R.D.2    Thompson, L.H.3    Jasin, M.4
  • 30
    • 0038700698 scopus 로고    scopus 로고
    • Molecular views of recombination proteins and their control
    • DOI 10.1038/nrm1127
    • West SC. Molecular views of recombination proteins and their control. Nat Rev Mol Cell Biol 2003;4:435-45. (Pubitemid 36648589)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.6 , pp. 435-445
    • West, S.C.1
  • 31
    • 0028981845 scopus 로고
    • Cell cycle perturbation by sodium butyrate in tumorigenic and non-tumorigenic human urothelial cell lines assessed by flow cytometric bromodeoxyuridine/DNA analysis
    • Larsen JK, Christensen IJ, Kieler J. Cell cycle perturbation by sodium butyrate in tumorigenic and non-tumorigenic human urothelial cell lines assessed by flow cytometric bromodeoxyuridine/DNA analysis. Cell Prolif 1995;28:359-71.
    • (1995) Cell Prolif , vol.28 , pp. 359-371
    • Larsen, J.K.1    Christensen, I.J.2    Kieler, J.3
  • 32
    • 33746338907 scopus 로고    scopus 로고
    • 1/S arrest induced by histone deacetylase inhibitor sodium butyrate in E1A + Ras-transformed cells is mediated through down-regulation of E2F activity and stabilization of beta-catenin
    • DOI 10.1074/jbc.M511059200
    • Abramova MV, Pospelova TV, Nikulenkov FP, Hollander CM, Fornace AJ Jr, Pospelov VA. G1/S arrest induced by histone deacetylase inhibitor sodium butyrate in E1A + Ras-transformed cells is mediated through down-regulation of E2F activity and stabilization of betacatenin. J Biol Chem 2006;281:21040-51. (Pubitemid 44115445)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.30 , pp. 21040-21051
    • Abramova, M.V.1    Pospelova, T.V.2    Nikulenkov, F.P.3    Hollander, C.M.4    Fornace Jr., A.J.5    Pospelov, V.A.6
  • 33
    • 0033558850 scopus 로고    scopus 로고
    • Sodium butyrate induces G2 arrest in the human breast cancer cells MDA- MB-231 and renders them competent for DNA rereplication
    • DOI 10.1006/excr.1998.4370
    • Lallemand F, Courilleau D, Buquet-Fagot C, Atfi A, Montagne MN, Mester J. Sodium butyrate induces G2 arrest in the human breast cancer cells MDA-MB-231 and renders them competent for DNA rereplication. Exp Cell Res 1999;247:432-40. (Pubitemid 29394781)
    • (1999) Experimental Cell Research , vol.247 , Issue.2 , pp. 432-440
    • Lallemand, F.1    Courilleau, D.2    Buquet-Fagot, C.3    Atfi, A.4    Montagne, M.-N.5    Mester, J.6
  • 34
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • DOI 10.1038/371346a0
    • Lazebnik YA, Kaufmann SH, Desnoyers S, Poirier GG, Earnshaw WC. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 1994;371:346-7. (Pubitemid 24300618)
    • (1994) Nature , vol.371 , Issue.6495 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 35
    • 14944375437 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor sodium butyrate induces breast cancer cell apoptosis through diverse cytotoxic actions including glutathione depletion and oxidative stress
    • Louis M, Rosato RR, Brault L, Osbild S, Battaglia E, Yang XH, et al. The histone deacetylase inhibitor sodium butyrate induces breast cancer cell apoptosis through diverse cytotoxic actions including glutathione depletion and oxidative stress. Int J Oncol 2004;25:1701-11.
    • (2004) Int J Oncol , vol.25 , pp. 1701-1711
    • Louis, M.1    Rosato, R.R.2    Brault, L.3    Osbild, S.4    Battaglia, E.5    Yang, X.H.6
  • 36
    • 0034682736 scopus 로고    scopus 로고
    • Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis
    • Ikura T, Ogryzko VV, Grigoriev M, Groisman R, Wang J, Horikoshi M, et al. Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell 2000;102:463-73.
    • (2000) Cell , vol.102 , pp. 463-473
    • Ikura, T.1    Ogryzko, V.V.2    Grigoriev, M.3    Groisman, R.4    Wang, J.5    Horikoshi, M.6
  • 37
    • 59849088152 scopus 로고    scopus 로고
    • RAD51 foci formation in response to DNA damage is modulated by TIP49
    • Gospodinov A, Tsaneva I, Anachkova B. RAD51 foci formation in response to DNA damage is modulated by TIP49. Int J Biochem Cell Biol 2009;41:925-33.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 925-933
    • Gospodinov, A.1    Tsaneva, I.2    Anachkova, B.3
  • 38
    • 79952270884 scopus 로고    scopus 로고
    • HDACs link the DNA damage response, processing of double-strand breaks and autophagy
    • Robert T, Vanoli F, Chiolo I, Shubassi G, Bernstein KA, Rothstein R, et al. HDACs link the DNA damage response, processing of double-strand breaks and autophagy. Nature 2011;471:74-9.
    • (2011) Nature , vol.471 , pp. 74-79
    • Robert, T.1    Vanoli, F.2    Chiolo, I.3    Shubassi, G.4    Bernstein, K.A.5    Rothstein, R.6
  • 39
    • 49149130029 scopus 로고    scopus 로고
    • The Fas death signaling pathway connecting reactive oxygen species generation and FLICE inhibitory protein down-regulation
    • Wang L, Azad N, Kongkaneramit L, Chen F, Lu Y, Jiang BH, et al. The Fas death signaling pathway connecting reactive oxygen species generation and FLICE inhibitory protein down-regulation. J Immunol 2008;180:3072-80.
    • (2008) J Immunol , vol.180 , pp. 3072-3080
    • Wang, L.1    Azad, N.2    Kongkaneramit, L.3    Chen, F.4    Lu, Y.5    Jiang, B.H.6
  • 40
    • 23844496672 scopus 로고    scopus 로고
    • Reactive oxygen species regulate caspase activation in tumor necrosis factor-related apoptosis-inducing ligand-resistant human colon carcinoma cell lines
    • DOI 10.1158/0008-5472.CAN-04-2628
    • Izeradjene K, Douglas L, Tillman DM, Delaney AB, Houghton JA. Reactive oxygen species regulate caspase activation in tumor necrosis factor-related apoptosis-inducing ligand-resistant human colon carcinoma cell lines. Cancer Res 2005;65:7436-45. (Pubitemid 41161278)
    • (2005) Cancer Research , vol.65 , Issue.16 , pp. 7436-7445
    • Izeradjene, K.1    Douglas, L.2    Tillman, D.M.3    Delaney, A.B.4    Houghton, J.A.5
  • 42
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • DOI 10.1016/j.cell.2004.12.041
    • Kamata H, Honda S, Maeda S, Chang L, Hirata H, Karin M. Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 2005;120:649-61. (Pubitemid 40343077)
    • (2005) Cell , vol.120 , Issue.5 , pp. 649-661
    • Kamata, H.1    Honda, S.-I.2    Maeda, S.3    Chang, L.4    Hirata, H.5    Karin, M.6
  • 43
    • 77955884095 scopus 로고    scopus 로고
    • Proteomic analysis revealed association of aberrant ROS signaling with suberoylanilide hydroxamic acid-induced autophagy in Jurkat T-leukemia cells
    • Li J, Liu R, Lei Y, Wang K, Lau QC, Xie N, et al. Proteomic analysis revealed association of aberrant ROS signaling with suberoylanilide hydroxamic acid-induced autophagy in Jurkat T-leukemia cells. Autophagy 2010;6:711-24.
    • (2010) Autophagy , vol.6 , pp. 711-724
    • Li, J.1    Liu, R.2    Lei, Y.3    Wang, K.4    Lau, Q.C.5    Xie, N.6
  • 44
    • 31544432335 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors modulate the sensitivity of tumor necrosis factor-related apoptosis-inducing ligand-resistant bladder tumor cells
    • DOI 10.1158/0008-5472.CAN-05-3017
    • Earel JK Jr, VanOosten RL, Griffith TS. Histone deacetylase inhibitors modulate the sensitivity of tumor necrosis factor-related apoptosis-inducing ligand-resistant bladder tumor cells. Cancer Res 2006;66:499-507. (Pubitemid 43166059)
    • (2006) Cancer Research , vol.66 , Issue.1 , pp. 499-507
    • Earel Jr., J.K.1    VanOosten, R.L.2    Griffith, T.S.3
  • 45
    • 33947584285 scopus 로고    scopus 로고
    • Effect of valproic acid, a histone deacetylase inhibitor, on cell death and molecular changes caused by low-dose irradiation
    • DOI 10.1196/annals.1378.082, Signal Transduction Pathways, Part B: Stress Signalling and Transcriptional Control
    • Zaskodova D, Rezacova M, Vavrova J, Vokurkova D, Tichy A. Effect of valproic acid, a histone deacetylase inhibitor, on cell death and molecular changes caused by low-dose irradiation. Ann N Y Acad Sci 2006;1091:385-98. (Pubitemid 47092252)
    • (2006) Annals of the New York Academy of Sciences , vol.1091 , pp. 385-398
    • Zaskodova, D.1    Rezacova, M.2    Vavrova, J.3    Vokurkova, D.4    Tichy, A.5
  • 46
    • 34247557008 scopus 로고    scopus 로고
    • Enhancement of cisplatin induced apoptosis by suberoylanilide hydroxamic acid in human oral squamous cell carcinoma cell lines
    • DOI 10.1016/j.bcp.2007.03.009, PII S0006295207001566
    • Shen J, Huang C, Jiang L, Gao F, Wang Z, Zhang Y, et al. Enhancement of cisplatin induced apoptosis by suberoylanilide hydroxamic acid in human oral squamous cell carcinoma cell lines. Biochem Pharmacol 2007;73:1901-9. (Pubitemid 46677907)
    • (2007) Biochemical Pharmacology , vol.73 , Issue.12 , pp. 1901-1909
    • Shen, J.1    Huang, C.2    Jiang, L.3    Gao, F.4    Wang, Z.5    Zhang, Y.6    Bai, J.7    Zhou, H.8    Chen, Q.9
  • 47
    • 79952697614 scopus 로고    scopus 로고
    • Potentiation of apoptosis by histone deacetylase inhibitors and doxorubicin combination: Cytoplasmic cathepsin B as a mediator of apoptosis in multiple myeloma
    • Cheriyath V, Kuhns MA, Kalaycio ME, Borden EC. Potentiation of apoptosis by histone deacetylase inhibitors and doxorubicin combination: cytoplasmic cathepsin B as a mediator of apoptosis in multiple myeloma. Br J Cancer 2011;104:957-67.
    • (2011) Br J Cancer , vol.104 , pp. 957-967
    • Cheriyath, V.1    Kuhns, M.A.2    Kalaycio, M.E.3    Borden, E.C.4
  • 48
    • 76049119711 scopus 로고    scopus 로고
    • HDAC inhibition radiosensitizes human normal tissue cells and reduces DNA double-strand break repair capacity
    • Purrucker JC, Fricke A, Ong MF, Rube C, Rube CE, Mahlknecht U. HDAC inhibition radiosensitizes human normal tissue cells and reduces DNA double-strand break repair capacity. Oncol Rep 2010;23:263-9.
    • (2010) Oncol Rep , vol.23 , pp. 263-269
    • Purrucker, J.C.1    Fricke, A.2    Ong, M.F.3    Rube, C.4    Rube, C.E.5    Mahlknecht, U.6
  • 49
    • 78651352243 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Potential targets responsible for their anti-cancer effect
    • Dickinson M, Johnstone RW, Prince HM. Histone deacetylase inhibitors: potential targets responsible for their anti-cancer effect. Invest New Drugs 2010;28 Suppl 1:S3-20.
    • (2010) Invest New Drugs , vol.28 , Issue.SUPPL. 1
    • Dickinson, M.1    Johnstone, R.W.2    Prince, H.M.3


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