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Volumn 306, Issue 2, 2011, Pages 223-229

Cooperation of the HDAC inhibitor vorinostat and radiation in metastatic neuroblastoma: Efficacy and underlying mechanisms

Author keywords

DNA repair; Metastatic neuroblastoma; Radiation; Vorinostat

Indexed keywords

HISTONE H2AX; HISTONE H4; KU 86 PROTEIN; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; RAD51 PROTEIN; UNCLASSIFIED DRUG; VORINOSTAT;

EID: 79955484293     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2011.03.010     Document Type: Article
Times cited : (72)

References (21)
  • 2
    • 33748360764 scopus 로고    scopus 로고
    • Vorinostat, a histone deacetylase inhibitor, enhances the response of human tumor cells to ionizing radiation through prolongation of gamma-H2AX foci
    • Munshi A., Tanaka T., Hobbs M.L., Tucker S.L., Richon V.M., Meyn R.E. Vorinostat, a histone deacetylase inhibitor, enhances the response of human tumor cells to ionizing radiation through prolongation of gamma-H2AX foci. Mol. Cancer Ther. 2006, 5:1967-1974.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 1967-1974
    • Munshi, A.1    Tanaka, T.2    Hobbs, M.L.3    Tucker, S.L.4    Richon, V.M.5    Meyn, R.E.6
  • 4
    • 30344476415 scopus 로고    scopus 로고
    • Butyric acid prodrugs are histone deacetylase inhibitors that show antineoplastic activity and radiosensitizing capacity in the treatment of malignant gliomas
    • Entin-Meer M., Rephaeli A., Yang X., Nudelman A., VandenBerg S.R., Haas-Kogan D.A. Butyric acid prodrugs are histone deacetylase inhibitors that show antineoplastic activity and radiosensitizing capacity in the treatment of malignant gliomas. Mol. Cancer Ther. 2005, 4:1952-1961.
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1952-1961
    • Entin-Meer, M.1    Rephaeli, A.2    Yang, X.3    Nudelman, A.4    VandenBerg, S.R.5    Haas-Kogan, D.A.6
  • 6
    • 65449177752 scopus 로고    scopus 로고
    • Radiosensitization by SAHA in experimental colorectal carcinoma models-in vivo effects and relevance of histone acetylation status
    • Folkvord S., Ree A.H., Furre T., Halvorsen T., Flatmark K. Radiosensitization by SAHA in experimental colorectal carcinoma models-in vivo effects and relevance of histone acetylation status. Int. J. Radiat. Oncol. Biol. Phys. 2009, 74:546-552.
    • (2009) Int. J. Radiat. Oncol. Biol. Phys. , vol.74 , pp. 546-552
    • Folkvord, S.1    Ree, A.H.2    Furre, T.3    Halvorsen, T.4    Flatmark, K.5
  • 8
    • 77952310681 scopus 로고    scopus 로고
    • Vorinostat, a histone deacetylase inhibitor, combined with pelvic palliative radiotherapy for gastrointestinal carcinoma: the Pelvic Radiation and Vorinostat (PRAVO) phase 1 study, Lancet Oncol.
    • A.H. Ree, S. Dueland, S. Folkvord, K.H. Hole, T. Seierstad, M. Johansen, T.W. Abrahamsen, K. Flatmark, Vorinostat, a histone deacetylase inhibitor, combined with pelvic palliative radiotherapy for gastrointestinal carcinoma: the Pelvic Radiation and Vorinostat (PRAVO) phase 1 study, Lancet Oncol. 11, 459-464.
    • , vol.11 , pp. 459-464
    • Ree, A.H.1    Dueland, S.2    Folkvord, S.3    Hole, K.H.4    Seierstad, T.5    Johansen, M.6    Abrahamsen, T.W.7    Flatmark, K.8
  • 10
    • 34347360705 scopus 로고    scopus 로고
    • In vivo bioluminescence imaging for early detection and monitoring of disease progression in a murine model of neuroblastoma
    • Dickson P.V., Hamner B., Ng C.Y., Hall M.M., Zhou J., Hargrove P.W., McCarville M.B., Davidoff A.M. In vivo bioluminescence imaging for early detection and monitoring of disease progression in a murine model of neuroblastoma. J. Pediatr. Surg. 2007, 42:1172-1179.
    • (2007) J. Pediatr. Surg. , vol.42 , pp. 1172-1179
    • Dickson, P.V.1    Hamner, B.2    Ng, C.Y.3    Hall, M.M.4    Zhou, J.5    Hargrove, P.W.6    McCarville, M.B.7    Davidoff, A.M.8
  • 11
    • 0029743372 scopus 로고    scopus 로고
    • Conditional expression of N-myc in human neuroblastoma cells increases expression of alpha-prothymosin and ornithine decarboxylase and accelerates progression into S-phase early after mitogenic stimulation of quiescent cells
    • Lutz W., Stohr M., Schurmann J., Wenzel A., Lohr A., Schwab M. Conditional expression of N-myc in human neuroblastoma cells increases expression of alpha-prothymosin and ornithine decarboxylase and accelerates progression into S-phase early after mitogenic stimulation of quiescent cells. Oncogene 1996, 13:803-812.
    • (1996) Oncogene , vol.13 , pp. 803-812
    • Lutz, W.1    Stohr, M.2    Schurmann, J.3    Wenzel, A.4    Lohr, A.5    Schwab, M.6
  • 14
    • 0036261707 scopus 로고    scopus 로고
    • Sensing and repairing DNA double-strand breaks
    • Jackson S.P. Sensing and repairing DNA double-strand breaks. Carcinogenesis 2002, 23:687-696.
    • (2002) Carcinogenesis , vol.23 , pp. 687-696
    • Jackson, S.P.1
  • 16
    • 31044432090 scopus 로고    scopus 로고
    • XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining
    • Ahnesorg P., Smith P., Jackson S.P. XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining. Cell 2006, 124:301-313.
    • (2006) Cell , vol.124 , pp. 301-313
    • Ahnesorg, P.1    Smith, P.2    Jackson, S.P.3
  • 17
    • 49049095275 scopus 로고    scopus 로고
    • Radiolabeled metaiodobenzylguanidine for the treatment of neuroblastoma
    • DuBois S.G., Matthay K.K. Radiolabeled metaiodobenzylguanidine for the treatment of neuroblastoma. Nucl. Med. Biol. 2008, 35(Suppl. 1):S35-S48.
    • (2008) Nucl. Med. Biol. , vol.35 , Issue.SUPPL. 1
    • DuBois, S.G.1    Matthay, K.K.2
  • 20
    • 77957091318 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor induces DNA damage, which normal but not transformed cells can repair
    • USA
    • J.H. Lee, M.L. Choy, L. Ngo, S.S. Foster, P.A. Marks, Histone deacetylase inhibitor induces DNA damage, which normal but not transformed cells can repair, Proc. Natl. Acad. Sci. USA 107, 14639-14644.
    • Proc. Natl. Acad. Sci. , vol.107 , pp. 14639-14644
    • Lee, J.H.1    Choy, M.L.2    Ngo, L.3    Foster, S.S.4    Marks, P.A.5
  • 21
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • Masumoto H., Hawke D., Kobayashi R., Verreault A. A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 2005, 436:294-298.
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.