메뉴 건너뛰기




Volumn 6, Issue 4, 2015, Pages 935-956

Epigenetic therapy for solid tumors: Highlighting the impact of tumor hypoxia

Author keywords

DNA methylation; Epigenetic drugs; Gene repression; Histone deacetylation; Histone methylation; Tumor hypoxia

Indexed keywords

AZACITIDINE; BELINOSTAT; BORTEZOMIB; BRCA1 PROTEIN; CASPASE; CISPLATIN; DECITABINE; DNA; DNA METHYLTRANSFERASE; ENTINOSTAT; ERLOTINIB; HISTONE; HISTONE DEACETYLASE INHIBITOR; HYDRALAZINE; PANOBINOSTAT; ROMIDEPSIN; SUPPRESSOR OF CYTOKINE SIGNALING; TOPOTECAN; VALPROIC ACID; VORINOSTAT;

EID: 84942778310     PISSN: None     EISSN: 20734425     Source Type: Journal    
DOI: 10.3390/genes6040935     Document Type: Review
Times cited : (44)

References (118)
  • 1
    • 84923782190 scopus 로고    scopus 로고
    • Histone exchange, chromatin structure and the regulation of transcription
    • Venkatesh, S.; Workman, J.L. Histone exchange, chromatin structure and the regulation of transcription. Nat. Rev. Mol. Cell Biol. 2015, 16, 178–189
    • (2015) Nat. Rev. Mol. Cell Biol , vol.16 , pp. 178-189
    • Venkatesh, S.1    Workman, J.L.2
  • 2
    • 80755153672 scopus 로고    scopus 로고
    • Chromatin as an oxygen sensor and active player in the hypoxia response
    • Melvin, A.; Rocha, S. Chromatin as an oxygen sensor and active player in the hypoxia response. Cell. Signal. 2012, 24, 35–43
    • (2012) Cell. Signal , vol.24 , pp. 35-43
    • Melvin, A.1    Rocha, S.2
  • 3
    • 84858295994 scopus 로고    scopus 로고
    • Gupta, S. Epigenetic modifications in cancer
    • Kanwal, R.; Gupta, S. Epigenetic modifications in cancer. Clin. Genet. 2012, 81, 303–311
    • (2012) Clin. Genet , vol.81 , pp. 303-311
    • Kanwal, R.1
  • 4
    • 84888090995 scopus 로고    scopus 로고
    • Histone lysine-specific methyltransferases and demethylases in carcinogenesis: New targets for cancer therapy and prevention
    • Tian, X.; Zhang, S.; Liu, H.M.; Zhang, Y.B.; Blair, C.A.; Mercola, D.; Sassone-Corsi, P.; Zi, X. Histone lysine-specific methyltransferases and demethylases in carcinogenesis: New targets for cancer therapy and prevention. Curr. Cancer Drug Targets 2013, 13, 558–579
    • (2013) Curr. Cancer Drug Targets , vol.13 , pp. 558-579
    • Tian, X.1    Zhang, S.2    Liu, H.M.3    Zhang, Y.B.4    Blair, C.A.5    Mercola, D.6    Sassone-Corsi, P.7    Zi, X.8
  • 6
    • 84923106261 scopus 로고    scopus 로고
    • DNMT1 and EZH2 mediated methylation silences the microRNA-200B/A/429 gene and promotes tumor progression
    • Ning, X.; Shi, Z.; Liu, X.; Zhang, A.; Han, L.; Jiang, K.; Kang, C.; Zhang, Q. DNMT1 and EZH2 mediated methylation silences the microRNA-200B/A/429 gene and promotes tumor progression. Cancer Lett. 2015, 359, 198–205
    • (2015) Cancer Lett , vol.359 , pp. 198-205
    • Ning, X.1    Shi, Z.2    Liu, X.3    Zhang, A.4    Han, L.5    Jiang, K.6    Kang, C.7    Zhang, Q.8
  • 7
    • 64049097640 scopus 로고    scopus 로고
    • The promises and pitfalls of epigenetic therapies in solid tumours
    • Graham, J.S.; Kaye, S.B.; Brown, R. The promises and pitfalls of epigenetic therapies in solid tumours. Eur. J. Cancer 2009, 45, 1129–1136
    • (2009) Eur. J. Cancer , vol.45 , pp. 1129-1136
    • Graham, J.S.1    Kaye, S.B.2    Brown, R.3
  • 9
    • 84874072228 scopus 로고    scopus 로고
    • Demethylation and re-expression of epigenetically silenced tumor suppressor genes: Sensitization of cancer cells by combination therapy
    • Sarkar, S.; Goldgar, S.; Byler, S.; Rosenthal, S.; Heerboth, S. Demethylation and re-expression of epigenetically silenced tumor suppressor genes: Sensitization of cancer cells by combination therapy. Epigenomics 2013, 5, 87–94
    • (2013) Epigenomics , vol.5 , pp. 87-94
    • Sarkar, S.1    Goldgar, S.2    Byler, S.3    Rosenthal, S.4    Heerboth, S.5
  • 11
    • 33646128506 scopus 로고    scopus 로고
    • Epigenetics as a mechanism driving polygenic clinical drug resistance
    • Glasspool, R.M.; Teodoridis, J.M.; Brown, R. Epigenetics as a mechanism driving polygenic clinical drug resistance. Br. J. Cancer 2006, 94, 1087–1092
    • (2006) Br. J. Cancer , vol.94 , pp. 1087-1092
    • Glasspool, R.M.1    Teodoridis, J.M.2    Brown, R.3
  • 14
    • 34249774568 scopus 로고    scopus 로고
    • Transcriptional silencing of the TMS1/ASC tumour suppressor gene by an epigenetic mechanism in hepatocellular carcinoma cells
    • Zhang, C.; Li, H.; Zhou, G.; Zhang, Q.; Zhang, T.; Li, J.; Zhang, J.; Hou, J.; Liew, C.T.; Yin, D. Transcriptional silencing of the TMS1/ASC tumour suppressor gene by an epigenetic mechanism in hepatocellular carcinoma cells. J. Pathol. 2007, 212, 134–142
    • (2007) J. Pathol , vol.212 , pp. 134-142
    • Zhang, C.1    Li, H.2    Zhou, G.3    Zhang, Q.4    Zhang, T.5    Li, J.6    Zhang, J.7    Hou, J.8    Liew, C.T.9    Yin, D.10
  • 15
    • 84927663989 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling (SOCS) genes are silenced by DNA hypermethylation and histone deacetylation and regulate response to radiotherapy in cervical cancer cells
    • Kim, M.H.; Kim, M.S.; Kim, W.; Kang, M.A.; Cacalano, N.A.; Kang, S.B.; Shin, Y.J.; Jeong, J.H. Suppressor of cytokine signaling (SOCS) genes are silenced by DNA hypermethylation and histone deacetylation and regulate response to radiotherapy in cervical cancer cells. PLoS ONE 2015, 10, e0123133
    • (2015) Plos ONE , vol.10
    • Kim, M.H.1    Kim, M.S.2    Kim, W.3    Kang, M.A.4    Cacalano, N.A.5    Kang, S.B.6    Shin, Y.J.7    Jeong, J.H.8
  • 16
    • 11144295220 scopus 로고    scopus 로고
    • Silencing of the retinoid response gene TIG1 by promoter hypermethylation in nasopharyngeal carcinoma
    • Kwong, J.; Lo, K.W.; Chow, L.S.; Chan, F.L.; To, K.F.; Huang, D.P. Silencing of the retinoid response gene TIG1 by promoter hypermethylation in nasopharyngeal carcinoma. Int. J. Cancer 2005, 113, 386–392
    • (2005) Int. J. Cancer , vol.113 , pp. 386-392
    • Kwong, J.1    Lo, K.W.2    Chow, L.S.3    Chan, F.L.4    To, K.F.5    Huang, D.P.6
  • 17
    • 76149096516 scopus 로고    scopus 로고
    • Methylation associated inactivation of RASSF1A and its synergistic effect with activated K-Ras in nasopharyngeal carcinoma
    • Wang, T.; Liu, H.; Chen, Y.; Liu, W.; Yu, J.; Wu, G. Methylation associated inactivation of RASSF1A and its synergistic effect with activated K-Ras in nasopharyngeal carcinoma. J. Exp. Clin. Cancer Res. 2009, doi:10.1186/1756-9966-28-160
    • (2009) J. Exp. Clin. Cancer Res
    • Wang, T.1    Liu, H.2    Chen, Y.3    Liu, W.4    Yu, J.5    Wu, G.6
  • 18
    • 77952989040 scopus 로고    scopus 로고
    • Putative tumour-suppressor gene DAB2 is frequently down regulated by promoter hypermethylation in nasopharyngeal carcinoma
    • Tong, J.H.; Ng, D.C.; Chau, S.L.; So, K.K.; Leung, P.P.; Lee, T.L.; Lung, R.W.; Chan, M.W.; Chan, A.W.; Lo, K.W., et al. Putative tumour-suppressor gene DAB2 is frequently down regulated by promoter hypermethylation in nasopharyngeal carcinoma. BMC Cancer 2010, doi:10.1186/1471-2407-10-253
    • (2010) BMC Cancer
    • Tong, J.H.1    Ng, D.C.2    Chau, S.L.3    So, K.K.4    Leung, P.P.5    Lee, T.L.6    Lung, R.W.7    Chan, M.W.8    Chan, A.W.9    Lo, K.W.10
  • 19
    • 84886997326 scopus 로고    scopus 로고
    • FEZF2, a novel 3P14 tumor suppressor gene, represses oncogene EZH2 and MDM2 expression and is frequently methylated in nasopharyngeal carcinoma
    • Shu, X.S.; Li, L.; Ji, M.; Cheng, Y.; Ying, J.; Fan, Y.; Zhong, L.; Liu, X.; Tsao, S.W.; Chan, A.T., et al. FEZF2, a novel 3P14 tumor suppressor gene, represses oncogene EZH2 and MDM2 expression and is frequently methylated in nasopharyngeal carcinoma. Carcinogenesis 2013, 34, 1984–1993
    • (2013) Carcinogenesis , vol.34 , pp. 1984-1993
    • Shu, X.S.1    Li, L.2    Ji, M.3    Cheng, Y.4    Ying, J.5    Fan, Y.6    Zhong, L.7    Liu, X.8    Tsao, S.W.9    Chan, A.T.10
  • 20
    • 84923446785 scopus 로고    scopus 로고
    • Targeting chromatin to improve radiation response
    • Olcina, M.M.; O’Dell, S.; Hammond, E.M. Targeting chromatin to improve radiation response. Br. J. Radiol. 2015, doi:10.1259/bjr.20140649
    • (2015) Br. J. Radiol
    • Olcina, M.M.1    O’Dell, S.2    Hammond, E.M.3
  • 21
    • 82955169581 scopus 로고    scopus 로고
    • Epigenetic-based therapies in cancer: Progress to date
    • Song, S.H.; Han, S.W.; Bang, Y.J. Epigenetic-based therapies in cancer: Progress to date. Drugs 2011, 71, 2391–2403
    • (2011) Drugs , vol.71 , pp. 2391-2403
    • Song, S.H.1    Han, S.W.2    Bang, Y.J.3
  • 23
    • 84930654453 scopus 로고    scopus 로고
    • Epigenetic therapy of cancer stem and progenitor cells by targeting DNA methylation machineries
    • Wongtrakoongate, P. Epigenetic therapy of cancer stem and progenitor cells by targeting DNA methylation machineries. World J. Stem Cells 2015, 7, 137–148
    • (2015) World J. Stem Cells , vol.7 , pp. 137-148
    • Wongtrakoongate, P.1
  • 24
    • 0037112369 scopus 로고    scopus 로고
    • Histone H3-lysine 9 methylation is associated with aberrant gene silencing in cancer cells and is rapidly reversed by 5-aza-2'-deoxycytidine
    • Nguyen, C.T.; Weisenberger, D.J.; Velicescu, M.; Gonzales, F.A.; Lin, J.C.; Liang, G.; Jones, P.A. Histone H3-lysine 9 methylation is associated with aberrant gene silencing in cancer cells and is rapidly reversed by 5-aza-2'-deoxycytidine. Cancer Res. 2002, 62, 6456–6461
    • (2002) Cancer Res , vol.62 , pp. 6456-6461
    • Nguyen, C.T.1    Weisenberger, D.J.2    Velicescu, M.3    Gonzales, F.A.4    Lin, J.C.5    Liang, G.6    Jones, P.A.7
  • 25
    • 0021723569 scopus 로고
    • Comparison of the antileukemic activity of 5-Aza-2'-deoxycytidine, 1-α-D-arabinofuranosylcytosine and 5-azacytidine against L1210 leukemia
    • Momparler, R.L.; Momparler, L.F.; Samson, J. Comparison of the antileukemic activity of 5-Aza-2'-deoxycytidine, 1-α-D-arabinofuranosylcytosine and 5-azacytidine against L1210 leukemia. Leuk. Res. 1984, 8, 1043–1049
    • (1984) Leuk. Res , vol.8 , pp. 1043-1049
    • Momparler, R.L.1    Momparler, L.F.2    Samson, J.3
  • 26
    • 0033988813 scopus 로고    scopus 로고
    • Methyltransferase dnmt1 associates with histone deacetylase activity. Nat
    • Fuks, F.; Burgers, W.A.; Brehm, A.; Hughes-Davies, L.; Kouzarides, T. DNA methyltransferase dnmt1 associates with histone deacetylase activity. Nat. Genet. 2000, 24, 88–91
    • (2000) Genet , vol.24 , pp. 88-91
    • Fuks, F.1    Burgers, W.A.2    Brehm, A.3    Hughes-Davies, L.4    Kouzarides, T.5
  • 27
    • 0033919595 scopus 로고    scopus 로고
    • DNMT1 forms a complex with RB, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters
    • Robertson, K.D.; Ait-Si-Ali, S.; Yokochi, T.; Wade, P.A.; Jones, P.L.; Wolffe, A.P. DNMT1 forms a complex with RB, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters. Nat. Genet. 2000, 25, 338–342
    • (2000) Nat. Genet , vol.25 , pp. 338-342
    • Robertson, K.D.1    Ait-Si-Ali, S.2    Yokochi, T.3    Wade, P.A.4    Jones, P.L.5    Wolffe, A.P.6
  • 28
    • 84929598341 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in clinical studies as templates for new anticancer agents
    • Mottamal, M.; Zheng, S.; Huang, T.L.; Wang, G. Histone deacetylase inhibitors in clinical studies as templates for new anticancer agents. Molecules 2015, 20, 3898–3941
    • (2015) Molecules , vol.20 , pp. 3898-3941
    • Mottamal, M.1    Zheng, S.2    Huang, T.L.3    Wang, G.4
  • 29
    • 77958199188 scopus 로고    scopus 로고
    • Epigenetic cancer therapy: Proof of concept and remaining challenges
    • Mund, C.; Lyko, F. Epigenetic cancer therapy: Proof of concept and remaining challenges. BioEssays News Rev. Mol. Cell. Dev. Biol. 2010, 32, 949–957
    • (2010) Bioessays News Rev. Mol. Cell. Dev. Biol , vol.32 , pp. 949-957
    • Mund, C.1    Lyko, F.2
  • 30
    • 84877574817 scopus 로고    scopus 로고
    • The future of epigenetic therapy in solid tumours—Lessons from the past
    • Azad, N.; Zahnow, C.A.; Rudin, C.M.; Baylin, S.B. The future of epigenetic therapy in solid tumours—Lessons from the past. Nat. Rev. Clin. Oncol. 2013, 10, 256–266
    • (2013) Nat. Rev. Clin. Oncol , vol.10 , pp. 256-266
    • Azad, N.1    Zahnow, C.A.2    Rudin, C.M.3    Baylin, S.B.4
  • 31
    • 84930865181 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor, vorinostat, represses hypoxia inducible factor 1α expression through translational inhibition
    • Hutt, D.M.; Roth, D.M.; Vignaud, H.; Cullin, C.; Bouchecareilh, M. The histone deacetylase inhibitor, vorinostat, represses hypoxia inducible factor 1α expression through translational inhibition. PLoS ONE 2014, 9, e106224
    • (2014) Plos ONE , vol.9
    • Hutt, D.M.1    Roth, D.M.2    Vignaud, H.3    Cullin, C.4    Bouchecareilh, M.5
  • 33
    • 84891837817 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: An overview of the clinical studies in solid tumors
    • Slingerland, M.; Guchelaar, H.J.; Gelderblom, H. Histone deacetylase inhibitors: An overview of the clinical studies in solid tumors. AntiCancer Drugs 2014, 25, 140–149
    • (2014) Anticancer Drugs , vol.25 , pp. 140-149
    • Slingerland, M.1    Guchelaar, H.J.2    Gelderblom, H.3
  • 34
    • 81555228390 scopus 로고    scopus 로고
    • Belinostat: Clinical applications in solid tumors and lymphoma. Expert Opin. Investig
    • Molife, L.R.; de Bono, J.S. Belinostat: Clinical applications in solid tumors and lymphoma. Expert Opin. Investig. Drugs 2011, 20, 1723–1732
    • (2011) Drugs , vol.20 , pp. 1723-1732
    • Molife, L.R.1    De Bono, J.S.2
  • 35
    • 0032053823 scopus 로고    scopus 로고
    • The unique physiology of solid tumors: Opportunities (and problems) for cancer therapy
    • Brown, J.M.; Giaccia, A.J. The unique physiology of solid tumors: Opportunities (and problems) for cancer therapy. Cancer Res. 1998, 58, 1408–1416
    • (1998) Cancer Res , vol.58 , pp. 1408-1416
    • Brown, J.M.1    Giaccia, A.J.2
  • 37
    • 58149242889 scopus 로고    scopus 로고
    • A phase II trial of vorinostat (Suberoylanilide hydroxamic acid) in metastatic breast cancer: A California cancer consortium study
    • Luu, T.H.; Morgan, R.J.; Leong, L.; Lim, D.; McNamara, M.; Portnow, J.; Frankel, P.; Smith, D.D.; Doroshow, J.H.; Wong, C., et al. A phase II trial of vorinostat (suberoylanilide hydroxamic acid) in metastatic breast cancer: A California cancer consortium study. Clin. Cancer Res. 2008, 14, 7138–7142
    • (2008) Clin. Cancer Res , vol.14 , pp. 7138-7142
    • Luu, T.H.1    Morgan, R.J.2    Leong, L.3    Lim, D.4    McNamara, M.5    Portnow, J.6    Frankel, P.7    Smith, D.D.8    Doroshow, J.H.9    Wong, C.10
  • 38
    • 43049091153 scopus 로고    scopus 로고
    • Study of vorinostat in the treatment of persistent or recurrent epithelial ovarian or primary peritoneal carcinoma: A gynecologic oncology group study
    • Modesitt, S.C.; Sill, M.; Hoffman, J.S.; Bender, D.P. A phase II study of vorinostat in the treatment of persistent or recurrent epithelial ovarian or primary peritoneal carcinoma: A gynecologic oncology group study. Gynecol. Oncol. 2008, 109, 182–186
    • (2008) Gynecol. Oncol , vol.109 , pp. 182-186
    • Modesitt, S.C.1    Sill, M.2    Hoffman, J.S.3    Bender, D.4    Phase, I.I.5
  • 39
    • 38149140216 scopus 로고    scopus 로고
    • Phase II trial of the histone deacetylase inhibitor vorinostat (Zolinza, suberoylanilide hydroxamic acid, saha) in patients with recurrent and/or metastatic head and neck cancer. Investig
    • Blumenschein, G.R., Jr.; Kies, M.S.; Papadimitrakopoulou, V.A.; Lu, C.; Kumar, A.J.; Ricker, J.L.; Chiao, J.H.; Chen, C.; Frankel, S.R. Phase II trial of the histone deacetylase inhibitor vorinostat (zolinza, suberoylanilide hydroxamic acid, saha) in patients with recurrent and/or metastatic head and neck cancer. Investig. New Drugs 2008, 26, 81–87
    • (2008) New Drugs , vol.26 , pp. 81-87
    • Blumenschein, G.R.1    Kies, M.S.2    Papadimitrakopoulou, V.A.3    Lu, C.4    Kumar, A.J.5    Ricker, J.L.6    Chiao, J.H.7    Chen, C.8    Frankel, S.R.9
  • 44
    • 70549105748 scopus 로고    scopus 로고
    • Phase II, two-stage, single-arm trial of the histone deacetylase inhibitor (HDACI) romidepsin in metastatic castration-resistant prostate cancer (CRPC)
    • Molife, L.R.; Attard, G.; Fong, P.C.; Karavasilis, V.; Reid, A.H.; Patterson, S.; Riggs, C.E., Jr.; Higano, C.; Stadler, W.M.; McCulloch, W., et al. Phase II, two-stage, single-arm trial of the histone deacetylase inhibitor (HDACI) romidepsin in metastatic castration-resistant prostate cancer (CRPC). Ann. Oncol. 2010, 21, 109–113
    • (2010) Ann. Oncol , vol.21 , pp. 109-113
    • Molife, L.R.1    Attard, G.2    Fong, P.C.3    Karavasilis, V.4    Reid, A.H.5    Patterson, S.6    Riggs, C.E.7    Higano, C.8    Stadler, W.M.9    McCulloch, W.10
  • 45
    • 77958185126 scopus 로고    scopus 로고
    • Phase II study of the histone deacetylase inhibitor romidepsin in relapsed small cell lung cancer (Cancer and leukemia group B 30304)
    • Otterson, G.A.; Hodgson, L.; Pang, H.; Vokes, E.E. Phase II study of the histone deacetylase inhibitor romidepsin in relapsed small cell lung cancer (cancer and leukemia group B 30304). J. Thoracic Oncol. 2010, 5, 1644–1648
    • (2010) J. Thoracic Oncol , vol.5 , pp. 1644-1648
    • Otterson, G.A.1    Hodgson, L.2    Pang, H.3    Vokes, E.E.4
  • 47
    • 79960197509 scopus 로고    scopus 로고
    • A phase II trial of panobinostat, a histone deacetylase inhibitor, in the treatment of patients with refractory metastatic renal cell carcinoma
    • Hainsworth, J.D.; Infante, J.R.; Spigel, D.R.; Arrowsmith, E.R.; Boccia, R.V.; Burris, H.A. A phase II trial of panobinostat, a histone deacetylase inhibitor, in the treatment of patients with refractory metastatic renal cell carcinoma. Cancer Investig. 2011, 29, 451–455
    • (2011) Cancer Investig , vol.29 , pp. 451-455
    • Hainsworth, J.D.1    Infante, J.R.2    Spigel, D.R.3    Arrowsmith, E.R.4    Boccia, R.V.5    Burris, H.A.6
  • 48
    • 84863339591 scopus 로고    scopus 로고
    • Phase II study of panobinostat and bortezomib in patients with pancreatic cancer progressing on gemcitabine-based therapy
    • Wang, H.; Cao, Q.; Dudek, A.Z. Phase II study of panobinostat and bortezomib in patients with pancreatic cancer progressing on gemcitabine-based therapy. Anticancer Res. 2012, 32, 1027–1031
    • (2012) Anticancer Res , vol.32 , pp. 1027-1031
    • Wang, H.1    Cao, Q.2    Dudek, A.Z.3
  • 49
    • 58149377828 scopus 로고    scopus 로고
    • Multicenter phase II trial of the histone deacetylase inhibitor pyridylmethyl-N-{4-[(2-aminophenyl)-carbamoyl]-benzyl}-carbamate in pretreated metastatic melanoma
    • Hauschild, A.; Trefzer, U.; Garbe, C.; Kaehler, K.C.; Ugurel, S.; Kiecker, F.; Eigentler, T.; Krissel, H.; Schott, A.; Schadendorf, D. Multicenter phase II trial of the histone deacetylase inhibitor pyridylmethyl-N-{4-[(2-aminophenyl)-carbamoyl]-benzyl}-carbamate in pretreated metastatic melanoma. Melanoma Res. 2008, 18, 274–278
    • (2008) Melanoma Res , vol.18 , pp. 274-278
    • Hauschild, A.1    Trefzer, U.2    Garbe, C.3    Kaehler, K.C.4    Ugurel, S.5    Kiecker, F.6    Eigentler, T.7    Krissel, H.8    Schott, A.9    Schadendorf, D.10
  • 50
    • 84864004796 scopus 로고    scopus 로고
    • Randomized phase II trial of erlotinib with and without entinostat in patients with advanced non-small-cell lung cancer who progressed on prior chemotherapy
    • Witta, S.E.; Jotte, R.M.; Konduri, K.; Neubauer, M.A.; Spira, A.I.; Ruxer, R.L.; Varella-Garcia, M.; Bunn, P.A., Jr.; Hirsch, F.R. Randomized phase II trial of erlotinib with and without entinostat in patients with advanced non-small-cell lung cancer who progressed on prior chemotherapy. J. Clin. Oncol. 2012, 30, 2248–2255
    • (2012) J. Clin. Oncol , vol.30 , pp. 2248-2255
    • Witta, S.E.1    Jotte, R.M.2    Konduri, K.3    Neubauer, M.A.4    Spira, A.I.5    Ruxer, R.L.6    Varella-Garcia, M.7    Bunn, P.A.8    Hirsch, F.R.9
  • 55
    • 79952266135 scopus 로고    scopus 로고
    • Phase 1B-2A study to reverse platinum resistance through use of a hypomethylating agent, azacitidine, in patients with platinum-resistant or platinum-refractory epithelial ovarian cancer
    • Fu, S.; Hu, W.; Iyer, R.; Kavanagh, J.J.; Coleman, R.L.; Levenback, C.F.; Sood, A.K.; Wolf, J.K.; Gershenson, D.M.; Markman, M., et al. Phase 1B-2A study to reverse platinum resistance through use of a hypomethylating agent, azacitidine, in patients with platinum-resistant or platinum-refractory epithelial ovarian cancer. Cancer 2011, 117, 1661–1669
    • (2011) Cancer , vol.117 , pp. 1661-1669
    • Fu, S.1    Hu, W.2    Iyer, R.3    Kavanagh, J.J.4    Coleman, R.L.5    Levenback, C.F.6    Sood, A.K.7    Wolf, J.K.8    Gershenson, D.M.9    Markman, M.10
  • 57
  • 59
    • 55249109006 scopus 로고    scopus 로고
    • Tumour hypoxia affects the responsiveness of cancer cells to chemotherapy and promotes cancer progression
    • Cosse, J.P.; Michiels, C. Tumour hypoxia affects the responsiveness of cancer cells to chemotherapy and promotes cancer progression. Anti-Cancer Agents Med. Chem. 2008, 8, 790–797
    • (2008) Anti-Cancer Agents Med. Chem , vol.8 , pp. 790-797
    • Cosse, J.P.1    Michiels, C.2
  • 60
    • 26444466467 scopus 로고    scopus 로고
    • Prognostic value of tumor oxygenation in 397 head and neck tumors after primary radiation therapy. An international multi-center study
    • Nordsmark, M.; Bentzen, S.M.; Rudat, V.; Brizel, D.; Lartigau, E.; Stadler, P.; Becker, A.; Adam, M.; Molls, M.; Dunst, J., et al. Prognostic value of tumor oxygenation in 397 head and neck tumors after primary radiation therapy. An international multi-center study. Radiother. Oncol. 2005, 77, 18–24
    • (2005) Radiother. Oncol , vol.77 , pp. 18-24
    • Nordsmark, M.1    Bentzen, S.M.2    Rudat, V.3    Brizel, D.4    Lartigau, E.5    Stadler, P.6    Becker, A.7    Adam, M.8    Molls, M.9    Dunst, J.10
  • 61
    • 0032190614 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1: Master regulator of O2 homeostasis
    • Semenza, G.L. Hypoxia-inducible factor 1: Master regulator of O2 homeostasis. Curr. Opin. Genet. Dev. 1998, 8, 588–594
    • (1998) Curr. Opin. Genet. Dev , vol.8 , pp. 588-594
    • Semenza, G.L.1
  • 62
    • 84879556042 scopus 로고    scopus 로고
    • Epigenetic regulation of hypoxia inducible factor in diseases and therapeutics
    • Nguyen, M.P.; Lee, S.; Lee, Y.M. Epigenetic regulation of hypoxia inducible factor in diseases and therapeutics. Arch. Pharm. Res. 2013, 36, 252–263
    • (2013) Arch. Pharm. Res , vol.36 , pp. 252-263
    • Nguyen, M.P.1    Lee, S.2    Lee, Y.M.3
  • 63
    • 67349201377 scopus 로고    scopus 로고
    • Targeting tumor angiogenesis with histone deacetylase inhibitors
    • Ellis, L.; Hammers, H.; Pili, R. Targeting tumor angiogenesis with histone deacetylase inhibitors. Cancer Lett. 2009, 280, 145–153
    • (2009) Cancer Lett , vol.280 , pp. 145-153
    • Ellis, L.1    Hammers, H.2    Pili, R.3
  • 64
    • 33751249589 scopus 로고    scopus 로고
    • Effects of histone deacetylase inhibitors on HIF-1
    • Liang, D.; Kong, X.; Sang, N. Effects of histone deacetylase inhibitors on HIF-1. Cell Cycle 2006, 5, 2430–2435
    • (2006) Cell Cycle , vol.5 , pp. 2430-2435
    • Liang, D.1    Kong, X.2    Sang, N.3
  • 65
    • 40949142209 scopus 로고    scopus 로고
    • The role of hypoxia-inducible factors in tumorigenesis
    • Rankin, E.B.; Giaccia, A.J. The role of hypoxia-inducible factors in tumorigenesis. Cell Death Differ. 2008, 15, 678–685
    • (2008) Cell Death Differ , vol.15 , pp. 678-685
    • Rankin, E.B.1    Giaccia, A.J.2
  • 66
    • 84904788576 scopus 로고    scopus 로고
    • The role of hypoxia inducible factor-1 in hepatocellular carcinoma
    • Luo, D.; Wang, Z.; Wu, J.; Jiang, C.; Wu, J. The role of hypoxia inducible factor-1 in hepatocellular carcinoma. BioMed Res. Int. 2014, doi:10.1155/2014/409272
    • (2014) Biomed Res. Int
    • Luo, D.1    Wang, Z.2    Wu, J.3    Jiang, C.4    Wu, J.5
  • 67
    • 34547124062 scopus 로고    scopus 로고
    • Hypoxia: A key regulator of angiogenesis in cancer
    • Liao, D.; Johnson, R.S. Hypoxia: A key regulator of angiogenesis in cancer. Cancer Metast. Rev. 2007, 26, 281–290
    • (2007) Cancer Metast. Rev , vol.26 , pp. 281-290
    • Liao, D.1    Johnson, R.S.2
  • 68
    • 77951215350 scopus 로고    scopus 로고
    • Lysyl oxidase expression is an independent marker of prognosis and a predictor of lymph node metastasis in oral and oropharyngeal squamous cell carcinoma (OSCC)
    • Albinger-Hegyi, A.; Stoeckli, S.J.; Schmid, S.; Storz, M.; Iotzova, G.; Probst-Hensch, N.M.; Rehrauer, H.; Tinguely, M.; Moch, H.; Hegyi, I. Lysyl oxidase expression is an independent marker of prognosis and a predictor of lymph node metastasis in oral and oropharyngeal squamous cell carcinoma (OSCC). Int. J. Cancer 2010, 126, 2653–2662
    • (2010) Int. J. Cancer , vol.126 , pp. 2653-2662
    • Albinger-Hegyi, A.1    Stoeckli, S.J.2    Schmid, S.3    Storz, M.4    Iotzova, G.5    Probst-Hensch, N.M.6    Rehrauer, H.7    Tinguely, M.8    Moch, H.9    Hegyi, I.10
  • 69
    • 70349307281 scopus 로고    scopus 로고
    • Validation of lysyl oxidase as a prognostic marker for metastasis and survival in head and neck squamous cell carcinoma: Radiation therapy oncology group trial 90-03
    • Le, Q.T.; Harris, J.; Magliocco, A.M.; Kong, C.S.; Diaz, R.; Shin, B.; Cao, H.; Trotti, A.; Erler, J.T.; Chung, C.H., et al. Validation of lysyl oxidase as a prognostic marker for metastasis and survival in head and neck squamous cell carcinoma: Radiation therapy oncology group trial 90-03. J. Clin. Oncol. 2009, 27, 4281–4286
    • (2009) J. Clin. Oncol , vol.27 , pp. 4281-4286
    • Le, Q.T.1    Harris, J.2    Magliocco, A.M.3    Kong, C.S.4    Diaz, R.5    Shin, B.6    Cao, H.7    Trotti, A.8    Erler, J.T.9    Chung, C.H.10
  • 70
    • 68949202238 scopus 로고    scopus 로고
    • Expression of lysyl oxidase is correlated with lymph node metastasis and poor prognosis in esophageal squamous cell carcinoma
    • Sakai, M.; Kato, H.; Sano, A.; Tanaka, N.; Inose, T.; Kimura, H.; Sohda, M.; Nakajima, M.; Kuwano, H. Expression of lysyl oxidase is correlated with lymph node metastasis and poor prognosis in esophageal squamous cell carcinoma. Ann. Surg. Oncol. 2009, 16, 2494–2501
    • (2009) Ann. Surg. Oncol , vol.16 , pp. 2494-2501
    • Sakai, M.1    Kato, H.2    Sano, A.3    Tanaka, N.4    Inose, T.5    Kimura, H.6    Sohda, M.7    Nakajima, M.8    Kuwano, H.9
  • 72
    • 40649114443 scopus 로고    scopus 로고
    • Hypoxia induces a novel signature of chromatin modifications and global repression of transcription
    • Johnson, A.B.; Denko, N.; Barton, M.C. Hypoxia induces a novel signature of chromatin modifications and global repression of transcription. Mutat. Res. 2008, 640, 174–179
    • (2008) Mutat. Res , vol.640 , pp. 174-179
    • Johnson, A.B.1    Denko, N.2    Barton, M.C.3
  • 74
    • 58249123443 scopus 로고    scopus 로고
    • Hypoxic silencing of tumor suppressor RUNX3 by histone modification in gastric cancer cells
    • Lee, S.H.; Kim, J.; Kim, W.H.; Lee, Y.M. Hypoxic silencing of tumor suppressor RUNX3 by histone modification in gastric cancer cells. Oncogene 2009, 28, 184–194
    • (2009) Oncogene , vol.28 , pp. 184-194
    • Lee, S.H.1    Kim, J.2    Kim, W.H.3    Lee, Y.M.4
  • 75
    • 79961131128 scopus 로고    scopus 로고
    • Hypoxia-induced epigenetic regulation and silencing of the BRCA1 promoter
    • Lu, Y.; Chu, A.; Turker, M.S.; Glazer, P.M. Hypoxia-induced epigenetic regulation and silencing of the BRCA1 promoter. Mol. Cell. Biol. 2011, 31, 3339–3350
    • (2011) Mol. Cell. Biol , vol.31 , pp. 3339-3350
    • Lu, Y.1    Chu, A.2    Turker, M.S.3    Glazer, P.M.4
  • 76
    • 84904792660 scopus 로고    scopus 로고
    • Silencing of the DNA mismatch repair gene MLH1 induced by hypoxic stress in a pathway dependent on the histone demethylase LSD1
    • Lu, Y.; Wajapeyee, N.; Turker, M.S.; Glazer, P.M. Silencing of the DNA mismatch repair gene MLH1 induced by hypoxic stress in a pathway dependent on the histone demethylase LSD1. Cell Rep. 2014, 8, 501–513
    • (2014) Cell Rep , vol.8 , pp. 501-513
    • Lu, Y.1    Wajapeyee, N.2    Turker, M.S.3    Glazer, P.M.4
  • 77
    • 3442888541 scopus 로고    scopus 로고
    • Silencing of the hypoxia-inducible cell death protein BNIP3 in pancreatic cancer
    • Okami, J.; Simeone, D.M.; Logsdon, C.D. Silencing of the hypoxia-inducible cell death protein BNIP3 in pancreatic cancer. Cancer Res. 2004, 64, 5338–5346
    • (2004) Cancer Res , vol.64 , pp. 5338-5346
    • Okami, J.1    Simeone, D.M.2    Logsdon, C.D.3
  • 79
    • 84958060718 scopus 로고    scopus 로고
    • H3K9me3 facilitates hypoxia-induced p53-dependent apoptosis through repression of APAK
    • Olcina, M.M.; Leszczynska, K.B.; Senra, J.M.; Isa, N.F.; Harada, H.; Hammond, E.M. H3K9me3 facilitates hypoxia-induced p53-dependent apoptosis through repression of APAK. Oncogene 2015, doi:10.1038/onc.2015.134
    • (2015) Oncogene
    • Olcina, M.M.1    Leszczynska, K.B.2    Senra, J.M.3    Isa, N.F.4    Harada, H.5    Hammond, E.M.6
  • 81
    • 84904249033 scopus 로고    scopus 로고
    • Hypoxic stress facilitates acute activation and chronic downregulation of fanconi anemia proteins
    • Scanlon, S.E.; Glazer, P.M. Hypoxic stress facilitates acute activation and chronic downregulation of fanconi anemia proteins. Mol. Cancer Res. 2014, 12, 1016–1028
    • (2014) Mol. Cancer Res , vol.12 , pp. 1016-1028
    • Scanlon, S.E.1    Glazer, P.M.2
  • 82
    • 79951831757 scopus 로고    scopus 로고
    • Expression of hypoxic marker ca ix is regulated by site-specific DNA methylation and is associated with the histology of gastric cancer
    • Nakamura, J.; Kitajima, Y.; Kai, K.; Hashiguchi, K.; Hiraki, M.; Noshiro, H.; Miyazaki, K. Expression of hypoxic marker ca ix is regulated by site-specific DNA methylation and is associated with the histology of gastric cancer. Am. J. Pathol. 2011, 178, 515–524
    • (2011) Am. J. Pathol , vol.178 , pp. 515-524
    • Nakamura, J.1    Kitajima, Y.2    Kai, K.3    Hashiguchi, K.4    Hiraki, M.5    Noshiro, H.6    Miyazaki, K.7
  • 83
    • 77956628814 scopus 로고    scopus 로고
    • DNA methylation analysis of the HIF-1[1] Prolyl hydroxylase domain genes PHD1, PHD2, PHD3 and the factor inhibiting HIF gene FIH in invasive breast carcinomas
    • Huang, K.T.; Mikeska, T.; Dobrovic, A.; Fox, S.B. DNA methylation analysis of the HIF-1[1] Prolyl hydroxylase domain genes PHD1, PHD2, PHD3 and the factor inhibiting HIF gene FIH in invasive breast carcinomas. Histopathology 2010, 57, 451–460
    • (2010) Histopathology , vol.57 , pp. 451-460
    • Huang, K.T.1    Mikeska, T.2    Dobrovic, A.3    Fox, S.B.4
  • 84
    • 84887346735 scopus 로고    scopus 로고
    • Expression and DNA methylation levels of Prolyl hydroxylases PHD1, PHD2, PHD3 and asparaginyl hydroxylase FIH in colorectal cancer
    • Rawluszko, A.A.; Bujnicka, K.E.; Horbacka, K.; Krokowicz, P.; Jagodzinski, P.P. Expression and DNA methylation levels of Prolyl hydroxylases PHD1, PHD2, PHD3 and asparaginyl hydroxylase FIH in colorectal cancer. BMC Cancer 2013, doi:10.1186/1471-2407-13-526
    • (2013) BMC Cancer
    • Rawluszko, A.A.1    Bujnicka, K.E.2    Horbacka, K.3    Krokowicz, P.4    Jagodzinski, P.P.5
  • 85
    • 79958710992 scopus 로고    scopus 로고
    • Hypoxia induces genomic DNA demethylation through the activation of HIF-1[1] and transcriptional upregulation of MAT2A in hepatoma cells. Mol
    • Liu, Q.; Liu, L.; Zhao, Y.; Zhang, J.; Wang, D.; Chen, J.; He, Y.; Wu, J.; Zhang, Z.; Liu, Z. Hypoxia induces genomic DNA demethylation through the activation of HIF-1[1] and transcriptional upregulation of MAT2A in hepatoma cells. Mol. Cancer Ther. 2011, 10, 1113–1123
    • (2011) Cancer Ther , vol.10 , pp. 1113-1123
    • Liu, Q.1    Liu, L.2    Zhao, Y.3    Zhang, J.4    Wang, D.5    Chen, J.6    He, Y.7    Wu, J.8    Zhang, Z.9    Liu, Z.10
  • 86
    • 77957336892 scopus 로고    scopus 로고
    • Ischemia dysregulates DNA methyltransferases and p16INK4a methylation in human colorectal cancer cells
    • Skowronski, K.; Dubey, S.; Rodenhiser, D.; Coomber, B. Ischemia dysregulates DNA methyltransferases and p16INK4a methylation in human colorectal cancer cells. Epigenetics 2010, 5, 547–556
    • (2010) Epigenetics , vol.5 , pp. 547-556
    • Skowronski, K.1    Dubey, S.2    Rodenhiser, D.3    Coomber, B.4
  • 89
    • 84942801781 scopus 로고    scopus 로고
    • Global DNA hypomethylation and hypoxia-induced expression of the ten eleven translocation (TET) family, TET1, in scleroderma fibroblasts
    • Hattori, M.; Yokoyama, Y.; Hattori, T.; Motegi, S.I.; Amano, H.; Hatada, I.; Ishikawa, O. Global DNA hypomethylation and hypoxia-induced expression of the ten eleven translocation (TET) family, TET1, in scleroderma fibroblasts. Exp. Dermatol. 2015, doi:10.1111/exd.12767
    • (2015) Exp. Dermatol
    • Hattori, M.1    Yokoyama, Y.2    Hattori, T.3    Motegi, S.I.4    Amano, H.5    Hatada, I.6    Ishikawa, O.7
  • 90
    • 33749494456 scopus 로고    scopus 로고
    • Hypoxic stress induces dimethylated histone H3 lysine 9 through histone methyltransferase G9a in mammalian cells
    • Chen, H.; Yan, Y.; Davidson, T.L.; Shinkai, Y.; Costa, M. Hypoxic stress induces dimethylated histone H3 lysine 9 through histone methyltransferase G9a in mammalian cells. Cancer Res. 2006, 66, 9009–9016
    • (2006) Cancer Res , vol.66 , pp. 9009-9016
    • Chen, H.1    Yan, Y.2    Davidson, T.L.3    Shinkai, Y.4    Costa, M.5
  • 91
    • 77952795537 scopus 로고    scopus 로고
    • Hypoxia induces trimethylated H3 lysine 4 by inhibition of JARID1A demethylase
    • Zhou, X.; Sun, H.; Chen, H.; Zavadil, J.; Kluz, T.; Arita, A.; Costa, M. Hypoxia induces trimethylated H3 lysine 4 by inhibition of JARID1A demethylase. Cancer Res. 2010, 70, 4214–4221
    • (2010) Cancer Res , vol.70 , pp. 4214-4221
    • Zhou, X.1    Sun, H.2    Chen, H.3    Zavadil, J.4    Kluz, T.5    Arita, A.6    Costa, M.7
  • 92
    • 78651086487 scopus 로고    scopus 로고
    • Hypoxia causes epigenetic gene regulation in macrophages by attenuating Jumonji histone demethylase activity
    • Tausendschon, M.; Dehne, N.; Brune, B. Hypoxia causes epigenetic gene regulation in macrophages by attenuating Jumonji histone demethylase activity. Cytokine 2011, 53, 256–262
    • (2011) Cytokine , vol.53 , pp. 256-262
    • Tausendschon, M.1    Dehne, N.2    Brune, B.3
  • 93
    • 84870375316 scopus 로고    scopus 로고
    • Histone lysine methylation dynamics: Establishment, regulation, and biological impact
    • Black, J.C.; van Rechem, C.; Whetstine, J.R. Histone lysine methylation dynamics: Establishment, regulation, and biological impact. Mol. Cell 2012, 48, 491–507
    • (2012) Mol. Cell , vol.48 , pp. 491-507
    • Black, J.C.1    Van Rechem, C.2    Whetstine, J.R.3
  • 94
    • 79956107316 scopus 로고    scopus 로고
    • Epigenetic regulation of surfactant protein a gene (Sp-a) expression in fetal lung reveals a critical role for SUV39H methyltransferases during development and hypoxia
    • Benlhabib, H.; Mendelson, C.R. Epigenetic regulation of surfactant protein a gene (sp-a) expression in fetal lung reveals a critical role for SUV39H methyltransferases during development and hypoxia. Mol. Cell. Biol. 2011, 31, 1949–1958
    • (2011) Mol. Cell. Biol , vol.31 , pp. 1949-1958
    • Benlhabib, H.1    Mendelson, C.R.2
  • 98
    • 84868593544 scopus 로고    scopus 로고
    • Kinetic analysis of iron-dependent histone demethylases: α-ketoglutarate substrate inhibition and potential relevance to the regulation of histone demethylation in cancer cells
    • Cascella, B.; Mirica, L.M. Kinetic analysis of iron-dependent histone demethylases: α-ketoglutarate substrate inhibition and potential relevance to the regulation of histone demethylation in cancer cells. Biochemistry 2012, 51, 8699–8701
    • (2012) Biochemistry , vol.51 , pp. 8699-8701
    • Cascella, B.1    Mirica, L.M.2
  • 99
    • 61349088682 scopus 로고    scopus 로고
    • The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF
    • Beyer, S.; Kristensen, M.M.; Jensen, K.S.; Johansen, J.V.; Staller, P. The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF. J. Biol. Chem. 2008, 283, 36542–36552
    • (2008) J. Biol. Chem , vol.283 , pp. 36542-36552
    • Beyer, S.1    Kristensen, M.M.2    Jensen, K.S.3    Johansen, J.V.4    Staller, P.5
  • 101
    • 84870608916 scopus 로고    scopus 로고
    • Histone demethylase JMJD2C is a coactivator for hypoxia-inducible factor 1 that is required for breast cancer progression
    • Luo, W.; Chang, R.; Zhong, J.; Pandey, A.; Semenza, G.L. Histone demethylase JMJD2C is a coactivator for hypoxia-inducible factor 1 that is required for breast cancer progression. Proc. Natl. Acad. Sci. USA 2012, 109, E3367–E3376
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109
    • Luo, W.1    Chang, R.2    Zhong, J.3    Pandey, A.4    Semenza, G.L.5
  • 102
    • 73549088729 scopus 로고    scopus 로고
    • Regulation of the histone demethylase jmjd1a by hypoxia-inducible factor 1 [1] enhances hypoxic gene expression and tumor growth
    • Krieg, A.J.; Rankin, E.B.; Chan, D.; Razorenova, O.; Fernandez, S.; Giaccia, A.J. Regulation of the histone demethylase jmjd1a by hypoxia-inducible factor 1 [1] enhances hypoxic gene expression and tumor growth. Mol. Cell. Biol. 2010, 30, 344–353
    • (2010) Mol. Cell. Biol , vol.30 , pp. 344-353
    • Krieg, A.J.1    Rankin, E.B.2    Chan, D.3    Razorenova, O.4    Fernandez, S.5    Giaccia, A.J.6
  • 103
    • 84865536482 scopus 로고    scopus 로고
    • HIF-1[1]-induced histone demethylase JMJD2B contributes to the malignant phenotype of colorectal cancer cells via an epigenetic mechanism
    • Fu, L.; Chen, L.; Yang, J.; Ye, T.; Chen, Y.; Fang, J. HIF-1[1]-induced histone demethylase JMJD2B contributes to the malignant phenotype of colorectal cancer cells via an epigenetic mechanism. Carcinogenesis 2012, 33, 1664–1673
    • (2012) Carcinogenesis , vol.33 , pp. 1664-1673
    • Fu, L.1    Chen, L.2    Yang, J.3    Ye, T.4    Chen, Y.5    Fang, J.6
  • 105
    • 0030025773 scopus 로고    scopus 로고
    • Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours
    • Graeber, T.G.; Osmanian, C.; Jacks, T.; Housman, D.E.; Koch, C.J.; Lowe, S.W.; Giaccia, A.J. Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours. Nature 1996, 379, 88–91
    • (1996) Nature , vol.379 , pp. 88-91
    • Graeber, T.G.1    Osmanian, C.2    Jacks, T.3    Housman, D.E.4    Koch, C.J.5    Lowe, S.W.6    Giaccia, A.J.7
  • 108
    • 79957440998 scopus 로고    scopus 로고
    • The hypoxia-associated factor switches cells from HIF-1- to HIF-2[1][1]-dependent signaling promoting stem cell characteristics, aggressive tumor growth and invasion
    • Koh, M.Y.; Lemos, R., Jr.; Liu, X.; Powis, G. The hypoxia-associated factor switches cells from HIF-1[1]- to HIF-2[1]-dependent signaling promoting stem cell characteristics, aggressive tumor growth and invasion. Cancer Res. 2011, 71, 4015–4027
    • (2011) Cancer Res , vol.71 , pp. 4015-4027
    • Koh, M.Y.1    Lemos, R.2    Liu, X.3    Powis, G.4
  • 109
    • 80055077899 scopus 로고    scopus 로고
    • HDAC4 protein regulates HIF1[1] protein lysine acetylation and cancer cell response to hypoxia
    • Geng, H.; Harvey, C.T.; Pittsenbarger, J.; Liu, Q.; Beer, T.M.; Xue, C.; Qian, D.Z. HDAC4 protein regulates HIF1[1] protein lysine acetylation and cancer cell response to hypoxia. J. Biol. Chem. 2011, 286, 38095–38102
    • (2011) J. Biol. Chem , vol.286 , pp. 38095-38102
    • Geng, H.1    Harvey, C.T.2    Pittsenbarger, J.3    Liu, Q.4    Beer, T.M.5    Xue, C.6    Qian, D.Z.7
  • 110
    • 0037225763 scopus 로고    scopus 로고
    • Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1[1] activity. Biochem. Biophys. Res
    • Mie Lee, Y.; Kim, S.H.; Kim, H.S.; Jin Son, M.; Nakajima, H.; Jeong Kwon, H.; Kim, K.W. Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1[1] activity. Biochem. Biophys. Res. Commun. 2003, 300, 241–246
    • (2003) Commun , vol.300 , pp. 241-246
    • Mie Lee, Y.1    Kim, S.H.2    Kim, H.S.3    Jin Son, M.4    Nakajima, H.5    Jeong Kwon, H.6    Kim, K.W.7
  • 112
    • 84858685501 scopus 로고    scopus 로고
    • Targeted cancer therapy: Giving histone deacetylase inhibitors all they need to succeed
    • Gryder, B.E.; Sodji, Q.H.; Oyelere, A.K. Targeted cancer therapy: Giving histone deacetylase inhibitors all they need to succeed. Future Med. Chem. 2012, 4, 505–524
    • (2012) Future Med. Chem , vol.4 , pp. 505-524
    • Gryder, B.E.1    Sodji, Q.H.2    Oyelere, A.K.3
  • 113
    • 84863710071 scopus 로고    scopus 로고
    • New lysine methyltransferase drug targets in cancer. Nat
    • Wagner, T.; Jung, M. New lysine methyltransferase drug targets in cancer. Nat. Biotechnol. 2012, 30, 622–623
    • (2012) Biotechnol , vol.30 , pp. 622-623
    • Wagner, T.1    Jung, M.2
  • 114
    • 75749102137 scopus 로고    scopus 로고
    • Reexpression of epigenetically silenced aml tumor suppressor genes by SUV39H1 inhibition
    • Lakshmikuttyamma, A.; Scott, S.A.; de Coteau, J.F.; Geyer, C.R. Reexpression of epigenetically silenced aml tumor suppressor genes by SUV39H1 inhibition. Oncogene 2010, 29, 576–588
    • (2010) Oncogene , vol.29 , pp. 576-588
    • Lakshmikuttyamma, A.1    Scott, S.A.2    De Coteau, J.F.3    Geyer, C.R.4
  • 115
    • 84874796156 scopus 로고    scopus 로고
    • Improved therapeutic effect against leukemia by a combination of the histone methyltransferase inhibitor chaetocin and the histone deacetylase inhibitor trichostatin A
    • Tran, H.T.; Kim, H.N.; Lee, I.K.; Nguyen-Pham, T.N.; Ahn, J.S.; Kim, Y.K.; Lee, J.J.; Park, K.S.; Kook, H.; Kim, H.J. Improved therapeutic effect against leukemia by a combination of the histone methyltransferase inhibitor chaetocin and the histone deacetylase inhibitor trichostatin A. J. Korean Med. Sci. 2013, 28, 237–246
    • (2013) J. Korean Med. Sci , vol.28 , pp. 237-246
    • Tran, H.T.1    Kim, H.N.2    Lee, I.K.3    Nguyen-Pham, T.N.4    Ahn, J.S.5    Kim, Y.K.6    Lee, J.J.7    Park, K.S.8    Kook, H.9    Kim, H.J.10
  • 116
  • 117
    • 73149118652 scopus 로고    scopus 로고
    • Novel oligoamine analogues inhibit lysine-specific demethylase 1 and induce reexpression of epigenetically silenced genes
    • Huang, Y.; Stewart, T.M.; Wu, Y.; Baylin, S.B.; Marton, L.J.; Perkins, B.; Jones, R.J.; Woster, P.M.; Casero, R.A.,. Novel oligoamine analogues inhibit lysine-specific demethylase 1 and induce reexpression of epigenetically silenced genes. Clin. Cancer Res. 2009, 15, 7217–7228
    • (2009) Clin. Cancer Res , vol.15 , pp. 7217-7228
    • Huang, Y.1    Stewart, T.M.2    Wu, Y.3    Baylin, S.B.4    Marton, L.J.5    Perkins, B.6    Jones, R.J.7    Woster, P.M.8    Casero, R.A.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.