메뉴 건너뛰기




Volumn 12, Issue 4, 2012, Pages 439-452

An epigenetic approach to pancreatic cancer treatment: The prospective role of histone deacetylase inhibitors

Author keywords

Cancer therapy; Epigenetic; Histone deacetylase; Histone deacetylase inhibitor; Molecular targeted therapy; Pancreatic ductal adenocarcinoma

Indexed keywords

BELINOSTAT; BORTEZOMIB; CAPECITABINE; DEPSIPEPTIDE; FLUOROPYRIMIDINE; FLUOROURACIL; GEMCITABINE; HISTONE DEACETYLASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE INHIBITOR; LAPATINIB; MOCETINOSTAT; PANOBINOSTAT; PEGINTERFERON ALPHA2B; PROTEASOME INHIBITOR; RESMINOSTAT; ROMIDEPSIN; SALINOSPORAMIDE A; TACEDINALINE; VALPROIC ACID; VORINOSTAT;

EID: 84860283904     PISSN: 15680096     EISSN: 18735576     Source Type: Journal    
DOI: 10.2174/156800912800190884     Document Type: Article
Times cited : (34)

References (163)
  • 3
    • 79953112266 scopus 로고    scopus 로고
    • A meta-analysis of gemcitabine containing chemotherapy for locally advanced and metastatic pancreatic adenocarcinoma
    • Hu, J.; Zhao, G.; Wang, H. X.; Tang, L.; Xu, Y. C.; Ma, Y.; Zhang, F. C. A meta-analysis of gemcitabine containing chemotherapy for locally advanced and metastatic pancreatic adenocarcinoma. J. Hematol. Oncol. 2011, 4, 11.
    • (2011) J. Hematol. Oncol , vol.4 , pp. 11
    • Hu, J.1    Zhao, G.2    Wang, H.X.3    Tang, L.4    Xu, Y.C.5    Ma, Y.6    Zhang, F.C.7
  • 8
    • 80053592994 scopus 로고    scopus 로고
    • FOLFIRINOX: A Small Step or a Great Leap Forward?
    • Ko, A. H. FOLFIRINOX: A Small Step or a Great Leap Forward? J. Clin. Oncol. 2011.
    • (2011) J. Clin. Oncol
    • Ko, A.H.1
  • 11
    • 84860298363 scopus 로고    scopus 로고
    • Therapeutic targeting of apoptotic pathways: Novel aspects in pancreatic cancer
    • Neesse, A.; Gress, T. M.; Michl, P. Therapeutic targeting of apoptotic pathways: novel aspects in pancreatic cancer. Curr. Pharm. Biotechnol. 2011.
    • (2011) Curr. Pharm. Biotechnol
    • Neesse, A.1    Gress, T.M.2    Michl, P.3
  • 13
    • 77957150824 scopus 로고    scopus 로고
    • KRAS, Hedgehog, Wnt and the twisted developmental biology of pancreatic ductal adenocarcinoma
    • Morris, J. P. t.; Wang, S. C.; Hebrok, M. KRAS, Hedgehog, Wnt and the twisted developmental biology of pancreatic ductal adenocarcinoma. Nat. Rev. Cancer 2010, 10 (10), 683-695.
    • (2010) Nat. Rev. Cancer , vol.10 , Issue.10 , pp. 683-695
    • Morris, J.P.T.1    Wang, S.C.2    Hebrok, M.3
  • 14
    • 80054826238 scopus 로고    scopus 로고
    • MicroRNA functional network in pancreatic cancer: From biology to biomarkers of disease
    • Wang, J.; Sen, S. MicroRNA functional network in pancreatic cancer: from biology to biomarkers of disease. J. Biosci. 2011, 36 (3), 481-491.
    • (2011) J. Biosci , vol.36 , Issue.3 , pp. 481-491
    • Wang, J.1    Sen, S.2
  • 16
    • 67149130222 scopus 로고    scopus 로고
    • Epigenetics and epigenetic alterations in pancreatic cancer
    • Omura, N.; Goggins, M. Epigenetics and epigenetic alterations in pancreatic cancer. Int. J. Clin. Exp. Pathol. 2009, 2 (4), 310-326.
    • (2009) Int. J. Clin Exp. Pathol , vol.2 , Issue.4 , pp. 310-326
    • Omura, N.1    Goggins, M.2
  • 17
    • 34249337761 scopus 로고    scopus 로고
    • Perceptions of epigenetics
    • Bird, A. Perceptions of epigenetics. Nature 2007, 447 (7143), 396-398.
    • (2007) Nature , vol.447 , Issue.7143 , pp. 396-398
    • Bird, A.1
  • 18
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • Jones, P. A.; Baylin, S. B. The epigenomics of cancer. Cell 2007, 128 (4), 683-692.
    • (2007) Cell , vol.128 , Issue.4 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 19
    • 34547897023 scopus 로고    scopus 로고
    • Histone deacetylases and cancer
    • Glozak, M. A.; Seto, E. Histone deacetylases and cancer. Oncogene 2007, 26 (37), 5420-5432.
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5420-5432
    • Glozak, M.A.1    Seto, E.2
  • 20
    • 34247109089 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors for epigenetic therapy of cancer
    • Monneret, C. Histone deacetylase inhibitors for epigenetic therapy of cancer. Anticancer Drugs 2007, 18 (4), 363-370.
    • (2007) Anticancer Drugs , vol.18 , Issue.4 , pp. 363-370
    • Monneret, C.1
  • 21
    • 0842324785 scopus 로고    scopus 로고
    • The nucleosome: From genomic organization to genomic regulation
    • Khorasanizadeh, S. The nucleosome: from genomic organization to genomic regulation. Cell 2004, 116 (2), 259-272.
    • (2004) Cell , vol.116 , Issue.2 , pp. 259-272
    • Khorasanizadeh, S.1
  • 22
    • 0037154963 scopus 로고    scopus 로고
    • Cooperation between complexes that regulate chromatin structure and transcription
    • Narlikar, G. J.; Fan, H. Y.; Kingston, R. E. Cooperation between complexes that regulate chromatin structure and transcription. Cell 2002, 108 (4), 475-487.
    • (2002) Cell , vol.108 , Issue.4 , pp. 475-487
    • Narlikar, G.J.1    Fan, H.Y.2    Kingston, R.E.3
  • 24
    • 79951713773 scopus 로고    scopus 로고
    • Protected from the inside: Endogenous histone deacetylase inhibitors and the road to cancer
    • di Marcotullio, L.; Canettieri, G.; Infante, P.; Greco, A.; Gulino, A. Protected from the inside: endogenous histone deacetylase inhibitors and the road to cancer. Biochim. Biophys. Acta 2011, 1815 (2), 241-252.
    • (2011) Biochim. Biophys. Acta , vol.1815 , Issue.2 , pp. 241-252
    • Di Marcotullio, L.1    Canettieri, G.2    Infante, P.3    Greco, A.4    Gulino, A.5
  • 25
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • Glozak, M. A.; Sengupta, N.; Zhang, X.; Seto, E. Acetylation and deacetylation of non-histone proteins. Gene 2005, 363, 15-23.
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 26
    • 79952204427 scopus 로고    scopus 로고
    • Beyond histone and deacetylase: An overview of cytoplasmic histone deacetylases and their nonhistone substrates
    • Yao, Y. L.; Yang, W. M. Beyond histone and deacetylase: an overview of cytoplasmic histone deacetylases and their nonhistone substrates. J. Biomed. Biotechnol. 2011, 2011, 146493.
    • (2011) J. Biomed. Biotechnol , vol.2011 , pp. 146493
    • Yao, Y.L.1    Yang, W.M.2
  • 27
    • 0037112901 scopus 로고    scopus 로고
    • MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation
    • Ito, A.; Kawaguchi, Y.; Lai, C. H.; Kovacs, J. J.; Higashimoto, Y.; Appella, E.; Yao, T. P. MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation. EMBO J. 2002, 21 (22), 6236-6245.
    • (2002) EMBO J , vol.21 , Issue.22 , pp. 6236-6245
    • Ito, A.1    Kawaguchi, Y.2    Lai, C.H.3    Kovacs, J.J.4    Higashimoto, Y.5    Appella, E.6    Yao, T.P.7
  • 28
    • 3142720638 scopus 로고    scopus 로고
    • Transforming growth factor-beta stimulates p300-dependent RUNX3 acetylation, which inhibits ubiquitination-mediated degradation
    • Jin, Y. H.; Jeon, E. J.; Li, Q. L.; Lee, Y. H.; Choi, J. K.; Kim, W. J.; Lee, K. Y.; Bae, S. C. Transforming growth factor-beta stimulates p300-dependent RUNX3 acetylation, which inhibits ubiquitination-mediated degradation. J. Biol. Chem. 2004, 279 (28), 29409-29417.
    • (2004) J. Biol. Chem , vol.279 , Issue.28 , pp. 29409-29417
    • Jin, Y.H.1    Jeon, E.J.2    Li, Q.L.3    Lee, Y.H.4    Choi, J.K.5    Kim, W.J.6    Lee, K.Y.7    Bae, S.C.8
  • 29
    • 79953157671 scopus 로고    scopus 로고
    • Histone deacetylases 9 and 10 are required for homologous recombination
    • Kotian, S.; Liyanarachchi, S.; Zelent, A.; Parvin, J. D. Histone deacetylases 9 and 10 are required for homologous recombination. J. Biol. Chem. 2011, 286 (10), 7722-7726.
    • (2011) J. Biol. Chem , vol.286 , Issue.10 , pp. 7722-7726
    • Kotian, S.1    Liyanarachchi, S.2    Zelent, A.3    Parvin, J.D.4
  • 32
    • 33749490850 scopus 로고    scopus 로고
    • The corepressor silencing mediator for retinoid and thyroid hormone receptor facilitates cellular recovery from DNA double-strand breaks
    • Yu, J.; Palmer, C.; Alenghat, T.; Li, Y.; Kao, G.; Lazar, M. A. The corepressor silencing mediator for retinoid and thyroid hormone receptor facilitates cellular recovery from DNA double-strand breaks. Cancer Res. 2006, 66 (18), 9316-9322.
    • (2006) Cancer Res , vol.66 , Issue.18 , pp. 9316-9322
    • Yu, J.1    Palmer, C.2    Alenghat, T.3    Li, Y.4    Kao, G.5    Lazar, M.A.6
  • 34
  • 35
    • 73949128107 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy
    • Lane, A. A.; Chabner, B. A. Histone deacetylase inhibitors in cancer therapy. J. Clin. Oncol. 2009, 27 (32), 5459-5468.
    • (2009) J. Clin. Oncol , vol.27 , Issue.32 , pp. 5459-5468
    • Lane, A.A.1    Chabner, B.A.2
  • 37
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander, G.; Guarente, L. The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 2004, 73, 417-435.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 38
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: Implications for disease and therapy
    • Haberland, M.; Montgomery, R. L.; Olson, E. N. The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat. Rev. Genet. 2009, 10 (1), 32-42.
    • (2009) Nat. Rev. Genet , vol.10 , Issue.1 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 40
    • 41549156540 scopus 로고    scopus 로고
    • Deletion of Histone Deacetylase 3 Reveals Critical Roles In S Phase Progression and DNA Damage Control
    • Bhaskara, S.; Chyla, B. J.; Amann, J. M.; Knutson, S. K.; Cortez, D.; Sun, Z. W.; Hiebert, S. W. Deletion of histone deacetylase 3 reveals critical roles in S phase progression and DNA damage control. Mol. Cell 2008, 30 (1), 61-72.
    • (2008) Mol. Cell , vol.30 , Issue.1 , pp. 61-72
    • Bhaskara, S.1    Chyla, B.J.2    Amann, J.M.3    Knutson, S.K.4    Cortez, D.5    Sun, Z.W.6    Hiebert, S.W.7
  • 41
    • 0037406061 scopus 로고    scopus 로고
    • Class II histone deacetylases: Versatile regulators
    • Verdin, E.; Dequiedt, F.; Kasler, H. G. Class II histone deacetylases: versatile regulators. Trends Genet. 2003, 19 (5), 286-293.
    • (2003) Trends Genet , vol.19 , Issue.5 , pp. 286-293
    • Verdin, E.1    Dequiedt, F.2    Kasler, H.G.3
  • 42
    • 0035862199 scopus 로고    scopus 로고
    • The human histone deacetylase family
    • Gray, S. G.; Ekstrom, T. J. The human histone deacetylase family. Exp. Cell Res. 2001, 262 (2), 75-83.
    • (2001) Exp. Cell Res , vol.262 , Issue.2 , pp. 75-83
    • Gray, S.G.1    Ekstrom, T.J.2
  • 43
    • 77952547233 scopus 로고    scopus 로고
    • Ten years of NAD-dependent SIR2 family deacetylases: Implications for metabolic diseases
    • Imai, S.; Guarente, L. Ten years of NAD-dependent SIR2 family deacetylases: implications for metabolic diseases. Trends Pharmacol. Sci. 2010, 31 (5), 212-220.
    • (2010) Trends Pharmacol. Sci , vol.31 , Issue.5 , pp. 212-220
    • Imai, S.1    Guarente, L.2
  • 44
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye, R. A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 2000, 273 (2), 793-798.
    • (2000) Biochem. Biophys. Res. Commun , vol.273 , Issue.2 , pp. 793-798
    • Frye, R.A.1
  • 46
    • 77949887506 scopus 로고    scopus 로고
    • Mammalian sirtuins: Biological insights and disease relevance
    • Haigis, M. C.; Sinclair, D. A. Mammalian sirtuins: biological insights and disease relevance. Annu. Rev. Pathol. 2010, 5, 253-295.
    • (2010) Annu. Rev. Pathol , vol.5 , pp. 253-295
    • Haigis, M.C.1    Sinclair, D.A.2
  • 47
    • 67349160499 scopus 로고    scopus 로고
    • HDAC expression and clinical prognosis in human malignancies
    • Weichert, W. HDAC expression and clinical prognosis in human malignancies. Cancer Lett. 2009, 280 (2), 168-176.
    • (2009) Cancer Lett , vol.280 , Issue.2 , pp. 168-176
    • Weichert, W.1
  • 48
    • 43049119236 scopus 로고    scopus 로고
    • The use of diversity profiling to characterize chemical modulators of the histone deacetylases
    • Blackwell, L.; Norris, J.; Suto, C. M.; Janzen, W. P. The use of diversity profiling to characterize chemical modulators of the histone deacetylases. Life Sci. 2008, 82 (21/22), 1050-1058.
    • (2008) Life Sci , vol.82 , Issue.21-22 , pp. 1050-1058
    • Blackwell, L.1    Norris, J.2    Suto, C.M.3    Janzen, W.P.4
  • 49
    • 79251541733 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in the treatment of hematological malignancies and solid tumors
    • Federico, M.; Bagella, L. Histone deacetylase inhibitors in the treatment of hematological malignancies and solid tumors. J. Biomed. Biotechnol. 2011, 2011, 475641.
    • (2011) J. Biomed. Biotechnol , vol.2011 , pp. 475641
    • Federico, M.1    Bagella, L.2
  • 50
    • 78650723028 scopus 로고    scopus 로고
    • Rationale for possible targeting of histone deacetylase signaling in cancer diseases with a special reference to pancreatic cancer
    • Ouaissi, M.; Giger, U.; Sielezneff, I.; Pirro, N.; Sastre, B.; Ouaissi, A. Rationale for possible targeting of histone deacetylase signaling in cancer diseases with a special reference to pancreatic cancer. J. Biomed. Biotechnol. 2011, 2011, 315939.
    • (2011) J. Biomed. Biotechnol , vol.2011 , pp. 315939
    • Ouaissi, M.1    Giger, U.2    Sielezneff, I.3    Pirro, N.4    Sastre, B.5    Ouaissi, A.6
  • 51
    • 34547122494 scopus 로고    scopus 로고
    • HDAC inhibitors: Clinical update and mechanismbased potential
    • Glaser, K. B. HDAC inhibitors: clinical update and mechanismbased potential. Biochem. Pharmacol. 2007, 74 (5), 659-671.
    • (2007) Biochem. Pharmacol , vol.74 , Issue.5 , pp. 659-671
    • Glaser, K.B.1
  • 52
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden, J. E.; Peart, M. J.; Johnstone, R. W. Anticancer activities of histone deacetylase inhibitors. Nat. Rev. Drug Discov. 2006, 5 (9), 769-784.
    • (2006) Nat. Rev. Drug Discov , vol.5 , Issue.9 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 53
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon, V. M.; Sandhoff, T. W.; Rifkind, R. A.; Marks, P. A. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc. Natl. Acad. Sci. U. S. A. 2000, 97 (18), 10014-10019.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , Issue.18 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 55
    • 80054735825 scopus 로고    scopus 로고
    • Evaluation of histone deacetylase inhibitors as therapeutics for neurodegenerative diseases
    • Soragni, E.; Xu, C.; Cooper, A.; Plasterer, H. L.; Rusche, J. R.; Gottesfeld, J. M. Evaluation of histone deacetylase inhibitors as therapeutics for neurodegenerative diseases. Methods Mol. Biol. 2011, 793, 495-508.
    • (2011) Methods Mol. Biol , vol.793 , pp. 495-508
    • Soragni, E.1    Xu, C.2    Cooper, A.3    Plasterer, H.L.4    Rusche, J.R.5    Gottesfeld, J.M.6
  • 57
    • 0020025385 scopus 로고
    • Effects of sodium butyrate, a new pharmacological agent, on cells in culture
    • Kruh, J. Effects of sodium butyrate, a new pharmacological agent, on cells in culture. Mol. Cell Biochem. 1982, 42 (2), 65-82.
    • (1982) Mol. Cell Biochem , vol.42 , Issue.2 , pp. 65-82
    • Kruh, J.1
  • 58
    • 0017767153 scopus 로고
    • N-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells
    • Riggs, M. G.; Whittaker, R. G.; Neumann, J. R.; Ingram, V. M. n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells. Nature 1977, 268 (5619), 462-464.
    • (1977) Nature , vol.268 , Issue.5619 , pp. 462-464
    • Riggs, M.G.1    Whittaker, R.G.2    Neumann, J.R.3    Ingram, V.M.4
  • 60
    • 43049104161 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of histone deacetylase (HDAC) inhibitors with triazole-linked cap group
    • Chen, P. C.; Patil, V.; Guerrant, W.; Green, P.; Oyelere, A. K. Synthesis and structure-activity relationship of histone deacetylase (HDAC) inhibitors with triazole-linked cap group. Bioorg. Med. Chem. 2008, 16 (9), 4839-4853.
    • (2008) Bioorg. Med. Chem , vol.16 , Issue.9 , pp. 4839-4853
    • Chen, P.C.1    Patil, V.2    Guerrant, W.3    Green, P.4    Oyelere, A.K.5
  • 61
    • 0242522928 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors
    • Miller, T. A.; Witter, D. J.; Belvedere, S. Histone deacetylase inhibitors. J. Med. Chem. 2003, 46 (24), 5097-5116.
    • (2003) J. Med. Chem , vol.46 , Issue.24 , pp. 5097-5116
    • Miller, T.A.1    Witter, D.J.2    Belvedere, S.3
  • 62
    • 33846122993 scopus 로고    scopus 로고
    • Dimethyl sulfoxide to vorinostat: Development of this histone deacetylase inhibitor as an anticancer drug
    • Marks, P. A.; Breslow, R. Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug. Nat. Biotechnol. 2007, 25 (1), 84-90.
    • (2007) Nat. Biotechnol , vol.25 , Issue.1 , pp. 84-90
    • Marks, P.A.1    Breslow, R.2
  • 63
    • 77649171884 scopus 로고    scopus 로고
    • Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents
    • Tan, J.; Cang, S.; Ma, Y.; Petrillo, R. L.; Liu, D. Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents. J. Hematol. Oncol. 2010, 3, 5.
    • (2010) J. Hematol. Oncol , vol.3 , pp. 5
    • Tan, J.1    Cang, S.2    Ma, Y.3    Petrillo, R.L.4    Liu, D.5
  • 64
    • 79957839068 scopus 로고    scopus 로고
    • Interpreting clinical assays for histone deacetylase inhibitors
    • Martinet, N.; Bertrand, P. Interpreting clinical assays for histone deacetylase inhibitors. Cancer Manag. Res. 2011, 3, 117-141.
    • (2011) Cancer Manag. Res , vol.3 , pp. 117-141
    • Martinet, N.1    Bertrand, P.2
  • 65
    • 67349227787 scopus 로고    scopus 로고
    • Isoform-specific histone deacetylase inhibitors: The next step?
    • Balasubramanian, S.; Verner, E.; Buggy, J. J. Isoform-specific histone deacetylase inhibitors: the next step? Cancer Lett. 2009, 280 (2), 211-221.
    • (2009) Cancer Lett , vol.280 , Issue.2 , pp. 211-221
    • Balasubramanian, S.1    Verner, E.2    Buggy, J.J.3
  • 66
    • 0033604457 scopus 로고    scopus 로고
    • Induction of apoptosis in U937 human leukemia cells by suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-XL, c-Jun, and p21CIP1, but independent of p53
    • Vrana, J. A.; Decker, R. H.; Johnson, C. R.; Wang, Z.; Jarvis, W. D.; Richon, V. M.; Ehinger, M.; Fisher, P. B.; Grant, S. Induction of apoptosis in U937 human leukemia cells by suberoylanilide hydroxamic acid (SAHA) proceeds through pathways that are regulated by Bcl-2/Bcl-XL, c-Jun, and p21CIP1, but independent of p53. Oncogene 1999, 18 (50), 7016-7025.
    • (1999) Oncogene , vol.18 , Issue.50 , pp. 7016-7025
    • Vrana, J.A.1    Decker, R.H.2    Johnson, C.R.3    Wang, Z.4    Jarvis, W.D.5    Richon, V.M.6    Ehinger, M.7    Fisher, P.B.8    Grant, S.9
  • 67
    • 44649127394 scopus 로고    scopus 로고
    • Histone deacetylase regulation of immune gene expression in tumor cells
    • Khan, A. N.; Tomasi, T. B. Histone deacetylase regulation of immune gene expression in tumor cells. Immunol. Res. 2008, 40 (2), 164-178.
    • (2008) Immunol. Res , vol.40 , Issue.2 , pp. 164-178
    • Khan, A.N.1    Tomasi, T.B.2
  • 68
    • 77951685547 scopus 로고    scopus 로고
    • The novel inhibitor of histone deacetylase resminostat (RAS2410) inhibits proliferation and induces apoptosis in multiple myeloma (MM) cells
    • Mandl-Weber, S.; Meinel, F. G.; Jankowsky, R.; Oduncu, F.; Schmidmaier, R.; Baumann, P. The novel inhibitor of histone deacetylase resminostat (RAS2410) inhibits proliferation and induces apoptosis in multiple myeloma (MM) cells. Br. J. Haematol. 2010, 149 (4), 518-528.
    • (2010) Br. J. Haematol , vol.149 , Issue.4 , pp. 518-528
    • Mandl-Weber, S.1    Meinel, F.G.2    Jankowsky, R.3    Oduncu, F.4    Schmidmaier, R.5    Baumann, P.6
  • 69
    • 77957091318 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor induces DNA damage, which normal but not transformed cells can repair
    • Lee, J. H.; Choy, M. L.; Ngo, L.; Foster, S. S.; Marks, P. A. Histone deacetylase inhibitor induces DNA damage, which normal but not transformed cells can repair. Proc. Natl. Acad. Sci. U. S. A. 2010, 107 (33), 14639-14644.
    • (2010) Proc. Natl. Acad. Sci. U. S. A , vol.107 , Issue.33 , pp. 14639-14644
    • Lee, J.H.1    Choy, M.L.2    Ngo, L.3    Foster, S.S.4    Marks, P.A.5
  • 71
    • 79956101962 scopus 로고    scopus 로고
    • The dual EGFR/HER2 inhibitor lapatinib synergistically enhances the antitumor activity of the histone deacetylase inhibitor panobinostat in colorectal cancer models
    • LaBonte, M. J.; Wilson, P. M.; Fazzone, W.; Russell, J.; Louie, S. G.; El-Khoueiry, A.; Lenz, H. J.; Ladner, R. D. The dual EGFR/HER2 inhibitor lapatinib synergistically enhances the antitumor activity of the histone deacetylase inhibitor panobinostat in colorectal cancer models. Cancer Res. 2011, 71 (10), 3635-3648.
    • (2011) Cancer Res , vol.71 , Issue.10 , pp. 3635-3648
    • Labonte, M.J.1    Wilson, P.M.2    Fazzone, W.3    Russell, J.4    Louie, S.G.5    El-Khoueiry, A.6    Lenz, H.J.7    Ladner, R.D.8
  • 73
    • 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 (8), 1967-1974.
    • (2006) Mol. Cancer. Ther , vol.5 , Issue.8 , 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
  • 74
    • 67349157687 scopus 로고    scopus 로고
    • Biomarkers for predicting clinical responses to HDAC inhibitors
    • Stimson, L.; La Thangue, N. B. Biomarkers for predicting clinical responses to HDAC inhibitors. Cancer Lett. 2009, 280 (2), 177-183.
    • (2009) Cancer Lett , vol.280 , Issue.2 , pp. 177-183
    • Stimson, L.1    la Thangue, N.B.2
  • 77
    • 0037169358 scopus 로고    scopus 로고
    • Apoptosis: A link between cancer genetics and chemotherapy
    • Johnstone, R. W.; Ruefli, A. A.; Lowe, S. W. Apoptosis: a link between cancer genetics and chemotherapy. Cell 2002, 108 (2), 153-164.
    • (2002) Cell , vol.108 , Issue.2 , pp. 153-164
    • Johnstone, R.W.1    Ruefli, A.A.2    Lowe, S.W.3
  • 78
    • 70349100446 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Current status and overview of recent clinical trials
    • Ma, X.; Ezzeldin, H. H.; Diasio, R. B. Histone deacetylase inhibitors: current status and overview of recent clinical trials. Drugs 2009, 69 (14), 1911-1934.
    • (2009) Drugs , vol.69 , Issue.14 , pp. 1911-1934
    • Ma, X.1    Ezzeldin, H.H.2    Diasio, R.B.3
  • 80
    • 77953712167 scopus 로고    scopus 로고
    • Mitochondrial signaling in cell death via the Bcl-2 family
    • Leibowitz, B.; Yu, J. Mitochondrial signaling in cell death via the Bcl-2 family. Cancer Biol. Ther. 2010, 9 (6), 417-422.
    • (2010) Cancer Biol. Ther , vol.9 , Issue.6 , pp. 417-422
    • Leibowitz, B.1    Yu, J.2
  • 81
    • 33847328289 scopus 로고    scopus 로고
    • The Bcl-2 apoptotic switch in cancer development and therapy
    • Adams, J. M.; Cory, S. The Bcl-2 apoptotic switch in cancer development and therapy. Oncogene 2007, 26 (9), 1324-1337.
    • (2007) Oncogene , vol.26 , Issue.9 , pp. 1324-1337
    • Adams, J.M.1    Cory, S.2
  • 82
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle, R. J.; Strasser, A. The BCL-2 protein family: opposing activities that mediate cell death. Nat. Rev. Mol. Cell. Biol. 2008, 9 (1), 47-59.
    • (2008) Nat. Rev. Mol. Cell. Biol , vol.9 , Issue.1 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 83
    • 0035845541 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species
    • Ruefli, A. A.; Ausserlechner, M. J.; Bernhard, D.; Sutton, V. R.; Tainton, K. M.; Kofler, R.; Smyth, M. J.; Johnstone, R. W. The histone deacetylase inhibitor and chemotherapeutic agent suberoylanilide hydroxamic acid (SAHA) induces a cell-death pathway characterized by cleavage of Bid and production of reactive oxygen species. Proc. Natl. Acad. Sci. U. S. A. 2001, 98 (19), 10833-10838.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , Issue.19 , pp. 10833-10838
    • Ruefli, A.A.1    Ausserlechner, M.J.2    Bernhard, D.3    Sutton, V.R.4    Tainton, K.M.5    Kofler, R.6    Smyth, M.J.7    Johnstone, R.W.8
  • 84
    • 27644556419 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylases target the Rb-E2F1 pathway for apoptosis induction through activation of proapoptotic protein Bim
    • Zhao, Y.; Tan, J.; Zhuang, L.; Jiang, X.; Liu, E. T.; Yu, Q. Inhibitors of histone deacetylases target the Rb-E2F1 pathway for apoptosis induction through activation of proapoptotic protein Bim. Proc. Natl. Acad. Sci. U. S. A. 2005, 102 (44), 16090-16095.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , Issue.44 , pp. 16090-16095
    • Zhao, Y.1    Tan, J.2    Zhuang, L.3    Jiang, X.4    Liu, E.T.5    Yu, Q.6
  • 86
    • 34249993174 scopus 로고    scopus 로고
    • SAHA induces apoptosis in hepatoma cells and synergistically interacts with the proteasome inhibitor Bortezomib
    • Emanuele, S.; Lauricella, M.; Carlisi, D.; Vassallo, B.; D'Anneo, A.; Di Fazio, P.; Vento, R.; Tesoriere, G. SAHA induces apoptosis in hepatoma cells and synergistically interacts with the proteasome inhibitor Bortezomib. Apoptosis 2007, 12 (7), 1327-1338.
    • (2007) Apoptosis , vol.12 , Issue.7 , pp. 1327-1338
    • Emanuele, S.1    Lauricella, M.2    Carlisi, D.3    Vassallo, B.4    D'Anneo, A.5    Di Fazio, P.6    Vento, R.7    Tesoriere, G.8
  • 87
    • 23244459828 scopus 로고    scopus 로고
    • Interactive effects of HDAC inhibitors and TRAIL on apoptosis are associated with changes in mitochondrial functions and expressions of cell cycle regulatory genes in multiple myeloma
    • Fandy, T. E.; Shankar, S.; Ross, D. D.; Sausville, E.; Srivastava, R. K. Interactive effects of HDAC inhibitors and TRAIL on apoptosis are associated with changes in mitochondrial functions and expressions of cell cycle regulatory genes in multiple myeloma. Neoplasia 2005, 7 (7), 646-657.
    • (2005) Neoplasia , vol.7 , Issue.7 , pp. 646-657
    • Fandy, T.E.1    Shankar, S.2    Ross, D.D.3    Sausville, E.4    Srivastava, R.K.5
  • 88
    • 4344666663 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors upregulate death receptor 5/TRAIL-R2 and sensitize apoptosis induced by TRAIL/APO2-L in human malignant tumor cells
    • Nakata, S.; Yoshida, T.; Horinaka, M.; Shiraishi, T.; Wakada, M.; Sakai, T. Histone deacetylase inhibitors upregulate death receptor 5/TRAIL-R2 and sensitize apoptosis induced by TRAIL/APO2-L in human malignant tumor cells. Oncogene 2004, 23 (37), 6261-6271.
    • (2004) Oncogene , vol.23 , Issue.37 , pp. 6261-6271
    • Nakata, S.1    Yoshida, T.2    Horinaka, M.3    Shiraishi, T.4    Wakada, M.5    Sakai, T.6
  • 90
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci, S.; Pelicci, P. G. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat. Rev. Cancer 2006, 6 (1), 38-51.
    • (2006) Nat. Rev. Cancer , vol.6 , Issue.1 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 92
    • 33644663872 scopus 로고    scopus 로고
    • Histone acetylationindependent effect of histone deacetylase inhibitors on Akt through the reshuffling of protein phosphatase 1 complexes
    • Chen, C. S.; Weng, S. C.; Tseng, P. H.; Lin, H. P. Histone acetylationindependent effect of histone deacetylase inhibitors on Akt through the reshuffling of protein phosphatase 1 complexes. J. Biol. Chem. 2005, 280 (46), 38879-38887.
    • (2005) J. Biol. Chem , vol.280 , Issue.46 , pp. 38879-38887
    • Chen, C.S.1    Weng, S.C.2    Tseng, P.H.3    Lin, H.P.4
  • 95
    • 0036842460 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis
    • Rossig, L.; Li, H.; Fisslthaler, B.; Urbich, C.; Fleming, I.; Forstermann, U.; Zeiher, A. M.; Dimmeler, S. Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis. Circ. Res. 2002, 91 (9), 837-844.
    • (2002) Circ. Res , vol.91 , Issue.9 , pp. 837-844
    • Rossig, L.1    Li, H.2    Fisslthaler, B.3    Urbich, C.4    Fleming, I.5    Forstermann, U.6    Zeiher, A.M.7    Dimmeler, S.8
  • 98
    • 1642415712 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor suberoylanilide hydroxamic acid reduces acute graft-versus-host disease and preserves graft-versus-leukemia effect
    • Reddy, P.; Maeda, Y.; Hotary, K.; Liu, C.; Reznikov, L. L.; Dinarello, C. A.; Ferrara, J. L. Histone deacetylase inhibitor suberoylanilide hydroxamic acid reduces acute graft-versus-host disease and preserves graft-versus-leukemia effect. Proc. Natl. Acad. Sci. U. S. A. 2004, 101 (11), 3921-3926.
    • (2004) Proc. Natl. Acad. Sci. U. S. A , vol.101 , Issue.11 , pp. 3921-3926
    • Reddy, P.1    Maeda, Y.2    Hotary, K.3    Liu, C.4    Reznikov, L.L.5    Dinarello, C.A.6    Ferrara, J.L.7
  • 99
    • 12244251445 scopus 로고    scopus 로고
    • Stat3 dimerization regulated by reversible acetylation of a single lysine residue
    • Yuan, Z. L.; Guan, Y. J.; Chatterjee, D.; Chin, Y. E. Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science 2005, 307 (5707), 269-273.
    • (2005) Science , vol.307 , Issue.5707 , pp. 269-273
    • Yuan, Z.L.1    Guan, Y.J.2    Chatterjee, D.3    Chin, Y.E.4
  • 100
    • 79958189845 scopus 로고    scopus 로고
    • Histone acetyltransferases are crucial regulators in NF-kappaB mediated inflammation
    • Ghizzoni, M.; Haisma, H. J.; Maarsingh, H.; Dekker, F. J. Histone acetyltransferases are crucial regulators in NF-kappaB mediated inflammation. Drug Discov. Today 2011, 16 (11-12), 504-511.
    • (2011) Drug Discov. Today , vol.16 , Issue.11-12 , pp. 504-511
    • Ghizzoni, M.1    Haisma, H.J.2    Maarsingh, H.3    Dekker, F.J.4
  • 101
    • 0035977063 scopus 로고    scopus 로고
    • Butyrate suppression of colonocyte NF-kappa B activation and cellular proteasome activity
    • Yin, L.; Laevsky, G.; Giardina, C. Butyrate suppression of colonocyte NF-kappa B activation and cellular proteasome activity. J. Biol. Chem. 2001, 276 (48), 44641-44646.
    • (2001) J. Biol. Chem , vol.276 , Issue.48 , pp. 44641-44646
    • Yin, L.1    Laevsky, G.2    Giardina, C.3
  • 102
    • 40949085551 scopus 로고    scopus 로고
    • HDAC2 deficiency sensitizes colon cancer cells to TNFalphainduced apoptosis through inhibition of NF-kappaB activity
    • Kaler, P.; Sasazuki, T.; Shirasawa, S.; Augenlicht, L.; Klampfer, L. HDAC2 deficiency sensitizes colon cancer cells to TNFalphainduced apoptosis through inhibition of NF-kappaB activity. Exp. Cell Res. 2008, 314 (7), 1507-1518.
    • (2008) Exp. Cell Res , vol.314 , Issue.7 , pp. 1507-1518
    • Kaler, P.1    Sasazuki, T.2    Shirasawa, S.3    Augenlicht, L.4    Klampfer, L.5
  • 103
    • 0038819943 scopus 로고    scopus 로고
    • Ineffectiveness of histone deacetylase inhibitors to induce apoptosis involves the transcriptional activation of NF-kappa B through the Akt pathway
    • Mayo, M. W.; Denlinger, C. E.; Broad, R. M.; Yeung, F.; Reilly, E. T.; Shi, Y.; Jones, D. R. Ineffectiveness of histone deacetylase inhibitors to induce apoptosis involves the transcriptional activation of NF-kappa B through the Akt pathway. J. Biol. Chem. 2003, 278 (21), 18980-18989.
    • (2003) J. Biol. Chem , vol.278 , Issue.21 , pp. 18980-18989
    • Mayo, M.W.1    Denlinger, C.E.2    Broad, R.M.3    Yeung, F.4    Reilly, E.T.5    Shi, Y.6    Jones, D.R.7
  • 104
    • 0034802887 scopus 로고    scopus 로고
    • The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression
    • Ashburner, B. P.; Westerheide, S. D.; Baldwin, A. S., Jr. The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression. Mol. Cell. Biol. 2001, 21 (20), 7065-7077.
    • (2001) Mol. Cell. Biol , vol.21 , Issue.20 , pp. 7065-7077
    • Ashburner, B.P.1    Westerheide, S.D.2    Baldwin Jr., A.S.3
  • 105
    • 51649119512 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor-induced cellular apoptosis involves stanniocalcin-1 activation
    • Law, A. Y.; Lai, K. P.; Lui, W. C.; Wan, H. T.; Wong, C. K. Histone deacetylase inhibitor-induced cellular apoptosis involves stanniocalcin-1 activation. Exp. Cell. Res. 2008, 314 (16), 2975-2984.
    • (2008) Exp. Cell. Res , vol.314 , Issue.16 , pp. 2975-2984
    • Law, A.Y.1    Lai, K.P.2    Lui, W.C.3    Wan, H.T.4    Wong, C.K.5
  • 106
    • 33846013917 scopus 로고    scopus 로고
    • NF-kappaB signaling pathway is involved in growth inhibition, G2/M arrest and apoptosis induced by Trichostatin A in human tongue carcinoma cells
    • Yao, J.; Duan, L.; Fan, M.; Wu, X. NF-kappaB signaling pathway is involved in growth inhibition, G2/M arrest and apoptosis induced by Trichostatin A in human tongue carcinoma cells. Pharmacol. Res. 2006, 54 (6), 406-413.
    • (2006) Pharmacol. Res , vol.54 , Issue.6 , pp. 406-413
    • Yao, J.1    Duan, L.2    Fan, M.3    Wu, X.4
  • 107
    • 77957287127 scopus 로고    scopus 로고
    • HDAC inhibitor-induced activation of NF-kappaB prevents apoptotic response of E1A+Ras-transformed cells to proapoptotic stimuli
    • Abramova, M. V.; Zatulovskiy, E. A.; Svetlikova, S. B.; Pospelov, V. A. HDAC inhibitor-induced activation of NF-kappaB prevents apoptotic response of E1A+Ras-transformed cells to proapoptotic stimuli. Int. J. Biochem. Cell Biol. 2010, 42 (11), 1847-1855.
    • (2010) Int. J. Biochem. Cell Biol , vol.42 , Issue.11 , pp. 1847-1855
    • Abramova, M.V.1    Zatulovskiy, E.A.2    Svetlikova, S.B.3    Pospelov, V.A.4
  • 110
    • 66149122282 scopus 로고    scopus 로고
    • Two modes of transcriptional activation at native promoters by NF-kappaB p65
    • van Essen, D.; Engist, B.; Natoli, G.; Saccani, S. Two modes of transcriptional activation at native promoters by NF-kappaB p65. PLoS Biol. 2009, 7 (3), e73.
    • (2009) PLoS Biol , vol.7 , Issue.3
    • van Essen, D.1    Engist, B.2    Natoli, G.3    Saccani, S.4
  • 111
    • 79953304257 scopus 로고    scopus 로고
    • Histone deacetylase 1 is required for exocrine pancreatic epithelial proliferation in development and cancer
    • Zhou, W.; Liang, I. C.; Yee, N. S. Histone deacetylase 1 is required for exocrine pancreatic epithelial proliferation in development and cancer. Cancer Biol. Ther. 2011, 11 (7), 659-670.
    • (2011) Cancer Biol. Ther , vol.11 , Issue.7 , pp. 659-670
    • Zhou, W.1    Liang, I.C.2    Yee, N.S.3
  • 112
    • 41149162821 scopus 로고    scopus 로고
    • Expression of hypoxia-inducible factor-1alpha, histone deacetylase 1, and metastasis-associated protein 1 in pancreatic carcinoma: Correlation with poor prognosis with possible regulation
    • Miyake, K.; Yoshizumi, T.; Imura, S.; Sugimoto, K.; Batmunkh, E.; Kanemura, H.; Morine, Y.; Shimada, M. Expression of hypoxia-inducible factor-1alpha, histone deacetylase 1, and metastasis-associated protein 1 in pancreatic carcinoma: correlation with poor prognosis with possible regulation. Pancreas 2008, 36 (3), e1-e9.
    • (2008) Pancreas , vol.36 , Issue.3
    • Miyake, K.1    Yoshizumi, T.2    Imura, S.3    Sugimoto, K.4    Batmunkh, E.5    Kanemura, H.6    Morine, Y.7    Shimada, M.8
  • 113
    • 70349309923 scopus 로고    scopus 로고
    • HDAC2 mediates therapeutic resistance of pancreatic cancer cells via the BH3-only protein NOXA
    • Fritsche, P.; Seidler, B.; Schuler, S.; Schnieke, A.; Gottlicher, M.; Schmid, R. M.; Saur, D.; Schneider, G. HDAC2 mediates therapeutic resistance of pancreatic cancer cells via the BH3-only protein NOXA. Gut 2009, 58 (10), 1399-1409.
    • (2009) Gut , vol.58 , Issue.10 , pp. 1399-1409
    • Fritsche, P.1    Seidler, B.2    Schuler, S.3    Schnieke, A.4    Gottlicher, M.5    Schmid, R.M.6    Saur, D.7    Schneider, G.8
  • 118
    • 50449091498 scopus 로고    scopus 로고
    • Advances in and applications of proteasome inhibitors
    • Moore, B. S.; Eustaquio, A. S.; McGlinchey, R. P. Advances in and applications of proteasome inhibitors. Curr. Opin. Chem. Biol. 2008, 12 (4), 434-440.
    • (2008) Curr. Opin. Chem. Biol , vol.12 , Issue.4 , pp. 434-440
    • Moore, B.S.1    Eustaquio, A.S.2    McGlinchey, R.P.3
  • 119
    • 42349091446 scopus 로고    scopus 로고
    • Role of the aggresome pathway in cancer: Targeting histone deacetylase 6-dependent protein degradation
    • Rodriguez-Gonzalez, A.; Lin, T.; Ikeda, A. K.; Simms-Waldrip, T.; Fu, C.; Sakamoto, K. M. Role of the aggresome pathway in cancer: targeting histone deacetylase 6-dependent protein degradation. Cancer Res. 2008, 68 (8), 2557-2560.
    • (2008) Cancer Res , vol.68 , Issue.8 , pp. 2557-2560
    • Rodriguez-Gonzalez, A.1    Lin, T.2    Ikeda, A.K.3    Simms-Waldrip, T.4    Fu, C.5    Sakamoto, K.M.6
  • 120
    • 77952420148 scopus 로고    scopus 로고
    • Proteasome inhibition: A new therapeutic strategy to cancer treatment
    • Wu, W. K.; Cho, C. H.; Lee, C. W.; Wu, K.; Fan, D.; Yu, J.; Sung, J. J. Proteasome inhibition: a new therapeutic strategy to cancer treatment. Cancer Lett. 2010, 293 (1), 15-22.
    • (2010) Cancer Lett , vol.293 , Issue.1 , pp. 15-22
    • Wu, W.K.1    Cho, C.H.2    Lee, C.W.3    Wu, K.4    Fan, D.5    Yu, J.6    Sung, J.J.7
  • 122
    • 45749114198 scopus 로고    scopus 로고
    • Chemistry, biology, and QSAR studies of substituted biaryl hydroxamates and mercaptoacetamides as HDAC inhibitors-nanomolar-potency inhibitors of pancreatic cancer cell growth
    • Kozikowski, A. P.; Chen, Y.; Gaysin, A. M.; Savoy, D. N.; Billadeau, D. D.; Kim, K. H. Chemistry, biology, and QSAR studies of substituted biaryl hydroxamates and mercaptoacetamides as HDAC inhibitors-nanomolar-potency inhibitors of pancreatic cancer cell growth. ChemMedChem 2008, 3 (3), 487-501.
    • (2008) ChemMedChem , vol.3 , Issue.3 , pp. 487-501
    • Kozikowski, A.P.1    Chen, Y.2    Gaysin, A.M.3    Savoy, D.N.4    Billadeau, D.D.5    Kim, K.H.6
  • 123
    • 81255179936 scopus 로고    scopus 로고
    • The 26S proteasome complex: An attractive target for cancer therapy
    • Frankland-Searby, S.; Bhaumik, S. R. The 26S proteasome complex: An attractive target for cancer therapy. Biochim. Biophys. Acta 2012, 1825 (1), 64-76.
    • (2012) Biochim. Biophys. Acta , vol.1825 , Issue.1 , pp. 64-76
    • Frankland-Searby, S.1    Bhaumik, S.R.2
  • 124
    • 84860279756 scopus 로고    scopus 로고
    • Contribution of Epithelial-to-Mesenchymal Transition and Cancer Stem Cells to Pancreatic Cancer Progression
    • Krantz, S. B.; Shields, M. A.; Dangi-Garimella, S.; Munshi, H. G.; Bentrem, D. J. Contribution of Epithelial-to-Mesenchymal Transition and Cancer Stem Cells to Pancreatic Cancer Progression. J. Surg. Res. 2011.
    • (2011) J. Surg. Res
    • Krantz, S.B.1    Shields, M.A.2    Dangi-Garimella, S.3    Munshi, H.G.4    Bentrem, D.J.5
  • 125
    • 44449144396 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition: At the crossroads of development and tumor metastasis
    • Yang, J.; Weinberg, R. A. Epithelial-mesenchymal transition: at the crossroads of development and tumor metastasis. Dev. Cell 2008, 14 (6), 818-829.
    • (2008) Dev. Cell , vol.14 , Issue.6 , pp. 818-829
    • Yang, J.1    Weinberg, R.A.2
  • 126
    • 0028691011 scopus 로고
    • Loss of membranous Ecadherin expression in pancreatic cancer: Correlation with lymph node metastasis, high grade, and advanced stage
    • Pignatelli, M.; Ansari, T. W.; Gunter, P.; Liu, D.; Hirano, S.; Takeichi, M.; Kloppel, G.; Lemoine, N. R. Loss of membranous Ecadherin expression in pancreatic cancer: correlation with lymph node metastasis, high grade, and advanced stage. J. Pathol. 1994, 174 (4), 243-248.
    • (1994) J. Pathol , vol.174 , Issue.4 , pp. 243-248
    • Pignatelli, M.1    Ansari, T.W.2    Gunter, P.3    Liu, D.4    Hirano, S.5    Takeichi, M.6    Kloppel, G.7    Lemoine, N.R.8
  • 129
    • 49749105155 scopus 로고    scopus 로고
    • Apoptotic pathways in pancreatic ductal adenocarcinoma
    • Hamacher, R.; Schmid, R. M.; Saur, D.; Schneider, G. Apoptotic pathways in pancreatic ductal adenocarcinoma. Mol. Cancer 2008, 7, 64.
    • (2008) Mol. Cancer , vol.7 , pp. 64
    • Hamacher, R.1    Schmid, R.M.2    Saur, D.3    Schneider, G.4
  • 130
    • 73449126835 scopus 로고    scopus 로고
    • MS275 enhances cytotoxicity induced by 5-fluorouracil in the colorectal cancer cells
    • Flis, S.; Gnyszka, A.; Flis, K.; Splawinski, J. MS275 enhances cytotoxicity induced by 5-fluorouracil in the colorectal cancer cells. Eur. J. Pharmacol. 2010, 627 (1-3), 26-32.
    • (2010) Eur. J. Pharmacol , vol.627 , Issue.1-3 , pp. 26-32
    • Flis, S.1    Gnyszka, A.2    Flis, K.3    Splawinski, J.4
  • 131
    • 80052357047 scopus 로고    scopus 로고
    • Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3B1, a novel epithelialmesenchymal transition inducer in pancreatic cancer
    • Song, K.; Li, Q.; Jiang, Z. Z.; Guo, C. W.; Li, P. Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3B1, a novel epithelialmesenchymal transition inducer in pancreatic cancer. Cancer Biol. Ther. 2011, 12 (5), 388-398.
    • (2011) Cancer Biol. Ther , vol.12 , Issue.5 , pp. 388-398
    • Song, K.1    Li, Q.2    Jiang, Z.Z.3    Guo, C.W.4    Li, P.5
  • 133
    • 6044264858 scopus 로고    scopus 로고
    • FR901228, a novel histone deacetylase inhibitor, induces cell cycle arrest and subsequent apoptosis in refractory human pancreatic cancer cells
    • Sato, N.; Ohta, T.; Kitagawa, H.; Kayahara, M.; Ninomiya, I.; Fushida, S.; Fujimura, T.; Nishimura, G.; Shimizu, K.; Miwa, K. FR901228, a novel histone deacetylase inhibitor, induces cell cycle arrest and subsequent apoptosis in refractory human pancreatic cancer cells. Int. J. Oncol. 2004, 24 (3), 679-685.
    • (2004) Int. J. Oncol , vol.24 , Issue.3 , pp. 679-685
    • Sato, N.1    Ohta, T.2    Kitagawa, H.3    Kayahara, M.4    Ninomiya, I.5    Fushida, S.6    Fujimura, T.7    Nishimura, G.8    Shimizu, K.9    Miwa, K.10
  • 134
    • 61449119672 scopus 로고    scopus 로고
    • Markers involved in resistance to cytotoxics and targeted therapeutics in pancreatic cancer
    • El Maalouf, G.; Le Tourneau, C.; Batty, G. N.; Faivre, S.; Raymond, E. Markers involved in resistance to cytotoxics and targeted therapeutics in pancreatic cancer. Cancer Treat. Rev. 2009, 35 (2), 167-174.
    • (2009) Cancer Treat. Rev , vol.35 , Issue.2 , pp. 167-174
    • El-Maalouf, G.1    Le Tourneau, C.2    Batty, G.N.3    Faivre, S.4    Raymond, E.5
  • 136
    • 33747874802 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor trichostatin A and proteasome inhibitor PS- 341 synergistically induce apoptosis in pancreatic cancer cells
    • Bai, J.; Demirjian, A.; Sui, J.; Marasco, W.; Callery, M. P. Histone deacetylase inhibitor trichostatin A and proteasome inhibitor PS- 341 synergistically induce apoptosis in pancreatic cancer cells. Biochem. Biophys. Res. Commun. 2006, 348 (4), 1245-1253.
    • (2006) Biochem. Biophys. Res. Commun , vol.348 , Issue.4 , pp. 1245-1253
    • Bai, J.1    Demirjian, A.2    Sui, J.3    Marasco, W.4    Callery, M.P.5
  • 138
    • 79956198574 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor MGCD0103 synergizes with gemcitabine in human pancreatic cells
    • Sung, V.; Richard, N.; Brady, H.; Maier, A.; Kelter, G.; Heise, C. Histone deacetylase inhibitor MGCD0103 synergizes with gemcitabine in human pancreatic cells. Cancer Sci. 2011, 102 (6), 1201-1207.
    • (2011) Cancer Sci , vol.102 , Issue.6 , pp. 1201-1207
    • Sung, V.1    Richard, N.2    Brady, H.3    Maier, A.4    Kelter, G.5    Heise, C.6
  • 140
    • 80051550908 scopus 로고    scopus 로고
    • Effects and mechanisms of the combination of suberoylanilide hydroxamic acid and bortezomib on the anticancer property of gemcitabine in pancreatic cancer
    • Lee, J. K.; Ryu, J. K.; Yang, K. Y.; Woo, S. M.; Park, J. K.; Yoon, W. J.; Lee, S. H.; Jeong, K. S.; Kim, Y. T.; Yoon, Y. B. Effects and mechanisms of the combination of suberoylanilide hydroxamic acid and bortezomib on the anticancer property of gemcitabine in pancreatic cancer. Pancreas 2011, 40 (6), 966-973.
    • (2011) Pancreas , vol.40 , Issue.6 , pp. 966-973
    • Lee, J.K.1    Ryu, J.K.2    Yang, K.Y.3    Woo, S.M.4    Park, J.K.5    Yoon, W.J.6    Lee, S.H.7    Jeong, K.S.8    Kim, Y.T.9    Yoon, Y.B.10
  • 142
    • 70349334004 scopus 로고    scopus 로고
    • Gene expression-signature of belinostat in cell lines is specific for histone deacetylase inhibitor treatment, with a corresponding signature in xenografts
    • Monks, A.; Hose, C. D.; Pezzoli, P.; Kondapaka, S.; Vansant, G.; Petersen, K. D.; Sehested, M.; Monforte, J.; Shoemaker, R. H. Gene expression-signature of belinostat in cell lines is specific for histone deacetylase inhibitor treatment, with a corresponding signature in xenografts. Anticancer Drugs 2009, 20 (8), 682-692.
    • (2009) Anticancer Drugs , vol.20 , Issue.8 , pp. 682-692
    • Monks, A.1    Hose, C.D.2    Pezzoli, P.3    Kondapaka, S.4    Vansant, G.5    Petersen, K.D.6    Sehested, M.7    Monforte, J.8    Shoemaker, R.H.9
  • 143
    • 79956071947 scopus 로고    scopus 로고
    • Synergistic activity of histone deacetylase and proteasome inhibition against pancreatic and hepatocellular cancer cell lines
    • Spratlin, J. L.; Pitts, T. M.; Kulikowski, G. N.; Morelli, M. P.; Tentler, J. J.; Serkova, N. J.; Eckhardt, S. G. Synergistic activity of histone deacetylase and proteasome inhibition against pancreatic and hepatocellular cancer cell lines. Anticancer Res. 2011, 31 (4), 1093-1103.
    • (2011) Anticancer Res , vol.31 , Issue.4 , pp. 1093-1103
    • Spratlin, J.L.1    Pitts, T.M.2    Kulikowski, G.N.3    Morelli, M.P.4    Tentler, J.J.5    Serkova, N.J.6    Eckhardt, S.G.7
  • 145
    • 67349232749 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors that target tubulin
    • Schemies, J.; Sippl, W.; Jung, M. Histone deacetylase inhibitors that target tubulin. Cancer Lett. 2009, 280 (2), 222-232.
    • (2009) Cancer Lett , vol.280 , Issue.2 , pp. 222-232
    • Schemies, J.1    Sippl, W.2    Jung, M.3
  • 146
    • 79959946212 scopus 로고    scopus 로고
    • C6-ceramide synergistically potentiates the anti-tumor effects of histone deacetylase inhibitors via AKT dephosphorylation and alpha-tubulin hyperacetylation both in vitro and in vivo
    • Zhu, Q. Y.; Wang, Z.; Ji, C.; Cheng, L.; Yang, Y. L.; Ren, J.; Jin, Y. H.; Wang, Q. J.; Gu, X. J.; Bi, Z. G.; Hu, G.; Yang, Y. C6-ceramide synergistically potentiates the anti-tumor effects of histone deacetylase inhibitors via AKT dephosphorylation and alpha-tubulin hyperacetylation both in vitro and in vivo. Cell Death Dis. 2011, 2, e117.
    • (2011) Cell Death Dis , vol.2
    • Zhu, Q.Y.1    Wang, Z.2    Ji, C.3    Cheng, L.4    Yang, Y.L.5    Ren, J.6    Jin, Y.H.7    Wang, Q.J.8    Gu, X.J.9    Bi, Z.G.10    Hu, G.11    Yang, Y.12
  • 147
    • 79953742165 scopus 로고    scopus 로고
    • Histone modification enhances the effectiveness of IL-13 receptor targeted immunotoxin in murine models of human pancreatic cancer
    • Fujisawa, T.; Joshi, B. H.; Puri, R. K. Histone modification enhances the effectiveness of IL-13 receptor targeted immunotoxin in murine models of human pancreatic cancer. J. Transl. Med. 2011, 9, 37.
    • (2011) J. Transl. Med , vol.9 , pp. 37
    • Fujisawa, T.1    Joshi, B.H.2    Puri, R.K.3
  • 148
    • 70149124715 scopus 로고    scopus 로고
    • Phase I and pharmacokinetic study of vorinostat (suberoylanilide hydroxamic acid) in Japanese patients with solid tumors
    • Fujiwara, Y.; Yamamoto, N.; Yamada, Y.; Yamada, K.; Otsuki, T.; Kanazu, S.; Iwasa, T.; Hardwick, J. S.; Tamura, T. Phase I and pharmacokinetic study of vorinostat (suberoylanilide hydroxamic acid) in Japanese patients with solid tumors. Cancer Sci. 2009, 100 (9), 1728-1734.
    • (2009) Cancer Sci , vol.100 , Issue.9 , pp. 1728-1734
    • Fujiwara, Y.1    Yamamoto, N.2    Yamada, Y.3    Yamada, K.4    Otsuki, T.5    Kanazu, S.6    Iwasa, T.7    Hardwick, J.S.8    Tamura, T.9
  • 149
    • 0028859363 scopus 로고
    • Human glioma cells overexpress receptors for interleukin 13 and are extremely sensitive to a novel chimeric protein composed of interleukin 13 and pseudomonas exotoxin
    • Debinski, W.; Obiri, N. I.; Powers, S. K.; Pastan, I.; Puri, R. K. Human glioma cells overexpress receptors for interleukin 13 and are extremely sensitive to a novel chimeric protein composed of interleukin 13 and pseudomonas exotoxin. Clin. Cancer Res. 1995, 1 (11), 1253-1258.
    • (1995) Clin. Cancer Res , vol.1 , Issue.11 , pp. 1253-1258
    • Debinski, W.1    Obiri, N.I.2    Powers, S.K.3    Pastan, I.4    Puri, R.K.5
  • 150
    • 67449145358 scopus 로고    scopus 로고
    • Rational combinations using HDAC inhibitors
    • Bots, M.; Johnstone, R. W. Rational combinations using HDAC inhibitors. Clin. Cancer Res. 2009, 15 (12), 3970-3977.
    • (2009) Clin. Cancer Res , vol.15 , Issue.12 , pp. 3970-3977
    • Bots, M.1    Johnstone, R.W.2
  • 151
    • 33745629366 scopus 로고    scopus 로고
    • Gemcitabine plus CI-994 offers no advantage over gemcitabine alone in the treatment of patients with advanced pancreatic cancer: Results of a phase II randomized, double-blind, placebo-controlled, multicenter study
    • Richards, D. A.; Boehm, K. A.; Waterhouse, D. M.; Wagener, D. J.; Krishnamurthi, S. S.; Rosemurgy, A.; Grove, W.; Macdonald, K.; Gulyas, S.; Clark, M.; Dasse, K. D. Gemcitabine plus CI-994 offers no advantage over gemcitabine alone in the treatment of patients with advanced pancreatic cancer: results of a phase II randomized, double-blind, placebo-controlled, multicenter study. Ann. Oncol. 2006, 17 (7), 1096-1102.
    • (2006) Ann. Oncol , vol.17 , Issue.7 , pp. 1096-1102
    • Richards, D.A.1    Boehm, K.A.2    Waterhouse, D.M.3    Wagener, D.J.4    Krishnamurthi, S.S.5    Rosemurgy, A.6    Grove, W.7    Macdonald, K.8    Gulyas, S.9    Clark, M.10    Dasse, K.D.11
  • 152
    • 70350443118 scopus 로고    scopus 로고
    • Phase I/II: The oral isotype-selective HDAC inhibitor MGCD0103 in combination with gemcitabine (Gem) in patients (pts) with refractory solid tumors
    • 15S-May 20
    • Hurwitz, H.; Nelson, B.; O'Dwyer, P. J.; Chiorean, E. G.; Gabrail, N.; Laille, E.; Drouin, M.; Rothenberg, M. L.; Chan, E. Phase I/II: The oral isotype-selective HDAC inhibitor MGCD0103 in combination with gemcitabine (Gem) in patients (pts) with refractory solid tumors. J. Clin. Oncol. 2008, 26 (15S-May 20).
    • (2008) J. Clin. Oncol , pp. 26
    • Hurwitz, H.1    Nelson, B.2    O'Dwyer, P.J.3    Chiorean, E.G.4    Gabrail, N.5    Laille, E.6    Drouin, M.7    Rothenberg, M.L.8    Chan, E.9
  • 153
    • 59149098431 scopus 로고    scopus 로고
    • A phase I trial of romidepsin in combination with gemcitabine in patients with pancreatic and other advanced solid tumors
    • 15S-May 20
    • Doss, H. H.; Jones, S. F.; Infante, J. R.; Spigel, D. R.; Willcutt, N.; Lamar, R.; Barton, J.; Keegan, M.; Burris, H. A. A phase I trial of romidepsin in combination with gemcitabine in patients with pancreatic and other advanced solid tumors. J. Clin. Oncol. 2008, 26 (15S-May 20).
    • (2008) J. Clin. Oncol , pp. 26
    • Doss, H.H.1    Jones, S.F.2    Infante, J.R.3    Spigel, D.R.4    Willcutt, N.5    Lamar, R.6    Barton, J.7    Keegan, M.8    Burris, H.A.9
  • 155
    • 84860276935 scopus 로고    scopus 로고
    • U.S. National Institutes of Health, Accessed November 30, 2011
    • U.S. National Institutes of Health. Health Information: Clinical Trials. http://www.clinicaltrials.gov/ct2/show/NCT00831493. (Accessed November 30, 2011).
    • Health Information: Clinical Trials
  • 156
    • 84860276935 scopus 로고    scopus 로고
    • U.S. National Institutes of Health, Accessed November 30, 2011
    • U.S. National Institutes of Health. Health Information: Clinical Trials. http://www.clinicaltrials.gov/ct2/show/NCT00983268. (Accessed November 30, 2011).
    • Health Information: Clinical Trials
  • 157
    • 84860276935 scopus 로고    scopus 로고
    • U.S. National Institutes of Health, Accessed November 30, 2011
    • U.S. National Institutes of Health. Health Information: Clinical Trials. http://www.clinicaltrials.gov/ct2/show/NCT00948688. (Accessed November 30, 2011).
    • Health Information: Clinical Trials
  • 158
    • 84860276935 scopus 로고    scopus 로고
    • U.S. National Institutes of Health, Accessed November 30, 2011
    • U.S. National Institutes of Health. Health Information: Clinical Trials. http://www.clinicaltrials.gov/ct2/show/NCT00667082. (Accessed November 30, 2011).
    • Health Information: Clinical Trials
  • 159
    • 84860276935 scopus 로고    scopus 로고
    • U.S. National Institutes of Health, Accessed November 30, 2011
    • U.S. National Institutes of Health. Health Information: Clinical Trials. http://www.clinicaltrials.gov/ct2/show/NCT01333631. (Accessed November 30, 2011).
    • Health Information: Clinical Trials
  • 162
    • 78650635358 scopus 로고    scopus 로고
    • The molecular targets for the diagnosis and treatment of pancreatic cancer
    • Strimpakos, A. S.; Syrigos, K. N.; Saif, M. W. The molecular targets for the diagnosis and treatment of pancreatic cancer. Gut Liver 2010, 4 (4), 433-449.
    • (2010) Gut Liver , vol.4 , Issue.4 , pp. 433-449
    • Strimpakos, A.S.1    Syrigos, K.N.2    Saif, M.W.3
  • 163
    • 80053161379 scopus 로고    scopus 로고
    • Combined inhibition of DNA methyltransferase and histone deacetylase restores caspase-8 expression and sensitizes SCLC cells to TRAIL
    • Kaminskyy, V. O.; Surova, O. V.; Vaculova, A.; Zhivotovsky, B. Combined inhibition of DNA methyltransferase and histone deacetylase restores caspase-8 expression and sensitizes SCLC cells to TRAIL. Carcinogenesis 2011.
    • (2011) Carcinogenesis
    • Kaminskyy, V.O.1    Surova, O.V.2    Vaculova, A.3    Zhivotovsky, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.