메뉴 건너뛰기




Volumn 41, Issue 1, 2009, Pages 21-25

Histone deacetylase inhibitors: Anticancer compounds

Author keywords

Acetylation; Cancer; Cell cycle; Chromatin; HDAC

Indexed keywords

3 PHENYLSULFAMOYLCINNAMOHYDROXAMIC ACID; ACETIC ACID DERIVATIVE; ANTINEOPLASTIC AGENT; APICIDIN; BELINOSTAT; BUTYRIC ACID; CYCLIN DEPENDENT KINASE INHIBITOR 1B; DEPSIPEPTIDE; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; N (2 AMINOPHENYL) 4 [4 (3 PYRIDINYL) 2 PYRIMIDINYLAMINOMETHYL]BENZAMIDE; RETINOIC ACID; ROMIDEPSIN; SODIUM PHENYLBUTYRATE; TRICHOSTATIN A; UNCLASSIFIED DRUG; VALPROIC ACID; VORINOSTAT;

EID: 55949083044     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2008.09.008     Document Type: Short Survey
Times cited : (86)

References (49)
  • 1
    • 9744223645 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor trichostatin A represses estrogen receptor alpha-dependent transcription and promotes proteasomal degradation of cyclin D1 in human breast carcinoma cell lines
    • Alao J.P., Lam E.W., Ali S., Buluwela L., Bordogna W., Lockey P., et al. Histone deacetylase inhibitor trichostatin A represses estrogen receptor alpha-dependent transcription and promotes proteasomal degradation of cyclin D1 in human breast carcinoma cell lines. Clin Cancer Res 10 (2004) 8094-8104
    • (2004) Clin Cancer Res , vol.10 , pp. 8094-8104
    • Alao, J.P.1    Lam, E.W.2    Ali, S.3    Buluwela, L.4    Bordogna, W.5    Lockey, P.6
  • 2
    • 40349100607 scopus 로고    scopus 로고
    • Valproic acid sensitizes chronic lymphocytic leukemia cells to apoptosis and restores the balance between pro- and antiapoptotic proteins
    • Bokelmann I., and Mahlknecht U. Valproic acid sensitizes chronic lymphocytic leukemia cells to apoptosis and restores the balance between pro- and antiapoptotic proteins. Mol Med 14 1-2 (2008) 20-27
    • (2008) Mol Med , vol.14 , Issue.1-2 , pp. 20-27
    • Bokelmann, I.1    Mahlknecht, U.2
  • 3
    • 34748878324 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors selectively suppress expression of HDAC7
    • Dokmanovic M., Perez G., Xu W., Ngo L., Clarke C., Parmigiani R.B., et al. Histone deacetylase inhibitors selectively suppress expression of HDAC7. Mol Cancer Ther 6 9 (2007) 2525-2534
    • (2007) Mol Cancer Ther , vol.6 , Issue.9 , pp. 2525-2534
    • Dokmanovic, M.1    Perez, G.2    Xu, W.3    Ngo, L.4    Clarke, C.5    Parmigiani, R.B.6
  • 4
    • 0032433144 scopus 로고    scopus 로고
    • Role of histone deacetylases in acute leukemia.
    • Fenrick R., and Hiebert S.W. Role of histone deacetylases in acute leukemia. J Cell Biochem Suppl 30-31 (1998) 194-202
    • (1998) J Cell Biochem Suppl , vol.30-31 , pp. 194-202
    • Fenrick, R.1    Hiebert, S.W.2
  • 5
    • 0033539092 scopus 로고    scopus 로고
    • Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
    • Finnin M.S., Donigian J.R., Cohen A., Richon V.M., Rifkind R.A., Marks P.A., et al. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401 6749 (1999) 188-193
    • (1999) Nature , vol.401 , Issue.6749 , pp. 188-193
    • Finnin, M.S.1    Donigian, J.R.2    Cohen, A.3    Richon, V.M.4    Rifkind, R.A.5    Marks, P.A.6
  • 7
    • 0042905956 scopus 로고    scopus 로고
    • Gene expression profiling of multiple histone deacetylase (HDAC) inhibitors: defining a common gene set produced by HDAC inhibition in T24 and MDA carcinoma cell lines
    • Glaser K.B., Staver M.J., Waring J.F., Stender J., Ulrich R.G., and Davidsen S.K. Gene expression profiling of multiple histone deacetylase (HDAC) inhibitors: defining a common gene set produced by HDAC inhibition in T24 and MDA carcinoma cell lines. Mol Cancer Ther 2 (2003) 151-163
    • (2003) Mol Cancer Ther , vol.2 , pp. 151-163
    • Glaser, K.B.1    Staver, M.J.2    Waring, J.F.3    Stender, J.4    Ulrich, R.G.5    Davidsen, S.K.6
  • 8
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • Glozak M.A., Sengupta N., Zhang X., and Seto E. Acetylation and deacetylation of non-histone proteins. Gene 363 (2005) 15-23
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1    Sengupta, N.2    Zhang, X.3    Seto, E.4
  • 9
    • 18244383806 scopus 로고    scopus 로고
    • Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells
    • Gottlicher M., Minucci S., Zhu P., Kramer O.H., Schimpf A., Giavara S., et al. Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells. EMBO J 20 24 (2001) 6969-6978
    • (2001) EMBO J , vol.20 , Issue.24 , pp. 6969-6978
    • Gottlicher, M.1    Minucci, S.2    Zhu, P.3    Kramer, O.H.4    Schimpf, A.5    Giavara, S.6
  • 10
    • 47749109128 scopus 로고    scopus 로고
    • Expression-based screening identifies the combination of histone deacetylase inhibitors and retinoids for neuroblastoma differentiation
    • Hahn C.K., Ross K.N., Warrington I.M., Mazitschek R., Kanegai C.M., Wright R.D., et al. Expression-based screening identifies the combination of histone deacetylase inhibitors and retinoids for neuroblastoma differentiation. Proc Natl Acad Sci USA 105 28 (2008) 9751-9756
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.28 , pp. 9751-9756
    • Hahn, C.K.1    Ross, K.N.2    Warrington, I.M.3    Mazitschek, R.4    Kanegai, C.M.5    Wright, R.D.6
  • 11
    • 34547911052 scopus 로고    scopus 로고
    • Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design
    • Hodawadekar S.C., and Marmorstein R. Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design. Oncogene 26 37 (2007) 5528-5540
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5528-5540
    • Hodawadekar, S.C.1    Marmorstein, R.2
  • 12
    • 13944274571 scopus 로고    scopus 로고
    • Histone deacetylase inhibition down-regulates cyclin D1 transcription by inhibiting nuclear factor-kappaB/p65 DNA binding
    • Hu J., and Colburn N.H. Histone deacetylase inhibition down-regulates cyclin D1 transcription by inhibiting nuclear factor-kappaB/p65 DNA binding. Mol Cancer Res 3 2 (2005) 100-109
    • (2005) Mol Cancer Res , vol.3 , Issue.2 , pp. 100-109
    • Hu, J.1    Colburn, N.H.2
  • 13
    • 40949162039 scopus 로고    scopus 로고
    • Modulation of cell cycles and apoptosis by apicidin in estrogen receptor (ER)-positive and-negative human breast cancer cells
    • Im J.Y., Park H., Kang K.W., Choi W.S., and Kim H.S. Modulation of cell cycles and apoptosis by apicidin in estrogen receptor (ER)-positive and-negative human breast cancer cells. Chem Biol Interact 172 3 (2008) 235-244
    • (2008) Chem Biol Interact , vol.172 , Issue.3 , pp. 235-244
    • Im, J.Y.1    Park, H.2    Kang, K.W.3    Choi, W.S.4    Kim, H.S.5
  • 14
    • 4344685827 scopus 로고    scopus 로고
    • Expression profiling of sodium butyrate (NaB)-treated cells: identification of regulation of genes related to cytokine signaling and cancer metastasis by NaB
    • Joseph J., Mudduluru G., Antony S., Vashistha S., Ajitkumar P., and Somasundaram K. Expression profiling of sodium butyrate (NaB)-treated cells: identification of regulation of genes related to cytokine signaling and cancer metastasis by NaB. Oncogene 23 37 (2004) 6304-6315
    • (2004) Oncogene , vol.23 , Issue.37 , pp. 6304-6315
    • Joseph, J.1    Mudduluru, G.2    Antony, S.3    Vashistha, S.4    Ajitkumar, P.5    Somasundaram, K.6
  • 15
    • 21244464349 scopus 로고    scopus 로고
    • Phase I study of an oral histone deacetylase inhibitor, suberoylanilide hydroxamic acid, in patients with advanced cancer
    • Kelly W.K., O'Connor O.A., Krug L.M., Chiao J.H., Heaney M., Curley T., et al. Phase I study of an oral histone deacetylase inhibitor, suberoylanilide hydroxamic acid, in patients with advanced cancer. J Clin Oncol 23 17 (2005) 3923-3931
    • (2005) J Clin Oncol , vol.23 , Issue.17 , pp. 3923-3931
    • Kelly, W.K.1    O'Connor, O.A.2    Krug, L.M.3    Chiao, J.H.4    Heaney, M.5    Curley, T.6
  • 16
    • 0033561497 scopus 로고    scopus 로고
    • Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase
    • Kim Y.B., Lee K.H., Sugita K., Yoshida M., and Horinouchi S. Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase. Oncogene 18 15 (1999) 2461-2470
    • (1999) Oncogene , vol.18 , Issue.15 , pp. 2461-2470
    • Kim, Y.B.1    Lee, K.H.2    Sugita, K.3    Yoshida, M.4    Horinouchi, S.5
  • 17
    • 34247850849 scopus 로고    scopus 로고
    • Regulation of the HIF-1alpha stability by histone deacetylases
    • Kim S.H., Jeong J.W., Park J.A., Lee J.W., Seo J.H., Jung B.K., et al. Regulation of the HIF-1alpha stability by histone deacetylases. Oncol Rep 17 3 (2007) 647-651
    • (2007) Oncol Rep , vol.17 , Issue.3 , pp. 647-651
    • Kim, S.H.1    Jeong, J.W.2    Park, J.A.3    Lee, J.W.4    Seo, J.H.5    Jung, B.K.6
  • 18
    • 33644875208 scopus 로고    scopus 로고
    • SAHA, a HDAC inhibitor, has profound anti-growth activity against non-small cell lung cancer cells
    • Komatsu N., Kawamata N., Takeuchi S., Yin D., Chien W., Miller C.W., et al. SAHA, a HDAC inhibitor, has profound anti-growth activity against non-small cell lung cancer cells. Oncol Rep 15 1 (2006) 187-191
    • (2006) Oncol Rep , vol.15 , Issue.1 , pp. 187-191
    • Komatsu, N.1    Kawamata, N.2    Takeuchi, S.3    Yin, D.4    Chien, W.5    Miller, C.W.6
  • 19
    • 0037925520 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor valproic acid selectively induces proteasomal degradation of HDAC2
    • Kramer O.H., Zhu P., Ostendorff H.P., Golebiewski M., Tiefenbach J., Peters M.A., et al. The histone deacetylase inhibitor valproic acid selectively induces proteasomal degradation of HDAC2. EMBO J 22 13 (2003) 3411-3420
    • (2003) EMBO J , vol.22 , Issue.13 , pp. 3411-3420
    • Kramer, O.H.1    Zhu, P.2    Ostendorff, H.P.3    Golebiewski, M.4    Tiefenbach, J.5    Peters, M.A.6
  • 20
    • 43249104204 scopus 로고    scopus 로고
    • Mechanism for ubiquitylation of the leukemia fusion proteins AML1-ETO and PML-RARalpha
    • Kramer O.H., Muller S., Buchwald M., Reichardt S., and Heinzel T. Mechanism for ubiquitylation of the leukemia fusion proteins AML1-ETO and PML-RARalpha. FASEB J 22 5 (2008) 1369-1379
    • (2008) FASEB J , vol.22 , Issue.5 , pp. 1369-1379
    • Kramer, O.H.1    Muller, S.2    Buchwald, M.3    Reichardt, S.4    Heinzel, T.5
  • 21
    • 34250810709 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor, suberoylanilide hydroxamic acid (Vorinostat SAHA) profoundly inhibits the growth of human pancreatic cancer cells
    • Kumagai T., Wakimoto N., Yin D., Gery S., Kawamata N., Takai N., et al. Histone deacetylase inhibitor, suberoylanilide hydroxamic acid (Vorinostat SAHA) profoundly inhibits the growth of human pancreatic cancer cells. Int J Cancer 121 3 (2007) 656-665
    • (2007) Int J Cancer , vol.121 , Issue.3 , pp. 656-665
    • Kumagai, T.1    Wakimoto, N.2    Yin, D.3    Gery, S.4    Kawamata, N.5    Takai, N.6
  • 23
    • 42049088710 scopus 로고    scopus 로고
    • Statins increase p21 through inhibition of histone deacetylase activity and release of promoter-associated HDAC1/2
    • Lin Y.C., Lin J.H., Chou C.W., Chang Y.F., Yeh S.H., and Chen C.C. Statins increase p21 through inhibition of histone deacetylase activity and release of promoter-associated HDAC1/2. Cancer Res 68 7 (2008) 2375-2383
    • (2008) Cancer Res , vol.68 , Issue.7 , pp. 2375-2383
    • Lin, Y.C.1    Lin, J.H.2    Chou, C.W.3    Chang, Y.F.4    Yeh, S.H.5    Chen, C.C.6
  • 24
    • 34249941680 scopus 로고    scopus 로고
    • Analysis of the apoptotic and therapeutic activities of histone deacetylase inhibitors by using a mouse model of B cell lymphoma
    • Lindemann R.K., Newbold A., Whitecross K.F., Cluse L.A., Frew A.J., Ellis L., et al. Analysis of the apoptotic and therapeutic activities of histone deacetylase inhibitors by using a mouse model of B cell lymphoma. Proc Natl Acad Sci USA 104 19 (2007) 8071-8076
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.19 , pp. 8071-8076
    • Lindemann, R.K.1    Newbold, A.2    Whitecross, K.F.3    Cluse, L.A.4    Frew, A.J.5    Ellis, L.6
  • 25
    • 36148950997 scopus 로고    scopus 로고
    • FDA approval summary: vorinostat for treatment of advanced primary cutaneous T-cell lymphoma
    • Mann B.S., Johnson J.R., Cohen M.H., Justice R., and Pazdur R. FDA approval summary: vorinostat for treatment of advanced primary cutaneous T-cell lymphoma. Oncologist 12 10 (2007) 1247-1252
    • (2007) Oncologist , vol.12 , Issue.10 , pp. 1247-1252
    • Mann, B.S.1    Johnson, J.R.2    Cohen, M.H.3    Justice, R.4    Pazdur, R.5
  • 26
    • 33847258674 scopus 로고    scopus 로고
    • Discovery and development of SAHA as an anticancer agent
    • Marks P.A. Discovery and development of SAHA as an anticancer agent. Oncogene 26 9 (2007) 1351-1356
    • (2007) Oncogene , vol.26 , Issue.9 , pp. 1351-1356
    • Marks, P.A.1
  • 28
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci S., and Pelicci P.G. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 6 (2006) 38-51
    • (2006) Nat Rev Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 29
    • 27644586649 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors radiosensitize human melanoma cells by suppressing DNA repair activity
    • Munshi A., Kurland J.F., Nishikawa T., Tanaka T., Hobbs M.L., Tucker S.L., et al. Histone deacetylase inhibitors radiosensitize human melanoma cells by suppressing DNA repair activity. Clin Cancer Res 11 13 (2005) 4912-4922
    • (2005) Clin Cancer Res , vol.11 , Issue.13 , pp. 4912-4922
    • Munshi, A.1    Kurland, J.F.2    Nishikawa, T.3    Tanaka, T.4    Hobbs, M.L.5    Tucker, S.L.6
  • 30
    • 14844353574 scopus 로고    scopus 로고
    • Identification and functional significance of genes regulated by structurally different histone deacetylase inhibitors
    • Peart M.J., Smyth G.K., van Laar R.K., Bowtell D.D., Richon V.M., Marks P.A., et al. Identification and functional significance of genes regulated by structurally different histone deacetylase inhibitors. Proc Natl Acad Sci USA 102 10 (2005) 3697-3702
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.10 , pp. 3697-3702
    • Peart, M.J.1    Smyth, G.K.2    van Laar, R.K.3    Bowtell, D.D.4    Richon, V.M.5    Marks, P.A.6
  • 31
    • 40849151859 scopus 로고    scopus 로고
    • Effects of FR235222, a novel HDAC inhibitor, in proliferation and apoptosis of human leukaemia cell lines: role of annexin A1
    • Petrella A., D'Acunto C.W., Rodriquez M., Festa M., Tosco A., Bruno I., et al. Effects of FR235222, a novel HDAC inhibitor, in proliferation and apoptosis of human leukaemia cell lines: role of annexin A1. Eur J Cancer 44 5 (2008) 740-749
    • (2008) Eur J Cancer , vol.44 , Issue.5 , pp. 740-749
    • Petrella, A.1    D'Acunto, C.W.2    Rodriquez, M.3    Festa, M.4    Tosco, A.5    Bruno, I.6
  • 32
    • 33749006252 scopus 로고    scopus 로고
    • Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1 alpha
    • Qian D.Z., Kachhap S.K., Collis S.J., Verheul H.M., Carducci M.A., Atadja P., et al. Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1 alpha. Cancer Res 66 17 (2006) 8814-8821
    • (2006) Cancer Res , vol.66 , Issue.17 , pp. 8814-8821
    • Qian, D.Z.1    Kachhap, S.K.2    Collis, S.J.3    Verheul, H.M.4    Carducci, M.A.5    Atadja, P.6
  • 33
    • 33744510851 scopus 로고    scopus 로고
    • HDAC1 acetylation is linked to progressive modulation of steroid receptor-induced gene transcription
    • Qiu Y., Zhao Y., Becker M., John S., Parekh B.S., Huang S., et al. HDAC1 acetylation is linked to progressive modulation of steroid receptor-induced gene transcription. Mol Cell 22 5 (2006) 669-679
    • (2006) Mol Cell , vol.22 , Issue.5 , pp. 669-679
    • Qiu, Y.1    Zhao, Y.2    Becker, M.3    John, S.4    Parekh, B.S.5    Huang, S.6
  • 34
    • 23744495968 scopus 로고    scopus 로고
    • Multiple mechanisms induce transcriptional silencing of a subset of genes, including oestrogen receptor alpha, in response to deacetylase inhibition by valproic acid and trichostatin A
    • Reid G., Metivier R., Lin C.Y., Denger S., Ibberson D., Ivacevic T., et al. Multiple mechanisms induce transcriptional silencing of a subset of genes, including oestrogen receptor alpha, in response to deacetylase inhibition by valproic acid and trichostatin A. Oncogene 24 (2005) 4894-4907
    • (2005) Oncogene , vol.24 , pp. 4894-4907
    • Reid, G.1    Metivier, R.2    Lin, C.Y.3    Denger, S.4    Ibberson, D.5    Ivacevic, T.6
  • 35
    • 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., and Marks P.A. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc Natl Acad Sci USA 97 18 (2000) 10014-10019
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.18 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 36
    • 33646354640 scopus 로고    scopus 로고
    • A truncating mutation of HDAC2 in human cancers confers resistance to histone deacetylase inhibition
    • Ropero S., Fraga M.F., Ballestar E., Hamelin R., Yamamoto H., Boix-Chornet M., et al. A truncating mutation of HDAC2 in human cancers confers resistance to histone deacetylase inhibition. Nat Genet 38 (2006) 566-569
    • (2006) Nat Genet , vol.38 , pp. 566-569
    • Ropero, S.1    Fraga, M.F.2    Ballestar, E.3    Hamelin, R.4    Yamamoto, H.5    Boix-Chornet, M.6
  • 37
    • 45549095066 scopus 로고    scopus 로고
    • Human HDAC7 Harbors a Class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity
    • Schuetz A., Min J., Allali-Hassani A., Schapira M., Shuen M., Loppnau P., et al. Human HDAC7 Harbors a Class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity. J Biol Chem 283 17 (2008) 11355-11363
    • (2008) J Biol Chem , vol.283 , Issue.17 , pp. 11355-11363
    • Schuetz, A.1    Min, J.2    Allali-Hassani, A.3    Schapira, M.4    Shuen, M.5    Loppnau, P.6
  • 38
    • 32944462300 scopus 로고    scopus 로고
    • Rapid alteration of microRNA levels by histone deacetylase inhibition
    • Scott G.K., Mattie M.D., Berger C.E., Benz S.C., and Benz C.C. Rapid alteration of microRNA levels by histone deacetylase inhibition. Cancer Res 66 3 (2006) 1277-1281
    • (2006) Cancer Res , vol.66 , Issue.3 , pp. 1277-1281
    • Scott, G.K.1    Mattie, M.D.2    Berger, C.E.3    Benz, S.C.4    Benz, C.C.5
  • 39
    • 38849088190 scopus 로고    scopus 로고
    • Competitive inhibition of histone deacetylase activity by trichostatin A and butyrate
    • Sekhavat A., Sun J.M., and Davie J.R. Competitive inhibition of histone deacetylase activity by trichostatin A and butyrate. Biochem Cell Biol 85 6 (2007) 751-758
    • (2007) Biochem Cell Biol , vol.85 , Issue.6 , pp. 751-758
    • Sekhavat, A.1    Sun, J.M.2    Davie, J.R.3
  • 40
    • 6344222799 scopus 로고    scopus 로고
    • Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor
    • Vannini A., Volpari C., Filocamo G., Casavola E.C., Brunetti M., Renzoni D., et al. Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor. Proc Natl Acad Sci USA 101 42 (2004) 15064-15069
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.42 , pp. 15064-15069
    • Vannini, A.1    Volpari, C.2    Filocamo, G.3    Casavola, E.C.4    Brunetti, M.5    Renzoni, D.6
  • 42
    • 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., et al. 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 18 50 (1999) 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
  • 43
    • 3643104150 scopus 로고    scopus 로고
    • Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase
    • Warrell Jr. R.P., He L.Z., Richon V., Calleja E., and Pandolfi P.P. Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase. J Natl Cancer Inst 90 21 (1998) 1621-1625
    • (1998) J Natl Cancer Inst , vol.90 , Issue.21 , pp. 1621-1625
    • Warrell Jr., R.P.1    He, L.Z.2    Richon, V.3    Calleja, E.4    Pandolfi, P.P.5
  • 44
    • 43249092663 scopus 로고    scopus 로고
    • HDAC inhibitor depsipeptide activates silenced genes through decreasing both CpG and H3K9 methylation on the promoter
    • Wu L.P., Wang X., Li L., Zhao Y., Lu S., Yu Y., et al. HDAC inhibitor depsipeptide activates silenced genes through decreasing both CpG and H3K9 methylation on the promoter. Mol Cell Biol (2008)
    • (2008) Mol Cell Biol
    • Wu, L.P.1    Wang, X.2    Li, L.3    Zhao, Y.4    Lu, S.5    Yu, Y.6
  • 45
    • 16844370410 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors decrease DNA methyltransferase-3B messenger RNA stability and down-regulate de novo DNA methyltransferase activity in human endometrial cells
    • Xiong Y., Dowdy S.C., Podratz K.C., Jin F., Attewell J.R., Eberhardt N.L., et al. Histone deacetylase inhibitors decrease DNA methyltransferase-3B messenger RNA stability and down-regulate de novo DNA methyltransferase activity in human endometrial cells. Cancer Res 65 7 (2005) 2684-2689
    • (2005) Cancer Res , vol.65 , Issue.7 , pp. 2684-2689
    • Xiong, Y.1    Dowdy, S.C.2    Podratz, K.C.3    Jin, F.4    Attewell, J.R.5    Eberhardt, N.L.6
  • 46
    • 39849091786 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor apicidin downregulates DNA methyltransferase 1 expression and induces repressive histone modifications via recruitment of corepressor complex to promoter region in human cervix cancer cells
    • You J.S., Kang J.K., Lee E.K., Lee J.C., Lee S.H., Jeon Y.J., et al. Histone deacetylase inhibitor apicidin downregulates DNA methyltransferase 1 expression and induces repressive histone modifications via recruitment of corepressor complex to promoter region in human cervix cancer cells. Oncogene 27 10 (2008) 1376-1386
    • (2008) Oncogene , vol.27 , Issue.10 , pp. 1376-1386
    • You, J.S.1    Kang, J.K.2    Lee, E.K.3    Lee, J.C.4    Lee, S.H.5    Jeon, Y.J.6
  • 47
    • 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., and Yu Q. Inhibitors of histone deacetylases target the Rb-E2F1 pathway for apoptosis induction through activation of proapoptotic protein Bim. Proc Natl Acad Sci USA 102 44 (2005) 16090-16095
    • (2005) Proc Natl Acad Sci USA , 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
  • 48
    • 33645230001 scopus 로고    scopus 로고
    • Acetylation of p53 at lysine 373/382 by the histone deacetylase inhibitor depsipeptide induces expression of p21(Waf1/Cip1)
    • Zhao Y., Lu S., Wu L., Chai G., Wang H., Chen Y., et al. Acetylation of p53 at lysine 373/382 by the histone deacetylase inhibitor depsipeptide induces expression of p21(Waf1/Cip1). Mol Cell Biol 26 7 (2006) 2782-2790
    • (2006) Mol Cell Biol , vol.26 , Issue.7 , pp. 2782-2790
    • Zhao, Y.1    Lu, S.2    Wu, L.3    Chai, G.4    Wang, H.5    Chen, Y.6
  • 49
    • 51049117752 scopus 로고    scopus 로고
    • Inhibition of histone deacetylases promotes ubiquitin-dependent proteasomal degradation of DNA methyltransferase 1 in human breast cancer cells
    • Zhou Q., Agoston A.T., Atadja P., Nelson W.G., and Davidson N.E. Inhibition of histone deacetylases promotes ubiquitin-dependent proteasomal degradation of DNA methyltransferase 1 in human breast cancer cells. Mol Cancer Res 6 5 (2008) 873-883
    • (2008) Mol Cancer Res , vol.6 , Issue.5 , pp. 873-883
    • Zhou, Q.1    Agoston, A.T.2    Atadja, P.3    Nelson, W.G.4    Davidson, N.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.