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Volumn 66, Issue 13, 2006, Pages 6785-6792

Inhibition of histone deacetylase class I but not class II is critical for the sensitization of leukemic cells to tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEAACETYLASE 8 ENZYME; HISTONE DEACETYLASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 3; HISTONE DEACETYLASE 6 ENZYME; HISTONE DEACETYLASE INHIBITOR; MC 1568; MC 1575; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; SB 379278 A; SB 556629; SMALL INTERFERING RNA; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UNCLASSIFIED DRUG; VALPROIC ACID;

EID: 33746144518     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-4563     Document Type: Article
Times cited : (127)

References (50)
  • 1
    • 0036598992 scopus 로고    scopus 로고
    • Targeting death and decoy receptors of the tumour-necrosis factor superfamily
    • Ashkenazi A. Targeting death and decoy receptors of the tumour-necrosis factor superfamily. Nat Rev Cancer 2002;2:420-30.
    • (2002) Nat Rev Cancer , vol.2 , pp. 420-430
    • Ashkenazi, A.1
  • 2
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel FC, Hellbardt S, Behrmann I, et al. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J 1995;14:5579-88.
    • (1995) EMBO J , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3
  • 3
    • 0033790715 scopus 로고    scopus 로고
    • TRAIL receptor-2 signals apoptosis through FADD and caspase-8
    • Bodmer JL, Holler N, Reynard S, et al. TRAIL receptor-2 signals apoptosis through FADD and caspase-8. Nat Cell Biol 2000;2:241-3.
    • (2000) Nat Cell Biol , vol.2 , pp. 241-243
    • Bodmer, J.L.1    Holler, N.2    Reynard, S.3
  • 4
    • 0033667778 scopus 로고    scopus 로고
    • FADD/MORT1 and caspase-8 are recruited to TRAIL receptors 1 and 2 and are essential for apoptosis mediated by TRAIL receptor 2
    • Sprick MR, Weigand MA, Rieser E, et al. FADD/MORT1 and caspase-8 are recruited to TRAIL receptors 1 and 2 and are essential for apoptosis mediated by TRAIL receptor 2. Immunity 2000;12:599-609.
    • (2000) Immunity , vol.12 , pp. 599-609
    • Sprick, M.R.1    Weigand, M.A.2    Rieser, E.3
  • 5
    • 0036141029 scopus 로고    scopus 로고
    • TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO
    • Deng Y, Lin Y, Wu X. TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO. Genes Dev 2002;16:33-45.
    • (2002) Genes Dev , vol.16 , pp. 33-45
    • Deng, Y.1    Lin, Y.2    Wu, X.3
  • 6
    • 0037376788 scopus 로고    scopus 로고
    • Cell surface death receptor signaling in normal and cancer cells
    • Ozoren N, El-Deiry WS. Cell surface death receptor signaling in normal and cancer cells. Semin Cancer Biol 2003;13:135-47.
    • (2003) Semin Cancer Biol , vol.13 , pp. 135-147
    • Ozoren, N.1    El-Deiry, W.S.2
  • 7
    • 0035755974 scopus 로고    scopus 로고
    • Histone deacetylases and cancer: Causes and therapies
    • Marks P, Rifkind RA, Richon VM, et al. Histone deacetylases and cancer: causes and therapies. Nat Rev Cancer 2001;1:194-202.
    • (2001) Nat Rev Cancer , vol.1 , pp. 194-202
    • Marks, P.1    Rifkind, R.A.2    Richon, V.M.3
  • 8
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • Johnstone RW. Histone-deacetylase inhibitors: novel drugs for the treatment of cancer. Nat Rev Drug Discov 2002;1:287-99.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 10
    • 16844362441 scopus 로고    scopus 로고
    • Histone deacetylation in epigenetics: An attractive target for anticancer therapy
    • Mai A, Massa S, Rotili D, et al. Histone deacetylation in epigenetics: an attractive target for anticancer therapy. Med Res Rev 2005;25:261-309.
    • (2005) Med Res Rev , vol.25 , pp. 261-309
    • Mai, A.1    Massa, S.2    Rotili, D.3
  • 12
    • 23644434852 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Insights into mechanisms of lethality
    • Rosato RR, Grant S. Histone deacetylase inhibitors: insights into mechanisms of lethality. Expert Opin Ther Targets 2005;9:809-24.
    • (2005) Expert Opin Ther Targets , vol.9 , pp. 809-824
    • Rosato, R.R.1    Grant, S.2
  • 13
    • 0141526319 scopus 로고    scopus 로고
    • Differential regulation of the Sir2 histone deacetylase gene family by inhibitors of class I and II histone deacetylases
    • Kyrylenko S, Kyrylenko O, Suuronen T, Salminen A. Differential regulation of the Sir2 histone deacetylase gene family by inhibitors of class I and II histone deacetylases. Cell Mol Life Sci 2003;60:1990-7.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1990-1997
    • Kyrylenko, S.1    Kyrylenko, O.2    Suuronen, T.3    Salminen, A.4
  • 14
    • 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 AA, Ausserlechner MJ, Bernhard D, et al. 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;98:10833-8.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 10833-10838
    • Ruefli, A.A.1    Ausserlechner, M.J.2    Bernhard, D.3
  • 15
    • 0038485588 scopus 로고    scopus 로고
    • Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA)
    • Henderson C, Mizzau M, Paroni G, et al. Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA). J Biol Chem 2003;278:12579-89.
    • (2003) J Biol Chem , vol.278 , pp. 12579-12589
    • Henderson, C.1    Mizzau, M.2    Paroni, G.3
  • 16
    • 0036584375 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors sensitize human colonic adenocarcinoma cell lines to TNF-related apoptosis inducing ligand-mediated apoptosis
    • Inoue H, Shiraki K, Ohmori S, et al. Histone deacetylase inhibitors sensitize human colonic adenocarcinoma cell lines to TNF-related apoptosis inducing ligand-mediated apoptosis. Int J Mol Med 2002;9:521-5.
    • (2002) Int J Mol Med , vol.9 , pp. 521-525
    • Inoue, H.1    Shiraki, K.2    Ohmori, S.3
  • 17
    • 2942584501 scopus 로고    scopus 로고
    • Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells
    • Rosato RR, Almenara JA, Dai Y, Grant S. Simultaneous activation of the intrinsic and extrinsic pathways by histone deacetylase (HDAC) inhibitors and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) synergistically induces mitochondrial damage and apoptosis in human leukemia cells. Mol Cancer Ther 2003;2:1273-84.
    • (2003) Mol Cancer Ther , vol.2 , pp. 1273-1284
    • Rosato, R.R.1    Almenara, J.A.2    Dai, Y.3    Grant, S.4
  • 18
    • 0346725822 scopus 로고    scopus 로고
    • Sensitization of mesothelioma to TRAIL apoptosis by inhibition of histone deacetylase: Role of Bcl-xL down-regulation
    • Neuzil J, Swettenham E, Gellert N. Sensitization of mesothelioma to TRAIL apoptosis by inhibition of histone deacetylase: role of Bcl-xL down-regulation. Biochem Biophys Res Commun 2004;314:186-91.
    • (2004) Biochem Biophys Res Commun , vol.314 , pp. 186-191
    • Neuzil, J.1    Swettenham, E.2    Gellert, N.3
  • 19
    • 0033199896 scopus 로고    scopus 로고
    • Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/CD95 ligand expression in human neuroblastoma
    • Glick RD, Swendeman SL, Coffey DC, et al. Hybrid polar histone deacetylase inhibitor induces apoptosis and CD95/CD95 ligand expression in human neuroblastoma. Cancer Res 1999;59:4392-9.
    • (1999) Cancer Res , vol.59 , pp. 4392-4399
    • Glick, R.D.1    Swendeman, S.L.2    Coffey, D.C.3
  • 20
    • 0035437171 scopus 로고    scopus 로고
    • TRAIL/Apo2L ligand selectively induces apoptosis and overcomes drug resistance in multiple myeloma: Therapeutic applications
    • Mitsiades CS, Treon SP, Mitsiades N, et al. TRAIL/Apo2L ligand selectively induces apoptosis and overcomes drug resistance in multiple myeloma: therapeutic applications. Blood 2001;98:795-804.
    • (2001) Blood , vol.98 , pp. 795-804
    • Mitsiades, C.S.1    Treon, S.P.2    Mitsiades, N.3
  • 21
    • 13444306459 scopus 로고    scopus 로고
    • Tumor-selective action of HDAC inhibitors involves TRAIL induction in acute myeloid leukemia cells
    • Nebbioso A, Clarke N, Voltz E, et al. Tumor-selective action of HDAC inhibitors involves TRAIL induction in acute myeloid leukemia cells. Nat Med 2005;11:77-84.
    • (2005) Nat Med , vol.11 , pp. 77-84
    • Nebbioso, A.1    Clarke, N.2    Voltz, E.3
  • 22
    • 14844345670 scopus 로고    scopus 로고
    • Depsipeptide (FR901228) enhances the cytotoxic activity of TRAIL by redistributing TRAIL receptor to membrane lipid rafts
    • VanOosten RL, Moore JM, Ludwig AT, Griffith TS. Depsipeptide (FR901228) enhances the cytotoxic activity of TRAIL by redistributing TRAIL receptor to membrane lipid rafts. Mol Ther 2005;11:542-52.
    • (2005) Mol Ther , vol.11 , pp. 542-552
    • Vanoosten, R.L.1    Moore, J.M.2    Ludwig, A.T.3    Griffith, T.S.4
  • 23
    • 0037015675 scopus 로고    scopus 로고
    • Mechanisms of resistance to TRAIL-induced apoptosis in primary B cell chronic lymphocytic leukaemia
    • MacFarlane M, Harper N, Snowden RT, et al. Mechanisms of resistance to TRAIL-induced apoptosis in primary B cell chronic lymphocytic leukaemia. Oncogene 2002;21:6809-18.
    • (2002) Oncogene , vol.21 , pp. 6809-6818
    • MacFarlane, M.1    Harper, N.2    Snowden, R.T.3
  • 24
    • 12744261484 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors potentiate TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in lymphoid malignancies
    • Inoue S, MacFarlane M, Harper N, et al. Histone deacetylase inhibitors potentiate TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in lymphoid malignancies. Cell Death Differ 2004;11 Suppl 2: S193-206.
    • (2004) Cell Death Differ , vol.11 , Issue.SUPPL. 2
    • Inoue, S.1    MacFarlane, M.2    Harper, N.3
  • 25
    • 11144358387 scopus 로고    scopus 로고
    • Cotreatment with histone deacetylase inhibitor LAQ824 enhances Apo-2L/tumor necrosis factor-related apoptosis inducing ligand-induced death inducing signaling complex activity and apoptosis of human acute leukemia cells
    • Guo F, Sigua C, Tao J, et al. Cotreatment with histone deacetylase inhibitor LAQ824 enhances Apo-2L/tumor necrosis factor-related apoptosis inducing ligand-induced death inducing signaling complex activity and apoptosis of human acute leukemia cells. Cancer Res 2004;64:2580-9.
    • (2004) Cancer Res , vol.64 , pp. 2580-2589
    • Guo, F.1    Sigua, C.2    Tao, J.3
  • 26
    • 21744448694 scopus 로고    scopus 로고
    • Chronic lymphocytic leukemic cells exhibit apoptotic signaling via TRAIL-R1
    • MacFarlane M, Inoue S, Kohlhaas SL, et al. Chronic lymphocytic leukemic cells exhibit apoptotic signaling via TRAIL-R1. Cell Death Differ 2005;12:773-82.
    • (2005) Cell Death Differ , vol.12 , pp. 773-782
    • MacFarlane, M.1    Inoue, S.2    Kohlhaas, S.L.3
  • 27
    • 29244483111 scopus 로고    scopus 로고
    • TRAIL Receptor-selective mutants signal to apoptosis via TRAIL-R1 in primary lymphoid malignancies
    • MacFarlane M, Kohlhaas SL, Sutcliffe MJ, Dyer MJ, Cohen GM. TRAIL Receptor-selective mutants signal to apoptosis via TRAIL-R1 in primary lymphoid malignancies. Cancer Res 2005;65:11265-70.
    • (2005) Cancer Res , vol.65 , pp. 11265-11270
    • MacFarlane, M.1    Kohlhaas, S.L.2    Sutcliffe, M.J.3    Dyer, M.J.4    Cohen, G.M.5
  • 28
    • 0030770614 scopus 로고    scopus 로고
    • Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL
    • MacFarlane M, Ahmad M, Srinivasula SM, et al. Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL. J Biol Chem 1997;272:25417-20.
    • (1997) J Biol Chem , vol.272 , pp. 25417-25420
    • MacFarlane, M.1    Ahmad, M.2    Srinivasula, S.M.3
  • 29
    • 0035361402 scopus 로고    scopus 로고
    • Cyclic hydroxamic-acid-containing peptide 31, a potent synthetic histone deacetylase inhibitor with antitumor activity
    • Komatsu Y, Tomizaki KY, Tsukamoto M, et al. Cyclic hydroxamic-acid- containing peptide 31, a potent synthetic histone deacetylase inhibitor with antitumor activity. Cancer Res 2001;61:4459-66.
    • (2001) Cancer Res , vol.61 , pp. 4459-4466
    • Komatsu, Y.1    Tomizaki, K.Y.2    Tsukamoto, M.3
  • 30
    • 0242362600 scopus 로고    scopus 로고
    • Discovery of (aryloxopropenyl)pyrrolyl hydroxyamides as selective inhibitors of class IIa histone deacetylase homologue HD1-A
    • Mai A, Massa S, Pezzi R, et al. Discovery of (aryloxopropenyl)pyrrolyl hydroxyamides as selective inhibitors of class IIa histone deacetylase homologue HD1-A. J Med Chem 2003;46:4826-9.
    • (2003) J Med Chem , vol.46 , pp. 4826-4829
    • Mai, A.1    Massa, S.2    Pezzi, R.3
  • 31
    • 20944435415 scopus 로고    scopus 로고
    • Class II (IIa)-selective histone deacetylase inhibitors. 1. Synthesis and biological evaluation of novel (aryloxopropenyl)pyrrolyl hydroxyamides
    • Mai A, Massa S, Pezzi R, et al. Class II (IIa)-selective histone deacetylase inhibitors. 1. Synthesis and biological evaluation of novel (aryloxopropenyl)pyrrolyl hydroxyamides. J Med Chem 2005;48:3344-53.
    • (2005) J Med Chem , vol.48 , pp. 3344-3353
    • Mai, A.1    Massa, S.2    Pezzi, R.3
  • 32
    • 0142179154 scopus 로고    scopus 로고
    • Identification of novel isoform-selective inhibitors within class I histone deacetylases
    • Hu E, Dul E, Sung CM, et al. Identification of novel isoform-selective inhibitors within class I histone deacetylases. J Pharmacol Exp Ther 2003;307:720-8.
    • (2003) J Pharmacol Exp Ther , vol.307 , pp. 720-728
    • Hu, E.1    Dul, E.2    Sung, C.M.3
  • 33
    • 0037815277 scopus 로고    scopus 로고
    • Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor 1 signaling complex during tumor necrosis factor-induced apoptosis
    • Harper N, Hughes M, MacFarlane M, Cohen GM. Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor 1 signaling complex during tumor necrosis factor-induced apoptosis. J Biol Chem 2003;278:25534-41.
    • (2003) J Biol Chem , vol.278 , pp. 25534-25541
    • Harper, N.1    Hughes, M.2    MacFarlane, M.3    Cohen, G.M.4
  • 34
    • 12244295468 scopus 로고    scopus 로고
    • In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation
    • Matsuyama A, Shimazu T, Sumida Y, et al. In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation. EMBO J 2002;21:6820-31.
    • (2002) EMBO J , vol.21 , pp. 6820-6831
    • Matsuyama, A.1    Shimazu, T.2    Sumida, Y.3
  • 35
    • 0037161744 scopus 로고    scopus 로고
    • HDAC6 is a microtubule-associated deacetylase
    • Hubbert C, Guardiola A, Shao R, et al. HDAC6 is a microtubule-associated deacetylase. Nature 2002;417:455-8.
    • (2002) Nature , vol.417 , pp. 455-458
    • Hubbert, C.1    Guardiola, A.2    Shao, R.3
  • 36
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin a and cyclic tetrapeptide antibiotics including trapoxin
    • Furumai R, Komatsu Y, Nishino N, et al. Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc Natl Acad Sci U S A 2001;98:87-92.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3
  • 37
    • 0036735385 scopus 로고    scopus 로고
    • FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases
    • Furumai R, Matsuyama A, Kobashi N, et al. FK228 (depsipeptide) as a natural prodrug that inhibits class I histone deacetylases. Cancer Res 2002;62:4916-21.
    • (2002) Cancer Res , vol.62 , pp. 4916-4921
    • Furumai, R.1    Matsuyama, A.2    Kobashi, N.3
  • 38
    • 0038079767 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor MS-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21CIP1/WAF1 1
    • Rosato RR, Almenara JA, Grant S. The histone deacetylase inhibitor MS-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21CIP1/WAF1 1. Cancer Res 2003;63:3637-45.
    • (2003) Cancer Res , vol.63 , pp. 3637-3645
    • Rosato, R.R.1    Almenara, J.A.2    Grant, S.3
  • 39
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes: Biological functions and the use of small-molecule inhibitors
    • Grozinger CM, Schreiber SL. Deacetylase enzymes: biological functions and the use of small-molecule inhibitors. Chem Biol 2002;9:3-16.
    • (2002) Chem Biol , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 40
    • 0034124166 scopus 로고    scopus 로고
    • A novel histone deacetylase inhibitor identified by high-throughput transcriptional screening of a compound library
    • Su GH, Sohn TA, Ryu B, Kern SE. A novel histone deacetylase inhibitor identified by high-throughput transcriptional screening of a compound library. Cancer Res 2000;60:3137-42.
    • (2000) Cancer Res , vol.60 , pp. 3137-3142
    • Su, G.H.1    Sohn, T.A.2    Ryu, B.3    Kern, S.E.4
  • 41
    • 24944458177 scopus 로고    scopus 로고
    • Activity of selective fully human agonistic antibodies to the TRAIL death receptors TRAIL-R1 and TRAIL-R2 in primary and cultured lymphoma cells: Induction of apoptosis and enhancement of doxorubicin- and bortezomib-induced cell death
    • Georgakis GV, Li Y, Humphreys R, et al. Activity of selective fully human agonistic antibodies to the TRAIL death receptors TRAIL-R1 and TRAIL-R2 in primary and cultured lymphoma cells: induction of apoptosis and enhancement of doxorubicin- and bortezomib-induced cell death. Br J Haematol 2005;130:501-10.
    • (2005) Br J Haematol , vol.130 , pp. 501-510
    • Georgakis, G.V.1    Li, Y.2    Humphreys, R.3
  • 42
    • 0141570564 scopus 로고    scopus 로고
    • Role of class I and class II histone deacetylases in carcinoma cells using siRNA
    • Glaser KB, Li J, Staver MJ, et al. Role of class I and class II histone deacetylases in carcinoma cells using siRNA. Biochem Biophys Res Commun 2003;310:529-36.
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 529-536
    • Glaser, K.B.1    Li, J.2    Staver, M.J.3
  • 43
    • 21144444486 scopus 로고    scopus 로고
    • HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor
    • Kovacs JJ, Murphy PJ, Gaillard S, et al. HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Mol Cell 2005;18:601-17.
    • (2005) Mol Cell , vol.18 , pp. 601-617
    • Kovacs, J.J.1    Murphy, P.J.2    Gaillard, S.3
  • 44
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis of antileukemia activity of histone deacetylase inhibitors
    • Bali P, Pranpat M, Bradner J, et al. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis of antileukemia activity of histone deacetylase inhibitors. J Biol Chem 2005;280:26729-34.
    • (2005) J Biol Chem , vol.280 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3
  • 45
    • 3142689788 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor MS-275 induces caspase-dependent apoptosis in B-cell chronic lymphocytic leukemia cells
    • Lucas DM, Davis ME, Parthun MR, et al. The histone deacetylase inhibitor MS-275 induces caspase-dependent apoptosis in B-cell chronic lymphocytic leukemia cells. Leukemia 2004;18:1207-14.
    • (2004) Leukemia , vol.18 , pp. 1207-1214
    • Lucas, D.M.1    Davis, M.E.2    Parthun, M.R.3
  • 46
    • 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, et al. Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells. EMBO J 2001;20:6969-78.
    • (2001) EMBO J , vol.20 , pp. 6969-6978
    • Gottlicher, M.1    Minucci, S.2    Zhu, P.3
  • 47
    • 28544439923 scopus 로고    scopus 로고
    • On the TRAIL of a new therapy for leukemia
    • Kaufmann SH, Steensma DP. On the TRAIL of a new therapy for leukemia. Leukemia 2005;19:2195-202.
    • (2005) Leukemia , vol.19 , pp. 2195-2202
    • Kaufmann, S.H.1    Steensma, D.P.2
  • 48
    • 0037192790 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-xL inhibit CD95-mediated apoptosis by preventing mitochondrial release of Smac/DIABLO and subsequent inactivation of X-linked inhibitor-of-apoptosis protein
    • Sun XM, Bratton SB, Butterworth M, MacFarlane M, Cohen GM. Bcl-2 and Bcl-xL inhibit CD95-mediated apoptosis by preventing mitochondrial release of Smac/DIABLO and subsequent inactivation of X-linked inhibitor-of-apoptosis protein. J Biol Chem 2002;277:11345-51.
    • (2002) J Biol Chem , vol.277 , pp. 11345-11351
    • Sun, X.M.1    Bratton, S.B.2    Butterworth, M.3    MacFarlane, M.4    Cohen, G.M.5
  • 49
    • 0037273845 scopus 로고    scopus 로고
    • Death receptors leave a caspase footprint that Smacs of XIAP
    • Bratton SB, Cohen GM. Death receptors leave a caspase footprint that Smacs of XIAP. Cell Death Differ 2003;10:4-6.
    • (2003) Cell Death Differ , vol.10 , pp. 4-6
    • Bratton, S.B.1    Cohen, G.M.2
  • 50
    • 2942594784 scopus 로고    scopus 로고
    • Activation of the growth-differentiation factor 11 gene by the histone deacetylase (HDAC) inhibitor trichostatin A and repression by HDAC3
    • Zhang X, Wharton W, Yuan Z, et al. Activation of the growth- differentiation factor 11 gene by the histone deacetylase (HDAC) inhibitor trichostatin A and repression by HDAC3. Mol Cell Biol 2004;24:5106-18.
    • (2004) Mol Cell Biol , vol.24 , pp. 5106-5118
    • Zhang, X.1    Wharton, W.2    Yuan, Z.3


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