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Volumn 128, Issue 1, 2008, Pages 13-21

Targeting protein acetylation for improving cancer therapy

Author keywords

Calreticulin; Histone acetyl transferases; Histone deacetylase inhibitors; Histone deacetylases; Polyphenolic acetates

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; 7 ACETOXY 4 METHYLCOUMARIN; 7,8 DIACETOXY 4 METHYLCOUMARIN; AG 957; ALPHA TUBULIN; ANTINEOPLASTIC AGENT; ARYLBUTYRIC ACID DERIVATIVE; BUTYRIC ACID; CAMPTOTHECIN; CISPLATIN; DNA; DOCETAXEL; DOXORUBICIN; EPOTHILONE B; ETOPOSIDE; FLUOROURACIL; GEMCITABINE; HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE PCAF; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; MYC PROTEIN; QUERCETIN; TRANSCRIPTION FACTOR E2F1; TRANSCRIPTION FACTOR GATA 1; TRASTUZUMAB; TRICHOSTATIN A; UNCLASSIFIED DRUG; UNINDEXED DRUG; VORINOSTAT; WORTMANNIN;

EID: 55849096208     PISSN: 09715916     EISSN: 09715916     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (24)

References (80)
  • 1
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000; 100: 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 25144440127 scopus 로고    scopus 로고
    • Rational development of histone deacetylase inhibitors as anticancer agents
    • Milin RA, Alex S, Jurgen V, William DF. Rational development of histone deacetylase inhibitors as anticancer agents. Mol Pharmacol 2005; 68: 917-32.
    • (2005) Mol Pharmacol , vol.68 , pp. 917-932
    • Milin, R.A.1    Alex, S.2    Jurgen, V.3    William, D.F.4
  • 3
    • 1642358490 scopus 로고    scopus 로고
    • Linking the epigenetic language of covalent histone modifications to cancer
    • Hake SB, Xiao A, Allis CD. Linking the epigenetic language of covalent histone modifications to cancer. Br J Cancer 2004; 90: 761-9.
    • (2004) Br J Cancer , vol.90 , pp. 761-769
    • Hake, S.B.1    Xiao, A.2    Allis, C.D.3
  • 4
    • 10344260184 scopus 로고    scopus 로고
    • CpG island methylator phenotype in cancer
    • Issa JP. CpG island methylator phenotype in cancer. Nat Rev Cancer 2004; 4: 988-93.
    • (2004) Nat Rev Cancer , vol.4 , pp. 988-993
    • Issa, J.P.1
  • 5
    • 0035986095 scopus 로고    scopus 로고
    • Dynamics of histone acetylation in vivo. A function for acetylation turnover?
    • Waterborg JH. Dynamics of histone acetylation in vivo. A function for acetylation turnover? Biochem Cell Biol 2002; 80: 363-78.
    • (2002) Biochem Cell Biol , vol.80 , pp. 363-378
    • Waterborg, J.H.1
  • 6
    • 0032530486 scopus 로고    scopus 로고
    • DNA damage activates p53 through a phosphorylationacetylation cascade
    • Sakaguchi K, Herrera JE, Soutos, Mirkit, Bustin M, Vassilev A, et al. DNA damage activates p53 through a phosphorylationacetylation cascade. Genes Dev 1998; 12: 2831-41.
    • (1998) Genes Dev , vol.12 , pp. 2831-2841
    • Sakaguchi, K.1    Herrera, J.E.2    Soutos, M.3    Bustin, M.4    Vassilev, A.5
  • 8
    • 0141757504 scopus 로고    scopus 로고
    • p53 and radiation responses
    • Peip, El-Deiery WS. p53 and radiation responses. Oncogene 2003; 22: 5774-83.
    • (2003) Oncogene , vol.22 , pp. 5774-5783
    • Peip1    El-Deiery, W.S.2
  • 9
    • 0033595893 scopus 로고    scopus 로고
    • How NF-kappa B is activated: The role of the IkappaB kinase (IKK) complex
    • Karin, M. How NF-kappa B is activated: the role of the IkappaB kinase (IKK) complex. Oncogene 1999; 18: 6867-74.
    • (1999) Oncogene , vol.18 , pp. 6867-6874
    • Karin, M.1
  • 10
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 2000; 351: 95-105.
    • (2000) Biochem J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 11
    • 0034632791 scopus 로고    scopus 로고
    • 3-(Hydroymethyl)-bearing phophatidylinositol ether lipid analogues and carbonate surrogates block PI3-K, Akt, and cancer cell growth
    • Hu Y, Qiao L, Wang S, Rong SB, Meuillet EJ, Berggren M, Gallegos A. 3-(Hydroymethyl)-bearing phophatidylinositol ether lipid analogues and carbonate surrogates block PI3-K, Akt, and cancer cell growth. J Med Chem 2000; 43: 3045-51.
    • (2000) J Med Chem , vol.43 , pp. 3045-3051
    • Hu, Y.1    Qiao, L.2    Wang, S.3    Rong, S.B.4    Meuillet, E.J.5    Berggren, M.6    Gallegos, A.7
  • 12
    • 0035477320 scopus 로고    scopus 로고
    • Synergistic activation of functional estrogen receptor (ER)-alpha by DNA methyl transferase asl and histone deacetylase inhibition in human ER-alpha-negative breast cancer cells
    • Yang, X, Phillips DL, Ferguson AT, Nelson WG, Herman JG, Davidson NE. Synergistic activation of functional estrogen receptor (ER)-alpha by DNA methyl transferase asl and histone deacetylase inhibition in human ER-alpha-negative breast cancer cells. Cancer Res 2001; 61: 7025-9.
    • (2001) Cancer Res , vol.61 , pp. 7025-7029
    • Yang, X.1    Phillips, D.L.2    Ferguson, A.T.3    Nelson, W.G.4    Herman, J.G.5    Davidson, N.E.6
  • 13
    • 15044354027 scopus 로고    scopus 로고
    • Polynucleosomal synthesis of poly (ADP-ribose) causes chromatin unfolding as determined by micrococcal nuclease digestion
    • Perez-Lamigueiro MA, Alvarez-Gonzalez R. Polynucleosomal synthesis of poly (ADP-ribose) causes chromatin unfolding as determined by micrococcal nuclease digestion. Ann NY Acad Sci 2004; 1030: 593-8.
    • (2004) Ann NY Acad Sci , vol.1030 , pp. 593-598
    • Perez-Lamigueiro, M.A.1    Alvarez-Gonzalez, R.2
  • 14
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu W, Roeder RG. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell 1997; 90: 595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 15
    • 0037011056 scopus 로고    scopus 로고
    • Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB
    • Chen LF, Mu Y, Greene WC. Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB. EMBO J 2002; 21: 6539-48.
    • (2002) EMBO J , vol.21 , pp. 6539-6548
    • Chen, L.F.1    Mu, Y.2    Greene, W.C.3
  • 16
    • 0036753547 scopus 로고    scopus 로고
    • Control of Smad7 stability by competition between acetylation and ubiqutination
    • Gronroos E, Hellman U, Heldin CH, Ericsson J. Control of Smad7 stability by competition between acetylation and ubiqutination. Mol Cell 2002; 10: 483-93.
    • (2002) Mol Cell , vol.10 , pp. 483-493
    • Gronroos, E.1    Hellman, U.2    Heldin, C.H.3    Ericsson, J.4
  • 17
    • 0035163063 scopus 로고    scopus 로고
    • Identification of components of the murine histone deacetylase 6 complex: Link between acetylation and ubiquitination signaling pathways
    • Seigneurin-Burnj D, Verdel A, Curtet S, Lemercier C, Garin J, Rousseaux S, et al. Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways. Mol Cell Biol 2001; 21: 8035-44.
    • (2001) Mol Cell Biol , vol.21 , pp. 8035-8044
    • Seigneurin-Burnj, D.1    Verdel, A.2    Curtet, S.3    Lemercier, C.4    Garin, J.5    Rousseaux, S.6
  • 18
    • 17844385784 scopus 로고    scopus 로고
    • Regulatory cross-talk between lysine acetylation and ubiquitination: Role in the control of protein stability
    • Caron C, Boyault C, Khochbin S. Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability Bioessays 2005; 27: 408-15.
    • (2005) Bioessays , vol.27 , pp. 408-415
    • Caron, C.1    Boyault, C.2    Khochbin, S.3
  • 19
    • 34547924046 scopus 로고    scopus 로고
    • HATs and HDACs: From structure, function and regulation to novel strategies for therapy and prevention
    • Yang XJ, Seto E. HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention. Oncogene 2007; 26: 5310-18.
    • (2007) Oncogene , vol.26 , pp. 5310-5318
    • Yang, X.J.1    Seto, E.2
  • 20
    • 55849089366 scopus 로고    scopus 로고
    • Cohen T, Yao TP. AcK-knowledge reversible acetylation. Sci STKE (Signal transduction knowledge environment) 2004; pe 42: 1-30
    • Cohen T, Yao TP. AcK-knowledge reversible acetylation. Sci STKE (Signal transduction knowledge environment) 2004; pe 42: 1-30
  • 21
    • 34547697009 scopus 로고    scopus 로고
    • Metabolism, cytoskeleton and cellular signalling in the grip of protein Nepsilon- and O-acetylation
    • Yang XJ, Gre'goire S. Metabolism, cytoskeleton and cellular signalling in the grip of protein Nepsilon- and O-acetylation. EMBO Rep 2007; 8: 556-62.
    • (2007) EMBO Rep , vol.8 , pp. 556-562
    • Yang, X.J.1    Gre'goire, S.2
  • 23
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides T. Acetylation: a regulatory modification to rival phosphorylation? EMBO J 2000; 19: 1176-9.
    • (2000) EMBO J , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 24
    • 0027102583 scopus 로고
    • Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau
    • Takemura R, Okabe S, Umeyama T, Kanai Y, Cowan NJ, Hirokawa N. Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau. J Cell Sci 1992; 103: 953-64.
    • (1992) J Cell Sci , vol.103 , pp. 953-964
    • Takemura, R.1    Okabe, S.2    Umeyama, T.3    Kanai, Y.4    Cowan, N.J.5    Hirokawa, N.6
  • 26
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-êappaB action regulated by reversible acetylation
    • Chen LF, Fischle W, Verdin E, Greene WC. Duration of nuclear NF-êappaB action regulated by reversible acetylation. Science 2001; 293: 1653-7.
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, L.F.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 27
    • 0037112901 scopus 로고    scopus 로고
    • MDM2-HDAC1 - mediated deacetylation of p53 is required for its degradation
    • Ito A, Kawaguchi Y, Lai CH, Kovacs JJ, Higashimoto Y, Appella E, et al. MDM2-HDAC1 - mediated deacetylation of p53 is required for its degradation. EMBO J 2002; 21: 6236-45.
    • (2002) EMBO J , vol.21 , pp. 6236-6245
    • Ito, A.1    Kawaguchi, Y.2    Lai, C.H.3    Kovacs, J.J.4    Higashimoto, Y.5    Appella, E.6
  • 28
    • 20444474176 scopus 로고    scopus 로고
    • The balance between acetylation and deacetylation controls Smad7 stability
    • Simonsson M, Heldinch, Ericsson J, Gronroos E. The balance between acetylation and deacetylation controls Smad7 stability. J Biol Chem 2005; 280: 21797-803.
    • (2005) J Biol Chem , vol.280 , pp. 21797-21803
    • Simonsson, M.1    Heldinch2    Ericsson, J.3    Gronroos, E.4
  • 29
    • 0035032345 scopus 로고    scopus 로고
    • Grant PA. A tale of histone modifications. Genome Biol 2001; 2: REVIEWS. 0003.1-0003.6.
    • Grant PA. A tale of histone modifications. Genome Biol 2001; 2: REVIEWS. 0003.1-0003.6.
  • 30
    • 0029835806 scopus 로고    scopus 로고
    • Transcription-linked acetylation by GCN5p of histones H3 and H4 at specific lysines
    • Kuo MH, Brownell JE, Sobel RE, Ranalli TA, Cook RG, Edmondson DG, et al. Transcription-linked acetylation by GCN5p of histones H3 and H4 at specific lysines. Nature 1996; 383: 269-72.
    • (1996) Nature , vol.383 , pp. 269-272
    • Kuo, M.H.1    Brownell, J.E.2    Sobel, R.E.3    Ranalli, T.A.4    Cook, R.G.5    Edmondson, D.G.6
  • 31
    • 0033826515 scopus 로고    scopus 로고
    • Role of histone N-terminal tails and their acetylation in nucleosome dynamics
    • Moralis V, Helene Richard-Foyn. Role of histone N-terminal tails and their acetylation in nucleosome dynamics. Mol Cell Biol 2000; 20: 7230-37.
    • (2000) Mol Cell Biol , vol.20 , pp. 7230-7237
    • Moralis, V.1    Richard-Foyn, H.2
  • 32
    • 0142123130 scopus 로고    scopus 로고
    • Facile synthesis of site-specifically acetylated and methylated histone proteins: Reagents for evaluation of the histone code hypothesis
    • He S, Bauman D, Davis JS, Loyola A, Nishioka K, Grolund JL, et al. Facile synthesis of site-specifically acetylated and methylated histone proteins: reagents for evaluation of the histone code hypothesis. Proc Nat Acad Sci USA 2003; 100: 12033-8.
    • (2003) Proc Nat Acad Sci USA , vol.100 , pp. 12033-12038
    • He, S.1    Bauman, D.2    Davis, J.S.3    Loyola, A.4    Nishioka, K.5    Grolund, J.L.6
  • 33
    • 0343924289 scopus 로고    scopus 로고
    • Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters
    • Kadosh D, Struhl K. Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters. Cell 1997; 89: 365-71.
    • (1997) Cell , vol.89 , pp. 365-371
    • Kadosh, D.1    Struhl, K.2
  • 34
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo MH, Allis CD. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 1998; 20: 615-626.
    • (1998) Bioessays , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 35
    • 27144452299 scopus 로고    scopus 로고
    • Chromosomal protein HMGN1 enhances the acetylation of lysine 14 in histone H3
    • Lim JH, West KL, Rubinstein Y, Bergel M, Postnikov YV, Bustin M. Chromosomal protein HMGN1 enhances the acetylation of lysine 14 in histone H3. EMBO J 2005; 24: 3038-48.
    • (2005) EMBO J , vol.24 , pp. 3038-3048
    • Lim, J.H.1    West, K.L.2    Rubinstein, Y.3    Bergel, M.4    Postnikov, Y.V.5    Bustin, M.6
  • 36
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner DE, Berger SL. Acetylation of histones and transcription-related factors. Microbiol Mol Biol Rev 2000; 64: 435-59.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 37
    • 0037444803 scopus 로고    scopus 로고
    • Annmieke, Gennip Van H Albert, Caron N Huib, Kemp S, Kuilenburg van PB Andre. Histone deacetylases (HDACs): Characterization of the classical HDAC family
    • Ruijter De MJ, Annmieke, Gennip Van H Albert, Caron N Huib, Kemp S, Kuilenburg van PB Andre. Histone deacetylases (HDACs): characterization of the classical HDAC family. Biochem J 2003; 370: 737-49.
    • (2003) Biochem J , vol.370 , pp. 737-749
    • Ruijter, D.M.1
  • 38
    • 0030271391 scopus 로고    scopus 로고
    • Histone acetylation and chromatin assembly: A single escort, multiple dances?
    • Roth SY, Allis CD. Histone acetylation and chromatin assembly: a single escort, multiple dances? Cell 1996; 87: 5-8.
    • (1996) Cell , vol.87 , pp. 5-8
    • Roth, S.Y.1    Allis, C.D.2
  • 39
    • 0031031755 scopus 로고    scopus 로고
    • Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo
    • Candau R, Zhou JX, Allis CD, Berger SL. Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo. EMBO J 1997; 16: 555-65.
    • (1997) EMBO J , vol.16 , pp. 555-565
    • Candau, R.1    Zhou, J.X.2    Allis, C.D.3    Berger, S.L.4
  • 40
    • 0029835806 scopus 로고    scopus 로고
    • Transcription-linked acetylvation by GCN5P of histones H3 and H4 at specific lysines
    • Kuo MH, Brownell JE, Sobel RE, Ranalli TA, Cook RG, Edmondson DG, et al. Transcription-linked acetylvation by GCN5P of histones H3 and H4 at specific lysines. Nature 1996; 383: 269-72.
    • (1996) Nature , vol.383 , pp. 269-272
    • Kuo, M.H.1    Brownell, J.E.2    Sobel, R.E.3    Ranalli, T.A.4    Cook, R.G.5    Edmondson, D.G.6
  • 41
    • 9544220768 scopus 로고    scopus 로고
    • The translocation t (8; 16) (p11; p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein
    • Borrow J, Stanton VP Jr, Andresen JM, Becher R, Behm FG, Chaganti RS, et al. The translocation t (8; 16) (p11; p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein. Nat Genet 1996; 14: 33-41.
    • (1996) Nat Genet , vol.14 , pp. 33-41
    • Borrow, J.1    Stanton Jr, V.P.2    Andresen, J.M.3    Becher, R.4    Behm, F.G.5    Chaganti, R.S.6
  • 42
    • 0029665857 scopus 로고    scopus 로고
    • A p300/ CBP-associated factor that competes with the adenoviral. Oncoprotein E1A
    • Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y. A p300/ CBP-associated factor that competes with the adenoviral. Oncoprotein E1A. Nature 1996; 382: 319-24.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 43
    • 0033524942 scopus 로고    scopus 로고
    • A viral mechanism for inhibition of p300 and PCAF acetyltransferase activity
    • Chakravarti D, Ogryzko V, Kao HY, Nash A, Chen H, Nakatani Y, et al. A viral mechanism for inhibition of p300 and PCAF acetyltransferase activity. Cell 1999; 96: 393-403.
    • (1999) Cell , vol.96 , pp. 393-403
    • Chakravarti, D.1    Ogryzko, V.2    Kao, H.Y.3    Nash, A.4    Chen, H.5    Nakatani, Y.6
  • 44
    • 0033525094 scopus 로고    scopus 로고
    • Regulation of histone acetyltransferases p300 and PCAF by the DHLH protein twist and adenoviral oncoprotein E1A
    • Hamamori Y, Sartorelli V, Ogryzko V, Puri PL, Wu HY, Wang JY, et al. Regulation of histone acetyltransferases p300 and PCAF by the DHLH protein twist and adenoviral oncoprotein E1A. Cell 1999; 96: 405-13.
    • (1999) Cell , vol.96 , pp. 405-413
    • Hamamori, Y.1    Sartorelli, V.2    Ogryzko, V.3    Puri, P.L.4    Wu, H.Y.5    Wang, J.Y.6
  • 45
    • 34547897023 scopus 로고    scopus 로고
    • Histone deacetylases and cancer
    • Glozak MA, Seto E. Histone deacetylases and cancer. Oncogene 2007; 26: 5420-32.
    • (2007) Oncogene , vol.26 , pp. 5420-5432
    • Glozak, M.A.1    Seto, E.2
  • 46
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylases, transcriptional control, and cancer
    • Cress WD, Seto E. Histone deacetylases, transcriptional control, and cancer. J Cell Physiol 2000; 184: 1-16.
    • (2000) J Cell Physiol , vol.184 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 48
    • 0035577768 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberoyanilide hydroxamic acid induces differentiation of human breast cancer cells
    • Munster PN, Troso Sandoval T, Rosen N, Rifkind R, Marks PA, Richon VM. The histone deacetylase inhibitor suberoyanilide hydroxamic acid induces differentiation of human breast cancer cells. Cancer Res 2001; 61: 8492-7.
    • (2001) Cancer Res , vol.61 , pp. 8492-8497
    • Munster, P.N.1    Troso Sandoval, T.2    Rosen, N.3    Rifkind, R.4    Marks, P.A.5    Richon, V.M.6
  • 49
    • 0037112901 scopus 로고    scopus 로고
    • MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation
    • Ito A, Kawaguchi Y, Lai CH, Kovacs JJ, Higashimoto Y, Appella E, et al. MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation. EMBO J 2002; 21: 6236-45.
    • (2002) EMBO J , vol.21 , pp. 6236-6245
    • Ito, A.1    Kawaguchi, Y.2    Lai, C.H.3    Kovacs, J.J.4    Higashimoto, Y.5    Appella, E.6
  • 50
    • 0035321333 scopus 로고    scopus 로고
    • Role of DNA methylation and histone acetylation in steroid receptor expression in breast cancer
    • Yan L, Yang X, Davidson NE. Role of DNA methylation and histone acetylation in steroid receptor expression in breast cancer. J Mammary Gland Biol Neoplasia 2001; 6: 183-92.
    • (2001) J Mammary Gland Biol Neoplasia , vol.6 , pp. 183-192
    • Yan, L.1    Yang, X.2    Davidson, N.E.3
  • 51
    • 33746054902 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors as a potential therapeutic agent for human cancer treatment
    • Kouraklis G, Misiakos EP, Theocharis S. Histone deacetylase inhibitors as a potential therapeutic agent for human cancer treatment. Targ Oncol 2006; 1: 34-41
    • (2006) Targ Oncol , vol.1 , pp. 34-41
    • Kouraklis, G.1    Misiakos, E.P.2    Theocharis, S.3
  • 52
    • 0001790293 scopus 로고    scopus 로고
    • Histone deacetylases and transcriptional therapy with their inhibitors
    • Pandolfi PP. Histone deacetylases and transcriptional therapy with their inhibitors. Cancer Chemother Pharmacol 2001; 48 (Suppl 1): S17-9.
    • (2001) Cancer Chemother Pharmacol , vol.48 , Issue.SUPPL. 1
    • Pandolfi, P.P.1
  • 53
    • 33947313218 scopus 로고    scopus 로고
    • HDACs, histone deacetylation and gene transcription:from molecular biology to cancer therapeutics
    • Gallinari P, Di Marco S, Jones P, Pallaoro M, Steinkuhler C. HDACs, histone deacetylation and gene transcription:from molecular biology to cancer therapeutics. Cell Res 2007; 17: 195-211.
    • (2007) Cell Res , vol.17 , pp. 195-211
    • Gallinari, P.1    Di Marco, S.2    Jones, P.3    Pallaoro, M.4    Steinkuhler, C.5
  • 55
    • 0036171675 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor trichostatin A blocks proliferation and triggers apoptotic programs in hepatoma cells
    • Herold C, Ganslmayer M, Ocker M, Hermann M, Geerts A, Hahn EG, et al. The histone deacetylase inhibitor trichostatin A blocks proliferation and triggers apoptotic programs in hepatoma cells. J Hepatol 2002; 36: 233-40.
    • (2002) J Hepatol , vol.36 , pp. 233-240
    • Herold, C.1    Ganslmayer, M.2    Ocker, M.3    Hermann, M.4    Geerts, A.5    Hahn, E.G.6
  • 56
    • 0028022785 scopus 로고
    • Trichostatin A induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines
    • Hoshikawa Y, Kwon HJ, Yoshida M, Horinouchi S, Beppu T. Trichostatin A induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines. Exp Cell Res 1994; 214: 189-97.
    • (1994) Exp Cell Res , vol.214 , pp. 189-197
    • Hoshikawa, Y.1    Kwon, H.J.2    Yoshida, M.3    Horinouchi, S.4    Beppu, T.5
  • 57
    • 0041532109 scopus 로고    scopus 로고
    • Cell cycle blockade and differentiation of ovarian cancer cells by the histone deacetylase inhibitor trichostatin A are associated with changes in p21, Rb, and Id proteins
    • Strait KA, Dabbas B, Hammond EH, Warnick CT, Iistrup SJ, Ford CD. Cell cycle blockade and differentiation of ovarian cancer cells by the histone deacetylase inhibitor trichostatin A are associated with changes in p21, Rb, and Id proteins. Mol Cancer Ther 2002; 1: 1181-90.
    • (2002) Mol Cancer Ther , vol.1 , pp. 1181-1190
    • Strait, K.A.1    Dabbas, B.2    Hammond, E.H.3    Warnick, C.T.4    Iistrup, S.J.5    Ford, C.D.6
  • 58
    • 85077951985 scopus 로고    scopus 로고
    • The mechanism of the anti-tumor activity of the histone deacetylase inhibitor, suberoylanilide hydroxamic acid (SAHA)
    • Marks PA. The mechanism of the anti-tumor activity of the histone deacetylase inhibitor, suberoylanilide hydroxamic acid (SAHA). Cell Cycle 2004; 3: 534-5.
    • (2004) Cell Cycle , vol.3 , pp. 534-535
    • Marks, P.A.1
  • 59
    • 0032539890 scopus 로고    scopus 로고
    • A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases
    • Richon VM, Emiliani S, Verdin E, Webb Y, Breslow R, Rifkind RA, et al. A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases. Proc Natl Acad Sci U S A 1998; 95: 3003-7.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 3003-3007
    • Richon, V.M.1    Emiliani, S.2    Verdin, E.3    Webb, Y.4    Breslow, R.5    Rifkind, R.A.6
  • 60
    • 0035046529 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Development of suberoylanilide hydroxamic acid (SAHA) for the treatment of cancers
    • Richon VM, Zhou X, Rifkind RA, Marks PA. Histone deacetylase inhibitors: development of suberoylanilide hydroxamic acid (SAHA) for the treatment of cancers. Blood Cells Mol Dis 2001; 27: 260-4.
    • (2001) Blood Cells Mol Dis , vol.27 , pp. 260-264
    • Richon, V.M.1    Zhou, X.2    Rifkind, R.A.3    Marks, P.A.4
  • 61
    • 0034297220 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid as a potential therapeutic agent for human breast cancer treatment
    • Huang L, Pardee AB. Suberoylanilide hydroxamic acid as a potential therapeutic agent for human breast cancer treatment. Mol Med 2000; 6: 849-66.
    • (2000) Mol Med , vol.6 , pp. 849-866
    • Huang, L.1    Pardee, A.B.2
  • 62
    • 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 JA, Decker RH, Johnson CR, Wang Z, Jarvis WD, Richon VM, 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 1999; 18: 7016-25.
    • (1999) Oncogene , vol.18 , 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
  • 63
    • 0035328528 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor, CBHA, inhibits growth of human neuroblastoma xenografts in vivo, alone and synergistically with all-trans retinoic acid
    • Coffey DC, Kutko MC, Glick RD, Butler LM, Heller G, Rifkind AR, et al. The histone deacetylase inhibitor, CBHA, inhibits growth of human neuroblastoma xenografts in vivo, alone and synergistically with all-trans retinoic acid. Cancer Res 2001; 61: 3591-4.
    • (2001) Cancer Res , vol.61 , pp. 3591-3594
    • Coffey, D.C.1    Kutko, M.C.2    Glick, R.D.3    Butler, L.M.4    Heller, G.5    Rifkind, A.R.6
  • 64
    • 1542588471 scopus 로고    scopus 로고
    • Second generation hybrid polar compounds are potent inducers of transformed cell differentiation
    • Richon VM, Webb Y, Merger R, Sheppard T, Jursic B, Ngo L, et al. Second generation hybrid polar compounds are potent inducers of transformed cell differentiation. Proc Natl Acad Sci U S A 1996; 93: 5705-8.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 5705-5708
    • Richon, V.M.1    Webb, Y.2    Merger, R.3    Sheppard, T.4    Jursic, B.5    Ngo, L.6
  • 65
    • 0024518889 scopus 로고
    • Chromatin decondensed by acetylation shows an elevated radiation response
    • Nackerdien Z, Michie J, Bohm L. Chromatin decondensed by acetylation shows an elevated radiation response. Radiat Res 1989; 117: 234-44.
    • (1989) Radiat Res , vol.117 , pp. 234-244
    • Nackerdien, Z.1    Michie, J.2    Bohm, L.3
  • 66
    • 55849115046 scopus 로고    scopus 로고
    • Trichostatin A, a histone deacetylase inhibitor, potentiated cytotoxic effect of ionizing radiation in human head and neck cancer cell lines
    • Kim J H, Jin H S, Eui K C, Hong-G W, Jae S K, Han K, et al. Trichostatin A, a histone deacetylase inhibitor, potentiated cytotoxic effect of ionizing radiation in human head and neck cancer cell lines. J Korean Soc Ther Radiol Oncol 2004; 22: 138-44.
    • (2004) J Korean Soc Ther Radiol Oncol , vol.22 , pp. 138-144
    • Kim, J.H.1    Jin, H.S.2    Eui, K.C.3    Hong-G, W.4    Jae, S.K.5    Han, K.6
  • 67
    • 0242610850 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase increases cytotoxicity to anticancer drugs targeting DNA
    • Kim MS, Blake M, Baek JH, Kohlhagen G, Pommier Y, Carrier F. Inhibition of histone deacetylase increases cytotoxicity to anticancer drugs targeting DNA. Cancer Res 2003; 63: 7291-300.
    • (2003) Cancer Res , vol.63 , pp. 7291-7300
    • Kim, M.S.1    Blake, M.2    Baek, J.H.3    Kohlhagen, G.4    Pommier, Y.5    Carrier, F.6
  • 68
    • 0031723393 scopus 로고    scopus 로고
    • Enhanced growth inhibition and differentiation of fluorodeoxyuridine-treated human colon carcinoma cells by phenylbutyrate
    • Huang Y, Waxman S. Enhanced growth inhibition and differentiation of fluorodeoxyuridine-treated human colon carcinoma cells by phenylbutyrate. Clin Cancer Res 1998; 4: 2503-9.
    • (1998) Clin Cancer Res , vol.4 , pp. 2503-2509
    • Huang, Y.1    Waxman, S.2
  • 69
    • 0034124452 scopus 로고    scopus 로고
    • Regrowth of 5-fluorouracil-treated human colon cancer cells is prevented by the combination of interferon gamma, indomethacin and phenylbutyrate
    • Huang Y, Horvath CM, Waxman S. Regrowth of 5-fluorouracil-treated human colon cancer cells is prevented by the combination of interferon gamma, indomethacin and phenylbutyrate. Cancer Res 2000; 60: 3200-6.
    • (2000) Cancer Res , vol.60 , pp. 3200-3206
    • Huang, Y.1    Horvath, C.M.2    Waxman, S.3
  • 70
    • 1642490813 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor LAQ824 down-regulates Her-2 and sensitizes human breast cancer cells to trastuzumab, taxotere, gemcitabine and epothilone B
    • Fuino L, Bali P, Wittmann S, Donapaty S, Guo F, Yamaguchi H, et al. Histone deacetylase inhibitor LAQ824 down-regulates Her-2 and sensitizes human breast cancer cells to trastuzumab, taxotere, gemcitabine and epothilone B. Mol Cancer Ther 2003; 2: 971-84.
    • (2003) Mol Cancer Ther , vol.2 , pp. 971-984
    • Fuino, L.1    Bali, P.2    Wittmann, S.3    Donapaty, S.4    Guo, F.5    Yamaguchi, H.6
  • 71
    • 0015237292 scopus 로고
    • Inhibition of prostaglandin synthesis as a mechanism of action for aspirin like drugs
    • Vane JR. Inhibition of prostaglandin synthesis as a mechanism of action for aspirin like drugs. Nat NewBiol 1971; 231: 232-5.
    • (1971) Nat NewBiol , vol.231 , pp. 232-235
    • Vane, J.R.1
  • 72
    • 0035014427 scopus 로고    scopus 로고
    • Mechanism of biochemical action of substituted Benzopyran-2-ones, part 8: Acetoxycoumarin: protein transacetylase-specificity for aromatic nuclear acetoxy groups in proximity to the oxygen heteroatom
    • Raj HG, Kohli E, Goswami R, Goel S, Rastogi RC, Jain SC, et al. Mechanism of biochemical action of substituted Benzopyran-2-ones, part 8: Acetoxycoumarin: protein transacetylase-specificity for aromatic nuclear acetoxy groups in proximity to the oxygen heteroatom. Bioorg Med Chem 2001; 9: 1085-9.
    • (2001) Bioorg Med Chem , vol.9 , pp. 1085-1089
    • Raj, H.G.1    Kohli, E.2    Goswami, R.3    Goel, S.4    Rastogi, R.C.5    Jain, S.C.6
  • 73
    • 34147160580 scopus 로고    scopus 로고
    • Characterization of protein transacetylase from human placenta as a signaling molecule calreticulin using polyphenolic peracetates as the acetyl group donors
    • Seema, Kumari R, Gupta G, Saluja D, Kumar A, Goel S, et al. Characterization of protein transacetylase from human placenta as a signaling molecule calreticulin using polyphenolic peracetates as the acetyl group donors. Cell Biochem Biophysics 2007; 47: 53-64.
    • (2007) Cell Biochem Biophysics , vol.47 , pp. 53-64
    • Seema1    Kumari, R.2    Gupta, G.3    Saluja, D.4    Kumar, A.5    Goel, S.6
  • 74
    • 18644361958 scopus 로고    scopus 로고
    • Establishment of the enzymatic protein acetylation independent of acetyl CoA: Recombinant glutathione S- transferase 3-3 is acetylated by a novel membrane-bound transacetylase using 7, 8-diacetoxy-4-methyl coumarin as the acetyl donor
    • Kohli E, Gaspari M, Raj HG, Parmar VS, Vender Greef J, Gupta G, et al. Establishment of the enzymatic protein acetylation independent of acetyl CoA: recombinant glutathione S- transferase 3-3 is acetylated by a novel membrane-bound transacetylase using 7, 8-diacetoxy-4-methyl coumarin as the acetyl donor.FEBS Lett 2002; 530: 139-42.
    • (2002) FEBS Lett , vol.530 , pp. 139-142
    • Kohli, E.1    Gaspari, M.2    Raj, H.G.3    Parmar, V.S.4    Vender Greef, J.5    Gupta, G.6
  • 75
    • 11144357313 scopus 로고    scopus 로고
    • Acetoxy drug: Protein transacetylase of buffalo liver-characterization and mass spectrometry of the acetylated protein product
    • Kohli E, Gaspari M, Raj HG, Parmar VS, Sharma SK, Vander Greef J, et al. Acetoxy drug: protein transacetylase of buffalo liver-characterization and mass spectrometry of the acetylated protein product. Biochim Biophys Acta 2004; 1698: 55-66.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 55-66
    • Kohli, E.1    Gaspari, M.2    Raj, H.G.3    Parmar, V.S.4    Sharma, S.K.5    Vander Greef, J.6
  • 76
    • 28844440477 scopus 로고    scopus 로고
    • Seema, Gupta Garima. Acetoxy drug: Protein transacetylase catalyzed activation of human platelet nitric oxide synthase by polyphenolic peracetates
    • Khurana P, Kumari R, Vohra P, Kumar Ajit, Seema, Gupta Garima. Acetoxy drug: protein transacetylase catalyzed activation of human platelet nitric oxide synthase by polyphenolic peracetates. Bioorg Med Chem 2006; 14: 575-83.
    • (2006) Bioorg Med Chem , vol.14 , pp. 575-583
    • Khurana, P.1    Kumari, R.2    Vohra, P.3    Ajit, K.4
  • 77
    • 34547911052 scopus 로고    scopus 로고
    • Chemistry of acetyl transfer by histone modifying enzymes: Structure, mechanism and implications for effector design
    • Hodawadekar SC, Marmorstein R. Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design. Oncogene 2007; 26: 5528-40.
    • (2007) Oncogene , vol.26 , pp. 5528-5540
    • Hodawadekar, S.C.1    Marmorstein, R.2
  • 79
    • 0030117803 scopus 로고    scopus 로고
    • Prooxidant effects of antioxidant vitamins. introduction
    • Herbert V. Prooxidant effects of antioxidant vitamins. introduction. J Nutr. 1996; 126 (4 Suppl): 1197S-200S.
    • (1996) J Nutr , vol.126 , Issue.4 SUPPL.
    • Herbert, V.1


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