메뉴 건너뛰기




Volumn 12, Issue 1-2, 2007, Pages 88-99

Pharmacological targeting of lysine acetyltransferases in human disease: a progress report

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLHISTAMINE; AMINO ACID ACETYLTRANSFERASE; ANACARDIC ACID; CORTICOSTEROID; CURCUMIN; ENZYME INHIBITOR; ERI 7; GARCINOL; HORMONE RECEPTOR BLOCKING AGENT; INDOLYLBUTENONE; ISOTHIAZOLONE; LYSINE ACETYLTRANSFERASE; LYSINE ACETYLTRANSFERASE INHIBITOR; MS 7972; NAPHTHOQUINOLINONE; PHENYLPROPANEDIAMINE; TAMOXIFEN; TRIAZOLOPYRIMIDINE; TRICHOSTATIN A; UNCLASSIFIED DRUG;

EID: 33845746277     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.drudis.2006.11.012     Document Type: Review
Times cited : (34)

References (107)
  • 1
    • 2342599619 scopus 로고    scopus 로고
    • The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases
    • Yang X.J. The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases. Nucleic Acids Res. 32 (2004) 959-976
    • (2004) Nucleic Acids Res. , vol.32 , pp. 959-976
    • Yang, X.J.1
  • 2
    • 23844472662 scopus 로고    scopus 로고
    • Human histone chaperone nucleophosmin enhances acetylation-dependent chromatin transcription
    • Swaminathan V., et al. Human histone chaperone nucleophosmin enhances acetylation-dependent chromatin transcription. Mol. Cell. Biol. 25 (2005) 7534-7545
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7534-7545
    • Swaminathan, V.1
  • 3
    • 28044471827 scopus 로고    scopus 로고
    • Acetylation and deacetylation of non-histone proteins
    • Glozak M.A., et al. Acetylation and deacetylation of non-histone proteins. Gene 363 (2005) 15-23
    • (2005) Gene , vol.363 , pp. 15-23
    • Glozak, M.A.1
  • 4
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner D.E., and Berger S.L. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 64 (2000) 435-459
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 5
    • 1042300238 scopus 로고    scopus 로고
    • Biochemical and structural characterization of recombinant histone acetyltransferase proteins
    • Marmorstein R. Biochemical and structural characterization of recombinant histone acetyltransferase proteins. Methods Enzymol. 376 (2004) 106-119
    • (2004) Methods Enzymol. , vol.376 , pp. 106-119
    • Marmorstein, R.1
  • 6
    • 1842420646 scopus 로고    scopus 로고
    • Regulation of the p300 HAT domain via a novel activation loop
    • Thompson P.R., et al. Regulation of the p300 HAT domain via a novel activation loop. Nat. Struct. Mol. Biol. 11 (2004) 308-315
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 308-315
    • Thompson, P.R.1
  • 7
    • 7044250740 scopus 로고    scopus 로고
    • Lysine acetylation and the bromodomain: a new partnership for signaling
    • Yang X.J. Lysine acetylation and the bromodomain: a new partnership for signaling. Bioessays 26 (2004) 1076-1087
    • (2004) Bioessays , vol.26 , pp. 1076-1087
    • Yang, X.J.1
  • 8
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery D.M., et al. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387 (1997) 733-736
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1
  • 9
    • 0042334873 scopus 로고    scopus 로고
    • Review of the in vivo functions of the p160 steroid receptor coactivator family
    • Xu J., and Li Q. Review of the in vivo functions of the p160 steroid receptor coactivator family. Mol. Endocrinol. 17 (2003) 1681-1692
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1681-1692
    • Xu, J.1    Li, Q.2
  • 10
    • 0032213219 scopus 로고    scopus 로고
    • Structure and specificity of nuclear receptor-coactivator interactions
    • Darimont B.D., et al. Structure and specificity of nuclear receptor-coactivator interactions. Genes Dev. 12 (1998) 3343-3356
    • (1998) Genes Dev. , vol.12 , pp. 3343-3356
    • Darimont, B.D.1
  • 11
    • 0030666852 scopus 로고    scopus 로고
    • Transformed cells require continuous activity of RNA polymerase II to resist oncogene-induced apoptosis
    • Koumenis C., and Giaccia A. Transformed cells require continuous activity of RNA polymerase II to resist oncogene-induced apoptosis. Mol. Cell. Biol. 17 (1997) 7306-7316
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7306-7316
    • Koumenis, C.1    Giaccia, A.2
  • 12
    • 0034466971 scopus 로고    scopus 로고
    • Acetyltransferases and tumour suppression
    • Phillips A.C., and Vousden K.H. Acetyltransferases and tumour suppression. Breast Cancer Res. 2 (2000) 244-246
    • (2000) Breast Cancer Res. , vol.2 , pp. 244-246
    • Phillips, A.C.1    Vousden, K.H.2
  • 13
    • 0034141475 scopus 로고    scopus 로고
    • Gene dose-dependent control of hematopoiesis and hematologic tumor suppression by CBP
    • Kung A.L., et al. Gene dose-dependent control of hematopoiesis and hematologic tumor suppression by CBP. Genes Dev. 14 (2000) 272-277
    • (2000) Genes Dev. , vol.14 , pp. 272-277
    • Kung, A.L.1
  • 14
    • 21744457108 scopus 로고    scopus 로고
    • Global histone modification patterns predict risk of prostate cancer recurrence
    • Seligson D.B., et al. Global histone modification patterns predict risk of prostate cancer recurrence. Nature 435 (2005) 1262-1266
    • (2005) Nature , vol.435 , pp. 1262-1266
    • Seligson, D.B.1
  • 15
    • 17444390135 scopus 로고    scopus 로고
    • Chromatin modifying activity of leukaemia associated fusion proteins
    • Di Croce L. Chromatin modifying activity of leukaemia associated fusion proteins. Hum. Mol. Genet. 14 (2005) 77-84
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 77-84
    • Di Croce, L.1
  • 16
    • 12644314103 scopus 로고    scopus 로고
    • MLL is fused to CBP, a histone acetyltransferase, in therapy-related acute myeloid leukemia with a t(11;16)(q23;p13.3)
    • Sobulo O.M., et al. MLL is fused to CBP, a histone acetyltransferase, in therapy-related acute myeloid leukemia with a t(11;16)(q23;p13.3). Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 8732-8737
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 8732-8737
    • Sobulo, O.M.1
  • 17
    • 2442591839 scopus 로고    scopus 로고
    • Extending the repertoire of the mixed-lineage leukemia gene MLL in leukemogenesis
    • Daser A., and Rabbitts T.H. Extending the repertoire of the mixed-lineage leukemia gene MLL in leukemogenesis. Genes Dev. 18 (2004) 965-974
    • (2004) Genes Dev. , vol.18 , pp. 965-974
    • Daser, A.1    Rabbitts, T.H.2
  • 18
    • 33646834126 scopus 로고    scopus 로고
    • MOZ fusion proteins in acute myeloid leukaemia
    • Troke P.J., et al. MOZ fusion proteins in acute myeloid leukaemia. Biochem. Soc. Symp. 73 (2005) 23-39
    • (2005) Biochem. Soc. Symp. , vol.73 , pp. 23-39
    • Troke, P.J.1
  • 19
    • 19944433555 scopus 로고    scopus 로고
    • MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by impairment of CBP function
    • Kindle K.B., et al. MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by impairment of CBP function. Mol. Cell. Biol. 25 (2005) 988-1002
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 988-1002
    • Kindle, K.B.1
  • 20
    • 0037981392 scopus 로고    scopus 로고
    • Molecular structure and biological function of the cancer-amplified nuclear receptor coactivator SRC-3/AIB1
    • Liao L., et al. Molecular structure and biological function of the cancer-amplified nuclear receptor coactivator SRC-3/AIB1. J. Steroid Biochem. Mol. Biol. 83 (2002) 3-14
    • (2002) J. Steroid Biochem. Mol. Biol. , vol.83 , pp. 3-14
    • Liao, L.1
  • 21
    • 0742324871 scopus 로고    scopus 로고
    • Expression of estrogen receptor coregulators in normal and malignant human endometrium
    • Kershah S.M., et al. Expression of estrogen receptor coregulators in normal and malignant human endometrium. Gynecol. Oncol. 92 (2004) 304-313
    • (2004) Gynecol. Oncol. , vol.92 , pp. 304-313
    • Kershah, S.M.1
  • 22
    • 0035101145 scopus 로고    scopus 로고
    • Cellular and molecular pharmacology of antiestrogen action and resistance
    • Clarke R., et al. Cellular and molecular pharmacology of antiestrogen action and resistance. Pharmacol. Rev. 53 (2001) 25-71
    • (2001) Pharmacol. Rev. , vol.53 , pp. 25-71
    • Clarke, R.1
  • 23
    • 33744960022 scopus 로고    scopus 로고
    • Structural diversity in p160/CREB-binding protein coactivator complexes
    • Waters L., et al. Structural diversity in p160/CREB-binding protein coactivator complexes. J. Biol. Chem. 281 (2006) 14787-14795
    • (2006) J. Biol. Chem. , vol.281 , pp. 14787-14795
    • Waters, L.1
  • 24
    • 4143114765 scopus 로고    scopus 로고
    • Acetylation of nuclear receptors in cellular growth and apoptosis
    • Fu M., et al. Acetylation of nuclear receptors in cellular growth and apoptosis. Biochem. Pharmacol. 68 (2004) 1199-1208
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 1199-1208
    • Fu, M.1
  • 25
    • 0034109837 scopus 로고    scopus 로고
    • Inhaled corticosteroids are not beneficial in chronic obstructive pulmonary disease
    • Barnes P.J. Inhaled corticosteroids are not beneficial in chronic obstructive pulmonary disease. Am. J. Respir. Crit. Care Med. 161 (2000) 342-344
    • (2000) Am. J. Respir. Crit. Care Med. , vol.161 , pp. 342-344
    • Barnes, P.J.1
  • 26
    • 21044458874 scopus 로고    scopus 로고
    • Decreased histone deacetylase activity in chronic obstructive pulmonary disease
    • Ito K., et al. Decreased histone deacetylase activity in chronic obstructive pulmonary disease. N. Engl. J. Med. 352 (2005) 1967-1976
    • (2005) N. Engl. J. Med. , vol.352 , pp. 1967-1976
    • Ito, K.1
  • 27
    • 14744285888 scopus 로고    scopus 로고
    • Histone acetylation and deacetylation: Importance in inflammatory lung diseases
    • Barnes P.J., et al. Histone acetylation and deacetylation: Importance in inflammatory lung diseases. Eur. Respir. J. 25 (2005) 552-563
    • (2005) Eur. Respir. J. , vol.25 , pp. 552-563
    • Barnes, P.J.1
  • 28
    • 4544379912 scopus 로고    scopus 로고
    • Theophylline restores histone deacetylase activity and steroid responses in COPD macrophages
    • Cosio B.G., et al. Theophylline restores histone deacetylase activity and steroid responses in COPD macrophages. J. Exp. Med. 200 (2004) 689-695
    • (2004) J. Exp. Med. , vol.200 , pp. 689-695
    • Cosio, B.G.1
  • 29
    • 33644784718 scopus 로고    scopus 로고
    • Corticosteroids: The drugs to beat
    • Barnes P.J. Corticosteroids: The drugs to beat. Eur. J. Pharmacol. 533 (2006) 2-14
    • (2006) Eur. J. Pharmacol. , vol.533 , pp. 2-14
    • Barnes, P.J.1
  • 30
    • 0347624643 scopus 로고    scopus 로고
    • Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter
    • Lusic M., et al. Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter. EMBO J. 22 (2003) 6550-6561
    • (2003) EMBO J. , vol.22 , pp. 6550-6561
    • Lusic, M.1
  • 31
    • 11444253965 scopus 로고    scopus 로고
    • HIV-1 TAR RNA: the target of molecular interactions between the virus and its host
    • Bannwarth S., and Gatignol A. HIV-1 TAR RNA: the target of molecular interactions between the virus and its host. Curr. HIV Res. 3 (2005) 61-71
    • (2005) Curr. HIV Res. , vol.3 , pp. 61-71
    • Bannwarth, S.1    Gatignol, A.2
  • 32
    • 0029919356 scopus 로고    scopus 로고
    • Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation
    • Van Lint C., et al. Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation. EMBO J. 15 (1996) 1112-1120
    • (1996) EMBO J. , vol.15 , pp. 1112-1120
    • Van Lint, C.1
  • 33
    • 0042671259 scopus 로고    scopus 로고
    • Acetylation of Tat defines a cyclinT1-independent step in HIV transactivation
    • Kaehlcke K., et al. Acetylation of Tat defines a cyclinT1-independent step in HIV transactivation. Mol. Cell 12 (2003) 167-176
    • (2003) Mol. Cell , vol.12 , pp. 167-176
    • Kaehlcke, K.1
  • 34
    • 0037013851 scopus 로고    scopus 로고
    • Transcriptional synergy between Tat and PCAF is dependent on the binding of acetylated Tat to the PCAF bromodomain
    • Dorr A., et al. Transcriptional synergy between Tat and PCAF is dependent on the binding of acetylated Tat to the PCAF bromodomain. EMBO J. 21 (2002) 2715-2723
    • (2002) EMBO J. , vol.21 , pp. 2715-2723
    • Dorr, A.1
  • 35
    • 0036839054 scopus 로고    scopus 로고
    • Synergistic activation of human immunodeficiency virus type 1 promoter activity by NF-κB and inhibitors of deacetylases: potential perspectives for the development of therapeutic strategies
    • Quivy V., et al. Synergistic activation of human immunodeficiency virus type 1 promoter activity by NF-κB and inhibitors of deacetylases: potential perspectives for the development of therapeutic strategies. J. Virol. 76 (2002) 11091-11103
    • (2002) J. Virol. , vol.76 , pp. 11091-11103
    • Quivy, V.1
  • 36
    • 4143089463 scopus 로고    scopus 로고
    • Administration of HDAC inhibitors to reactivate HIV-1 expression in latent cellular reservoirs: implications for the development of therapeutic strategies
    • Demonte D., et al. Administration of HDAC inhibitors to reactivate HIV-1 expression in latent cellular reservoirs: implications for the development of therapeutic strategies. Biochem. Pharmacol. 68 (2004) 1231-1238
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 1231-1238
    • Demonte, D.1
  • 37
    • 10944243759 scopus 로고    scopus 로고
    • Curcumin, a novel p300/CREB-binding protein-specific inhibitor of acetyltransferase, represses the acetylation of histone/nonhistone proteins and histone acetyltransferase-dependent chromatin transcription
    • Balasubramanyam K., et al. Curcumin, a novel p300/CREB-binding protein-specific inhibitor of acetyltransferase, represses the acetylation of histone/nonhistone proteins and histone acetyltransferase-dependent chromatin transcription. J. Biol. Chem. 279 (2004) 51163-51171
    • (2004) J. Biol. Chem. , vol.279 , pp. 51163-51171
    • Balasubramanyam, K.1
  • 38
    • 33744736618 scopus 로고    scopus 로고
    • Chromatin modifications (acetylation/ deacetylation/ methylation) as new targets for HIV therapy
    • Varier R.A., and Kundu T.K. Chromatin modifications (acetylation/ deacetylation/ methylation) as new targets for HIV therapy. Curr. Pharm. Des. 12 (2006) 1975-1993
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 1975-1993
    • Varier, R.A.1    Kundu, T.K.2
  • 39
    • 0038820063 scopus 로고    scopus 로고
    • Glucose regulates insulin gene transcription by hyperacetylation of histone h4
    • Mosley A.L., and Ozcan S. Glucose regulates insulin gene transcription by hyperacetylation of histone h4. J. Biol. Chem. 278 (2003) 19660-19666
    • (2003) J. Biol. Chem. , vol.278 , pp. 19660-19666
    • Mosley, A.L.1    Ozcan, S.2
  • 40
    • 0038607422 scopus 로고    scopus 로고
    • Covalent histone modifications underlie the developmental regulation of insulin gene transcription in pancreatic beta cells
    • Chakrabarti S.K., et al. Covalent histone modifications underlie the developmental regulation of insulin gene transcription in pancreatic beta cells. J. Biol. Chem. 278 (2003) 23617-23623
    • (2003) J. Biol. Chem. , vol.278 , pp. 23617-23623
    • Chakrabarti, S.K.1
  • 41
    • 24944496184 scopus 로고    scopus 로고
    • Role of histone and transcription factor acetylation in diabetes pathogenesis
    • Gray S.G., and De Meyts P. Role of histone and transcription factor acetylation in diabetes pathogenesis. Diabetes Metab. Res. Rev. 21 (2005) 416-433
    • (2005) Diabetes Metab. Res. Rev. , vol.21 , pp. 416-433
    • Gray, S.G.1    De Meyts, P.2
  • 42
    • 0036478904 scopus 로고    scopus 로고
    • Increased insulin sensitivity despite lipodystrophy in CREBbp heterozygous mice
    • Yamauchi T., et al. Increased insulin sensitivity despite lipodystrophy in CREBbp heterozygous mice. Nat. Genet. 30 (2002) 221-226
    • (2002) Nat. Genet. , vol.30 , pp. 221-226
    • Yamauchi, T.1
  • 43
    • 15744369973 scopus 로고    scopus 로고
    • Nuclear receptors as targets for drug development: molecular mechanisms for regulation of obesity and insulin resistance by peroxisome proliferator-activated receptor gamma, CREB-binding protein, and adiponectin
    • Tsuchida A., et al. Nuclear receptors as targets for drug development: molecular mechanisms for regulation of obesity and insulin resistance by peroxisome proliferator-activated receptor gamma, CREB-binding protein, and adiponectin. J. Pharmacol. Sci. 97 (2005) 164-170
    • (2005) J. Pharmacol. Sci. , vol.97 , pp. 164-170
    • Tsuchida, A.1
  • 44
    • 1042300239 scopus 로고    scopus 로고
    • Selective HAT inhibitors as mechanistic tools for protein acetylation
    • Zheng Y., et al. Selective HAT inhibitors as mechanistic tools for protein acetylation. Methods Enzymol. 376 (2004) 188-199
    • (2004) Methods Enzymol. , vol.376 , pp. 188-199
    • Zheng, Y.1
  • 45
    • 0038692967 scopus 로고    scopus 로고
    • Synthesis and analysis of potential prodrugs of coenzyme A analogues for the inhibition of the histone acetyltransferase p300
    • Cebrat M., et al. Synthesis and analysis of potential prodrugs of coenzyme A analogues for the inhibition of the histone acetyltransferase p300. Bioorg. Med. Chem. 11 (2003) 3307-3313
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 3307-3313
    • Cebrat, M.1
  • 46
    • 29044440879 scopus 로고    scopus 로고
    • Synthesis and evaluation of a potent and selective cell-permeable p300 histone acetyltransferase inhibitor
    • Zheng Y., et al. Synthesis and evaluation of a potent and selective cell-permeable p300 histone acetyltransferase inhibitor. J. Am. Chem. Soc. 127 (2005) 17182-17183
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17182-17183
    • Zheng, Y.1
  • 47
    • 0037805679 scopus 로고    scopus 로고
    • Small molecule modulators of histone acetyltransferase p300
    • Balasubramanyam K., et al. Small molecule modulators of histone acetyltransferase p300. J. Biol. Chem. 278 (2003) 19134-19140
    • (2003) J. Biol. Chem. , vol.278 , pp. 19134-19140
    • Balasubramanyam, K.1
  • 48
    • 4143089466 scopus 로고    scopus 로고
    • Implications of small molecule activators and inhibitors of histone acetyltransferases in chromatin therapy
    • Varier R.A., et al. Implications of small molecule activators and inhibitors of histone acetyltransferases in chromatin therapy. Biochem. Pharmacol. 68 (2004) 1215-1220
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 1215-1220
    • Varier, R.A.1
  • 49
    • 33644901007 scopus 로고    scopus 로고
    • Multiple biological activities of curcumin: a short review
    • Maheshwari R.K., et al. Multiple biological activities of curcumin: a short review. Life Sci. 78 (2006) 2081-2087
    • (2006) Life Sci. , vol.78 , pp. 2081-2087
    • Maheshwari, R.K.1
  • 50
    • 33746127271 scopus 로고    scopus 로고
    • Curcumin is an inhibitor of p300 histone acetyltransferase
    • Marcu M.G., et al. Curcumin is an inhibitor of p300 histone acetyltransferase. Med. Chem. 2 (2006) 169-174
    • (2006) Med. Chem. , vol.2 , pp. 169-174
    • Marcu, M.G.1
  • 51
    • 0035823497 scopus 로고    scopus 로고
    • Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity
    • Thompson P.R., et al. Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity. J. Biol. Chem. 276 (2001) 33721-33729
    • (2001) J. Biol. Chem. , vol.276 , pp. 33721-33729
    • Thompson, P.R.1
  • 52
    • 0035504278 scopus 로고    scopus 로고
    • Functional analysis of the p300 acetyltransferase domain: the PHD finger of p300 but not of CBP is dispensable for enzymatic activity
    • Bordoli L., et al. Functional analysis of the p300 acetyltransferase domain: the PHD finger of p300 but not of CBP is dispensable for enzymatic activity. Nucleic Acids Res. 29 (2001) 4462-4471
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4462-4471
    • Bordoli, L.1
  • 53
    • 15744370742 scopus 로고    scopus 로고
    • Curcumin-induced histone hypoacetylation: the role of reactive oxygen species
    • Kang J., et al. Curcumin-induced histone hypoacetylation: the role of reactive oxygen species. Biochem. Pharmacol. 69 (2005) 1205-1213
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 1205-1213
    • Kang, J.1
  • 54
    • 3042586299 scopus 로고    scopus 로고
    • Curcumin-induced apoptosis in scleroderma lung fibroblasts: role of protein kinase cepsilon
    • Tourkina E., et al. Curcumin-induced apoptosis in scleroderma lung fibroblasts: role of protein kinase cepsilon. Am. J. Respir. Cell Mol. Biol. 31 (2004) 28-35
    • (2004) Am. J. Respir. Cell Mol. Biol. , vol.31 , pp. 28-35
    • Tourkina, E.1
  • 55
    • 0037051106 scopus 로고    scopus 로고
    • Curcumin exerts multiple suppressive effects on human breast carcinoma cells
    • Shao Z.M., et al. Curcumin exerts multiple suppressive effects on human breast carcinoma cells. Int. J. Cancer 98 (2002) 234-240
    • (2002) Int. J. Cancer , vol.98 , pp. 234-240
    • Shao, Z.M.1
  • 56
    • 18044369271 scopus 로고    scopus 로고
    • Differential apoptotic and redox regulatory activities of curcumin and its derivatives
    • Mishra S., et al. Differential apoptotic and redox regulatory activities of curcumin and its derivatives. Free Radic. Biol. Med. 38 (2005) 1353-1360
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1353-1360
    • Mishra, S.1
  • 57
    • 18144364014 scopus 로고    scopus 로고
    • Anti-oxidant activities of curcumin and related enones
    • Weber W.M., et al. Anti-oxidant activities of curcumin and related enones. Bioorg. Med. Chem. 13 (2005) 3811-3820
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 3811-3820
    • Weber, W.M.1
  • 58
    • 6044276740 scopus 로고    scopus 로고
    • Phase I clinical trial of oral curcumin: biomarkers of systemic activity and compliance
    • Sharma R.A., et al. Phase I clinical trial of oral curcumin: biomarkers of systemic activity and compliance. Clin. Cancer Res. 10 (2004) 6847-6854
    • (2004) Clin. Cancer Res. , vol.10 , pp. 6847-6854
    • Sharma, R.A.1
  • 59
    • 33646028804 scopus 로고    scopus 로고
    • Molecular targets of dietary agents for prevention and therapy of cancer
    • Aggarwal B.B., and Shishodia S. Molecular targets of dietary agents for prevention and therapy of cancer. Biochem. Pharmacol. 71 (2006) 1397-1421
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 1397-1421
    • Aggarwal, B.B.1    Shishodia, S.2
  • 60
    • 0032926620 scopus 로고    scopus 로고
    • Biotransformation of curcumin through reduction and glucuronidation in mice
    • Pan M.H., et al. Biotransformation of curcumin through reduction and glucuronidation in mice. Drug Metab. Dispos. 27 (1999) 486-494
    • (1999) Drug Metab. Dispos. , vol.27 , pp. 486-494
    • Pan, M.H.1
  • 61
    • 4043146501 scopus 로고    scopus 로고
    • Polyisoprenylated benzophenone, garcinol, a natural histone acetyltransferase inhibitor, represses chromatin transcription and alters global gene expression
    • Balasubramanyam K., et al. Polyisoprenylated benzophenone, garcinol, a natural histone acetyltransferase inhibitor, represses chromatin transcription and alters global gene expression. J. Biol. Chem. 279 (2004) 33716-33726
    • (2004) J. Biol. Chem. , vol.279 , pp. 33716-33726
    • Balasubramanyam, K.1
  • 62
    • 0034836540 scopus 로고    scopus 로고
    • Induction of apoptosis by garcinol and curcumin through cytochrome C release and activation of caspases in human leukemia HL-60 cells
    • Pan M.-H., et al. Induction of apoptosis by garcinol and curcumin through cytochrome C release and activation of caspases in human leukemia HL-60 cells. J. Agric. Food Chem. 49 (2001) 1464-1474
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 1464-1474
    • Pan, M.-H.1
  • 63
    • 17444418982 scopus 로고    scopus 로고
    • Bioactive benzophenones from Garcinia xanthochymus fruits
    • Baggett S., et al. Bioactive benzophenones from Garcinia xanthochymus fruits. J. Nat. Prod. 68 (2005) 354-360
    • (2005) J. Nat. Prod. , vol.68 , pp. 354-360
    • Baggett, S.1
  • 64
    • 0034691064 scopus 로고    scopus 로고
    • St. John's wort induces hepatic drug metabolism through activation of the pregnane X receptor
    • Moore L.B., et al. St. John's wort induces hepatic drug metabolism through activation of the pregnane X receptor. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 7500-7502
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 7500-7502
    • Moore, L.B.1
  • 65
    • 0033826492 scopus 로고    scopus 로고
    • St John's wort, a herbal antidepressant, activates the steroid X receptor
    • Wentworth J.M., et al. St John's wort, a herbal antidepressant, activates the steroid X receptor. J. Endocrinol. 166 (2000) R11-R16
    • (2000) J. Endocrinol. , vol.166
    • Wentworth, J.M.1
  • 66
    • 0037482859 scopus 로고    scopus 로고
    • Hyperforin a constituent of St John's wort (Hypericum perforatum L.) extract induces apoptosis by triggering activation of caspases and with hypericin synergistically exerts cytotoxicity towards human malignant cell lines
    • Hostanska K., et al. Hyperforin a constituent of St John's wort (Hypericum perforatum L.) extract induces apoptosis by triggering activation of caspases and with hypericin synergistically exerts cytotoxicity towards human malignant cell lines. Eur. J. Pharm. Biopharm. 56 (2003) 121-132
    • (2003) Eur. J. Pharm. Biopharm. , vol.56 , pp. 121-132
    • Hostanska, K.1
  • 67
    • 8644228186 scopus 로고    scopus 로고
    • Inhibition of tumour cell growth by hyperforin, a novel anticancer drug from St. John's wort that acts by induction of apoptosis
    • Schempp C.M., et al. Inhibition of tumour cell growth by hyperforin, a novel anticancer drug from St. John's wort that acts by induction of apoptosis. Oncogene 21 (2002) 1242-1250
    • (2002) Oncogene , vol.21 , pp. 1242-1250
    • Schempp, C.M.1
  • 68
    • 12344280271 scopus 로고    scopus 로고
    • Aristoforin, a novel stable derivative of hyperforin, is a potent anticancer agent
    • Gartner M., et al. Aristoforin, a novel stable derivative of hyperforin, is a potent anticancer agent. ChemBioChem 6 (2005) 171-177
    • (2005) ChemBioChem , vol.6 , pp. 171-177
    • Gartner, M.1
  • 69
    • 4544318283 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of a small-molecule inhibitor of the histone acetyltransferase Gcn5
    • Biel M., et al. Design, synthesis, and biological evaluation of a small-molecule inhibitor of the histone acetyltransferase Gcn5. Angew. Chem. Int. Ed. Engl. 43 (2004) 3974-3976
    • (2004) Angew. Chem. Int. Ed. Engl. , vol.43 , pp. 3974-3976
    • Biel, M.1
  • 70
    • 27644473204 scopus 로고    scopus 로고
    • Isothiazolones as inhibitors of PCAF and p300 histone acetyltransferase activity
    • Stimson L., et al. Isothiazolones as inhibitors of PCAF and p300 histone acetyltransferase activity. Mol. Cancer Ther. 4 (2005) 1521-1532
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1521-1532
    • Stimson, L.1
  • 71
    • 27744593102 scopus 로고    scopus 로고
    • Potent inhibitors of LXXLL-based protein-protein interactions
    • Galande A.K., et al. Potent inhibitors of LXXLL-based protein-protein interactions. ChemBioChem 6 (2005) 1991-1998
    • (2005) ChemBioChem , vol.6 , pp. 1991-1998
    • Galande, A.K.1
  • 72
    • 1642581072 scopus 로고    scopus 로고
    • Design, synthesis, and in vitro biological evaluation of small molecule inhibitors of estrogen receptor alpha coactivator binding
    • Rodriguez A.L., et al. Design, synthesis, and in vitro biological evaluation of small molecule inhibitors of estrogen receptor alpha coactivator binding. J. Med. Chem. 47 (2004) 600-611
    • (2004) J. Med. Chem. , vol.47 , pp. 600-611
    • Rodriguez, A.L.1
  • 73
    • 2442502910 scopus 로고    scopus 로고
    • Identification of novel estrogen receptor alpha antagonists
    • Shao D., et al. Identification of novel estrogen receptor alpha antagonists. J. Steroid Biochem. Mol. Biol. 88 (2004) 351-360
    • (2004) J. Steroid Biochem. Mol. Biol. , vol.88 , pp. 351-360
    • Shao, D.1
  • 74
    • 30044433051 scopus 로고    scopus 로고
    • Discovery of small molecule inhibitors of the interaction of the thyroid hormone receptor with transcriptional coregulators
    • Arnold L.A., et al. Discovery of small molecule inhibitors of the interaction of the thyroid hormone receptor with transcriptional coregulators. J. Biol. Chem. 280 (2005) 43048-43055
    • (2005) J. Biol. Chem. , vol.280 , pp. 43048-43055
    • Arnold, L.A.1
  • 75
    • 0035794168 scopus 로고    scopus 로고
    • Core LXXLL motif sequences in CREB-binding protein, SRC1, and RIP140 define affinity and selectivity for steroid and retinoid receptors
    • Heery D.M., et al. Core LXXLL motif sequences in CREB-binding protein, SRC1, and RIP140 define affinity and selectivity for steroid and retinoid receptors. J. Biol. Chem. 276 (2001) 6695-6702
    • (2001) J. Biol. Chem. , vol.276 , pp. 6695-6702
    • Heery, D.M.1
  • 76
    • 0038514176 scopus 로고    scopus 로고
    • An extended LXXLL motif sequence determines the nuclear receptor binding specificity of TRAP220
    • Coulthard V.H., et al. An extended LXXLL motif sequence determines the nuclear receptor binding specificity of TRAP220. J. Biol. Chem. 278 (2003) 10942-10951
    • (2003) J. Biol. Chem. , vol.278 , pp. 10942-10951
    • Coulthard, V.H.1
  • 77
    • 0037138363 scopus 로고    scopus 로고
    • Bromodomain: an acetyl-lysine binding domain
    • Zeng L., and Zhou M.M. Bromodomain: an acetyl-lysine binding domain. FEBS Lett. 513 (2002) 124-128
    • (2002) FEBS Lett. , vol.513 , pp. 124-128
    • Zeng, L.1    Zhou, M.M.2
  • 78
    • 0034669210 scopus 로고    scopus 로고
    • The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p
    • Owen D.J., et al. The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p. EMBO J. 19 (2000) 6141-6149
    • (2000) EMBO J. , vol.19 , pp. 6141-6149
    • Owen, D.J.1
  • 79
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • Dhalluin C., et al. Structure and ligand of a histone acetyltransferase bromodomain. Nature 399 (1999) 491-496
    • (1999) Nature , vol.399 , pp. 491-496
    • Dhalluin, C.1
  • 80
    • 10744233648 scopus 로고    scopus 로고
    • Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation
    • Mujtaba S., et al. Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation. Mol. Cell 13 (2004) 251-263
    • (2004) Mol. Cell , vol.13 , pp. 251-263
    • Mujtaba, S.1
  • 81
    • 0034717183 scopus 로고    scopus 로고
    • Structure and function of a human TAFII250 double bromodomain module
    • Jacobson R.H., et al. Structure and function of a human TAFII250 double bromodomain module. Science 288 (2000) 1422-1425
    • (2000) Science , vol.288 , pp. 1422-1425
    • Jacobson, R.H.1
  • 82
    • 0036206045 scopus 로고    scopus 로고
    • Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain
    • Mujtaba S., et al. Structural basis of lysine-acetylated HIV-1 Tat recognition by PCAF bromodomain. Mol. Cell 9 (2002) 575-586
    • (2002) Mol. Cell , vol.9 , pp. 575-586
    • Mujtaba, S.1
  • 83
    • 0034387879 scopus 로고    scopus 로고
    • Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
    • Hudson B.P., et al. Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain. J. Mol. Biol. 304 (2000) 355-370
    • (2000) J. Mol. Biol. , vol.304 , pp. 355-370
    • Hudson, B.P.1
  • 84
    • 30744456492 scopus 로고    scopus 로고
    • Target structure-based discovery of small molecules that block human p53 and CREB binding protein association
    • Sachchidanand R.-S.L., et al. Target structure-based discovery of small molecules that block human p53 and CREB binding protein association. Chem. Biol. 13 (2006) 81-90
    • (2006) Chem. Biol. , vol.13 , pp. 81-90
    • Sachchidanand, R.-S.L.1
  • 85
    • 14744276712 scopus 로고    scopus 로고
    • Selective small molecules blocking HIV-1 Tat and coactivator PCAF association
    • Zeng L., et al. Selective small molecules blocking HIV-1 Tat and coactivator PCAF association. J. Am. Chem. Soc. 127 (2005) 2376-2377
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2376-2377
    • Zeng, L.1
  • 86
    • 33644856123 scopus 로고    scopus 로고
    • Epigenetic therapy of cancer: past, present and future
    • Yoo C.B., and Jones P.A. Epigenetic therapy of cancer: past, present and future. Nat. Rev. Drug Discov. 5 (2006) 37-50
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 37-50
    • Yoo, C.B.1    Jones, P.A.2
  • 87
    • 25144452721 scopus 로고    scopus 로고
    • Chemical approaches to transcriptional regulation
    • Majmudar C.Y., and Mapp A.K. Chemical approaches to transcriptional regulation. Curr. Opin. Chem. Biol. 9 (2005) 467-474
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 467-474
    • Majmudar, C.Y.1    Mapp, A.K.2
  • 88
    • 0028885077 scopus 로고
    • Identification of a gene encoding a yeast histone H4 acetyltransferase
    • Kleff S., et al. Identification of a gene encoding a yeast histone H4 acetyltransferase. J. Biol. Chem. 270 (1995) 24674-24677
    • (1995) J. Biol. Chem. , vol.270 , pp. 24674-24677
    • Kleff, S.1
  • 89
    • 0037242383 scopus 로고    scopus 로고
    • The MYST family of histone acetyltransferases
    • Utley R.T., and Cote J. The MYST family of histone acetyltransferases. Curr. Top. Microbiol. Immunol. 274 (2003) 203-236
    • (2003) Curr. Top. Microbiol. Immunol. , vol.274 , pp. 203-236
    • Utley, R.T.1    Cote, J.2
  • 90
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell J.E., et al. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84 (1996) 843-851
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1
  • 91
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang X.J., et al. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382 (1996) 319-324
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1
  • 92
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko V.V., et al. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87 (1996) 953-959
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1
  • 93
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister A.J., and Kouzarides T. The CBP co-activator is a histone acetyltransferase. Nature 384 (1996) 641-643
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 94
    • 0030768745 scopus 로고    scopus 로고
    • Steroid receptor coactivator-1 is a histone acetyltransferase
    • Spencer T.E., et al. Steroid receptor coactivator-1 is a histone acetyltransferase. Nature 389 (1997) 194-198
    • (1997) Nature , vol.389 , pp. 194-198
    • Spencer, T.E.1
  • 95
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen H., et al. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90 (1997) 569-580
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1
  • 96
    • 0032744688 scopus 로고    scopus 로고
    • The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity
    • Hsieh Y.J., et al. The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity. Mol. Cell. Biol. 19 (1999) 7697-7704
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7697-7704
    • Hsieh, Y.J.1
  • 97
    • 0034636554 scopus 로고    scopus 로고
    • ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation
    • Kawasaki H., et al. ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation. Nature 405 (2000) 195-200
    • (2000) Nature , vol.405 , pp. 195-200
    • Kawasaki, H.1
  • 98
    • 0035106263 scopus 로고    scopus 로고
    • Transcriptional coactivator, CIITA, is an acetyltransferase that bypasses a promoter requirement for TAF(II)250
    • Raval A., et al. Transcriptional coactivator, CIITA, is an acetyltransferase that bypasses a promoter requirement for TAF(II)250. Mol. Cell 7 (2001) 105-115
    • (2001) Mol. Cell , vol.7 , pp. 105-115
    • Raval, A.1
  • 99
    • 0030447943 scopus 로고    scopus 로고
    • The TAF(II)250 subunit of TFIID has histone acetyltransferase activity
    • Mizzen C.A., et al. The TAF(II)250 subunit of TFIID has histone acetyltransferase activity. Cell 87 (1996) 1261-1270
    • (1996) Cell , vol.87 , pp. 1261-1270
    • Mizzen, C.A.1
  • 100
    • 0037173065 scopus 로고    scopus 로고
    • Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis
    • Lahn B.T., et al. Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 8707-8712
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 8707-8712
    • Lahn, B.T.1
  • 101
    • 0042358902 scopus 로고    scopus 로고
    • Transcription factor IIB acetylates itself to regulate transcription
    • Choi C.H., et al. Transcription factor IIB acetylates itself to regulate transcription. Nature 424 (2003) 965-969
    • (2003) Nature , vol.424 , pp. 965-969
    • Choi, C.H.1
  • 102
    • 0035097884 scopus 로고    scopus 로고
    • MCM3AP, a novel acetyltransferase that acetylates replication protein MCM3
    • Takei Y., et al. MCM3AP, a novel acetyltransferase that acetylates replication protein MCM3. EMBO Rep. 2 (2001) 119-123
    • (2001) EMBO Rep. , vol.2 , pp. 119-123
    • Takei, Y.1
  • 103
    • 0037133040 scopus 로고    scopus 로고
    • Eco1 is a novel acetyltransferase that can acetylate proteins involved in cohesion
    • Ivanov D., et al. Eco1 is a novel acetyltransferase that can acetylate proteins involved in cohesion. Curr. Biol. 12 (2002) 323-328
    • (2002) Curr. Biol. , vol.12 , pp. 323-328
    • Ivanov, D.1
  • 104
    • 18744375998 scopus 로고    scopus 로고
    • Regulation and destabilization of HIF-1α by ARD1-mediated acetylation
    • Jeong J.W., et al. Regulation and destabilization of HIF-1α by ARD1-mediated acetylation. Cell 111 (2002) 709-720
    • (2002) Cell , vol.111 , pp. 709-720
    • Jeong, J.W.1
  • 105
    • 33646145721 scopus 로고    scopus 로고
    • Circadian regulator CLOCK is a histone acetyltransferase
    • Doi M., et al. Circadian regulator CLOCK is a histone acetyltransferase. Cell 125 (2006) 497-508
    • (2006) Cell , vol.125 , pp. 497-508
    • Doi, M.1
  • 106
    • 0037195124 scopus 로고    scopus 로고
    • Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor
    • Poux A.N., et al. Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 14065-14070
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14065-14070
    • Poux, A.N.1
  • 107
    • 11144246904 scopus 로고    scopus 로고
    • Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities
    • Toleman C., et al. Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities. J. Biol. Chem. 279 (2004) 53665-53673
    • (2004) J. Biol. Chem. , vol.279 , pp. 53665-53673
    • Toleman, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.