메뉴 건너뛰기




Volumn 13, Issue 5, 2009, Pages 826-852

Targeting histone deacetylases for the treatment of disease: Epigenetics Review Series

Author keywords

Cancer; Chromatin; Disease; Histone deacetylase; Targeting

Indexed keywords

ANTIDIABETIC AGENT; ANTINEOPLASTIC AGENT; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; NONSTEROID ANTIINFLAMMATORY AGENT;

EID: 67249116835     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1582-4934.2008.00571.x     Document Type: Article
Times cited : (41)

References (359)
  • 1
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. Translating the histone code. Science. 2001 293 : 1074 80.
    • (2001) Science. , vol.293 , pp. 1074-80
    • Jenuwein, T.1    Allis, C.D.2
  • 2
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. The language of covalent histone modifications. Nature. 2000 403 : 41 5.
    • (2000) Nature. , vol.403 , pp. 41-5
    • Strahl, B.D.1    Allis, C.D.2
  • 3
    • 33845877732 scopus 로고    scopus 로고
    • Defining an epigenetic code
    • DOI 10.1038/ncb0107-2, PII NCB0107-2
    • Turner BM. Defining an epigenetic code. Nat Cell Biol. 2007 9 : 2 6. (Pubitemid 46024187)
    • (2007) Nature Cell Biology , vol.9 , Issue.1 , pp. 2-6
    • Turner, B.M.1
  • 4
    • 33947532026 scopus 로고    scopus 로고
    • Histone acetyl-transferase complexes: One size doesn't fit all
    • Lee KK, Workman JL. Histone acetyl-transferase complexes: one size doesn't fit all. Nat Rev Mol Cell Biol. 2007 8 : 284 95.
    • (2007) Nat Rev Mol Cell Biol. , vol.8 , pp. 284-95
    • Lee, K.K.1    Workman, J.L.2
  • 6
    • 0035862199 scopus 로고    scopus 로고
    • The human histone deacetylase family
    • DOI 10.1006/excr.2000.5080
    • Gray SG, Ekström TJ. The human histone deacetylase family. Exp Cell Res. 2001 262 : 75 83. (Pubitemid 32980246)
    • (2001) Experimental Cell Research , vol.262 , Issue.2 , pp. 75-83
    • Gray, S.G.1    Ekstrom, T.J.2
  • 7
    • 34249793710 scopus 로고    scopus 로고
    • Reversible acetylation of non histone proteins: Role in cellular function and disease
    • Batta K, Das C, Gadad S, Shandilya J, Kundu TK. Reversible acetylation of non histone proteins: role in cellular function and disease. Subcell Biochem. 2007 41 : 193 212.
    • (2007) Subcell Biochem. , vol.41 , pp. 193-212
    • Batta, K.1    Das, C.2    Gadad, S.3    Shandilya, J.4    Kundu, T.K.5
  • 8
    • 38049016277 scopus 로고    scopus 로고
    • A shifting paradigm: Histone deacetylases and transcriptional actiation
    • Smith CL. A shifting paradigm: histone deacetylases and transcriptional actiation. Bioessays. 2008 30 : 15 24.
    • (2008) Bioessays. , vol.30 , pp. 15-24
    • Smith, C.L.1
  • 10
    • 42049103914 scopus 로고    scopus 로고
    • From natural products to small molecule ketone histone deacetylase inhibitors: Development of new class specific agents
    • Jones P, Steinkuhler C. From natural products to small molecule ketone histone deacetylase inhibitors: development of new class specific agents. Curr Pharm Des. 2008 14 : 545 61.
    • (2008) Curr Pharm Des. , vol.14 , pp. 545-61
    • Jones, P.1    Steinkuhler, C.2
  • 11
    • 35648983903 scopus 로고    scopus 로고
    • Inflammation and cancer: An ancient link with novel potentials
    • Perwez Hussain S, Harris CC. Inflammation and cancer: an ancient link with novel potentials. Int J Cancer. 2007 121 : 2373 80.
    • (2007) Int J Cancer. , vol.121 , pp. 2373-80
    • Perwez Hussain, S.1    Harris, C.C.2
  • 12
    • 33745298519 scopus 로고    scopus 로고
    • Nuclear factor-kappaB in cancer development and progression
    • Karin M. Nuclear factor-kappaB in cancer development and progression. Nature. 2006 441 : 431 6.
    • (2006) Nature. , vol.441 , pp. 431-6
    • Karin, M.1
  • 13
    • 34250773451 scopus 로고    scopus 로고
    • Mechanisms of obesity-associated insulin resistance: Many choices on the menu
    • Qatanani M, Lazar MA. Mechanisms of obesity-associated insulin resistance: many choices on the menu. Genes Dev. 2007 21 : 1443 55.
    • (2007) Genes Dev. , vol.21 , pp. 1443-55
    • Qatanani, M.1    Lazar, M.A.2
  • 14
    • 33847625011 scopus 로고    scopus 로고
    • The interplay between inflammation and neurodegeneration in CNS disease
    • DOI 10.1016/j.jneuroim.2006.11.013, PII S0165572806004644, Inflammation, Neurodegeneration and Neuroprotection in the Central Nervous System
    • Esiri MM. The interplay between inflammation and neurodegeneration in CNS disease. J Neuroimmunol. 2007 184 : 4 16. (Pubitemid 46365987)
    • (2007) Journal of Neuroimmunology , vol.184 , Issue.1-2 , pp. 4-16
    • Esiri, M.M.1
  • 16
    • 0030614504 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by cyclin-dependent kinases associated with the p300 coactivator
    • Perkins ND, Felzien LK, Betts JC, Leung K, Beach DH, Nabel GJ. Regulation of NF-kappaB by cyclin-dependent kinases associated with the p300 coactivator. Science. 1997 275 : 523 7.
    • (1997) Science. , vol.275 , pp. 523-7
    • Perkins, N.D.1    Felzien, L.K.2    Betts, J.C.3    Leung, K.4    Beach, D.H.5    Nabel, G.J.6
  • 18
    • 0032231652 scopus 로고    scopus 로고
    • Rett syndrome: Confirmation of X-linked dominant inheritance, and localization of the gene to Xq28
    • Sirianni N, Naidu S, Pereira J, Pillotto RF, Hoffman E P. Rett syndrome: confirmation of X-linked dominant inheritance, and localization of the gene to Xq28. Am J Hum Genet. 1998 63 : 1552 8.
    • (1998) Am J Hum Genet. , vol.63 , pp. 1552-8
    • Sirianni, N.1    Naidu, S.2    Pereira, J.3    Pillotto, R.F.4    Hoffman, E.P.5
  • 19
    • 0034802887 scopus 로고    scopus 로고
    • The p65 (RelA) subunit of NF-kappaB interacts with the histone deacety-lase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression
    • Ashburner BP, Westerheide SD, Baldwin AS Jr. The p65 (RelA) subunit of NF-kappaB interacts with the histone deacety-lase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression. Mol Cell Biol. 2001 21 : 7065 77.
    • (2001) Mol Cell Biol. , vol.21 , pp. 7065-77
    • Ashburner, B.P.1    Westerheide, S.D.2    Baldwin Jr., A.S.3
  • 21
    • 33847060910 scopus 로고    scopus 로고
    • Sirtuin regulates cigarette smoke-induced proin-flammatory mediator release via RelA-p65 NF-kappaB in macrophages in vitro and in rat lungs in vivo: Implications for chronic inflammation and aging
    • Yang SR, Wright J, Bauter M, Seweryniak K, Kode A, Rahman I. Sirtuin regulates cigarette smoke-induced proin-flammatory mediator release via RelA-p65 NF-kappaB in macrophages in vitro and in rat lungs in vivo: implications for chronic inflammation and aging. Am J Physiol Lung Cell Mol Physiol. 2007 292 : L567 76.
    • (2007) Am J Physiol Lung Cell Mol Physiol. , vol.292 , pp. 567-76
    • Yang, S.R.1    Wright, J.2    Bauter, M.3    Seweryniak, K.4    Kode, A.5    Rahman, I.6
  • 22
    • 30744458869 scopus 로고    scopus 로고
    • IkappaB kinase alpha-mediated dere-pression of SMRT potentiates acetylation of RelA-p65 by p300
    • Hoberg JE, Popko AE, Ramsey CS, Mayo MW. IkappaB kinase alpha-mediated dere-pression of SMRT potentiates acetylation of RelA-p65 by p300. Mol Cell Biol. 2006 26 : 457 71.
    • (2006) Mol Cell Biol. , vol.26 , pp. 457-71
    • Hoberg, J.E.1    Popko, A.E.2    Ramsey, C.S.3    Mayo, M.W.4
  • 23
    • 6344241039 scopus 로고    scopus 로고
    • SMRT derepression by the IkappaB kinase alpha: A prerequisite to NF-kappaB transcription and survival
    • Hoberg JE, Yeung F, Mayo MW. SMRT derepression by the IkappaB kinase alpha: a prerequisite to NF-kappaB transcription and survival. Mol Cell. 2004 16 : 245 55.
    • (2004) Mol Cell. , vol.16 , pp. 245-55
    • Hoberg, J.E.1    Yeung, F.2    Mayo, M.W.3
  • 25
    • 0037101953 scopus 로고    scopus 로고
    • Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek
    • Hollenbach AD, McPherson CJ, Mientjes EJ, Iyengar R, Grosveld G. Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek. J Cell Sci. 2002 115 : 3319 30.
    • (2002) J Cell Sci. , vol.115 , pp. 3319-30
    • Hollenbach, A.D.1    McPherson, C.J.2    Mientjes, E.J.3    Iyengar, R.4    Grosveld, G.5
  • 26
    • 28044437730 scopus 로고    scopus 로고
    • SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx
    • Kuo HY, Chang CC, Jeng JC, Hu HM, Lin DY, Maul GG, Kwok RP, Shih HM. SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx. Proc Natl Acad Sci USA. 2005 102 : 16973 8.
    • (2005) Proc Natl Acad Sci USA. , vol.102 , pp. 16973-8
    • Kuo, H.Y.1    Chang, C.C.2    Jeng, J.C.3    Hu, H.M.4    Lin, D.Y.5    Maul, G.G.6    Kwok, R.P.7    Shih, H.M.8
  • 29
    • 0348222671 scopus 로고    scopus 로고
    • Inflammation: The link between insulin resistance, obesity and diabetes
    • DOI 10.1016/j.it.2003.10.013
    • Dandona P, Aljada A, Bandyopadhyay A. Inflammation: the link between insulin resistance, obesity and diabetes. Trends Immunol. 2004 25 : 4 7. (Pubitemid 38032801)
    • (2004) Trends in Immunology , vol.25 , Issue.1 , pp. 4-7
    • Dandona, P.1    Aljada, A.2    Bandyopadhyay, A.3
  • 30
    • 0033527448 scopus 로고    scopus 로고
    • The nuclear factor-kappa B engages CBP-p300 and histone acetyltransferase activity for transcriptional activation of the interleukin-6 gene promoter
    • Vanden Berghe W, De Bosscher K, Boone E, Plaisance S, Haegeman G. The nuclear factor-kappa B engages CBP-p300 and histone acetyltransferase activity for transcriptional activation of the interleukin-6 gene promoter. J Biol Chem. 1999 274 : 32091 8.
    • (1999) J Biol Chem. , vol.274 , pp. 32091-8
    • Vanden Berghe, W.1    De Bosscher, K.2    Boone, E.3    Plaisance, S.4    Haegeman, G.5
  • 31
    • 33845207648 scopus 로고    scopus 로고
    • Breast cancer metastasis suppressor 1 functions as a corepressor by enhancing histone deacetylase 1-mediated deacetylation of RelA-p65 and promoting apoptosis
    • Liu Y, Smith PW, Jones DR. Breast cancer metastasis suppressor 1 functions as a corepressor by enhancing histone deacetylase 1-mediated deacetylation of RelA-p65 and promoting apoptosis. Mol Cell Biol. 2006 26 : 8683 96.
    • (2006) Mol Cell Biol. , vol.26 , pp. 8683-96
    • Liu, Y.1    Smith, P.W.2    Jones, D.R.3
  • 32
    • 46149125241 scopus 로고    scopus 로고
    • A pervasive role of histone acetyltransferases and deacetylases in an NF-kappaB-signaling code
    • Calao M, Burny A, Quivy V, Dekoninck A, Van Lint C. A pervasive role of histone acetyltransferases and deacetylases in an NF-kappaB-signaling code. Trends Biochem Sci. 2008 33 : 339 49.
    • (2008) Trends Biochem Sci. , vol.33 , pp. 339-49
    • Calao, M.1    Burny, A.2    Quivy, V.3    Dekoninck, A.4    Van Lint, C.5
  • 34
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • Hebert DN, Molinari M. In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol Rev. 2007 87 : 1377 408.
    • (2007) Physiol Rev. , vol.87 , pp. 1377-408
    • Hebert, D.N.1    Molinari, M.2
  • 35
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport TA. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature. 2007 450 : 663 9.
    • (2007) Nature. , vol.450 , pp. 663-9
    • Rapoport, T.A.1
  • 36
    • 34447527676 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Signaling the unfolded protein response
    • Lai E, Teodoro T, Volchuk A. Endoplasmic reticulum stress: signaling the unfolded protein response. Physiology (Bethesda). 2007 22 : 193 201.
    • (2007) Physiology (Bethesda). , vol.22 , pp. 193-201
    • Lai, E.1    Teodoro, T.2    Volchuk, A.3
  • 37
    • 38449105601 scopus 로고    scopus 로고
    • Systems biology of the endoplasmic reticulum stress response
    • Caruso ME, Chevet E. Systems biology of the endoplasmic reticulum stress response. Subcell Biochem. 2007 43 : 277 98.
    • (2007) Subcell Biochem. , vol.43 , pp. 277-98
    • Caruso, M.E.1    Chevet, E.2
  • 38
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol. 2007 8 : 519 29.
    • (2007) Nat Rev Mol Cell Biol. , vol.8 , pp. 519-29
    • Ron, D.1    Walter, P.2
  • 39
    • 0031081340 scopus 로고    scopus 로고
    • The ER-overload response: Activation of NF-kappa B
    • Pahl HL, Baeuerle PA. The ER-overload response: activation of NF-kappa B. Trends Biochem Sci. 1997 22 : 63 7.
    • (1997) Trends Biochem Sci. , vol.22 , pp. 63-7
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 40
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • Xu C, Bailly-Maitre B, Reed JC. Endoplasmic reticulum stress: cell life and death decisions. J Clin Invest. 2005 115 : 2656 64.
    • (2005) J Clin Invest. , vol.115 , pp. 2656-64
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 41
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • Rao RV, Ellerby HM, Bredesen DE. Coupling endoplasmic reticulum stress to the cell death program. Cell Death Differ. 2004 11 : 372 80.
    • (2004) Cell Death Differ. , vol.11 , pp. 372-80
    • Rao, R.V.1    Ellerby, H.M.2    Bredesen, D.E.3
  • 42
    • 39149104320 scopus 로고    scopus 로고
    • The role for endoplasmic reticulum stress in diabetes mellitus
    • Eizirik DL, Cardozo AK, Cnop M. The role for endoplasmic reticulum stress in diabetes mellitus. Endocr Rev. 2007 29 : 42 61.
    • (2007) Endocr Rev. , vol.29 , pp. 42-61
    • Eizirik, D.L.1    Cardozo, A.K.2    Cnop, M.3
  • 43
    • 34247098374 scopus 로고    scopus 로고
    • Accumulation of misfolded protein through nitrosative stress linked to neurodegenerative disorders
    • DOI 10.1089/ars.2006.1517
    • Uehara T. Accumulation of misfolded protein through nitrosative stress linked to neurodegenerative disorders. Antioxid Redox Signal. 2007 9 : 597 601. (Pubitemid 46598257)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.5 , pp. 597-601
    • Uehara, T.1
  • 44
    • 38849146956 scopus 로고    scopus 로고
    • ER and oxidative stresses are common mediators of apoptosis in both neurodegenerative and non-neurodegenerative lysosomal storage disorders and are alleviated by chemical chaperones
    • Wei H, Kim SJ, Zhang Z, Tsai PC, Wisniewski KE, Mukherjee AB. ER and oxidative stresses are common mediators of apoptosis in both neurodegenerative and non-neurodegenerative lysosomal storage disorders and are alleviated by chemical chaperones. Hum Mol Genet. 2008 17 : 469 77.
    • (2008) Hum Mol Genet. , vol.17 , pp. 469-77
    • Wei, H.1    Kim, S.J.2    Zhang, Z.3    Tsai, P.C.4    Wisniewski, K.E.5    Mukherjee, A.B.6
  • 45
    • 36348943088 scopus 로고    scopus 로고
    • Integrated endoplasmic reticulum stress responses in cancer
    • Moenner M, Pluquet O, Bouchecareilh M, Chevet E. Integrated endoplasmic reticulum stress responses in cancer. Cancer Res. 2007 67 : 10631 4.
    • (2007) Cancer Res. , vol.67 , pp. 10631-4
    • Moenner, M.1    Pluquet, O.2    Bouchecareilh, M.3    Chevet, E.4
  • 46
    • 34548213726 scopus 로고    scopus 로고
    • Mallory body formation is associated with epigenetic phenotypic change in hepatocytes in vivo
    • Bardag-Gorce F, Dedes J, French BA, Oliva JV, Li J, French SW. Mallory body formation is associated with epigenetic phenotypic change in hepatocytes in vivo. Exp Mol Pathol. 2007 83 : 160 8.
    • (2007) Exp Mol Pathol. , vol.83 , pp. 160-8
    • Bardag-Gorce, F.1    Dedes, J.2    French, B.A.3    Oliva, J.V.4    Li, J.5    French, S.W.6
  • 48
    • 37249059260 scopus 로고    scopus 로고
    • Critical and functional regulation of CHOP (C-EBP homologous protein) through the N-terminal portion
    • Ohoka N, Hattori T, Kitagawa M, Onozaki K, Hayashi H. Critical and functional regulation of CHOP (C-EBP homologous protein) through the N-terminal portion. J Biol Chem. 2007 282 : 35687 94.
    • (2007) J Biol Chem. , vol.282 , pp. 35687-94
    • Ohoka, N.1    Hattori, T.2    Kitagawa, M.3    Onozaki, K.4    Hayashi, H.5
  • 49
    • 18944390015 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induction of the Grp78-BiP promoter: Activating mechanisms mediated by YY1 and its interactive chromatin modifiers
    • Baumeister P, Luo S, Skarnes WC, Sui G, Seto E, Shi Y, Lee AS. Endoplasmic reticulum stress induction of the Grp78-BiP promoter: activating mechanisms mediated by YY1 and its interactive chromatin modifiers. Mol Cell Biol. 2005 25 : 4529 40.
    • (2005) Mol Cell Biol. , vol.25 , pp. 4529-40
    • Baumeister, P.1    Luo, S.2    Skarnes, W.C.3    Sui, G.4    Seto, E.5    Shi, Y.6    Lee, A.S.7
  • 50
    • 33745135117 scopus 로고    scopus 로고
    • Dynamic recruitment of transcription factors and epigenetic changes on the ER stress response gene promoters
    • Donati G, Imbriano C, Mantovani R. Dynamic recruitment of transcription factors and epigenetic changes on the ER stress response gene promoters. Nucleic Acids Res. 2006 34 : 3116 27.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3116-27
    • Donati, G.1    Imbriano, C.2    Mantovani, R.3
  • 51
    • 33745381226 scopus 로고    scopus 로고
    • BLIMP-1 is a target of cellular stress and downstream of the unfolded protein response
    • Doody GM, Stephenson S, Tooze RM. BLIMP-1 is a target of cellular stress and downstream of the unfolded protein response. Eur J Immunol. 2006 36 : 1572 82.
    • (2006) Eur J Immunol. , vol.36 , pp. 1572-82
    • Doody, G.M.1    Stephenson, S.2    Tooze, R.M.3
  • 52
    • 0034073382 scopus 로고    scopus 로고
    • Transcriptional repression by blimp-1 (PRDI-BF1) involves recruitment of histone deacetylase
    • Yu J, Angelin-Duclos C, Greenwood J, Liao J, Calame K. Transcriptional repression by blimp-1 (PRDI-BF1) involves recruitment of histone deacetylase. Mol Cell Biol. 2000 20 : 2592 603.
    • (2000) Mol Cell Biol. , vol.20 , pp. 2592-603
    • Yu, J.1    Angelin-Duclos, C.2    Greenwood, J.3    Liao, J.4    Calame, K.5
  • 53
    • 0034099743 scopus 로고    scopus 로고
    • Sodium 4-phenylbutyrate downregulates Hsc70: Implications for intracellular trafficking of DeltaF508-CFTR
    • Rubenstein RC, Zeitlin PL. Sodium 4-phenylbutyrate downregulates Hsc70: implications for intracellular trafficking of DeltaF508-CFTR. Am J Physiol Cell Physiol. 2000 278 : C259 67.
    • (2000) Am J Physiol Cell Physiol. , vol.278 , pp. 259-67
    • Rubenstein, R.C.1    Zeitlin, P.L.2
  • 54
    • 0034652248 scopus 로고    scopus 로고
    • Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency
    • Burrows JA, Willis LK, Perlmutter DH. Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: a potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency. Proc Natl Acad Sci USA. 2000 97 : 1796 801.
    • (2000) Proc Natl Acad Sci USA. , vol.97 , pp. 1796-801
    • Burrows, J.A.1    Willis, L.K.2    Perlmutter, D.H.3
  • 55
    • 4844224132 scopus 로고    scopus 로고
    • Sodium 4-phenylbutyrate protects against cerebral ischemic injury
    • DOI 10.1124/mol.104.001339
    • Qi X, Hosoi T, Okuma Y, Kaneko M, Nomura Y. Sodium 4-phenylbutyrate protects against cerebral ischemic injury. Mol Pharmacol. 2004 66 : 899 908. (Pubitemid 39319462)
    • (2004) Molecular Pharmacology , vol.66 , Issue.4 , pp. 899-908
    • Qi, X.1    Hosoi, T.2    Okuma, Y.3    Kaneko, M.4    Nomura, Y.5
  • 56
    • 24344495336 scopus 로고    scopus 로고
    • Sodium 4-phenylbutyrate protects against liver ischemia reperfusion injury by inhibition of endoplasmic reticulum-stress mediated apoptosis
    • Vilatoba M, Eckstein C, Bilbao G, Smyth CA, Jenkins S, Thompson JA, Eckhoff DE, Contreras JL. Sodium 4-phenylbutyrate protects against liver ischemia reperfusion injury by inhibition of endoplasmic reticulum-stress mediated apoptosis. Surgery. 2005 138 : 342 51.
    • (2005) Surgery. , vol.138 , pp. 342-51
    • Vilatoba, M.1    Eckstein, C.2    Bilbao, G.3    Smyth, C.A.4    Jenkins, S.5    Thompson, J.A.6    Eckhoff, D.E.7    Contreras, J.L.8
  • 57
    • 34547881945 scopus 로고    scopus 로고
    • Cellular osmolytes reduce lens epithelial cell death and alleviate cataract formation in galactosemic rats
    • Mulhern ML, Madson CJ, Kador PF, Randazzo J, Shinohara T. Cellular osmolytes reduce lens epithelial cell death and alleviate cataract formation in galactosemic rats. Mol Vis. 2007 13 : 1397 405.
    • (2007) Mol Vis. , vol.13 , pp. 1397-405
    • Mulhern, M.L.1    Madson, C.J.2    Kador, P.F.3    Randazzo, J.4    Shinohara, T.5
  • 59
    • 4344597286 scopus 로고    scopus 로고
    • Chemical chaperones protect from effects of apoptosis-inducing mutation in carbonic anhydrase IV identified in retinitis pigmentosa 17
    • Bonapace G, Waheed A, Shah GN, Sly WS. Chemical chaperones protect from effects of apoptosis-inducing mutation in carbonic anhydrase IV identified in retinitis pigmentosa 17. Proc Natl Acad Sci USA. 2004 101 : 12300 5.
    • (2004) Proc Natl Acad Sci USA. , vol.101 , pp. 12300-5
    • Bonapace, G.1    Waheed, A.2    Shah, G.N.3    Sly, W.S.4
  • 60
    • 34248376062 scopus 로고    scopus 로고
    • Sodium 4-phenylbutyrate acts as a chemical chaperone on misfolded myocilin to rescue cells from endoplasmic reticulum stress and apoptosis
    • Yam GH, Gaplovska-Kysela K, Zuber C, Roth J. Sodium 4-phenylbutyrate acts as a chemical chaperone on misfolded myocilin to rescue cells from endoplasmic reticulum stress and apoptosis. Invest Ophthalmol Vis Sci. 2007 48 : 1683 90.
    • (2007) Invest Ophthalmol Vis Sci. , vol.48 , pp. 1683-90
    • Yam, G.H.1    Gaplovska-Kysela, K.2    Zuber, C.3    Roth, J.4
  • 61
    • 33745190973 scopus 로고    scopus 로고
    • Selective inhibition of endoplasmic reticulum-associated degradation rescues DeltaF508-cystic fibrosis transmembrane regulator and suppresses interleukin-8 levels: Therapeutic implications
    • Vij N, Fang S, Zeitlin PL. Selective inhibition of endoplasmic reticulum-associated degradation rescues DeltaF508-cystic fibrosis transmembrane regulator and suppresses interleukin-8 levels: therapeutic implications. J Biol Chem. 2006 281 : 17369 78.
    • (2006) J Biol Chem. , vol.281 , pp. 17369-78
    • Vij, N.1    Fang, S.2    Zeitlin, P.L.3
  • 64
    • 0033050865 scopus 로고    scopus 로고
    • Differential display PCR reveals novel targets for the mood-stabilizing drug valproate including the molecular chaperone GRP78
    • Wang JF, Bown C, Young LT. Differential display PCR reveals novel targets for the mood-stabilizing drug valproate including the molecular chaperone GRP78. Mol Pharmacol. 1999 55 : 521 7.
    • (1999) Mol Pharmacol. , vol.55 , pp. 521-7
    • Wang, J.F.1    Bown, C.2    Young, L.T.3
  • 65
    • 0033845743 scopus 로고    scopus 로고
    • Increased expression of endoplasmic reticulum stress proteins following chronic valproate treatment of rat C6 glioma cells
    • Bown CD, Wang JF, Young LT. Increased expression of endoplasmic reticulum stress proteins following chronic valproate treatment of rat C6 glioma cells. Neuropharmacology. 2000 39 : 2162 9.
    • (2000) Neuropharmacology. , vol.39 , pp. 2162-9
    • Bown, C.D.1    Wang, J.F.2    Young, L.T.3
  • 66
    • 0034307061 scopus 로고    scopus 로고
    • Chronic valproate treatment increases expression of endoplasmic reticulum stress proteins in the rat cerebral cortex and hippocampus
    • Chen B, Wang JF, Young LT. Chronic valproate treatment increases expression of endoplasmic reticulum stress proteins in the rat cerebral cortex and hippocampus. Biol Psychiatry. 2000 48 : 658 64.
    • (2000) Biol Psychiatry. , vol.48 , pp. 658-64
    • Chen, B.1    Wang, J.F.2    Young, L.T.3
  • 67
    • 32044462724 scopus 로고    scopus 로고
    • Mood stabilizing drug lithium increases expression of endoplasmic reticulum stress proteins in primary cultured rat cerebral cortical cells
    • Shao L, Sun X, Xu L, Young LT, Wang JF. Mood stabilizing drug lithium increases expression of endoplasmic reticulum stress proteins in primary cultured rat cerebral cortical cells. Life Sci. 2006 78 : 1317 23.
    • (2006) Life Sci. , vol.78 , pp. 1317-23
    • Shao, L.1    Sun, X.2    Xu, L.3    Young, L.T.4    Wang, J.F.5
  • 68
    • 0037474040 scopus 로고    scopus 로고
    • Valproate inhibits oxidative damage to lipid and protein in primary cultured rat cerebrocortical cells
    • Wang JF, Azzam JE, Young LT. Valproate inhibits oxidative damage to lipid and protein in primary cultured rat cerebrocortical cells. Neuroscience. 2003 116 : 485 9.
    • (2003) Neuroscience. , vol.116 , pp. 485-9
    • Wang, J.F.1    Azzam, J.E.2    Young, L.T.3
  • 69
    • 29044447411 scopus 로고    scopus 로고
    • Chronic treatment with mood stabilizers lithium and valproate prevents excitotoxicity by inhibiting oxidative stress in rat cerebral cortical cells
    • Shao L, Young LT, Wang JF. Chronic treatment with mood stabilizers lithium and valproate prevents excitotoxicity by inhibiting oxidative stress in rat cerebral cortical cells. Biol Psychiatry. 2005 58 : 879 84.
    • (2005) Biol Psychiatry. , vol.58 , pp. 879-84
    • Shao, L.1    Young, L.T.2    Wang, J.F.3
  • 70
    • 33846303907 scopus 로고    scopus 로고
    • Role of glutathione in neuroprotective effects of mood stabilizing drugs lithium and val-proate
    • Cui J, Shao L, Young LT, Wang JF. Role of glutathione in neuroprotective effects of mood stabilizing drugs lithium and val-proate. Neuroscience. 2007 144 : 1447 53.
    • (2007) Neuroscience. , vol.144 , pp. 1447-53
    • Cui, J.1    Shao, L.2    Young, L.T.3    Wang, J.F.4
  • 71
    • 34547792388 scopus 로고    scopus 로고
    • Epigenetic gene silencing in cancer: The DNA hypermethylome
    • Esteller M. Epigenetic gene silencing in cancer: the DNA hypermethylome. Hum Mol Genet. 2007 16 : R50 9.
    • (2007) Hum Mol Genet. , vol.16 , pp. 50-9
    • Esteller, M.1
  • 73
    • 4544250024 scopus 로고    scopus 로고
    • Gene-promoter hypermethylation as a biomarker in lung cancer
    • Belinsky SA. Gene-promoter hypermethylation as a biomarker in lung cancer. Nat Rev Cancer. 2004 4 : 707 17.
    • (2004) Nat Rev Cancer. , vol.4 , pp. 707-17
    • Belinsky, S.A.1
  • 76
    • 35349030895 scopus 로고    scopus 로고
    • Targeting systemic inflammation: Novel therapies for the treatment of chronic obstructive pulmonary disease
    • Cazzola M, Ciaprini C, Page CP, Matera MG. Targeting systemic inflammation: novel therapies for the treatment of chronic obstructive pulmonary disease. Expert Opin Ther Targets. 2007 11 : 1273 86.
    • (2007) Expert Opin Ther Targets. , vol.11 , pp. 1273-86
    • Cazzola, M.1    Ciaprini, C.2    Page, C.P.3    Matera, M.G.4
  • 79
    • 0035315925 scopus 로고    scopus 로고
    • Cigarette smoking reduces histone deacetylase 2 expression, enhances cytokine expression, and inhibits glucocorticoid actions in alveolar macrophages
    • Ito K, Lim S, Caramori G, Chung KF, Barnes PJ, Adcock IM. Cigarette smoking reduces histone deacetylase 2 expression, enhances cytokine expression, and inhibits glucocorticoid actions in alveolar macrophages. FASEB J. 2001 15 : 1110 2.
    • (2001) FASEB J. , vol.15 , pp. 1110-2
    • Ito, K.1    Lim, S.2    Caramori, G.3    Chung, K.F.4    Barnes, P.J.5    Adcock, I.M.6
  • 82
    • 22044434278 scopus 로고    scopus 로고
    • Comparative application of antibody and gene array for expression profiling in human squamous cell lung carcinoma
    • Bartling B, Hofmann HS, Boettger T, Hansen G, Burdach S, Silber RE, Simm A. Comparative application of antibody and gene array for expression profiling in human squamous cell lung carcinoma. Lung Cancer. 2005 49 : 145 54.
    • (2005) Lung Cancer. , vol.49 , pp. 145-54
    • Bartling, B.1    Hofmann, H.S.2    Boettger, T.3    Hansen, G.4    Burdach, S.5    Silber, R.E.6    Simm, A.7
  • 83
    • 4544322261 scopus 로고    scopus 로고
    • Reduced expression of class II histone deacetylase genes is associated with poor prognosis in lung cancer patients
    • DOI 10.1002/ijc.20395
    • Osada H, Tatematsu Y, Saito H, Yatabe Y, Mitsudomi T, Takahashi T. Reduced expression of class II histone deacetylase genes is associated with poor prognosis in lung cancer patients. Int J Cancer. 2004 112 : 26 32. (Pubitemid 39249488)
    • (2004) International Journal of Cancer , vol.112 , Issue.1 , pp. 26-32
    • Osada, H.1    Tatematsu, Y.2    Saito, H.3    Yatabe, Y.4    Mitsudomi, T.5    Takahashi, T.6
  • 84
    • 42649146208 scopus 로고    scopus 로고
    • SIRT1, an antiinflammatory and anti-aging protein, is decreased in lungs of patients with COPD
    • Rajendrasozhan S, Yang SR, Kinnula VL, Rahman I. SIRT1, an antiinflammatory and anti-aging protein, is decreased in lungs of patients with COPD. Am J Respir Crit Care Med. 2008 117 : 861 70.
    • (2008) Am J Respir Crit Care Med. , vol.117 , pp. 861-70
    • Rajendrasozhan, S.1    Yang, S.R.2    Kinnula, V.L.3    Rahman, I.4
  • 85
    • 37549006745 scopus 로고    scopus 로고
    • Decreased expression of the SIN3A gene, a candidate tumor suppressor located at the prevalent allelic loss region 15q23 in non-small cell lung cancer
    • Suzuki H, Ouchida M, Yamamoto H, Yano M, Toyooka S, Aoe M, Shimizu N, Date H, Shimizu K. Decreased expression of the SIN3A gene, a candidate tumor suppressor located at the prevalent allelic loss region 15q23 in non-small cell lung cancer. Lung Cancer. 2008 59 : 24 31.
    • (2008) Lung Cancer. , vol.59 , pp. 24-31
    • Suzuki, H.1    Ouchida, M.2    Yamamoto, H.3    Yano, M.4    Toyooka, S.5    Aoe, M.6    Shimizu, N.7    Date, H.8    Shimizu, K.9
  • 87
    • 0034203533 scopus 로고    scopus 로고
    • Expression of MTA1, a metastasis-associated gene with histone deacetylase activity in pancreatic cancer
    • Iguchi H, Imura G, Toh Y, Ogata Y. Expression of MTA1, a metastasis-associated gene with histone deacetylase activity in pancreatic cancer. Int J Oncol. 2000 16 : 1211 4.
    • (2000) Int J Oncol. , vol.16 , pp. 1211-4
    • Iguchi, H.1    Imura, G.2    Toh, Y.3    Ogata, Y.4
  • 90
    • 0032252209 scopus 로고    scopus 로고
    • NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities
    • Xue Y, Wong J, Moreno GT, Young MK, Cote J, Wang W. NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities. Mol Cell. 1998 2 : 851 61.
    • (1998) Mol Cell. , vol.2 , pp. 851-61
    • Xue, Y.1    Wong, J.2    Moreno, G.T.3    Young, M.K.4    Cote, J.5    Wang, W.6
  • 91
    • 0142211208 scopus 로고    scopus 로고
    • The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity
    • Yao YL, Yang WM. The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity. J Biol Chem. 2003 278 : 42560 8.
    • (2003) J Biol Chem. , vol.278 , pp. 42560-8
    • Yao, Y.L.1    Yang, W.M.2
  • 92
    • 0035852637 scopus 로고    scopus 로고
    • CoREST is an integral component of the CoREST- human histone deacetylase complex
    • You A, Tong JK, Grozinger CM, Schreiber SL. CoREST is an integral component of the CoREST- human histone deacetylase complex. Proc Natl Acad Sci USA. 2001 98 : 1454 8.
    • (2001) Proc Natl Acad Sci USA. , vol.98 , pp. 1454-8
    • You, A.1    Tong, J.K.2    Grozinger, C.M.3    Schreiber, S.L.4
  • 94
    • 0036194173 scopus 로고    scopus 로고
    • Histone acetyltrans-ferase activities of cAMP-regulated enhancer-binding protein and p300 in tissues of fetal, young, and old mice
    • Li Q, Xiao H, Isobe K. Histone acetyltrans-ferase activities of cAMP-regulated enhancer-binding protein and p300 in tissues of fetal, young, and old mice. J Gerontol A Biol Sci Med Sci. 2002 57 : B93 8.
    • (2002) J Gerontol A Biol Sci Med Sci. , vol.57 , pp. 93-8
    • Li, Q.1    Xiao, H.2    Isobe, K.3
  • 96
  • 99
    • 0022648947 scopus 로고
    • Effects of sodium butyrate on the synthesis and methylation of DNA in normal cells and their transformed counterparts
    • de Haan JB, Gevers W, Parker MI. Effects of sodium butyrate on the synthesis and methylation of DNA in normal cells and their transformed counterparts. Cancer Res. 1986 46 : 713 6.
    • (1986) Cancer Res. , vol.46 , pp. 713-6
    • De Haan, J.B.1    Gevers, W.2    Parker, M.I.3
  • 100
    • 0022979422 scopus 로고
    • DNA hypermethylation in sodium butyrate-treated WI-38 fibroblasts
    • Parker MI, de Haan JB, Gevers W. DNA hypermethylation in sodium butyrate-treated WI-38 fibroblasts. J Biol Chem. 1986 261 : 2786 90.
    • (1986) J Biol Chem. , vol.261 , pp. 2786-90
    • Parker, M.I.1    De Haan, J.B.2    Gevers, W.3
  • 101
    • 0022553742 scopus 로고
    • Effect of butyric acid on lung-colonizing ability of cloned low-metastatic Lewis lung carcinoma cells
    • Takenaga K. Effect of butyric acid on lung-colonizing ability of cloned low-metastatic Lewis lung carcinoma cells. Cancer Res. 1986 46 : 1244 9.
    • (1986) Cancer Res. , vol.46 , pp. 1244-9
    • Takenaga, K.1
  • 103
    • 0029737436 scopus 로고    scopus 로고
    • Enhancement of sensitivity of human lung adenocarcinoma cells to growth-inhibitory activity of interferon alpha by differentiation-inducing agents
    • Goto I, Yamamoto-Yamaguchi Y, Honma Y. Enhancement of sensitivity of human lung adenocarcinoma cells to growth-inhibitory activity of interferon alpha by differentiation-inducing agents. Br J Cancer. 1996 74 : 546 54.
    • (1996) Br J Cancer. , vol.74 , pp. 546-54
    • Goto, I.1    Yamamoto-Yamaguchi, Y.2    Honma, Y.3
  • 104
    • 0033520944 scopus 로고    scopus 로고
    • Histone deacetylase inhibition selectively alters the activity and expression of cell cycle proteins leading to specific chromatin acetylation and antiproliferative effects
    • Sambucetti LC, Fischer DD, Zabludoff S, Zabludoff S, Kwon PO, Chamberlin H, Trogani N, Xu H, Cohen D. Histone deacetylase inhibition selectively alters the activity and expression of cell cycle proteins leading to specific chromatin acetylation and antiproliferative effects. J Biol Chem. 1999 274 : 34940 7.
    • (1999) J Biol Chem. , vol.274 , pp. 34940-7
    • Sambucetti, L.C.1    Fischer, D.D.2    Zabludoff, S.3    Zabludoff, S.4    Kwon, P.O.5    Chamberlin, H.6    Trogani, N.7    Xu, H.8    Cohen, D.9
  • 105
    • 0037236445 scopus 로고    scopus 로고
    • Chemopreventive efficacy of suberoylanilide hydroxamic acid (SAHA) against 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK)-induced lung tumorigenesis in female A/J mice
    • Desai D, Das A, Cohen L, el-Bayoumy K, Amin S. Chemopreventive efficacy of suberoylanilide hydroxamic acid (SAHA) against 4-(methylnitrosamino)-1-(3- pyridyl)-1-butanone (NNK)-induced lung tumorigenesis in female A-J mice. Anticancer Res. 2003 23 : 499 503. (Pubitemid 36358560)
    • (2003) Anticancer Research , vol.23 , pp. 499-503
    • Desai, D.1    Das, A.2    Cohen, L.3    El-Bayoumy, K.4    Amin, S.5
  • 106
    • 33644875208 scopus 로고    scopus 로고
    • SAHA, a HDAC inhibitor, has profound anti-growth activity against non-small cell lung cancer cells
    • Komatsu N, Kawamata N, Takeuchi S, Yin D, Chien W, Miller CW, Koeffler HP. SAHA, a HDAC inhibitor, has profound anti-growth activity against non-small cell lung cancer cells. Oncol Rep. 2006 15 : 187 91.
    • (2006) Oncol Rep. , vol.15 , pp. 187-91
    • Komatsu, N.1    Kawamata, N.2    Takeuchi, S.3    Yin, D.4    Chien, W.5    Miller, C.W.6    Koeffler, H.P.7
  • 108
    • 0038408486 scopus 로고    scopus 로고
    • Histone Deacetylase Inhibitor Up-Regulates RECK to Inhibit MMP-2 Activation and Cancer Cell Invasion
    • Liu L-T, Chang H-C, Chiang L-C, Hung W-C. Histone Deacetylase Inhibitor Up-Regulates RECK to Inhibit MMP-2 Activation and Cancer Cell Invasion. Cancer Res. 2003 63 : 3069 72.
    • (2003) Cancer Res. , vol.63 , pp. 3069-72
    • Liu, L.-T.1    Chang, H.-C.2    Chiang, L.-C.3    Hung, W.-C.4
  • 113
    • 33644688961 scopus 로고    scopus 로고
    • Induction of apoptosis by trichostatin A, a histone deacetylase inhibitor, is associated with inhibition of cyclooxygenase-2 activity in human non-small cell lung cancer cells
    • Choi YH. Induction of apoptosis by trichostatin A, a histone deacetylase inhibitor, is associated with inhibition of cyclooxygenase-2 activity in human non-small cell lung cancer cells. Int J Oncol. 2005 27 : 473 9.
    • (2005) Int J Oncol. , vol.27 , pp. 473-9
    • Choi, Y.H.1
  • 114
    • 33747184291 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and transforming growth factor-beta induce 15-hydroxyprostaglandin dehydrogenase expression in human lung adenocarcinoma cells
    • Tong M, Ding Y, Tai HH. Histone deacetylase inhibitors and transforming growth factor-beta induce 15-hydroxyprostaglandin dehydrogenase expression in human lung adenocarcinoma cells. Biochem Pharmacol. 2006 72 : 701 9.
    • (2006) Biochem Pharmacol. , vol.72 , pp. 701-9
    • Tong, M.1    Ding, Y.2    Tai, H.H.3
  • 115
    • 31644442355 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors require cas-pase activity to induce apoptosis in lung and prostate carcinoma cells
    • Sonnemann J, Hartwig M, Plath A, Saravana Kumar K, Muller C, Beck JF. Histone deacetylase inhibitors require cas-pase activity to induce apoptosis in lung and prostate carcinoma cells. Cancer Lett. 2006 232 : 148 60.
    • (2006) Cancer Lett. , vol.232 , pp. 148-60
    • Sonnemann, J.1    Hartwig, M.2    Plath, A.3    Saravana Kumar, K.4    Muller, C.5    Beck, J.F.6
  • 116
    • 33846199978 scopus 로고    scopus 로고
    • Trichostatin A induces apoptosis in lung cancer cells via simultaneous activation of the death receptor-mediated and mitochondrial pathway?
    • Kim HR, Kim EJ, Yang SH, Jeong ET, Park C, Lee JH, Youn MJ, So HS, Park R. Trichostatin A induces apoptosis in lung cancer cells via simultaneous activation of the death receptor-mediated and mitochondrial pathway? Exp Mol Med. 2006 38 : 616 24.
    • (2006) Exp Mol Med. , vol.38 , pp. 616-24
    • Kim, H.R.1    Kim, E.J.2    Yang, S.H.3    Jeong, E.T.4    Park, C.5    Lee, J.H.6    Youn, M.J.7    So, H.S.8    Park, R.9
  • 117
    • 33744938927 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors suppress the inducibility of nuclear factor-kappaB by tumor necrosis factor-alpha receptor-1 down-regulation
    • Imre G, Gekeler V, Leja A, Beckers T, Boehm M. Histone deacetylase inhibitors suppress the inducibility of nuclear factor-kappaB by tumor necrosis factor-alpha receptor-1 down-regulation. Cancer Res. 2006 66 : 5409 18.
    • (2006) Cancer Res. , vol.66 , pp. 5409-18
    • Imre, G.1    Gekeler, V.2    Leja, A.3    Beckers, T.4    Boehm, M.5
  • 118
    • 0038060250 scopus 로고    scopus 로고
    • Effects of FK228, a novel histone deacetylase inhibitor, on tumor growth and expression of p21 and c-myc genes in vivo
    • Sasakawa Y, Naoe Y, Inoue T, Sasakawa T, Matsuo M, Manda T, Mutoh S. Effects of FK228, a novel histone deacetylase inhibitor, on tumor growth and expression of p21 and c-myc genes in vivo. Cancer Lett. 2003 195 : 161 8.
    • (2003) Cancer Lett. , vol.195 , pp. 161-8
    • Sasakawa, Y.1    Naoe, Y.2    Inoue, T.3    Sasakawa, T.4    Matsuo, M.5    Manda, T.6    Mutoh, S.7
  • 119
    • 33846861339 scopus 로고    scopus 로고
    • Depsipeptide a histone deacetlyase inhibitor down regulates levels of matrix metalloproteinases 2 and 9 mRNA and protein expressions in lung cancer cells (A549)
    • Vinodhkumar R, Song YS, Ravikumar V, Ramakrishnan G, Devaki T. Depsipeptide a histone deacetlyase inhibitor down regulates levels of matrix metalloproteinases 2 and 9 mRNA and protein expressions in lung cancer cells (A549). Chem Biol Interact. 2007 165 : 220 9.
    • (2007) Chem Biol Interact. , vol.165 , pp. 220-9
    • Vinodhkumar, R.1    Song, Y.S.2    Ravikumar, V.3    Ramakrishnan, G.4    Devaki, T.5
  • 120
    • 38949140475 scopus 로고    scopus 로고
    • Romidepsin (depsipeptide) induced cell cycle arrest, apoptosis and histone hyperacetylation in lung carcinoma cells (A549) are associated with increase in p21 and hypophosphorylated retinoblastoma proteins expression
    • DOI 10.1016/j.biopha.2007.06.002, PII S0753332207001163
    • Radhakrishnan V, Song YS, Thiruvengadam D. Romidepsin (depsipeptide) induced cell cycle arrest, apop-tosis and histone hyperacetylation in lung carcinoma cells (A549) are associated with increase in p21 and hypophosphorylated retinoblastoma proteins expression. Biomed Pharmacother. 2008 62 : 85 93. (Pubitemid 351215810)
    • (2008) Biomedicine and Pharmacotherapy , vol.62 , Issue.2 , pp. 85-93
    • Radhakrishnan, V.1    Song, Y.-S.2    Thiruvengadam, D.3
  • 124
    • 0032948005 scopus 로고    scopus 로고
    • Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    • Cameron EE, Bachman KE, Myohanen S, Herman JG, Baylin SB. Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. Nat Genet. 1999 21 : 103 7.
    • (1999) Nat Genet. , vol.21 , pp. 103-7
    • Cameron, E.E.1    Bachman, K.E.2    Myohanen, S.3    Herman, J.G.4    Baylin, S.B.5
  • 125
    • 0035866353 scopus 로고    scopus 로고
    • DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors
    • Zhu WG, Lakshmanan RR, Beal MD, Otterson GA. DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors. Cancer Res. 2001 61 : 1327 33.
    • (2001) Cancer Res. , vol.61 , pp. 1327-33
    • Zhu, W.G.1    Lakshmanan, R.R.2    Beal, M.D.3    Otterson, G.A.4
  • 127
    • 0036746906 scopus 로고    scopus 로고
    • Antineoplastic action of 5-aza-2'-deoxycytidine and phenylbutyrate on human lung carcinoma cells
    • Boivin AJ, Momparler LF, Hurtubise A, Momparler RL. Antineoplastic action of 5-aza-2'-deoxycytidine and phenylbutyrate on human lung carcinoma cells. Anticancer Drugs. 2002 13 : 869 74.
    • (2002) Anticancer Drugs. , vol.13 , pp. 869-74
    • Boivin, A.J.1    Momparler, L.F.2    Hurtubise, A.3    Momparler, R.L.4
  • 130
    • 4644335119 scopus 로고    scopus 로고
    • In vitro antitumor potential of 4-BPRE, a butyryl aminophenyl ester of retinoic acid: Role of the butyryl group
    • Um SJ, Han HS, Kwon YJ, Park SH, Bae TS, Rho YS, Sin HS. In vitro antitumor potential of 4-BPRE, a butyryl aminophenyl ester of retinoic acid: role of the butyryl group. Oncol Rep. 2004 11 : 719 26.
    • (2004) Oncol Rep. , vol.11 , pp. 719-26
    • Um, S.J.1    Han, H.S.2    Kwon, Y.J.3    Park, S.H.4    Bae, T.S.5    Rho, Y.S.6    Sin, H.S.7
  • 132
    • 6344229760 scopus 로고    scopus 로고
    • Proteasome inhibition sensitizes non-small cell lung cancer to histone deacetylase inhibitor-induced apoptosis through the generation of reactive oxygen species
    • Denlinger CE, Rundall BK, Jones DR. Proteasome inhibition sensitizes non-small cell lung cancer to histone deacetylase inhibitor-induced apoptosis through the generation of reactive oxygen species. J Thorac Cardiovasc Surg. 2004 128 : 740 8.
    • (2004) J Thorac Cardiovasc Surg. , vol.128 , pp. 740-8
    • Denlinger, C.E.1    Rundall, B.K.2    Jones, D.R.3
  • 133
    • 3843103805 scopus 로고    scopus 로고
    • Combined histone deacetylase and NF-kappaB inhibition sensitizes non-small cell lung cancer to cell death
    • Rundall BK, Denlinger CE, Jones DR. Combined histone deacetylase and NF-kappaB inhibition sensitizes non-small cell lung cancer to cell death. Surgery. 2004 136 : 416 25.
    • (2004) Surgery. , vol.136 , pp. 416-25
    • Rundall, B.K.1    Denlinger, C.E.2    Jones, D.R.3
  • 134
    • 11144284854 scopus 로고    scopus 로고
    • Induction of apoptosis of lung and esophageal cancer cells treated with the combination of histone deacetylase inhibitor (trichostatin A) and protein kinase C inhibitor (calphostin C)
    • DOI 10.1016/j.jtcvs.2004.07.051, PII S0022522304011742
    • Maxhimer JB, Reddy RM, Zuo J, Cole GW, Schrump DS, Nguyen DM. Induction of apoptosis of lung and esophageal cancer cells treated with the combination of histone deacetylase inhibitor (trichostatin A) and protein kinase C inhibitor (calphostin C). J Thorac Cardiovasc Surg. 2005 129 : 53 63. (Pubitemid 40038096)
    • (2005) Journal of Thoracic and Cardiovascular Surgery , vol.129 , Issue.1 , pp. 53-63
    • Maxhimer, J.B.1    Reddy, R.M.2    Zuo, J.3    Cole Jr., G.W.4    Schrump, D.S.5    Nguyen, D.M.6
  • 135
    • 15244343927 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors interact synergistically with tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) to induce apoptosis in carcinoma cell lines
    • DOI 10.1007/s10637-005-5854-9
    • Sonnemann J, Gange J, Kumar KS, Muller C, Bader P, Beck JF. Histone deacetylase inhibitors interact synergisti-cally with tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) to induce apoptosis in carcinoma cell lines. Invest New Drugs. 2005 23 : 99 109. (Pubitemid 40386226)
    • (2005) Investigational New Drugs , vol.23 , Issue.2 , pp. 99-109
    • Sonnemann, J.1    Gange, J.2    Kumar, K.S.3    Muller, C.4    Bader, P.5    Beck, J.F.6
  • 136
    • 24344498688 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid combined with gemcitabine enhances apopto-sis in non-small cell lung cancer
    • Rundall BK, Denlinger CE, Jones DR. Suberoylanilide hydroxamic acid combined with gemcitabine enhances apopto-sis in non-small cell lung cancer. Surgery. 2005 138 : 360 7.
    • (2005) Surgery. , vol.138 , pp. 360-7
    • Rundall, B.K.1    Denlinger, C.E.2    Jones, D.R.3
  • 137
    • 33845640064 scopus 로고    scopus 로고
    • Combination phenylbutyrate-gemcitabine therapy effectively inhibits in vitro and in vivo growth of NSCLC by intrinsic apoptotic pathways
    • Schniewind B, Heintz K, Kurdow R, Ammerpohl O, Trauzold A, Emme D, Dohrmann P, Kalthoff H. Combination phenylbutyrate-gemcitabine therapy effectively inhibits in vitro and in vivo growth of NSCLC by intrinsic apoptotic pathways. J Carcinog. 2006 5 : 25 35.
    • (2006) J Carcinog. , vol.5 , pp. 25-35
    • Schniewind, B.1    Heintz, K.2    Kurdow, R.3    Ammerpohl, O.4    Trauzold, A.5    Emme, D.6    Dohrmann, P.7    Kalthoff, H.8
  • 138
    • 27544505166 scopus 로고    scopus 로고
    • Inhibition of phosphatidylinositol 3-kinase-Akt and histone deacetylase activity induces apoptosis in non-small cell lung cancer in vitro and in vivo
    • Denlinger CE, Rundall BK, Jones DR. Inhibition of phosphatidylinositol 3-kinase-Akt and histone deacetylase activity induces apoptosis in non-small cell lung cancer in vitro and in vivo. J Thorac Cardiovasc Surg. 2005 130 : 1422 9.
    • (2005) J Thorac Cardiovasc Surg. , vol.130 , pp. 1422-9
    • Denlinger, C.E.1    Rundall, B.K.2    Jones, D.R.3
  • 139
    • 33947242973 scopus 로고    scopus 로고
    • Abrogation of MAPK and Akt signaling by AEE788 synergistically potentiates histone deacetylase inhibitor-induced apoptosis through reactive oxygen species generation
    • Yu C, Friday BB, Lai JP, McCollum A, Atadja P, Roberts LR, Adjei AA. Abrogation of MAPK and Akt signaling by AEE788 synergistically potentiates histone deacetylase inhibitor-induced apoptosis through reactive oxygen species generation. Clin Cancer Res. 2007 13 : 1140 8.
    • (2007) Clin Cancer Res. , vol.13 , pp. 1140-8
    • Yu, C.1    Friday, B.B.2    Lai, J.P.3    McCollum, A.4    Atadja, P.5    Roberts, L.R.6    Adjei, A.A.7
  • 140
    • 34347261742 scopus 로고    scopus 로고
    • Apoptosis induced by depsipeptide FK228 coincides with inhibition of survival signaling in lung cancer cells
    • Yu XD, Wang SY, Chen GA, Hou CM, Zhao M, Hong JA, Nguyen DM, Schrump DS. Apoptosis induced by depsipeptide FK228 coincides with inhibition of survival signaling in lung cancer cells. Cancer J. 2007 13 : 105 13.
    • (2007) Cancer J. , vol.13 , pp. 105-13
    • Yu, X.D.1    Wang, S.Y.2    Chen, G.A.3    Hou, C.M.4    Zhao, M.5    Hong, J.A.6    Nguyen, D.M.7    Schrump, D.S.8
  • 141
    • 29144485434 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor FR901228 enhances the antitumor effect of telomerase-specific replication-selective adenoviral agent OBP-301 in human lung cancer cells
    • Watanabe T, Hioki M, Fujiwara T, Nishizaki M, Kagawa S, Taki M, Kishimoto H, Endo Y, Urata Y, Tanaka N, Fujiwara T. Histone deacetylase inhibitor FR901228 enhances the antitumor effect of telomerase-specific replication-selective adenoviral agent OBP-301 in human lung cancer cells. Exp Cell Res. 2006 312 : 256 65.
    • (2006) Exp Cell Res. , vol.312 , pp. 256-65
    • Watanabe, T.1    Hioki, M.2    Fujiwara, T.3    Nishizaki, M.4    Kagawa, S.5    Taki, M.6    Kishimoto, H.7    Endo, Y.8    Urata, Y.9    Tanaka, N.10    Fujiwara, T.11
  • 142
    • 33646871234 scopus 로고    scopus 로고
    • Bombesin-gastrin-releasing peptide receptor antagonists increase the ability of histone deacetylase inhibitors to reduce lung cancer proliferation
    • Moody TW, Nakagawa T, Kang Y, Jakowlew S, Chan D, Jensen RT. Bombesin-gastrin-releasing peptide receptor antagonists increase the ability of histone deacetylase inhibitors to reduce lung cancer proliferation. J Mol Neurosci. 2006 28 : 231 8.
    • (2006) J Mol Neurosci. , vol.28 , pp. 231-8
    • Moody, T.W.1    Nakagawa, T.2    Kang, Y.3    Jakowlew, S.4    Chan, D.5    Jensen, R.T.6
  • 143
    • 33845741562 scopus 로고    scopus 로고
    • Histone deacetylase (HDAC) inhibitor LBH589 increases duration of gamma-H2AX foci and confines HDAC4 to the cytoplasm in irradiated non-small cell lung cancer
    • Geng L, Cuneo KC, Fu A, Tu T, Atadja PW, Hallahan DE. Histone deacetylase (HDAC) inhibitor LBH589 increases duration of gamma-H2AX foci and confines HDAC4 to the cytoplasm in irradiated non-small cell lung cancer. Cancer Res. 2006 66 : 11298 304.
    • (2006) Cancer Res. , vol.66 , pp. 11298-304
    • Geng, L.1    Cuneo, K.C.2    Fu, A.3    Tu, T.4    Atadja, P.W.5    Hallahan, D.E.6
  • 144
    • 34250805910 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor NVP-LAQ824 sensitizes human nonsmall cell lung cancer to the cytotoxic effects of ionizing radiation
    • DOI 10.1097/CAD.0b013e3280b10d57, PII 0000181320070800000006
    • Cuneo KC, Fu A, Osusky K, Huamani J, Hallahan DE, Geng L. Histone deacetylase inhibitor NVP-LAQ824 sensitizes human nonsmall cell lung cancer to the cytotoxic effects of ionizing radiation. Anticancer Drugs. 2007 18 : 793 800. (Pubitemid 46975965)
    • (2007) Anti-Cancer Drugs , vol.18 , Issue.7 , pp. 793-800
    • Cuneo, K.C.1    Fu, A.2    Osusky, K.3    Huamani, J.4    Hallahan, D.E.5    Geng, L.6
  • 146
    • 34748840882 scopus 로고    scopus 로고
    • Effect of the histone deacetylase inhibitor LBH589 against epidermal growth factor receptor-dependent human lung cancer cells
    • Edwards A, Li J, Atadja P, Bhalla K, Haura EB. Effect of the histone deacetylase inhibitor LBH589 against epidermal growth factor receptor-dependent human lung cancer cells. Mol Cancer Ther. 2007 6 : 2515 24.
    • (2007) Mol Cancer Ther. , vol.6 , pp. 2515-24
    • Edwards, A.1    Li, J.2    Atadja, P.3    Bhalla, K.4    Haura, E.B.5
  • 147
    • 43749087604 scopus 로고    scopus 로고
    • Combinatorial action of the HDAC inhibitor trichostatin A and etoposide induces caspase-mediated AIF-dependent apoptotic cell death in non-small cell lung carcinoma cells
    • Hajji N, Wallenborg K, Vlachos P, Nyman U, Hermanson O, Joseph B. Combinatorial action of the HDAC inhibitor trichostatin A and etoposide induces caspase-mediated AIF-dependent apoptotic cell death in non-small cell lung carcinoma cells. Oncogene. 2008 27 : 3134 44.
    • (2008) Oncogene. , vol.27 , pp. 3134-44
    • Hajji, N.1    Wallenborg, K.2    Vlachos, P.3    Nyman, U.4    Hermanson, O.5    Joseph, B.6
  • 149
    • 0033209757 scopus 로고    scopus 로고
    • Methylation, gene expression and the chromatin connection in cancer (review)
    • Gray SG, Eriksson T, Ekstrom TJ. Methylation, gene expression and the chromatin connection in cancer (review). Int J Mol Med. 1999 4 : 333 50.
    • (1999) Int J Mol Med. , vol.4 , pp. 333-50
    • Gray, S.G.1    Eriksson, T.2    Ekstrom, T.J.3
  • 152
    • 37049001617 scopus 로고    scopus 로고
    • Clinical significance of histone deacetylase 1 expression in patients with hepatocellular carcinoma
    • DOI 10.1159/000111106
    • Rikimaru T, Taketomi A, Yamashita Y, Yamashita Y, Shirabe K, Hamatsu T, Shimada M, Maehara Y. Clinical significance of histone deacetylase 1 expression in patients with hepatocellular carcinoma. Oncology. 2007 72 : 69 74. (Pubitemid 350249132)
    • (2007) Oncology , vol.72 , Issue.1-2 , pp. 69-74
    • Rikimaru, T.1    Taketomi, A.2    Yamashita, Y.-I.3    Shirabe, K.4    Hamatsu, T.5    Shimada, M.6    Maehara, Y.7
  • 155
    • 34547683485 scopus 로고    scopus 로고
    • Evaluation and management of obesity-related nonalcoholic fatty liver disease
    • Nugent C, Younossi ZM. Evaluation and management of obesity-related nonalcoholic fatty liver disease. Nat Clin Pract Gastroenterol Hepatol. 2007 4 : 432 41.
    • (2007) Nat Clin Pract Gastroenterol Hepatol. , vol.4 , pp. 432-41
    • Nugent, C.1    Younossi, Z.M.2
  • 156
    • 27144496194 scopus 로고    scopus 로고
    • A variable number of tandem repeats polymorphism in an E2F-1 binding element in the 5' flanking region of SMYD3 is a risk factor for human cancers
    • Tsuge M, Hamamoto R, Silva FP, Ohnishi Y, Chayama K, Kamatani N, Furukawa Y, Nakamura Y. A variable number of tandem repeats polymorphism in an E2F-1 binding element in the 5' flanking region of SMYD3 is a risk factor for human cancers. Nat Genet. 2005 37 : 1104 7.
    • (2005) Nat Genet. , vol.37 , pp. 1104-7
    • Tsuge, M.1    Hamamoto, R.2    Silva, F.P.3    Ohnishi, Y.4    Chayama, K.5    Kamatani, N.6    Furukawa, Y.7    Nakamura, Y.8
  • 158
    • 34547907882 scopus 로고    scopus 로고
    • Deregulated expression of a novel component of TFTC-STAGA histone acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma: Possible implication for the oncogenic potential of c-Myc
    • Kurabe N, Katagiri K, Komiya Y, Ito R, Sugiyama A, Kawasaki Y, Tashiro F. Deregulated expression of a novel component of TFTC-STAGA histone acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma: possible implication for the oncogenic potential of c-Myc. Oncogene. 2007 26 : 5626 34.
    • (2007) Oncogene. , vol.26 , pp. 5626-34
    • Kurabe, N.1    Katagiri, K.2    Komiya, Y.3    Ito, R.4    Sugiyama, A.5    Kawasaki, Y.6    Tashiro, F.7
  • 160
    • 1942517813 scopus 로고    scopus 로고
    • Overexpression of metastatic tumor antigen 1 in hepatocellular carcinoma: Relationship to vascular invasion and estrogen receptor-alpha
    • Moon WS, Chang K, Tarnawski AS. Overexpression of metastatic tumor antigen 1 in hepatocellular carcinoma: relationship to vascular invasion and estrogen receptor-alpha. Hum Pathol. 2004 35 : 424 9.
    • (2004) Hum Pathol. , vol.35 , pp. 424-9
    • Moon, W.S.1    Chang, K.2    Tarnawski, A.S.3
  • 161
    • 38449109636 scopus 로고    scopus 로고
    • Metastasis-associated protein 1 inhibits p53-induced apoptosis
    • Moon HE, Cheon H, Lee MS. Metastasis-associated protein 1 inhibits p53-induced apoptosis. Oncol Rep. 2007 18 : 1311 4.
    • (2007) Oncol Rep. , vol.18 , pp. 1311-4
    • Moon, H.E.1    Cheon, H.2    Lee, M.S.3
  • 162
    • 0033629140 scopus 로고    scopus 로고
    • Modulating IGFBP-3 expression by trichostatin A: Potential therapeutic role in the treatment of hepatocellular carcinoma
    • Gray SG, Kytola S, Lui WO, Larsson C, Ekstrom TJ. Modulating IGFBP-3 expression by trichostatin A: potential therapeutic role in the treatment of hepatocellular carcinoma. Int J Mol Med. 2000 5 : 33 41.
    • (2000) Int J Mol Med. , vol.5 , pp. 33-41
    • Gray, S.G.1    Kytola, S.2    Lui, W.O.3    Larsson, C.4    Ekstrom, T.J.5
  • 165
    • 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, Schuppan D. 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. 233-40
    • Herold, C.1    Ganslmayer, M.2    Ocker, M.3    Hermann, M.4    Geerts, A.5    Hahn, E.G.6    Schuppan, D.7
  • 166
    • 0037455825 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor trichostatin A induces cell-cycle arrest-apoptosis and hepatocyte differentiation in human hepatoma cells
    • Yamashita Y, Shimada M, Harimoto N, Rikimaru T, Shirabe K, Tanaka S, Sugimachi K. Histone deacetylase inhibitor trichostatin A induces cell-cycle arrest-apoptosis and hepatocyte differentiation in human hepatoma cells. Int J Cancer. 2003 103 : 572 6.
    • (2003) Int J Cancer. , vol.103 , pp. 572-6
    • Yamashita, Y.1    Shimada, M.2    Harimoto, N.3    Rikimaru, T.4    Shirabe, K.5    Tanaka, S.6    Sugimachi, K.7
  • 167
    • 1842830815 scopus 로고    scopus 로고
    • Microarray profiling of the effects of histone deacetylase inhibitors on gene expression in cancer cell lines
    • Gray SG, Qian CN, Furge K, Guo X, Teh BT. Microarray profiling of the effects of histone deacetylase inhibitors on gene expression in cancer cell lines. Int J Oncol. 2004 24 : 773 95.
    • (2004) Int J Oncol. , vol.24 , pp. 773-95
    • Gray, S.G.1    Qian, C.N.2    Furge, K.3    Guo, X.4    Teh, B.T.5
  • 168
    • 4344683925 scopus 로고    scopus 로고
    • Identification of genes up-regulated by histone deacetylase inhibition with cDNA microarray and exploration of epigenetic alterations on hepatoma cells
    • Chiba T, Yokosuka O, Arai M, Tada M, Fukai K, Imazeki F, Kato M, Seki N, Saisho H. Identification of genes up-regulated by histone deacetylase inhibition with cDNA microarray and exploration of epigenetic alterations on hepatoma cells. J Hepatol. 2004 41 : 436 45.
    • (2004) J Hepatol. , vol.41 , pp. 436-45
    • Chiba, T.1    Yokosuka, O.2    Arai, M.3    Tada, M.4    Fukai, K.5    Imazeki, F.6    Kato, M.7    Seki, N.8    Saisho, H.9
  • 169
    • 4344639284 scopus 로고    scopus 로고
    • Cell growth inhibition and gene expression induced by the histone deacetylase inhibitor, trichostatin A, on human hepatoma cells
    • Chiba T, Yokosuka O, Fukai K, Kojima H, Tada M, Arai M, Imazeki F, Saisho H. Cell growth inhibition and gene expression induced by the histone deacetylase inhibitor, trichostatin A, on human hepatoma cells. Oncology. 2004 66 : 481 91.
    • (2004) Oncology. , vol.66 , pp. 481-91
    • Chiba, T.1    Yokosuka, O.2    Fukai, K.3    Kojima, H.4    Tada, M.5    Arai, M.6    Imazeki, F.7    Saisho, H.8
  • 170
    • 21644433994 scopus 로고    scopus 로고
    • Gene expression associated with the decrease in malignant phenotype of human liver cancer cells following stimulation with a histone deacetylase inhibitor
    • Wakabayashi K, Saito H, Kaneko F, Nakamoto N, Tada S, Hibi T. Gene expression associated with the decrease in malignant phenotype of human liver cancer cells following stimulation with a histone deacetylase inhibitor. Int J Oncol. 2005 26 : 233 9.
    • (2005) Int J Oncol. , vol.26 , pp. 233-9
    • Wakabayashi, K.1    Saito, H.2    Kaneko, F.3    Nakamoto, N.4    Tada, S.5    Hibi, T.6
  • 175
    • 1842852640 scopus 로고    scopus 로고
    • Down-regulation of matrix-invasive potential of human liver cancer cells by type i interferon and a histone deacetylase inhibitor sodium butyrate
    • Kaneko F, Saito H, Saito Y, Wakabayashi K, Nakamoto N, Tada S, Suzuki H, Tsunematsu S, Kumagai N, Ishii H. Down-regulation of matrix-invasive potential of human liver cancer cells by type I interferon and a histone deacetylase inhibitor sodium butyrate. Int J Oncol. 2004 24 : 837 45.
    • (2004) Int J Oncol. , vol.24 , pp. 837-45
    • Kaneko, F.1    Saito, H.2    Saito, Y.3    Wakabayashi, K.4    Nakamoto, N.5    Tada, S.6    Suzuki, H.7    Tsunematsu, S.8    Kumagai, N.9    Ishii, H.10
  • 182
    • 33645239495 scopus 로고    scopus 로고
    • HDAC inhibitor treatment of hepatoma cells induces both TRAIL-independent apoptosis and restoration of sensitivity to TRAIL
    • Pathil A, Armeanu S, Venturelli S, Mascagni P, Weiss TS, Gregor M, Lauer UM, Bitzer M. HDAC inhibitor treatment of hepatoma cells induces both TRAIL-independent apoptosis and restoration of sensitivity to TRAIL. Hepatology. 2006 43 : 425 34.
    • (2006) Hepatology. , vol.43 , pp. 425-34
    • Pathil, A.1    Armeanu, S.2    Venturelli, S.3    Mascagni, P.4    Weiss, T.S.5    Gregor, M.6    Lauer, U.M.7    Bitzer, M.8
  • 184
    • 24944496184 scopus 로고    scopus 로고
    • Role of histone and transcription factor acetylation in diabetes pathogenesis
    • Gray SG, De Meyts P. Role of histone and transcription factor acetylation in diabetes pathogenesis. Diabetes Metab Res Rev. 2005 21 : 416 33.
    • (2005) Diabetes Metab Res Rev. , vol.21 , pp. 416-33
    • Gray, S.G.1    De Meyts, P.2
  • 186
    • 67249096278 scopus 로고    scopus 로고
    • Methods for identification of compounds modulating insulin resistance
    • In. J.S. K.C. editors.
    • James S, Kaiser C. Methods for identification of compounds modulating insulin resistance. In : JS, KC, editors. BIOVITRUM AB (SE), 2003.
    • (2003) BIOVITRUM AB (SE)
    • James, S.1    Kaiser, C.2
  • 187
    • 0014183930 scopus 로고
    • The use of nicotinamide to modify the toxicity of streptozotocin diabetes without loss of antitumor activity
    • Schein PS, Cooney DA, Vernon ML. The use of nicotinamide to modify the toxicity of streptozotocin diabetes without loss of antitumor activity. Cancer Res. 1967 27 : 2324 32.
    • (1967) Cancer Res. , vol.27 , pp. 2324-32
    • Schein, P.S.1    Cooney, D.A.2    Vernon, M.L.3
  • 188
    • 0014704059 scopus 로고
    • Streptozotocin diabetes: Time course of irreversible B-cell damage; Further observations on prevention by nicotinamide
    • Stauffacher W, Burr I, Gutzeit A, Beaven D, Veleminsky J, Renold AE. Streptozotocin diabetes: time course of irreversible B-cell damage; further observations on prevention by nicotinamide. Proc Soc Exp Biol Med. 1970 133 : 194 200.
    • (1970) Proc Soc Exp Biol Med. , vol.133 , pp. 194-200
    • Stauffacher, W.1    Burr, I.2    Gutzeit, A.3    Beaven, D.4    Veleminsky, J.5    Renold, A.E.6
  • 189
    • 0024497869 scopus 로고
    • Tissue culture of human fetal pancreas. Effects of nicotinamide on insulin production and formation of isletlike cell clusters
    • Sandler S, Andersson A, Korsgren O, Tollemar J, Petersson B, Groth CG, Hellerstrom C. Tissue culture of human fetal pancreas. Effects of nicotinamide on insulin production and formation of isletlike cell clusters. Diabetes. 1989 38 : 168 71.
    • (1989) Diabetes. , vol.38 , pp. 168-71
    • Sandler, S.1    Andersson, A.2    Korsgren, O.3    Tollemar, J.4    Petersson, B.5    Groth, C.G.6    Hellerstrom, C.7
  • 190
    • 0027499291 scopus 로고
    • Pretreatment of fetal porcine pancreas in culture with nicotinamide accelerates reversal of diabetes after transplantation to nude mice
    • Korsgren O, Andersson A, Sandler S. Pretreatment of fetal porcine pancreas in culture with nicotinamide accelerates reversal of diabetes after transplantation to nude mice. Surgery. 1993 113 : 205 14.
    • (1993) Surgery. , vol.113 , pp. 205-14
    • Korsgren, O.1    Andersson, A.2    Sandler, S.3
  • 191
    • 1642277657 scopus 로고    scopus 로고
    • European Nicotinamide Diabetes Intervention Trial (ENDIT): A randomised controlled trial of intervention before the onset of type 1 diabetes
    • Gale EA, Bingley PJ, Emmett CL, Collier T. European Nicotinamide Diabetes Intervention Trial (ENDIT): a randomised controlled trial of intervention before the onset of type 1 diabetes. Lancet. 2004 363 : 925 31.
    • (2004) Lancet. , vol.363 , pp. 925-31
    • Gale, E.A.1    Bingley, P.J.2    Emmett, C.L.3    Collier, T.4
  • 192
    • 33646352455 scopus 로고    scopus 로고
    • Nicotinamide reduces high secretion of IFN-gamma in high-risk relatives even though it does not prevent type 1 diabetes
    • Hedman M, Ludvigsson J, Faresjo MK. Nicotinamide reduces high secretion of IFN-gamma in high-risk relatives even though it does not prevent type 1 diabetes. J Interferon Cytokine Res. 2006 26 : 207 13.
    • (2006) J Interferon Cytokine Res. , vol.26 , pp. 207-13
    • Hedman, M.1    Ludvigsson, J.2    Faresjo, M.K.3
  • 193
    • 1842533604 scopus 로고    scopus 로고
    • Effects of long-term exposure to nicotinamide and sodium butyrate on growth, viability, and the function of clonal insulin secreting cells
    • Liu HK, Green BD, Flatt PR, McClenaghan NH, McCluskey JT. Effects of long-term exposure to nicotinamide and sodium butyrate on growth, viability, and the function of clonal insulin secreting cells. Endocr Res. 2004 30 : 61 8.
    • (2004) Endocr Res. , vol.30 , pp. 61-8
    • Liu, H.K.1    Green, B.D.2    Flatt, P.R.3    McClenaghan, N.H.4    McCluskey, J.T.5
  • 195
    • 34247172594 scopus 로고    scopus 로고
    • 4-Phenylbutyrate restores the functionality of a misfolded mutant low-density lipoprotein receptor
    • Tveten K, Holla OL, Ranheim T, Berge KE, Leren TP, Kulseth MA. 4-Phenylbutyrate restores the functionality of a misfolded mutant low-density lipoprotein receptor. FEBS J. 2007 274 : 1881 93.
    • (2007) FEBS J. , vol.274 , pp. 1881-93
    • Tveten, K.1    Holla, O.L.2    Ranheim, T.3    Berge, K.E.4    Leren, T.P.5    Kulseth, M.A.6
  • 197
    • 1042302747 scopus 로고    scopus 로고
    • Histone deacetylase activity is required for embryonic stem cell differentiation
    • Lee JH, Hart SR, Skalnik DG. Histone deacetylase activity is required for embryonic stem cell differentiation. Genesis. 2004 38 : 32 8.
    • (2004) Genesis. , vol.38 , pp. 32-8
    • Lee, J.H.1    Hart, S.R.2    Skalnik, D.G.3
  • 199
    • 34249711861 scopus 로고    scopus 로고
    • Oxygen, epigenetics and stem cell fate
    • Okazaki K, Maltepe E. Oxygen, epigenetics and stem cell fate. Regen Med. 2006 1 : 71 83.
    • (2006) Regen Med. , vol.1 , pp. 71-83
    • Okazaki, K.1    Maltepe, E.2
  • 200
    • 0035906902 scopus 로고    scopus 로고
    • Differentiation of embryonic stem cells to insulin-secreting structures similar to pancreatic islets
    • Lumelsky N, Blondel O, Laeng P, Velasco I, Ravin R, McKay R. Differentiation of embryonic stem cells to insulin-secreting structures similar to pancreatic islets. Science. 2001 292 : 1389 94.
    • (2001) Science. , vol.292 , pp. 1389-94
    • Lumelsky, N.1    Blondel, O.2    Laeng, P.3    Velasco, I.4    Ravin, R.5    McKay, R.6
  • 201
    • 33845999530 scopus 로고    scopus 로고
    • Chromatin-remodeling factors allow differentiation of bone marrow cells into insulin-producing cells
    • Tayaramma T, Ma B, Rohde M, Mayer H. Chromatin-remodeling factors allow differentiation of bone marrow cells into insulin-producing cells. Stem Cells. 2006 24 : 2858 67.
    • (2006) Stem Cells. , vol.24 , pp. 2858-67
    • Tayaramma, T.1    Ma, B.2    Rohde, M.3    Mayer, H.4
  • 202
    • 34248652441 scopus 로고    scopus 로고
    • Differentiation of bone marrow-derived mesenchymal stem cells from diabetic patients into insulin-producing cells in vitro
    • Sun Y, Chen L, Hou XG, Hou WK, Dong JJ, Sun L, Tang KX, Wang B, Song J, Li H, Wang KX. Differentiation of bone marrow-derived mesenchymal stem cells from diabetic patients into insulin-producing cells in vitro. Chin Med J. 2007 120 : 771 6.
    • (2007) Chin Med J. , vol.120 , pp. 771-6
    • Sun, Y.1    Chen, L.2    Hou, X.G.3    Hou, W.K.4    Dong, J.J.5    Sun, L.6    Tang, K.X.7    Wang, B.8    Song, J.9    Li, H.10    Wang, K.X.11
  • 204
    • 34547857040 scopus 로고    scopus 로고
    • Generation of insulin-producing islet-like clusters from human embryonic stem cells
    • Jiang J, Au M, Lu K, Eshpeter A, Korbutt G, Fisk G, Majumdar AS. Generation of insulin-producing islet-like clusters from human embryonic stem cells. Stem Cells. 2007 25 : 1940 53.
    • (2007) Stem Cells. , vol.25 , pp. 1940-53
    • Jiang, J.1    Au, M.2    Lu, K.3    Eshpeter, A.4    Korbutt, G.5    Fisk, G.6    Majumdar, A.S.7
  • 205
    • 53549088061 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors modify pancreatic cell fate determination and amplify endocrine progenitors
    • Haumaitre C, Lenoir O, Scharfmann R. Histone deacetylase inhibitors modify pancreatic cell fate determination and amplify endocrine progenitors. Mol Cell Biol. 2008 28 : 6373 83.
    • (2008) Mol Cell Biol. , vol.28 , pp. 6373-83
    • Haumaitre, C.1    Lenoir, O.2    Scharfmann, R.3
  • 206
    • 0016658293 scopus 로고
    • A comparative study of histone acetylation in neuronal and glial nuclei enriched rat brain fractions
    • Sarkander HI, Fleischer-Lambropoulos H, Brade WP. A comparative study of histone acetylation in neuronal and glial nuclei enriched rat brain fractions. FEBS Lett. 1975 52 : 40 3.
    • (1975) FEBS Lett. , vol.52 , pp. 40-3
    • Sarkander, H.I.1    Fleischer-Lambropoulos, H.2    Brade, W.P.3
  • 207
    • 38849201941 scopus 로고    scopus 로고
    • Developmental expression of histone deacetylase 11 in the murine brain
    • Liu H, Hu Q, Kaufman A, D'Ercole AJ, Ye P. Developmental expression of histone deacetylase 11 in the murine brain. J Neurosci Res. 2008 86 : 537 43.
    • (2008) J Neurosci Res. , vol.86 , pp. 537-43
    • Liu, H.1    Hu, Q.2    Kaufman, A.3    D'Ercole, A.J.4    Ye, P.5
  • 208
    • 33750590721 scopus 로고    scopus 로고
    • CoREST-like complexes regulate chromatin modification and neuronal gene expression
    • Lakowski B, Roelens I, Jacob S. CoREST-like complexes regulate chromatin modification and neuronal gene expression. J Mol Neurosci. 2006 29 : 227 39.
    • (2006) J Mol Neurosci. , vol.29 , pp. 227-39
    • Lakowski, B.1    Roelens, I.2    Jacob, S.3
  • 211
    • 38449092452 scopus 로고    scopus 로고
    • Rationale for the use of histone deacetylase inhibitors as a dual therapeutic modality in multiple sclerosis
    • Gray SG, Dangond F. Rationale for the use of histone deacetylase inhibitors as a dual therapeutic modality in multiple sclerosis. Epigenetics. 2006 1 : 67 75.
    • (2006) Epigenetics. , vol.1 , pp. 67-75
    • Gray, S.G.1    Dangond, F.2
  • 212
    • 19344378337 scopus 로고    scopus 로고
    • REST and its corepressors mediate plasticity of neuronal gene chro-matin throughout neurogenesis
    • Ballas N, Grunseich C, Lu DD, Speh JC, Mandel G. REST and its corepressors mediate plasticity of neuronal gene chro-matin throughout neurogenesis. Cell. 2005 121 : 645 57.
    • (2005) Cell. , vol.121 , pp. 645-57
    • Ballas, N.1    Grunseich, C.2    Lu, D.D.3    Speh, J.C.4    Mandel, G.5
  • 216
    • 1842687455 scopus 로고    scopus 로고
    • Microarray detection of E2F pathway activation and other targets in multiple sclerosis peripheral blood mononuclear cells
    • Iglesias AH, Camelo S, Hwang D, Villanueva R, Stephanopoulos G, Dangond F. Microarray detection of E2F pathway activation and other targets in multiple sclerosis peripheral blood mononuclear cells. J Neuroimmunol. 2004 150 : 163 77.
    • (2004) J Neuroimmunol. , vol.150 , pp. 163-77
    • Iglesias, A.H.1    Camelo, S.2    Hwang, D.3    Villanueva, R.4    Stephanopoulos, G.5    Dangond, F.6
  • 221
    • 34447343304 scopus 로고    scopus 로고
    • Effects of histone deacetylation inhibition on neuronal differentiation of embryonic mouse neural stem cells
    • Balasubramaniyan V, Boddeke E, Bakels R, Kust B, Kooistra S, Veneman A, Copray S. Effects of histone deacetylation inhibition on neuronal differentiation of embryonic mouse neural stem cells. Neuroscience. 2006 143 : 939 51.
    • (2006) Neuroscience. , vol.143 , pp. 939-51
    • Balasubramaniyan, V.1    Boddeke, E.2    Bakels, R.3    Kust, B.4    Kooistra, S.5    Veneman, A.6    Copray, S.7
  • 222
    • 35448949103 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity induces developmental plasticity in oligodendrocyte precursor cells
    • Lyssiotis CA, Walker J, Wu C, Kondo T, Schultz PG, Wu X. Inhibition of histone deacetylase activity induces developmental plasticity in oligodendrocyte precursor cells. Proc Natl Acad Sci USA. 2007 104 : 14982 7.
    • (2007) Proc Natl Acad Sci USA. , vol.104 , pp. 14982-7
    • Lyssiotis, C.A.1    Walker, J.2    Wu, C.3    Kondo, T.4    Schultz, P.G.5    Wu, X.6
  • 223
    • 34447130226 scopus 로고    scopus 로고
    • The glial or neuronal fate choice of oligodendrocyte progenitors is modulated by their ability to acquire an epigenetic memory
    • Liu A, Han YR, Li J, Sun D, Ouyang M, Plummer MR, Casaccia-Bonnefil P. The glial or neuronal fate choice of oligodendrocyte progenitors is modulated by their ability to acquire an epigenetic memory. J Neurosci. 2007 27 : 7339 43.
    • (2007) J Neurosci. , vol.27 , pp. 7339-43
    • Liu, A.1    Han, Y.R.2    Li, J.3    Sun, D.4    Ouyang, M.5    Plummer, M.R.6    Casaccia-Bonnefil, P.7
  • 225
    • 34848818037 scopus 로고    scopus 로고
    • Orphan nuclear receptor TLX recruits histone deacetylases to repress transcription and regulate neural stem cell proliferation
    • Sun G, Yu RT, Evans RM, Shi Y. Orphan nuclear receptor TLX recruits histone deacetylases to repress transcription and regulate neural stem cell proliferation. Proc Natl Acad Sci USA. 2007 104 : 15282 7.
    • (2007) Proc Natl Acad Sci USA. , vol.104 , pp. 15282-7
    • Sun, G.1    Yu, R.T.2    Evans, R.M.3    Shi, Y.4
  • 226
    • 4444220683 scopus 로고    scopus 로고
    • Activation of REST-NRSF target genes in neural stem cells is sufficient to cause neuronal differentiation
    • Su X, Kameoka S, Lentz S, Majumder S. Activation of REST-NRSF target genes in neural stem cells is sufficient to cause neuronal differentiation. Mol Cell Biol. 2004 24 : 8018 25.
    • (2004) Mol Cell Biol. , vol.24 , pp. 8018-25
    • Su, X.1    Kameoka, S.2    Lentz, S.3    Majumder, S.4
  • 227
    • 33846936237 scopus 로고    scopus 로고
    • RE1 silencing transcription factor maintains a repressive chromatin environment in embryonic hippocampal neural stem cells
    • Greenway DJ, Street M, Jeffries A, Buckley NJ. RE1 silencing transcription factor maintains a repressive chromatin environment in embryonic hippocampal neural stem cells. Stem Cells. 2007 25 : 354 63.
    • (2007) Stem Cells. , vol.25 , pp. 354-63
    • Greenway, D.J.1    Street, M.2    Jeffries, A.3    Buckley, N.J.4
  • 229
    • 0037239011 scopus 로고    scopus 로고
    • Modulation of splicing events in histone deacetylase 3 by various extracellular and signal transduction pathways
    • Gray SG, Iglesias AH, Teh BT, Dangond F. Modulation of splicing events in histone deacetylase 3 by various extracellular and signal transduction pathways. Gene Expr. 2003 11 : 13 21. (Pubitemid 36395881)
    • (2003) Gene Expression , vol.11 , Issue.1 , pp. 13-21
    • Gray, S.G.1    Iglesias, A.H.2    Teh, B.T.3    Dangond, F.4
  • 230
    • 34147136044 scopus 로고    scopus 로고
    • CREB-binding protein modulates repeat instability in a Drosophila model for polyQ disease
    • Jung J, Bonini N. CREB-binding protein modulates repeat instability in a Drosophila model for polyQ disease. Science. 2007 315 : 1857 9.
    • (2007) Science. , vol.315 , pp. 1857-9
    • Jung, J.1    Bonini, N.2
  • 231
    • 28844474597 scopus 로고    scopus 로고
    • SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB signaling
    • Chen J, Zhou Y, Mueller-Steiner S, Chen LF, Kwon H, Yi S, Mucke L, Gan L. SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB signaling. J Biol Chem. 2005 280 : 40364 74.
    • (2005) J Biol Chem. , vol.280 , pp. 40364-74
    • Chen, J.1    Zhou, Y.2    Mueller-Steiner, S.3    Chen, L.F.4    Kwon, H.5    Yi, S.6    Mucke, L.7    Gan, L.8
  • 233
    • 35748955537 scopus 로고    scopus 로고
    • A reversible form of lysine acetylation in the ER and Golgi lumen controls the molecular stabilization of BACE1
    • Costantini C, Ko MH, Jonas MC, Puglielli L. A reversible form of lysine acetylation in the ER and Golgi lumen controls the molecular stabilization of BACE1. Biochem J. 2007 407 : 383 95.
    • (2007) Biochem J. , vol.407 , pp. 383-95
    • Costantini, C.1    Ko, M.H.2    Jonas, M.C.3    Puglielli, L.4
  • 236
    • 33749583553 scopus 로고    scopus 로고
    • Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity
    • Kontopoulos E, Parvin JD, Feany MB. Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity. Hum Mol Genet. 2006 15 : 3012 23.
    • (2006) Hum Mol Genet. , vol.15 , pp. 3012-23
    • Kontopoulos, E.1    Parvin, J.D.2    Feany, M.B.3
  • 238
    • 33645076252 scopus 로고    scopus 로고
    • Additive neuroprotective effects of a his-tone deacetylase inhibitor and a catalytic antioxidant in a transgenic mouse model of amyotrophic lateral sclerosis
    • Petri S, Kiaei M, Kipiani K, Chen J, Calingasan NY, Crow JP, Beal MF. Additive neuroprotective effects of a his-tone deacetylase inhibitor and a catalytic antioxidant in a transgenic mouse model of amyotrophic lateral sclerosis. Neurobiol Dis. 2006 22 : 40 9.
    • (2006) Neurobiol Dis. , vol.22 , pp. 40-9
    • Petri, S.1    Kiaei, M.2    Kipiani, K.3    Chen, J.4    Calingasan, N.Y.5    Crow, J.P.6    Beal, M.F.7
  • 239
    • 34250612194 scopus 로고    scopus 로고
    • Sodium valproate exerts neuroprotective effects in vivo through CREB-binding protein-dependent mechanisms but does not improve survival in an amy-otrophic lateral sclerosis mouse model
    • Rouaux C, Panteleeva I, Rene F, Gonzalez de Aguilar JL, Echaniz-Laguna A, Dupuis L, Menger Y, Boutillier AL, Loeffler J P. Sodium valproate exerts neuroprotective effects in vivo through CREB-binding protein-dependent mechanisms but does not improve survival in an amy-otrophic lateral sclerosis mouse model. J Neurosci. 2007 27 : 5535 45.
    • (2007) J Neurosci. , vol.27 , pp. 5535-45
    • Rouaux, C.1    Panteleeva, I.2    Rene, F.3    Gonzalez De Aguilar, J.L.4    Echaniz-Laguna, A.5    Dupuis, L.6    Menger, Y.7    Boutillier, A.L.8    Loeffler, J.P.9
  • 240
    • 36148950997 scopus 로고    scopus 로고
    • FDA approval summary: Vorinostat for treatment of advanced primary cutaneous T-cell lymphoma
    • Mann BS, Johnson JR, Cohen MH, Justice R, Pazdur R. FDA approval summary: vorinostat for treatment of advanced primary cutaneous T-cell lymphoma. Oncologist. 2007 12 : 1247 52.
    • (2007) Oncologist. , vol.12 , pp. 1247-52
    • Mann, B.S.1    Johnson, J.R.2    Cohen, M.H.3    Justice, R.4    Pazdur, R.5
  • 241
    • 0036892569 scopus 로고    scopus 로고
    • Major phase i biotransformation pathways of Trichostatin a in rat hepatocytes and in rat and human liver microsomes
    • Elaut G, Torok G, Vinken M, Laus G, Papeleu P, Tourwe D, Rogiers V. Major phase I biotransformation pathways of Trichostatin a in rat hepatocytes and in rat and human liver microsomes. Drug Metab Dispos. 2002 30 : 1320 8.
    • (2002) Drug Metab Dispos. , vol.30 , pp. 1320-8
    • Elaut, G.1    Torok, G.2    Vinken, M.3    Laus, G.4    Papeleu, P.5    Tourwe, D.6    Rogiers, V.7
  • 242
    • 4644314055 scopus 로고    scopus 로고
    • Plasma pharmacokinetics and metabolism of the histone deacetylase inhibitor trichostatin a after intraperitoneal administration to mice
    • Sanderson L, Taylor GW, Aboagye EO, Alao JP, Latigo JR, Coombes RC, Vigushin DM. Plasma pharmacokinetics and metabolism of the histone deacetylase inhibitor trichostatin a after intraperitoneal administration to mice. Drug Metab Dispos. 2004 32 : 1132 8.
    • (2004) Drug Metab Dispos. , vol.32 , pp. 1132-8
    • Sanderson, L.1    Taylor, G.W.2    Aboagye, E.O.3    Alao, J.P.4    Latigo, J.R.5    Coombes, R.C.6    Vigushin, D.M.7
  • 243
    • 18444395839 scopus 로고    scopus 로고
    • Identification of cytochrome P450 enzymes involved in the metabolism of FK228, a potent histone deacetylase inhibitor, in human liver micro-somes
    • Shiraga T, Tozuka Z, Ishimura R, Kawamura A, Kagayama A. Identification of cytochrome P450 enzymes involved in the metabolism of FK228, a potent histone deacetylase inhibitor, in human liver micro-somes. Biol Pharm Bull. 2005 28 : 124 9.
    • (2005) Biol Pharm Bull. , vol.28 , pp. 124-9
    • Shiraga, T.1    Tozuka, Z.2    Ishimura, R.3    Kawamura, A.4    Kagayama, A.5
  • 245
    • 33846261713 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors for cancer therapy
    • Kim TY, Bang YJ, Robertson KD. Histone deacetylase inhibitors for cancer therapy. Epigenetics. 2006 1 : 14 23.
    • (2006) Epigenetics. , vol.1 , pp. 14-23
    • Kim, T.Y.1    Bang, Y.J.2    Robertson, K.D.3
  • 248
    • 33244458274 scopus 로고    scopus 로고
    • Potential role of histone deacetylase inhibitors in mesothelioma: Clinical experience with suberoylanilide hydroxamic acid
    • Krug LM, Curley T, Schwartz L, Richardson S, Marks P, Chiao J, Kelly WK. Potential role of histone deacetylase inhibitors in mesothelioma: clinical experience with suberoylanilide hydroxamic acid. Clin Lung Cancer. 2006 7 : 257 61.
    • (2006) Clin Lung Cancer. , vol.7 , pp. 257-61
    • Krug, L.M.1    Curley, T.2    Schwartz, L.3    Richardson, S.4    Marks, P.5    Chiao, J.6    Kelly, W.K.7
  • 251
    • 38149140216 scopus 로고    scopus 로고
    • Phase II trial of the histone deacetylase inhibitor vorinostat (Zolinzatrade mark, suberoylanilide hydroxamic acid, SAHA) in patients with recurrent and-or metastatic head and neck cancer
    • Blumenschein GR Jr., Kies MS, Papadimitrakopoulou VA, Lu C, Kumar AJ, Ricker JL, Chiao JH, Chen C, Frankel SR. Phase II trial of the histone deacetylase inhibitor vorinostat (Zolinzatrade mark, suberoylanilide hydroxamic acid, SAHA) in patients with recurrent and-or metastatic head and neck cancer. Invest New Drugs. 2008 26 : 81 7.
    • (2008) Invest New Drugs. , vol.26 , pp. 81-7
    • Blumenschein Jr., G.R.1    Kies, M.S.2    Papadimitrakopoulou, V.A.3    Lu, C.4    Kumar, A.J.5    Ricker, J.L.6    Chiao, J.H.7    Chen, C.8    Frankel, S.R.9
  • 253
  • 257
    • 36248970599 scopus 로고    scopus 로고
    • Sodium phenylbutyrate in Huntington's disease: A dose-finding study
    • Hogarth P, Lovrecic L, Krainc D. Sodium phenylbutyrate in Huntington's disease: a dose-finding study. Mov Disord. 2007 22 : 1962 4.
    • (2007) Mov Disord. , vol.22 , pp. 1962-4
    • Hogarth, P.1    Lovrecic, L.2    Krainc, D.3
  • 262
    • 33845898832 scopus 로고    scopus 로고
    • Phase i dose escalation clinical trial of phenylbu-tyrate sodium administered twice daily to patients with advanced solid tumors
    • Camacho LH, Olson J, Tong WP, Young CW, Spriggs DR, Malkin MG. Phase I dose escalation clinical trial of phenylbu-tyrate sodium administered twice daily to patients with advanced solid tumors. Invest New Drugs. 2007 25 : 131 8.
    • (2007) Invest New Drugs. , vol.25 , pp. 131-8
    • Camacho, L.H.1    Olson, J.2    Tong, W.P.3    Young, C.W.4    Spriggs, D.R.5    Malkin, M.G.6
  • 265
    • 67249141113 scopus 로고    scopus 로고
    • A phase II clinical trial of oral valproic acid in patients with castration-resistant prostate cancers using an intensive biomarker sampling Strategy
    • Sharma S, Symanowski J, Wong B, Dino P, Manno P, Vogelzang N. A phase II clinical trial of oral valproic acid in patients with castration-resistant prostate cancers using an intensive biomarker sampling Strategy. Transl Oncol. 2008 1 : 141 7.
    • (2008) Transl Oncol. , vol.1 , pp. 141-7
    • Sharma, S.1    Symanowski, J.2    Wong, B.3    Dino, P.4    Manno, P.5    Vogelzang, N.6
  • 273
    • 10844248177 scopus 로고    scopus 로고
    • Phase i study of oral CI-994 in combination with carboplatin and paclitaxel in the treatment of patients with advanced solid tumors
    • Pauer LR, Olivares J, Cunningham C, Williams A, Grove W, Kraker A, Olson S, Nemunaitis J. Phase I study of oral CI-994 in combination with carboplatin and paclitaxel in the treatment of patients with advanced solid tumors. Cancer Invest. 2004 22 : 886 96.
    • (2004) Cancer Invest. , vol.22 , pp. 886-96
    • Pauer, L.R.1    Olivares, J.2    Cunningham, C.3    Williams, A.4    Grove, W.5    Kraker, A.6    Olson, S.7    Nemunaitis, J.8
  • 278
    • 38949144400 scopus 로고    scopus 로고
    • Tolerability, pharmacodynamics, and pharmacokinetics studies of depsipeptide (romidepsin) in patients with acute myelogenous leukemia or advanced myelodysplastic syndromes
    • Klimek VM, Fircanis S, Maslak P, Guernah I, Baum M, Wu N, Panageas K, Wright JJ, Pandolfi PP, Nimer SD. Tolerability, pharmacodynamics, and pharmacokinetics studies of depsipeptide (romidepsin) in patients with acute myelogenous leukemia or advanced myelodysplastic syndromes. Clin Cancer Res. 2008 14 : 826 32.
    • (2008) Clin Cancer Res. , vol.14 , pp. 826-32
    • Klimek, V.M.1    Fircanis, S.2    Maslak, P.3    Guernah, I.4    Baum, M.5    Wu, N.6    Panageas, K.7    Wright, J.J.8    Pandolfi, P.P.9    Nimer, S.D.10
  • 281
    • 33746035691 scopus 로고    scopus 로고
    • Cardiotoxicity of histone deacetylase inhibitor depsipeptide in patients with metastatic neuroendocrine tumors
    • DOI 10.1158/1078-0432.CCR-05-2689
    • Shah MH, Binkley P, Chan K, Xiao J, Arbogast D, Collamore M, Farra Y, Young D, Grever M. Cardiotoxicity of histone deacetylase inhibitor depsipeptide in patients with metastatic neuroendocrine tumors. Clin Cancer Res. 2006 12 : 3997 4003. (Pubitemid 44078086)
    • (2006) Clinical Cancer Research , vol.12 , Issue.13 , pp. 3997-4003
    • Shah, M.H.1    Binkley, P.2    Chan, K.3    Xiao, J.4    Arbogast, D.5    Collamore, M.6    Farra, Y.7    Young, D.8    Grever, M.9
  • 286
    • 58149377828 scopus 로고    scopus 로고
    • Multicenter phase II trial of the histone deacetylase inhibitor pyridylmethyl-N-{4-[(2-aminophenyl)-carbamoyl]-benzyl}-carbamate in pretreated metastatic melanoma
    • Hauschild A, Trefzer U, Garbe C, Kaehler KC, Ugurel S, Kiecker F, Eigentler T, Krissel H, Schott A, Schadendorf D. Multicenter phase II trial of the histone deacetylase inhibitor pyridylmethyl-N-{4-[(2-aminophenyl)-carbamoyl] -benzyl}-carbamate in pretreated metastatic melanoma. Melanoma Res. 2008 18 : 274 8.
    • (2008) Melanoma Res. , vol.18 , pp. 274-8
    • Hauschild, A.1    Trefzer, U.2    Garbe, C.3    Kaehler, K.C.4    Ugurel, S.5    Kiecker, F.6    Eigentler, T.7    Krissel, H.8    Schott, A.9    Schadendorf, D.10
  • 290
    • 49349104503 scopus 로고    scopus 로고
    • A phase i clinical trial of the histone deacetylase inhibitor belinostat in patients with advanced hematological neoplasia
    • Gimsing P, Hansen M, Knudsen LM, Knoblauch P, Christensen IJ, Ooi CE, Buhl-Jensen P. A phase I clinical trial of the histone deacetylase inhibitor belinostat in patients with advanced hematological neoplasia. Eur J Haematol. 2008 81 : 170 6.
    • (2008) Eur J Haematol. , vol.81 , pp. 170-6
    • Gimsing, P.1    Hansen, M.2    Knudsen, L.M.3    Knoblauch, P.4    Christensen, I.J.5    Ooi, C.E.6    Buhl-Jensen, P.7
  • 293
    • 31444438952 scopus 로고    scopus 로고
    • Pilot study of combination transcriptional modulation therapy with sodium phenylbutyrate and 5-azacytidine in patients with acute myeloid leukemia or myelodysplastic syndrome
    • Maslak P, Chanel S, Camacho LH, Soignet S, Pandolfi PP, Guernah I, Warrell R, Nimer S. Pilot study of combination transcriptional modulation therapy with sodium phenylbutyrate and 5-azacytidine in patients with acute myeloid leukemia or myelodysplastic syndrome. Leukemia. 2006 20 : 212 7.
    • (2006) Leukemia. , vol.20 , pp. 212-7
    • Maslak, P.1    Chanel, S.2    Camacho, L.H.3    Soignet, S.4    Pandolfi, P.P.5    Guernah, I.6    Warrell, R.7    Nimer, S.8
  • 296
    • 29744454120 scopus 로고    scopus 로고
    • The histone deacetylase (HDAC) inhibitor valproic acid as monotherapy or in combination with all-trans retinoic acid in patients with acute myeloid leukemia
    • Kuendgen A, Schmid M, Schlenk R, Knipp S, Hildebrandt B, Steidl C, Germing U, Haas R, Dohner H, Gattermann N. The histone deacetylase (HDAC) inhibitor valproic acid as monotherapy or in combination with all-trans retinoic acid in patients with acute myeloid leukemia. Cancer. 2006 106 : 112 9.
    • (2006) Cancer. , vol.106 , pp. 112-9
    • Kuendgen, A.1    Schmid, M.2    Schlenk, R.3    Knipp, S.4    Hildebrandt, B.5    Steidl, C.6    Germing, U.7    Haas, R.8    Dohner, H.9    Gattermann, N.10
  • 297
    • 29144481615 scopus 로고    scopus 로고
    • Results of a phase 2 study of valproic acid alone or in combination with all-trans retinoic acid in 75 patients with myelodysplastic syndrome and relapsed or refractory acute myeloid leukemia
    • Kuendgen A, Knipp S, Fox F, Strupp C, Hildebrandt B, Steidl C, Germing U, Haas R, Gattermann N. Results of a phase 2 study of valproic acid alone or in combination with all-trans retinoic acid in 75 patients with myelodysplastic syndrome and relapsed or refractory acute myeloid leukemia. Ann Hematol. 2005 84 : 61 6.
    • (2005) Ann Hematol. , vol.84 , pp. 61-6
    • Kuendgen, A.1    Knipp, S.2    Fox, F.3    Strupp, C.4    Hildebrandt, B.5    Steidl, C.6    Germing, U.7    Haas, R.8    Gattermann, N.9
  • 301
    • 34247152663 scopus 로고    scopus 로고
    • Combination of cytotoxic-differentiation therapy with 5-fluorouracil and phenylbutyrate in patients with advanced colorectal cancer
    • Sung MW, Waxman S. Combination of cytotoxic-differentiation therapy with 5-fluorouracil and phenylbutyrate in patients with advanced colorectal cancer. Anticancer Res. 2007 27 : 995 1001. (Pubitemid 46587012)
    • (2007) Anticancer Research , vol.27 , Issue.2 , pp. 995-1001
    • Sung, M.W.1    Waxman, S.2
  • 302
    • 33745629366 scopus 로고    scopus 로고
    • Gemcitabine plus CI-994 offers no advantage over gemcitabine alone in the treatment of patients with advanced pancreatic cancer: Results of a phase II randomized, double-blind, placebo-controlled, multi-center study
    • Richards DA, Boehm KA, Waterhouse DM, Wagener DJ, Krishnamurthi SS, Rosemurgy A, Grove W, Macdonald K, Gulyas S, Clark M, Dasse KD. Gemcitabine plus CI-994 offers no advantage over gemcitabine alone in the treatment of patients with advanced pancreatic cancer: results of a phase II randomized, double-blind, placebo-controlled, multi-center study. Ann Oncol. 2006 17 : 1096 102.
    • (2006) Ann Oncol. , vol.17 , pp. 1096-102
    • Richards, D.A.1    Boehm, K.A.2    Waterhouse, D.M.3    Wagener, D.J.4    Krishnamurthi, S.S.5    Rosemurgy, A.6    Grove, W.7    MacDonald, K.8    Gulyas, S.9    Clark, M.10    Dasse, K.D.11
  • 303
    • 0038819943 scopus 로고    scopus 로고
    • Ineffectiveness of histone deacetylase inhibitors to induce apoptosis involves the transcriptional activation of NF-kappa B through the Akt pathway
    • Mayo MW, Denlinger CE, Broad RM, Yeung F, Reilly ET, Shi Y, Jones DR. Ineffectiveness of histone deacetylase inhibitors to induce apoptosis involves the transcriptional activation of NF-kappa B through the Akt pathway. J Biol Chem. 2003 278 : 18980 9.
    • (2003) J Biol Chem. , vol.278 , pp. 18980-9
    • Mayo, M.W.1    Denlinger, C.E.2    Broad, R.M.3    Yeung, F.4    Reilly, E.T.5    Shi, Y.6    Jones, D.R.7
  • 304
    • 33845997798 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid induces Akt-mediated phosphorylation of p300, which promotes acetylation and transcriptional activation of RelA-p65
    • Liu Y, Denlinger CE, Rundall BK, Smith PW, Jones DR. Suberoylanilide hydroxamic acid induces Akt-mediated phosphorylation of p300, which promotes acetylation and transcriptional activation of RelA-p65. J Biol Chem. 2006 281 : 31359 68.
    • (2006) J Biol Chem. , vol.281 , pp. 31359-68
    • Liu, Y.1    Denlinger, C.E.2    Rundall, B.K.3    Smith, P.W.4    Jones, D.R.5
  • 305
    • 33645064880 scopus 로고    scopus 로고
    • Leptin, ghrelin, and adiponectin in epileptic patients treated with valproic acid
    • Greco R, Latini G, Chiarelli F, Iannetti P, Verrotti A. Leptin, ghrelin, and adiponectin in epileptic patients treated with valproic acid. Neurology. 2005 65 : 1808 9.
    • (2005) Neurology. , vol.65 , pp. 1808-9
    • Greco, R.1    Latini, G.2    Chiarelli, F.3    Iannetti, P.4    Verrotti, A.5
  • 307
    • 33748677979 scopus 로고    scopus 로고
    • Characterization of insulin secretion in Valproate-treated patients with epilepsy
    • Pylvanen V, Pakarinen A, Knip M, Isojarvi J. Characterization of insulin secretion in Valproate-treated patients with epilepsy. Epilepsia. 2006 47 : 1460 4.
    • (2006) Epilepsia. , vol.47 , pp. 1460-4
    • Pylvanen, V.1    Pakarinen, A.2    Knip, M.3    Isojarvi, J.4
  • 308
    • 33646091507 scopus 로고    scopus 로고
    • Insulin-related metabolic changes during treatment with valproate in patients with epilepsy
    • Pylvanen V, Pakarinen A, Knip M, Isojarvi J. Insulin-related metabolic changes during treatment with valproate in patients with epilepsy. Epilepsy Behav. 2006 8 : 643 8.
    • (2006) Epilepsy Behav. , vol.8 , pp. 643-8
    • Pylvanen, V.1    Pakarinen, A.2    Knip, M.3    Isojarvi, J.4
  • 309
    • 30944450833 scopus 로고    scopus 로고
    • Suppression of adiponectin gene expression by histone deacetylase inhibitor valproic acid
    • Qiao L, Schaack J, Shao J. Suppression of adiponectin gene expression by histone deacetylase inhibitor valproic acid. Endocrinology. 2006 147 : 865 74.
    • (2006) Endocrinology. , vol.147 , pp. 865-74
    • Qiao, L.1    Schaack, J.2    Shao, J.3
  • 311
    • 0346103734 scopus 로고    scopus 로고
    • Serum Insulin and Leptin Levels and Valproate-associated Obesity [3]
    • DOI 10.1111/j.0013-9580.2003.t01-2-33003.x
    • Verrotti A, di Corcia G, Salladini C, Trotta D, Morgese G, Chiarelli F. Serum insulin and leptin levels and valproate-associated obesity. Epilepsia. 2003 44 : 1606. (Pubitemid 38020203)
    • (2003) Epilepsia , vol.44 , Issue.12 , pp. 1606
    • Verrotti, A.1    Di Corcia, G.2    Salladini, C.3    Trotta, D.4    Morgese, G.5    Chiarelli, F.6
  • 312
    • 2442448425 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity by valproic acid blocks adipogenesis
    • Lagace DC, Nachtigal MW. Inhibition of histone deacetylase activity by valproic acid blocks adipogenesis. J Biol Chem. 2004 279 : 18851 60.
    • (2004) J Biol Chem. , vol.279 , pp. 18851-60
    • Lagace, D.C.1    Nachtigal, M.W.2
  • 314
    • 0141884374 scopus 로고    scopus 로고
    • Regulation of microglial inflammatory response by histone deacetylase inhibitors
    • Suuronen T, Huuskonen J, Pihlaja R, Kyrylenko S, Salminen A. Regulation of microglial inflammatory response by histone deacetylase inhibitors. J Neurochem. 2003 87 : 407 16.
    • (2003) J Neurochem. , vol.87 , pp. 407-16
    • Suuronen, T.1    Huuskonen, J.2    Pihlaja, R.3    Kyrylenko, S.4    Salminen, A.5
  • 315
    • 0038522853 scopus 로고    scopus 로고
    • Multidimensional chemical genetic analysis of diversity-oriented synthesis-derived deacetylase inhibitors using cell-based assays
    • Haggarty SJ, Koeller KM, Wong JC, Butcher RA, Schreiber SL. Multidimensional chemical genetic analysis of diversity-oriented synthesis-derived deacetylase inhibitors using cell-based assays. Chem Biol. 2003 10 : 383 96.
    • (2003) Chem Biol. , vol.10 , pp. 383-96
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Butcher, R.A.4    Schreiber, S.L.5
  • 317
    • 16544381001 scopus 로고    scopus 로고
    • Lack of effect of oral 4-phenylbutyrate on serum alpha-1-antit-rypsin in patients with alpha-1-antitrypsin deficiency: A preliminary study
    • Teckman JH. Lack of effect of oral 4-phenylbutyrate on serum alpha-1-antit-rypsin in patients with alpha-1-antitrypsin deficiency: a preliminary study. J Pediatr Gastroenterol Nutr. 2004 39 : 34 7.
    • (2004) J Pediatr Gastroenterol Nutr. , vol.39 , pp. 34-7
    • Teckman, J.H.1
  • 321
    • 37549010715 scopus 로고    scopus 로고
    • Histone deacetylase 6 regulates growth factor-induced actin remodeling and endocytosis
    • Gao YS, Hubbert CC, Lu J, Lee YS, Lee JY, Yao TP. Histone deacetylase 6 regulates growth factor-induced actin remodeling and endocytosis. Mol Cell Biol. 2007 27 : 8637 47.
    • (2007) Mol Cell Biol. , vol.27 , pp. 8637-47
    • Gao, Y.S.1    Hubbert, C.C.2    Lu, J.3    Lee, Y.S.4    Lee, J.Y.5    Yao, T.P.6
  • 322
    • 34548075217 scopus 로고    scopus 로고
    • Hydroxamic acid analogue histone deacetylase inhibitors attenuate estrogen receptor-alpha levels and transcriptional activity: A result of hyperacetylation and inhibition of chaperone function of heat shock protein 90
    • Fiskus W, Ren Y, Mohapatra A, Bali P, Mandawat A, Rao R, Herger B, Yang Y, Atadja P, Wu J, Bhalla K. Hydroxamic acid analogue histone deacetylase inhibitors attenuate estrogen receptor-alpha levels and transcriptional activity: a result of hyperacetylation and inhibition of chaperone function of heat shock protein 90. Clin Cancer Res. 2007 13 : 4882 90.
    • (2007) Clin Cancer Res. , vol.13 , pp. 4882-90
    • Fiskus, W.1    Ren, Y.2    Mohapatra, A.3    Bali, P.4    Mandawat, A.5    Rao, R.6    Herger, B.7    Yang, Y.8    Atadja, P.9    Wu, J.10    Bhalla, K.11
  • 325
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali P, Pranpat M, Bradner J, Balasis M, Fiskus W, Guo F, Rocha K, Kumaraswamy S, Boyapalle S, Atadja P, Seto E, Bhalla K. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J Biol Chem. 2005 280 : 26729 34.
    • (2005) J Biol Chem. , vol.280 , pp. 26729-34
    • Bali, P.1    Pranpat, M.2    Bradner, J.3    Balasis, M.4    Fiskus, W.5    Guo, F.6    Rocha, K.7    Kumaraswamy, S.8    Boyapalle, S.9    Atadja, P.10    Seto, E.11    Bhalla, K.12
  • 326
    • 33644780111 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1alpha
    • Kong X, Lin Z, Liang D, Fath D, Sang N, Caro J. Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1alpha. Mol Cell Biol. 2006 26 : 2019 28.
    • (2006) Mol Cell Biol. , vol.26 , pp. 2019-28
    • Kong, X.1    Lin, Z.2    Liang, D.3    Fath, D.4    Sang, N.5    Caro, J.6
  • 327
    • 0037088610 scopus 로고    scopus 로고
    • Human Class i Histone Deacetylase Complexes Show Enhanced Catalytic Activity in the Presence of ATP and Co-immunoprecipitate with the ATP-dependent Chaperone Protein Hsp70
    • Johnson CA, White DA, Lavender JS, O'Neill LP, Turner BM. Human Class I Histone Deacetylase Complexes Show Enhanced Catalytic Activity in the Presence of ATP and Co-immunoprecipitate with the ATP-dependent Chaperone Protein Hsp70. J Biol Chem. 2002 277 : 9590 7.
    • (2002) J Biol Chem. , vol.277 , pp. 9590-7
    • Johnson, C.A.1    White, D.A.2    Lavender, J.S.3    O'Neill, L.P.4    Turner, B.M.5
  • 329
    • 34447103301 scopus 로고    scopus 로고
    • 4-Phenylbutyrate rescues trafficking incompetent mutant alpha-galactosidase A without restoring its functionality
    • Yam GH, Roth J, Zuber C. 4-Phenylbutyrate rescues trafficking incompetent mutant alpha-galactosidase A without restoring its functionality. Biochem Biophys Res Commun. 2007 360 : 375 80.
    • (2007) Biochem Biophys Res Commun. , vol.360 , pp. 375-80
    • Yam, G.H.1    Roth, J.2    Zuber, C.3
  • 330
    • 38049180869 scopus 로고    scopus 로고
    • Signal sequence mutation in autosomal dominant form of hypoparathyroidism induces apoptosis that is corrected by a chemical chaperone
    • Datta R, Waheed A, Shah GN, Sly WS. Signal sequence mutation in autosomal dominant form of hypoparathyroidism induces apoptosis that is corrected by a chemical chaperone. Proc Natl Acad Sci USA. 2007 104 : 19989 94.
    • (2007) Proc Natl Acad Sci USA. , vol.104 , pp. 19989-94
    • Datta, R.1    Waheed, A.2    Shah, G.N.3    Sly, W.S.4
  • 331
    • 41249096143 scopus 로고    scopus 로고
    • BAX inhibitor-1 modulates endoplasmic reticulum stress-mediated programmed cell death in Arabidopsis
    • Watanabe N, Lam E. BAX inhibitor-1 modulates endoplasmic reticulum stress-mediated programmed cell death in Arabidopsis. J Biol Chem. 2008 283 : 3200 10.
    • (2008) J Biol Chem. , vol.283 , pp. 3200-10
    • Watanabe, N.1    Lam, E.2
  • 332
    • 0842328581 scopus 로고    scopus 로고
    • Cell-type specific regulation of calreticulin and Bcl-2 expression by mood stabilizer drugs
    • Corson TW, Woo KK, Li PP, Warsh JJ. Cell-type specific regulation of calreticulin and Bcl-2 expression by mood stabilizer drugs. Eur Neuropsychopharmacol. 2004 14 : 143 50.
    • (2004) Eur Neuropsychopharmacol. , vol.14 , pp. 143-50
    • Corson, T.W.1    Woo, K.K.2    Li, P.P.3    Warsh, J.J.4
  • 334
    • 34248530339 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors exhibit anti-inflammatory and neuroprotective effects in a rat permanent ischemic model of stroke: Multiple mechanisms of action
    • DOI 10.1124/jpet.107.120188
    • Kim HJ, Rowe M, Ren M, Hong JS, Chen PS, Chuang DM. Histone deacetylase inhibitors exhibit anti-inflammatory and neuroprotective effects in a rat permanent ischemic model of stroke: multiple mechanisms of action. J Pharmacol Exp Ther. 2007 321 : 892 901. (Pubitemid 46762687)
    • (2007) Journal of Pharmacology and Experimental Therapeutics , vol.321 , Issue.3 , pp. 892-901
    • Hyeon, J.K.1    Rowe, M.2    Ren, M.3    Hong, J.-S.4    Chen, P.-S.5    Chuang, D.-M.6
  • 335
    • 3042651448 scopus 로고    scopus 로고
    • Valproic acid reduces brain damage induced by transient focal cerebral ischemia in rats: Potential roles of histone deacetylase inhibition and heat shock protein induction
    • Ren M, Leng Y, Jeong M, Leeds PR, Chuang DM. Valproic acid reduces brain damage induced by transient focal cerebral ischemia in rats: potential roles of histone deacetylase inhibition and heat shock protein induction. J Neurochem. 2004 89 : 1358 67.
    • (2004) J Neurochem. , vol.89 , pp. 1358-67
    • Ren, M.1    Leng, Y.2    Jeong, M.3    Leeds, P.R.4    Chuang, D.M.5
  • 336
    • 8344270103 scopus 로고    scopus 로고
    • Valproate is neuroprotective against malonate toxicity in rat striatum: An association with augmentation of high-affinity glutamate uptake
    • Morland C, Boldingh KA, Iversen EG, Hassel B. Valproate is neuroprotective against malonate toxicity in rat striatum: an association with augmentation of high-affinity glutamate uptake. J Cereb Blood Flow Metab. 2004 24 : 1226 34.
    • (2004) J Cereb Blood Flow Metab. , vol.24 , pp. 1226-34
    • Morland, C.1    Boldingh, K.A.2    Iversen, E.G.3    Hassel, B.4
  • 338
    • 28844480953 scopus 로고    scopus 로고
    • Valproic acid-mediated Hsp70 induction and anti-apoptotic neuroprotection in SH-SY5Y cells
    • Pan T, Li X, Xie W, Jankovic J, Le W. Valproic acid-mediated Hsp70 induction and anti-apoptotic neuroprotection in SH-SY5Y cells. FEBS Lett. 2005 579 : 6716 20.
    • (2005) FEBS Lett. , vol.579 , pp. 6716-20
    • Pan, T.1    Li, X.2    Xie, W.3    Jankovic, J.4    Le, W.5
  • 339
    • 16344382201 scopus 로고    scopus 로고
    • Protracted lithium treatment protects against the ER stress elicited by thapsigargin in rat PC12 cells: Roles of intracellular calcium, GRP78 and Bcl-2
    • Hiroi T, Wei H, Hough C, Leeds P, Chuang DM. Protracted lithium treatment protects against the ER stress elicited by thapsigargin in rat PC12 cells: roles of intracellular calcium, GRP78 and Bcl-2. Pharmacogenomics J. 2005 5 : 102 11.
    • (2005) Pharmacogenomics J. , vol.5 , pp. 102-11
    • Hiroi, T.1    Wei, H.2    Hough, C.3    Leeds, P.4    Chuang, D.M.5
  • 341
    • 0031889082 scopus 로고    scopus 로고
    • A pilot clinical trial of oral sodium 4-phenylbutyrate (Buphenyl) in deltaF508-homozygous cystic fibrosis patients: Partial restoration of nasal epithelial CFTR function
    • Rubenstein RC, Zeitlin PL. A pilot clinical trial of oral sodium 4-phenylbutyrate (Buphenyl) in deltaF508-homozygous cystic fibrosis patients: partial restoration of nasal epithelial CFTR function. Am J Respir Crit Care Med. 1998 157 : 484 90.
    • (1998) Am J Respir Crit Care Med. , vol.157 , pp. 484-90
    • Rubenstein, R.C.1    Zeitlin, P.L.2
  • 342
    • 0034805392 scopus 로고    scopus 로고
    • Sodium 4-phenylbutyrate downregulates HSC70 expression by facilitating mRNA degradation
    • Rubenstein RC, Lyons BM. Sodium 4-phenylbutyrate downregulates HSC70 expression by facilitating mRNA degradation. Am J Physiol Lung Cell Mol Physiol. 2001 281 : L43 51.
    • (2001) Am J Physiol Lung Cell Mol Physiol. , vol.281 , pp. 43-51
    • Rubenstein, R.C.1    Lyons, B.M.2
  • 343
    • 0030809817 scopus 로고    scopus 로고
    • In vitro pharmacologic restoration of CFTR-mediated chloride transport with sodium 4-phenylbutyrate in cystic fibrosis epithelial cells containing delta F508-CFTR
    • Rubenstein RC, Egan ME, Zeitlin PL. In vitro pharmacologic restoration of CFTR-mediated chloride transport with sodium 4-phenylbutyrate in cystic fibrosis epithelial cells containing delta F508-CFTR. J Clin Invest. 1997 100 : 2457 65.
    • (1997) J Clin Invest. , vol.100 , pp. 2457-65
    • Rubenstein, R.C.1    Egan, M.E.2    Zeitlin, P.L.3
  • 344
    • 4444371518 scopus 로고    scopus 로고
    • Modulation of deltaF508 cystic fibrosis transmembrane regulator trafficking and function with 4-phenylbutyrate and flavonoids
    • Lim M, McKenzie K, Floyd AD, Kwon E, Zeitlin PL. Modulation of deltaF508 cystic fibrosis transmembrane regulator trafficking and function with 4-phenylbutyrate and flavonoids. Am J Respir Cell Mol Biol. 2004 31 : 351 7.
    • (2004) Am J Respir Cell Mol Biol. , vol.31 , pp. 351-7
    • Lim, M.1    McKenzie, K.2    Floyd, A.D.3    Kwon, E.4    Zeitlin, P.L.5
  • 346
    • 33646897427 scopus 로고    scopus 로고
    • Functional and trafficking defects in ATP binding cassette A3 mutants associated with respiratory distress syndrome
    • Cheong N, Madesh M, Gonzales LW, Zhao M, Yu K, Ballard PL, Shuman H. Functional and trafficking defects in ATP binding cassette A3 mutants associated with respiratory distress syndrome. J Biol Chem. 2006 281 : 9791 800.
    • (2006) J Biol Chem. , vol.281 , pp. 9791-800
    • Cheong, N.1    Madesh, M.2    Gonzales, L.W.3    Zhao, M.4    Yu, K.5    Ballard, P.L.6    Shuman, H.7
  • 347
    • 34250339695 scopus 로고    scopus 로고
    • 4-phenylbutyrate enhances the cell surface expression and the transport capacity of wild-type and mutated bile salt export pumps
    • Hayashi H, Sugiyama Y. 4-phenylbutyrate enhances the cell surface expression and the transport capacity of wild-type and mutated bile salt export pumps. Hepatology. 2007 45 : 1506 16.
    • (2007) Hepatology. , vol.45 , pp. 1506-16
    • Hayashi, H.1    Sugiyama, Y.2
  • 348
    • 14044261099 scopus 로고    scopus 로고
    • Valproate protects cells fom ER stress-induced lipid accumulation and apoptosis by inhibiting glycogen synthase kinase-3
    • DOI 10.1242/jcs.01562
    • Kim AJ, Shi Y, Austin RC, Werstuck GH. Valproate protects cells from ER stress-induced lipid accumulation and apoptosis by inhibiting glycogen synthase kinase-3. J Cell Sci. 2005 118 : 89 99. (Pubitemid 40277107)
    • (2005) Journal of Cell Science , vol.118 , Issue.1 , pp. 89-99
    • Kim, A.J.1    Shi, Y.2    Austin, R.C.3    Werstuck, G.H.4
  • 349
    • 23044487814 scopus 로고    scopus 로고
    • It's about time: Scheduling alters effect of histone deacetylase inhibitors on camptothecin-treated cells
    • Bevins RL, Zimmer SG. It's about time: scheduling alters effect of histone deacetylase inhibitors on camptothecin-treated cells. Cancer Res. 2005 65 : 6957 66.
    • (2005) Cancer Res. , vol.65 , pp. 6957-66
    • Bevins, R.L.1    Zimmer, S.G.2
  • 351
    • 42049118549 scopus 로고    scopus 로고
    • Isoform-selective histone deacetylase inhibitors
    • Itoh Y, Suzuki T, Miyata N. Isoform-selective histone deacetylase inhibitors. Curr Pharm Des. 2008 14 : 529 44.
    • (2008) Curr Pharm Des. , vol.14 , pp. 529-44
    • Itoh, Y.1    Suzuki, T.2    Miyata, N.3
  • 352
    • 42049096372 scopus 로고    scopus 로고
    • Chemical origins of isoform selectivity in histone deacetylase inhibitors
    • Butler KV, Kozikowski A P. Chemical origins of isoform selectivity in histone deacetylase inhibitors. Curr Pharm Des. 2008 14 : 505 28.
    • (2008) Curr Pharm Des. , vol.14 , pp. 505-28
    • Butler, K.V.1    Kozikowski, A.P.2
  • 353
    • 43749109171 scopus 로고    scopus 로고
    • A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas
    • Balasubramanian S, Ramos J, Luo W, Sirisawad M, Verner E, Buggy JJ. A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas. Leukemia. 2008 22 : 1026 34.
    • (2008) Leukemia. , vol.22 , pp. 1026-34
    • Balasubramanian, S.1    Ramos, J.2    Luo, W.3    Sirisawad, M.4    Verner, E.5    Buggy, J.J.6
  • 354
    • 33744805399 scopus 로고    scopus 로고
    • Specific activation of microRNA-127 with downregulation of the protooncogene BCL6 by chromatin-modifying drugs in human cancer cells
    • Saito Y, Liang G, Egger G, Friedman JM, Chuang JC, Coetzee GA, Jones PA. Specific activation of microRNA-127 with downregulation of the protooncogene BCL6 by chromatin-modifying drugs in human cancer cells. Cancer Cell. 2006 9 : 435 43.
    • (2006) Cancer Cell. , vol.9 , pp. 435-43
    • Saito, Y.1    Liang, G.2    Egger, G.3    Friedman, J.M.4    Chuang, J.C.5    Coetzee, G.A.6    Jones, P.A.7
  • 355
    • 32944462300 scopus 로고    scopus 로고
    • Rapid alteration of microRNA levels by histone deacetylase inhibition
    • Scott GK, Mattie MD, Berger CE, Benz SC, Benz CC. Rapid alteration of microRNA levels by histone deacetylase inhibition. Cancer Res. 2006 66 : 1277 81.
    • (2006) Cancer Res. , vol.66 , pp. 1277-81
    • Scott, G.K.1    Mattie, M.D.2    Berger, C.E.3    Benz, S.C.4    Benz, C.C.5
  • 356
    • 38349191617 scopus 로고    scopus 로고
    • CpG island hypermethylation of tumor suppressor microRNAs in human cancer
    • Lujambio A, Esteller M. CpG island hypermethylation of tumor suppressor microRNAs in human cancer. Cell Cycle. 2007 6 : 1455 9.
    • (2007) Cell Cycle. , vol.6 , pp. 1455-9
    • Lujambio, A.1    Esteller, M.2
  • 358
    • 57749089758 scopus 로고    scopus 로고
    • Downregulation of microRNA-1 (miR-1) in lung cancer: Suppression of tumorigenic property of lung cancer cells and their sensitization to doxorubicin induced apoptosis bymiR-1
    • Epub ahead of print M, Kettmann R, Dequiedt F. Class IIa histone deacetylases: regulating the regulators. Oncogene. 2007 26 : 5450 67
    • Nasser MW, Datta J, Nuovo G, Kutay H, Motiwala T, Majumder S, Wang B, Suster S, Jacob ST, Ghoshal K. Downregulation of microRNA-1 (miR-1) in lung cancer: Suppression of tumorigenic property of lung cancer cells and their sensitization to doxorubicin induced apoptosis bymiR-1. J Biol Chem. 2008 M804788200 Epub ahead of print M, Kettmann R, Dequiedt F. Class IIa histone deacetylases: regulating the regulators. Oncogene. 2007 26 : 5450 67.
    • (2008) J Biol Chem. , pp. 804788200
    • Nasser, M.W.1    Datta, J.2    Nuovo, G.3    Kutay, H.4    Motiwala, T.5    Majumder, S.6    Wang, B.7    Suster, S.8    Jacob, S.T.9    Ghoshal, K.10
  • 359
    • 39749127166 scopus 로고    scopus 로고
    • The Rpd3-Hda1 family of lysine deacetylases: From bacteria and yeast to mice and men
    • Yang XJ, Seto E. The Rpd3-Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men. Nat Rev Mol Cell Biol. 2008 9 : 206 18.
    • (2008) Nat Rev Mol Cell Biol. , vol.9 , pp. 206-18
    • Yang, X.J.1    Seto, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.