메뉴 건너뛰기




Volumn , Issue , 2011, Pages 273-309

Natural product inhibitors and activators of histone deacetylases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84973098864     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1142/9789814335386_0004     Document Type: Chapter
Times cited : (1)

References (104)
  • 1
    • 1542514783 scopus 로고    scopus 로고
    • Targeted histone deacetylase inhibition for cancer therapy
    • Vigushin DM, Coombes RC. (2004) Targeted histone deacetylase inhibition for cancer therapy. Curr Cancer Drug Targets 4: 205-218.
    • (2004) Curr Cancer Drug Targets , vol.4 , pp. 205-218
    • Vigushin, D.M.1    Coombes, R.C.2
  • 3
  • 4
  • 5
    • 18544367699 scopus 로고    scopus 로고
    • Apicidin, a histone deacetylase inhibitor, induces apoptosis and Fas/Fas ligand expression in human acute promyelocytic leukemia cells
    • Kwon SH, Ahn SH, Kim YK, Bae GU, Yoon JW, Hong S, Lee HY, Lee YW, Lee HW, Han JW. (2002) Apicidin, a histone deacetylase inhibitor, induces apoptosis and Fas/Fas ligand expression in human acute promyelocytic leukemia cells. J Biol Chem 277: 2073-2080.
    • (2002) J Biol Chem , vol.277 , pp. 2073-2080
    • Kwon, S.H.1    Ahn, S.H.2    Kim, Y.K.3    Bae, G.U.4    Yoon, J.W.5    Hong, S.6    Lee, H.Y.7    Lee, Y.W.8    Lee, H.W.9    Han, J.W.10
  • 8
    • 0842277812 scopus 로고    scopus 로고
    • Histone deacety-lase (HDAC) inhibitor activation of p21WAF1 involves changes in promoter-associated proteins, including HDAC1
    • Gui CV, Ngo L, Xu WS, Richon VM, Marks PA. (2004) Histone deacety-lase (HDAC) inhibitor activation of p21WAF1 involves changes in promoter-associated proteins, including HDAC1. Proc Natl Acad Sci USA 101: 1241-1246.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1241-1246
    • Gui, C.V.1    Ngo, L.2    Xu, W.S.3    Richon, V.M.4    Marks, P.A.5
  • 9
    • 0038676409 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity by butyrate
    • Davie JR. (2003) Inhibition of histone deacetylase activity by butyrate. J Nutr 133: 2485S-2493S.
    • (2003) J Nutr , vol.133
    • Davie, J.R.1
  • 11
    • 0036939240 scopus 로고    scopus 로고
    • Growth arrest of HPV-positive cells after histone deacetylase inhibition is independent of E6/E7 oncogene expression
    • Finzer P, Ventz R, Kuntzen C, Seibert N, Soto U, Rosl F. (2002) Growth arrest of HPV-positive cells after histone deacetylase inhibition is independent of E6/E7 oncogene expression. Virology 304: 265-273.
    • (2002) Virology , vol.304 , pp. 265-273
    • Finzer, P.1    Ventz, R.2    Kuntzen, C.3    Seibert, N.4    Soto, U.5    Rosl, F.6
  • 12
    • 18644367141 scopus 로고    scopus 로고
    • Induction and superinduction of growth arrest and DNA damage gene45(GADD45) alpha and beta messenger RNAs by histone deactylase inhibitors trichostatin A (TSA) and butyrate in SW620 human colon carcinoma cells
    • Chen Z, Clark S, Birkeland M, Sung CM, Lago A, Liu R, Kirkpatrick R, Johnanson K, Winkler JD, Hu E. (2002) Induction and superinduction of growth arrest and DNA damage gene45(GADD45) alpha and beta messenger RNAs by histone deactylase inhibitors trichostatin A (TSA) and butyrate in SW620 human colon carcinoma cells. Cancer Lett 188: 127-140.
    • (2002) Cancer Lett , vol.188 , pp. 127-140
    • Chen, Z.1    Clark, S.2    Birkeland, M.3    Sung, C.M.4    Lago, A.5    Liu, R.6    Kirkpatrick, R.7    Johnanson, K.8    Winkler, J.D.9    Hu, E.10
  • 13
    • 0036252352 scopus 로고    scopus 로고
    • The effects of short-chain fatty acids on human colon cancer cell phenotype are associated with histone hyperacetylation
    • Hinnebusch BF, Meng S, Wu JT, Archer SY, Hodin RA. (2002) The effects of short-chain fatty acids on human colon cancer cell phenotype are associated with histone hyperacetylation. J Nutr 132: 1012-1017.
    • (2002) J Nutr , vol.132 , pp. 1012-1017
    • Hinnebusch, B.F.1    Meng, S.2    Wu, J.T.3    Archer, S.Y.4    Hodin, R.A.5
  • 14
    • 0033740191 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors decrease proliferation and modulate cell cycle gene expression in normal mammary epithelial cells
    • Davis T, Kennedy C, Chiew YE, Clarke CL, deFaxio A. (2000) Histone deacetylase inhibitors decrease proliferation and modulate cell cycle gene expression in normal mammary epithelial cells. Clin Cancer Res 6: 4334-4342.
    • (2000) Clin Cancer Res , vol.6 , pp. 4334-4342
    • Davis, T.1    Kennedy, C.2    Chiew, Y.E.3    Clarke, C.L.4    Defaxio, A.5
  • 15
    • 0035837658 scopus 로고    scopus 로고
    • Paradoxical effects of trichostatin A: Inhibition of NF-Y-associated histone acetyltransferase activity, phosphorylation of hGCN5 and down-regulation of cyclin A and B1 mRNA
    • Nair AR, Boersma LJ, Schilz L, Chaudhry MA, Muschel RJ, Chaudry A. (2001) Paradoxical effects of trichostatin A: Inhibition of NF-Y-associated histone acetyltransferase activity, phosphorylation of hGCN5 and down-regulation of cyclin A and B1 mRNA. Cancer Lett 166: 55-64.
    • (2001) Cancer Lett , vol.166 , pp. 55-64
    • Nair, A.R.1    Boersma, L.J.2    Schilz, L.3    Chaudhry, M.A.4    Muschel, R.J.5    Chaudry, A.6
  • 16
    • 0029693220 scopus 로고    scopus 로고
    • The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation
    • Van Lint C, Emiliani S, Verdin E. (1996) The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expression 5: 245-253.
    • (1996) Gene Expression , vol.5 , pp. 245-253
    • Van Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 17
  • 18
    • 0020693603 scopus 로고
    • Effect of polar organic compounds on leukemic cells. Butyrate-induced partial remission of acute myelogenous leukemia in a child
    • Novogrodsky A, Dvir A, Ravid A, Shkolnik T, Stenzel KH, Rubin AL, Zaizov R. (1983) Effect of polar organic compounds on leukemic cells. Butyrate-induced partial remission of acute myelogenous leukemia in a child. Cancer 51: 9-14.
    • (1983) Cancer , vol.51 , pp. 9-14
    • Novogrodsky, A.1    Dvir, A.2    Ravid, A.3    Shkolnik, T.4    Stenzel, K.H.5    Rubin, A.L.6    Zaizov, R.7
  • 19
    • 31544481927 scopus 로고    scopus 로고
    • Histone deacetylases as targets for dietary cancer preventive agents: Lessons learned with butyrate, diallyl disulfide, and sulforaphane
    • Myzak MC, Dashwood RH. (2006) Histone deacetylases as targets for dietary cancer preventive agents: Lessons learned with butyrate, diallyl disulfide, and sulforaphane. Current Drug Targets 7: 443-452.
    • (2006) Current Drug Targets , vol.7 , pp. 443-452
    • Myzak, M.C.1    Dashwood, R.H.2
  • 20
    • 0035000305 scopus 로고    scopus 로고
    • Transient vs. Prolonged histone hyperacetylation: Effects on colon cancer cell growth, differentiation, and apoptosis
    • Wu JT, Archer SY, Hinnebusch B, Meng S, Hodin RA. (2001) Transient vs. prolonged histone hyperacetylation: Effects on colon cancer cell growth, differentiation, and apoptosis. Am J Physiol Gastrointest Liver Physiol 280: G482-G490.
    • (2001) Am J Physiol Gastrointest Liver Physiol , vol.280 , pp. G482-G490
    • Wu, J.T.1    Archer, S.Y.2    Hinnebusch, B.3    Meng, S.4    Hodin, R.A.5
  • 21
    • 0035165096 scopus 로고    scopus 로고
    • Short-chain fatty acids inhibit invasive human colon cancer by modulating uPA, TIMP-1, TIMP-2, mutant p53, Bcl-2, BAX, p21 and PCNA protein expression in an in vitro cell culture model
    • Emenaker NJ, Calaf GM, Cox D, Basson MD, Qureshi N. (2001) Short-chain fatty acids inhibit invasive human colon cancer by modulating uPA, TIMP-1, TIMP-2, mutant p53, Bcl-2, BAX, p21 and PCNA protein expression in an in vitro cell culture model. JNutr 131: 3041S-3046S.
    • (2001) Jnutr , vol.131
    • Emenaker, N.J.1    Calaf, G.M.2    Cox, D.3    Basson, M.D.4    Qureshi, N.5
  • 22
    • 7244256107 scopus 로고    scopus 로고
    • Butyrate reduces liver metastasis of rat colon carcinoma cells in vivo and resistance to oxidative stress in vivo
    • Li X, Mikkelsen IM, Mortensen B, Winberg JO, Huseby NE. (2004) Butyrate reduces liver metastasis of rat colon carcinoma cells in vivo and resistance to oxidative stress in vivo. Clin Exp Metastasis 21: 331-338.
    • (2004) Clin Exp Metastasis , vol.21 , pp. 331-338
    • Li, X.1    Mikkelsen, I.M.2    Mortensen, B.3    Winberg, J.O.4    Huseby, N.E.5
  • 23
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • Johnstone RW. (2002) Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer. Nat Rev Drug Discov 1: 287-299.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 25
    • 0033173102 scopus 로고    scopus 로고
    • Increased acetylation of histones induced by diallyl disulfide and structurally related molecules
    • Lea MA, Randolph VM, Patel M. (1999) Increased acetylation of histones induced by diallyl disulfide and structurally related molecules. Int J Oncol 15: 347-352.
    • (1999) Int J Oncol , vol.15 , pp. 347-352
    • Lea, M.A.1    Randolph, V.M.2    Patel, M.3
  • 26
    • 0035156867 scopus 로고    scopus 로고
    • Induction of histone acetylation in rat liver and hepatoma by organosulfur compounds including diallyl disulfide
    • Lea MA, Randolph VM. (2001) Induction of histone acetylation in rat liver and hepatoma by organosulfur compounds including diallyl disulfide. Anticancer Res 21: 2841-2845.
    • (2001) Anticancer Res , vol.21 , pp. 2841-2845
    • Lea, M.A.1    Randolph, V.M.2
  • 27
    • 72249122960 scopus 로고    scopus 로고
    • Dietary Sulforaphane, a histone deacetylase inhibitor for cancer prevention
    • Ho E, Clarke JD, Dashwood RH. (2009) Dietary Sulforaphane, a histone deacetylase inhibitor for cancer prevention. J Nutr 139: 2393-2396.
    • (2009) J Nutr , vol.139 , pp. 2393-2396
    • Ho, E.1    Clarke, J.D.2    Dashwood, R.H.3
  • 28
    • 3242755145 scopus 로고    scopus 로고
    • Dially disulfide (DADS) increase histone acetylation and p21/waf1/cip1 expression in human colon tumor cell lines
    • Druesne N, Pagniez A, Mayeur C, Thomas M, Cherbuy C, Duee PH, Martel P, Chaumontet C. (2004) Dially disulfide (DADS) increase histone acetylation and p21/waf1/cip1 expression in human colon tumor cell lines. Carcinogenesis 25: 1227-1236.
    • (2004) Carcinogenesis , vol.25 , pp. 1227-1236
    • Druesne, N.1    Pagniez, A.2    Mayeur, C.3    Thomas, M.4    Cherbuy, C.5    Duee, P.H.6    Martel, P.7    Chaumontet, C.8
  • 29
    • 0036437194 scopus 로고    scopus 로고
    • Induction of histone acetylation and inhibition of growth of mouse erythroleukemai cells by S-allylmercaptocysteine
    • Lea MA, Rasheed M, Randolph VM, Khan F, Shareef A, desBordes C. (2002) Induction of histone acetylation and inhibition of growth of mouse erythroleukemai cells by S-allylmercaptocysteine. Nutr Cancer 43: 90-102.
    • (2002) Nutr Cancer , vol.43 , pp. 90-102
    • Lea, M.A.1    Rasheed, M.2    Randolph, V.M.3    Khan, F.4    Shareef, A.5    Desbordes, C.6
  • 31
    • 0141885036 scopus 로고    scopus 로고
    • Novel hydrozmate and anilide derivatives as potent histone deacetylase inhibitors: Synthesis and antiproliferative evaluation
    • Bouchain G, Delorme D. (2003) Novel hydrozmate and anilide derivatives as potent histone deacetylase inhibitors: Synthesis and antiproliferative evaluation. Curr Med Chem 10: 2359-2372.
    • (2003) Curr Med Chem , vol.10 , pp. 2359-2372
    • Bouchain, G.1    Delorme, D.2
  • 34
    • 0346433748 scopus 로고    scopus 로고
    • Antioxidant isoflavones in Osage orange, Maclura pomifera (Raf.) Schneid
    • Tsao R, Yang R, Young JC. (2003) Antioxidant isoflavones in Osage orange, Maclura pomifera (Raf.) Schneid. J Agric Food Chem 51: 6445-6451.
    • (2003) J Agric Food Chem , vol.51 , pp. 6445-6451
    • Tsao, R.1    Yang, R.2    Young, J.C.3
  • 35
    • 0019488061 scopus 로고
    • Antimicrobial components from Maclura pomifera fruit
    • Mahmoud ZF. (1981) Antimicrobial components from Maclura pomifera fruit. Planta Med 42: 299-301.
    • (1981) Planta Med , vol.42 , pp. 299-301
    • Mahmoud, Z.F.1
  • 36
    • 34547529740 scopus 로고    scopus 로고
    • Pomiferin, histone deacetylase inhibitor isolated from the fruits of Maclura pomifera
    • Son IH, Chung IM, Lee SI, Yang HD, Moon HI. (2007) Pomiferin, histone deacetylase inhibitor isolated from the fruits of Maclura pomifera. Bioorg Med Chem Lett 17: 4753-4755.
    • (2007) Bioorg Med Chem Lett , vol.17 , pp. 4753-4755
    • Son, I.H.1    Chung, I.M.2    Lee, S.I.3    Yang, H.D.4    Moon, H.I.5
  • 37
    • 0034525122 scopus 로고    scopus 로고
    • Chemoprevention of colonic aberrant crypt foci in Fisher rats by sulfroraphane and phenethyl isothiocyanate
    • Chung IL, Conaway CC, Rao CV, Reddy BS. (2000) Chemoprevention of colonic aberrant crypt foci in Fisher rats by sulfroraphane and phenethyl isothiocyanate. Carcinogenesis 21: 2287-2291.
    • (2000) Carcinogenesis , vol.21 , pp. 2287-2291
    • Chung, I.L.1    Conaway, C.C.2    Rao, C.V.3    Reddy, B.S.4
  • 38
    • 0030931522 scopus 로고    scopus 로고
    • Broccoli sprouts: An exceptionally rich source of inducers of enzymes that protect against chemical carcinogens
    • Fahey JW, Zhang Y, Talalay P. (1997) Broccoli sprouts: An exceptionally rich source of inducers of enzymes that protect against chemical carcinogens. Proc Natl Acad Sci USA 94: 10367-10372.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10367-10372
    • Fahey, J.W.1    Zhang, Y.2    Talalay, P.3
  • 39
    • 0037093463 scopus 로고    scopus 로고
    • High cellular accumulation of sulphoraphane, a dietary anticarcinogen, is followed by rapid transporter-mediated export as a glutathione conjugate
    • Zhang Y, Callaway EC. (2002) High cellular accumulation of sulphoraphane, a dietary anticarcinogen, is followed by rapid transporter-mediated export as a glutathione conjugate. Biochem J 364: 301-307.
    • (2002) Biochem J , vol.364 , pp. 301-307
    • Zhang, Y.1    Callaway, E.C.2
  • 40
    • 0030781225 scopus 로고    scopus 로고
    • Biotransformation of the naturally occurring isothiocyante sulforaphane in the rat: Identification of phase I metabolities and glutathione conjugates
    • Kassahun K, Davis M, Hu P, Martin B, Baillie T. (1997) Biotransformation of the naturally occurring isothiocyante sulforaphane in the rat: Identification of phase I metabolities and glutathione conjugates. Chem Res Toxicol 10: 1228-1233.
    • (1997) Chem Res Toxicol , vol.10 , pp. 1228-1233
    • Kassahun, K.1    Davis, M.2    Hu, P.3    Martin, B.4    Baillie, T.5
  • 41
    • 4143130097 scopus 로고    scopus 로고
    • A novel mechanism of chemoprotection by sulforaphane: Inhibition of histone deacetylase
    • Myzak MC, Karplus PA, Chung FL, Dashwood RH. (2004) A novel mechanism of chemoprotection by sulforaphane: Inhibition of histone deacetylase. Cancer Res 64: 5767-5774.
    • (2004) Cancer Res , vol.64 , pp. 5767-5774
    • Myzak, M.C.1    Karplus, P.A.2    Chung, F.L.3    Dashwood, R.H.4
  • 42
    • 58549090733 scopus 로고    scopus 로고
    • Sulforaphanc induces CYP1A1 mRNA, protein, and catalytic activity levels via an AhR-dependant pathway in murine hepatoma Hepa Iclc7 and human Hep62 cells
    • Anwar-Mohamed A, El-Kadi, AOS. (2009) Sulforaphanc induces CYP1A1 mRNA, protein, and catalytic activity levels via an AhR-dependant pathway in murine hepatoma Hepa Iclc7 and human Hep62 cells. Cancer Lett 275: 93-101.
    • (2009) Cancer Lett , vol.275 , pp. 93-101
    • Anwar-Mohamed, A.1    El-Kadi, A.O.S.2
  • 43
    • 63049105405 scopus 로고    scopus 로고
    • Modulation of histone deacetylase activity by dietary isothio-cyanates and allyl sulfides: Studies with sulforaphane and garlic organosulfur compounds
    • Nian H, Delage B, Ho E, Dashwood RH. (2009) Modulation of histone deacetylase activity by dietary isothio-cyanates and allyl sulfides: Studies with sulforaphane and garlic organosulfur compounds. Environ Mol Mutagen 50: 213-221.
    • (2009) Environ Mol Mutagen , vol.50 , pp. 213-221
    • Nian, H.1    Delage, B.2    Ho, E.3    Dashwood, R.H.4
  • 44
    • 34147135143 scopus 로고    scopus 로고
    • Sulforaphane induces cell type-specific apoptosis in human breast cancer cell lines
    • Pledgie-Tracy A, Sobolewski MD, Davidson NE. (2007) Sulforaphane induces cell type-specific apoptosis in human breast cancer cell lines. Mol Cancer Ther 6: 1013-1021.
    • (2007) Mol Cancer Ther , vol.6 , pp. 1013-1021
    • Pledgie-Tracy, A.1    Sobolewski, M.D.2    Davidson, N.E.3
  • 45
    • 38449089515 scopus 로고    scopus 로고
    • Sulforaphane induces cell cycle arrest and apoptosis in murine osteosarcoma cells in vitro and inhibits tumor growth in vivo
    • Matsui TA, Murata H, Sakabe T, Sowa Y, Horie N, Nakanishi R, Sakai T, Kubo T. (2007) Sulforaphane induces cell cycle arrest and apoptosis in murine osteosarcoma cells in vitro and inhibits tumor growth in vivo. Oncol Rep 18: 1263-1268.
    • (2007) Oncol Rep , vol.18 , pp. 1263-1268
    • Matsui, T.A.1    Murata, H.2    Sakabe, T.3    Sowa, Y.4    Horie, N.5    Nakanishi, R.6    Sakai, T.7    Kubo, T.8
  • 46
    • 33846838750 scopus 로고    scopus 로고
    • Sulforaphane retards the growth of human PC-3 xenographs and inhibits HDAC activity in human subjects
    • Myzak MC, Tong P, Dashwood WM, Dashwood RH, Ho E. (2007) Sulforaphane retards the growth of human PC-3 xenographs and inhibits HDAC activity in human subjects. Exp Biol Med 232: 227-234.
    • (2007) Exp Biol Med , vol.232 , pp. 227-234
    • Myzak, M.C.1    Tong, P.2    Dashwood, W.M.3    Dashwood, R.H.4    Ho, E.5
  • 47
    • 1642545614 scopus 로고    scopus 로고
    • Sulforaphane induces caspase-mediated apoptosis in cultured PC-3 human prostate cancer cells and retards growth of PC-3 xenografts in vivo
    • Singh AV, Xiao D, Lew KL, Dhir R, Singh SV. (2004) Sulforaphane induces caspase-mediated apoptosis in cultured PC-3 human prostate cancer cells and retards growth of PC-3 xenografts in vivo. Carcinogenesis 25: 83-90.
    • (2004) Carcinogenesis , vol.25 , pp. 83-90
    • Singh, A.V.1    Xiao, D.2    Lew, K.L.3    Dhir, R.4    Singh, S.V.5
  • 48
    • 0028203252 scopus 로고
    • Anticarcinogenic activities of sulforaphane and structurally related synthetic norbornyl isothiocyanates
    • Zhang Y, Kensler TW, Cho CG, Posner GH, Tallalay P. (1994) Anticarcinogenic activities of sulforaphane and structurally related synthetic norbornyl isothiocyanates. Proc Natl Acad Sci USA 91: 3147-3150.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3147-3150
    • Zhang, Y.1    Kensler, T.W.2    Cho, C.G.3    Posner, G.H.4    Tallalay, P.5
  • 49
    • 33645825587 scopus 로고    scopus 로고
    • Sulforaphane inhibits histone deacetylase in vivo and suppresses tumorige-nesis in Apc-minus mice
    • Myzak MC, Dashwood WM, Orner GA, Ho E, Dashwood, RH. (2006) Sulforaphane inhibits histone deacetylase in vivo and suppresses tumorige-nesis in Apc-minus mice. FASEB J 20: 506-8.
    • (2006) FASEB J , vol.20 , pp. 506-508
    • Myzak, M.C.1    Dashwood, W.M.2    Orner, G.A.3    Ho, E.4    Dashwood, R.H.5
  • 52
    • 0007247909 scopus 로고
    • Cycloenantiomerism, and cyclodias-teromerism
    • Prelog IV, Gerlach H. (1964) Cycloenantiomerism, and cyclodias-teromerism. Helv Chim Acta 47: 2288-2294.
    • (1964) Helv Chim Acta , vol.47 , pp. 2288-2294
    • Prelog, I.V.1    Gerlach, H.2
  • 53
    • 33845560283 scopus 로고
    • On the concept of linear modified retro-peptide structures
    • Goodman M, Chorev M. (1979) On the concept of linear modified retro-peptide structures. Acc Chem Res 12: 1-7.
    • (1979) Acc Chem Res , vol.12 , pp. 1-7
    • Goodman, M.1    Chorev, M.2
  • 56
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin
    • Furumai R, Komatsu Y, Nishino N, Khochbin S, Yoshida M, Horinouchi S. (2001) Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc Natl Acad Sci USA 98: 87-92.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 57
    • 21844495631 scopus 로고
    • Relationships between structural features and biological activities of HC-toxin
    • Kim SD. (1995) Relationships between structural features and biological activities of HC-toxin. J Biochem Mol Biol 28: 227-231.
    • (1995) J Biochem Mol Biol , vol.28 , pp. 227-231
    • Kim, S.D.1
  • 58
    • 0028365944 scopus 로고
    • Bioactive marine metabolities. 59. Cyclostellettamines A-F, pyridine alkaloids which inhibit binding of methyl quinuclidinyl benzylate (QNB) to muscarinic acetylcholine receptors, from the marine sponge, Stelletta maxima
    • Fusetani N, Asai N, Matsunaga S, Honda K, Yasumuro K. (1994) Bioactive marine metabolities. 59. Cyclostellettamines A-F, pyridine alkaloids which inhibit binding of methyl quinuclidinyl benzylate (QNB) to muscarinic acetylcholine receptors, from the marine sponge, Stelletta maxima. Tetrahedron Lett 35: 3967-3970.
    • (1994) Tetrahedron Lett , vol.35 , pp. 3967-3970
    • Fusetani, N.1    Asai, N.2    Matsunaga, S.3    Honda, K.4    Yasumuro, K.5
  • 59
    • 1942438219 scopus 로고    scopus 로고
    • Three new cyclostellettamines, which inhibit histone deacetylase, from a marine sponge of the genus Xestospongia
    • Oku N, Nagai K, Shindoh N, Terada Y, Van Soest RWM, Matsunaga S, Fusetani N. (2004) Three new cyclostellettamines, which inhibit histone deacetylase, from a marine sponge of the genus Xestospongia. Biorg Med Chem Lett 14: 2617-2620.
    • (2004) Biorg Med Chem Lett , vol.14 , pp. 2617-2620
    • Oku, N.1    Nagai, K.2    Shindoh, N.3    Terada, Y.4    Van Soest, R.5    Matsunaga, S.6    Fusetani, N.7
  • 60
    • 7044262248 scopus 로고    scopus 로고
    • Ingenamine G and cyclostellettamines G-I, K, and L from the new Brazilian species of marine sponge Pachychalina sp
    • De Oliveira JHHL, Grube A, Koeck M, Berlinck RGS, Macedo ML, Ferreira AG, Hajdu E. (2004) Ingenamine G and cyclostellettamines G-I, K, and L from the new Brazilian species of marine sponge Pachychalina sp. J Nat Prod 67: 1685-1689.
    • (2004) J Nat Prod , vol.67 , pp. 1685-1689
    • De Oliveira, J.1    Grube, A.2    Koeck, M.3    Berlinck, R.4    Macedo, M.L.5    Ferreira, A.G.6    Hajdu, E.7
  • 62
    • 0000055673 scopus 로고
    • Phenolic constituent of Psammaplysilla
    • Quinoa E, Crews P. (1987) Phenolic constituent of Psammaplysilla Tetrahedron Lett 28: 3229-3232.
    • (1987) Tetrahedron Lett , vol.28 , pp. 3229-3232
    • Quinoa, E.1    Crews, P.2
  • 63
    • 37349061341 scopus 로고    scopus 로고
    • A natural histone deacetylase inhibitor, Psammaplin A, induces cell cycle arrest and apoptosis in human endometrial cancer cells
    • Ahn MY, Jung JH, Na YJ, Kim HS. (2008) A natural histone deacetylase inhibitor, Psammaplin A, induces cell cycle arrest and apoptosis in human endometrial cancer cells. Gynecol Oncol 108: 27-33.
    • (2008) Gynecol Oncol , vol.108 , pp. 27-33
    • Ahn, M.Y.1    Jung, J.H.2    Na, Y.J.3    Kim, H.S.4
  • 64
  • 66
    • 0037039919 scopus 로고    scopus 로고
    • Structure and chemistry of apicidins, a class of novel cyclic tetrapeptides without a terminal a-keto epoxide as inhibitors of histone deacetylase with potent antiprotozoal activities
    • Singh SB, Zink DL, Liesch JM, Mosley RT, Dombrowski AW, Bills GF, Darkin-Rattray SJ, Schmatz DM, Goetz MA. (2002) Structure and chemistry of apicidins, a class of novel cyclic tetrapeptides without a terminal a-keto epoxide as inhibitors of histone deacetylase with potent antiprotozoal activities. J Org Chem 67: 815-825.
    • (2002) J Org Chem , vol.67 , pp. 815-825
    • Singh, S.B.1    Zink, D.L.2    Liesch, J.M.3    Mosley, R.T.4    Dombrowski, A.W.5    Bills, G.F.6    Darkin-Rattray, S.J.7    Schmatz, D.M.8    Goetz, M.A.9
  • 67
    • 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. (2008) From natural products to small molecule ketone histone deacetylase inhibitors: Development of new class specific agents. Curr Pharm Des 14: 545-561.
    • (2008) Curr Pharm Des , vol.14 , pp. 545-561
    • Jones, P.1    Steinkuhler, C.2
  • 68
    • 0016366116 scopus 로고
    • Isolation and structural clarification of chlamydocin
    • Closse A, Hugenin R. (1974) Isolation and structural clarification of chlamydocin. Helv Chim Acta 57: 533-545.
    • (1974) Helv Chim Acta , vol.57 , pp. 533-545
    • Closse, A.1    Hugenin, R.2
  • 71
    • 33645892015 scopus 로고    scopus 로고
    • Chlamydocin analogs bearing carbonyl group as possible ligand toward zinc atom in histone deacetylases
    • Bhuiyan MPI, Kato T, Okauchi T, Nishino N, Mueda S, Nishino TG, Yoshida M. (2006) Chlamydocin analogs bearing carbonyl group as possible ligand toward zinc atom in histone deacetylases. Bioorg Med Chem Lett 14: 3438-3446.
    • (2006) Bioorg Med Chem Lett , vol.14 , pp. 3438-3446
    • Bhuiyan, M.1    Kato, T.2    Okauchi, T.3    Nishino, N.4    Mueda, S.5    Nishino, T.G.6    Yoshida, M.7
  • 72
    • 0037300444 scopus 로고    scopus 로고
    • FR235222, a fungal metabolite, is a novel immunosuppressant that inhibits ammalian histone deacetylase (HDAC). I. Taxonomy, fermentation, isolation and biological activities
    • Mori H, Urano Y, Abe F, Furukawa S, Tsurumi Y, Sakamoto K, Hashimoto M, Takase S, Hino M, Fujii T. (2003) FR235222, a fungal metabolite, is a novel immunosuppressant that inhibits ammalian histone deacetylase (HDAC). I. Taxonomy, fermentation, isolation and biological activities. J Antibiot 56: 72-79.
    • (2003) J Antibiot , vol.56 , pp. 72-79
    • Mori, H.1    Urano, Y.2    Abe, F.3    Furukawa, S.4    Tsurumi, Y.5    Sakamoto, K.6    Hashimoto, M.7    Takase, S.8    Hino, M.9    Fujii, T.10
  • 74
    • 0029411482 scopus 로고
    • Inhibition of maize histone deacetylases by HC Toxin, the host-selective toxin of cochliobolus carbonum
    • Brosch G, Ransom R, Lechner T, Walton JD, Loidl P. (1995) Inhibition of maize histone deacetylases by HC Toxin, the host-selective toxin of cochliobolus carbonum. Plant Cell 7: 1941-1950.
    • (1995) Plant Cell , vol.7 , pp. 1941-1950
    • Brosch, G.1    Ransom, R.2    Lechner, T.3    Walton, J.D.4    Loidl, P.5
  • 75
    • 17344366283 scopus 로고    scopus 로고
    • Antiproliferative effect of Trichostatin A and HC-Toxin in T47D Human Breast Cancer Cells
    • Joung KE, Kim DK, Shenn YY. (2004) Antiproliferative effect of Trichostatin A and HC-Toxin in T47D Human Breast Cancer Cells. Arch Pharm Res 27: 640-645.
    • (2004) Arch Pharm Res , vol.27 , pp. 640-645
    • Joung, K.E.1    Kim, D.K.2    Shenn, Y.Y.3
  • 77
    • 54049152858 scopus 로고    scopus 로고
    • A concise total synthesis of largazole, solution structure, and some preliminary structure activity relationships
    • Nasveschuk CG, Ungermannova D, Liu X, Phillips AJ. (2008) A concise total synthesis of largazole, solution structure, and some preliminary structure activity relationships. Org Lett 10: 3595-3598.
    • (2008) Org Lett , vol.10 , pp. 3595-3598
    • Nasveschuk, C.G.1    Ungermannova, D.2    Liu, X.3    Phillips, A.J.4
  • 78
    • 46049100010 scopus 로고    scopus 로고
    • Total synthesis and molecular target of largazole, a histone deacetylase inhibitor
    • Ying Y, Taori K, Kim H, Hong, Luesch H. (2008) Total synthesis and molecular target of largazole, a histone deacetylase inhibitor. J Am Chem Soc 130: 8455-8459.
    • (2008) J am Chem Soc , vol.130 , pp. 8455-8459
    • Ying, Y.1    Taori, K.2    Kim, H.3    Hong, L.H.4
  • 79
    • 77949831890 scopus 로고    scopus 로고
    • Total synthesis and biological evaluation of largazole and derivatives with promising selectivity for cancer cells
    • Zeng X, Yin B, Hu Z, Liao C, Liu J, Li S, Li Z, Nicklaus MC, Zhou G Jiang S. (2010) Total synthesis and biological evaluation of largazole and derivatives with promising selectivity for cancer cells. Org Lett 12: 1368-1371.
    • (2010) Org Lett , vol.12 , pp. 1368-1371
    • Zeng, X.1    Yin, B.2    Hu, Z.3    Liao, C.4    Liu, J.5    Li, S.6    Li, Z.7    Nicklaus, M.C.8    Zhou G Jiang, S.9
  • 80
    • 0029795991 scopus 로고    scopus 로고
    • Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function
    • Taunton J, Collins JL, Schreiber SL. (1996) Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function. J Am Chem Soc 118: 10412-10422.
    • (1996) J am Chem Soc , vol.118 , pp. 10412-10422
    • Taunton, J.1    Collins, J.L.2    Schreiber, S.L.3
  • 81
    • 0027378351 scopus 로고
    • Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase
    • Kijima M, Yoshida M, Susita K, Horinouchi S, Beppu T. (1993) Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase. J Biol Chem 30: 22429-22435.
    • (1993) J Biol Chem , vol.30 , pp. 22429-22435
    • Kijima, M.1    Yoshida, M.2    Susita, K.3    Horinouchi, S.4    Beppu, T.5
  • 83
    • 0018114158 scopus 로고
    • Trichostatin C, a glucopyranosyl hydroxamate
    • Tsuji N, Kobayashi M. (1978) Trichostatin C, a glucopyranosyl hydroxamate. J Antibiot 31: 939-944.
    • (1978) J Antibiot , vol.31 , pp. 939-944
    • Tsuji, N.1    Kobayashi, M.2
  • 85
    • 0021990106 scopus 로고
    • Trichostatin C, a new inducer of differentiation of friend leukemic cells
    • Yoshida M, Iwamoto Y, Uozumi T, Beeppu T. (1985) Trichostatin C, a new inducer of differentiation of friend leukemic cells. Agric Biol Chem 49: 563-565.
    • (1985) Agric Biol Chem , vol.49 , pp. 563-565
    • Yoshida, M.1    Iwamoto, Y.2    Uozumi, T.3    Beeppu, T.4
  • 86
    • 0023195737 scopus 로고
    • Effects of trichostatins on differentiation of murine erythroleukemia cells
    • Yoshida M, Nomura S, Beppu T. (1987) Effects of trichostatins on differentiation of murine erythroleukemia cells. Cancer Res 47: 3688-3691.
    • (1987) Cancer Res , vol.47 , pp. 3688-3691
    • Yoshida, M.1    Nomura, S.2    Beppu, T.3
  • 87
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida, M, Kijima M, Akita M, Beppu T. (1990) Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem 265: 17174-17179.
    • (1990) J Biol Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 88
    • 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. (2002) The histone-deacetylase inhibitor trichostatin A blocks proliferation and triggers apoptotic programs in hepatoma cells. J Hepatol 36: 233-240.
    • (2002) J Hepatol , vol.36 , pp. 233-240
    • Herold, C.1    Ganslmayer, M.2    Ocker, M.3    Hermann, M.4    Geerts, A.5    Hahn, E.G.6    Schuppan, D.7
  • 89
    • 0035169123 scopus 로고    scopus 로고
    • Trichostatin A inhibits ß-casein expression in mammary epithelial cells
    • Pujuguet P, Radisky D, Levy D, Lacza C, Bissell MJ. (2001) Trichostatin A inhibits ß-casein expression in mammary epithelial cells. J Cell Biochem 83: 660-670.
    • (2001) J Cell Biochem , vol.83 , pp. 660-670
    • Pujuguet, P.1    Radisky, D.2    Levy, D.3    Lacza, C.4    Bissell, M.J.5
  • 90
    • 0032989027 scopus 로고    scopus 로고
    • Antitumor activity in vitro and in vivo of selective differentiating agents containing hydroxamate
    • Qiu L, Kelso MJ, Hansen C, West ML, Fairlie DP, Parsons PG. (1999) Antitumor activity in vitro and in vivo of selective differentiating agents containing hydroxamate. Br J Cancer 80: 1252-1258.
    • (1999) Br J Cancer , vol.80 , pp. 1252-1258
    • Qiu, L.1    Kelso, M.J.2    Hansen, C.3    West, M.L.4    Fairlie, D.P.5    Parsons, P.G.6
  • 95
    • 0942265466 scopus 로고    scopus 로고
    • Total synthesis of spiruchostatin A, a potent histone deacetylase inhibitor
    • Yurek-George A, Habens F, Brimmell M, Packham G Ganesan A. (2004) Total synthesis of spiruchostatin A, a potent histone deacetylase inhibitor. JAm Chem Soc 126: 1030-1031.
    • (2004) Jam Chem Soc , vol.126 , pp. 1030-1031
    • Yurek-George, A.1    Habens, F.2    Brimmell, M.3    Packham G Ganesan, A.4
  • 96
    • 70350507928 scopus 로고    scopus 로고
    • Total synthesis of the bicyclic depsipeptide HDAC inhibitors spiruchostatins A and B, 5"-epi-spiruchostatin B, FK228 (FR901228) and preliminary evaluation of their biological activity
    • Narita K, Kikuchi T, Watanabe K, Takizawa T, Oguchi T, Kudo K, Matsuhara K, Abe H, Yamori T, Yoshida M, Katoh T. (2009) Total synthesis of the bicyclic depsipeptide HDAC inhibitors spiruchostatins A and B, 5"-epi-spiruchostatin B, FK228 (FR901228) and preliminary evaluation of their biological activity. Chem Eur J15: 11174-11186.
    • (2009) Chem Eur , vol.J15 , pp. 11174-11186
    • Narita, K.1    Kikuchi, T.2    Watanabe, K.3    Takizawa, T.4    Oguchi, T.5    Kudo, K.6    Matsuhara, K.7    Abe, H.8    Yamori, T.9    Yoshida, M.10    Katoh, T.11
  • 97
    • 59349084488 scopus 로고    scopus 로고
    • Role of HDAC2 in the pathophysiology of COPD
    • Barnes PJ. (2009) Role of HDAC2 in the pathophysiology of COPD. Annu Rev Physiol 71: 451-464.
    • (2009) Annu Rev Physiol , vol.71 , pp. 451-464
    • Barnes, P.J.1
  • 99
    • 28844497060 scopus 로고    scopus 로고
    • Oxidative stress causes HDAC2 reduction by nitration, ubiquitinylation and proteasomal degradation
    • (Abstr.)
    • Osoata G Adcock IM, Barnes PJ, Ito K. (2005) Oxidative stress causes HDAC2 reduction by nitration, ubiquitinylation and proteasomal degradation. Proc Am Thorac Soc 2: A755 (Abstr.)
    • (2005) Proc am Thorac Soc , vol.2
    • Osoata G Adcock, I.M.1    Barnes, P.J.2    Ito, K.3
  • 100
    • 57349158300 scopus 로고    scopus 로고
    • Oxidative stress-induced PI3-kinase activation reduces HDAC activity and is inhibited by theophylline
    • :, (Abstr.)
    • Failla M, To Y, Ito M, Adcock IM, Barnes PJ, Ito K. (2007) Oxidative stress-induced PI3-kinase activation reduces HDAC activity and is inhibited by theophylline. Proc Am Thorac Soc 2: A45 (Abstr.)
    • (2007) Proc am Thorac Soc , vol.2
    • Failla, M.1    To, Y.2    Ito, M.3    Adcock, I.M.4    Barnes, P.J.5    Ito, K.6
  • 101
    • 84973118454 scopus 로고    scopus 로고
    • Activation of histone deaetylases 1 (Hdac1) protects against dna damage and increases neuronal survival. Wolf Greenfield & Sacks PC, Boston MA, US Applicaton #20100075926
    • Tsai LH, Haggarty SJ, Kim D (2010) Activation of histone deaetylases 1 (hdac1) protects against dna damage and increases neuronal survival. Wolf Greenfield & Sacks PC, Boston MA, US Applicaton #20100075926, USPTO Class 514 82.
    • (2010) USPTO Class , vol.514 , pp. 82
    • Tsai, L.H.1    Haggarty, S.J.2    Kim, D.3
  • 102
    • 33750541268 scopus 로고    scopus 로고
    • Down-regulation of androgen receptor by 3,3,-diindolylmethane contributes to inhibition of cell proliferation and induction of apooptosis in both hormone-sensitive LNCaP and insensitive C4-2B Prosate Cancer Cells
    • Bhuiyan MMR, Li Y, Banerjee S, Ahmed F, Wang Z, Ali S, Sarkar FH. (2006) Down-regulation of androgen receptor by 3,3-diindolylmethane contributes to inhibition of cell proliferation and induction of apooptosis in both hormone-sensitive LNCaP and insensitive C4-2B Prosate Cancer Cells. Cancer Res 66: 10064-10072.
    • (2006) Cancer Res , vol.66 , pp. 10064-10072
    • Bhuiyan, M.1    Li, Y.2    Banerjee, S.3    Ahmed, F.4    Wang, Z.5    Ali, S.6    Sarkar, F.H.7
  • 103
    • 40949131914 scopus 로고    scopus 로고
    • Mammalian target of rapamycin repression by 3,3,-diindolylmethane inhibits invasion and angiogenesis in platelet-derived growth factor-d-over-expressing PC3 cells
    • Kong D, Banerjee S, Huang W, Li Y, Wang Z, Kim HRC, Sarkar FH. (2008) Mammalian target of rapamycin repression by 3,3-diindolylmethane inhibits invasion and angiogenesis in platelet-derived growth factor-d-over-expressing PC3 cells. Cancer Res 68: 1927-1934.
    • (2008) Cancer Res , vol.68 , pp. 1927-1934
    • Kong, D.1    Banerjee, S.2    Huang, W.3    Li, Y.4    Wang, Z.5    Kim, H.6    Sarkar, F.H.7
  • 104
    • 76549093815 scopus 로고    scopus 로고
    • Chemopreventive agent 3,3,-diinolylmethane selectively induces proteasomal degradation of class I histone deacetylases
    • Li Y, Li X, Guo B. (2010) Chemopreventive agent 3,3-diinolylmethane selectively induces proteasomal degradation of class I histone deacetylases. Cancer Res 70: 646-654.
    • (2010) Cancer Res , vol.70 , pp. 646-654
    • Li, Y.1    Li, X.2    Guo, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.