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Volumn 5, Issue 4, 2002, Pages 487-499

Recent advances in the discovery of small molecule histone deacetylase inhibitors

Author keywords

Apicidin; Cancer; CHAPs; FK 228; Histone deacetylase; MS 275; SAHA; Trapoxin; Trichostatin

Indexed keywords

2 AMINO 9,10 EPOXY 8 OXODECANOIC ACID; 3 [(3 CHOLAMIDOPROPYL)DIMETHYLAMMONIO] 1 PROPANESULFONIC ACID; AMINO ACID; APICIDIN; BUTYRIC ACID; CHLAMYDOCIN; CYCLO[LEUCYLPIPECOLYL (2 AMINO 8 OXO 9,10 EPOXYDECANOYL) DEXTRO PHENYLALANYL]; FR 901228; HC TOXIN; HISTONE; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE INHIBITOR; HYDROXAMIC ACID; LYSINE; MS 27275; N (2 AMINOPHENYL) 2 PROPENAMIDE; N (2 AMINOPHENYL) 4 (3 PYRIDINYLMETHOXYCARBONYLAMINOMETHYL)BENZAMIDE; OXAMFLATIN; PYROXAMIDE; PYRROL 2 YL 2 PROPENAMIDE INHIBITOR; PYRROLE DERIVATIVE; SODIUM PHENYLBUTYRATE; TETRAPEPTIDE; TRAPOXIN; TRAPOXIN A; TRICHOSTATIN A; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALPROIC ACID; VORINOSTAT; ENZYME INHIBITOR; HISTONE DEACETYLASE;

EID: 0036651788     PISSN: 13676733     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (49)

References (84)
  • 1
    • 0035313770 scopus 로고    scopus 로고
    • Higher-order structure of chromatin and chromosomes
    • Woodcock CL, Dimitrov S: Higher-order structure of chromatin and chromosomes. Curr Opin Genet Dev (2001) 11:130-135. General introduction to nucleosome structure.
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 130-135
    • Woodcock, C.L.1    Dimitrov, S.2
  • 2
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
    • Komberg RD, Lorch Y: Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome. Cell (1999) 98:285-294. Review of nucleosome structure and an introduction to chromatin remodeling.
    • (1999) Cell , vol.98 , pp. 285-294
    • Komberg, R.D.1    Lorch, Y.2
  • 3
    • 0034387004 scopus 로고    scopus 로고
    • 25 Years after the nucleosome model: Chromatin modifications
    • Wu J, Grunstein M: 25 years after the nucleosome model: Chromatin modifications. Trends Biochem Sci (2000) 25:619-623.
    • (2000) Trends Biochem Sci , vol.25 , pp. 619-623
    • Wu, J.1    Grunstein, M.2
  • 4
    • 0035962646 scopus 로고    scopus 로고
    • Chromatin remodeling and transcriptional activation: The cast (in order of appearance)
    • Umov FD, Wolffe AP: Chromatin remodeling and transcriptional activation: The cast (in order of appearance). Oncogene (2001) 20:2991-3006.
    • (2001) Oncogene , vol.20 , pp. 2991-3006
    • Umov, F.D.1    Wolffe, A.P.2
  • 5
    • 0035962651 scopus 로고    scopus 로고
    • An embarrassment of niches: The many covalent modifications of histones in transcriptional regulation
    • Berger SL: An embarrassment of niches: The many covalent modifications of histones in transcriptional regulation. Oncogene (2001) 20:3007-3013.
    • (2001) Oncogene , vol.20 , pp. 3007-3013
    • Berger, S.L.1
  • 6
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD: The language of covalent histone modifications. Nature (2000) 403:41-45. Proposal that histone modifications form a 'code' read by proteins to initiate downstream events.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 7
    • 0032558998 scopus 로고    scopus 로고
    • Structure and function of the core histone N-termini: More than meets the eye
    • Hansen JC, Tse C, Wolffe AP: Structure and function of the core histone N-termini: More than meets the eye. Biochemistry (1998) 37:17637-17641.
    • (1998) Biochemistry , vol.37 , pp. 17637-17641
    • Hansen, J.C.1    Tse, C.2    Wolffe, A.P.3
  • 8
    • 0035325163 scopus 로고    scopus 로고
    • Histone acetylation and chromatin remodeling
    • Gregory PD, Wagner K, Horz W: Histone acetylation and chromatin remodeling. Exp Cell Res (2001) 265:195-202.
    • (2001) Exp Cell Res , vol.265 , pp. 195-202
    • Gregory, P.D.1    Wagner, K.2    Horz, W.3
  • 10
    • 0035862199 scopus 로고    scopus 로고
    • The human histone deacetylase family
    • Gray SG, Ekstrom TJ: The human histone deacetylase family. Exp Cell Res (2001) 262:75-83. Good review of the characteristics of HDACs known in 2001.
    • (2001) Exp Cell Res , vol.262 , pp. 75-83
    • Gray, S.G.1    Ekstrom, T.J.2
  • 11
    • 0035853455 scopus 로고    scopus 로고
    • Histone deacetylase complexes: Functional entities or molecular reservoirs
    • Khochbin S, Kao HY: Histone deacetylase complexes: Functional entities or molecular reservoirs. FEBS Lett (2001) 494:141-144.
    • (2001) FEBS Lett , vol.494 , pp. 141-144
    • Khochbin, S.1    Kao, H.Y.2
  • 12
    • 0035313874 scopus 로고    scopus 로고
    • Functional significance of histone deacetylase diversity
    • Khochbin S, Verdel A, Lemercier C, Seigneurin-Bemy D: Functional significance of histone deacetylase diversity. Curr Opin Genet Dev (2001) 11:162-166. Good review of HDAC families and their diversity.
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 162-166
    • Khochbin, S.1    Verdel, A.2    Lemercier, C.3    Seigneurin-Bemy, D.4
  • 13
    • 0035500502 scopus 로고    scopus 로고
    • Emerging roles for chromatin remodeling in cancer biology
    • Caims BR: Emerging roles for chromatin remodeling in cancer biology. Trends Cell Biol (2001) 11:S15-S21.
    • (2001) Trends Cell Biol , vol.11
    • Caims, B.R.1
  • 15
    • 0034252183 scopus 로고    scopus 로고
    • Histone acetylation modifiers in the pathogenesis of malignant disease
    • Mahlknecht U, Hoelzer D: Histone acetylation modifiers in the pathogenesis of malignant disease. Mol Med (2000) 6:623-644.
    • (2000) Mol Med , vol.6 , pp. 623-644
    • Mahlknecht, U.1    Hoelzer, D.2
  • 16
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylases, transcriptional control, and cancer
    • Cress WD, Seto E: Histone deacetylases, transcriptional control, and cancer. J Cell Physiol (2000) 184:1-16.
    • (2000) J Cell Physiol , vol.184 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 17
    • 0020403437 scopus 로고
    • Inhibition of histone acetylation by N-[2-(S-coenzyme A)acetyl] spermidine amide, a multisubstrate analog
    • Cullis PM, Woffenden R, Cousens LS, Alberts BM: Inhibition of histone acetylation by N-[2-(S-coenzyme A)acetyl] spermidine amide, a multisubstrate analog. J Biol Chem (1982) 257:12165-12169.
    • (1982) J Biol Chem , vol.257 , pp. 12165-12169
    • Cullis, P.M.1    Woffenden, R.2    Cousens, L.S.3    Alberts, B.M.4
  • 18
    • 0021772472 scopus 로고
    • Differential inhibition of histone and polyamine acetylases by multisubstrate analogs
    • Erwin BG, Persson L, Pegg AE: Differential inhibition of histone and polyamine acetylases by multisubstrate analogs. Biochemistry (1984) 23:4250-4255.
    • (1984) Biochemistry , vol.23 , pp. 4250-4255
    • Erwin, B.G.1    Persson, L.2    Pegg, A.E.3
  • 19
    • 0004951746 scopus 로고
    • Chemical synthesis of multisubstrate inhibitors of histone acetyltransferase by covalently linking spermidine to an S-terminal fragment of coenzyme A
    • Parello J, Roblot G, Wylde R, Martin A: Chemical synthesis of multisubstrate inhibitors of histone acetyltransferase by covalently linking spermidine to an S-terminal fragment of coenzyme A. C R Acad Sci Ser 2 (1990) 310:1441-1446.
    • (1990) C R Acad Sci Ser 2 , vol.310 , pp. 1441-1446
    • Parello, J.1    Roblot, G.2    Wylde, R.3    Martin, A.4
  • 20
    • 0025830106 scopus 로고
    • Regulation of nuclear histone acetyltransferase by nucleic acids, histone. DNA complex, and chromatin
    • Wong LJ, Sharpe DJ: Regulation of nuclear histone acetyltransferase by nucleic acids, histone. DNA complex, and chromatin. Biochem Genet (1991) 29:13-28.
    • (1991) Biochem Genet , vol.29 , pp. 13-28
    • Wong, L.J.1    Sharpe, D.J.2
  • 21
    • 0027249898 scopus 로고
    • Regioselective synthesis of inhibitors of histone acetyl transferase covalently linking spermidine to the S-terminus of coenzyme A and fragments
    • Roblot G, Wylde R, Martin A, Parello J: Regioselective synthesis of inhibitors of histone acetyl transferase covalently linking spermidine to the S-terminus of coenzyme A and fragments. Tetrahedron (1993) 49:6381-6398.
    • (1993) Tetrahedron , vol.49 , pp. 6381-6398
    • Roblot, G.1    Wylde, R.2    Martin, A.3    Parello, J.4
  • 23
    • 0036008097 scopus 로고    scopus 로고
    • Deacetylase enzymes. Biological functions and the use of small-molecule inhibitors
    • Grozinger CM, Schreiber SL: Deacetylase enzymes. Biological functions and the use of small-molecule inhibitors. Chem Biol (2002) 9:3-16. Recent review of HDAC families, their protein complexes and mechanisms of deacetylation.
    • (2002) Chem Biol , vol.9 , pp. 3-16
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 24
    • 0035964743 scopus 로고    scopus 로고
    • Histone deacetylase and DNA methyltransferase in human prostate cancer
    • Patra SK, Patra A, Dahiya R: Histone deacetylase and DNA methyltransferase in human prostate cancer. Biochem Biophys Res Commun (2001) 287:705-713.
    • (2001) Biochem Biophys Res Commun , vol.287 , pp. 705-713
    • Patra, S.K.1    Patra, A.2    Dahiya, R.3
  • 27
    • 0017767153 scopus 로고
    • n-Butyrate causes histone modification in HeLa and Friend erythroleukemia cells
    • Riggs MG, Whittaker RG, Neumann JR, Ingram VM: n-Butyrate causes histone modification in HeLa and Friend erythroleukemia cells. Nature (1977) 268:462-464.
    • (1977) Nature , vol.268 , pp. 462-464
    • Riggs, M.G.1    Whittaker, R.G.2    Neumann, J.R.3    Ingram, V.M.4
  • 28
    • 0017898940 scopus 로고
    • Suppression of histone deacetylation in vivo and in vitro by sodium butyrate
    • Boffa LC, Vidali G, Mann RS, Allfrey VG: Suppression of histone deacetylation in vivo and in vitro by sodium butyrate. J Biol Chem (1978) 253:3364-3366.
    • (1978) J Biol Chem , vol.253 , pp. 3364-3366
    • Boffa, L.C.1    Vidali, G.2    Mann, R.S.3    Allfrey, V.G.4
  • 29
    • 0028983190 scopus 로고
    • Discordant effects of butyrate analogues on erythroleukemia cell proliferation, differentiation and histone deacetylase
    • Lea MA, Tulsyan N: Discordant effects of butyrate analogues on erythroleukemia cell proliferation, differentiation and histone deacetylase. Anticancer Res (1995) 15:879-883.
    • (1995) Anticancer Res , vol.15 , pp. 879-883
    • Lea, M.A.1    Tulsyan, N.2
  • 30
    • 0035965343 scopus 로고    scopus 로고
    • Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen
    • Phiel CJ, Zhang F, Huang EY, Guenther MG, Lazar MA, Klein PS: Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. J Biol Chem (2001) 276:36734-36741.
    • (2001) J Biol Chem , vol.276 , pp. 36734-36741
    • Phiel, C.J.1    Zhang, F.2    Huang, E.Y.3    Guenther, M.G.4    Lazar, M.A.5    Klein, P.S.6
  • 31
    • 3643104150 scopus 로고    scopus 로고
    • Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase
    • Warrell RP Jr, He LZ, Richon V, Calleja E, Pandolfi PP: Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase. J Natl Cancer Inst (1998) 90:1621-1625.
    • (1998) J Natl Cancer Inst , vol.90 , pp. 1621-1625
    • Warrell R.P., Jr.1    He, L.Z.2    Richon, V.3    Calleja, E.4    Pandolfi, P.P.5
  • 33
    • 0033672431 scopus 로고    scopus 로고
    • Modifying histones to tame cancer: Clinical development of sodium phenylbutyrate and other histone deacetylase inhibitors
    • Gore SD, Carducci MA: Modifying histones to tame cancer: Clinical development of sodium phenylbutyrate and other histone deacetylase inhibitors. Expert Opin Investig Drugs (2000) 9:2923-2934.
    • (2000) Expert Opin Investig Drugs , vol.9 , pp. 2923-2934
    • Gore, S.D.1    Carducci, M.A.2
  • 35
    • 0344431240 scopus 로고    scopus 로고
    • FR901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor
    • Nakajima H, Kim YB, Terano H, Yoshida M, Horinouchi S: FR901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor. Exp Cell Res (1998) 241:126-133.
    • (1998) Exp Cell Res , vol.241 , pp. 126-133
    • Nakajima, H.1    Kim, Y.B.2    Terano, H.3    Yoshida, M.4    Horinouchi, S.5
  • 36
    • 0035525781 scopus 로고    scopus 로고
    • Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: A case report
    • Piekarz RL, Robey R, Sandor V, Bakke S, Wilson WH, Dahmoush L, Kingma DM, Tumer ML, Altemus R, Bates SE: Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: A case report. Blood (2001) 98:2865-2868. First report of the clinical responses from an HDAI administered as a single agent.
    • (2001) Blood , vol.98 , pp. 2865-2868
    • Piekarz, R.L.1    Robey, R.2    Sandor, V.3    Bakke, S.4    Wilson, W.H.5    Dahmoush, L.6    Kingma, D.M.7    Tumer, M.L.8    Altemus, R.9    Bates, S.E.10
  • 37
    • 0033551152 scopus 로고    scopus 로고
    • A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors
    • Saito A, Yamashita T, Mariko Y, Nosaka Y, Tsuchiya K, Ando T, Suzuki T, Tsuruo T, Nakanishi O: A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors. Proc Natl Acad Sci USA (1999) 96:4592-4597. First report of preclinical efficacy with an orally administered HDAI.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4592-4597
    • Saito, A.1    Yamashita, T.2    Mariko, Y.3    Nosaka, Y.4    Tsuchiya, K.5    Ando, T.6    Suzuki, T.7    Tsuruo, T.8    Nakanishi, O.9
  • 39
    • 0033523895 scopus 로고    scopus 로고
    • Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation
    • Jung M, Brosch G, Koelle D, Scherf H, Gerhaeuser C, Loidl P: Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation. J Med Chem (1999) 42:4669-4679.
    • (1999) J Med Chem , vol.42 , pp. 4669-4679
    • Jung, M.1    Brosch, G.2    Koelle, D.3    Scherf, H.4    Gerhaeuser, C.5    Loidl, P.6
  • 40
    • 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: Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J Biol Chem (1990) 265:17174-17179.
    • (1990) J Biol Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 41
    • 0033562343 scopus 로고    scopus 로고
    • waf1 promoter activity induced by histone deacetylase inhibitor in NIH3T3 cells
    • waf1 promoter activity induced by histone deacetylase inhibitor in NIH3T3 cells. J Cell Biochem (1999) 73:291-302.
    • (1999) J Cell Biochem , vol.73 , pp. 291-302
    • Xiao, H.1    Hasegawa, T.2    Isobe, K.3
  • 42
    • 0028022785 scopus 로고
    • Trichostatin A induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines
    • Hoshikawa Y, Kwon HJ, Yoshida M, Horinouchi S, Beppu T: Trichostatin A induces morphological changes and gelsolin expression by inhibiting histone deacetylase in human carcinoma cell lines. Exp Cell Res (1994) 214:189-197.
    • (1994) Exp Cell Res , vol.214 , pp. 189-197
    • Hoshikawa, Y.1    Kwon, H.J.2    Yoshida, M.3    Horinouchi, S.4    Beppu, T.5
  • 43
    • 0030597111 scopus 로고    scopus 로고
    • Involvement of histone hyperacetylation in triggering DNA fragmentation of rat thymocytes undergoing apoptosis
    • Lee E, Furukubo T, Miyabe T, Yamauchi A, Kariya K: Involvement of histone hyperacetylation in triggering DNA fragmentation of rat thymocytes undergoing apoptosis. FEBS Lett (1996) 395:183-187.
    • (1996) FEBS Lett , vol.395 , pp. 183-187
    • Lee, E.1    Furukubo, T.2    Miyabe, T.3    Yamauchi, A.4    Kariya, K.5
  • 44
    • 0034901985 scopus 로고    scopus 로고
    • Trichostatin A is a histone deacetylase inhibitor with potent antitumor activity against breast cancer in vivo
    • Vigushin DM, Ali S, Pace PE, Mirsaidi N, Ito K, Adcock I, Coombes RC: Trichostatin A is a histone deacetylase inhibitor with potent antitumor activity against breast cancer in vivo. Clin Cancer Res (2001) 7:971-976.
    • (2001) Clin Cancer Res , vol.7 , pp. 971-976
    • Vigushin, D.M.1    Ali, S.2    Pace, P.E.3    Mirsaidi, N.4    Ito, K.5    Adcock, I.6    Coombes, R.C.7
  • 46
    • 0025083327 scopus 로고
    • Structural specificity for biological activity of trichostatin A, a specific inhibitor of mammalian cell cycle with potent differentiation-inducing activity in Friend leukemia cells
    • Yoshida M, Hoshikawa Y, Koseki K, Mori K, Beppu T: Structural specificity for biological activity of trichostatin A, a specific inhibitor of mammalian cell cycle with potent differentiation-inducing activity in Friend leukemia cells. J Antibiot (1990) 43:1101-1106.
    • (1990) J Antibiot , vol.43 , pp. 1101-1106
    • Yoshida, M.1    Hoshikawa, Y.2    Koseki, K.3    Mori, K.4    Beppu, T.5
  • 47
    • 0029974613 scopus 로고    scopus 로고
    • Modulation of growth and differentiation of human colon carcinoma cells by histone deacetylase inhibitory trichostatins
    • Li X, Yoshida M, Beppu T, Lotan R: Modulation of growth and differentiation of human colon carcinoma cells by histone deacetylase inhibitory trichostatins. Int J Oncol (1996) 8:431-437.
    • (1996) Int J Oncol , vol.8 , pp. 431-437
    • Li, X.1    Yoshida, M.2    Beppu, T.3    Lotan, R.4
  • 48
    • 0029946960 scopus 로고    scopus 로고
    • Oxamflatin: A novel compound which reverses malignant phenotype to normal one via induction of JunD
    • Sonoda H, Nishida K, Takayuki N, Yoshioka T, Ohtani M, Sugita K: Oxamflatin: A novel compound which reverses malignant phenotype to normal one via induction of JunD. Oncogene (1996) 13:143-149.
    • (1996) Oncogene , vol.13 , pp. 143-149
    • Sonoda, H.1    Nishida, K.2    Takayuki, N.3    Yoshioka, T.4    Ohtani, M.5    Sugita, K.6
  • 49
    • 0029998412 scopus 로고    scopus 로고
    • (2E)-5-[3-[(phenylsulfonyl)amino]phenyl]-pent-2-en-4-ynohydroxamic acid and its derivatives as novel and potent inhibitors of ras transformation
    • Ohtani M, Matsuura T, Shirahase K, Sugita K: (2E)-5-[3-[(phenylsulfonyl)amino]phenyl]-pent-2-en-4-ynohydroxamic acid and its derivatives as novel and potent inhibitors of ras transformation. J Med Chem (1996) 39:2871-2873.
    • (1996) J Med Chem , vol.39 , pp. 2871-2873
    • Ohtani, M.1    Matsuura, T.2    Shirahase, K.3    Sugita, K.4
  • 50
    • 0033561497 scopus 로고    scopus 로고
    • Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase
    • Kim YB, Lee KH, Sugita K, Yoshida M, Horinouchi S: Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase. Oncogene (1999) 18:2461-2470.
    • (1999) Oncogene , vol.18 , pp. 2461-2470
    • Kim, Y.B.1    Lee, K.H.2    Sugita, K.3    Yoshida, M.4    Horinouchi, S.5
  • 53
    • 0035577768 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells
    • Munster PN, Troso-Sandoval T, Rosen N, Rifkind R, Marks PA, Richon VM: The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells. Cancer Res (2001) 61:8492-8497.
    • (2001) Cancer Res , vol.61 , pp. 8492-8497
    • Munster, P.N.1    Troso-Sandoval, T.2    Rosen, N.3    Rifkind, R.4    Marks, P.A.5    Richon, V.M.6
  • 54
    • 0034297220 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid as a potential therapeutic agent for human breast cancer treatment
    • Huang L, Pardee AB: Suberoylanilide hydroxamic acid as a potential therapeutic agent for human breast cancer treatment. Mol Med (2000) 6:849-866.
    • (2000) Mol Med , vol.6 , pp. 849-866
    • Huang, L.1    Pardee, A.B.2
  • 56
    • 0035724488 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce caspase-dependent apoptosis and downregulation of daxx in acute promyelocytic leukaemia with t(15;17)
    • Amin HM, Saeed S, Alkan S: Histone deacetylase inhibitors induce caspase-dependent apoptosis and downregulation of daxx in acute promyelocytic leukaemia with t(15;17). Br J Haematol (2001) 115:287-297.
    • (2001) Br J Haematol , vol.115 , pp. 287-297
    • Amin, H.M.1    Saeed, S.2    Alkan, S.3
  • 57
    • 0033367018 scopus 로고    scopus 로고
    • Chemoprevention of carcinogen-induced mammary tumorigenesis by the hybrid polar cytodifferentiation agent, suberanilohydroxamic acid (SAHA)
    • Cohen LA, Amin S, Marks PA, Rifkind RA, Desai D, Richon VM: Chemoprevention of carcinogen-induced mammary tumorigenesis by the hybrid polar cytodifferentiation agent, suberanilohydroxamic acid (SAHA). Anticancer Res (1999) 19:4999-5005.
    • (1999) Anticancer Res , vol.19 , pp. 4999-5005
    • Cohen, L.A.1    Amin, S.2    Marks, P.A.3    Rifkind, R.A.4    Desai, D.5    Richon, V.M.6
  • 59
    • 0030744926 scopus 로고    scopus 로고
    • Analogs of trichostatin A and trapoxin B as histone deacetylase inhibitors
    • Jung M, Hoffmann K, Brosch G, Loidl P: Analogs of trichostatin A and trapoxin B as histone deacetylase inhibitors. Bioorg Med Chem Lett (1997) 7:1655-1658.
    • (1997) Bioorg Med Chem Lett , vol.7 , pp. 1655-1658
    • Jung, M.1    Hoffmann, K.2    Brosch, G.3    Loidl, P.4
  • 60
    • 0037075081 scopus 로고    scopus 로고
    • Inhibitors of human histone deacetylase: Synthesis and enzyme and cellular activity of straight chain details of hydroxamates
    • Remiszewski SW, Sambucetti LC, Atadja P, Bair KW, Comell WD, Green MA, Howell KL, Jung M, Kwon P, Trogani N, Walker H: Inhibitors of human histone deacetylase: Synthesis and enzyme and cellular activity of straight chain details of hydroxamates. J Med Chem (2002) 45:753-757. Presents details of cell growth inhibition for an amide compound in human tumor cell lines.
    • (2002) J Med Chem , vol.45 , pp. 753-757
    • Remiszewski, S.W.1    Sambucetti, L.C.2    Atadja, P.3    Bair, K.W.4    Comell, W.D.5    Green, M.A.6    Howell, K.L.7    Jung, M.8    Kwon, P.9    Trogani, N.10    Walker, H.11
  • 61
    • 0035927427 scopus 로고    scopus 로고
    • 3-(4-aroyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides, a new class of synthetic histone deacetylase inhibitors
    • Massa S, Mai A, Sbardella G, Esposito M, Ragno R, Loidl P, Brosch G: 3-(4-aroyl-1H-pyrrol-2-yl)-N-hydroxy-2-propenamides, a new class of synthetic histone deacetylase inhibitors. J Med Chem (2001) 44:2069-2072. Describes a novel heteroaromatic spacer.
    • (2001) J Med Chem , vol.44 , pp. 2069-2072
    • Massa, S.1    Mai, A.2    Sbardella, G.3    Esposito, M.4    Ragno, R.5    Loidl, P.6    Brosch, G.7
  • 63
    • 0035961036 scopus 로고    scopus 로고
    • Synthesis of 7200 small molecules based on a substructural analysis of the histone deacetylase inhibitors trichostatin and trapoxin
    • Stemson SM, Wong JC, Grozinger CM, Schreiber SL: Synthesis of 7200 small molecules based on a substructural analysis of the histone deacetylase inhibitors trichostatin and trapoxin. Org Lett (2001) 3:4239-4242.
    • (2001) Org Lett , vol.3 , pp. 4239-4242
    • Stemson, S.M.1    Wong, J.C.2    Grozinger, C.M.3    Schreiber, S.L.4
  • 64
    • 0035024737 scopus 로고    scopus 로고
    • Histone deacetylase: A target for antiproliferative and antiprotozoal agents
    • Meinke PT, Liberator P: Histone deacetylase: A target for antiproliferative and antiprotozoal agents. Curr Med Chem (2001) 8:211-235.
    • (2001) Curr Med Chem , vol.8 , pp. 211-235
    • Meinke, P.T.1    Liberator, P.2
  • 65
    • 0016334991 scopus 로고
    • Cytostatic activity of chlamydocin, a rapidly inactivated cyclic tetrapeptide
    • Staehelin H, Trippmacher A: Cytostatic activity of chlamydocin, a rapidly inactivated cyclic tetrapeptide. Eur J Cancer (1974) 10:801-808.
    • (1974) Eur J Cancer , vol.10 , pp. 801-808
    • Staehelin, H.1    Trippmacher, A.2
  • 66
    • 0023065338 scopus 로고
    • Analogs of the cytostatic and antimitogenic agents chlamydocin and HC-toxin: Synthesis and biological activity of chloromethyl ketone and diazomethyl ketone-functionalized cyclic tetrapeptides
    • Shute RE, Dunlap B, Rich DH: Analogs of the cytostatic and antimitogenic agents chlamydocin and HC-toxin: Synthesis and biological activity of chloromethyl ketone and diazomethyl ketone-functionalized cyclic tetrapeptides. J Med Chem (1987) 30:71-78.
    • (1987) J Med Chem , vol.30 , pp. 71-78
    • Shute, R.E.1    Dunlap, B.2    Rich, D.H.3
  • 70
    • 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: Apicidin, a histone deacetylase inhibitor, induces apoptosis and Fas/Fas ligand expression in human acute promyelocytic leukemia cells. J Biol Chem (2002) 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
  • 74
    • 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: Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc Natl Acad Sci USA (2001) 98:87-92. List of cyclic peptide hydroxamates and their activities in human HDAC-1 and mouse HDAC-6.
    • (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
  • 76
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton J, Hassig CA, Schreiber SL: A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science (1996) 272:408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 77
    • 0029795991 scopus 로고    scopus 로고
    • Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function
    • Taunton J, Collins JL, Schreiber SL: Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function. J Am Chem Soc (1996) 118:10412-10422.
    • (1996) J Am Chem Soc , vol.118 , pp. 10412-10422
    • Taunton, J.1    Collins, J.L.2    Schreiber, S.L.3
  • 78
    • 4243833322 scopus 로고    scopus 로고
    • Valproic acid and derivatives thereof as histone deacetylase inhibitors. EP-01170008 (2002)
    • CHEMOTHERAPEUTISCHES FORSCHUNGSINSTITUT GEORG-SPEYER-HAUS (Göttlicher M, Heinzel T, Groner B, Herrlich P): Valproic acid and derivatives thereof as histone deacetylase inhibitors. EP-01170008 (2002).
    • Göttlicher, M.1    Heinzel, T.2    Groner, B.3    Herrlich, P.4
  • 79
  • 80
    • 0038287618 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylase. WO-00138322 (2001)
    • METHYLGENE INC (Delorme D, Ruel R, Lavoie R, Thibault C, Abou-Khalil E): Inhibitors of histone deacetylase. WO-00138322 (2001). Lists a variety of HDA/structural types.
    • Delorme, D.1    Ruel, R.2    Lavoie, R.3    Thibault, C.4    Abou-Khalil, E.5
  • 81
    • 0037612163 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylase. WO-00170675 (2001)
    • METHYLGENE INC (Delorme D, Woo SH, Vaisburg A): Inhibitors of histone deacetylase. WO-00170675 (2001) List a variety of HDA/structural types.
    • Delorme, D.1    Woo, S.H.2    Vaisburg, A.3
  • 82
    • 0037950272 scopus 로고    scopus 로고
    • Preparation of sulfonamidoaryl hydroxamic acids as inflammation and tumor inhibitors. WO-09312075 (1993)
    • SHIONOGI AND CO LTD (Ohtani M, Arita H, Sugita K, Matsuura T, Shirahase K): Preparation of sulfonamidoaryl hydroxamic acids as inflammation and tumor inhibitors. WO-09312075 (1993).
    • Ohtani, M.1    Arita, H.2    Sugita, K.3    Matsuura, T.4    Shirahase, K.5
  • 83
    • 0037950233 scopus 로고    scopus 로고
    • Novel potent inducers of terminal differentiation and methods of use thereof. WO-09307148 (1993)
    • SLOAN-KETTERING INSTITUTE FOR CANCER RESEARCH/COLUMBIA UNIVERSITY (Breslow R, Marks PA, Rifkind RA, Jursic B): Novel potent inducers of terminal differentiation and methods of use thereof. WO-09307148 (1993).
    • Breslow, R.1    Marks, P.A.2    Rifkind, R.A.3    Jursic, B.4
  • 84
    • 0037950234 scopus 로고    scopus 로고
    • Histone deacetylases, and uses related thereto. WO-09735990 (1997)
    • PRESIDENT AND FELLOWS OF HARVARD COLLEGE (Schreiber SL, Taunton J, Hassig CA, Jamison TF): Histone deacetylases, and uses related thereto. WO-09735990 (1997).
    • Schreiber, S.L.1    Taunton, J.2    Hassig, C.A.3    Jamison, T.F.4


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