메뉴 건너뛰기




Volumn 32, Issue 3, 2006, Pages 157-165

Histone deacetylase inhibitors: Multifunctional anticancer agents

Author keywords

Angiogenesis; Blood flow; Carcinogenesis; Histone deacetylase; Histone deacetylase inhibitor; Invasion; Migration

Indexed keywords

4 [N (2 HYDROXYETHYL) N [2 (3 INDOLYL)ETHYL]AMINOMETHYL]CINNAMOHYDROXAMIC ACID; ANGIOGENESIS INHIBITOR; ARYLBUTYRIC ACID DERIVATIVE; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE INHIBITOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; RETINOIC ACID; VASCULOTROPIN; VATALANIB;

EID: 33645950778     PISSN: 03057372     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ctrv.2005.12.006     Document Type: Review
Times cited : (225)

References (89)
  • 1
    • 2942724589 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Development as cancer therapy
    • discussion 281-268
    • Marks P.A., Richon V.M., Kelly W.K., Chiao J.H., and Miller T. Histone deacetylase inhibitors: Development as cancer therapy. Novartis Found Symp 259 (2004) 269-281 discussion 281-268
    • (2004) Novartis Found Symp , vol.259 , pp. 269-281
    • Marks, P.A.1    Richon, V.M.2    Kelly, W.K.3    Chiao, J.H.4    Miller, T.5
  • 2
    • 18144373452 scopus 로고    scopus 로고
    • Valproic acid alters chromatin structure by regulation of chromatin modulation proteins
    • Marchion D.C., Bicaku E., Daud A.I., Sullivan D.M., and Munster P.N. Valproic acid alters chromatin structure by regulation of chromatin modulation proteins. Cancer Res 65 (2005) 3815-3822
    • (2005) Cancer Res , vol.65 , pp. 3815-3822
    • Marchion, D.C.1    Bicaku, E.2    Daud, A.I.3    Sullivan, D.M.4    Munster, P.N.5
  • 3
    • 0344431240 scopus 로고    scopus 로고
    • Fr901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor
    • Nakajima H., Kim Y.B., Terano H., Yoshida M., and Horinouchi S. Fr901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor. Exp Cell Res 241 (1998) 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
  • 4
    • 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., et al. A synthetic inhibitor of histone deacetylase, ms-27-275, with marked in vivo antitumor activity against human tumors. Proc Natl Acad Sci USA 96 (1999) 4592-4597
    • (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
  • 7
    • 0036527775 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer
    • Johnstone R.W. Histone-deacetylase inhibitors: Novel drugs for the treatment of cancer. Nat Rev Drug Discov 1 (2002) 287-299
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 287-299
    • Johnstone, R.W.1
  • 8
    • 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 M.W., Denlinger C.E., Broad R.M., Yeung F., Reilly E.T., Shi Y., et al. Ineffectiveness of histone deacetylase inhibitors to induce apoptosis involves the transcriptional activation of nf-kappa b through the akt pathway. J Biol Chem 278 (2003) 18980-18989
    • (2003) J Biol Chem , vol.278 , pp. 18980-18989
    • Mayo, M.W.1    Denlinger, C.E.2    Broad, R.M.3    Yeung, F.4    Reilly, E.T.5    Shi, Y.6
  • 9
    • 10444282190 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors for the treatment of cancer
    • Lindemann R.K., Gabrielli B., and Johnstone R.W. Histone-deacetylase inhibitors for the treatment of cancer. Cell Cycle 3 (2004) 779-788
    • (2004) Cell Cycle , vol.3 , pp. 779-788
    • Lindemann, R.K.1    Gabrielli, B.2    Johnstone, R.W.3
  • 10
    • 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., and Verdin E. The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. Gene Expr 5 (1996) 245-253
    • (1996) Gene Expr , vol.5 , pp. 245-253
    • Van Lint, C.1    Emiliani, S.2    Verdin, E.3
  • 11
  • 12
    • 0037015071 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor saha arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin
    • Butler L.M., Zhou X., Xu W.S., Scher H.I., Rifkind R.A., Marks P.A., et al. The histone deacetylase inhibitor saha arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin. Proc Natl Acad Sci USA 99 (2002) 11700-11705
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11700-11705
    • Butler, L.M.1    Zhou, X.2    Xu, W.S.3    Scher, H.I.4    Rifkind, R.A.5    Marks, P.A.6
  • 13
    • 0042905956 scopus 로고    scopus 로고
    • Gene expression profiling of multiple histone deacetylase (hdac) inhibitors: Defining a common gene set produced by hdac inhibition in t24 and mda carcinoma cell lines
    • Glaser K.B., Staver M.J., Waring J.F., Stender J., Ulrich R.G., and Davidsen S.K. Gene expression profiling of multiple histone deacetylase (hdac) inhibitors: Defining a common gene set produced by hdac inhibition in t24 and mda carcinoma cell lines. Mol Cancer Ther 2 (2003) 151-163
    • (2003) Mol Cancer Ther , vol.2 , pp. 151-163
    • Glaser, K.B.1    Staver, M.J.2    Waring, J.F.3    Stender, J.4    Ulrich, R.G.5    Davidsen, S.K.6
  • 14
    • 14844353574 scopus 로고    scopus 로고
    • Identification and functional significance of genes regulated by structurally different histone deacetylase inhibitors
    • Peart M.J., Smyth G.K., van Laar R.K., Bowtell D.D., Richon V.M., Marks P.A., et al. Identification and functional significance of genes regulated by structurally different histone deacetylase inhibitors. Proc Natl Acad Sci USA 102 (2005) 3697-3702
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3697-3702
    • Peart, M.J.1    Smyth, G.K.2    van Laar, R.K.3    Bowtell, D.D.4    Richon, V.M.5    Marks, P.A.6
  • 15
    • 24944535335 scopus 로고    scopus 로고
    • Regulation of lsd1 histone demethylase activity by its associated factors
    • Shi Y.J., Matson C., Lan F., Iwase S., Baba T., and Shi Y. Regulation of lsd1 histone demethylase activity by its associated factors. Mol Cell 19 (2005) 857-864
    • (2005) Mol Cell , vol.19 , pp. 857-864
    • Shi, Y.J.1    Matson, C.2    Lan, F.3    Iwase, S.4    Baba, T.5    Shi, Y.6
  • 16
    • 24144470824 scopus 로고    scopus 로고
    • Taking lsd 1 to a new high
    • Wysocka J., Milne T.A., and Allis C.D. Taking lsd 1 to a new high. Cell 122 (2005) 654-658
    • (2005) Cell , vol.122 , pp. 654-658
    • Wysocka, J.1    Milne, T.A.2    Allis, C.D.3
  • 17
    • 0041347519 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy: Is transcription the primary target?
    • Johnstone R.W., and Licht J.D. Histone deacetylase inhibitors in cancer therapy: Is transcription the primary target?. Cancer Cell 4 (2003) 13-18
    • (2003) Cancer Cell , vol.4 , pp. 13-18
    • Johnstone, R.W.1    Licht, J.D.2
  • 18
    • 0038079767 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor ms-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21cip1/waf1 1
    • Rosato R.R., Almenara J.A., and Grant S. The histone deacetylase inhibitor ms-275 promotes differentiation or apoptosis in human leukemia cells through a process regulated by generation of reactive oxygen species and induction of p21cip1/waf1 1. Cancer Res 63 (2003) 3637-3645
    • (2003) Cancer Res , vol.63 , pp. 3637-3645
    • Rosato, R.R.1    Almenara, J.A.2    Grant, S.3
  • 19
    • 16344376556 scopus 로고    scopus 로고
    • Ku70 acetylation mediates neuroblastoma cell death induced by histone deacetylase inhibitors
    • Subramanian C., Opipari Jr. A.W., Bian X., Castle V.P., and Kwok R.P. Ku70 acetylation mediates neuroblastoma cell death induced by histone deacetylase inhibitors. Proc Natl Acad Sci USA 102 (2005) 4842-4847
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4842-4847
    • Subramanian, C.1    Opipari Jr., A.W.2    Bian, X.3    Castle, V.P.4    Kwok, R.P.5
  • 20
    • 12144286529 scopus 로고    scopus 로고
    • Acetylation of the c terminus of ku70 by cbp and pcaf controls bax-mediated apoptosis
    • Cohen H.Y., Lavu S., Bitterman K.J., Hekking B., Imahiyerobo T.A., Miller C., et al. Acetylation of the c terminus of ku70 by cbp and pcaf controls bax-mediated apoptosis. Mol Cell 13 (2004) 627-638
    • (2004) Mol Cell , vol.13 , pp. 627-638
    • Cohen, H.Y.1    Lavu, S.2    Bitterman, K.J.3    Hekking, B.4    Imahiyerobo, T.A.5    Miller, C.6
  • 21
    • 20044390016 scopus 로고    scopus 로고
    • Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors
    • Ungerstedt J.S., Sowa Y., Xu W.S., Shao Y., Dokmanovic M., Perez G., et al. Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors. Proc Natl Acad Sci USA 102 (2005) 673-678
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 673-678
    • Ungerstedt, J.S.1    Sowa, Y.2    Xu, W.S.3    Shao, Y.4    Dokmanovic, M.5    Perez, G.6
  • 22
    • 18544367699 scopus 로고    scopus 로고
    • Apicidin, a histone deacetylase inhibitor, induces apoptosis and fas/fas ligand expression in human acute promyelocytic leukemia cells
    • Kwon S.H., Ahn S.H., Kim Y.K., Bae G.U., Yoon J.W., Hong S., et al. Apicidin, a histone deacetylase inhibitor, induces apoptosis and fas/fas ligand expression in human acute promyelocytic leukemia cells. J Biol Chem 277 (2002) 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
  • 23
    • 0033199896 scopus 로고    scopus 로고
    • Hybrid polar histone deacetylase inhibitor induces apoptosis and cd95/cd95 ligand expression in human neuroblastoma
    • Glick R.D., Swendeman S.L., Coffey D.C., Rifkind R.A., Marks P.A., Richon V.M., et al. Hybrid polar histone deacetylase inhibitor induces apoptosis and cd95/cd95 ligand expression in human neuroblastoma. Cancer Res 59 (1999) 4392-4399
    • (1999) Cancer Res , vol.59 , pp. 4392-4399
    • Glick, R.D.1    Swendeman, S.L.2    Coffey, D.C.3    Rifkind, R.A.4    Marks, P.A.5    Richon, V.M.6
  • 24
    • 13444306459 scopus 로고    scopus 로고
    • Tumor-selective action of hdac inhibitors involves trail induction in acute myeloid leukemia cells
    • Nebbioso A., Clarke N., Voltz E., Germain E., Ambrosino C., Bontempo P., et al. Tumor-selective action of hdac inhibitors involves trail induction in acute myeloid leukemia cells. Nat Med 11 (2005) 77-84
    • (2005) Nat Med , vol.11 , pp. 77-84
    • Nebbioso, A.1    Clarke, N.2    Voltz, E.3    Germain, E.4    Ambrosino, C.5    Bontempo, P.6
  • 25
    • 13444274622 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylases induce tumor-selective apoptosis through activation of the death receptor pathway
    • Insinga A., Monestiroli S., Ronzoni S., Gelmetti V., Marchesi F., Viale A., et al. Inhibitors of histone deacetylases induce tumor-selective apoptosis through activation of the death receptor pathway. Nat Med 11 (2005) 71-76
    • (2005) Nat Med , vol.11 , pp. 71-76
    • Insinga, A.1    Monestiroli, S.2    Ronzoni, S.3    Gelmetti, V.4    Marchesi, F.5    Viale, A.6
  • 26
    • 11144221007 scopus 로고    scopus 로고
    • Apoptotic and autophagic cell death induced by histone deacetylase inhibitors
    • Shao Y., Gao Z., Marks P.A., and Jiang X. Apoptotic and autophagic cell death induced by histone deacetylase inhibitors. Proc Natl Acad Sci USA 101 (2004) 18030-18035
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 18030-18035
    • Shao, Y.1    Gao, Z.2    Marks, P.A.3    Jiang, X.4
  • 27
    • 20144388146 scopus 로고    scopus 로고
    • Loss of acetylation at lys16 and trimethylation at lys20 of histone h4 is a common hallmark of human cancer
    • Fraga M.F., Ballestar E., Villar-Garea A., Boix-Chornet M., Espada J., Schotta G., et al. Loss of acetylation at lys16 and trimethylation at lys20 of histone h4 is a common hallmark of human cancer. Nat Genet 37 (2005) 391-400
    • (2005) Nat Genet , vol.37 , pp. 391-400
    • Fraga, M.F.1    Ballestar, E.2    Villar-Garea, A.3    Boix-Chornet, M.4    Espada, J.5    Schotta, G.6
  • 29
    • 21044447215 scopus 로고    scopus 로고
    • Increased expression of histone deacetylase 2 is found in human gastric cancer
    • Song J., Noh J.H., Lee J.H., Eun J.W., Ahn Y.M., Kim S.Y., et al. Increased expression of histone deacetylase 2 is found in human gastric cancer. Apmis 113 (2005) 264-268
    • (2005) Apmis , vol.113 , pp. 264-268
    • Song, J.1    Noh, J.H.2    Lee, J.H.3    Eun, J.W.4    Ahn, Y.M.5    Kim, S.Y.6
  • 30
    • 0028816996 scopus 로고
    • Tumors in rubinstein-taybi syndrome
    • Miller R.W., and Rubinstein J.H. Tumors in rubinstein-taybi syndrome. Am J Med Genet 56 (1995) 112-115
    • (1995) Am J Med Genet , vol.56 , pp. 112-115
    • Miller, R.W.1    Rubinstein, J.H.2
  • 32
    • 0033634946 scopus 로고    scopus 로고
    • Acquisition of oncogenic potential by rar chimeras in acute promyelocytic leukemia through formation of homodimers
    • Lin R.J., and Evans R.M. Acquisition of oncogenic potential by rar chimeras in acute promyelocytic leukemia through formation of homodimers. Mol Cell 5 (2000) 821-830
    • (2000) Mol Cell , vol.5 , pp. 821-830
    • Lin, R.J.1    Evans, R.M.2
  • 33
    • 0035099686 scopus 로고    scopus 로고
    • The growth suppressor pml represses transcription by functionally and physically interacting with histone deacetylases
    • Wu W.S., Vallian S., Seto E., Yang W.M., Edmondson D., Roth S., et al. The growth suppressor pml represses transcription by functionally and physically interacting with histone deacetylases. Mol Cell Biol 21 (2001) 2259-2268
    • (2001) Mol Cell Biol , vol.21 , pp. 2259-2268
    • Wu, W.S.1    Vallian, S.2    Seto, E.3    Yang, W.M.4    Edmondson, D.5    Roth, S.6
  • 34
    • 0034817075 scopus 로고    scopus 로고
    • Eto, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds msin3a through its oligomerization domain
    • Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., et al. Eto, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds msin3a through its oligomerization domain. Mol Cell Biol 21 (2001) 6470-6483
    • (2001) Mol Cell Biol , vol.21 , pp. 6470-6483
    • Amann, J.M.1    Nip, J.2    Strom, D.K.3    Lutterbach, B.4    Harada, H.5    Lenny, N.6
  • 35
    • 0032516221 scopus 로고    scopus 로고
    • Histone deacetylase associated with msin3a mediates repression by the acute promyelocytic leukemia-associated plzf protein
    • David G., Alland L., Hong S.H., Wong C.W., DePinho R.A., and Dejean A. Histone deacetylase associated with msin3a mediates repression by the acute promyelocytic leukemia-associated plzf protein. Oncogene 16 (1998) 2549-2556
    • (1998) Oncogene , vol.16 , pp. 2549-2556
    • David, G.1    Alland, L.2    Hong, S.H.3    Wong, C.W.4    DePinho, R.A.5    Dejean, A.6
  • 36
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukaemia
    • Lin R.J., Nagy L., Inoue S., Shao W., Miller Jr. W.H., and Evans R.M. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature 391 (1998) 811-814
    • (1998) Nature , vol.391 , pp. 811-814
    • Lin, R.J.1    Nagy, L.2    Inoue, S.3    Shao, W.4    Miller Jr., W.H.5    Evans, R.M.6
  • 37
    • 9544220768 scopus 로고    scopus 로고
    • The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the creb-binding protein
    • Borrow J., Stanton Jr. V.P., Andresen J.M., Becher R., Behm F.G., Chaganti R.S., et al. The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the creb-binding protein. Nat Genet 14 (1996) 33-41
    • (1996) Nat Genet , vol.14 , pp. 33-41
    • Borrow, J.1    Stanton Jr., V.P.2    Andresen, J.M.3    Becher, R.4    Behm, F.G.5    Chaganti, R.S.6
  • 38
    • 0030792867 scopus 로고    scopus 로고
    • All patients with the t(11;16)(q23;p13.3) that involves mll and cbp have treatment-related hematologic disorders
    • Rowley J.D., Reshmi S., Sobulo O., Musvee T., Anastasi J., Raimondi S., et al. All patients with the t(11;16)(q23;p13.3) that involves mll and cbp have treatment-related hematologic disorders. Blood 90 (1997) 535-541
    • (1997) Blood , vol.90 , pp. 535-541
    • Rowley, J.D.1    Reshmi, S.2    Sobulo, O.3    Musvee, T.4    Anastasi, J.5    Raimondi, S.6
  • 39
    • 0032531688 scopus 로고    scopus 로고
    • The laz3(bcl-6) oncoprotein recruits a smrt/msin3a/histone deacetylase containing complex to mediate transcriptional repression
    • Dhordain P., Lin R.J., Quief S., Lantoine D., Kerckaert J.P., Evans R.M., et al. The laz3(bcl-6) oncoprotein recruits a smrt/msin3a/histone deacetylase containing complex to mediate transcriptional repression. Nucl Acids Res 26 (1998) 4645-4651
    • (1998) Nucl Acids Res , vol.26 , pp. 4645-4651
    • Dhordain, P.1    Lin, R.J.2    Quief, S.3    Lantoine, D.4    Kerckaert, J.P.5    Evans, R.M.6
  • 41
    • 0036134288 scopus 로고    scopus 로고
    • Induction of differentiation and suppression of malignant phenotype of human neuroblastoma be(2)-c cells by valproic acid: Enhancement by combination with interferon-alpha
    • Cinatl Jr. J., Kotchetkov R., Blaheta R., Driever P.H., Vogel J.U., and Cinatl J. Induction of differentiation and suppression of malignant phenotype of human neuroblastoma be(2)-c cells by valproic acid: Enhancement by combination with interferon-alpha. Int J Oncol 20 (2002) 97-106
    • (2002) Int J Oncol , vol.20 , pp. 97-106
    • Cinatl Jr., J.1    Kotchetkov, R.2    Blaheta, R.3    Driever, P.H.4    Vogel, J.U.5    Cinatl, J.6
  • 42
    • 0043016178 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor laq824 both lowers expression and promotes proteasomal degradation of bcr-abl and induces apoptosis of imatinib mesylate-sensitive or -refractory chronic myelogenous leukemia-blast crisis cells
    • Nimmanapalli R., Fuino L., Bali P., Gasparetto M., Glozak M., Tao J., et al. Histone deacetylase inhibitor laq824 both lowers expression and promotes proteasomal degradation of bcr-abl and induces apoptosis of imatinib mesylate-sensitive or -refractory chronic myelogenous leukemia-blast crisis cells. Cancer Res 63 (2003) 5126-5135
    • (2003) Cancer Res , vol.63 , pp. 5126-5135
    • Nimmanapalli, R.1    Fuino, L.2    Bali, P.3    Gasparetto, M.4    Glozak, M.5    Tao, J.6
  • 43
    • 1642490813 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor laq824 down-regulates her-2 and sensitizes human breast cancer cells to trastuzumab, taxotere, gemcitabine, and epothilone b
    • Fuino L., Bali P., Wittmann S., Donapaty S., Guo F., Yamaguchi H., et al. Histone deacetylase inhibitor laq824 down-regulates her-2 and sensitizes human breast cancer cells to trastuzumab, taxotere, gemcitabine, and epothilone b. Mol Cancer Ther 2 (2003) 971-984
    • (2003) Mol Cancer Ther , vol.2 , pp. 971-984
    • Fuino, L.1    Bali, P.2    Wittmann, S.3    Donapaty, S.4    Guo, F.5    Yamaguchi, H.6
  • 44
    • 0037012344 scopus 로고    scopus 로고
    • Modulation of p53, erbb1, erbb2, and raf-1 expression in lung cancer cells by depsipeptide fr901228
    • Yu X., Guo Z.S., Marcu M.G., Neckers L., Nguyen D.M., Chen G.A., et al. Modulation of p53, erbb1, erbb2, and raf-1 expression in lung cancer cells by depsipeptide fr901228. J Natl Cancer Inst 94 (2002) 504-513
    • (2002) J Natl Cancer Inst , vol.94 , pp. 504-513
    • Yu, X.1    Guo, Z.S.2    Marcu, M.G.3    Neckers, L.4    Nguyen, D.M.5    Chen, G.A.6
  • 45
    • 18944403682 scopus 로고    scopus 로고
    • Regulation of tissue-specific and extracellular matrix-related genes by a class i histone deacetylase
    • Whetstine J.R., Ceron J., Ladd B., Dufourcq P., Reinke V., and Shi Y. Regulation of tissue-specific and extracellular matrix-related genes by a class i histone deacetylase. Mol Cell 18 (2005) 483-490
    • (2005) Mol Cell , vol.18 , pp. 483-490
    • Whetstine, J.R.1    Ceron, J.2    Ladd, B.3    Dufourcq, P.4    Reinke, V.5    Shi, Y.6
  • 46
    • 2442430362 scopus 로고    scopus 로고
    • Expression of the metastasis-associated mta1 protein and its relationship to deacetylation of the histone h4 in esophageal squamous cell carcinomas
    • Toh Y., Ohga T., Endo K., Adachi E., Kusumoto H., Haraguchi M., et al. Expression of the metastasis-associated mta1 protein and its relationship to deacetylation of the histone h4 in esophageal squamous cell carcinomas. Int J Cancer 110 (2004) 362-367
    • (2004) Int J Cancer , vol.110 , pp. 362-367
    • Toh, Y.1    Ohga, T.2    Endo, K.3    Adachi, E.4    Kusumoto, H.5    Haraguchi, M.6
  • 47
    • 4344685827 scopus 로고    scopus 로고
    • Expression profiling of sodium butyrate (nab)-treated cells: Identification of regulation of genes related to cytokine signaling and cancer metastasis by nab
    • Joseph J., Mudduluru G., Antony S., Vashistha S., Ajitkumar P., and Somasundaram K. Expression profiling of sodium butyrate (nab)-treated cells: Identification of regulation of genes related to cytokine signaling and cancer metastasis by nab. Oncogene 23 (2004) 6304-6315
    • (2004) Oncogene , vol.23 , pp. 6304-6315
    • Joseph, J.1    Mudduluru, G.2    Antony, S.3    Vashistha, S.4    Ajitkumar, P.5    Somasundaram, K.6
  • 48
    • 3142702962 scopus 로고    scopus 로고
    • Invasion of v-fos(fbr)-transformed cells is dependent upon histone deacetylase activity and suppression of histone deacetylase regulated genes
    • McGarry L.C., Winnie J.N., and Ozanne B.W. Invasion of v-fos(fbr)-transformed cells is dependent upon histone deacetylase activity and suppression of histone deacetylase regulated genes. Oncogene 23 (2004) 5284-5292
    • (2004) Oncogene , vol.23 , pp. 5284-5292
    • McGarry, L.C.1    Winnie, J.N.2    Ozanne, B.W.3
  • 49
    • 10744221583 scopus 로고    scopus 로고
    • Apicidin is a histone deacetylase inhibitor with anti-invasive and anti-angiogenic potentials
    • Kim S.H., Ahn S., Han J.W., Lee H.W., Lee H.Y., Lee Y.W., et al. Apicidin is a histone deacetylase inhibitor with anti-invasive and anti-angiogenic potentials. Biochem Biophys Res Commun 315 (2004) 964-970
    • (2004) Biochem Biophys Res Commun , vol.315 , pp. 964-970
    • Kim, S.H.1    Ahn, S.2    Han, J.W.3    Lee, H.W.4    Lee, H.Y.5    Lee, Y.W.6
  • 50
    • 0037057516 scopus 로고    scopus 로고
    • Phenylbutyrate inhibits the invasive properties of prostate and breast cancer cell lines in the sea urchin embryo basement membrane invasion assay
    • Dyer E.S., Paulsen M.T., Markwart S.M., Goh M., Livant D.L., and Ljungman M. Phenylbutyrate inhibits the invasive properties of prostate and breast cancer cell lines in the sea urchin embryo basement membrane invasion assay. Int J Cancer 101 (2002) 496-499
    • (2002) Int J Cancer , vol.101 , pp. 496-499
    • Dyer, E.S.1    Paulsen, M.T.2    Markwart, S.M.3    Goh, M.4    Livant, D.L.5    Ljungman, M.6
  • 51
    • 21044449385 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid (saha) has potent anti-glioma properties in vitro, ex vivo and in vivo
    • Eyupoglu I.Y., Hahnen E., Buslei R., Siebzehnrubl F.A., Savaskan N.E., Luders M., et al. Suberoylanilide hydroxamic acid (saha) has potent anti-glioma properties in vitro, ex vivo and in vivo. J Neurochem 93 (2005) 992-999
    • (2005) J Neurochem , vol.93 , pp. 992-999
    • Eyupoglu, I.Y.1    Hahnen, E.2    Buslei, R.3    Siebzehnrubl, F.A.4    Savaskan, N.E.5    Luders, M.6
  • 53
    • 3242661597 scopus 로고    scopus 로고
    • Inhibition of hepatocellular carcinomas in vitro and hepatic metastases in vivo in mice by the histone deacetylase inhibitor habut
    • Coradini D., Zorzet S., Rossin R., Scarlata I., Pellizzaro C., Turrin C., et al. Inhibition of hepatocellular carcinomas in vitro and hepatic metastases in vivo in mice by the histone deacetylase inhibitor habut. Clin Cancer Res 10 (2004) 4822-4830
    • (2004) Clin Cancer Res , vol.10 , pp. 4822-4830
    • Coradini, D.1    Zorzet, S.2    Rossin, R.3    Scarlata, I.4    Pellizzaro, C.5    Turrin, C.6
  • 54
    • 0242552447 scopus 로고    scopus 로고
    • Emerging roles of mta family members in human cancers
    • Kumar R., Wang R.A., and Bagheri-Yarmand R. Emerging roles of mta family members in human cancers. Semin Oncol 30 (2003) 30-37
    • (2003) Semin Oncol , vol.30 , pp. 30-37
    • Kumar, R.1    Wang, R.A.2    Bagheri-Yarmand, R.3
  • 55
    • 0035146442 scopus 로고    scopus 로고
    • Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor
    • Mazumdar A., Wang R.A., Mishra S.K., Adam L., Bagheri-Yarmand R., Mandal M., et al. Transcriptional repression of oestrogen receptor by metastasis-associated protein 1 corepressor. Nat Cell Biol 3 (2001) 30-37
    • (2001) Nat Cell Biol , vol.3 , pp. 30-37
    • Mazumdar, A.1    Wang, R.A.2    Mishra, S.K.3    Adam, L.4    Bagheri-Yarmand, R.5    Mandal, M.6
  • 56
    • 0035689707 scopus 로고    scopus 로고
    • Characterization of mouse metastasis-associated gene 2: Genomic structure, nuclear localization signal, and alternative potentials as transcriptional activator and repressor
    • Matsusue K., Takiguchi S., Toh Y., and Kono A. Characterization of mouse metastasis-associated gene 2: Genomic structure, nuclear localization signal, and alternative potentials as transcriptional activator and repressor. DNA Cell Biol 20 (2001) 603-611
    • (2001) DNA Cell Biol , vol.20 , pp. 603-611
    • Matsusue, K.1    Takiguchi, S.2    Toh, Y.3    Kono, A.4
  • 59
    • 17244378084 scopus 로고    scopus 로고
    • Transcriptional regulation of a metastasis suppressor gene by tip60 and beta-catenin complexes
    • Kim J.H., Kim B., Cai L., Choi H.J., Ohgi K.A., Tran C., et al. Transcriptional regulation of a metastasis suppressor gene by tip60 and beta-catenin complexes. Nature 434 (2005) 921-926
    • (2005) Nature , vol.434 , pp. 921-926
    • Kim, J.H.1    Kim, B.2    Cai, L.3    Choi, H.J.4    Ohgi, K.A.5    Tran, C.6
  • 60
    • 85047696569 scopus 로고    scopus 로고
    • Gamma-catenin expression is reduced or absent in a subset of human lung cancers and re-expression inhibits transformed cell growth
    • Winn R.A., Bremnes R.M., Bemis L., Franklin W.A., Miller Y.E., Cool C., et al. Gamma-catenin expression is reduced or absent in a subset of human lung cancers and re-expression inhibits transformed cell growth. Oncogene 21 (2002) 7497-7506
    • (2002) Oncogene , vol.21 , pp. 7497-7506
    • Winn, R.A.1    Bremnes, R.M.2    Bemis, L.3    Franklin, W.A.4    Miller, Y.E.5    Cool, C.6
  • 61
    • 11944258124 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors upregulate plakoglobin expression in bladder carcinoma cells and display antineoplastic activity in vitro and in vivo
    • Canes D., Chiang G.J., Billmeyer B.R., Austin C.A., Kosakowski M., Rieger-Christ K.M., et al. Histone deacetylase inhibitors upregulate plakoglobin expression in bladder carcinoma cells and display antineoplastic activity in vitro and in vivo. Int J Cancer 113 (2005) 841-848
    • (2005) Int J Cancer , vol.113 , pp. 841-848
    • Canes, D.1    Chiang, G.J.2    Billmeyer, B.R.3    Austin, C.A.4    Kosakowski, M.5    Rieger-Christ, K.M.6
  • 62
    • 22044448094 scopus 로고    scopus 로고
    • Restoration of plakoglobin expression in bladder carcinoma cell lines suppresses cell migration and tumorigenic potential
    • Rieger-Christ K.M., Ng L., Hanley R.S., Durrani O., Ma H., Yee A.S., et al. Restoration of plakoglobin expression in bladder carcinoma cell lines suppresses cell migration and tumorigenic potential. Br J Cancer 92 (2005) 2153-2159
    • (2005) Br J Cancer , vol.92 , pp. 2153-2159
    • Rieger-Christ, K.M.1    Ng, L.2    Hanley, R.S.3    Durrani, O.4    Ma, H.5    Yee, A.S.6
  • 63
    • 0142088869 scopus 로고    scopus 로고
    • Histone deacetylase 1 represses the small gtpase rhob expression in human nonsmall lung carcinoma cell line
    • Wang S., Yan-Neale Y., Fischer D., Zeremski M., Cai R., Zhu J., et al. Histone deacetylase 1 represses the small gtpase rhob expression in human nonsmall lung carcinoma cell line. Oncogene 22 (2003) 6204-6213
    • (2003) Oncogene , vol.22 , pp. 6204-6213
    • Wang, S.1    Yan-Neale, Y.2    Fischer, D.3    Zeremski, M.4    Cai, R.5    Zhu, J.6
  • 65
    • 0142105414 scopus 로고    scopus 로고
    • Ezh2 is downstream of the prb-e2f pathway, essential for proliferation and amplified in cancer
    • Bracken A.P., Pasini D., Capra M., Prosperini E., Colli E., and Helin K. Ezh2 is downstream of the prb-e2f pathway, essential for proliferation and amplified in cancer. EMBO J 22 (2003) 5323-5335
    • (2003) EMBO J , vol.22 , pp. 5323-5335
    • Bracken, A.P.1    Pasini, D.2    Capra, M.3    Prosperini, E.4    Colli, E.5    Helin, K.6
  • 66
    • 0141816752 scopus 로고    scopus 로고
    • Ezh2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells
    • Kleer C.G., Cao Q., Varambally S., Shen R., Ota I., Tomlins S.A., et al. Ezh2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells. Proc Natl Acad Sci USA 100 (2003) 11606-11611
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11606-11611
    • Kleer, C.G.1    Cao, Q.2    Varambally, S.3    Shen, R.4    Ota, I.5    Tomlins, S.A.6
  • 67
    • 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., and Hung W.C. Histone deacetylase inhibitor up-regulates reck to inhibit mmp-2 activation and cancer cell invasion. Cancer Res 63 (2003) 3069-3072
    • (2003) Cancer Res , vol.63 , pp. 3069-3072
    • Liu, L.T.1    Chang, H.C.2    Chiang, L.C.3    Hung, W.C.4
  • 68
    • 18244367390 scopus 로고    scopus 로고
    • The membrane-anchored mmp inhibitor reck is a key regulator of extracellular matrix integrity and angiogenesis
    • Oh J., Takahashi R., Kondo S., Mizoguchi A., Adachi E., Sasahara R.M., et al. The membrane-anchored mmp inhibitor reck is a key regulator of extracellular matrix integrity and angiogenesis. Cell 107 (2001) 789-800
    • (2001) Cell , vol.107 , pp. 789-800
    • Oh, J.1    Takahashi, R.2    Kondo, S.3    Mizoguchi, A.4    Adachi, E.5    Sasahara, R.M.6
  • 69
    • 16444373352 scopus 로고    scopus 로고
    • Epigenetic up-regulation of c-c chemokine receptor 7 and c-x-c chemokine receptor 4 expression in melanoma cells
    • Mori T., Kim J., Yamano T., Takeuchi H., Huang S., Umetani N., et al. Epigenetic up-regulation of c-c chemokine receptor 7 and c-x-c chemokine receptor 4 expression in melanoma cells. Cancer Res 65 (2005) 1800-1807
    • (2005) Cancer Res , vol.65 , pp. 1800-1807
    • Mori, T.1    Kim, J.2    Yamano, T.3    Takeuchi, H.4    Huang, S.5    Umetani, N.6
  • 70
    • 0037081299 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-a(165) induces progression of melanoma brain metastases without induction of sprouting angiogenesis
    • Kusters B., Leenders W.P., Wesseling P., Smits D., Verrijp K., Ruiter D.J., et al. Vascular endothelial growth factor-a(165) induces progression of melanoma brain metastases without induction of sprouting angiogenesis. Cancer Res 62 (2002) 341-345
    • (2002) Cancer Res , vol.62 , pp. 341-345
    • Kusters, B.1    Leenders, W.P.2    Wesseling, P.3    Smits, D.4    Verrijp, K.5    Ruiter, D.J.6
  • 71
    • 0141816826 scopus 로고    scopus 로고
    • Differential effects of vascular endothelial growth factor a isoforms in a mouse brain metastasis model of human melanoma
    • Kusters B., de Waal R.M., Wesseling P., Verrijp K., Maass C., Heerschap A., et al. Differential effects of vascular endothelial growth factor a isoforms in a mouse brain metastasis model of human melanoma. Cancer Res 63 (2003) 5408-5413
    • (2003) Cancer Res , vol.63 , pp. 5408-5413
    • Kusters, B.1    de Waal, R.M.2    Wesseling, P.3    Verrijp, K.4    Maass, C.5    Heerschap, A.6
  • 72
    • 3242793175 scopus 로고    scopus 로고
    • Expression of histone deacetylase 8, a class i histone deacetylase, is restricted to cells showing smooth muscle differentiation in normal human tissues
    • Waltregny D., De Leval L., Glenisson W., Ly Tran S., North B.J., Bellahcene A., et al. Expression of histone deacetylase 8, a class i histone deacetylase, is restricted to cells showing smooth muscle differentiation in normal human tissues. Am J Pathol 165 (2004) 553-564
    • (2004) Am J Pathol , vol.165 , pp. 553-564
    • Waltregny, D.1    De Leval, L.2    Glenisson, W.3    Ly Tran, S.4    North, B.J.5    Bellahcene, A.6
  • 73
    • 21644485961 scopus 로고    scopus 로고
    • The expression of endothelial nitric-oxide synthase is controlled by a cell-specific histone code
    • Fish J.E., Matouk C.C., Rachlis A., Lin S., Tai S.C., D'Abreo C., et al. The expression of endothelial nitric-oxide synthase is controlled by a cell-specific histone code. J Biol Chem 280 (2005) 24824-24838
    • (2005) J Biol Chem , vol.280 , pp. 24824-24838
    • Fish, J.E.1    Matouk, C.C.2    Rachlis, A.3    Lin, S.4    Tai, S.C.5    D'Abreo, C.6
  • 74
    • 0036842460 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis
    • Rossig L., Li H., Fisslthaler B., Urbich C., Fleming I., Forstermann U., et al. Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis. Circ Res 91 (2002) 837-844
    • (2002) Circ Res , vol.91 , pp. 837-844
    • Rossig, L.1    Li, H.2    Fisslthaler, B.3    Urbich, C.4    Fleming, I.5    Forstermann, U.6
  • 75
    • 4444237596 scopus 로고    scopus 로고
    • Post-transcriptional regulation of endothelial nitric-oxide synthase by an overlapping antisense mRNA transcript
    • Robb G.B., Carson A.R., Tai S.C., Fish J.E., Singh S., Yamada T., et al. Post-transcriptional regulation of endothelial nitric-oxide synthase by an overlapping antisense mRNA transcript. J Biol Chem 279 (2004) 37982-37996
    • (2004) J Biol Chem , vol.279 , pp. 37982-37996
    • Robb, G.B.1    Carson, A.R.2    Tai, S.C.3    Fish, J.E.4    Singh, S.5    Yamada, T.6
  • 76
    • 0042355363 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterase activity, expression, and targeting in cells of the cardiovascular system
    • Maurice D.H., Palmer D., Tilley D.G., Dunkerley H.A., Netherton S.J., Raymond D.R., et al. Cyclic nucleotide phosphodiesterase activity, expression, and targeting in cells of the cardiovascular system. Mol Pharmacol 64 (2003) 533-546
    • (2003) Mol Pharmacol , vol.64 , pp. 533-546
    • Maurice, D.H.1    Palmer, D.2    Tilley, D.G.3    Dunkerley, H.A.4    Netherton, S.J.5    Raymond, D.R.6
  • 77
    • 23944467322 scopus 로고    scopus 로고
    • Vascular smooth muscle cell phenotype-dependent phosphodiesterase 4d short form expression: Role of differential histone acetylation on camp-regulated function
    • Tilley D., and Maurice D.H. Vascular smooth muscle cell phenotype-dependent phosphodiesterase 4d short form expression: Role of differential histone acetylation on camp-regulated function. Mol Pharmacol 68 (2005) 596-605
    • (2005) Mol Pharmacol , vol.68 , pp. 596-605
    • Tilley, D.1    Maurice, D.H.2
  • 78
    • 0035048449 scopus 로고    scopus 로고
    • Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes
    • Kim M.S., Kwon H.J., Lee Y.M., Baek J.H., Jang J.E., Lee S.W., et al. Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes. Nat Med 7 (2001) 437-443
    • (2001) Nat Med , vol.7 , pp. 437-443
    • Kim, M.S.1    Kwon, H.J.2    Lee, Y.M.3    Baek, J.H.4    Jang, J.E.5    Lee, S.W.6
  • 79
    • 0035887011 scopus 로고    scopus 로고
    • Fih-1: A novel protein that interacts with hif-1alpha and vhl to mediate repression of hif-1 transcriptional activity
    • Mahon P.C., Hirota K., and Semenza G.L. Fih-1: A novel protein that interacts with hif-1alpha and vhl to mediate repression of hif-1 transcriptional activity. Genes Dev 15 (2001) 2675-2686
    • (2001) Genes Dev , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 80
    • 4744368147 scopus 로고    scopus 로고
    • Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity
    • Kato H., Tamamizu-Kato S., and Shibasaki F. Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity. J Biol Chem 279 (2004) 41966-41974
    • (2004) J Biol Chem , vol.279 , pp. 41966-41974
    • Kato, H.1    Tamamizu-Kato, S.2    Shibasaki, F.3
  • 81
    • 0037137896 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor fk228 inhibits tumor angiogenesis
    • Kwon H.J., Kim M.S., Kim M.J., Nakajima H., and Kim K.W. Histone deacetylase inhibitor fk228 inhibits tumor angiogenesis. Int J Cancer 97 (2002) 290-296
    • (2002) Int J Cancer , vol.97 , pp. 290-296
    • Kwon, H.J.1    Kim, M.S.2    Kim, M.J.3    Nakajima, H.4    Kim, K.W.5
  • 82
    • 0042261694 scopus 로고    scopus 로고
    • Antitumor efficacy of fk228, a novel histone deacetylase inhibitor, depends on the effect on expression of angiogenesis factors
    • Sasakawa Y., Naoe Y., Noto T., Inoue T., Sasakawa T., Matsuo M., et al. Antitumor efficacy of fk228, a novel histone deacetylase inhibitor, depends on the effect on expression of angiogenesis factors. Biochem Pharmacol 66 (2003) 897-906
    • (2003) Biochem Pharmacol , vol.66 , pp. 897-906
    • Sasakawa, Y.1    Naoe, Y.2    Noto, T.3    Inoue, T.4    Sasakawa, T.5    Matsuo, M.6
  • 83
    • 1642312811 scopus 로고    scopus 로고
    • Modulation of angiogenesis-related protein synthesis by valproic acid
    • Zgouras D., Becker U., Loitsch S., and Stein J. Modulation of angiogenesis-related protein synthesis by valproic acid. Biochem Biophys Res Commun 316 (2004) 693-697
    • (2004) Biochem Biophys Res Commun , vol.316 , pp. 693-697
    • Zgouras, D.1    Becker, U.2    Loitsch, S.3    Stein, J.4
  • 84
    • 0037462884 scopus 로고    scopus 로고
    • Butyrate impairs intestinal tumor cell-induced angiogenesis by inhibiting hif-1alpha nuclear translocation
    • Zgouras D., Wachtershauser A., Frings D., and Stein J. Butyrate impairs intestinal tumor cell-induced angiogenesis by inhibiting hif-1alpha nuclear translocation. Biochem Biophys Res Commun 300 (2003) 832-838
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 832-838
    • Zgouras, D.1    Wachtershauser, A.2    Frings, D.3    Stein, J.4
  • 85
    • 85047699941 scopus 로고    scopus 로고
    • Histone deacetylases inhibitors as anti-angiogenic agents altering vascular endothelial growth factor signaling
    • Deroanne C.F., Bonjean K., Servotte S., Devy L., Colige A., Clausse N., et al. Histone deacetylases inhibitors as anti-angiogenic agents altering vascular endothelial growth factor signaling. Oncogene 21 (2002) 427-436
    • (2002) Oncogene , vol.21 , pp. 427-436
    • Deroanne, C.F.1    Bonjean, K.2    Servotte, S.3    Devy, L.4    Colige, A.5    Clausse, N.6
  • 86
    • 16644379041 scopus 로고    scopus 로고
    • Valproic acid and interferon-alpha synergistically inhibit neuroblastoma cell growth in vitro and in vivo
    • Michaelis M., Suhan T., Cinatl J., Driever P.H., and Cinatl Jr. J. Valproic acid and interferon-alpha synergistically inhibit neuroblastoma cell growth in vitro and in vivo. Int J Oncol 25 (2004) 1795-1799
    • (2004) Int J Oncol , vol.25 , pp. 1795-1799
    • Michaelis, M.1    Suhan, T.2    Cinatl, J.3    Driever, P.H.4    Cinatl Jr., J.5
  • 87
    • 4644364508 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor nvp-laq824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyrosine kinase inhibitor ptk787/zk222584
    • Qian D.Z., Wang X., Kachhap S.K., Kato Y., Wei Y., Zhang L., et al. The histone deacetylase inhibitor nvp-laq824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyrosine kinase inhibitor ptk787/zk222584. Cancer Res 64 (2004) 6626-6634
    • (2004) Cancer Res , vol.64 , pp. 6626-6634
    • Qian, D.Z.1    Wang, X.2    Kachhap, S.K.3    Kato, Y.4    Wei, Y.5    Zhang, L.6
  • 88
    • 0036947771 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors such as sodium butyrate and trichostatin a inhibit vascular endothelial growth factor (vegf) secretion from human glioblastoma cells
    • Sawa H., Murakami H., Ohshima Y., Murakami M., Yamazaki I., Tamura Y., et al. Histone deacetylase inhibitors such as sodium butyrate and trichostatin a inhibit vascular endothelial growth factor (vegf) secretion from human glioblastoma cells. Brain Tumor Pathol 19 (2002) 77-81
    • (2002) Brain Tumor Pathol , vol.19 , pp. 77-81
    • Sawa, H.1    Murakami, H.2    Ohshima, Y.3    Murakami, M.4    Yamazaki, I.5    Tamura, Y.6
  • 89
    • 0035866341 scopus 로고    scopus 로고
    • Combination of phenylbutyrate and 13-cis retinoic acid inhibits prostate tumor growth and angiogenesis
    • Pili R., Kruszewski M.P., Hager B.W., Lantz J., and Carducci M.A. Combination of phenylbutyrate and 13-cis retinoic acid inhibits prostate tumor growth and angiogenesis. Cancer Res 61 (2001) 1477-1485
    • (2001) Cancer Res , vol.61 , pp. 1477-1485
    • Pili, R.1    Kruszewski, M.P.2    Hager, B.W.3    Lantz, J.4    Carducci, M.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.