메뉴 건너뛰기




Volumn 69, Issue 4, 2005, Pages 603-616

Marker genes to predict sensitivity to FK228, a histone deacetylase inhibitor

Author keywords

Caspase 9; FK228; FR901228; GeneChip; Histone deacetylase inhibitor; MKP 1

Indexed keywords

CASPASE 9; CYCLIN A; CYCLIN DEPENDENT KINASE INHIBITOR 1; FR 901228; HISTONE DEACETYLASE INHIBITOR; HISTONE H1; INTERLEUKIN 8; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1;

EID: 12744251611     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2004.11.008     Document Type: Article
Times cited : (51)

References (44)
  • 1
    • 0028258610 scopus 로고
    • FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum no. 968. I. Taxonomy, fermentation, isolation, physico-chemical and biological properties, and antitumor activity
    • H. Ueda, H. Nakajima, Y. Hori, T. Fujita, M. Nishimura, and T. Goto FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum no. 968. I. Taxonomy, fermentation, isolation, physico-chemical and biological properties, and antitumor activity J Antibiot (Tokyo) 47 1994 301 310
    • (1994) J Antibiot (Tokyo) , vol.47 , pp. 301-310
    • Ueda, H.1    Nakajima, H.2    Hori, Y.3    Fujita, T.4    Nishimura, M.5    Goto, T.6
  • 2
    • 0028299638 scopus 로고
    • FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum no. 968. II. Structure determination
    • N. Shigematsu, H. Ueda, S. Takase, H. Tanaka, K. Yamamoto, and T. Tada FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum no. 968. II. Structure determination J Antibiot (Tokyo) 47 1994 311 314
    • (1994) J Antibiot (Tokyo) , vol.47 , pp. 311-314
    • Shigematsu, N.1    Ueda, H.2    Takase, S.3    Tanaka, H.4    Yamamoto, K.5    Tada, T.6
  • 3
    • 0028267278 scopus 로고
    • FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum no. 968. III. Antitumor activities on experimental tumors in mice
    • H. Ueda, T. Manda, S. Matsumoto, S. Mukumoto, F. Nishigaki, and I. Kawamura FR901228, a novel antitumor bicyclic depsipeptide produced by Chromobacterium violaceum no. 968. III. Antitumor activities on experimental tumors in mice J Antibiot (Tokyo) 47 1994 315 323
    • (1994) J Antibiot (Tokyo) , vol.47 , pp. 315-323
    • Ueda, H.1    Manda, T.2    Matsumoto, S.3    Mukumoto, S.4    Nishigaki, F.5    Kawamura, I.6
  • 4
    • 0031768386 scopus 로고    scopus 로고
    • Effects of a novel antitumor depsipeptide, FR901228, on human breast cancer cells
    • G. Rajgolikar, K.K. Chan, and H.C. Wang Effects of a novel antitumor depsipeptide, FR901228, on human breast cancer cells Breast Cancer Res Treat 51 1998 29 38
    • (1998) Breast Cancer Res Treat , vol.51 , pp. 29-38
    • Rajgolikar, G.1    Chan, K.K.2    Wang, H.C.3
  • 5
    • 0344431240 scopus 로고    scopus 로고
    • FR901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor
    • H. Nakajima, Y.B. Kim, H. Terano, M. Yoshida, and S. Horinouchi 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
  • 6
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • M. Grunstein Histone acetylation in chromatin structure and transcription Nature 389 1997 349 352
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 7
    • 0027525056 scopus 로고
    • Decoding the nucleosome
    • B.M. Turner Decoding the nucleosome Cell 75 1993 5 8
    • (1993) Cell , vol.75 , pp. 5-8
    • Turner, B.M.1
  • 8
    • 0036775301 scopus 로고    scopus 로고
    • Effects of FK228, a novel histone deacetylase inhibitor, on human lymphoma U-937 cells in vitro and in vivo
    • Y. Sasakawa, Y. Naoe, T. Inoue, T. Sasakawa, M. Matsuo, and T. Manda Effects of FK228, a novel histone deacetylase inhibitor, on human lymphoma U-937 cells in vitro and in vivo Biochem Pharmacol 64 2002 1079 1090
    • (2002) Biochem Pharmacol , vol.64 , pp. 1079-1090
    • Sasakawa, Y.1    Naoe, Y.2    Inoue, T.3    Sasakawa, T.4    Matsuo, M.5    Manda, T.6
  • 9
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin a
    • M. Yoshida, M. Kijima, M. Akita, and T. Beppu Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A J Biol Chem 265 1990 17174 17179
    • (1990) J Biol Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 10
    • 0033551152 scopus 로고    scopus 로고
    • A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors
    • A. Saito, T. Yamashita, Y. Mariko, Y. Nosaka, K. Tsuchiya, and T. Ando 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
  • 11
    • 0032539890 scopus 로고    scopus 로고
    • A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases
    • V.M. Richon, S. Emiliani, E. Verdin, Y. Webb, R. Breslow, and R.A. Rifkind A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases Proc Natl Acad Sci USA 95 1998 3003 3007
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3003-3007
    • Richon, V.M.1    Emiliani, S.2    Verdin, E.3    Webb, Y.4    Breslow, R.5    Rifkind, R.A.6
  • 12
    • 0029693220 scopus 로고    scopus 로고
    • The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation
    • C. Van Lint, S. Emiliani, and E. Verdin 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
  • 13
    • 0038060250 scopus 로고    scopus 로고
    • Effects of FK228, a novel histone deacetylase inhibitor, on tumor growth and expression of p21 and c-myc genes in vivo
    • Y. Sasakawa, Y. Naoe, T. Inoue, T. Sasakawa, M. Matsuo, and T. Manda Effects of FK228, a novel histone deacetylase inhibitor, on tumor growth and expression of p21 and c-myc genes in vivo Cancer Lett 195 2003 161 168
    • (2003) Cancer Lett , vol.195 , pp. 161-168
    • Sasakawa, Y.1    Naoe, Y.2    Inoue, T.3    Sasakawa, T.4    Matsuo, M.5    Manda, T.6
  • 14
    • 0032879920 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors are the potent inducer/enhancer of differentiation in acute myeloid leukemia: A new approach to anti-leukemia therapy
    • H. Kosugi, M. Towatari, S. Hatano, K. Kitamura, H. Kiyoi, and T. Kinoshita Histone deacetylase inhibitors are the potent inducer/enhancer of differentiation in acute myeloid leukemia: a new approach to anti-leukemia therapy Leukemia 13 1999 1316 1324
    • (1999) Leukemia , vol.13 , pp. 1316-1324
    • Kosugi, H.1    Towatari, M.2    Hatano, S.3    Kitamura, K.4    Kiyoi, H.5    Kinoshita, T.6
  • 15
    • 0026059424 scopus 로고
    • P52(PAI-1) and actin expression in butyrate-induced flat revertants of v-ras-transformed rat kidney cells
    • P.J. Higgins, and M.P. Ryan p52(PAI-1) and actin expression in butyrate-induced flat revertants of v-ras-transformed rat kidney cells Biochem J 279 1991 883 890
    • (1991) Biochem J , vol.279 , pp. 883-890
    • Higgins, P.J.1    Ryan, M.P.2
  • 16
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • V.M. Richon, T.W. Sandhoff, R.A. Rifkind, and P.A. Marks Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation Proc Natl Acad Sci USA 97 2000 10014 10019
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 17
    • 0034802887 scopus 로고    scopus 로고
    • The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression
    • B.P. Ashburner, S.D. Westerheide, and A.S. Baldwin Jr. The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression Mol Cell Biol 21 2001 7065 7077
    • (2001) Mol Cell Biol , vol.21 , pp. 7065-7077
    • Ashburner, B.P.1    Westerheide, S.D.2    Baldwin Jr., A.S.3
  • 18
    • 0036681989 scopus 로고    scopus 로고
    • Sulfonamide anilides, a novel class of histone deacetylase inhibitors, are antiproliferative against human tumors
    • M. Fournel, M.C. Trachy-Bourget, P.T. Yan, A. Kalita, C. Bonfils, and C. Beaulieu Sulfonamide anilides, a novel class of histone deacetylase inhibitors, are antiproliferative against human tumors Cancer Res 62 2002 4325 4330
    • (2002) Cancer Res , vol.62 , pp. 4325-4330
    • Fournel, M.1    Trachy-Bourget, M.C.2    Yan, P.T.3    Kalita, A.4    Bonfils, C.5    Beaulieu, C.6
  • 19
    • 0033520944 scopus 로고    scopus 로고
    • Histone deacetylase inhibition selectively alters the activity and expression of cell cycle proteins leading to specific chromatin acetylation and antiproliferative effects
    • L.C. Sambucetti, D.D. Fischer, S. Zabludoff, P.O. Kwon, H. Chamberlin, and N. Trogani Histone deacetylase inhibition selectively alters the activity and expression of cell cycle proteins leading to specific chromatin acetylation and antiproliferative effects J Biol Chem 274 1999 34940 34947
    • (1999) J Biol Chem , vol.274 , pp. 34940-34947
    • Sambucetti, L.C.1    Fischer, D.D.2    Zabludoff, S.3    Kwon, P.O.4    Chamberlin, H.5    Trogani, N.6
  • 20
    • 0035691356 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce apoptosis in peripheral blood lymphocytes along with histone H4 acetylation and the expression of the linker histone variant, H1 degrees
    • T.G. Sourlingas, D.S. Tsapali, A.D. Kaldis, and E. Sekeri-Pataryas Histone deacetylase inhibitors induce apoptosis in peripheral blood lymphocytes along with histone H4 acetylation and the expression of the linker histone variant, H1 degrees Eur J Cell Biol 80 2001 726 732
    • (2001) Eur J Cell Biol , vol.80 , pp. 726-732
    • Sourlingas, T.G.1    Tsapali, D.S.2    Kaldis, A.D.3    Sekeri-Pataryas, E.4
  • 21
    • 0038281349 scopus 로고    scopus 로고
    • JunB gene expression is inactivated by methylation in chronic myeloid leukemia
    • M.Y. Yang, T.C. Liu, J.G. Chang, P.M. Lin, and S.F. Lin JunB gene expression is inactivated by methylation in chronic myeloid leukemia Blood 101 2003 3205 3211
    • (2003) Blood , vol.101 , pp. 3205-3211
    • Yang, M.Y.1    Liu, T.C.2    Chang, J.G.3    Lin, P.M.4    Lin, S.F.5
  • 22
    • 0142165059 scopus 로고    scopus 로고
    • P38 MAP kinase activation mediates gamma-globin gene induction in erythroid progenitors
    • B.S. Pace, X.H. Qian, J. Sangerman, S.F. Ofori-Acquah, B.S. Baliga, and J. Han p38 MAP kinase activation mediates gamma-globin gene induction in erythroid progenitors Exp Hematol 31 2003 1089 1096
    • (2003) Exp Hematol , vol.31 , pp. 1089-1096
    • Pace, B.S.1    Qian, X.H.2    Sangerman, J.3    Ofori-Acquah, S.F.4    Baliga, B.S.5    Han, J.6
  • 23
    • 0242493856 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib interacts synergistically with histone deacetylase inhibitors to induce apoptosis in Bcr/Abl+ cells sensitive and resistant to STI571
    • C. Yu, M. Rahmani, D. Conrad, M. Subler, P. Dent, and S. Grant The proteasome inhibitor bortezomib interacts synergistically with histone deacetylase inhibitors to induce apoptosis in Bcr/Abl+ cells sensitive and resistant to STI571 Blood 102 2003 3765 3774
    • (2003) Blood , vol.102 , pp. 3765-3774
    • Yu, C.1    Rahmani, M.2    Conrad, D.3    Subler, M.4    Dent, P.5    Grant, S.6
  • 24
    • 0030780804 scopus 로고    scopus 로고
    • Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene
    • D.D. Yang, C.Y. Kuan, A.J. Whitmarsh, M. Rincon, T.S. Zheng, and R.J. Davis Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene Nature 389 1997 865 870
    • (1997) Nature , vol.389 , pp. 865-870
    • Yang, D.D.1    Kuan, C.Y.2    Whitmarsh, A.J.3    Rincon, M.4    Zheng, T.S.5    Davis, R.J.6
  • 25
    • 0029923193 scopus 로고    scopus 로고
    • Identification of mi togen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase
    • M.M. McLaughlin, S. Kumar, P.C. McDonnell, S. Van Horn, J.C. Lee, and G.P. Livi Identification of mi togen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase J Biol Chem 271 1996 8488 8492
    • (1996) J Biol Chem , vol.271 , pp. 8488-8492
    • McLaughlin, M.M.1    Kumar, S.2    McDonnell, P.C.3    Van Horn, S.4    Lee, J.C.5    Livi, G.P.6
  • 26
    • 0038677606 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity increases chromosomal instability by the aberrant regulation of mitotic checkpoint activation
    • H.J. Shin, K.H. Baek, A.H. Jeon, S.J. Kim, K.L. Jang, and Y.C. Sung Inhibition of histone deacetylase activity increases chromosomal instability by the aberrant regulation of mitotic checkpoint activation Oncogene 22 2003 3853 3858
    • (2003) Oncogene , vol.22 , pp. 3853-3858
    • Shin, H.J.1    Baek, K.H.2    Jeon, A.H.3    Kim, S.J.4    Jang, K.L.5    Sung, Y.C.6
  • 27
    • 0023932697 scopus 로고
    • Responsiveness of human gastric tumors implanted in nude mice to clinically equivalent doses of various antitumor agents
    • M. Inaba, T. Tashiro, T. Kobayashi, Y. Sakurai, K. Maruo, and Y. Ohnishi Responsiveness of human gastric tumors implanted in nude mice to clinically equivalent doses of various antitumor agents Jpn J Cancer Res 79 1988 517 522
    • (1988) Jpn J Cancer Res , vol.79 , pp. 517-522
    • Inaba, M.1    Tashiro, T.2    Kobayashi, T.3    Sakurai, Y.4    Maruo, K.5    Ohnishi, Y.6
  • 28
    • 0024363349 scopus 로고
    • Responsiveness of human lung cancer/nude mouse to antitumor agents in a model using clinically equivalent doses
    • T. Tashiro, M. Inaba, T. Kobayashi, Y. Sakurai, K. Maruo, and Y. Ohnishi Responsiveness of human lung cancer/nude mouse to antitumor agents in a model using clinically equivalent doses Cancer Chemother Pharmacol 24 1989 187 192
    • (1989) Cancer Chemother Pharmacol , vol.24 , pp. 187-192
    • Tashiro, T.1    Inaba, M.2    Kobayashi, T.3    Sakurai, Y.4    Maruo, K.5    Ohnishi, Y.6
  • 30
    • 0034674306 scopus 로고    scopus 로고
    • Transduction of Apaf-1 or caspase-9 induces apoptosis in A-172 cells that are resistant to p53-mediated apoptosis
    • N. Shinoura, S. Sakurai, A. Asai, T. Kirino, and H. Hamada Transduction of Apaf-1 or caspase-9 induces apoptosis in A-172 cells that are resistant to p53-mediated apoptosis Biochem Biophys Res Commun 272 2000 667 673
    • (2000) Biochem Biophys Res Commun , vol.272 , pp. 667-673
    • Shinoura, N.1    Sakurai, S.2    Asai, A.3    Kirino, T.4    Hamada, H.5
  • 31
    • 0035210529 scopus 로고    scopus 로고
    • Cyclophosphamide induces caspase 9-dependent apoptosis in 9L tumor cells
    • P.S. Schwartz, and D.J. Waxman Cyclophosphamide induces caspase 9-dependent apoptosis in 9L tumor cells Mol Pharmacol 60 2001 1268 1279
    • (2001) Mol Pharmacol , vol.60 , pp. 1268-1279
    • Schwartz, P.S.1    Waxman, D.J.2
  • 32
    • 0037205401 scopus 로고    scopus 로고
    • Activation of caspase-9 is required for UV-induced apoptosis of human keratinocytes
    • L.A. Sitailo, S.S. Tibudan, and M.F. Denning Activation of caspase-9 is required for UV-induced apoptosis of human keratinocytes J Biol Chem 277 2002 19346 19352
    • (2002) J Biol Chem , vol.277 , pp. 19346-19352
    • Sitailo, L.A.1    Tibudan, S.S.2    Denning, M.F.3
  • 33
    • 0032493870 scopus 로고    scopus 로고
    • Differential requirement for caspase 9 in apoptotic pathways in vivo
    • R. Hakem, A. Hakem, G.S. Duncan, J.T. Henderson, M. Woo, and M.S. Soengas Differential requirement for caspase 9 in apoptotic pathways in vivo Cell 94 1998 339 352
    • (1998) Cell , vol.94 , pp. 339-352
    • Hakem, R.1    Hakem, A.2    Duncan, G.S.3    Henderson, J.T.4    Woo, M.5    Soengas, M.S.6
  • 34
    • 0038485588 scopus 로고    scopus 로고
    • Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA)
    • C. Henderson, M. Mizzau, G. Paroni, R. Maestro, C. Schneider, and C. Brancolini Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA) J Biol Chem 278 2003 12579 12589
    • (2003) J Biol Chem , vol.278 , pp. 12579-12589
    • Henderson, C.1    Mizzau, M.2    Paroni, G.3    Maestro, R.4    Schneider, C.5    Brancolini, C.6
  • 35
    • 0033970533 scopus 로고    scopus 로고
    • Dual specificity phosphatases: A gene family for control of MAP kinase function
    • M. Camps, A. Nichols, and S. Arkinstall Dual specificity phosphatases: a gene family for control of MAP kinase function FASEB J 14 2000 6 16
    • (2000) FASEB J , vol.14 , pp. 6-16
    • Camps, M.1    Nichols, A.2    Arkinstall, S.3
  • 36
    • 0027358722 scopus 로고
    • MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo
    • H. Sun, C.H. Charles, L.F. Lau, and N.K. Tonks MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo Cell 75 1993 487 493
    • (1993) Cell , vol.75 , pp. 487-493
    • Sun, H.1    Charles, C.H.2    Lau, L.F.3    Tonks, N.K.4
  • 37
    • 0035168692 scopus 로고    scopus 로고
    • Transcriptional induction of MKP-1 in response to stress is associated with histone H3 phosphorylation-acetylation
    • J. Li, M. Gorospe, D. Hutter, J. Barnes, S.M. Keyse, and Y. Liu Transcriptional induction of MKP-1 in response to stress is associated with histone H3 phosphorylation-acetylation Mol Cell Biol 21 2001 8213 8224
    • (2001) Mol Cell Biol , vol.21 , pp. 8213-8224
    • Li, J.1    Gorospe, M.2    Hutter, D.3    Barnes, J.4    Keyse, S.M.5    Liu, Y.6
  • 38
    • 0029852580 scopus 로고    scopus 로고
    • Use of a cDNA microarray to analyse gene expression patterns in human cancer
    • J. DeRisi, L. Penland, P.O. Brown, M.L. Bittner, P.S. Meltzer, and M. Ray Use of a cDNA microarray to analyse gene expression patterns in human cancer Nat Genet 14 1996 457 460
    • (1996) Nat Genet , vol.14 , pp. 457-460
    • Derisi, J.1    Penland, L.2    Brown, P.O.3    Bittner, M.L.4    Meltzer, P.S.5    Ray, M.6
  • 40
    • 0028806048 scopus 로고
    • Quantitative monitoring of gene expression patterns with a complementary DNA microarray
    • M. Schena, D. Shalon, R.W. Davis, and P.O. Brown Quantitative monitoring of gene expression patterns with a complementary DNA microarray Science 270 1995 467 470
    • (1995) Science , vol.270 , pp. 467-470
    • Schena, M.1    Shalon, D.2    Davis, R.W.3    Brown, P.O.4
  • 41
    • 0035420014 scopus 로고    scopus 로고
    • Prediction of sensitivity of esophageal tumors to adjuvant chemotherapy by cDNA microarray analysis of gene-expression profiles
    • C. Kihara, T. Tsunoda, T. Tanaka, H. Yamana, Y. Furukawa, and K. Ono Prediction of sensitivity of esophageal tumors to adjuvant chemotherapy by cDNA microarray analysis of gene-expression profiles Cancer Res 61 2001 6474 6479
    • (2001) Cancer Res , vol.61 , pp. 6474-6479
    • Kihara, C.1    Tsunoda, T.2    Tanaka, T.3    Yamana, H.4    Furukawa, Y.5    Ono, K.6
  • 42
    • 0033569406 scopus 로고    scopus 로고
    • Molecular classification of cancer: Class discovery and class prediction by gene expression monitoring
    • T.R. Golub, D.K. Slonim, P. Tamayo, C. Huard, M. Gaasenbeek, and J.P. Mesirov Molecular classification of cancer: class discovery and class prediction by gene expression monitoring Science 286 1999 531 537
    • (1999) Science , vol.286 , pp. 531-537
    • Golub, T.R.1    Slonim, D.K.2    Tamayo, P.3    Huard, C.4    Gaasenbeek, M.5    Mesirov, J.P.6
  • 43
    • 0034598746 scopus 로고    scopus 로고
    • Distinct types of diffuse large B-cell lymphoma identified by gene expression profiling
    • A.A. Alizadeh, M.B. Eisen, R.E. Davis, C. Ma, I.S. Lossos, and A. Rosenwald Distinct types of diffuse large B-cell lymphoma identified by gene expression profiling Nature 403 2000 503 511
    • (2000) Nature , vol.403 , pp. 503-511
    • Alizadeh, A.A.1    Eisen, M.B.2    Davis, R.E.3    Ma, C.4    Lossos, I.S.5    Rosenwald, A.6
  • 44


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.