메뉴 건너뛰기




Volumn 96, Issue 6, 2005, Pages 1137-1148

Histone modifying enzymes and cancer: Going beyond histones

Author keywords

Aurora kinase; Cancer; Chromatin; Histone acetyltransferase (HAT) deacetylase (HDAC); Histone methyltransferase (HMT)

Indexed keywords

AURORA KINASE; CENTROMERE PROTEIN E; CHAPERONE; CYTOSKELETON PROTEIN; HIGH MOBILITY GROUP PROTEIN; HISTONE; INTERFERON REGULATORY FACTOR 1; PHOSPHOTRANSFERASE; RIBONUCLEOPROTEIN; STAT PROTEIN; TRANSCRIPTION FACTOR; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG;

EID: 27944501617     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcb.20615     Document Type: Review
Times cited : (133)

References (54)
  • 1
    • 0035252654 scopus 로고    scopus 로고
    • Chromosomal passengers and the (aurora) ABCs of mitosis
    • Adams RR, Carmena M, Earnshaw WC. 2001. Chromosomal passengers and the (aurora) ABCs of mitosis. Trends Cell Biol 11:49-54.
    • (2001) Trends Cell Biol , vol.11 , pp. 49-54
    • Adams, R.R.1    Carmena, M.2    Earnshaw, W.C.3
  • 2
    • 0036849262 scopus 로고    scopus 로고
    • Epigenetic consequences of nucleosome dynamics
    • Ahmad K, Henikoff S. 2002. Epigenetic consequences of nucleosome dynamics. Cell 111:281-284.
    • (2002) Cell , vol.111 , pp. 281-284
    • Ahmad, K.1    Henikoff, S.2
  • 3
    • 11844276610 scopus 로고    scopus 로고
    • Sterile 20 kinase phosphorylates histone H2B at serine 10 during hydrogen peroxide-induced apoptosis in S. cerevisiae
    • Ahn SH, Cheung WL, Hsu JY, Diaz RL, Smith MM, Allis CD. 2005. Sterile 20 kinase phosphorylates histone H2B at serine 10 during hydrogen peroxide-induced apoptosis in S. cerevisiae. Cell 120:25-36.
    • (2005) Cell , vol.120 , pp. 25-36
    • Ahn, S.H.1    Cheung, W.L.2    Hsu, J.Y.3    Diaz, R.L.4    Smith, M.M.5    Allis, C.D.6
  • 5
    • 0018903045 scopus 로고
    • Proteolytic processing of histone H3 in chromatin: A physiologically regulated event in Tetrahymena micronuclei
    • Allis CD, Bowen JK, Abraham GN, Glover CV, Gorovsky MA. 1980. Proteolytic processing of histone H3 in chromatin: A physiologically regulated event in Tetrahymena micronuclei. Cell 20:55-64.
    • (1980) Cell , vol.20 , pp. 55-64
    • Allis, C.D.1    Bowen, J.K.2    Abraham, G.N.3    Glover, C.V.4    Gorovsky, M.A.5
  • 7
    • 2442706035 scopus 로고    scopus 로고
    • H2AX may function as an anchor to hold broken chromosomal DNA ends in close proximity
    • Bassing CH, Alt FW. 2004. H2AX may function as an anchor to hold broken chromosomal DNA ends in close proximity. Cell Cycle 3:149-153.
    • (2004) Cell Cycle , vol.3 , pp. 149-153
    • Bassing, C.H.1    Alt, F.W.2
  • 8
    • 4944255743 scopus 로고    scopus 로고
    • Post-translational modification of p53 in tumorigenesis
    • Bode AM, Dong Z. 2004. Post-translational modification of p53 in tumorigenesis. Nat Rev Cancer 4:793-805.
    • (2004) Nat Rev Cancer , vol.4 , pp. 793-805
    • Bode, A.M.1    Dong, Z.2
  • 9
    • 0029079892 scopus 로고
    • Phosphorylation of transcription factors and control of the cell cycle
    • Boulikas T. 1995. Phosphorylation of transcription factors and control of the cell cycle. Crit Rev Eukaryot Gene Expr 5:1-77.
    • (1995) Crit Rev Eukaryot Gene Expr , vol.5 , pp. 1-77
    • Boulikas, T.1
  • 10
    • 10944230851 scopus 로고    scopus 로고
    • Around the world of DNA damage INO80 days
    • Cairns BR. 2004. Around the world of DNA damage INO80 days. Cell 119:733-735.
    • (2004) Cell , vol.119 , pp. 733-735
    • Cairns, B.R.1
  • 11
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • Cheung P, Tanner KG, Cheung WL, Sassone-Corsi P, Denu JM, Allis CD. 2000. Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation [in process citation]. Mol Cell 5:905-915.
    • (2000) Mol Cell , vol.5 , pp. 905-915
    • Cheung, P.1    Tanner, K.G.2    Cheung, W.L.3    Sassone-Corsi, P.4    Denu, J.M.5    Allis, C.D.6
  • 14
    • 13844252061 scopus 로고    scopus 로고
    • The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment
    • Dai J, Sultan S, Taylor SS, Higgins JM. 2005. The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment. Genes Dev 19:472-488.
    • (2005) Genes Dev , vol.19 , pp. 472-488
    • Dai, J.1    Sultan, S.2    Taylor, S.S.3    Higgins, J.M.4
  • 15
    • 18344372831 scopus 로고    scopus 로고
    • Cyclins andcdks in development and cancer: A perspective
    • Deshpande A, Sicinski P, Hinds PW. 2005. Cyclins andcdks in development and cancer: A perspective. Oncogene 24:2909-2915.
    • (2005) Oncogene , vol.24 , pp. 2909-2915
    • Deshpande, A.1    Sicinski, P.2    Hinds, P.W.3
  • 16
  • 20
    • 17444368701 scopus 로고    scopus 로고
    • Histone modifying and chromatin remodelling enzymes in cancer and dysplastic syndromes
    • Gibbons RJ. 2005. Histone modifying and chromatin remodelling enzymes in cancer and dysplastic syndromes. Hum Mol Genet 14 Spec No 1:R85-92.
    • (2005) Hum Mol Genet , vol.14 , Issue.1 SPEC. NO.
    • Gibbons, R.J.1
  • 21
    • 9644270520 scopus 로고    scopus 로고
    • Chromatin modifiers and carcinogenesis
    • Gregory RI, Shiekhattar R. 2004. Chromatin modifiers and carcinogenesis. Trends Cell Biol 14:695-702.
    • (2004) Trends Cell Biol , vol.14 , pp. 695-702
    • Gregory, R.I.1    Shiekhattar, R.2
  • 22
    • 1642358490 scopus 로고    scopus 로고
    • Linking the epigenetic 'language' of covalent histone modifications to cancer
    • Hake SB, Xiao A, Allis CD. 2004. Linking the epigenetic 'language' of covalent histone modifications to cancer. Br J Cancer 90:761-769.
    • (2004) Br J Cancer , vol.90 , pp. 761-769
    • Hake, S.B.1    Xiao, A.2    Allis, C.D.3
  • 24
    • 10344260184 scopus 로고    scopus 로고
    • CpG island methylator phenotype in cancer
    • Issa JP. 2004. CpG island methylator phenotype in cancer. Nat Rev Cancer 4:988-993.
    • (2004) Nat Rev Cancer , vol.4 , pp. 988-993
    • Issa, J.P.1
  • 25
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. 2001. Translating the histone code. Science 293:1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 26
    • 0031984480 scopus 로고    scopus 로고
    • SET domain proteins modulate chromatin domains in eu- and heterochromatin
    • Jenuwein T, Laible G, Dorn R, Reuter G. 1998. SET domain proteins modulate chromatin domains in eu- and heterochromatin. Cell Mol Life Sci 54:80-93.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 80-93
    • Jenuwein, T.1    Laible, G.2    Dorn, R.3    Reuter, G.4
  • 27
    • 0142123293 scopus 로고    scopus 로고
    • The Drosophila Ste20 family kinase dMST functions as a tumor suppressor by restricting cell proliferation and promoting apoptosis
    • Jia J, Zhang W, Wang B, Trinko R, Jiang J. 2003. The Drosophila Ste20 family kinase dMST functions as a tumor suppressor by restricting cell proliferation and promoting apoptosis. Genes Dev 17:2514-2519.
    • (2003) Genes Dev , vol.17 , pp. 2514-2519
    • Jia, J.1    Zhang, W.2    Wang, B.3    Trinko, R.4    Jiang, J.5
  • 28
    • 0038341158 scopus 로고    scopus 로고
    • The Aurora kinases: Role in cell transformation and tumorigenesis
    • Katayama H, Brinkley WR, Sen S. 2003. The Aurora kinases: Role in cell transformation and tumorigenesis. Cancer Metastasis Rev 22:451-464.
    • (2003) Cancer Metastasis Rev , vol.22 , pp. 451-464
    • Katayama, H.1    Brinkley, W.R.2    Sen, S.3
  • 29
    • 1542577669 scopus 로고    scopus 로고
    • Histone methyltransferases in tumor suppression
    • Kim KC, Huang S. 2003. Histone methyltransferases in tumor suppression. Cancer Biol Ther 2:491-499.
    • (2003) Cancer Biol Ther , vol.2 , pp. 491-499
    • Kim, K.C.1    Huang, S.2
  • 30
    • 1942534675 scopus 로고    scopus 로고
    • Gene-specific modulation of TAF10 function by SET9-mediated methylation
    • Kouskouti A, Scheer E, Staub A, Tora L, Talianidis I. 2004. Gene-specific modulation of TAF10 function by SET9-mediated methylation. Mol Cell 14:175-182.
    • (2004) Mol Cell , vol.14 , pp. 175-182
    • Kouskouti, A.1    Scheer, E.2    Staub, A.3    Tora, L.4    Talianidis, I.5
  • 31
    • 0033000990 scopus 로고    scopus 로고
    • Histone acetylases and deacetylases in cell proliferation
    • Kouzarides T. 1999. Histone acetylases and deacetylases in cell proliferation. Curr Opin Genet Dev 9:40-48.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 40-48
    • Kouzarides, T.1
  • 32
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • Kouzarides T. 2002. Histone methylation in transcriptional control. Curr Opin Genet Dev 12:198-209.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 33
    • 4744344066 scopus 로고    scopus 로고
    • Epigenetics and cancer
    • Lund AH, van Lohuizen M. 2004. Epigenetics and cancer. Genes Dev 18:2315-2335.
    • (2004) Genes Dev , vol.18 , pp. 2315-2335
    • Lund, A.H.1    Van Lohuizen, M.2
  • 34
    • 0035854372 scopus 로고    scopus 로고
    • State of the arg: Protein methylation at arginine comes of age
    • McBride AE, Silver PA. 2001. State of the arg: Protein methylation at arginine comes of age. Cell 106:5-8.
    • (2001) Cell , vol.106 , pp. 5-8
    • McBride, A.E.1    Silver, P.A.2
  • 35
    • 0344022572 scopus 로고    scopus 로고
    • Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity
    • Ng HH, Robert F, Young RA, Struhl K. 2003. Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. Mol Cell 11:709-719.
    • (2003) Mol Cell , vol.11 , pp. 709-719
    • Ng, H.H.1    Robert, F.2    Young, R.A.3    Struhl, K.4
  • 36
    • 0035839110 scopus 로고    scopus 로고
    • Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries
    • Noma K, Allis CD, Grewal SI. 2001. Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries. Science 293:1150-1155.
    • (2001) Science , vol.293 , pp. 1150-1155
    • Noma, K.1    Allis, C.D.2    Grewal, S.I.3
  • 37
    • 1642326716 scopus 로고    scopus 로고
    • Phosphorylation of histone H3: A balancing act between chromosome condensation and transcriptional activation
    • Nowak SJ, Corces VG. 2004. Phosphorylation of histone H3: A balancing act between chromosome condensation and transcriptional activation. Trends Genet 20:214-220.
    • (2004) Trends Genet , vol.20 , pp. 214-220
    • Nowak, S.J.1    Corces, V.G.2
  • 40
    • 13444267442 scopus 로고    scopus 로고
    • Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation
    • Pray-Grant MG, Daniel JA, Schieltz D, Yates JR III, Grant PA. 2005. Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation. Nature 433:434-438.
    • (2005) Nature , vol.433 , pp. 434-438
    • Pray-Grant, M.G.1    Daniel, J.A.2    Schieltz, D.3    Yates III, J.R.4    Grant, P.A.5
  • 45
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. 2000. The language of covalent histone modifications. Nature 403:41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 46
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun ZW, Allis CD. 2002. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418:104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 47
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner BM. 2002. Cellular memory and the histone code. Cell 111:285-291.
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 48
    • 0141616617 scopus 로고    scopus 로고
    • Hippo promotes proliferation arrest and apoptosis in the Salvador/Warts pathway
    • Udan RS, Kango-Singh M, Nolo R, Tao C, Halder G. 2003. Hippo promotes proliferation arrest and apoptosis in the Salvador/Warts pathway. Nat Cell Biol 5:914-920.
    • (2003) Nat Cell Biol , vol.5 , pp. 914-920
    • Udan, R.S.1    Kango-Singh, M.2    Nolo, R.3    Tao, C.4    Halder, G.5
  • 49
    • 0033515426 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation
    • Wei Y, Yu L, Bowen J, Gorovsky MA, Allis CD. 1999. Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell 97:99-109.
    • (1999) Cell , vol.97 , pp. 99-109
    • Wei, Y.1    Yu, L.2    Bowen, J.3    Gorovsky, M.A.4    Allis, C.D.5
  • 50
    • 19644381697 scopus 로고    scopus 로고
    • Differential subnuclear localization and replication timing of histone H3 lysine 9 methylation states
    • Wu R, Terry AV, Singh PB, Gilbert DM. 2005. Differential subnuclear localization and replication timing of histone H3 lysine 9 methylation states. Mol Biol Cell 16:2872-2881.
    • (2005) Mol Biol Cell , vol.16 , pp. 2872-2881
    • Wu, R.1    Terry, A.V.2    Singh, P.B.3    Gilbert, D.M.4
  • 52
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • Xu F, Zhang K, Grunstein M. 2005. Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell 121:375-385.
    • (2005) Cell , vol.121 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 53
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Zhang Y, Reinberg D. 2001. Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails. Genes Dev 15:2343-2360.
    • (2001) Genes Dev , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.