메뉴 건너뛰기




Volumn 29, Issue 7, 2013, Pages 394-402

WEE1 tyrosine kinase, a novel epigenetic modifier

Author keywords

Cancer; Cell cycle; Epigenetics; Histones; Tyrosine phosphorylation; WEE1

Indexed keywords

HISTONE H2B; PROTEIN TYROSINE KINASE; PROTEIN WEE1; TYROSINE; UNCLASSIFIED DRUG;

EID: 84879607314     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tig.2013.02.003     Document Type: Review
Times cited : (43)

References (104)
  • 1
    • 0022482135 scopus 로고
    • Normal stoichiometry of histone dimer sets is necessary for high fidelity of mitotic chromosome transmission
    • Meeks-Wagner D., Hartwell L.H. Normal stoichiometry of histone dimer sets is necessary for high fidelity of mitotic chromosome transmission. Cell 1986, 44:43-52.
    • (1986) Cell , vol.44 , pp. 43-52
    • Meeks-Wagner, D.1    Hartwell, L.H.2
  • 2
    • 0025863511 scopus 로고
    • The regulation of histone synthesis in the cell cycle
    • Osley M.A. The regulation of histone synthesis in the cell cycle. Annu. Rev. Biochem. 1991, 60:827-861.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 827-861
    • Osley, M.A.1
  • 3
    • 84862777348 scopus 로고    scopus 로고
    • Driver mutations in histone H3.3 and chromatin remodelling genes in paediatric glioblastoma
    • Schwartzentruber J., et al. Driver mutations in histone H3.3 and chromatin remodelling genes in paediatric glioblastoma. Nature 2012, 482:226-231.
    • (2012) Nature , vol.482 , pp. 226-231
    • Schwartzentruber, J.1
  • 4
    • 84862777410 scopus 로고    scopus 로고
    • Somatic histone H3 alterations in pediatric diffuse intrinsic pontine gliomas and non-brainstem glioblastomas
    • Wu G., et al. Somatic histone H3 alterations in pediatric diffuse intrinsic pontine gliomas and non-brainstem glioblastomas. Nat. Genet. 2012, 44:251-253.
    • (2012) Nat. Genet. , vol.44 , pp. 251-253
    • Wu, G.1
  • 5
    • 84865863019 scopus 로고    scopus 로고
    • K27M mutation in histone H3.3 defines clinically and biologically distinct subgroups of pediatric diffuse intrinsic pontine gliomas
    • Khuong-Quang D.A., et al. K27M mutation in histone H3.3 defines clinically and biologically distinct subgroups of pediatric diffuse intrinsic pontine gliomas. Acta Neuropathol. 2012, 124:439-447.
    • (2012) Acta Neuropathol. , vol.124 , pp. 439-447
    • Khuong-Quang, D.A.1
  • 6
    • 68249094946 scopus 로고    scopus 로고
    • Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis
    • Singh R.K., et al. Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat. Cell Biol. 2009, 11:925-933.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 925-933
    • Singh, R.K.1
  • 7
    • 84868246832 scopus 로고    scopus 로고
    • Asymmetric division of Drosophila male germline stem cell shows asymmetric histone distribution
    • Tran V., et al. Asymmetric division of Drosophila male germline stem cell shows asymmetric histone distribution. Science 2012, 338:679-682.
    • (2012) Science , vol.338 , pp. 679-682
    • Tran, V.1
  • 8
    • 84868682266 scopus 로고    scopus 로고
    • Epigenetic control of cell cycle-dependent histone gene expression is a principal component of the abbreviated pluripotent cell cycle
    • Medina R., et al. Epigenetic control of cell cycle-dependent histone gene expression is a principal component of the abbreviated pluripotent cell cycle. Mol. Cell. Biol. 2012, 32:3860-3871.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 3860-3871
    • Medina, R.1
  • 9
    • 0022531173 scopus 로고
    • Isolation of two genes that affect mitotic chromosome transmission in S. cerevisiae
    • Meeks-Wagner D., et al. Isolation of two genes that affect mitotic chromosome transmission in S. cerevisiae. Cell 1986, 44:53-63.
    • (1986) Cell , vol.44 , pp. 53-63
    • Meeks-Wagner, D.1
  • 10
    • 77950579010 scopus 로고    scopus 로고
    • Hsk1- and SCF(Pof3)-dependent proteolysis of S. pombe Ams2 ensures histone homeostasis and centromere function
    • Takayama Y., et al. Hsk1- and SCF(Pof3)-dependent proteolysis of S. pombe Ams2 ensures histone homeostasis and centromere function. Dev. Cell 2010, 18:385-396.
    • (2010) Dev. Cell , vol.18 , pp. 385-396
    • Takayama, Y.1
  • 11
    • 84879602911 scopus 로고    scopus 로고
    • The role of dicentric chromosome formation and secondary centromere deletion in the evolution of myeloid malignancy
    • Mackinnon R.N., Campbell L.J. The role of dicentric chromosome formation and secondary centromere deletion in the evolution of myeloid malignancy. Genet. Res. Int. 2011, 2011:643628.
    • (2011) Genet. Res. Int. , vol.2011 , pp. 643628
    • Mackinnon, R.N.1    Campbell, L.J.2
  • 12
    • 33644542460 scopus 로고    scopus 로고
    • Mislocalization of the Drosophila centromere-specific histone CID promotes formation of functional ectopic kinetochores
    • Heun P., et al. Mislocalization of the Drosophila centromere-specific histone CID promotes formation of functional ectopic kinetochores. Dev. Cell 2006, 10:303-315.
    • (2006) Dev. Cell , vol.10 , pp. 303-315
    • Heun, P.1
  • 13
    • 84866914587 scopus 로고    scopus 로고
    • Cnp1 in fission yeast
    • Cnp1 in fission yeast. PLoS Genet. 2012, 8:e1002985.
    • (2012) PLoS Genet. , vol.8
    • Choi, E.S.1
  • 14
    • 0344688414 scopus 로고    scopus 로고
    • A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. cerevisiae
    • Gunjan A., Verreault A. A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. cerevisiae. Cell 2003, 115:537-549.
    • (2003) Cell , vol.115 , pp. 537-549
    • Gunjan, A.1    Verreault, A.2
  • 15
    • 0020600551 scopus 로고
    • Regulation of human histone gene expression: kinetics of accumulation and changes in the rate of synthesis and in the half-lives of individual histone mRNAs during the HeLa cell cycle
    • Heintz N., et al. Regulation of human histone gene expression: kinetics of accumulation and changes in the rate of synthesis and in the half-lives of individual histone mRNAs during the HeLa cell cycle. Mol. Cell. Biol. 1983, 3:539-550.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 539-550
    • Heintz, N.1
  • 16
    • 0034665635 scopus 로고    scopus 로고
    • NPAT by cyclin E/Cdk2 in Cajal bodies promotes histone gene transcription
    • NPAT by cyclin E/Cdk2 in Cajal bodies promotes histone gene transcription. Genes Dev. 2000, 14:2298-2313.
    • (2000) Genes Dev. , vol.14 , pp. 2298-2313
    • Ma, T.1
  • 17
    • 84866112974 scopus 로고    scopus 로고
    • H2B Tyr37 phosphorylation suppresses expression of replication-dependent core histone genes
    • Mahajan K., et al. H2B Tyr37 phosphorylation suppresses expression of replication-dependent core histone genes. Nat. Struct. Mol. Biol. 2012, 19:930-937.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 930-937
    • Mahajan, K.1
  • 18
    • 0036429193 scopus 로고    scopus 로고
    • The human and mouse replication-dependent histone genes
    • Marzluff W.F., et al. The human and mouse replication-dependent histone genes. Genomics 2002, 80:487-498.
    • (2002) Genomics , vol.80 , pp. 487-498
    • Marzluff, W.F.1
  • 19
    • 0019503177 scopus 로고
    • Cell-cycle regulation of yeast histone mRNA
    • Hereford L.M., et al. Cell-cycle regulation of yeast histone mRNA. Cell 1981, 24:367-375.
    • (1981) Cell , vol.24 , pp. 367-375
    • Hereford, L.M.1
  • 20
    • 0020411152 scopus 로고
    • Periodic transcription of yeast histone genes
    • Hereford L., et al. Periodic transcription of yeast histone genes. Cell 1982, 30:305-310.
    • (1982) Cell , vol.30 , pp. 305-310
    • Hereford, L.1
  • 21
    • 54149091257 scopus 로고    scopus 로고
    • Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail
    • Marzluff W.F., et al. Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail. Nat. Rev. 2008, 9:843-854.
    • (2008) Nat. Rev. , vol.9 , pp. 843-854
    • Marzluff, W.F.1
  • 22
    • 47049128024 scopus 로고    scopus 로고
    • Phosphorylation of threonine 61 by cyclin a/Cdk1 triggers degradation of stem-loop binding protein at the end of S phase
    • Koseoglu M.M., et al. Phosphorylation of threonine 61 by cyclin a/Cdk1 triggers degradation of stem-loop binding protein at the end of S phase. Mol. Cell. Biol. 2008, 28:4469-4479.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4469-4479
    • Koseoglu, M.M.1
  • 23
    • 84868686181 scopus 로고    scopus 로고
    • The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitination
    • Krishnan N., et al. The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitination. Mol. Cell. Biol. 2012, 32:4306-4322.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 4306-4322
    • Krishnan, N.1
  • 24
    • 0025924328 scopus 로고
    • wee1 mitotic inhibitor is a tyrosine/serine kinase
    • wee1 mitotic inhibitor is a tyrosine/serine kinase. Nature 1991, 349:808-811.
    • (1991) Nature , vol.349 , pp. 808-811
    • Featherstone, C.1    Russell, P.2
  • 25
    • 0029000155 scopus 로고
    • Cell cycle regulation of human WEE1
    • McGowan C.H., Russell P. Cell cycle regulation of human WEE1. EMBO J. 1995, 14:2166-2175.
    • (1995) EMBO J. , vol.14 , pp. 2166-2175
    • McGowan, C.H.1    Russell, P.2
  • 26
    • 0023662312 scopus 로고
    • +, a gene encoding a protein kinase homolog
    • +, a gene encoding a protein kinase homolog. Cell 1987, 49:559-567.
    • (1987) Cell , vol.49 , pp. 559-567
    • Russell, P.1    Nurse, P.2
  • 27
    • 0024959919 scopus 로고
    • + protein kinase regulates entry into mitosis
    • + protein kinase regulates entry into mitosis. Nature 1989, 342:39-45.
    • (1989) Nature , vol.342 , pp. 39-45
    • Gould, K.L.1    Nurse, P.2
  • 28
    • 0029048491 scopus 로고
    • Regulation of the human WEE1Hu CDK tyrosine 15-kinase during the cell cycle
    • Watanabe N., et al. Regulation of the human WEE1Hu CDK tyrosine 15-kinase during the cell cycle. EMBO J. 1995, 14:1878-1891.
    • (1995) EMBO J. , vol.14 , pp. 1878-1891
    • Watanabe, N.1
  • 29
    • 0034665757 scopus 로고    scopus 로고
    • NPAT links cyclin E-Cdk2 to the regulation of replication-dependent histone gene transcription
    • Zhao J., et al. NPAT links cyclin E-Cdk2 to the regulation of replication-dependent histone gene transcription. Genes Dev. 2000, 14:2283-2297.
    • (2000) Genes Dev. , vol.14 , pp. 2283-2297
    • Zhao, J.1
  • 30
    • 0032520093 scopus 로고    scopus 로고
    • Expression of NPAT, a novel substrate of cyclin E-CDK2, promotes S-phase entry
    • Zhao J., et al. Expression of NPAT, a novel substrate of cyclin E-CDK2, promotes S-phase entry. Genes Dev. 1998, 12:456-461.
    • (1998) Genes Dev. , vol.12 , pp. 456-461
    • Zhao, J.1
  • 31
    • 78650754693 scopus 로고    scopus 로고
    • Asf1/HIRA facilitate global histone deacetylation and associate with HP1 to promote nucleosome occupancy at heterochromatic loci
    • Yamane K., et al. Asf1/HIRA facilitate global histone deacetylation and associate with HP1 to promote nucleosome occupancy at heterochromatic loci. Mol. Cell 2011, 41:56-66.
    • (2011) Mol. Cell , vol.41 , pp. 56-66
    • Yamane, K.1
  • 32
    • 0023055514 scopus 로고
    • Identification of sequences in a yeast histone promoter involved in periodic transcription
    • Osley M.A., et al. Identification of sequences in a yeast histone promoter involved in periodic transcription. Cell 1986, 45:537-544.
    • (1986) Cell , vol.45 , pp. 537-544
    • Osley, M.A.1
  • 33
    • 0026730193 scopus 로고
    • Identification of a new set of cell cycle-regulatory genes that regulate S-phase transcription of histone genes in Saccharomyces cerevisiae
    • Xu H., et al. Identification of a new set of cell cycle-regulatory genes that regulate S-phase transcription of histone genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 1992, 12:5249-5259.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5249-5259
    • Xu, H.1
  • 34
    • 0035131425 scopus 로고    scopus 로고
    • HIRA, the human homologue of yeast Hir1p and Hir2p, is a novel cyclin-cdk2 substrate whose expression blocks S-phase progression
    • Hall C., et al. HIRA, the human homologue of yeast Hir1p and Hir2p, is a novel cyclin-cdk2 substrate whose expression blocks S-phase progression. Mol. Cell. Biol. 2001, 21:1854-1865.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1854-1865
    • Hall, C.1
  • 35
    • 0015954720 scopus 로고
    • Genetic control of the cell division cycle in yeast
    • Hartwell L.H., et al. Genetic control of the cell division cycle in yeast. Science 1974, 183:46-51.
    • (1974) Science , vol.183 , pp. 46-51
    • Hartwell, L.H.1
  • 36
    • 0041312681 scopus 로고    scopus 로고
    • The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase
    • Gray C.H., et al. The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase. EMBO J. 2003, 22:3524-3535.
    • (2003) EMBO J. , vol.22 , pp. 3524-3535
    • Gray, C.H.1
  • 37
    • 77953077420 scopus 로고    scopus 로고
    • A global protein kinase and phosphatase interaction network in yeast
    • Breitkreutz A., et al. A global protein kinase and phosphatase interaction network in yeast. Science 2010, 328:1043-1046.
    • (2010) Science , vol.328 , pp. 1043-1046
    • Breitkreutz, A.1
  • 38
    • 0032560517 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena
    • Wei Y., et al. Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:7480-7484.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 7480-7484
    • Wei, Y.1
  • 39
    • 0033520367 scopus 로고    scopus 로고
    • Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation
    • Goto H., et al. Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation. J. Biol. Chem. 1999, 274:25543-25549.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25543-25549
    • Goto, H.1
  • 40
    • 0037324194 scopus 로고    scopus 로고
    • Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase
    • Preuss U., et al. Novel mitosis-specific phosphorylation of histone H3 at Thr11 mediated by Dlk/ZIP kinase. Nucleic Acids Res. 2003, 31:878-885.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 878-885
    • Preuss, U.1
  • 41
    • 77957814604 scopus 로고    scopus 로고
    • Reduced histone biosynthesis and chromatin changes arising from a damage signal at telomeres
    • O'Sullivan R.J., et al. Reduced histone biosynthesis and chromatin changes arising from a damage signal at telomeres. Nat. Struct. Mol. Biol. 2010, 17:1218-1225.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1218-1225
    • O'Sullivan, R.J.1
  • 42
    • 0028847955 scopus 로고
    • Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4
    • Sobel R.E., et al. Conservation of deposition-related acetylation sites in newly synthesized histones H3 and H4. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:1237-1241.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1237-1241
    • Sobel, R.E.1
  • 43
    • 79959629469 scopus 로고    scopus 로고
    • Analysis of protein dynamics at active, stalled, and collapsed replication forks
    • Sirbu B.M., et al. Analysis of protein dynamics at active, stalled, and collapsed replication forks. Genes Dev. 2011, 25:1320-1327.
    • (2011) Genes Dev. , vol.25 , pp. 1320-1327
    • Sirbu, B.M.1
  • 44
    • 7644232055 scopus 로고    scopus 로고
    • WD dipeptide motifs and LXXLL motif of chicken HIRA are essential for interactions with the p48 subunit of chromatin assembly factor-1 and histone deacetylase-2 in vitro and in vivo
    • Ahmad A., et al. WD dipeptide motifs and LXXLL motif of chicken HIRA are essential for interactions with the p48 subunit of chromatin assembly factor-1 and histone deacetylase-2 in vitro and in vivo. Gene 2004, 342:125-136.
    • (2004) Gene , vol.342 , pp. 125-136
    • Ahmad, A.1
  • 45
    • 0142135133 scopus 로고    scopus 로고
    • Differential contribution of inhibitory phosphorylation of CDC2 and CDK2 for unperturbed cell cycle control and DNA integrity checkpoints
    • Chow J.P., et al. Differential contribution of inhibitory phosphorylation of CDC2 and CDK2 for unperturbed cell cycle control and DNA integrity checkpoints. J. Biol. Chem. 2003, 278:40815-40828.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40815-40828
    • Chow, J.P.1
  • 46
    • 0030926775 scopus 로고    scopus 로고
    • Regulation of Schizosaccharomyces pombe Wee1 tyrosine kinase
    • Aligue R., et al. Regulation of Schizosaccharomyces pombe Wee1 tyrosine kinase. J. Biol. Chem. 1997, 272:13320-13325.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13320-13325
    • Aligue, R.1
  • 47
    • 0031034628 scopus 로고    scopus 로고
    • Cdc2 tyrosine phosphorylation is required for the DNA damage checkpoint in fission yeast
    • Rhind N., et al. Cdc2 tyrosine phosphorylation is required for the DNA damage checkpoint in fission yeast. Genes Dev. 1997, 11:504-511.
    • (1997) Genes Dev. , vol.11 , pp. 504-511
    • Rhind, N.1
  • 48
    • 77956517283 scopus 로고    scopus 로고
    • In silico analysis of kinase expression identifies WEE1 as a gatekeeper against mitotic catastrophe in glioblastoma
    • Mir S.E., et al. In silico analysis of kinase expression identifies WEE1 as a gatekeeper against mitotic catastrophe in glioblastoma. Cancer Cell 2010, 18:244-257.
    • (2010) Cancer Cell , vol.18 , pp. 244-257
    • Mir, S.E.1
  • 49
    • 33744905789 scopus 로고    scopus 로고
    • Murine Wee1 plays a critical role in cell cycle regulation and pre-implantation stages of embryonic development
    • Tominaga Y., et al. Murine Wee1 plays a critical role in cell cycle regulation and pre-implantation stages of embryonic development. Int. J. Biol. Sci. 2006, 2:161-170.
    • (2006) Int. J. Biol. Sci. , vol.2 , pp. 161-170
    • Tominaga, Y.1
  • 50
    • 77949410508 scopus 로고    scopus 로고
    • Regulators of cyclin-dependent kinases are crucial for maintaining genome integrity in S phase
    • Beck H., et al. Regulators of cyclin-dependent kinases are crucial for maintaining genome integrity in S phase. J. Cell Biol. 2010, 188:629-638.
    • (2010) J. Cell Biol. , vol.188 , pp. 629-638
    • Beck, H.1
  • 51
    • 84855908936 scopus 로고    scopus 로고
    • Safeguarding genome integrity: the checkpoint kinases ATR, CHK1 and WEE1 restrain CDK activity during normal DNA replication
    • Sorensen C.S., Syljuasen R.G. Safeguarding genome integrity: the checkpoint kinases ATR, CHK1 and WEE1 restrain CDK activity during normal DNA replication. Nucleic Acids Res. 2012, 40:477-486.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 477-486
    • Sorensen, C.S.1    Syljuasen, R.G.2
  • 52
    • 77958498222 scopus 로고    scopus 로고
    • The ATM-Chk2 and ATR-Chk1 pathways in DNA damage signaling and cancer
    • Smith J., et al. The ATM-Chk2 and ATR-Chk1 pathways in DNA damage signaling and cancer. Adv. Cancer Res. 2010, 108:73-112.
    • (2010) Adv. Cancer Res. , vol.108 , pp. 73-112
    • Smith, J.1
  • 53
    • 0012966157 scopus 로고    scopus 로고
    • Chk1 regulates the S phase checkpoint by coupling the physiological turnover and ionizing radiation-induced accelerated proteolysis of Cdc25A
    • Sorensen C.S., et al. Chk1 regulates the S phase checkpoint by coupling the physiological turnover and ionizing radiation-induced accelerated proteolysis of Cdc25A. Cancer Cell 2003, 3:247-258.
    • (2003) Cancer Cell , vol.3 , pp. 247-258
    • Sorensen, C.S.1
  • 54
    • 84858405757 scopus 로고    scopus 로고
    • Chk1 and Wee1 kinases coordinate DNA replication, chromosome condensation, and anaphase entry
    • Fasulo B., et al. Chk1 and Wee1 kinases coordinate DNA replication, chromosome condensation, and anaphase entry. Mol. Biol. Cell 2012, 23:1047-1057.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 1047-1057
    • Fasulo, B.1
  • 55
    • 0031035528 scopus 로고    scopus 로고
    • Chk1 is a wee1 kinase in the G2 DNA damage checkpoint inhibiting cdc2 by Y15 phosphorylation
    • O'Connell M.J., et al. Chk1 is a wee1 kinase in the G2 DNA damage checkpoint inhibiting cdc2 by Y15 phosphorylation. EMBO J. 1997, 16:545-554.
    • (1997) EMBO J. , vol.16 , pp. 545-554
    • O'Connell, M.J.1
  • 56
    • 84864557192 scopus 로고    scopus 로고
    • Forced mitotic entry of S-phase cells as a therapeutic strategy induced by inhibition of WEE1
    • Aarts M., et al. Forced mitotic entry of S-phase cells as a therapeutic strategy induced by inhibition of WEE1. Cancer Discov. 2012, 2:524-539.
    • (2012) Cancer Discov. , vol.2 , pp. 524-539
    • Aarts, M.1
  • 57
    • 80655141261 scopus 로고    scopus 로고
    • Chk1 inhibition and Wee1 inhibition combine synergistically to impede cellular proliferation
    • Davies K.D., et al. Chk1 inhibition and Wee1 inhibition combine synergistically to impede cellular proliferation. Cancer Biol. Ther. 2011, 12:788-796.
    • (2011) Cancer Biol. Ther. , vol.12 , pp. 788-796
    • Davies, K.D.1
  • 58
    • 84868689115 scopus 로고    scopus 로고
    • Cyclin-dependent kinase suppression by WEE1 kinase protects the genome through control of replication initiation and nucleotide consumption
    • Beck H., et al. Cyclin-dependent kinase suppression by WEE1 kinase protects the genome through control of replication initiation and nucleotide consumption. Mol. Cell. Biol. 2012, 32:4226-4236.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 4226-4236
    • Beck, H.1
  • 59
    • 80052632895 scopus 로고    scopus 로고
    • Wee1 controls genomic stability during replication by regulating the Mus81-Eme1 endonuclease
    • Dominguez-Kelly R., et al. Wee1 controls genomic stability during replication by regulating the Mus81-Eme1 endonuclease. J. Cell Biol. 2011, 194:567-579.
    • (2011) J. Cell Biol. , vol.194 , pp. 567-579
    • Dominguez-Kelly, R.1
  • 60
    • 62549132126 scopus 로고    scopus 로고
    • Cyclin A-Cdk1 regulates the origin firing program in mammalian cells
    • Katsuno Y., et al. Cyclin A-Cdk1 regulates the origin firing program in mammalian cells. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:3184-3189.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 3184-3189
    • Katsuno, Y.1
  • 61
    • 0034635462 scopus 로고    scopus 로고
    • Interaction of Xenopus Cdc2 × cyclin A1 with the origin recognition complex
    • Romanowski P., et al. Interaction of Xenopus Cdc2 × cyclin A1 with the origin recognition complex. J. Biol. Chem. 2000, 275:4239-4243.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4239-4243
    • Romanowski, P.1
  • 62
    • 0036850262 scopus 로고    scopus 로고
    • Stable association of mitotic cyclin B/Cdc2 to replication origins prevents endoreduplication
    • Wuarin J., et al. Stable association of mitotic cyclin B/Cdc2 to replication origins prevents endoreduplication. Cell 2002, 111:419-431.
    • (2002) Cell , vol.111 , pp. 419-431
    • Wuarin, J.1
  • 63
    • 63849151495 scopus 로고    scopus 로고
    • Generation and management of excess histones during the cell cycle
    • Singh R.K., et al. Generation and management of excess histones during the cell cycle. Front. Biosci. 2009, 14:3145-3158.
    • (2009) Front. Biosci. , vol.14 , pp. 3145-3158
    • Singh, R.K.1
  • 64
    • 84868089767 scopus 로고    scopus 로고
    • Histone dosage regulates DNA damage sensitivity in a checkpoint-independent manner by the homologous recombination pathway
    • Liang D., et al. Histone dosage regulates DNA damage sensitivity in a checkpoint-independent manner by the homologous recombination pathway. Nucleic Acids Res. 2012, 40:9604-9620.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 9604-9620
    • Liang, D.1
  • 65
    • 84860516339 scopus 로고    scopus 로고
    • Novel E3 ubiquitin ligases that regulate histone protein levels in the budding yeast Saccharomyces cerevisiae
    • Singh R.K., et al. Novel E3 ubiquitin ligases that regulate histone protein levels in the budding yeast Saccharomyces cerevisiae. PLoS ONE 2012, 7:e36295.
    • (2012) PLoS ONE , vol.7
    • Singh, R.K.1
  • 66
    • 34249025702 scopus 로고    scopus 로고
    • Contribution of Trf4/5 and the nuclear exosome to genome stability through regulation of histone mRNA levels in Saccharomyces cerevisiae
    • Reis C.C., Campbell J.L. Contribution of Trf4/5 and the nuclear exosome to genome stability through regulation of histone mRNA levels in Saccharomyces cerevisiae. Genetics 2007, 175:993-1010.
    • (2007) Genetics , vol.175 , pp. 993-1010
    • Reis, C.C.1    Campbell, J.L.2
  • 67
    • 79951882529 scopus 로고    scopus 로고
    • Prediction of associations between microRNAs and gene expression in glioma biology
    • Wuchty S., et al. Prediction of associations between microRNAs and gene expression in glioma biology. PLoS ONE 2011, 6:e14681.
    • (2011) PLoS ONE , vol.6
    • Wuchty, S.1
  • 68
    • 65249161106 scopus 로고    scopus 로고
    • Integrated functional, gene expression and genomic analysis for the identification of cancer targets
    • Iorns E., et al. Integrated functional, gene expression and genomic analysis for the identification of cancer targets. PLoS ONE 2009, 4:e5120.
    • (2009) PLoS ONE , vol.4
    • Iorns, E.1
  • 69
    • 77955655940 scopus 로고    scopus 로고
    • Identification of WEE1 as a potential molecular target in cancer cells by RNAi screening of the human tyrosine kinome
    • Murrow L.M., et al. Identification of WEE1 as a potential molecular target in cancer cells by RNAi screening of the human tyrosine kinome. Breast Cancer Res. Treat. 2010, 122:347-357.
    • (2010) Breast Cancer Res. Treat. , vol.122 , pp. 347-357
    • Murrow, L.M.1
  • 70
    • 84862185038 scopus 로고    scopus 로고
    • High expression of Wee1 is associated with poor disease-free survival in malignant melanoma: potential for targeted therapy
    • Magnussen G.I., et al. High expression of Wee1 is associated with poor disease-free survival in malignant melanoma: potential for targeted therapy. PLoS ONE 2012, 7:e38254.
    • (2012) PLoS ONE , vol.7
    • Magnussen, G.I.1
  • 71
    • 70949083026 scopus 로고    scopus 로고
    • Small-molecule inhibition of Wee1 kinase by MK-1775 selectively sensitizes p53-deficient tumor cells to DNA-damaging agents
    • Hirai H., et al. Small-molecule inhibition of Wee1 kinase by MK-1775 selectively sensitizes p53-deficient tumor cells to DNA-damaging agents. Mol. Cancer Ther. 2009, 8:2992-3000.
    • (2009) Mol. Cancer Ther. , vol.8 , pp. 2992-3000
    • Hirai, H.1
  • 72
    • 83355174034 scopus 로고    scopus 로고
    • 2 checkpoint activation with the Wee-1 inhibitor MK-1775 in glioblastoma cell lines
    • 2 checkpoint activation with the Wee-1 inhibitor MK-1775 in glioblastoma cell lines. Mol. Cancer Ther. 2011, 10:2405-2414.
    • (2011) Mol. Cancer Ther. , vol.10 , pp. 2405-2414
    • Sarcar, B.1
  • 73
    • 77953711939 scopus 로고    scopus 로고
    • MK-1775, a small molecule Wee1 inhibitor, enhances anti-tumor efficacy of various DNA-damaging agents, including 5-fluorouracil
    • Hirai H., et al. MK-1775, a small molecule Wee1 inhibitor, enhances anti-tumor efficacy of various DNA-damaging agents, including 5-fluorouracil. Cancer Biol. Ther. 2010, 9:514-522.
    • (2010) Cancer Biol. Ther. , vol.9 , pp. 514-522
    • Hirai, H.1
  • 74
    • 79952117003 scopus 로고    scopus 로고
    • Targeting Wee1-like protein kinase to treat cancer
    • Stathis A., Oza A. Targeting Wee1-like protein kinase to treat cancer. Drug News Perspect. 2010, 23:425-429.
    • (2010) Drug News Perspect. , vol.23 , pp. 425-429
    • Stathis, A.1    Oza, A.2
  • 75
    • 80052491760 scopus 로고    scopus 로고
    • MK-1775, a novel Wee1 kinase inhibitor, radiosensitizes p53-defective human tumor cells
    • Bridges K.A., et al. MK-1775, a novel Wee1 kinase inhibitor, radiosensitizes p53-defective human tumor cells. Clin. Cancer Res. 2011, 17:5638-5648.
    • (2011) Clin. Cancer Res. , vol.17 , pp. 5638-5648
    • Bridges, K.A.1
  • 76
    • 79960339454 scopus 로고    scopus 로고
    • WEE1 kinase targeting combined with DNA-damaging cancer therapy catalyzes mitotic catastrophe
    • De Witt Hamer P.C., et al. WEE1 kinase targeting combined with DNA-damaging cancer therapy catalyzes mitotic catastrophe. Clin. Cancer Res. 2011, 17:4200-4207.
    • (2011) Clin. Cancer Res. , vol.17 , pp. 4200-4207
    • De Witt Hamer, P.C.1
  • 77
    • 78650012970 scopus 로고    scopus 로고
    • To selectivity and beyond
    • Mack G.S. To selectivity and beyond. Nat. Biotechnol. 2010, 28:1259-1266.
    • (2010) Nat. Biotechnol. , vol.28 , pp. 1259-1266
    • Mack, G.S.1
  • 78
    • 80052029516 scopus 로고    scopus 로고
    • Frequent mutation of histone-modifying genes in non-Hodgkin lymphoma
    • Morin R.D., et al. Frequent mutation of histone-modifying genes in non-Hodgkin lymphoma. Nature 2011, 476:298-303.
    • (2011) Nature , vol.476 , pp. 298-303
    • Morin, R.D.1
  • 79
    • 75749124332 scopus 로고    scopus 로고
    • Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin
    • Morin R.D., et al. Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin. Nat. Genet. 2010, 42:181-185.
    • (2010) Nat. Genet. , vol.42 , pp. 181-185
    • Morin, R.D.1
  • 80
    • 84863165348 scopus 로고    scopus 로고
    • Mutation of A677 in histone methyltransferase EZH2 in human B-cell lymphoma promotes hypertrimethylation of histone H3 on lysine 27 (H3K27)
    • McCabe M.T., et al. Mutation of A677 in histone methyltransferase EZH2 in human B-cell lymphoma promotes hypertrimethylation of histone H3 on lysine 27 (H3K27). Proc. Natl. Acad. Sci. U.S.A. 2012, 109:2989-2994.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 2989-2994
    • McCabe, M.T.1
  • 81
    • 80053279825 scopus 로고    scopus 로고
    • The Y641C mutation of EZH2 alters substrate specificity for histone H3 lysine 27 methylation states
    • Wigle T.J., et al. The Y641C mutation of EZH2 alters substrate specificity for histone H3 lysine 27 methylation states. FEBS Lett. 2011, 585:3011-3014.
    • (2011) FEBS Lett. , vol.585 , pp. 3011-3014
    • Wigle, T.J.1
  • 82
    • 79952167230 scopus 로고    scopus 로고
    • Somatic mutations at EZH2 Y641 act dominantly through a mechanism of selectively altered PRC2 catalytic activity, to increase H3K27 trimethylation
    • Yap D.B., et al. Somatic mutations at EZH2 Y641 act dominantly through a mechanism of selectively altered PRC2 catalytic activity, to increase H3K27 trimethylation. Blood 2011, 117:2451-2459.
    • (2011) Blood , vol.117 , pp. 2451-2459
    • Yap, D.B.1
  • 83
    • 84867632489 scopus 로고    scopus 로고
    • A selective inhibitor of EZH2 blocks H3K27 methylation and kills mutant lymphoma cells
    • Knutson S.K., et al. A selective inhibitor of EZH2 blocks H3K27 methylation and kills mutant lymphoma cells. Nat. Chem. Biol. 2012, 8:890-896.
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 890-896
    • Knutson, S.K.1
  • 84
    • 84870573126 scopus 로고    scopus 로고
    • EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations
    • McCabe M.T., et al. EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations. Nature 2012, 492:108-112.
    • (2012) Nature , vol.492 , pp. 108-112
    • McCabe, M.T.1
  • 85
    • 84867606428 scopus 로고    scopus 로고
    • Hotspot mutations in H3F3A and IDH1 define distinct epigenetic and biological subgroups of glioblastoma
    • Sturm D., et al. Hotspot mutations in H3F3A and IDH1 define distinct epigenetic and biological subgroups of glioblastoma. Cancer Cell 2012, 22:425-437.
    • (2012) Cancer Cell , vol.22 , pp. 425-437
    • Sturm, D.1
  • 86
    • 84870912857 scopus 로고    scopus 로고
    • A role for H2B ubiquitylation in DNA replication
    • Trujillo K.M., Osley M.A. A role for H2B ubiquitylation in DNA replication. Mol. Cell 2012, 48:734-746.
    • (2012) Mol. Cell , vol.48 , pp. 734-746
    • Trujillo, K.M.1    Osley, M.A.2
  • 87
    • 84860518345 scopus 로고    scopus 로고
    • Codependency of H2B monoubiquitination and nucleosome reassembly on Chd1
    • Lee J.S., et al. Codependency of H2B monoubiquitination and nucleosome reassembly on Chd1. Genes Dev. 2012, 26:914-919.
    • (2012) Genes Dev. , vol.26 , pp. 914-919
    • Lee, J.S.1
  • 88
    • 79951974992 scopus 로고    scopus 로고
    • Requirement of ATM-dependent monoubiquitylation of histone H2B for timely repair of DNA double-strand breaks
    • Moyal L., et al. Requirement of ATM-dependent monoubiquitylation of histone H2B for timely repair of DNA double-strand breaks. Mol. Cell 2011, 41:529-542.
    • (2011) Mol. Cell , vol.41 , pp. 529-542
    • Moyal, L.1
  • 89
    • 0023666061 scopus 로고
    • Histone H2B repression causes cell-cycle-specific arrest in yeast: effects on chromosomal segregation, replication, and transcription
    • Han M., et al. Histone H2B repression causes cell-cycle-specific arrest in yeast: effects on chromosomal segregation, replication, and transcription. Cell 1987, 48:589-597.
    • (1987) Cell , vol.48 , pp. 589-597
    • Han, M.1
  • 90
    • 0023955508 scopus 로고
    • Changes in histone gene dosage alter transcription in yeast
    • Clark-Adams C.D., et al. Changes in histone gene dosage alter transcription in yeast. Genes Dev. 1988, 2:150-159.
    • (1988) Genes Dev. , vol.2 , pp. 150-159
    • Clark-Adams, C.D.1
  • 91
    • 0029915879 scopus 로고    scopus 로고
    • Differential effect of H1 variant overexpression on cell cycle progression and gene expression
    • Brown D.T., et al. Differential effect of H1 variant overexpression on cell cycle progression and gene expression. Nucleic Acids Res. 1996, 24:486-493.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 486-493
    • Brown, D.T.1
  • 92
    • 0033621414 scopus 로고    scopus 로고
    • Effects of H1 histone variant overexpression on chromatin structure
    • Gunjan A., et al. Effects of H1 histone variant overexpression on chromatin structure. J. Biol. Chem. 1999, 274:37950-37956.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37950-37956
    • Gunjan, A.1
  • 93
    • 0035863061 scopus 로고    scopus 로고
    • Drosophila stem loop binding protein coordinates accumulation of mature histone mRNA with cell cycle progression
    • Sullivan E., et al. Drosophila stem loop binding protein coordinates accumulation of mature histone mRNA with cell cycle progression. Genes Dev. 2001, 15:173-187.
    • (2001) Genes Dev. , vol.15 , pp. 173-187
    • Sullivan, E.1
  • 94
    • 0038721220 scopus 로고    scopus 로고
    • H1 linker histones are essential for mouse development and affect nucleosome spacing in vivo
    • Fan Y., et al. H1 linker histones are essential for mouse development and affect nucleosome spacing in vivo. Mol. Cell. Biol. 2003, 23:4559-4572.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4559-4572
    • Fan, Y.1
  • 95
    • 13444270604 scopus 로고    scopus 로고
    • Partial depletion of histone H4 increases homologous recombination-mediated genetic instability
    • Prado F., Aguilera A. Partial depletion of histone H4 increases homologous recombination-mediated genetic instability. Mol. Cell. Biol. 2005, 25:1526-1536.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1526-1536
    • Prado, F.1    Aguilera, A.2
  • 96
    • 84866948612 scopus 로고    scopus 로고
    • An essential role of variant histone h3.3 for ectomesenchyme potential of the cranial neural crest
    • Cox S.G., et al. An essential role of variant histone h3.3 for ectomesenchyme potential of the cranial neural crest. PLoS Genet. 2012, 8:e1002938.
    • (2012) PLoS Genet. , vol.8
    • Cox, S.G.1
  • 97
    • 58149242430 scopus 로고    scopus 로고
    • WSTF regulates the H2A.X. DNA damage response via a novel tyrosine kinase activity
    • Xiao A., et al. WSTF regulates the H2A.X. DNA damage response via a novel tyrosine kinase activity. Nature 2009, 457:57-62.
    • (2009) Nature , vol.457 , pp. 57-62
    • Xiao, A.1
  • 98
    • 70349975711 scopus 로고    scopus 로고
    • JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin
    • Dawson M.A., et al. JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin. Nature 2009, 461:819-822.
    • (2009) Nature , vol.461 , pp. 819-822
    • Dawson, M.A.1
  • 99
    • 63849187827 scopus 로고    scopus 로고
    • Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions
    • Cook P.J., et al. Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions. Nature 2009, 458:591-596.
    • (2009) Nature , vol.458 , pp. 591-596
    • Cook, P.J.1
  • 100
    • 52449114574 scopus 로고    scopus 로고
    • Ataxia-telangiectasia: from a rare disorder to a paradigm for cell signalling and cancer
    • Lavin M.F. Ataxia-telangiectasia: from a rare disorder to a paradigm for cell signalling and cancer. Nat. Rev. Mol. Cell Biol. 2008, 9:759-769.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 759-769
    • Lavin, M.F.1
  • 101
    • 51649110069 scopus 로고    scopus 로고
    • Heterochromatin links to centromeric protection by recruiting shugoshin
    • Yamagishi Y., et al. Heterochromatin links to centromeric protection by recruiting shugoshin. Nature 2008, 455:251-255.
    • (2008) Nature , vol.455 , pp. 251-255
    • Yamagishi, Y.1
  • 102
    • 34547751335 scopus 로고    scopus 로고
    • HP1alpha guides neuronal fate by timing E2F-targeted genes silencing during terminal differentiation
    • Panteleeva I., et al. HP1alpha guides neuronal fate by timing E2F-targeted genes silencing during terminal differentiation. EMBO J. 2007, 26:3616-3628.
    • (2007) EMBO J. , vol.26 , pp. 3616-3628
    • Panteleeva, I.1
  • 103
    • 84866891646 scopus 로고    scopus 로고
    • Three distinct patterns of histone H3Y41 phosphorylation mark active genes
    • Dawson M.A., et al. Three distinct patterns of histone H3Y41 phosphorylation mark active genes. Cell Rep. 2012, 2s:470-477.
    • (2012) Cell Rep. , vol.2 S , pp. 470-477
    • Dawson, M.A.1
  • 104
    • 78650516974 scopus 로고    scopus 로고
    • LIF-independent JAK signalling to chromatin in embryonic stem cells uncovered from an adult stem cell disease
    • Griffiths D.S., et al. LIF-independent JAK signalling to chromatin in embryonic stem cells uncovered from an adult stem cell disease. Nat. Cell Biol. 2011, 13:13-21.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 13-21
    • Griffiths, D.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.