메뉴 건너뛰기




Volumn 6, Issue 1, 2011, Pages

A specific inhibitor of protein kinase CK2 delays gamma-H2Ax foci removal and reduces clonogenic survival of irradiated mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

4',6 DIAMIDINO 2 PHENYLINDOLE; 4,5,6,7 TETRABROMOBENZOTRIAZOLE; CASEIN KINASE II; DNA FRAGMENT; HISTONE H2AX; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN SERINE THREONINE KINASE INHIBITOR; UNCLASSIFIED DRUG; 4,5,6,7-TETRABROMOBENZOTRIAZOLE; H2AFX PROTEIN, HUMAN; HISTONE; PROTEIN KINASE INHIBITOR; TRIAZOLE DERIVATIVE;

EID: 79751528817     PISSN: None     EISSN: 1748717X     Source Type: Journal    
DOI: 10.1186/1748-717X-6-15     Document Type: Article
Times cited : (21)

References (49)
  • 1
    • 0036568813 scopus 로고    scopus 로고
    • Joining the survival squad: an emerging role for protein kinase CK2
    • 10.1016/S0962-8924(02)02279-1, 12062170
    • Ahmed K, Gerber DA, Cochet C. Joining the survival squad: an emerging role for protein kinase CK2. Trends Cell Biol 2002, 12:226-230. 10.1016/S0962-8924(02)02279-1, 12062170.
    • (2002) Trends Cell Biol , vol.12 , pp. 226-230
    • Ahmed, K.1    Gerber, D.A.2    Cochet, C.3
  • 2
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: structure, regulation and role in cellular decisions of life and death
    • Litchfield DW. Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem J 2003, 269:1-15.
    • (2003) Biochem J , vol.269 , pp. 1-15
    • Litchfield, D.W.1
  • 3
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • 10.1096/fj.02-0473rev, 12631575
    • Meggio F, Pinna LA. One-thousand-and-one substrates of protein kinase CK2?. FASEB J 2003, 17:349-368. 10.1096/fj.02-0473rev, 12631575.
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 4
    • 0037151103 scopus 로고    scopus 로고
    • Unique activation mechanism of protein kinase CK2. The N-terminal segment is essential for constitutive activity of the catalytic subunit but not of the holoenzyme
    • 10.1074/jbc.M200486200, 11956194
    • Sarno S, Ghisellini P, Pinna LA. Unique activation mechanism of protein kinase CK2. The N-terminal segment is essential for constitutive activity of the catalytic subunit but not of the holoenzyme. J Biol Chem 2002, 277:22509-22514. 10.1074/jbc.M200486200, 11956194.
    • (2002) J Biol Chem , vol.277 , pp. 22509-22514
    • Sarno, S.1    Ghisellini, P.2    Pinna, L.A.3
  • 5
    • 1542409972 scopus 로고    scopus 로고
    • Protein kinase CK2 as regulator of cell survival: implications for cancer therapy
    • 10.2174/1568009043481687, 14965269
    • Unger GM, Davis AT, Slaton JW, Ahmed K. Protein kinase CK2 as regulator of cell survival: implications for cancer therapy. Curr Cancer Drug Targets 2004, 4:77-84. 10.2174/1568009043481687, 14965269.
    • (2004) Curr Cancer Drug Targets , vol.4 , pp. 77-84
    • Unger, G.M.1    Davis, A.T.2    Slaton, J.W.3    Ahmed, K.4
  • 6
    • 50649124915 scopus 로고    scopus 로고
    • Protein kinase CK2 - a key suppressor of apoptosis
    • 10.1016/j.advenzreg.2008.04.002, 2593134, 18492491
    • Ahmad KA, Wang G, Unger G, Slaton J, Ahmed K. Protein kinase CK2 - a key suppressor of apoptosis. Adv Enzyme Regul 2008, 48:179-187. 10.1016/j.advenzreg.2008.04.002, 2593134, 18492491.
    • (2008) Adv Enzyme Regul , vol.48 , pp. 179-187
    • Ahmad, K.A.1    Wang, G.2    Unger, G.3    Slaton, J.4    Ahmed, K.5
  • 7
    • 38349116517 scopus 로고    scopus 로고
    • Too much of a good thing: the role of protein kinase CK2 in tumorgenesis and prospects for therapeutic inhibition of CK2
    • Duncan JS, Litchfield DW. Too much of a good thing: the role of protein kinase CK2 in tumorgenesis and prospects for therapeutic inhibition of CK2. Biochim Biophys Acta 2008, 1784:33-47.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 33-47
    • Duncan, J.S.1    Litchfield, D.W.2
  • 8
    • 0034707047 scopus 로고    scopus 로고
    • The DNA damage response: putting checkpoints in perspective
    • 10.1038/35044005, 11100718
    • Zhou SB, Elledge SJ. The DNA damage response: putting checkpoints in perspective. Nature 2000, 408:433-439. 10.1038/35044005, 11100718.
    • (2000) Nature , vol.408 , pp. 433-439
    • Zhou, S.B.1    Elledge, S.J.2
  • 9
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-strand breaks induce histone H2AX phosphorylation on serine 139
    • 10.1074/jbc.273.10.5858, 9488723
    • Rogaku EP, Boon C, Redon C, Bonner WM. DNA double-strand breaks induce histone H2AX phosphorylation on serine 139. J Biol Chem 1998, 273:5858-5868. 10.1074/jbc.273.10.5858, 9488723.
    • (1998) J Biol Chem , vol.273 , pp. 5858-5868
    • Rogaku, E.P.1    Boon, C.2    Redon, C.3    Bonner, W.M.4
  • 10
    • 55249116558 scopus 로고    scopus 로고
    • γ-H2AX in recognition and signaling of DNA double-strand breaks in the context of chromatin
    • 10.1093/nar/gkn550, 2553572, 18772227
    • Kinner A, Wu W, Staudt C, Iliakis G. γ-H2AX in recognition and signaling of DNA double-strand breaks in the context of chromatin. Nucl Acids Res 2008, 36:5678-5694. 10.1093/nar/gkn550, 2553572, 18772227.
    • (2008) Nucl Acids Res , vol.36 , pp. 5678-5694
    • Kinner, A.1    Wu, W.2    Staudt, C.3    Iliakis, G.4
  • 11
    • 59849089955 scopus 로고    scopus 로고
    • Repair of ionizing radiation-induced DNA double-strand breaks by non-homologous end-joining
    • 10.1042/BJ20080413, 2975036, 19133841
    • Mahaney B, Meek K, Lees-Miller SP. Repair of ionizing radiation-induced DNA double-strand breaks by non-homologous end-joining. Biochem J 2009, 417:639-650. 10.1042/BJ20080413, 2975036, 19133841.
    • (2009) Biochem J , vol.417 , pp. 639-650
    • Mahaney, B.1    Meek, K.2    Lees-Miller, S.P.3
  • 12
    • 6344238643 scopus 로고    scopus 로고
    • Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV
    • 10.1038/sj.emboj.7600375, 522785, 15385968
    • Koch CA, Agyei R, Galicia S, Metalnikov P, O'Donnell P, Starostine A, Weinfeld M, Durocher D. Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV. EMBO J 2004, 23:3874-3885. 10.1038/sj.emboj.7600375, 522785, 15385968.
    • (2004) EMBO J , vol.23 , pp. 3874-3885
    • Koch, C.A.1    Agyei, R.2    Galicia, S.3    Metalnikov, P.4    O'Donnell, P.5    Starostine, A.6    Weinfeld, M.7    Durocher, D.8
  • 14
    • 42449086413 scopus 로고    scopus 로고
    • Phosphorylation of SDT repeats in the MDC1 N terminus triggers retention of NBS1 at the DNA damage-modified chromatin
    • 10.1083/jcb.200708210, 2315670, 18411307
    • Melander F, Bekker-Jensen S, Falck J, Bartek J, Mailand N, Lukas J. Phosphorylation of SDT repeats in the MDC1 N terminus triggers retention of NBS1 at the DNA damage-modified chromatin. J Cell Biol 2008, 181:213-226. 10.1083/jcb.200708210, 2315670, 18411307.
    • (2008) J Cell Biol , vol.181 , pp. 213-226
    • Melander, F.1    Bekker-Jensen, S.2    Falck, J.3    Bartek, J.4    Mailand, N.5    Lukas, J.6
  • 15
    • 42449115711 scopus 로고    scopus 로고
    • Constitutive phosphorylation of MDC1 physically links the MRE11-RAD50-NBS1 complex to damaged chromatin
    • 10.1083/jcb.200709008, 2315671, 18411308
    • Spycher C, Miller ES, Townsend K, Pavic L, Morrice NA, Janscak P, Stewart GS, Stucki M. Constitutive phosphorylation of MDC1 physically links the MRE11-RAD50-NBS1 complex to damaged chromatin. J Cell Biol 2008, 181:227-240. 10.1083/jcb.200709008, 2315671, 18411308.
    • (2008) J Cell Biol , vol.181 , pp. 227-240
    • Spycher, C.1    Miller, E.S.2    Townsend, K.3    Pavic, L.4    Morrice, N.A.5    Janscak, P.6    Stewart, G.S.7    Stucki, M.8
  • 16
    • 48649100438 scopus 로고    scopus 로고
    • Phospho-dependent interactions between NBS1 and MDC1 mediate chromatin retention of the MRN complex at sites of DNA damage
    • 10.1038/embor.2008.103, 2442910, 18583988
    • Chapman JR, Jackson SP. Phospho-dependent interactions between NBS1 and MDC1 mediate chromatin retention of the MRN complex at sites of DNA damage. EMBO reports 2008, 9:795-801. 10.1038/embor.2008.103, 2442910, 18583988.
    • (2008) EMBO reports , vol.9 , pp. 795-801
    • Chapman, J.R.1    Jackson, S.P.2
  • 17
    • 3242891189 scopus 로고    scopus 로고
    • The Mre11 complex and the metabolism of chromosome breaks: the importance of communicating and holding things together
    • 10.1016/j.dnarep.2004.03.014, 15279769
    • Stracker TH, Theunissen JW, Morales M, Petrini JH. The Mre11 complex and the metabolism of chromosome breaks: the importance of communicating and holding things together. DNA Repair 2004, 3:845-854. 10.1016/j.dnarep.2004.03.014, 15279769.
    • (2004) DNA Repair , vol.3 , pp. 845-854
    • Stracker, T.H.1    Theunissen, J.W.2    Morales, M.3    Petrini, J.H.4
  • 18
    • 49649089537 scopus 로고    scopus 로고
    • MDC1 regulates intra-S-phase checkpoint by targeting NBS1 to DNA double-strand breaks
    • 10.1073/pnas.0802885105, 2516250, 18678890
    • Wu L, Luo K, Lou Z, Chen J. MDC1 regulates intra-S-phase checkpoint by targeting NBS1 to DNA double-strand breaks. Proc Natl Acad Sci USA 2008, 105:11200-11205. 10.1073/pnas.0802885105, 2516250, 18678890.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11200-11205
    • Wu, L.1    Luo, K.2    Lou, Z.3    Chen, J.4
  • 19
    • 44449136965 scopus 로고    scopus 로고
    • HP1-β mobilization promotes chromatin changes that initiate the DNA damage response
    • 10.1038/nature06875, 18438399
    • Ayoub N, Jeyasekharan AD, Bernal JA, Venkitaraman AR. HP1-β mobilization promotes chromatin changes that initiate the DNA damage response. Nature 2008, 453:682-686. 10.1038/nature06875, 18438399.
    • (2008) Nature , vol.453 , pp. 682-686
    • Ayoub, N.1    Jeyasekharan, A.D.2    Bernal, J.A.3    Venkitaraman, A.R.4
  • 20
    • 44349122537 scopus 로고    scopus 로고
    • HP1: a functionally multifaceted protein
    • 10.1016/j.gde.2008.01.009, 18329871
    • Fanti L, Pimpinelli S. HP1: a functionally multifaceted protein. Curr Opin Genet Dev 2008, 18:169-174. 10.1016/j.gde.2008.01.009, 18329871.
    • (2008) Curr Opin Genet Dev , vol.18 , pp. 169-174
    • Fanti, L.1    Pimpinelli, S.2
  • 21
    • 70349336104 scopus 로고    scopus 로고
    • Cellular functions of protein kinase CK2: a dynamic affair
    • 10.1007/s00018-009-9151-1, 19387551
    • Filhol O, Cochet C. Cellular functions of protein kinase CK2: a dynamic affair. Cell Mol Life Sci 2009, 66:1830-1839. 10.1007/s00018-009-9151-1, 19387551.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1830-1839
    • Filhol, O.1    Cochet, C.2
  • 22
    • 20144370844 scopus 로고    scopus 로고
    • CK2 inhibits apoptosis and changes ist cellular localisation following ionizing radiation
    • 10.1158/0008-5472.CAN-04-3941, 15899828
    • Yamane K, Kinsella TJ. CK2 inhibits apoptosis and changes ist cellular localisation following ionizing radiation. Cancer Res 2005, 65:4362-4367. 10.1158/0008-5472.CAN-04-3941, 15899828.
    • (2005) Cancer Res , vol.65 , pp. 4362-4367
    • Yamane, K.1    Kinsella, T.J.2
  • 24
    • 0035099457 scopus 로고    scopus 로고
    • Overexpression of the DNA-binding domain of poly(ADP-ribose) polymerase inhibits rejoining of ionizing radiation-induced DNA-double-strand breaks
    • 10.1080/09553000010009026, 11258844
    • Rudat V, Bachmann N, Kuepper JH, Weber KJ. Overexpression of the DNA-binding domain of poly(ADP-ribose) polymerase inhibits rejoining of ionizing radiation-induced DNA-double-strand breaks. Int J Radiat Biol 2001, 77:303-307. 10.1080/09553000010009026, 11258844.
    • (2001) Int J Radiat Biol , vol.77 , pp. 303-307
    • Rudat, V.1    Bachmann, N.2    Kuepper, J.H.3    Weber, K.J.4
  • 25
    • 0036896782 scopus 로고    scopus 로고
    • Suppression of apoptosis and clonogenic survival in irradiated human lymphoblasts with different TP53 status
    • Schäfer J, Bachtler J, Engling A, Little JB, Weber KJ, Wenz F. Suppression of apoptosis and clonogenic survival in irradiated human lymphoblasts with different TP53 status. Radiat Res 2002, 158:699-706.
    • (2002) Radiat Res , vol.158 , pp. 699-706
    • Schäfer, J.1    Bachtler, J.2    Engling, A.3    Little, J.B.4    Weber, K.J.5    Wenz, F.6
  • 27
    • 63249109714 scopus 로고    scopus 로고
    • Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK
    • Ali AAE, Jukes RM, Pearl LH, Oliver AW. Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK. Nucleic Acids Research 2009, 1-12.
    • (2009) Nucleic Acids Research , pp. 1-12
    • Ali, A.A.E.1    Jukes, R.M.2    Pearl, L.H.3    Oliver, A.W.4
  • 28
    • 77953364327 scopus 로고    scopus 로고
    • XRCC1 phosphorylation by CK2 is required for its stability and efficient DNA repair
    • 10.1016/j.dnarep.2010.04.008, 20471329
    • Parson JL, Dianova II, Finch D, Tait PS, Ström CE, Helleday T, Dianov GL. XRCC1 phosphorylation by CK2 is required for its stability and efficient DNA repair. DNA Repair 2010, 9:835-841. 10.1016/j.dnarep.2010.04.008, 20471329.
    • (2010) DNA Repair , vol.9 , pp. 835-841
    • Parson, J.L.1    Dianova, I.I.2    Finch, D.3    Tait, P.S.4    Ström, C.E.5    Helleday, T.6    Dianov, G.L.7
  • 29
    • 0036271813 scopus 로고    scopus 로고
    • Rejoining of radiation-induced DNA double-strand breaks: pulsed-field electrophoresis analysis of fragment size distributions after incubation for repair
    • 10.1667/0033-7587(2002)157[0721:RORIDD]2.0.CO;2, 12005552
    • Gauter B, Zlobinskaya O, Weber KJ. Rejoining of radiation-induced DNA double-strand breaks: pulsed-field electrophoresis analysis of fragment size distributions after incubation for repair. Radiat Res 2002, 157:721-733. 10.1667/0033-7587(2002)157[0721:RORIDD]2.0.CO;2, 12005552.
    • (2002) Radiat Res , vol.157 , pp. 721-733
    • Gauter, B.1    Zlobinskaya, O.2    Weber, K.J.3
  • 30
    • 0037372948 scopus 로고    scopus 로고
    • Cell cycle dependent regulation of protein kinase CK2 signaling to the nuclear matrix
    • 10.1002/jcb.10438, 12577315
    • Wang H, Yu S, Davis AT, Ahmed K. Cell cycle dependent regulation of protein kinase CK2 signaling to the nuclear matrix. J Cell Biochem 2003, 88:812-22. 10.1002/jcb.10438, 12577315.
    • (2003) J Cell Biochem , vol.88 , pp. 812-822
    • Wang, H.1    Yu, S.2    Davis, A.T.3    Ahmed, K.4
  • 31
    • 33947277697 scopus 로고    scopus 로고
    • Mdm2: p53's lifesaver?
    • 10.1016/j.molcel.2007.03.006, 17386256
    • Shmueli A, Oren M. Mdm2: p53's lifesaver?. Mol Cell 2007, 25:794-796. 10.1016/j.molcel.2007.03.006, 17386256.
    • (2007) Mol Cell , vol.25 , pp. 794-796
    • Shmueli, A.1    Oren, M.2
  • 32
    • 0037093352 scopus 로고    scopus 로고
    • Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoetic lineage cell-specific protein 1 (HS1) in Jurkat cells
    • 1222543, 11988074
    • Ruzzene M, Penzo D, Pinna LA. Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoetic lineage cell-specific protein 1 (HS1) in Jurkat cells. Biochem J 2002, 364:41-47. 1222543, 11988074.
    • (2002) Biochem J , vol.364 , pp. 41-47
    • Ruzzene, M.1    Penzo, D.2    Pinna, L.A.3
  • 33
    • 73449102163 scopus 로고    scopus 로고
    • P53 is dispensable for the induction of apoptosis after inhibition of protein kinase CK2
    • Schneider CC, Hessenauer A, Montenarh M, Götz C. p53 is dispensable for the induction of apoptosis after inhibition of protein kinase CK2. Prostate 2009, 70:126-134.
    • (2009) Prostate , vol.70 , pp. 126-134
    • Schneider, C.C.1    Hessenauer, A.2    Montenarh, M.3    Götz, C.4
  • 35
    • 47349107760 scopus 로고    scopus 로고
    • ATM signaling facilitates repair of DNA double-strand breaks associated with heterochromatin
    • 10.1016/j.molcel.2008.05.017, 18657500
    • Goodarzi AA, Noon AT, Deckbar D, Ziv Y, Shiloh Y, Löbrich M, Jeggo PA. ATM signaling facilitates repair of DNA double-strand breaks associated with heterochromatin. Mol Cell 2008, 31:167-177. 10.1016/j.molcel.2008.05.017, 18657500.
    • (2008) Mol Cell , vol.31 , pp. 167-177
    • Goodarzi, A.A.1    Noon, A.T.2    Deckbar, D.3    Ziv, Y.4    Shiloh, Y.5    Löbrich, M.6    Jeggo, P.A.7
  • 36
    • 67749093497 scopus 로고    scopus 로고
    • The impact of heterochromatin on DSB repair
    • 10.1042/BST0370569, 19442252
    • Goodarzi AA, Noon AT, Jeggo PA. The impact of heterochromatin on DSB repair. Biochem Soc Trans 2009, 37:569-576. 10.1042/BST0370569, 19442252.
    • (2009) Biochem Soc Trans , vol.37 , pp. 569-576
    • Goodarzi, A.A.1    Noon, A.T.2    Jeggo, P.A.3
  • 37
    • 75949122330 scopus 로고    scopus 로고
    • 53BP1-dependent robust localized KAP-1 phosphorylation is essential for heterochromatic DNA double-strand break repair
    • Noon AT, Shibata A, Rief N, Löbrich M, Stewart GS, Jeggo PA, Goodarzi AA. 53BP1-dependent robust localized KAP-1 phosphorylation is essential for heterochromatic DNA double-strand break repair. Nat Cell Biol 2010, 12:1-8.
    • (2010) Nat Cell Biol , vol.12 , pp. 1-8
    • Noon, A.T.1    Shibata, A.2    Rief, N.3    Löbrich, M.4    Stewart, G.S.5    Jeggo, P.A.6    Goodarzi, A.A.7
  • 38
    • 28444483130 scopus 로고    scopus 로고
    • γ-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA double-strand break repair
    • 10.1016/j.molcel.2005.10.003, 16310392
    • Chowdhury D, Keogh MC, Ishii H, Peterson CL, Buratowski S, Lieberman J. γ-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA double-strand break repair. Mol Cell 2005, 20:801-809. 10.1016/j.molcel.2005.10.003, 16310392.
    • (2005) Mol Cell , vol.20 , pp. 801-809
    • Chowdhury, D.1    Keogh, M.C.2    Ishii, H.3    Peterson, C.L.4    Buratowski, S.5    Lieberman, J.6
  • 40
    • 33646769992 scopus 로고    scopus 로고
    • The loss of γH2AX signal is a marker of DNA double strand breaks repair only at low levels of DNA damage
    • 10.4161/cc.5.10.2799, 16721046
    • Bouquet F, Muller C, Salles B. The loss of γH2AX signal is a marker of DNA double strand breaks repair only at low levels of DNA damage. Cell Cycle 2006, 5:1116-1122. 10.4161/cc.5.10.2799, 16721046.
    • (2006) Cell Cycle , vol.5 , pp. 1116-1122
    • Bouquet, F.1    Muller, C.2    Salles, B.3
  • 42
    • 34248576179 scopus 로고    scopus 로고
    • Elimination of radiation-induced γH2AX foci in mammalian nucleus can occur by histone exchange
    • 10.1016/j.bbrc.2007.04.188, 17498657
    • Svetlova M, Solovjeva L, Nishi K, Nazarov I, Siino J, Tomilin N. Elimination of radiation-induced γH2AX foci in mammalian nucleus can occur by histone exchange. Biochem Biophys Res Comm 2007, 358:650-654. 10.1016/j.bbrc.2007.04.188, 17498657.
    • (2007) Biochem Biophys Res Comm , vol.358 , pp. 650-654
    • Svetlova, M.1    Solovjeva, L.2    Nishi, K.3    Nazarov, I.4    Siino, J.5    Tomilin, N.6
  • 43
    • 25444490915 scopus 로고    scopus 로고
    • Induction and repair of DNA double-strand breaks in human cells: dephosphorylation of histone H2AX and its inhibition by calyculin A
    • 10.1667/RR3379.1, 16187759
    • Antonelli F, Belli M, Cuttone G, Dini V, Esposito G, Simone G, Sorrentino E, Tabocchini MA. Induction and repair of DNA double-strand breaks in human cells: dephosphorylation of histone H2AX and its inhibition by calyculin A. Radiat Res 2005, 164:514-517. 10.1667/RR3379.1, 16187759.
    • (2005) Radiat Res , vol.164 , pp. 514-517
    • Antonelli, F.1    Belli, M.2    Cuttone, G.3    Dini, V.4    Esposito, G.5    Simone, G.6    Sorrentino, E.7    Tabocchini, M.A.8
  • 44
    • 0032983271 scopus 로고    scopus 로고
    • How does radiation kill cells?
    • 10.1016/S1367-5931(99)80014-3, 10021401
    • Cohen-Jonathan E, Bernhard EJ, McKenna WG. How does radiation kill cells?. Curr Opin Chem Biol 1999, 3:77-83. 10.1016/S1367-5931(99)80014-3, 10021401.
    • (1999) Curr Opin Chem Biol , vol.3 , pp. 77-83
    • Cohen-Jonathan, E.1    Bernhard, E.J.2    McKenna, W.G.3
  • 45
    • 0033014858 scopus 로고    scopus 로고
    • Regulation of p53 mediated transactivation by the β-subunit of protein kinase CK2
    • 10.1016/S0014-5793(99)00273-2, 10214938
    • Schuster N, Prowald A, Schneider E, Scheidtmann KH, Montenarh M. Regulation of p53 mediated transactivation by the β-subunit of protein kinase CK2. FEBS Letters 1999, 447:160-166. 10.1016/S0014-5793(99)00273-2, 10214938.
    • (1999) FEBS Letters , vol.447 , pp. 160-166
    • Schuster, N.1    Prowald, A.2    Schneider, E.3    Scheidtmann, K.H.4    Montenarh, M.5
  • 46
    • 0033059744 scopus 로고    scopus 로고
    • Protein kinase CK2-dependent regulation of p53 function: evidence that the phosphorylation status of the serine 386 (CK2) site of p53 is constitutive and stable
    • McKendrick L, Milne D, Meek D. Protein kinase CK2-dependent regulation of p53 function: evidence that the phosphorylation status of the serine 386 (CK2) site of p53 is constitutive and stable. Mol Cell Biochem 1999, 191:197-199.
    • (1999) Mol Cell Biochem , vol.191 , pp. 197-199
    • McKendrick, L.1    Milne, D.2    Meek, D.3
  • 48
    • 2942556504 scopus 로고    scopus 로고
    • Mutation of a CK2 phosphorylation site in cdc25C impairs importin α/β binding and results in cytoplasmic retention
    • 10.1038/sj.onc.1207566, 15064744
    • Schwindling SL, Noll A, Montenarh M, Götz C. Mutation of a CK2 phosphorylation site in cdc25C impairs importin α/β binding and results in cytoplasmic retention. Oncogene 2004, 23:4155-4165. 10.1038/sj.onc.1207566, 15064744.
    • (2004) Oncogene , vol.23 , pp. 4155-4165
    • Schwindling, S.L.1    Noll, A.2    Montenarh, M.3    Götz, C.4
  • 49
    • 50349086574 scopus 로고    scopus 로고
    • Regulation of intra-S phase checkpoint by ionizingradiation (IR)-dependent and IR-independent phosphorylation of SMC3
    • Luo H, Li Y, Mu JJ, Zhang J, Tonaka T, Hamamori Y, Jung SY, Wang Y, Qin J. Regulation of intra-S phase checkpoint by ionizingradiation (IR)-dependent and IR-independent phosphorylation of SMC3. JBC 2008, 283:19176-19183.
    • (2008) JBC , vol.283 , pp. 19176-19183
    • Luo, H.1    Li, Y.2    Mu, J.J.3    Zhang, J.4    Tonaka, T.5    Hamamori, Y.6    Jung, S.Y.7    Wang, Y.8    Qin, J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.