메뉴 건너뛰기




Volumn 11, Issue 3, 2010, Pages 184-198

Regulation of the DNA damage response to DSBs by post-translational modifications

Author keywords

Cell cycle arrest; DNA double strand breaks; Homologous recombination; Non homologous endjoining; Post translational modifications

Indexed keywords

APOPTOSIS; ARTICLE; CELL CYCLE ARREST; DNA DAMAGE; DNA MODIFICATION; DNA REPAIR; DOUBLE STRANDED DNA BREAK; RNA TRANSLATION; SIGNAL TRANSDUCTION;

EID: 77952526095     PISSN: 13892029     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920210791110979     Document Type: Article
Times cited : (24)

References (184)
  • 1
    • 0035961198 scopus 로고    scopus 로고
    • DNA repair mechanisms
    • Hoeijmakers, J.H. DNA repair mechanisms. Maturitas, 2001, 38, 17-22.
    • (2001) Maturitas , vol.38 , pp. 17-22
    • Hoeijmakers, J.H.1
  • 2
    • 0035093737 scopus 로고    scopus 로고
    • DNA double-strand breaks: Signaling, repair and the cancer connection
    • Khanna, K.K.; Jackson, S.P. DNA double-strand breaks: signaling, repair and the cancer connection. Nat. Genet., 2001, 27, 247-254.
    • (2001) Nat. Genet , vol.27 , pp. 247-254
    • Khanna, K.K.1    Jackson, S.P.2
  • 3
    • 33747188326 scopus 로고    scopus 로고
    • Initiation of meiotic recombination by formation of DNA double-strand breaks: Mechanism and regulation
    • Keeney, S.; Neale, M.J. Initiation of meiotic recombination by formation of DNA double-strand breaks: mechanism and regulation. Biochem. Soc. Trans., 2006, 34, 523-525.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 523-525
    • Keeney, S.1    Neale, M.J.2
  • 4
    • 41149132841 scopus 로고    scopus 로고
    • Fixing DNA breaks during class switch recombination
    • Jolly, C.J.; Cook, A.J.; Manis, J.P. Fixing DNA breaks during class switch recombination. J. Exp. Med., 2008, 205, 509-513.
    • (2008) J. Exp. Med , vol.205 , pp. 509-513
    • Jolly, C.J.1    Cook, A.J.2    Manis, J.P.3
  • 5
    • 33847625356 scopus 로고    scopus 로고
    • Base damage and single-strand break repair: Mechanisms and functional significance of short- and longpatch repair subpathways
    • Fortini, P.; Dogliotti, E. Base damage and single-strand break repair: mechanisms and functional significance of short- and longpatch repair subpathways. DNA Repair (Amst), 2007, 6, 398-409.
    • (2007) DNA Repair (Amst) , vol.6 , pp. 398-409
    • Fortini, P.1    Dogliotti, E.2
  • 6
    • 62349131315 scopus 로고    scopus 로고
    • DNA repair in mammalian cells: Nucleotide excision repair: Variations on versatility
    • Nouspikel, T. DNA repair in mammalian cells: Nucleotide excision repair: variations on versatility. Cell Mol. Life Sci., 2009, 66, 994-1009.
    • (2009) Cell Mol. Life Sci , vol.66 , pp. 994-1009
    • Nouspikel, T.1
  • 7
    • 45449103427 scopus 로고    scopus 로고
    • DNA mismatch repair: Molecular mechanism, cancer, and ageing
    • Hsieh, P.; Yamane, K. DNA mismatch repair: molecular mechanism, cancer, and ageing. Mech. Ageing Dev., 2008, 129, 391-407.
    • (2008) Mech. Ageing Dev , vol.129 , pp. 391-407
    • Hsieh, P.1    Yamane, K.2
  • 8
    • 66249102308 scopus 로고    scopus 로고
    • Multisite protein phosphorylation-from molecular mechanisms to kinetic models
    • Salazar, C.; Hofer, T. Multisite protein phosphorylation-from molecular mechanisms to kinetic models. FEBS J., 2009, 276, 3177-3198.
    • (2009) FEBS J , vol.276 , pp. 3177-3198
    • Salazar, C.1    Hofer, T.2
  • 9
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: Mechanism through structure
    • Shi, Y. Serine/threonine phosphatases: mechanism through structure. Cell, 2009, 139, 468-484.
    • (2009) Cell , vol.139 , pp. 468-484
    • Shi, Y.1
  • 10
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides, T. Acetylation: a regulatory modification to rival phosphorylation? EMBO J., 2000, 19, 1176-1179.
    • (2000) EMBO J , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 11
    • 33847678615 scopus 로고    scopus 로고
    • Historical review: The field of protein methylation
    • Paik, W.K.; Paik, D.C.; Kim, S. Historical review: the field of protein methylation. Trends Biochem. Sci., 2007, 32, 146-152.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 146-152
    • Paik, W.K.1    Paik, D.C.2    Kim, S.3
  • 12
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • Gu, W.; Roeder, R.G. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell, 1997, 90, 595-606.
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 14
    • 0023768491 scopus 로고
    • Ubiquitin-mediated protein degradation
    • Hershko, A. Ubiquitin-mediated protein degradation. J. Biol. Chem., 1988, 263, 15237-15240.
    • (1988) J. Biol. Chem , vol.263 , pp. 15237-15240
    • Hershko, A.1
  • 15
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher, O.; Felberbaum, R.; Hochstrasser, M. Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu. Rev. Cell Dev. Biol., 2006, 22, 159-180.
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 16
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser, M. Origin and function of ubiquitin-like proteins. Nature, 2009, 458, 422-429.
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 17
    • 71749086813 scopus 로고    scopus 로고
    • The ubiquitin pathway: An emerging drug target in cancer therapy
    • Ande, S.R.; Chen, J.; Maddika, S. The ubiquitin pathway: An emerging drug target in cancer therapy. Eur. J. Pharmacol., 2009, 625(1-3), 199-205
    • (2009) Eur. J. Pharmacol , vol.625 , Issue.1-3 , pp. 199-205
    • Ande, S.R.1    Chen, J.2    Maddika, S.3
  • 18
    • 33750529154 scopus 로고    scopus 로고
    • Working out coupled monoubiquitination
    • Haglund, K.; Stenmark, H. Working out coupled monoubiquitination. Nat. Cell Biol., 2006, 8, 1218-1219.
    • (2006) Nat. Cell Biol , vol.8 , pp. 1218-1219
    • Haglund, K.1    Stenmark, H.2
  • 19
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series
    • Ikeda, F.; Dikic, I. Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series. EMBO Rep., 2008, 9, 536-542.
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 20
    • 34248379575 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins in protein regulation
    • Herrmann, J.; Lerman, L.O.; Lerman, A. Ubiquitin and ubiquitin-like proteins in protein regulation. Circ. Res., 2007, 100, 1276-1291.
    • (2007) Circ. Res , vol.100 , pp. 1276-1291
    • Herrmann, J.1    Lerman, L.O.2    Lerman, A.3
  • 21
    • 60549107173 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome
    • Saeki, Y.; Kudo, T.; Sone, T.; Kikuchi, Y.; Yokosawa, H.; Toh-e A; Tanaka, K. Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome. EMBO J., 2009, 28, 359-371.
    • (2009) EMBO J , vol.28 , pp. 359-371
    • Saeki, Y.1    Kudo, T.2    Sone, T.3    Kikuchi, Y.4    Yokosawa, H.5    Toh-E, A.6    Tanaka, K.7
  • 22
    • 36749025467 scopus 로고    scopus 로고
    • Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage
    • Wang, B.; Elledge, S.J. Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage. Proc. Natl. Acad. Sci. USA, 2007, 104, 20759-20763.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20759-20763
    • Wang, B.1    Elledge, S.J.2
  • 23
    • 33750530169 scopus 로고    scopus 로고
    • Itch/AIP4 mediates Deltex degradation through the formation of K29-linked polyubiquitin chains
    • Chastagner, P.; Israel, A.; Brou, C. Itch/AIP4 mediates Deltex degradation through the formation of K29-linked polyubiquitin chains. EMBO Rep., 2006, 7, 1147-1153.
    • (2006) EMBO Rep , vol.7 , pp. 1147-1153
    • Chastagner, P.1    Israel, A.2    Brou, C.3
  • 24
    • 34547130325 scopus 로고    scopus 로고
    • Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages
    • Kim, H.T.; Kim, K.P.; Lledias, F.; Kisselev, A.F.; Scaglione, K.M.; Skowyra, D.; Gygi, S.P.; Goldberg, A.L. Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages. J. Biol. Chem., 2007, 282, 17375-17386.
    • (2007) J. Biol. Chem , vol.282 , pp. 17375-17386
    • Kim, H.T.1    Kim, K.P.2    Lledias, F.3    Kisselev, A.F.4    Scaglione, K.M.5    Skowyra, D.6    Gygi, S.P.7    Goldberg, A.L.8
  • 25
    • 65249173891 scopus 로고    scopus 로고
    • The multiple layers of ubiquitin-dependent cell cycle control
    • Wickliffe, K.; Williamson, A.; Jin, L.; Rape, M. The multiple layers of ubiquitin-dependent cell cycle control. Chem. Rev., 2009, 109, 1537-1548.
    • (2009) Chem. Rev , vol.109 , pp. 1537-1548
    • Wickliffe, K.1    Williamson, A.2    Jin, L.3    Rape, M.4
  • 26
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay, R.T. SUMO: a history of modification. Mol. Cell, 2005, 18, 1-12.
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 27
    • 37749006669 scopus 로고    scopus 로고
    • Signalling pathways and the regulation of SUMO modification
    • Guo, B.; Yang, S.H.; Witty, J.; Sharrocks, A.D. Signalling pathways and the regulation of SUMO modification. Biochem. Soc. Trans., 2007, 35, 1414-1418.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1414-1418
    • Guo, B.1    Yang, S.H.2    Witty, J.3    Sharrocks, A.D.4
  • 28
    • 20444384040 scopus 로고    scopus 로고
    • Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex
    • Reverter, D.; Lima, C.D. Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature, 2005, 435, 687-692.
    • (2005) Nature , vol.435 , pp. 687-692
    • Reverter, D.1    Lima, C.D.2
  • 29
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and Ran-GAP1
    • Bernier-Villamor, V.; Sampson, D.A.; Matunis, M.J.; Lima, C.D. Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and Ran-GAP1. Cell, 2002, 108, 345-356.
    • (2002) Cell , vol.108 , pp. 345-356
    • Bernier-Villamor, V.1    Sampson, D.A.2    Matunis, M.J.3    Lima, C.D.4
  • 30
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez, M.S.; Dargemont, C.; Hay, R.T. SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J. Biol. Chem., 2001, 276, 12654-12659.
    • (2001) J. Biol. Chem , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 31
    • 33745360876 scopus 로고    scopus 로고
    • Automated identification of SUMOylation sites using mass spectrometry and SUMmOn pattern recognition software
    • Pedrioli, P.G.; Raught, B.; Zhang, X.D.; Rogers, R.; Aitchison, J.; Matunis, M.; Aebersold, R. Automated identification of SUMOylation sites using mass spectrometry and SUMmOn pattern recognition software. Nat. Methods, 2006, 3, 533-539.
    • (2006) Nat. Methods , vol.3 , pp. 533-539
    • Pedrioli, P.G.1    Raught, B.2    Zhang, X.D.3    Rogers, R.4    Aitchison, J.5    Matunis, M.6    Aebersold, R.7
  • 32
    • 26444593473 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry for the analysis of small ubiquitin-like modifier (SUMO) modification: Identification of lysines in RanBP2 and SUMO targeted for modification during the E3 auto-SUMOylation reaction
    • Cooper, H.J.; Tatham, M.H.; Jaffray, E.; Heath, J.K.; Lam, T.T.; Marshall, A.G.; Hay, R.T. Fourier transform ion cyclotron resonance mass spectrometry for the analysis of small ubiquitin-like modifier (SUMO) modification: identification of lysines in RanBP2 and SUMO targeted for modification during the E3 auto-SUMOylation reaction. Anal. Chem., 2005, 77, 6310-6319.
    • (2005) Anal. Chem , vol.77 , pp. 6310-6319
    • Cooper, H.J.1    Tatham, M.H.2    Jaffray, E.3    Heath, J.K.4    Lam, T.T.5    Marshall, A.G.6    Hay, R.T.7
  • 34
    • 33750439105 scopus 로고    scopus 로고
    • An extended consensus motif enhances the specificity of substrate modification by SUMO
    • Yang, S.H.; Galanis, A.; Witty, J.; Sharrocks, A.D. An extended consensus motif enhances the specificity of substrate modification by SUMO. EMBO J., 2006, 25, 5083-5093.
    • (2006) EMBO J , vol.25 , pp. 5083-5093
    • Yang, S.H.1    Galanis, A.2    Witty, J.3    Sharrocks, A.D.4
  • 35
    • 4344685954 scopus 로고    scopus 로고
    • Association of Ubc9, an E2 ligase for SUMO conjugation, with p53 is regulated by phosphorylation of p53
    • Lin, J.Y.; Ohshima, T.; Shimotohno, K. Association of Ubc9, an E2 ligase for SUMO conjugation, with p53 is regulated by phosphorylation of p53. FEBS Lett., 2004, 573, 15-18.
    • (2004) FEBS Lett , vol.573 , pp. 15-18
    • Lin, J.Y.1    Ohshima, T.2    Shimotohno, K.3
  • 36
    • 0034523266 scopus 로고    scopus 로고
    • SUMO--nonclassical ubiquitin
    • Melchior, F. SUMO--nonclassical ubiquitin. Annu. Rev. Cell Dev. Biol., 2000, 16, 591-626.
    • (2000) Annu. Rev. Cell Dev. Biol , vol.16 , pp. 591-626
    • Melchior, F.1
  • 38
    • 3042644131 scopus 로고    scopus 로고
    • A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus
    • Bohren, K.M.; Nadkarni, V.; Song, J.H.; Gabbay, K.H.; Owerbach, D. A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus. J. Biol. Chem., 2004, 279, 27233-27238.
    • (2004) J. Biol. Chem , vol.279 , pp. 27233-27238
    • Bohren, K.M.1    Nadkarni, V.2    Song, J.H.3    Gabbay, K.H.4    Owerbach, D.5
  • 40
    • 33646353695 scopus 로고    scopus 로고
    • Assembly of a polymeric chain of SUMO1 on human topoisomerase I in vitro
    • Yang, M.; Hsu, C.T.; Ting, C.Y.; Liu, L.F.; Hwang, J. Assembly of a polymeric chain of SUMO1 on human topoisomerase I in vitro. J. Biol. Chem., 2006, 281, 8264-8274.
    • (2006) J. Biol. Chem , vol.281 , pp. 8264-8274
    • Yang, M.1    Hsu, C.T.2    Ting, C.Y.3    Liu, L.F.4    Hwang, J.5
  • 41
    • 53849109540 scopus 로고    scopus 로고
    • Novel substrates and functions for the ubiquitin-like molecule NEDD8
    • Xirodimas, D.P. Novel substrates and functions for the ubiquitin-like molecule NEDD8. Biochem. Soc. Trans., 2008, 36, 802-806.
    • (2008) Biochem. Soc. Trans , vol.36 , pp. 802-806
    • Xirodimas, D.P.1
  • 42
    • 64049106276 scopus 로고    scopus 로고
    • Revisiting the COP9 signalosome as a transcriptional regulator
    • Chamovitz, D.A. Revisiting the COP9 signalosome as a transcriptional regulator. EMBO Rep., 2009, 10, 352-358.
    • (2009) EMBO Rep , vol.10 , pp. 352-358
    • Chamovitz, D.A.1
  • 43
    • 36949026694 scopus 로고    scopus 로고
    • Activation and regulation of ATM kinase activity in response to DNA double-strand breaks
    • Lee, J.H.; Paull, T.T. Activation and regulation of ATM kinase activity in response to DNA double-strand breaks. Oncogene, 2007, 26, 7741-7748.
    • (2007) Oncogene , vol.26 , pp. 7741-7748
    • Lee, J.H.1    Paull, T.T.2
  • 46
    • 0037472924 scopus 로고    scopus 로고
    • DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation
    • Bakkenist, C.J.; Kastan, M.B. DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation. Nature, 2003, 421, 499-506.
    • (2003) Nature , vol.421 , pp. 499-506
    • Bakkenist, C.J.1    Kastan, M.B.2
  • 47
    • 33747614605 scopus 로고    scopus 로고
    • Involvement of novel autophosphorylation sites in ATM activation
    • Kozlov, S.V.; Graham, M.E.; Peng, C.; Chen, P.; Robinson, P.J.; Lavin, M.F. Involvement of novel autophosphorylation sites in ATM activation. EMBO J., 2006, 25, 3504-3514.
    • (2006) EMBO J , vol.25 , pp. 3504-3514
    • Kozlov, S.V.1    Graham, M.E.2    Peng, C.3    Chen, P.4    Robinson, P.J.5    Lavin, M.F.6
  • 48
    • 33745058037 scopus 로고    scopus 로고
    • Two-step activation of ATM by DNA and the Mre11-Rad50-Nbs1 complex
    • Dupre, A.; Boyer-Chatenet, L.; Gautier, J. Two-step activation of ATM by DNA and the Mre11-Rad50-Nbs1 complex. Nat. Struct. Mol. Biol., 2006, 13, 451-457.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 451-457
    • Dupre, A.1    Boyer-Chatenet, L.2    Gautier, J.3
  • 51
    • 37549028411 scopus 로고    scopus 로고
    • DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase activity
    • Sun, Y.; Xu, Y.; Roy, K.; Price, B.D. DNA damage-induced acetylation of lysine 3016 of ATM activates ATM kinase activity. Mol. Cell Biol., 2007, 27, 8502-8509.
    • (2007) Mol. Cell Biol , vol.27 , pp. 8502-8509
    • Sun, Y.1    Xu, Y.2    Roy, K.3    Price, B.D.4
  • 53
    • 0027397867 scopus 로고
    • The DNA-dependent protein kinase: Requirement for DNA ends and association with Ku antigen
    • Gottlieb, T.M.; Jackson, S.P. The DNA-dependent protein kinase: requirement for DNA ends and association with Ku antigen. Cell, 1993, 72, 131-142.
    • (1993) Cell , vol.72 , pp. 131-142
    • Gottlieb, T.M.1    Jackson, S.P.2
  • 54
    • 0035833552 scopus 로고    scopus 로고
    • Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair
    • Walker, J.R.; Corpina, R.A.; Goldberg, J. Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. Nature, 2001, 412, 607-614.
    • (2001) Nature , vol.412 , pp. 607-614
    • Walker, J.R.1    Corpina, R.A.2    Goldberg, J.3
  • 55
    • 0032781658 scopus 로고    scopus 로고
    • Phosphorylation by DNAPK inhibits the DNA-binding function of p53/T antigen complex in vitro
    • Sheppard, H.M.; Liu, X. Phosphorylation by DNAPK inhibits the DNA-binding function of p53/T antigen complex in vitro. Anticancer Res., 1999, 19, 2079-2083.
    • (1999) Anticancer Res , vol.19 , pp. 2079-2083
    • Sheppard, H.M.1    Liu, X.2
  • 56
    • 1942538492 scopus 로고    scopus 로고
    • ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation
    • Stiff, T.; O'Driscoll, M.; Rief, N.; Iwabuchi, K.; Lobrich, M.; Jeggo, P.A. ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation. Cancer Res., 2004, 64, 2390-2396.
    • (2004) Cancer Res , vol.64 , pp. 2390-2396
    • Stiff, T.1    O'Driscoll, M.2    Rief, N.3    Iwabuchi, K.4    Lobrich, M.5    Jeggo, P.A.6
  • 58
    • 52049117396 scopus 로고    scopus 로고
    • DNA-PK and ATM phosphorylation sites in XLF/Cernunnos are not required for repair of DNA double strand breaks
    • Yu, Y.; Mahaney, B.L.; Yano, K.; Ye, R.; Fang, S.; Douglas, P.; Chen, D.J.; Lees-Miller, S.P. DNA-PK and ATM phosphorylation sites in XLF/Cernunnos are not required for repair of DNA double strand breaks. DNA Repair (Amst), 2008, 7, 1680-1692.
    • (2008) DNA Repair (Amst) , vol.7 , pp. 1680-1692
    • Yu, Y.1    Mahaney, B.L.2    Yano, K.3    Ye, R.4    Fang, S.5    Douglas, P.6    Chen, D.J.7    Lees-Miller, S.P.8
  • 59
    • 0037106180 scopus 로고    scopus 로고
    • Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks
    • Chan, D.W.; Chen, B.P.; Prithivirajsingh, S.; Kurimasa, A.; Story, M.D.; Qin, J.; Chen, D.J. Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks. Genes Dev., 2002, 16, 2333-2338.
    • (2002) Genes Dev , vol.16 , pp. 2333-2338
    • Chan, D.W.1    Chen, B.P.2    Prithivirajsingh, S.3    Kurimasa, A.4    Story, M.D.5    Qin, J.6    Chen, D.J.7
  • 60
    • 33745496607 scopus 로고    scopus 로고
    • Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4
    • Maas, N.L.; Miller, K.M.; DeFazio, L.G.; Toczyski, D.P. Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4. Mol. Cell, 2006, 23, 109-119.
    • (2006) Mol. Cell , vol.23 , pp. 109-119
    • Maas, N.L.1    Miller, K.M.2    Defazio, L.G.3    Toczyski, D.P.4
  • 61
    • 33646269070 scopus 로고    scopus 로고
    • Recruitment of the type B histone acetyl-transferase Hat1p to chromatin is linked to DNA double-strand breaks
    • Qin, S.; Parthun, M.R. Recruitment of the type B histone acetyl-transferase Hat1p to chromatin is linked to DNA double-strand breaks. Mol. Cell Biol., 2006, 26, 3649-3658.
    • (2006) Mol. Cell Biol , vol.26 , pp. 3649-3658
    • Qin, S.1    Parthun, M.R.2
  • 62
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan, M.V.; Lee, J.; Ward, I.M.; Kim, J.E.; Thompson, J.R.; Chen, J.; Mer, G. Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell, 2006, 127, 1361-1373.
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3    Kim, J.E.4    Thompson, J.R.5    Chen, J.6    Mer, G.7
  • 63
    • 0034700511 scopus 로고    scopus 로고
    • A role for Saccharomyces cerevisiae histone H2A in DNA repair
    • Downs, J.A.; Lowndes, N.F.; Jackson, S.P. A role for Saccharomyces cerevisiae histone H2A in DNA repair. Nature, 2000, 408, 1001-1004.
    • (2000) Nature , vol.408 , pp. 1001-1004
    • Downs, J.A.1    Lowndes, N.F.2    Jackson, S.P.3
  • 64
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • Rogakou, E.P.; Pilch, D.R.; Orr, A.H.; Ivanova, V.S.; Bonner, W.M. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J. Biol. Chem., 1998, 273, 5858-5868.
    • (1998) J. Biol. Chem , vol.273 , pp. 5858-5868
    • Rogakou, E.P.1    Pilch, D.R.2    Orr, A.H.3    Ivanova, V.S.4    Bonner, W.M.5
  • 65
    • 33744781568 scopus 로고    scopus 로고
    • Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage
    • Wang, H.; Zhai, L.; Xu, J.; Joo, H.Y.; Jackson, S.; Erdjument-Bromage, H.; Tempst, P.; Xiong, Y.; Zhang, Y. Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol. Cell, 2006, 22, 383-394.
    • (2006) Mol. Cell , vol.22 , pp. 383-394
    • Wang, H.1    Zhai, L.2    Xu, J.3    Joo, H.Y.4    Jackson, S.5    Erdjument-Bromage, H.6    Tempst, P.7    Xiong, Y.8    Zhang, Y.9
  • 67
    • 0343280013 scopus 로고    scopus 로고
    • A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage
    • Paull, T.T.; Rogakou, E.P.; Yamazaki, V.; Kirchgessner, C.U.; Gellert, M.; Bonner, W.M. A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage. Curr. Biol., 2000, 10, 886-895.
    • (2000) Curr. Biol , vol.10 , pp. 886-895
    • Paull, T.T.1    Rogakou, E.P.2    Yamazaki, V.3    Kirchgessner, C.U.4    Gellert, M.5    Bonner, W.M.6
  • 69
    • 29244434544 scopus 로고    scopus 로고
    • MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks
    • Stucki, M.; Clapperton, J.A.; Mohammad, D.; Yaffe, M.B.; Smerdon, S.J.; Jackson, S.P. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell, 2005, 123, 1213-1226.
    • (2005) Cell , vol.123 , pp. 1213-1226
    • Stucki, M.1    Clapperton, J.A.2    Mohammad, D.3    Yaffe, M.B.4    Smerdon, S.J.5    Jackson, S.P.6
  • 71
    • 0032721091 scopus 로고    scopus 로고
    • The Mre11-Rad50-Xrs2 protein complex facilitates homologous recombination-based double-strand break repair in Saccharomyces cerevisiae
    • Bressan, D.A.; Baxter, B.K.; Petrini, J.H. The Mre11-Rad50-Xrs2 protein complex facilitates homologous recombination-based double-strand break repair in Saccharomyces cerevisiae. Mol. Cell Biol., 1999, 19, 7681-7687.
    • (1999) Mol. Cell Biol , vol.19 , pp. 7681-7687
    • Bressan, D.A.1    Baxter, B.K.2    Petrini, J.H.3
  • 72
    • 0032931844 scopus 로고    scopus 로고
    • The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance
    • Moreau, S.; Ferguson, J.R.; Symington, L.S. The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance. Mol. Cell Biol., 1999, 19, 556-566.
    • (1999) Mol. Cell Biol , vol.19 , pp. 556-566
    • Moreau, S.1    Ferguson, J.R.2    Symington, L.S.3
  • 73
    • 1842421286 scopus 로고    scopus 로고
    • Intracellular redistribution and modification of proteins of the Mre11/Rad50/Nbs1 DNA repair complex following irradiation and heat-shock
    • Seno, J.D.; Dynlacht, J.R. Intracellular redistribution and modification of proteins of the Mre11/Rad50/Nbs1 DNA repair complex following irradiation and heat-shock. J. Cell Physiol., 2004, 199, 157-170.
    • (2004) J. Cell Physiol , vol.199 , pp. 157-170
    • Seno, J.D.1    Dynlacht, J.R.2
  • 74
    • 0032085295 scopus 로고    scopus 로고
    • The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks
    • Paull, T.T.; Gellert, M. The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks. Mol. Cell, 1998, 1, 969-979.
    • (1998) Mol. Cell , vol.1 , pp. 969-979
    • Paull, T.T.1    Gellert, M.2
  • 77
    • 20444468899 scopus 로고    scopus 로고
    • The Rad50 hook domain is a critical determinant of Mre11 complex functions
    • Wiltzius, J.J.; Hohl, M.; Fleming, J.C.; Petrini, J.H. The Rad50 hook domain is a critical determinant of Mre11 complex functions. Nat. Struct. Mol. Biol., 2005, 12, 403-407.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 403-407
    • Wiltzius, J.J.1    Hohl, M.2    Fleming, J.C.3    Petrini, J.H.4
  • 80
    • 0035936554 scopus 로고    scopus 로고
    • Targeted disruption of the Nijmegen breakage syndrome gene NBS1 leads to early embryonic lethality in mice
    • Zhu, J.; Petersen, S.; Tessarollo, L.; Nussenzweig, A. Targeted disruption of the Nijmegen breakage syndrome gene NBS1 leads to early embryonic lethality in mice. Curr. Biol., 2001, 11, 105-109.
    • (2001) Curr. Biol , vol.11 , pp. 105-109
    • Zhu, J.1    Petersen, S.2    Tessarollo, L.3    Nussenzweig, A.4
  • 81
    • 0030749867 scopus 로고    scopus 로고
    • Conditional gene targeted deletion by Cre recombinase demonstrates the requirement for the double-strand break repair Mre11 protein in murine embryonic stem cells
    • Xiao, Y.; Weaver, D.T. Conditional gene targeted deletion by Cre recombinase demonstrates the requirement for the double-strand break repair Mre11 protein in murine embryonic stem cells. Nucleic Acids Res., 1997, 25, 2985-2991.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2985-2991
    • Xiao, Y.1    Weaver, D.T.2
  • 82
    • 33847655393 scopus 로고    scopus 로고
    • Nijmegen breakage syndrome and functions of the responsible protein, NBS1
    • Antoccia, A.; Kobayashi, J.; Tauchi, H.; Matsuura, S.; Komatsu, K. Nijmegen breakage syndrome and functions of the responsible protein, NBS1. Genome Dyn., 2006, 1, 191-205.
    • (2006) Genome Dyn , vol.1 , pp. 191-205
    • Antoccia, A.1    Kobayashi, J.2    Tauchi, H.3    Matsuura, S.4    Komatsu, K.5
  • 83
    • 3242889151 scopus 로고    scopus 로고
    • Ataxia-telangiectasia-like disorder (ATLD)-its clinical presentation and molecular basis
    • Taylor, A.M.; Groom, A.; Byrd, P.J. Ataxia-telangiectasia-like disorder (ATLD)-its clinical presentation and molecular basis. DNA Repair (Amst), 2004, 3, 1219-1225.
    • (2004) DNA Repair (Amst) , vol.3 , pp. 1219-1225
    • Taylor, A.M.1    Groom, A.2    Byrd, P.J.3
  • 84
    • 17644409069 scopus 로고    scopus 로고
    • ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex
    • Lee, J.H.; Paull, T.T. ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex. Science, 2005, 308, 551-554.
    • (2005) Science , vol.308 , pp. 551-554
    • Lee, J.H.1    Paull, T.T.2
  • 85
    • 0037142619 scopus 로고    scopus 로고
    • Nbs1 promotes ATM dependent phosphorylation events including those required for G1/S arrest
    • Girard, P.M.; Riballo, E.; Begg, A.C.; Waugh, A.; Jeggo, P.A. Nbs1 promotes ATM dependent phosphorylation events including those required for G1/S arrest. Oncogene, 2002, 21, 4191-4199.
    • (2002) Oncogene , vol.21 , pp. 4191-4199
    • Girard, P.M.1    Riballo, E.2    Begg, A.C.3    Waugh, A.4    Jeggo, P.A.5
  • 86
    • 2942687831 scopus 로고    scopus 로고
    • Phosphorylation of SMC1 is a critical downstream event in the ATM-NBS1-BRCA1 pathway
    • Kitagawa, R.; Bakkenist, C.J.; McKinnon, P.J.; Kastan, M.B. Phosphorylation of SMC1 is a critical downstream event in the ATM-NBS1-BRCA1 pathway. Genes Dev., 2004, 18, 1423-1438.
    • (2004) Genes Dev , vol.18 , pp. 1423-1438
    • Kitagawa, R.1    Bakkenist, C.J.2    McKinnon, P.J.3    Kastan, M.B.4
  • 87
    • 47949121598 scopus 로고    scopus 로고
    • Mre11-Rad50-Nbs1-dependent processing of DNA breaks generates oligonucleotides that stimulate ATM activity
    • Jazayeri, A.; Balestrini, A.; Garner, E.; Haber, J.E.; Costanzo, V. Mre11-Rad50-Nbs1-dependent processing of DNA breaks generates oligonucleotides that stimulate ATM activity. EMBO J., 2008, 27, 1953-1962.
    • (2008) EMBO J , vol.27 , pp. 1953-1962
    • Jazayeri, A.1    Balestrini, A.2    Garner, E.3    Haber, J.E.4    Costanzo, V.5
  • 88
    • 23744447715 scopus 로고    scopus 로고
    • Independent and sequential recruitment of NHEJ and HR factors to DNA damage sites in mammalian cells
    • Kim, J.S.; Krasieva, T.B.; Kurumizaka, H.; Chen, D.J.; Taylor, A.M.; Yokomori, K. Independent and sequential recruitment of NHEJ and HR factors to DNA damage sites in mammalian cells. J. Cell Biol., 2005, 170, 341-347.
    • (2005) J. Cell Biol , vol.170 , pp. 341-347
    • Kim, J.S.1    Krasieva, T.B.2    Kurumizaka, H.3    Chen, D.J.4    Taylor, A.M.5    Yokomori, K.6
  • 90
  • 92
    • 0142240342 scopus 로고    scopus 로고
    • BRCT repeats as phosphopeptide-binding modules involved in protein targeting
    • Manke, I.A.; Lowery, D.M.; Nguyen, A.; Yaffe, M.B. BRCT repeats as phosphopeptide-binding modules involved in protein targeting. Science, 2003, 302, 636-639.
    • (2003) Science , vol.302 , pp. 636-639
    • Manke, I.A.1    Lowery, D.M.2    Nguyen, A.3    Yaffe, M.B.4
  • 95
    • 22944462083 scopus 로고    scopus 로고
    • Dynamic assembly and sustained retention of 53BP1 at the sites of DNA damage are controlled by Mdc1/NFBD1
    • Bekker-Jensen, S.; Lukas, C.; Melander, F.; Bartek, J.; Lukas, J. Dynamic assembly and sustained retention of 53BP1 at the sites of DNA damage are controlled by Mdc1/NFBD1. J. Cell Biol., 2005, 170, 201-211.
    • (2005) J. Cell Biol , vol.170 , pp. 201-211
    • Bekker-Jensen, S.1    Lukas, C.2    Melander, F.3    Bartek, J.4    Lukas, J.5
  • 96
    • 36248966246 scopus 로고    scopus 로고
    • RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins
    • Mailand, N.; Bekker-Jensen, S.; Faustrup, H.; Melander, F.; Bartek, J.; Lukas, C.; Lukas, J. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell, 2007, 131, 887-900.
    • (2007) Cell , vol.131 , pp. 887-900
    • Mailand, N.1    Bekker-Jensen, S.2    Faustrup, H.3    Melander, F.4    Bartek, J.5    Lukas, C.6    Lukas, J.7
  • 98
  • 100
    • 6344264992 scopus 로고    scopus 로고
    • DNA damage-induced cell cycle checkpoint control requires CtIP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains
    • Yu, X.; Chen, J. DNA damage-induced cell cycle checkpoint control requires CtIP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains. Mol. Cell Biol., 2004, 24, 9478-9486.
    • (2004) Mol. Cell Biol , vol.24 , pp. 9478-9486
    • Yu, X.1    Chen, J.2
  • 101
    • 0345276495 scopus 로고    scopus 로고
    • Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair
    • Dong, Y.; Hakimi, M.A.; Chen, X.; Kumaraswamy, E.; Cooch, N.S.; Godwin, A.K.; Shiekhattar, R. Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair. Mol. Cell, 2003, 12, 1087-1099.
    • (2003) Mol. Cell , vol.12 , pp. 1087-1099
    • Dong, Y.1    Hakimi, M.A.2    Chen, X.3    Kumaraswamy, E.4    Cooch, N.S.5    Godwin, A.K.6    Shiekhattar, R.7
  • 102
    • 33744944054 scopus 로고    scopus 로고
    • BRCC36 is essential for ionizing radiation-induced BRCA1 phosphorylation and nuclear foci formation
    • Chen, X.; Arciero, C.A.; Wang, C.; Broccoli, D.; Godwin, A.K. BRCC36 is essential for ionizing radiation-induced BRCA1 phosphorylation and nuclear foci formation. Cancer Res., 2006, 66, 5039-5046.
    • (2006) Cancer Res , vol.66 , pp. 5039-5046
    • Chen, X.1    Arciero, C.A.2    Wang, C.3    Broccoli, D.4    Godwin, A.K.5
  • 103
    • 62549140202 scopus 로고    scopus 로고
    • The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks
    • Shao, G.; Lilli, D.R.; Patterson-Fortin, J.; Coleman, K.A.; Morrissey, D.E.; Greenberg, R.A. The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks. Proc. Natl. Acad. Sci. USA, 2009, 106, 3166-3171.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3166-3171
    • Shao, G.1    Lilli, D.R.2    Patterson-Fortin, J.3    Coleman, K.A.4    Morrissey, D.E.5    Greenberg, R.A.6
  • 105
    • 57349169242 scopus 로고    scopus 로고
    • Rapid recruitment of BRCA1 to DNA double-strand breaks is dependent on its association with Ku80
    • Wei, L.; Lan, L.; Hong, Z.; Yasui, A.; Ishioka, C.; Chiba, N. Rapid recruitment of BRCA1 to DNA double-strand breaks is dependent on its association with Ku80. Mol. Cell Biol., 2008, 28, 7380-7393.
    • (2008) Mol. Cell Biol , vol.28 , pp. 7380-7393
    • Wei, L.1    Lan, L.2    Hong, Z.3    Yasui, A.4    Ishioka, C.5    Chiba, N.6
  • 107
    • 57049114872 scopus 로고    scopus 로고
    • S1219 residue of 53BP1 is phosphorylated by ATM kinase upon DNA damage and required for proper execution of DNA damage response
    • Lee, H.; Kwak, H.J.; Cho, I.T.; Park, S.H.; Lee, C.H. S1219 residue of 53BP1 is phosphorylated by ATM kinase upon DNA damage and required for proper execution of DNA damage response. Biochem. Biophys. Res. Commun., 2009, 378, 32-36.
    • (2009) Biochem. Biophys. Res. Commun , vol.378 , pp. 32-36
    • Lee, H.1    Kwak, H.J.2    Cho, I.T.3    Park, S.H.4    Lee, C.H.5
  • 108
    • 0037112212 scopus 로고    scopus 로고
    • 53BP1, a mediator of the DNA damage checkpoint
    • Wang, B.; Matsuoka, S.; Carpenter, P.B.; Elledge, S.J. 53BP1, a mediator of the DNA damage checkpoint. Science, 2002, 298, 1435-1438.
    • (2002) Science , vol.298 , pp. 1435-1438
    • Wang, B.1    Matsuoka, S.2    Carpenter, P.B.3    Elledge, S.J.4
  • 109
    • 0346059615 scopus 로고    scopus 로고
    • 53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways activating ataxia-telangiectasia mutated (ATM) in response to DNA damage
    • Mochan, T.A.; Venere, M.; Ditullio, R.A., Jr.; Halazonetis, T.D. 53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways activating ataxia-telangiectasia mutated (ATM) in response to DNA damage. Cancer Res., 2003, 63, 8586-8591.
    • (2003) Cancer Res , vol.63 , pp. 8586-8591
    • Mochan, T.A.1    Venere, M.2    Ditullio Jr., R.A.3    Halazonetis, T.D.4
  • 110
    • 0032530658 scopus 로고    scopus 로고
    • Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells
    • Takata, M.; Sasaki, M.S.; Sonoda, E.; Morrison, C.; Hashimoto, M.; Utsumi, H.; Yamaguchi-Iwai, Y.; Shinohara, A.; Takeda, S. Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells. EMBO J., 1998, 17, 5497-5508.
    • (1998) EMBO J , vol.17 , pp. 5497-5508
    • Takata, M.1    Sasaki, M.S.2    Sonoda, E.3    Morrison, C.4    Hashimoto, M.5    Utsumi, H.6    Yamaguchi-Iwai, Y.7    Shinohara, A.8    Takeda, S.9
  • 111
    • 0042632901 scopus 로고    scopus 로고
    • Pathways of DNA double-strand break repair during the mammalian cell cycle
    • Rothkamm, K.; Kruger, I.; Thompson, L.H.; Lobrich, M. Pathways of DNA double-strand break repair during the mammalian cell cycle. Mol. Cell Biol., 2003, 23, 5706-5715.
    • (2003) Mol. Cell Biol , vol.23 , pp. 5706-5715
    • Rothkamm, K.1    Kruger, I.2    Thompson, L.H.3    Lobrich, M.4
  • 112
    • 0036682122 scopus 로고    scopus 로고
    • An xrcc4 defect or Wortmannin stimulates homologous recombination specifically induced by double-strand breaks in mammalian cells
    • Delacote, F.; Han, M.; Stamato, T.D.; Jasin, M.; Lopez, B.S. An xrcc4 defect or Wortmannin stimulates homologous recombination specifically induced by double-strand breaks in mammalian cells. Nucleic Acids Res., 2002, 30, 3454-3463.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3454-3463
    • Delacote, F.1    Han, M.2    Stamato, T.D.3    Jasin, M.4    Lopez, B.S.5
  • 113
    • 0036864626 scopus 로고    scopus 로고
    • Transient stability of DNA ends allows nonhomologous end joining to precede homologous recombination
    • Frank-Vaillant, M.; Marcand, S. Transient stability of DNA ends allows nonhomologous end joining to precede homologous recombination. Mol. Cell, 2002, 10, 1189-1199.
    • (2002) Mol. Cell , vol.10 , pp. 1189-1199
    • Frank-Vaillant, M.1    Marcand, S.2
  • 114
    • 0034234487 scopus 로고    scopus 로고
    • DNA double-strand break repair in cell-free extracts from Ku80-deficient cells: Implications for Ku serving as an alignment factor in non-homologous DNA end joining
    • Feldmann, E.; Schmiemann, V.; Goedecke, W.; Reichenberger, S.; Pfeiffer, P. DNA double-strand break repair in cell-free extracts from Ku80-deficient cells: implications for Ku serving as an alignment factor in non-homologous DNA end joining. Nucleic Acids Res., 2000, 28, 2585-2596.
    • (2000) Nucleic Acids Res , vol.28 , pp. 2585-2596
    • Feldmann, E.1    Schmiemann, V.2    Goedecke, W.3    Reichenberger, S.4    Pfeiffer, P.5
  • 117
    • 0032544413 scopus 로고    scopus 로고
    • Requirement for an interaction of XRCC4 with DNA ligase IV for wild-type V(D)J recombination and DNA double-strand break repair in vivo
    • Grawunder, U.; Zimmer, D.; Kulesza, P.; Lieber, M.R. Requirement for an interaction of XRCC4 with DNA ligase IV for wild-type V(D)J recombination and DNA double-strand break repair in vivo. J. Biol. Chem., 1998, 273, 24708-24714.
    • (1998) J. Biol. Chem , vol.273 , pp. 24708-24714
    • Grawunder, U.1    Zimmer, D.2    Kulesza, P.3    Lieber, M.R.4
  • 118
    • 31044432090 scopus 로고    scopus 로고
    • XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining
    • Ahnesorg, P.; Smith, P.; Jackson, S.P. XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining. Cell, 2006, 124, 301-313.
    • (2006) Cell , vol.124 , pp. 301-313
    • Ahnesorg, P.1    Smith, P.2    Jackson, S.P.3
  • 122
    • 4544362838 scopus 로고    scopus 로고
    • The mechanism of non-homologous end-joining: A synopsis of synapsis
    • Weterings, E.; van Gent, D.C. The mechanism of non-homologous end-joining: a synopsis of synapsis. DNA Repair (Amst), 2004, 3, 1425-1435.
    • (2004) DNA Repair (Amst) , vol.3 , pp. 1425-1435
    • Weterings, E.1    van Gent, D.C.2
  • 123
    • 0027512522 scopus 로고
    • Characterization of the DNA double strand break repair defect in scid mice
    • Chang, C.; Biedermann, K.A.; Mezzina, M.; Brown, J.M. Characterization of the DNA double strand break repair defect in scid mice. Cancer Res., 1993, 53, 1244-1248.
    • (1993) Cancer Res , vol.53 , pp. 1244-1248
    • Chang, C.1    Biedermann, K.A.2    Mezzina, M.3    Brown, J.M.4
  • 124
    • 0030907318 scopus 로고    scopus 로고
    • Ku proteins join DNA fragments as shown by atomic force microscopy
    • Pang, D.; Yoo, S.; Dynan, W.S.; Jung, M.; Dritschilo, A. Ku proteins join DNA fragments as shown by atomic force microscopy. Cancer Res., 1997, 57, 1412-1415.
    • (1997) Cancer Res , vol.57 , pp. 1412-1415
    • Pang, D.1    Yoo, S.2    Dynan, W.S.3    Jung, M.4    Dritschilo, A.5
  • 125
    • 0032052815 scopus 로고    scopus 로고
    • Interaction of Ku protein and DNA-dependent protein kinase catalytic subunit with nucleic acids
    • Dynan, W.S.; Yoo, S. Interaction of Ku protein and DNA-dependent protein kinase catalytic subunit with nucleic acids. Nucleic Acids Res., 1998, 26, 1551-1559.
    • (1998) Nucleic Acids Res , vol.26 , pp. 1551-1559
    • Dynan, W.S.1    Yoo, S.2
  • 128
    • 0347683431 scopus 로고    scopus 로고
    • Implication of DNA polymerase lambda in alignment-based gap filling for nonhomologous DNA end joining in human nuclear extracts
    • Lee, J.W.; Blanco, L.; Zhou, T.; Garcia-Diaz, M.; Bebenek, K.; Kunkel, T.A.; Wang, Z.; Povirk, L.F. Implication of DNA polymerase lambda in alignment-based gap filling for nonhomologous DNA end joining in human nuclear extracts. J. Biol. Chem., 2004, 279, 805-811.
    • (2004) J. Biol. Chem , vol.279 , pp. 805-811
    • Lee, J.W.1    Blanco, L.2    Zhou, T.3    Garcia-Diaz, M.4    Bebenek, K.5    Kunkel, T.A.6    Wang, Z.7    Povirk, L.F.8
  • 129
    • 0037155703 scopus 로고    scopus 로고
    • Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination
    • Ma, Y.; Pannicke, U.; Schwarz, K.; Lieber, M.R. Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination. Cell, 2002, 108, 781-794.
    • (2002) Cell , vol.108 , pp. 781-794
    • Ma, Y.1    Pannicke, U.2    Schwarz, K.3    Lieber, M.R.4
  • 130
    • 0030743386 scopus 로고    scopus 로고
    • Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells
    • Grawunder, U.; Wilm, M.; Wu, X.; Kulesza, P.; Wilson, T.E.; Mann, M.; Lieber, M.R. Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells. Nature, 1997, 388, 492-495.
    • (1997) Nature , vol.388 , pp. 492-495
    • Grawunder, U.1    Wilm, M.2    Wu, X.3    Kulesza, P.4    Wilson, T.E.5    Mann, M.6    Lieber, M.R.7
  • 131
    • 0032971199 scopus 로고    scopus 로고
    • Absence of DNA ligase IV protein in XR-1 cells: Evidence for stabilization by XRCC4
    • Bryans, M.; Valenzano, M.C.; Stamato, T.D. Absence of DNA ligase IV protein in XR-1 cells: evidence for stabilization by XRCC4. Mutat. Res., 1999, 433, 53-58.
    • (1999) Mutat. Res , vol.433 , pp. 53-58
    • Bryans, M.1    Valenzano, M.C.2    Stamato, T.D.3
  • 133
    • 30944443320 scopus 로고    scopus 로고
    • Monoubiquitination of the nonhomologous end joining protein XRCC4
    • Foster, R.E.; Nnakwe, C.; Woo, L.; Frank, K.M. Monoubiquitination of the nonhomologous end joining protein XRCC4. Biochem. Biophys. Res. Commun., 2006, 341, 175-183.
    • (2006) Biochem. Biophys. Res. Commun , vol.341 , pp. 175-183
    • Foster, R.E.1    Nnakwe, C.2    Woo, L.3    Frank, K.M.4
  • 134
    • 33644540769 scopus 로고    scopus 로고
    • SUMO modification of human XRCC4 regulates its localization and function in DNA double-strand break repair
    • Yurchenko, V.; Xue, Z.; Sadofsky, M.J. SUMO modification of human XRCC4 regulates its localization and function in DNA double-strand break repair. Mol. Cell Biol., 2006, 26, 1786-1794.
    • (2006) Mol. Cell Biol , vol.26 , pp. 1786-1794
    • Yurchenko, V.1    Xue, Z.2    Sadofsky, M.J.3
  • 135
    • 37349113779 scopus 로고    scopus 로고
    • Crystal structure of human XLF: A twist in nonhomologous DNA end-joining
    • Andres, S.N.; Modesti, M.; Tsai, C.J.; Chu, G.; Junop, M.S. Crystal structure of human XLF: a twist in nonhomologous DNA end-joining. Mol. Cell, 2007, 28, 1093-1101.
    • (2007) Mol. Cell , vol.28 , pp. 1093-1101
    • Andres, S.N.1    Modesti, M.2    Tsai, C.J.3    Chu, G.4    Junop, M.S.5
  • 140
    • 68249146431 scopus 로고    scopus 로고
    • Role of mammalian Mre11 in classical and alternative nonhomologous end joining
    • Xie, A.; Kwok, A.; Scully, R. Role of mammalian Mre11 in classical and alternative nonhomologous end joining. Nat. Struct. Mol. Biol., 2009, 16, 814-818.
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 814-818
    • Xie, A.1    Kwok, A.2    Scully, R.3
  • 141
    • 0031004885 scopus 로고    scopus 로고
    • A single-stranded DNA-binding protein is needed for efficient presynaptic complex formation by the Saccharomyces cerevisiae Rad51 protein
    • Sugiyama, T.; Zaitseva, E.M.; Kowalczykowski, S.C. A single-stranded DNA-binding protein is needed for efficient presynaptic complex formation by the Saccharomyces cerevisiae Rad51 protein. J. Biol. Chem., 1997, 272, 7940-7945.
    • (1997) J. Biol. Chem , vol.272 , pp. 7940-7945
    • Sugiyama, T.1    Zaitseva, E.M.2    Kowalczykowski, S.C.3
  • 142
    • 0030908093 scopus 로고    scopus 로고
    • Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
    • Wold, M.S. Replication protein A: a heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism. Annu. Rev. Biochem., 1997, 66, 61-92.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 61-92
    • Wold, M.S.1
  • 143
    • 0030995362 scopus 로고    scopus 로고
    • Yeast Rad55 and Rad57 proteins form a heterodimer that functions with replication protein A to promote DNA strand exchange by Rad51 recombinase
    • Sung, P. Yeast Rad55 and Rad57 proteins form a heterodimer that functions with replication protein A to promote DNA strand exchange by Rad51 recombinase. Genes Dev., 1997, 11, 1111-1121.
    • (1997) Genes Dev , vol.11 , pp. 1111-1121
    • Sung, P.1
  • 144
    • 0029112483 scopus 로고
    • DNA strand exchange mediated by a RAD51-ssDNA nucleoprotein filament with polarity opposite to that of RecA
    • Sung, P.; Robberson, D.L. DNA strand exchange mediated by a RAD51-ssDNA nucleoprotein filament with polarity opposite to that of RecA. Cell, 1995, 82, 453-461.
    • (1995) Cell , vol.82 , pp. 453-461
    • Sung, P.1    Robberson, D.L.2
  • 145
    • 0027978039 scopus 로고
    • Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein
    • Sung, P. Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein. Science, 1994, 265, 1241-1243.
    • (1994) Science , vol.265 , pp. 1241-1243
    • Sung, P.1
  • 146
    • 0026751113 scopus 로고
    • Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein
    • Shinohara, A.; Ogawa, H.; Ogawa, T. Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein. Cell, 1992, 69, 457-470.
    • (1992) Cell , vol.69 , pp. 457-470
    • Shinohara, A.1    Ogawa, H.2    Ogawa, T.3
  • 147
    • 0035796042 scopus 로고    scopus 로고
    • Homologous recombinational repair ofHomologous recombinational repair of DNA ensures mammalian chromosome stability
    • Thompson, L.H.; Schild, D. Homologous recombinational repair ofHomologous recombinational repair of DNA ensures mammalian chromosome stability. Mutat. Res., 2001, 477, 131-153.
    • (2001) Mutat. Res. , vol.477 , pp. 131-153
    • Thompson, L.H.1
  • 148
    • 0031466027 scopus 로고    scopus 로고
    • RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2
    • Wong, A.K.; Pero, R.; Ormonde, P.A.; Tavtigian, S.V.; Bartel, P.L. RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2. J. Biol. Chem., 1997, 272, 31941-31944.
    • (1997) J. Biol. Chem , vol.272 , pp. 31941-31944
    • Wong, A.K.1    Pero, R.2    Ormonde, P.A.3    Tavtigian, S.V.4    Bartel, P.L.5
  • 150
    • 33744950933 scopus 로고    scopus 로고
    • Recombination mediator and Rad51 targeting activities of a human BRCA2 polypeptide
    • San Filippo, J.; Chi, P.; Sehorn, M.G.; Etchin, J.; Krejci, L.; Sung, P. Recombination mediator and Rad51 targeting activities of a human BRCA2 polypeptide. J. Biol. Chem., 2006, 281, 11649-11657.
    • (2006) J. Biol. Chem , vol.281 , pp. 11649-11657
    • San Filippo, J.1    Chi, P.2    Sehorn, M.G.3    Etchin, J.4    Krejci, L.5    Sung, P.6
  • 151
    • 0042626553 scopus 로고    scopus 로고
    • Recruitmentof the recombinational repair machinery to a DNA double-strand break in yeast
    • Wolner, B.; Van Komen, S.; Sung, P.; Peterson, C.L. Recruitmentof the recombinational repair machinery to a DNA double-strand break in yeast. Mol. Cell, 2003, 12, 221-232.
    • (2003) Mol. Cell. , vol.12 , pp. 221-232
    • Wolner, B.1    van Komen, S.2    Sung, P.3    Peterson, C.L.4
  • 152
    • 54049139260 scopus 로고    scopus 로고
    • Rad51 protein stimulates the branch migration activity of Rad54 protein
    • Rossi, M.J.; Mazin, A.V. Rad51 protein stimulates the branch migration activity of Rad54 protein. J. Biol. Chem., 2008, 283, 24698-24706.
    • (2008) J. Biol. Chem , vol.283 , pp. 24698-24706
    • Rossi, M.J.1    Mazin, A.V.2
  • 153
    • 38949107602 scopus 로고    scopus 로고
    • DNA polymerase delta is preferentially recruited during homologous recombination to promote heteroduplex DNA extension
    • Maloisel, L.; Fabre, F.; Gangloff, S. DNA polymerase delta is preferentially recruited during homologous recombination to promote heteroduplex DNA extension. Mol. Cell Biol., 2008, 28, 1373-1382.
    • (2008) Mol. Cell Biol , vol.28 , pp. 1373-1382
    • Maloisel, L.1    Fabre, F.2    Gangloff, S.3
  • 154
    • 0346340054 scopus 로고    scopus 로고
    • RAD51C is required for Holliday junction processing in mammalian cells
    • Liu, Y.; Masson, J.Y.; Shah, R.; O'Regan, P.; West, S.C. RAD51C is required for Holliday junction processing in mammalian cells. Science, 2004, 303, 243-246.
    • (2004) Science , vol.303 , pp. 243-246
    • Liu, Y.1    Masson, J.Y.2    Shah, R.3    O'Regan, P.4    West, S.C.5
  • 156
    • 33847307543 scopus 로고    scopus 로고
    • Role of RAD51C and XRCC3 in genetic recombination and DNA repair
    • Liu, Y.; Tarsounas, M.; O'Regan, P.; West, S.C. Role of RAD51C and XRCC3 in genetic recombination and DNA repair. J. Biol. Chem., 2007, 282, 1973-1979.
    • (2007) J. Biol. Chem , vol.282 , pp. 1973-1979
    • Liu, Y.1    Tarsounas, M.2    O'Regan, P.3    West, S.C.4
  • 157
    • 3242890575 scopus 로고    scopus 로고
    • Mammalian cell cycle checkpoints: Signalling pathways and their organization in space and time
    • Lukas, J.; Lukas, C.; Bartek, J. Mammalian cell cycle checkpoints: signalling pathways and their organization in space and time. DNA Repair (Amst), 2004, 3, 997-1007.
    • (2004) DNA Repair (Amst) , vol.3 , pp. 997-1007
    • Lukas, J.1    Lukas, C.2    Bartek, J.3
  • 158
    • 0034326802 scopus 로고    scopus 로고
    • Threonine 68 phosphorylation by ataxia telangiectasia mutated is required for efficient activation of Chk2 in response to ionizing radiation
    • Ahn, J.Y.; Schwarz, J.K.; Piwnica-Worms, H.; Canman, C.E. Threonine 68 phosphorylation by ataxia telangiectasia mutated is required for efficient activation of Chk2 in response to ionizing radiation. Cancer Res., 2000, 60, 5934-5936.
    • (2000) Cancer Res , vol.60 , pp. 5934-5936
    • Ahn, J.Y.1    Schwarz, J.K.2    Piwnica-Worms, H.3    Canman, C.E.4
  • 159
    • 0032484084 scopus 로고    scopus 로고
    • Linkage of ATM to cell cycle regulation by the Chk2 protein kinase
    • Matsuoka, S.; Huang, M.; Elledge, S.J. Linkage of ATM to cell cycle regulation by the Chk2 protein kinase. Science, 1998, 282, 1893-1897.
    • (1998) Science , vol.282 , pp. 1893-1897
    • Matsuoka, S.1    Huang, M.2    Elledge, S.J.3
  • 160
    • 0034142325 scopus 로고    scopus 로고
    • Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53
    • Chehab, N.H.; Malikzay, A.; Appel, M.; Halazonetis, T.D. Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53. Genes Dev., 2000, 14, 278-288.
    • (2000) Genes Dev , vol.14 , pp. 278-288
    • Chehab, N.H.1    Malikzay, A.2    Appel, M.3    Halazonetis, T.D.4
  • 161
    • 0037795780 scopus 로고    scopus 로고
    • Regulation of the Chk2 protein kinase by oligomerization-mediated cis- and trans-phosphorylation
    • Schwarz, J.K.; Lovly, C.M.; Piwnica-Worms, H. Regulation of the Chk2 protein kinase by oligomerization-mediated cis- and trans-phosphorylation. Mol. Cancer Res., 2003, 1, 598-609.
    • (2003) Mol. Cancer Res , vol.1 , pp. 598-609
    • Schwarz, J.K.1    Lovly, C.M.2    Piwnica-Worms, H.3
  • 162
    • 0035848819 scopus 로고    scopus 로고
    • The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis
    • Falck, J.; Mailand, N.; Syljuasen, R.G.; Bartek, J.; Lukas, J. The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis. Nature, 2001, 410, 842-847.
    • (2001) Nature , vol.410 , pp. 842-847
    • Falck, J.1    Mailand, N.2    Syljuasen, R.G.3    Bartek, J.4    Lukas, J.5
  • 164
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt, Y.; Maya, R.; Kazaz, A.; Oren, M. Mdm2 promotes the rapid degradation of p53. Nature, 1997, 387, 296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 166
    • 18644365597 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors differentially stabilize acetylated p53 and induce cell cycle arrest or apoptosis in prostate cancer cells
    • Roy, S.; Packman, K.; Jeffrey, R.; Tenniswood, M. Histone deacetylase inhibitors differentially stabilize acetylated p53 and induce cell cycle arrest or apoptosis in prostate cancer cells. Cell Death Differ., 2005, 12, 482-491.
    • (2005) Cell Death Differ , vol.12 , pp. 482-491
    • Roy, S.1    Packman, K.2    Jeffrey, R.3    Tenniswood, M.4
  • 167
    • 0033609306 scopus 로고    scopus 로고
    • Mutations in serines 15 and 20 of human p53 impair its apoptotic activity
    • Unger, T.; Sionov, R.V.; Moallem, E.; Yee, C.L.; Howley, P.M.; Oren, M.; Haupt, Y. Mutations in serines 15 and 20 of human p53 impair its apoptotic activity. Oncogene, 1999, 18, 3205-3212.
    • (1999) Oncogene , vol.18 , pp. 3205-3212
    • Unger, T.1    Sionov, R.V.2    Moallem, E.3    Yee, C.L.4    Howley, P.M.5    Oren, M.6    Haupt, Y.7
  • 169
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • Miyashita, T.; Reed, J.C. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell, 1995, 80, 293-299.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 170
    • 0035265686 scopus 로고    scopus 로고
    • PUMA, a novel proapoptotic gene, is induced by p53
    • Nakano, K.; Vousden, K.H. PUMA, a novel proapoptotic gene, is induced by p53. Mol. Cell, 2001, 7, 683-694.
    • (2001) Mol. Cell , vol.7 , pp. 683-694
    • Nakano, K.1    Vousden, K.H.2
  • 173
    • 0028988585 scopus 로고
    • Inhibitors of mammalian G1 cyclindependent kinases
    • Sherr, C.J.; Roberts, J.M. Inhibitors of mammalian G1 cyclindependent kinases. Genes Dev., 1995, 9, 1149-1163.
    • (1995) Genes Dev , vol.9 , pp. 1149-1163
    • Sherr, C.J.1    Roberts, J.M.2
  • 174
    • 0030998797 scopus 로고    scopus 로고
    • Regulation of CDK/cyclin complexes during the cell cycle
    • Arellano, M.; Moreno, S. Regulation of CDK/cyclin complexes during the cell cycle. Int. J. Biochem. Cell Biol., 1997, 29, 559-573.
    • (1997) Int. J. Biochem. Cell Biol , vol.29 , pp. 559-573
    • Arellano, M.1    Moreno, S.2
  • 175
    • 0026537277 scopus 로고
    • The interaction of RB with E2F coincides with an inhibition of the transcriptional activity of E2F
    • Hiebert, S.W.; Chellappan, S.P.; Horowitz, J.M.; Nevins, J.R. The interaction of RB with E2F coincides with an inhibition of the transcriptional activity of E2F. Genes Dev., 1992, 6, 177-185.
    • (1992) Genes Dev , vol.6 , pp. 177-185
    • Hiebert, S.W.1    Chellappan, S.P.2    Horowitz, J.M.3    Nevins, J.R.4
  • 176
    • 0025905183 scopus 로고
    • The E2F transcription factor is a cellular target for the RB protein
    • Chellappan, S.P.; Hiebert, S.; Mudryj, M.; Horowitz, J.M.; Nevins, J.R. The E2F transcription factor is a cellular target for the RB protein. Cell, 1991, 65, 1053-1061.
    • (1991) Cell , vol.65 , pp. 1053-1061
    • Chellappan, S.P.1    Hiebert, S.2    Mudryj, M.3    Horowitz, J.M.4    Nevins, J.R.5
  • 177
    • 0026802989 scopus 로고
    • Regulation of retinoblastoma protein functions by ectopic expression of human cyclins
    • Hinds, P.W.; Mittnacht, S.; Dulic, V.; Arnold, A.; Reed, S.I.; Weinberg, R.A. Regulation of retinoblastoma protein functions by ectopic expression of human cyclins. Cell, 1992, 70, 993-1006.
    • (1992) Cell , vol.70 , pp. 993-1006
    • Hinds, P.W.1    Mittnacht, S.2    Dulic, V.3    Arnold, A.4    Reed, S.I.5    Weinberg, R.A.6
  • 178
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J.F.; Wyllie, A.H.; Currie, A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer, 1972, 26, 239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 179
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner, M.O. The biochemistry of apoptosis. Nature, 2000, 407, 770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 180
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green, D.R.; Kroemer, G. The pathophysiology of mitochondrial cell death. Science, 2004, 305, 626-629.
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 182
    • 46749117587 scopus 로고    scopus 로고
    • p53's mitochondrial translocation and MOMP action is independent of Puma and Bax and severely disrupts mitochondrial membrane integrity
    • Wolff, S.; Erster, S.; Palacios, G.; Moll, U.M. p53's mitochondrial translocation and MOMP action is independent of Puma and Bax and severely disrupts mitochondrial membrane integrity. Cell Res., 2008, 18, 733-744.
    • (2008) Cell Res , vol.18 , pp. 733-744
    • Wolff, S.1    Erster, S.2    Palacios, G.3    Moll, U.M.4
  • 183
    • 13544256594 scopus 로고    scopus 로고
    • The post-translational phosphorylation and acetylation modification profile is not the determining factor in targeting endogenous stress-induced p53 to mitochondria
    • Nemajerova, A.; Erster, S.; Moll, U.M. The post-translational phosphorylation and acetylation modification profile is not the determining factor in targeting endogenous stress-induced p53 to mitochondria. Cell Death Differ., 2005, 12, 197-200.
    • (2005) Cell Death Differ , vol.12 , pp. 197-200
    • Nemajerova, A.1    Erster, S.2    Moll, U.M.3
  • 184
    • 33847276654 scopus 로고    scopus 로고
    • Monoubiquitylation promotes mitochondrial p53 translocation
    • Marchenko, N.D.; Wolff, S.; Erster, S.; Becker, K.; Moll, U.M. Monoubiquitylation promotes mitochondrial p53 translocation. EMBO J., 2007, 26, 923-934.
    • (2007) EMBO J , vol.26 , pp. 923-934
    • Marchenko, N.D.1    Wolff, S.2    Erster, S.3    Becker, K.4    Moll, U.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.