메뉴 건너뛰기




Volumn 14, Issue 10, 2013, Pages 661-672

Push back to respond better: Regulatory inhibition of the DNA double-strand break response

Author keywords

[No Author keywords available]

Indexed keywords

ATM PROTEIN;

EID: 84886429265     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3659     Document Type: Review
Times cited : (144)

References (119)
  • 1
    • 54249116230 scopus 로고
    • Genetic regulatory mechanisms in the synthesis of proteins
    • Jacob, F. & Monod, J. Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 3, 318-356 (1961).
    • (1961) J. Mol. Biol. , vol.3 , pp. 318-356
    • Jacob, F.1    Monod, J.2
  • 2
    • 84872824241 scopus 로고    scopus 로고
    • Design principles of regulatory networks: Searching for the molecular algorithms of the cell
    • Lim, W. A., Lee, C. M. & Tang, C. Design principles of regulatory networks: searching for the molecular algorithms of the cell. Mol. Cell 49, 202-212 (2013).
    • (2013) Mol. Cell , vol.49 , pp. 202-212
    • Lim, W.A.1    Lee, C.M.2    Tang, C.3
  • 3
    • 28444483130 scopus 로고    scopus 로고
    • γ-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA double-strand break repair
    • Chowdhury, D. et al. γ-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA double-strand break repair. Mol. Cell 20, 801-809 (2005).
    • (2005) Mol. Cell , vol.20 , pp. 801-809
    • Chowdhury, D.1
  • 4
    • 84865232294 scopus 로고    scopus 로고
    • TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes
    • Gudjonsson, T. et al. TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes. Cell 150, 697-709 (2012).
    • (2012) Cell , vol.150 , pp. 697-709
    • Gudjonsson, T.1
  • 5
    • 53249100305 scopus 로고    scopus 로고
    • PP4 is a γh2AX phosphatase required for recovery from the DNA damage checkpoint
    • Nakada, S., Chen, G. I., Gingras, A. C. & Durocher, D. PP4 is a γH2AX phosphatase required for recovery from the DNA damage checkpoint. EMBO Rep. 9, 1019-1026 (2008).
    • (2008) EMBO Rep. , vol.9 , pp. 1019-1026
    • Nakada, S.1    Chen, G.I.2    Gingras, A.C.3    Durocher, D.4
  • 6
    • 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. et al. The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8- Ubc13-dependent ubiquitination events at DNA double strand breaks. Proc. Natl Acad. Sci. USA 106, 3166-3171 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 3166-3171
    • Shao, G.1
  • 7
    • 82955233157 scopus 로고    scopus 로고
    • The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks
    • Acs, K. et al. The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks. Nature Struct. Mol. Biol. 18, 1345-1350 (2011).
    • (2011) Nature Struct. Mol. Biol. , vol.18 , pp. 1345-1350
    • Acs, K.1
  • 8
    • 84883599853 scopus 로고    scopus 로고
    • Prolyl isomerase PIN1 regulates DNA double-strand break repair by counteracting DNA end resection
    • Steger, M. et al. Prolyl isomerase PIN1 regulates DNA double-strand break repair by counteracting DNA end resection. Mol. Cell 50, 333-343 (2013).
    • (2013) Mol. Cell , vol.50 , pp. 333-343
    • Steger, M.1
  • 9
    • 79952235291 scopus 로고    scopus 로고
    • Dynamics of DNA damage response proteins at DNA breaks: A focus on protein modifications
    • Polo, S. E. & Jackson, S. P. Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications. Genes Dev. 25, 409-433 (2011).
    • (2011) Genes Dev. , vol.25 , pp. 409-433
    • Polo, S.E.1    Jackson, S.P.2
  • 10
    • 84878677036 scopus 로고    scopus 로고
    • KAT5 tyrosine phosphorylation couples chromatin sensing to ATM signalling
    • Kaidi, A. & Jackson, S. P. KAT5 tyrosine phosphorylation couples chromatin sensing to ATM signalling. Nature 498, 70-74 (2013).
    • (2013) Nature , vol.498 , pp. 70-74
    • Kaidi, A.1    Jackson, S.P.2
  • 11
    • 29244434544 scopus 로고    scopus 로고
    • MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks
    • Stucki, M. et al. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell 123, 1213-1226 (2005).
    • (2005) Cell , vol.123 , pp. 1213-1226
    • Stucki, M.1
  • 12
    • 34748902384 scopus 로고    scopus 로고
    • Global chromatin compaction limits the strength of the DNA damage response
    • Murga, M. et al. Global chromatin compaction limits the strength of the DNA damage response. J. Cell Biol. 178, 1101-1108 (2007).
    • (2007) J. Cell Biol. , vol.178 , pp. 1101-1108
    • Murga, M.1
  • 13
    • 84878972552 scopus 로고    scopus 로고
    • The bromodomain protein Brd4 insulates chromatin from DNA damage signalling
    • Floyd, S. R. et al. The bromodomain protein Brd4 insulates chromatin from DNA damage signalling. Nature 498, 246-250 (2013).
    • (2013) Nature , vol.498 , pp. 246-250
    • Floyd, S.R.1
  • 14
    • 31444445458 scopus 로고    scopus 로고
    • A phosphatase complex that dephosphorylates γh2AX regulates DNA damage checkpoint recovery
    • Keogh, M. C. et al. A phosphatase complex that dephosphorylates γH2AX regulates DNA damage checkpoint recovery. Nature 439, 497-501 (2006).
    • (2006) Nature , vol.439 , pp. 497-501
    • Keogh, M.C.1
  • 15
    • 46149117962 scopus 로고    scopus 로고
    • A PP4-phosphatase complex dephosphorylates γ-H2AX generated during DNA replication
    • Chowdhury, D. et al. A PP4-phosphatase complex dephosphorylates γ-H2AX generated during DNA replication. Mol. Cell 31, 33-46 (2008).
    • (2008) Mol. Cell , vol.31 , pp. 33-46
    • Chowdhury, D.1
  • 16
    • 77952825226 scopus 로고    scopus 로고
    • Wip1 directly dephosphorylates γ-H2AX and attenuates the DNA damage response
    • Cha, H. et al. Wip1 directly dephosphorylates γ-H2AX and attenuates the DNA damage response. Cancer Res. 70, 4112-4122 (2010).
    • (2010) Cancer Res. , vol.70 , pp. 4112-4122
    • Cha, H.1
  • 17
    • 77749334700 scopus 로고    scopus 로고
    • Protein phosphatase 6 interacts with the DNA-dependent protein kinase catalytic subunit and dephosphorylates γ-H2AX
    • Douglas, P. et al. Protein phosphatase 6 interacts with the DNA-dependent protein kinase catalytic subunit and dephosphorylates γ-H2AX. Mol. Cell. Biol. 30, 1368-1381 (2010).
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1368-1381
    • Douglas, P.1
  • 18
    • 77951064789 scopus 로고    scopus 로고
    • Wip1 phosphatase is associated with chromatin and dephosphorylates γh2AX to promote checkpoint inhibition
    • Macurek, L. et al. Wip1 phosphatase is associated with chromatin and dephosphorylates γH2AX to promote checkpoint inhibition. Oncogene 29, 2281-2291 (2010).
    • (2010) Oncogene , vol.29 , pp. 2281-2291
    • Macurek, L.1
  • 19
    • 77951244965 scopus 로고    scopus 로고
    • Wild-type p53-induced phosphatase 1 dephosphorylates histone variant γ-H2AX and suppresses DNA double strand break repair
    • Moon, S. H. et al. Wild-type p53-induced phosphatase 1 dephosphorylates histone variant γ-H2AX and suppresses DNA double strand break repair. J. Biol. Chem. 285, 12935-12947 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 12935-12947
    • Moon, S.H.1
  • 20
    • 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 457, 57-64 (2008).
    • (2008) Nature , vol.457 , pp. 57-64
    • Xiao, A.1
  • 21
    • 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 458, 591-596 (2009).
    • (2009) Nature , vol.458 , pp. 591-596
    • Cook, P.J.1
  • 22
    • 84865975058 scopus 로고    scopus 로고
    • Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1
    • Singh, N. et al. Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1. Proc. Natl Acad. Sci. USA 109, 14381-14386 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 14381-14386
    • Singh, N.1
  • 23
    • 67650034511 scopus 로고    scopus 로고
    • BRIT1/MCPH1 links chromatin remodelling to DNA damage response
    • Peng, G. et al. BRIT1/MCPH1 links chromatin remodelling to DNA damage response. Nature Cell Biol. 11, 865-872 (2009).
    • (2009) Nature Cell Biol. , vol.11 , pp. 865-872
    • Peng, G.1
  • 24
    • 36849000716 scopus 로고    scopus 로고
    • MCPH1 functions in an H2AX-dependent but MDC1-independent pathway in response to DNA damage
    • Wood, J. L., Singh, N., Mer, G. & Chen, J. MCPH1 functions in an H2AX-dependent but MDC1-independent pathway in response to DNA damage. J. Biol. Chem. 282, 35416-35423 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 35416-35423
    • Wood, J.L.1    Singh, N.2    Mer, G.3    Chen, J.4
  • 25
    • 67650230540 scopus 로고    scopus 로고
    • Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A. X is mediated by the protein phosphatase eyes absent
    • Krishnan, N. et al. Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A. X is mediated by the protein phosphatase eyes absent. J. Biol. Chem. 284, 16066-16070 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 16066-16070
    • Krishnan, N.1
  • 26
    • 84861765707 scopus 로고    scopus 로고
    • RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair
    • Galanty, Y., Belotserkovskaya, R., Coates, J. & Jackson, S. P. RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair. Genes Dev. 26, 1179-1195 (2012).
    • (2012) Genes Dev. , vol.26 , pp. 1179-1195
    • Galanty, Y.1    Belotserkovskaya, R.2    Coates, J.3    Jackson, S.P.4
  • 27
    • 84863846456 scopus 로고    scopus 로고
    • Sumoylation of MDC1 is important for proper DNA damage response
    • Luo, K., Zhang, H., Wang, L., Yuan, J. & Lou, Z. Sumoylation of MDC1 is important for proper DNA damage response. EMBO J. 31, 3008-30019 (2012).
    • (2012) EMBO J. , vol.31 , pp. 3008-30019
    • Luo, K.1    Zhang, H.2    Wang, L.3    Yuan, J.4    Lou, Z.5
  • 28
    • 57649130600 scopus 로고    scopus 로고
    • Disassembly of MDC1 foci is controlled by ubiquitin-proteasome-dependent degradation
    • Shi, W. et al. Disassembly of MDC1 foci is controlled by ubiquitin-proteasome-dependent degradation. J. Biol. Chem. 283, 31608-31616 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 31608-31616
    • Shi, W.1
  • 29
    • 84873704658 scopus 로고    scopus 로고
    • RNF4 is required for DNA double-strand break repair in vivo
    • Vyas, R. et al. RNF4 is required for DNA double-strand break repair in vivo. Cell Death Differ. 20, 490-502 (2013).
    • (2013) Cell Death Differ. , vol.20 , pp. 490-502
    • Vyas, R.1
  • 30
    • 84861784690 scopus 로고    scopus 로고
    • SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage
    • Yin, Y. et al. SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage. Genes Dev. 26, 1196-1208 (2012).
    • (2012) Genes Dev. , vol.26 , pp. 1196-1208
    • Yin, Y.1
  • 32
    • 33746766974 scopus 로고    scopus 로고
    • A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response
    • Zhang, D., Zaugg, K., Mak, T. W. & Elledge, S. J. A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response. Cell 126, 529-542 (2006).
    • (2006) Cell , vol.126 , pp. 529-542
    • Zhang, D.1    Zaugg, K.2    Mak, T.W.3    Elledge, S.J.4
  • 33
    • 36249031962 scopus 로고    scopus 로고
    • RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly
    • Huen, M. S. Y. et al. RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell 131, 901-914 (2007).
    • (2007) Cell , vol.131 , pp. 901-914
    • Huen, M.S.Y.1
  • 34
    • 36749084931 scopus 로고    scopus 로고
    • Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase
    • Kolas, N. K. et al. Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase. Science 318, 1637-1640 (2007).
    • (2007) Science , vol.318 , pp. 1637-1640
    • Kolas, N.K.1
  • 35
    • 36248966246 scopus 로고    scopus 로고
    • RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins
    • Mailand, N. et al. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 131, 887-900 (2007).
    • (2007) Cell , vol.131 , pp. 887-900
    • Mailand, N.1
  • 36
    • 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 104, 20759-20763 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 20759-20763
    • Wang, B.1    Elledge, S.J.2
  • 37
    • 59049091728 scopus 로고    scopus 로고
    • RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins
    • Doil, C. et al. RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell 136, 435-446 (2009).
    • (2009) Cell , vol.136 , pp. 435-446
    • Doil, C.1
  • 38
    • 84864919890 scopus 로고    scopus 로고
    • Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks
    • Panier, S. et al. Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks. Mol. Cell 47, 383-395 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 383-395
    • Panier, S.1
  • 39
    • 59049103900 scopus 로고    scopus 로고
    • The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage
    • Stewart, G. S. et al. The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell 136, 420-434 (2009).
    • (2009) Cell , vol.136 , pp. 420-434
    • Stewart, G.S.1
  • 40
    • 63049101044 scopus 로고    scopus 로고
    • Regulatory ubiquitylation in response to DNA double-strand breaks
    • Panier, S. & Durocher, D. Regulatory ubiquitylation in response to DNA double-strand breaks. DNA Repair 8, 436-443 (2009).
    • (2009) DNA Repair , vol.8 , pp. 436-443
    • Panier, S.1    Durocher, D.2
  • 41
    • 84876886904 scopus 로고    scopus 로고
    • Regulation of DNA damage responses by ubiquitin and SUMO
    • Jackson, S. P. & Durocher, D. Regulation of DNA damage responses by ubiquitin and SUMO. Mol. Cell 49, 795-807 (2013).
    • (2013) Mol. Cell , vol.49 , pp. 795-807
    • Jackson, S.P.1    Durocher, D.2
  • 42
    • 67349168142 scopus 로고    scopus 로고
    • RAD18 transmits DNA damage signalling to elicit homologous recombination repair
    • Huang, J. et al. RAD18 transmits DNA damage signalling to elicit homologous recombination repair. Nature Cell Biol. 11, 592-603 (2009).
    • (2009) Nature Cell Biol. , vol.11 , pp. 592-603
    • Huang, J.1
  • 43
    • 77953720192 scopus 로고    scopus 로고
    • ATM-dependent chromatin changes silence transcription in cis to DNA double-strand breaks
    • Shanbhag, N. M., Rafalska-Metcalf, I. U., Balane- Bolivar, C., Janicki, S. M. & Greenberg, R. A. ATM-dependent chromatin changes silence transcription in cis to DNA double-strand breaks. Cell 141, 970-981 (2010).
    • (2010) Cell , vol.141 , pp. 970-981
    • Shanbhag, N.M.1    Rafalska-Metcalf, I.U.2    Balane- Bolivar, C.3    Janicki, S.M.4    Greenberg, R.A.5
  • 44
    • 84862986431 scopus 로고    scopus 로고
    • HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes
    • Bekker-Jensen, S. et al. HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Nature Cell Biol. 12, 80-86 (2009).
    • (2009) Nature Cell Biol. , vol.12 , pp. 80-86
    • Bekker-Jensen, S.1
  • 45
    • 84861941745 scopus 로고    scopus 로고
    • DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding zinc finger
    • Danielsen, J. R. et al. DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding zinc finger. J. Cell Biol. 197, 179-187 (2012).
    • (2012) J. Cell Biol. , vol.197 , pp. 179-187
    • Danielsen, J.R.1
  • 46
    • 84885940995 scopus 로고    scopus 로고
    • The ubiquitin specific protease USP34 promotes ubiquitin signaling at DNA double-strand breaks
    • Sy, S. M. et al. The ubiquitin specific protease USP34 promotes ubiquitin signaling at DNA double-strand breaks. Nucleic Acids Res. http://dx.doi.org/10. 1093/nar/gkt622 (2013).
    • (2013) Nucleic Acids Res.
    • Sy, S.M.1
  • 47
    • 77955867565 scopus 로고    scopus 로고
    • Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1
    • Nakada, S. et al. Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1. Nature 466, 941-946 (2010).
    • (2010) Nature , vol.466 , pp. 941-946
    • Nakada, S.1
  • 48
    • 61449120240 scopus 로고    scopus 로고
    • Structural basis and specificity of human otubain 1-mediated deubiquitination
    • Edelmann, M. J. et al. Structural basis and specificity of human otubain 1-mediated deubiquitination. Biochem. J. 418, 379-390 (2009).
    • (2009) Biochem. J. , vol.418 , pp. 379-390
    • Edelmann, M.J.1
  • 49
    • 84866388311 scopus 로고    scopus 로고
    • RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage signaling
    • Mattiroli, F. et al. RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage signaling. Cell 150, 1182-1195 (2012).
    • (2012) Cell , vol.150 , pp. 1182-1195
    • Mattiroli, F.1
  • 50
    • 84856801739 scopus 로고    scopus 로고
    • OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function
    • Juang, Y.-C. et al. OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function. Mol. Cell 45, 384-397 (2012).
    • (2012) Mol. Cell , vol.45 , pp. 384-397
    • Juang, Y.-C.1
  • 51
    • 84864386119 scopus 로고    scopus 로고
    • Molecular basis of K63-linked polyubiquitination inhibition by the interaction between human deubiquitinating enzyme OTUB1 and ubiquitin- conjugating enzyme UBC13
    • Sato, Y. et al. Molecular basis of K63-linked polyubiquitination inhibition by the interaction between human deubiquitinating enzyme OTUB1 and ubiquitin-conjugating enzyme UBC13. J. Biol. Chem. 287, 25860-25868 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 25860-25868
    • Sato, Y.1
  • 52
    • 84862806447 scopus 로고    scopus 로고
    • The mechanism of OTUB1-mediated inhibition of ubiquitination
    • Wiener, R., Zhang, X., Wang, T. & Wolberger, C. The mechanism of OTUB1-mediated inhibition of ubiquitination. Nature 483, 618-622 (2012).
    • (2012) Nature , vol.483 , pp. 618-622
    • Wiener, R.1    Zhang, X.2    Wang, T.3    Wolberger, C.4
  • 53
    • 84864977706 scopus 로고    scopus 로고
    • Ring finger protein RNF169 antagonises the ubiquitin-dependent signaling cascade at sites of DNA damage
    • Chen, J., Feng, W., Jiang, J., Deng, Y. & Huen, M. S. Y. Ring finger protein RNF169 antagonises the ubiquitin-dependent signaling cascade at sites of DNA damage. J. Biol. Chem.287, 27715-2722 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 27715-32722
    • Chen, J.1    Feng, W.2    Jiang, J.3    Deng, Y.4    Huen, M.S.Y.5
  • 54
    • 84861948252 scopus 로고    scopus 로고
    • Human RNF169 is a negative regulator of the ubiquitin-dependent response to DNA double-strand breaks
    • Poulsen, M., Lukas, C., Lukas, J., Bekker-Jensen, S. & Mailand, N. Human RNF169 is a negative regulator of the ubiquitin-dependent response to DNA double-strand breaks. J. Cell Biol. 197, 189-199 (2012).
    • (2012) J. Cell Biol. , vol.197 , pp. 189-199
    • Poulsen, M.1    Lukas, C.2    Lukas, J.3    Bekker-Jensen, S.4    Mailand, N.5
  • 55
    • 62649104153 scopus 로고    scopus 로고
    • K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1
    • Cooper, E. M. et al. K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1. EMBO J. 28, 621-631 (2009).
    • (2009) EMBO J. , vol.28 , pp. 621-631
    • Cooper, E.M.1
  • 56
    • 77951227161 scopus 로고    scopus 로고
    • Specificity of the BRISC deubiquitinating enzyme is not due to selective binding to Lys63-linked polyubiquitin
    • Cooper, E. M., Boeke, J. D. & Cohen, R. E. Specificity of the BRISC deubiquitinating enzyme is not due to selective binding to Lys63-linked polyubiquitin. J. Biol. Chem. 285, 10344-10352 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 10344-10352
    • Cooper, E.M.1    Boeke, J.D.2    Cohen, R.E.3
  • 57
    • 77957260099 scopus 로고    scopus 로고
    • The Lys63-specific deubiquitinating enzyme BRCC36 is regulated by two scaffold proteins localizing in different subcellular compartments
    • Feng, L., Wang, J. & Chen, J. The Lys63-specific deubiquitinating enzyme BRCC36 is regulated by two scaffold proteins localizing in different subcellular compartments. J. Biol. Chem. 285, 30982-30988 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 30982-30988
    • Feng, L.1    Wang, J.2    Chen, J.3
  • 58
    • 33744944054 scopus 로고    scopus 로고
    • BRCC36 is essential for ionizing radiation-induced BRCA1 phosphorylation and nuclear foci formation
    • Chen, X. BRCC36 is essential for ionizing radiation-induced BRCA1 phosphorylation and nuclear foci formation. Cancer Res. 66, 5039-5046 (2006).
    • (2006) Cancer Res. , vol.66 , pp. 5039-5046
    • Chen, X.1
  • 59
    • 34249949779 scopus 로고    scopus 로고
    • RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites
    • Sobhian, B. et al. RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites. Science 316, 1198-1202 (2007).
    • (2007) Science , vol.316 , pp. 1198-1202
    • Sobhian, B.1
  • 60
    • 34249950879 scopus 로고    scopus 로고
    • Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response
    • Kim, H., Chen, J. & Yu, X. Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response. Science 316, 1202-1205 (2007).
    • (2007) Science , vol.316 , pp. 1202-1205
    • Kim, H.1    Chen, J.2    Yu, X.3
  • 61
    • 34249946686 scopus 로고    scopus 로고
    • Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response
    • Wang, B. et al. Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response. Science 316, 1194-1198 (2007).
    • (2007) Science , vol.316 , pp. 1194-1198
    • Wang, B.1
  • 62
    • 79953869356 scopus 로고    scopus 로고
    • The BRCA1- RAP80 complex regulates DNA repair mechanism utilization by restricting end resection
    • Coleman, K. A. & Greenberg, R. A. The BRCA1- RAP80 complex regulates DNA repair mechanism utilization by restricting end resection. J. Biol. Chem. 286, 13669-13680 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 13669-13680
    • Coleman, K.A.1    Greenberg, R.A.2
  • 63
    • 84863793933 scopus 로고    scopus 로고
    • A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase
    • Gatti, M. et al. A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase. Cell Cycle 11, 2538-2544 (2012).
    • (2012) Cell Cycle , vol.11 , pp. 2538-2544
    • Gatti, M.1
  • 64
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander, D., Clague, M. J. & Urbé, S. Breaking the chains: structure and function of the deubiquitinases. Nature Rev. Mol. Cell Biol. 10, 550-563 (2009).
    • (2009) Nature Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbé, S.3
  • 65
    • 34447549100 scopus 로고    scopus 로고
    • Proteasomes and proteasome activator 200 kDa (PA200) accumulate on chromatin in response to ionizing radiation
    • Blickwedehl, J. et al. Proteasomes and proteasome activator 200 kDa (PA200) accumulate on chromatin in response to ionizing radiation. Radi. Res. 167, 663-674 (2007).
    • (2007) Radi. Res. , vol.167 , pp. 663-674
    • Blickwedehl, J.1
  • 66
    • 84867101138 scopus 로고    scopus 로고
    • The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response
    • Butler, L. R. et al. The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response. EMBO J. 31, 3918-3934 (2012).
    • (2012) EMBO J. , vol.31 , pp. 3918-3934
    • Butler, L.R.1
  • 67
    • 84878758649 scopus 로고    scopus 로고
    • The deubiquitylating enzyme USP44 counteracts the DNA double-strand break response mediated by the RNF8 and RNF168 ubiquitin ligases
    • Mosbech, A., Lukas, C., Bekker-Jensen, S. & Mailand, N. The deubiquitylating enzyme USP44 counteracts the DNA double-strand break response mediated by the RNF8 and RNF168 ubiquitin ligases. J. Biol. Chem. 288, 16579-16587 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 16579-16587
    • Mosbech, A.1    Lukas, C.2    Bekker-Jensen, S.3    Mailand, N.4
  • 68
    • 35548986309 scopus 로고    scopus 로고
    • Regulation of cell cycle progression and gene expression by H2A deubiquitination
    • Joo, H.-Y. et al. Regulation of cell cycle progression and gene expression by H2A deubiquitination. Nature 449, 1068-1072 (2007).
    • (2007) Nature , vol.449 , pp. 1068-1072
    • Joo, H.-Y.1
  • 69
    • 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. et al. Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 127, 1361-1373 (2006).
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1
  • 70
    • 84879888213 scopus 로고    scopus 로고
    • 53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark
    • Fradet-Turcotte, A. et al. 53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark. Nature 499, 50-54 (2013).
    • (2013) Nature , vol.499 , pp. 50-54
    • Fradet-Turcotte, A.1
  • 71
    • 59449094470 scopus 로고    scopus 로고
    • An oligomerized 53BP1 Tudor domain suffices for recognition of DNA double-strand breaks
    • Zgheib, O., Pataky, K., Brugger, J. & Halazonetis, T. D. An oligomerized 53BP1 Tudor domain suffices for recognition of DNA double-strand breaks. Mol. Cell. Biol. 29, 1050-1058 (2009).
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1050-1058
    • Zgheib, O.1    Pataky, K.2    Brugger, J.3    Halazonetis, T.D.4
  • 72
    • 84859895529 scopus 로고    scopus 로고
    • RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites
    • Mallette, F. A. et al. RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites. EMBO J. 31, 1865-1878 (2012).
    • (2012) EMBO J. , vol.31 , pp. 1865-1878
    • Mallette, F.A.1
  • 73
    • 84886387458 scopus 로고    scopus 로고
    • Role of p97/VCP (Cdc48) in genome stability
    • Vaz, B., Halder, S. & Ramadan, K. Role of p97/VCP (Cdc48) in genome stability. Front. Genet. 4, 60 (2013).
    • (2013) Front. Genet. , vol.4 , pp. 60
    • Vaz, B.1    Halder, S.2    Ramadan, K.3
  • 74
    • 80455145246 scopus 로고    scopus 로고
    • The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA double-strand breaks
    • Meerang, M. et al. The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA double-strand breaks. Nature Cell Biol. 13, 1376-1382 (2011).
    • (2011) Nature Cell Biol. , vol.13 , pp. 1376-1382
    • Meerang, M.1
  • 75
    • 84877976173 scopus 로고    scopus 로고
    • Histone H4 deacetylation facilitates 53BP1 DNA damage signaling and double-strand break repair
    • Hsiao, K. Y. & Mizzen, C. A. Histone H4 deacetylation facilitates 53BP1 DNA damage signaling and double-strand break repair. J. Mol. Cell Biol. 5, 157-165 (2013).
    • (2013) J. Mol. Cell Biol. , vol.5 , pp. 157-165
    • Hsiao, K.Y.1    Mizzen, C.A.2
  • 76
    • 84875224166 scopus 로고    scopus 로고
    • Acetylation limits 53BP1 association with damaged chromatin to promote homologous recombination
    • Tang, J. et al. Acetylation limits 53BP1 association with damaged chromatin to promote homologous recombination. Nature Struct. Mol. Biol. 20, 317-325 (2013).
    • (2013) Nature Struct. Mol. Biol. , vol.20 , pp. 317-325
    • Tang, J.1
  • 77
    • 84860456242 scopus 로고    scopus 로고
    • Removal of shelterin reveals the telomere end-protection problem
    • Sfeir, A. & de Lange, T. Removal of shelterin reveals the telomere end-protection problem. Science 336, 593-597 (2012).
    • (2012) Science , vol.336 , pp. 593-597
    • Sfeir, A.1    De Lange, T.2
  • 78
    • 80052398381 scopus 로고    scopus 로고
    • How shelterin solves the telomere end-protection problem
    • de Lange, T. How shelterin solves the telomere end-protection problem. Cold Spring Harb. Symp. Quant. Biol. 75, 167-177 (2010).
    • (2010) Cold Spring Harb. Symp. Quant. Biol. , vol.75 , pp. 167-177
    • De Lange, T.1
  • 79
    • 0344441890 scopus 로고    scopus 로고
    • A DNA damage checkpoint response in telomere-initiated senescence
    • d'Adda di Fagagna, F. et al. A DNA damage checkpoint response in telomere-initiated senescence. Nature 426, 194-198 (2003).
    • (2003) Nature , vol.426 , pp. 194-198
    • D'adda Di Fagagna, F.1
  • 80
    • 34548317418 scopus 로고    scopus 로고
    • Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1
    • Denchi, E. L. & de Lange, T. Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1. Nature 448, 1068-1071 (2007).
    • (2007) Nature , vol.448 , pp. 1068-1071
    • Denchi, E.L.1    De Lange, T.2
  • 81
    • 0042420304 scopus 로고    scopus 로고
    • DNA damage foci at dysfunctional telomeres
    • Takai, H., Smogorzewska, A. & de Lange, T. DNA damage foci at dysfunctional telomeres. Curr. Biol. 13, 1549-1556 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 1549-1556
    • Takai, H.1    Smogorzewska, A.2    De Lange, T.3
  • 82
    • 0032489012 scopus 로고    scopus 로고
    • TRF2 protects human telomeres from end-to-end fusions
    • van Steensel, B., Smogorzewska, A. & de Lange, T. TRF2 protects human telomeres from end-to-end fusions. Cell 92, 401-413 (1998).
    • (1998) Cell , vol.92 , pp. 401-413
    • Van Steensel, B.1    Smogorzewska, A.2    De Lange, T.3
  • 83
    • 84874351566 scopus 로고    scopus 로고
    • A two-step mechanism for TRF2-mediated chromosome-end protection
    • Okamoto, K. et al. A two-step mechanism for TRF2-mediated chromosome-end protection. Nature 494, 502-505 (2013).
    • (2013) Nature , vol.494 , pp. 502-505
    • Okamoto, K.1
  • 84
    • 19344374569 scopus 로고    scopus 로고
    • The telomeric protein TRF2 binds the ATM kinase and can inhibit the ATM-dependent DNA damage response
    • Karlseder, J. et al. The telomeric protein TRF2 binds the ATM kinase and can inhibit the ATM-dependent DNA damage response. PLoS Biol. 2, E240 (2004).
    • (2004) PLoS Biol. , vol.2
    • Karlseder, J.1
  • 85
    • 77954997032 scopus 로고    scopus 로고
    • DNA damage signaling in response to double-strand breaks during mitosis
    • Giunta, S., Belotserkovskaya, R. & Jackson, S. P. DNA damage signaling in response to double-strand breaks during mitosis. J. Cell Biol. 190, 197-207 (2010).
    • (2010) J. Cell Biol. , vol.190 , pp. 197-207
    • Giunta, S.1    Belotserkovskaya, R.2    Jackson, S.P.3
  • 86
    • 75749130721 scopus 로고    scopus 로고
    • A mitotic phosphorylation feedback network connects Cdk1, Plk1, 53BP1, and Chk2 to inactivate the G2/M DNA damage checkpoint
    • van Vugt, M. A. et al. A mitotic phosphorylation feedback network connects Cdk1, Plk1, 53BP1, and Chk2 to inactivate the G2/M DNA damage checkpoint. PLoS Biol. 8, e1000287 (2010).
    • (2010) PLoS Biol. , vol.8
    • Van Vugt, M.A.1
  • 87
    • 80053903895 scopus 로고    scopus 로고
    • DNA damage response is suppressed by the high cyclin-dependent kinase 1 activity in mitotic mammalian cells
    • Zhang, W., Peng, G., Lin, S. Y. & Zhang, P. DNA damage response is suppressed by the high cyclin-dependent kinase 1 activity in mitotic mammalian cells. J. Biol. Chem. 286, 35899-35905 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 35899-35905
    • Zhang, W.1    Peng, G.2    Lin, S.Y.3    Zhang, P.4
  • 88
    • 79959848568 scopus 로고    scopus 로고
    • The intrinsic antiviral defense to incoming HSV-1 genomes includes specific DNA repair proteins and is counteracted by the viral protein ICP0
    • Lilley, C. E., Chaurushiya, M. S., Boutell, C., Everett, R. D. & Weitzman, M. D. The intrinsic antiviral defense to incoming HSV-1 genomes includes specific DNA repair proteins and is counteracted by the viral protein ICP0. PLoS Pathog. 7, e1002084 (2011).
    • (2011) PLoS Pathog. , vol.7
    • Lilley, C.E.1    Chaurushiya, M.S.2    Boutell, C.3    Everett, R.D.4    Weitzman, M.D.5
  • 89
    • 77649338569 scopus 로고    scopus 로고
    • A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses
    • Lilley, C. E. et al. A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses. EMBO J. 29, 943-955 (2010).
    • (2010) EMBO J. , vol.29 , pp. 943-955
    • Lilley, C.E.1
  • 90
    • 84859731169 scopus 로고    scopus 로고
    • Viral E3 ubiquitin ligase-mediated degradation of a cellular E3: Viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA domain
    • Chaurushiya, M. S. et al. Viral E3 ubiquitin ligase-mediated degradation of a cellular E3: viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA domain. Mol. Cell 46, 79-90 (2012).
    • (2012) Mol. Cell , vol.46 , pp. 79-90
    • Chaurushiya, M.S.1
  • 91
    • 80053459914 scopus 로고    scopus 로고
    • A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence
    • Boutell, C. et al. A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence. PLoS Pathog. 7, e1002245 (2011).
    • (2011) PLoS Pathog. , vol.7
    • Boutell, C.1
  • 92
    • 80052757401 scopus 로고    scopus 로고
    • Changing the ubiquitin landscape during viral manipulation of the DNA damage response
    • Weitzman, M. D., Lilley, C. E. & Chaurushiya, M. S. Changing the ubiquitin landscape during viral manipulation of the DNA damage response. FEBS Lett. 585, 2897-2906 (2011).
    • (2011) FEBS Lett. , vol.585 , pp. 2897-2906
    • Weitzman, M.D.1    Lilley, C.E.2    Chaurushiya, M.S.3
  • 93
    • 80755187806 scopus 로고    scopus 로고
    • Double-strand break end resection and repair pathway choice
    • Symington, L. S. & Gautier, J. Double-strand break end resection and repair pathway choice. Annu. Rev. Genet. 45, 247-271 (2011).
    • (2011) Annu. Rev. Genet. , vol.45 , pp. 247-271
    • Symington, L.S.1    Gautier, J.2
  • 94
    • 84865364870 scopus 로고    scopus 로고
    • Playing the end game: DNA double-strand break repair pathway choice
    • Chapman, J. R., Taylor, M. R. G. & Boulton, S. J. Playing the end game: DNA double-strand break repair pathway choice. Mol. Cell 47, 497-510 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 497-510
    • Chapman, J.R.1    Taylor, M.R.G.2    Boulton, S.J.3
  • 95
    • 77953229115 scopus 로고    scopus 로고
    • The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway
    • Lieber, M. R. The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway. Annu. Rev. Biochem. 79, 181-211 (2010).
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 181-211
    • Lieber, M.R.1
  • 96
    • 84873488846 scopus 로고    scopus 로고
    • 53BP1 regulates DSB repair using Rif1 to control 5′ end resection
    • Zimmermann, M., Lottersberger, F., Buonomo, S. B., Sfeir, A. & de Lange, T. 53BP1 regulates DSB repair using Rif1 to control 5′ end resection. Science 339, 700-704 (2013).
    • (2013) Science , vol.339 , pp. 700-704
    • Zimmermann, M.1    Lottersberger, F.2    Buonomo, S.B.3    Sfeir, A.4    De Lange, T.5
  • 97
    • 84876527317 scopus 로고    scopus 로고
    • RIF1 counteracts BRCA1-mediated end resection during DNA repair
    • Feng, L., Fong, K.-W., Wang, J., Wang, W. & Chen, J. RIF1 counteracts BRCA1-mediated end resection during DNA repair. J. Biol. Chem. 288, 11135-11143 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 11135-11143
    • Feng, L.1    Fong, K.-W.2    Wang, J.3    Wang, W.4    Chen, J.5
  • 98
    • 84876877091 scopus 로고    scopus 로고
    • A cell cycle-dependent regulatory circuit composed of 53BP1-RIF1 and BRCA1-CtIP controls DNA repair pathway choice
    • Escribano-Diaz, C. et al. A cell cycle-dependent regulatory circuit composed of 53BP1-RIF1 and BRCA1-CtIP controls DNA repair pathway choice. Mol. Cell 49, 872-883 (2013).
    • (2013) Mol. Cell , vol.49 , pp. 872-883
    • Escribano-Diaz, C.1
  • 99
    • 84873526612 scopus 로고    scopus 로고
    • Rif1 prevents resection of DNA breaks and promotes immunoglobulin class switching
    • Di Virgilio, M. et al. Rif1 prevents resection of DNA breaks and promotes immunoglobulin class switching. Science 339, 711-715 (2013).
    • (2013) Science , vol.339 , pp. 711-715
    • Di Virgilio, M.1
  • 100
    • 84876855215 scopus 로고    scopus 로고
    • RIF1 is essential for 53BP1-dependent nonhomologous end joining and suppression of DNA double-strand break resection
    • Chapman, J. R. et al. RIF1 is essential for 53BP1-dependent nonhomologous end joining and suppression of DNA double-strand break resection. Mol. Cell 49, 858-871 (2013).
    • (2013) Mol. Cell , vol.49 , pp. 858-871
    • Chapman, J.R.1
  • 101
    • 84878893538 scopus 로고    scopus 로고
    • 53BP1 mediates productive and mutagenic DNA repair through distinct phosphoprotein interactions
    • Callen, E. et al. 53BP1 mediates productive and mutagenic DNA repair through distinct phosphoprotein interactions. Cell 153, 1266-1280 (2013).
    • (2013) Cell , vol.153 , pp. 1266-1280
    • Callen, E.1
  • 102
    • 80053447704 scopus 로고    scopus 로고
    • Release of Ku and MRN from DNA ends by Mre11 nuclease activity and Ctp1 is required for homologous recombination repair of double-strand breaks
    • Langerak, P., Mejia-Ramirez, E., Limbo, O. & Russell, P. Release of Ku and MRN from DNA ends by Mre11 nuclease activity and Ctp1 is required for homologous recombination repair of double-strand breaks. PLoS Genet. 7, e1002271 (2011).
    • (2011) PLoS Genet. , vol.7
    • Langerak, P.1    Mejia-Ramirez, E.2    Limbo, O.3    Russell, P.4
  • 103
    • 77956550868 scopus 로고    scopus 로고
    • Human SIRT6 promotes DNA end resection through CtIP deacetylation
    • Kaidi, A., Weinert, B. T., Choudhary, C. & Jackson, S. P. Human SIRT6 promotes DNA end resection through CtIP deacetylation. Science 329, 1348-1353 (2010).
    • (2010) Science , vol.329 , pp. 1348-1353
    • Kaidi, A.1    Weinert, B.T.2    Choudhary, C.3    Jackson, S.P.4
  • 104
    • 77955475870 scopus 로고    scopus 로고
    • Regulation of DNA repair through deSUMOylation and SUMOylation of replication protein A complex
    • Dou, H., Huang, C., Singh, M., Carpenter, P. B. & Yeh, E. T. Regulation of DNA repair through deSUMOylation and SUMOylation of replication protein A complex. Mol. Cell 39, 333-345 (2010).
    • (2010) Mol. Cell , vol.39 , pp. 333-345
    • Dou, H.1    Huang, C.2    Singh, M.3    Carpenter, P.B.4    Yeh, E.T.5
  • 105
    • 67649637509 scopus 로고    scopus 로고
    • Srs2 disassembles Rad51 filaments by a protein-protein interaction triggering ATP turnover and dissociation of Rad51 from DNA
    • Antony, E. et al. Srs2 disassembles Rad51 filaments by a protein-protein interaction triggering ATP turnover and dissociation of Rad51 from DNA. Mol. Cell 35, 105-115 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 105-115
    • Antony, E.1
  • 106
    • 0037673941 scopus 로고    scopus 로고
    • DNA helicase Srs2 disrupts the Rad51 presynaptic filament
    • Krejci, L. et al. DNA helicase Srs2 disrupts the Rad51 presynaptic filament. Nature 423, 305-309 (2003).
    • (2003) Nature , vol.423 , pp. 305-309
    • Krejci, L.1
  • 107
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments
    • Veaute, X. et al. The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments. Nature 423, 309-312 (2003).
    • (2003) Nature , vol.423 , pp. 309-312
    • Veaute, X.1
  • 108
    • 84855901029 scopus 로고    scopus 로고
    • Inhibition of homologous recombination by the PCNA-interacting protein PARI
    • Moldovan, G.-L. et al. Inhibition of homologous recombination by the PCNA-interacting protein PARI. Mol. Cell 45, 75-86 (2012).
    • (2012) Mol. Cell , vol.45 , pp. 75-86
    • Moldovan, G.-L.1
  • 109
    • 84555196106 scopus 로고    scopus 로고
    • BRCA1 and BRCA2: Different roles in a common pathway of genome protection
    • Roy, R., Chun, J. & Powell, S. N. BRCA1 and BRCA2: different roles in a common pathway of genome protection. Nature Rev. Cancer 12, 68-78 (2012).
    • (2012) Nature Rev. Cancer , vol.12 , pp. 68-78
    • Roy, R.1    Chun, J.2    Powell, S.N.3
  • 110
    • 15844373362 scopus 로고    scopus 로고
    • CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for recombinational repair
    • Esashi, F. et al. CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for recombinational repair. Nature 434, 598-604 (2005).
    • (2005) Nature , vol.434 , pp. 598-604
    • Esashi, F.1
  • 111
    • 81955161844 scopus 로고    scopus 로고
    • DNA double-strand break repair pathways, chromosomal rearrangements and cancer
    • Kasparek, T. R. & Humphrey, T. C. DNA double-strand break repair pathways, chromosomal rearrangements and cancer. Seminars Cell Dev. Biol. 22, 886-897 (2011).
    • (2011) Seminars Cell Dev. Biol. , vol.22 , pp. 886-897
    • Kasparek, T.R.1    Humphrey, T.C.2
  • 112
    • 3543064379 scopus 로고    scopus 로고
    • Human Rif1, ortholog of a yeast telomeric protein, is regulated by ATM and 53BP1 and functions in the S-phase checkpoint
    • Silverman, J., Takai, H., Buonomo, S. B. C., Eisenhaber, F. & de Lange, T. Human Rif1, ortholog of a yeast telomeric protein, is regulated by ATM and 53BP1 and functions in the S-phase checkpoint. Genes Dev. 18, 2108-2119 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 2108-2119
    • Silverman, J.1    Takai, H.2    Buonomo, S.B.C.3    Eisenhaber, F.4    De Lange, T.5
  • 113
    • 77956886919 scopus 로고    scopus 로고
    • Rif1 provides a new DNA-binding interface for the Bloom syndrome complex to maintain normal replication
    • Xu, D. et al. Rif1 provides a new DNA-binding interface for the Bloom syndrome complex to maintain normal replication. EMBO J. 29, 3140-3155 (2010).
    • (2010) EMBO J. , vol.29 , pp. 3140-3155
    • Xu, D.1
  • 114
    • 59649114341 scopus 로고    scopus 로고
    • Inactivation of murine Usp1 results in genomic instability and a Fanconi anemia phenotype
    • Kim, J. M. et al. Inactivation of murine Usp1 results in genomic instability and a Fanconi anemia phenotype. Dev. Cell 16, 314-320 (2009).
    • (2009) Dev. Cell , vol.16 , pp. 314-320
    • Kim, J.M.1
  • 115
    • 73949101221 scopus 로고    scopus 로고
    • Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation
    • Harreman, M. et al. Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. Proc. Natl Acad. Sci. USA 106, 20705-20710 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 20705-20710
    • Harreman, M.1
  • 116
    • 65549120715 scopus 로고    scopus 로고
    • Modes of p53 regulation
    • Kruse, J.-P. & Gu, W. Modes of p53 regulation. Cell 137, 609-622 (2009).
    • (2009) Cell , vol.137 , pp. 609-622
    • Kruse, J.-P.1    Gu, W.2
  • 117
    • 84862270480 scopus 로고    scopus 로고
    • P53 dynamics control cell fate
    • Purvis, J. E. et al. p53 dynamics control cell fate. Science 336, 1440-1444 (2012).
    • (2012) Science , vol.336 , pp. 1440-1444
    • Purvis, J.E.1
  • 118
    • 84879340762 scopus 로고    scopus 로고
    • Guarding against collateral damage during chromatin transactions
    • Altmeyer, M. & Lukas, J. Guarding against collateral damage during chromatin transactions. Cell 153, 1431-1434 (2013).
    • (2013) Cell , vol.153 , pp. 1431-1434
    • Altmeyer, M.1    Lukas, J.2
  • 119
    • 78149425175 scopus 로고    scopus 로고
    • Regulation of homologous recombination in eukaryotes
    • Heyer, W.-D., Ehmsen, K. T. & Liu, J. Regulation of homologous recombination in eukaryotes. Annu. Rev. Genet. 44, 113-139 (2010).
    • (2010) Annu. Rev. Genet. , vol.44 , pp. 113-139
    • Heyer, W.-D.1    Ehmsen, K.T.2    Liu, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.