메뉴 건너뛰기




Volumn 33, Issue 7, 2014, Pages 805-813

DNA damage emergency: Cellular garbage disposal to the rescue

Author keywords

53BP1; DNA repair; POH1; proteasome; ubiquitin

Indexed keywords

ANIMALS; ANTINEOPLASTIC AGENTS; CHROMATIN; DNA DAMAGE; DNA REPAIR; DNA-BINDING PROTEINS; HUMANS; NEOPLASMS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEASOME INHIBITORS; UBIQUITINATION;

EID: 84894071974     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2013.60     Document Type: Review
Times cited : (19)

References (145)
  • 1
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • Hochstrasser M. Evolution and function of ubiquitin-like protein-conjugation systems. Nat Cell Biol 2000; 2: E153-E157.
    • (2000) Nat Cell Biol , vol.2
    • Hochstrasser, M.1
  • 2
    • 0035170874 scopus 로고    scopus 로고
    • Solution structure of ThiS and implications for the evolutionary roots of ubiquitin
    • Wang C, Xi J, Begley TP, Nicholson LK. Solution structure of ThiS and implications for the evolutionary roots of ubiquitin. Nat Struct Mol Biol 2001; 8: 47-51.
    • (2001) Nat Struct Mol Biol , vol.8 , pp. 47-51
    • Wang, C.1    Xi, J.2    Begley, T.P.3    Nicholson, L.K.4
  • 3
    • 2442437350 scopus 로고
    • Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells
    • Goldstein G, Scheid M, Hammerling U, Boyse EA, Schlesinger DH, Niall HD. Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells. Proc Natl Acad Sci USA 1975; 72: 11-15.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 11-15
    • Goldstein, G.1    Scheid, M.2    Hammerling, U.3    Boyse, E.A.4    Schlesinger, D.H.5    Niall, H.D.6
  • 4
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. Protein regulation by monoubiquitin. Nat Rev Mol Cell Biol 2001; 2: 195-201.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 195-201
    • Hicke, L.1
  • 6
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko A, Heller H, Elias S, Ciechanover A. Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J Biol Chem 1983; 258: 8206-8214.
    • (1983) J Biol Chem , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 7
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik AY, Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochim Biophys Acta 2004; 1695: 189-207.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 8
    • 33750219981 scopus 로고    scopus 로고
    • A ubiquitin ligase complex assembles linear polyubiquitin chains
    • Kirisako T, Kamei K, Murata S, Kato M, Fukumoto H, Kanie M et al. A ubiquitin ligase complex assembles linear polyubiquitin chains. EMBO J 2006; 25: 4877-4887.
    • (2006) EMBO J , vol.25 , pp. 4877-4887
    • Kirisako, T.1    Kamei, K.2    Murata, S.3    Kato, M.4    Fukumoto, H.5    Kanie, M.6
  • 9
    • 0017601447 scopus 로고
    • Isopeptide linkage between nonhistone and histone-2A polypeptides of chromosomal conjugate-proteins-A24
    • Goldknopf IL, Busch H. Isopeptide linkage between nonhistone and histone-2A polypeptides of chromosomal conjugate-proteins-A24. Proc Natl Acad Sci USA 1977; 74: 864-868.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 864-868
    • Goldknopf, I.L.1    Busch, H.2
  • 11
    • 0036922992 scopus 로고    scopus 로고
    • Structural properties of polyubiquitin chains in solution
    • Varadan R, Walker O, Pickart C, Fushman D. Structural properties of polyubiquitin chains in solution. J Mol Biol 2002; 324: 637-647.
    • (2002) J Mol Biol , vol.324 , pp. 637-647
    • Varadan, R.1    Walker, O.2    Pickart, C.3    Fushman, D.4
  • 12
    • 73649116305 scopus 로고    scopus 로고
    • Exploring the linkage dependence of polyubiquitin conformations using molecular modeling
    • Fushman D, Walker O. Exploring the linkage dependence of polyubiquitin conformations using molecular modeling. J Mol Biol 2010; 395: 803-814.
    • (2010) J Mol Biol , vol.395 , pp. 803-814
    • Fushman, D.1    Walker, O.2
  • 13
    • 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 HT, Kim KP, Lledias F, Kisselev AF, Scaglione KM, Skowyra D et al. 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
  • 14
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa ME, Bennett EJ, Gygi SP, Harper JW. Defining the human deubiquitinating enzyme interaction landscape. Cell 2009; 138: 389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 15
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbe S. Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 2009; 10: 550-563.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 16
    • 72149130935 scopus 로고    scopus 로고
    • The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome
    • Jacobson AD, Zhang NY, Xu P, Han KJ, Noone S, Peng J et al. The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome. J Biol Chem 2009; 284: 35485-35494.
    • (2009) J Biol Chem , vol.284 , pp. 35485-35494
    • Jacobson, A.D.1    Zhang, N.Y.2    Xu, P.3    Han, K.J.4    Noone, S.5    Peng, J.6
  • 17
    • 71149107057 scopus 로고    scopus 로고
    • Ubiquitinated proteins activate the proteasome by binding to Usp14/Ubp6, which causes 20S gate opening
    • Peth A, Besche HC, Goldberg AL. Ubiquitinated proteins activate the proteasome by binding to Usp14/Ubp6, which causes 20S gate opening. Mol Cell 2009; 36: 794-804.
    • (2009) Mol Cell , vol.36 , pp. 794-804
    • Peth, A.1    Besche, H.C.2    Goldberg, A.L.3
  • 18
    • 78649289427 scopus 로고    scopus 로고
    • ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation
    • Peth A, Uchiki T, Goldberg AL. ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation. Mol Cell 2010; 40: 671-681.
    • (2010) Mol Cell , vol.40 , pp. 671-681
    • Peth, A.1    Uchiki, T.2    Goldberg, A.L.3
  • 19
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson ES, Ma PCM, Ota IM, Varshavsky A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J Biol Chem 1995; 270: 17442-17456.
    • (1995) J Biol Chem , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.M.2    Ota, I.M.3    Varshavsky, A.4
  • 21
    • 62649104153 scopus 로고    scopus 로고
    • K63-specific deubiquitination by two JAMM/MPN\+ complexes: BRISC-associated Brcc36 and proteasomal Poh1
    • Cooper EM, Cutcliffe C, Kristiansen TZ, Pandey A, Pickart CM, Cohen RE. K63-specific deubiquitination by two JAMM/MPN\+ complexes: BRISC-associated Brcc36 and proteasomal Poh1. EMBO J 2009; 28: 621-631.
    • (2009) EMBO J , vol.28 , pp. 621-631
    • Cooper, E.M.1    Cutcliffe, C.2    Kristiansen, T.Z.3    Pandey, A.4    Pickart, C.M.5    Cohen, R.E.6
  • 22
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu P, Duong DM, Seyfried NT, Cheng DM, Xie Y, Robert J et al. Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 2009; 137: 133-145.
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.M.4    Xie, Y.5    Robert, J.6
  • 23
    • 77956903406 scopus 로고    scopus 로고
    • Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase
    • Virdee S, Ye Y, Nguyen DP, Komander D, Chin JW. Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase. Nat Chem Biol 2010; 6: 750-757.
    • (2010) Nat Chem Biol , vol.6 , pp. 750-757
    • Virdee, S.1    Ye, Y.2    Nguyen, D.P.3    Komander, D.4    Chin, J.W.5
  • 24
    • 1042278177 scopus 로고    scopus 로고
    • Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase
    • Nishikawa H, Ooka S, Sato K, Arima K, Okamoto J, Klevit RE et al. Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase. J Biol Chem 2003; 279: 3916-3924.
    • (2003) J Biol Chem , vol.279 , pp. 3916-3924
    • Nishikawa, H.1    Ooka, S.2    Sato, K.3    Arima, K.4    Okamoto, J.5    Klevit, R.E.6
  • 25
    • 33751515474 scopus 로고    scopus 로고
    • The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity
    • Ben-Saadon R, Zaaroor D, Ziv T, Ciechanover A. The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity. Mol Cell 2006; 24: 701-711.
    • (2006) Mol Cell , vol.24 , pp. 701-711
    • Ben-Saadon, R.1    Zaaroor, D.2    Ziv, T.3    Ciechanover, A.4
  • 26
    • 77957284673 scopus 로고    scopus 로고
    • Differential regulation of JAMM domain deubiquitinating enzyme activity within the RAP80 complex
    • Patterson-Fortin J, Shao G, Bretscher H, Messick TE, Greenberg RA. Differential regulation of JAMM domain deubiquitinating enzyme activity within the RAP80 complex. J Biol Chem 2010; 285: 30971-30981.
    • (2010) J Biol Chem , vol.285 , pp. 30971-30981
    • Patterson-Fortin, J.1    Shao, G.2    Bretscher, H.3    Messick, T.E.4    Greenberg, R.A.5
  • 28
    • 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 TA, Venere M, DiTullio Jr. RA, Halazonetis TD. 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
  • 29
    • 0038496703 scopus 로고    scopus 로고
    • Mediator of DNA damage checkpoint protein 1 regulates BRCA1 localization and phosphorylation in DNA damage checkpoint control
    • Lou Z, Chini CC, Minter-Dykhouse K, Chen J. Mediator of DNA damage checkpoint protein 1 regulates BRCA1 localization and phosphorylation in DNA damage checkpoint control. J Biol Chem 2003; 278: 13599-13602.
    • (2003) J Biol Chem , vol.278 , pp. 13599-13602
    • Lou, Z.1    Chini, C.C.2    Minter-Dykhouse, K.3    Chen, J.4
  • 30
    • 36249031962 scopus 로고    scopus 로고
    • RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly
    • Huen MS, Grant R, Manke I, Minn K, Yu X, Yaffe MB et al. RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell 2007; 131: 901-914.
    • (2007) Cell , vol.131 , pp. 901-914
    • Huen, M.S.1    Grant, R.2    Manke, I.3    Minn, K.4    Yu, X.5    Yaffe, M.B.6
  • 32
    • 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 et al. 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
  • 33
    • 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 SJ. 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
  • 34
    • 59049091728 scopus 로고    scopus 로고
    • RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins
    • Doil C, Mailand N, Bekker-Jensen S, Menard P, Larsen DH, Pepperkok R et al. RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell 2009; 136: 435-446.
    • (2009) Cell , vol.136 , pp. 435-446
    • Doil, C.1    Mailand, N.2    Bekker-Jensen, S.3    Menard, P.4    Larsen, D.H.5    Pepperkok, R.6
  • 35
    • 59049103900 scopus 로고    scopus 로고
    • The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage
    • Stewart GS, Panier S, Townsend K, Al-Hakim AK, Kolas NK, Miller ES et al. The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell 2009; 136: 420-434.
    • (2009) Cell , vol.136 , pp. 420-434
    • Stewart, G.S.1    Panier, S.2    Townsend, K.3    Al-Hakim, A.K.4    Kolas, N.K.5    Miller, E.S.6
  • 36
    • 34249946686 scopus 로고    scopus 로고
    • Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response
    • Wang B, Matsuoka S, Ballif BA, Zhang D, Smogorzewska A, Gygi SP et al. Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response. Science 2007; 316: 1194-1198.
    • (2007) Science , vol.316 , pp. 1194-1198
    • Wang, B.1    Matsuoka, S.2    Ballif, B.A.3    Zhang, D.4    Smogorzewska, A.5    Gygi, S.P.6
  • 37
    • 67349168142 scopus 로고    scopus 로고
    • RAD18 transmits DNA damage signalling to elicit homologous recombination repair
    • Huang J, Huen MS, Kim H, Leung CC, Glover JN, Yu X et al. RAD18 transmits DNA damage signalling to elicit homologous recombination repair. Nat Cell Biol 2009; 11: 592-603.
    • (2009) Nat Cell Biol , vol.11 , pp. 592-603
    • Huang, J.1    Huen, M.S.2    Kim, H.3    Leung, C.C.4    Glover, J.N.5    Yu, X.6
  • 38
    • 70349944658 scopus 로고    scopus 로고
    • Nucleotide excision repair-induced H2A ubiquitination is dependent on MDC1 and RNF8 and reveals a universal DNA damage response
    • Marteijn JA, Bekker-Jensen S, Mailand N, Lans H, Schwertman P, Gourdin AM et al. Nucleotide excision repair-induced H2A ubiquitination is dependent on MDC1 and RNF8 and reveals a universal DNA damage response. J Cell Biol 2009; 186: 835-847.
    • (2009) J Cell Biol , vol.186 , pp. 835-847
    • Marteijn, J.A.1    Bekker-Jensen, S.2    Mailand, N.3    Lans, H.4    Schwertman, P.5    Gourdin, A.M.6
  • 39
    • 84859895529 scopus 로고    scopus 로고
    • RNF8-and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites
    • Mallette FA, Mattiroli F, Cui G, Young LC, Hendzel MJ, Mer G et al. RNF8-and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites. EMBO J 2012; 31: 1865-1878.
    • (2012) EMBO J , vol.31 , pp. 1865-1878
    • Mallette, F.A.1    Mattiroli, F.2    Cui, G.3    Young, L.C.4    Hendzel, M.J.5    Mer, G.6
  • 40
    • 84867101138 scopus 로고    scopus 로고
    • The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response
    • Butler LR, Densham RM, Jia J, Garvin AJ, Stone HR, Shah V et al. The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response. EMBO J 2012; 31: 3918-3934.
    • (2012) EMBO J , vol.31 , pp. 3918-3934
    • Butler, L.R.1    Densham, R.M.2    Jia, J.3    Garvin, A.J.4    Stone, H.R.5    Shah, V.6
  • 42
    • 53249113644 scopus 로고    scopus 로고
    • RAP80 and RNF8, key players in the recruitment of repair proteins to DNA damage sites
    • Yan J, Jetten AM. RAP80 and RNF8, key players in the recruitment of repair proteins to DNA damage sites. Cancer Lett 2008; 271: 179-190.
    • (2008) Cancer Lett , vol.271 , pp. 179-190
    • Yan, J.1    Jetten, A.M.2
  • 43
    • 84863315246 scopus 로고    scopus 로고
    • Rap80 is important for genomic stability and is required for stabilizing the BRCA1-A complex at DNA damage sites in vivo
    • Wu J, Liu C, Chen J, Yu X. Rap80 is important for genomic stability and is required for stabilizing the BRCA1-A complex at DNA damage sites in vivo. J Biol Chem 2012; 287: 22919-22926.
    • (2012) J Biol Chem , vol.287 , pp. 22919-22926
    • Wu, J.1    Liu, C.2    Chen, J.3    Yu, X.4
  • 44
    • 34249949779 scopus 로고    scopus 로고
    • RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites
    • Sobhian B, Shao G, Lilli DR, Culhane AC, Moreau LA, Xia B et al. RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites. Science 2007; 316: 1198-1202.
    • (2007) Science , vol.316 , pp. 1198-1202
    • Sobhian, B.1    Shao, G.2    Lilli, D.R.3    Culhane, A.C.4    Moreau, L.A.5    Xia, B.6
  • 45
    • 84867115508 scopus 로고    scopus 로고
    • RNF8 regulates assembly of RAD51 at DNA double-strand breaks in the absence of BRCA1 and 53BP1
    • Nakada S, Yonamine RM, Matsuo K. RNF8 regulates assembly of RAD51 at DNA double-strand breaks in the absence of BRCA1 and 53BP1. Cancer Res 2012; 72: 4974-4983.
    • (2012) Cancer Res , vol.72 , pp. 4974-4983
    • Nakada, S.1    Yonamine, R.M.2    Matsuo, K.3
  • 46
    • 79952694801 scopus 로고    scopus 로고
    • RAD51-independent inverted-repeat recombination by a strand-annealing mechanism
    • Mott C, Symington LS. RAD51-independent inverted-repeat recombination by a strand-annealing mechanism. DNA Repair 2011; 10: 408-415.
    • (2011) DNA Repair , vol.10 , pp. 408-415
    • Mott, C.1    Symington, L.S.2
  • 47
    • 0035893241 scopus 로고    scopus 로고
    • Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange
    • Sigurdsson S, Van Komen S, Bussen W, Schild D, Albala JS, Sung P. Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange. Genes Develop 2001; 15: 3308-3318.
    • (2001) Genes Develop , vol.15 , pp. 3308-3318
    • Sigurdsson, S.1    Van Komen, S.2    Bussen, W.3    Schild, D.4    Albala, J.S.5    Sung, P.6
  • 48
    • 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 PB, Yeh ET. Regulation of DNA repair through deSUMOylation and SUMOylation of replication protein A complex. Mol Cell 2010; 39: 333-345.
    • (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
  • 49
    • 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 SP. RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair. Genes Develop 2012; 26: 1179-1195.
    • (2012) Genes Develop , vol.26 , pp. 1179-1195
    • Galanty, Y.1    Belotserkovskaya, R.2    Coates, J.3    Jackson, S.P.4
  • 50
    • 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 2012; 31: 3008-3019.
    • (2012) EMBO J , vol.31 , pp. 3008-3019
    • Luo, K.1    Zhang, H.2    Wang, L.3    Yuan, J.4    Lou, Z.5
  • 51
    • 84861784690 scopus 로고    scopus 로고
    • SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage
    • Yin Y, Seifert A, Chua JS, Maure JF, Golebiowski F, Hay RT. SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage. Genes Develop 2012; 26: 1196-1208.
    • (2012) Genes Develop , vol.26 , pp. 1196-1208
    • Yin, Y.1    Seifert, A.2    Chua, J.S.3    Maure, J.F.4    Golebiowski, F.5    Hay, R.T.6
  • 53
    • 33746766974 scopus 로고    scopus 로고
    • A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response
    • Zhang D, Zaugg K, Mak TW, Elledge SJ. A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response. Cell 2006; 126: 529-542.
    • (2006) Cell , vol.126 , pp. 529-542
    • Zhang, D.1    Zaugg, K.2    Mak, T.W.3    Elledge, S.J.4
  • 54
    • 35848942129 scopus 로고    scopus 로고
    • Fbw7 and Usp28 regulate Myc protein stability in response to DNA damage
    • Popov N, Herold S, Llamazares M, Schulein C, Eilers M. Fbw7 and Usp28 regulate Myc protein stability in response to DNA damage. Cell Cycle 2007; 6: 2327-2331.
    • (2007) Cell Cycle , vol.6 , pp. 2327-2331
    • Popov, N.1    Herold, S.2    Llamazares, M.3    Schulein, C.4    Eilers, M.5
  • 55
    • 36049036216 scopus 로고    scopus 로고
    • Human USP3 is a chromatin modifier required for S phase progression and genome stability
    • Nicassio F, Corrado N, Vissers JH, Areces LB, Bergink S, Marteijn JA et al. Human USP3 is a chromatin modifier required for S phase progression and genome stability. Curr Biol 2007; 17: 1972-1977.
    • (2007) Curr Biol , vol.17 , pp. 1972-1977
    • Nicassio, F.1    Corrado, N.2    Vissers, J.H.3    Areces, L.B.4    Bergink, S.5    Marteijn, J.A.6
  • 56
    • 35548986309 scopus 로고    scopus 로고
    • Regulation of cell cycle progression and gene expression by H2A deubiquitination
    • Joo HY, Zhai L, Yang C, Nie S, Erdjument-Bromage H, Tempst P et al. Regulation of cell cycle progression and gene expression by H2A deubiquitination. Nature 2007; 449: 1068-1072.
    • (2007) Nature , vol.449 , pp. 1068-1072
    • Joo, H.Y.1    Zhai, L.2    Yang, C.3    Nie, S.4    Erdjument-Bromage, H.5    Tempst, P.6
  • 57
    • 77955867565 scopus 로고    scopus 로고
    • Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1
    • Nakada S, Tai I, Panier S, Al-Hakim A, Iemura S, Juang YC et al. Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1. Nature 2010; 466: 941-946.
    • (2010) Nature , vol.466 , pp. 941-946
    • Nakada, S.1    Tai, I.2    Panier, S.3    Al-Hakim, A.4    Iemura, S.5    Juang, Y.C.6
  • 58
    • 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 2012; 483: 618-622.
    • (2012) Nature , vol.483 , pp. 618-622
    • Wiener, R.1    Zhang, X.2    Wang, T.3    Wolberger, C.4
  • 60
    • 84864386119 scopus 로고    scopus 로고
    • Molecular basis of Lys-63-linked polyubiquitination inhibition by the interaction between human deubiquitinating enzyme OTUB1 and ubiquitin- conjugating enzyme UBC13
    • Sato Y, Yamagata A, Goto-Ito S, Kubota K, Miyamoto R, Nakada S et al. Molecular basis of Lys-63-linked polyubiquitination inhibition by the interaction between human deubiquitinating enzyme OTUB1 and ubiquitin- conjugating enzyme UBC13. J Biol Chem 2012; 287: 25860-25868.
    • (2012) J Biol Chem , vol.287 , pp. 25860-25868
    • Sato, Y.1    Yamagata, A.2    Goto-Ito, S.3    Kubota, K.4    Miyamoto, R.5    Nakada, S.6
  • 61
    • 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 2010; 285: 30982-30988.
    • (2010) J Biol Chem , vol.285 , pp. 30982-30988
    • Feng, L.1    Wang, J.2    Chen, J.3
  • 64
    • 80455145246 scopus 로고    scopus 로고
    • The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA double-strand breaks
    • Meerang M, Ritz D, Paliwal S, Garajova Z, Bosshard M, Mailand N et al. The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA double-strand breaks. Nat Cell Biol 2011; 13: 1376-1382.
    • (2011) Nat Cell Biol , vol.13 , pp. 1376-1382
    • Meerang, M.1    Ritz, D.2    Paliwal, S.3    Garajova, Z.4    Bosshard, M.5    Mailand, N.6
  • 65
    • 33645731673 scopus 로고    scopus 로고
    • A dynamic ubiquitin equilibrium couples proteasomal activity to chromatin remodeling
    • Dantuma NP, Groothuis TA, Salomons FA, Neefjes J. A dynamic ubiquitin equilibrium couples proteasomal activity to chromatin remodeling. J Cell Biol 2006; 173: 19-26.
    • (2006) J Cell Biol , vol.173 , pp. 19-26
    • Dantuma, N.P.1    Groothuis, T.A.2    Salomons, F.A.3    Neefjes, J.4
  • 66
    • 57649130600 scopus 로고    scopus 로고
    • Disassembly of MDC1 foci is controlled by ubiquitin-proteasome-dependent degradation
    • Shi W, Ma Z, Willers H, Akhtar K, Scott SP, Zhang J et al. Disassembly of MDC1 foci is controlled by ubiquitin-proteasome-dependent degradation. J Biol Chem 2008; 283: 31608-31616.
    • (2008) J Biol Chem , vol.283 , pp. 31608-31616
    • Shi, W.1    Ma, Z.2    Willers, H.3    Akhtar, K.4    Scott, S.P.5    Zhang, J.6
  • 67
    • 34548807121 scopus 로고    scopus 로고
    • Inhibitors of the proteasome suppress homologous DNA recombination in mammalian cells
    • Murakawa Y, Sonoda E, Barber LJ, Zeng W, Yokomori K, Kimura H et al. Inhibitors of the proteasome suppress homologous DNA recombination in mammalian cells. Cancer Res 2007; 67: 8536-8543.
    • (2007) Cancer Res , vol.67 , pp. 8536-8543
    • Murakawa, Y.1    Sonoda, E.2    Barber, L.J.3    Zeng, W.4    Yokomori, K.5    Kimura, H.6
  • 68
    • 34547628200 scopus 로고    scopus 로고
    • Proteasome function is required for DNA damage response and fanconi anemia pathway activation
    • Jacquemont C, Taniguchi T. Proteasome function is required for DNA damage response and fanconi anemia pathway activation. Cancer Res 2007; 67: 7395-7405.
    • (2007) Cancer Res , vol.67 , pp. 7395-7405
    • Jacquemont, C.1    Taniguchi, T.2
  • 69
    • 36749022182 scopus 로고    scopus 로고
    • The proteasome is involved in determining differential utilization of double-strand break repair pathways
    • Gudmundsdottir K, Lord CJ, Ashworth A. The proteasome is involved in determining differential utilization of double-strand break repair pathways. Oncogene 2007; 26: 7601-7606.
    • (2007) Oncogene , vol.26 , pp. 7601-7606
    • Gudmundsdottir, K.1    Lord, C.J.2    Ashworth, A.3
  • 70
    • 77649196564 scopus 로고    scopus 로고
    • Proteasome nuclear activity affects chromosome stability by controlling the turnover of Mms22, a protein important for DNA repair
    • Ben-Aroya S, Agmon N, Yuen K, Kwok T, McManus K, Kupiec M et al. Proteasome nuclear activity affects chromosome stability by controlling the turnover of Mms22, a protein important for DNA repair. PLoS Genet 2010; 6: e1000852.
    • (2010) PLoS Genet , vol.6
    • Ben-Aroya, S.1    Agmon, N.2    Yuen, K.3    Kwok, T.4    McManus, K.5    Kupiec, M.6
  • 71
    • 65849488473 scopus 로고    scopus 로고
    • Regulation of ErbB2 receptor status by the proteasomal DUB POH1
    • Liu H, Buus R, Clague MJ, Urbe S. Regulation of ErbB2 receptor status by the proteasomal DUB POH1. PLoS ONE 2009; 4: e5544.
    • (2009) PLoS ONE , vol.4
    • Liu, H.1    Buus, R.2    Clague, M.J.3    Urbe, S.4
  • 72
    • 0344629427 scopus 로고    scopus 로고
    • Ubiquitin depletion as a key mediator of toxicity by translational inhibitors
    • Hanna J, Leggett DS, Finley D. Ubiquitin depletion as a key mediator of toxicity by translational inhibitors. Mol Cell Biol 2003; 23: 9251-9261.
    • (2003) Mol Cell Biol , vol.23 , pp. 9251-9261
    • Hanna, J.1    Leggett, D.S.2    Finley, D.3
  • 75
    • 0031105037 scopus 로고    scopus 로고
    • Structural and functional properties of proteasome activator PA28
    • Kuehn L, Dahlmann B. Structural and functional properties of proteasome activator PA28. Mol Biol Rep 1997; 24: 89-93.
    • (1997) Mol Biol Rep , vol.24 , pp. 89-93
    • Kuehn, L.1    Dahlmann, B.2
  • 76
    • 0036646488 scopus 로고    scopus 로고
    • PA200, a nuclear proteasome activator involved in DNA repair
    • Ustrell V, Hoffman L, Pratt G, Rechsteiner M. PA200, a nuclear proteasome activator involved in DNA repair. EMBO J 2002; 21: 3516-3525.
    • (2002) EMBO J , vol.21 , pp. 3516-3525
    • Ustrell, V.1    Hoffman, L.2    Pratt, G.3    Rechsteiner, M.4
  • 77
    • 55849123303 scopus 로고    scopus 로고
    • Role for proteasome activator PA200 and postglutamyl proteasome activity in genomic stability
    • Blickwedehl J, Agarwal M, Seong C, Pandita RK, Melendy T, Sung P et al. Role for proteasome activator PA200 and postglutamyl proteasome activity in genomic stability. Proc Natl Acad Sci USA 2008; 105: 16165-16170.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 16165-16170
    • Blickwedehl, J.1    Agarwal, M.2    Seong, C.3    Pandita, R.K.4    Melendy, T.5    Sung, P.6
  • 78
    • 34447549100 scopus 로고    scopus 로고
    • Proteasomes and proteasome activator 200 kDa (PA200) accumulate on chromatin in response to ionizing radiation
    • Blickwedehl J, McEvoy S, Wong I, Kousis P, Clements J, Elliott R et al. Proteasomes and proteasome activator 200 kDa (PA200) accumulate on chromatin in response to ionizing radiation. Radiat Res 2007; 167: 663-674.
    • (2007) Radiat Res , vol.167 , pp. 663-674
    • Blickwedehl, J.1    McEvoy, S.2    Wong, I.3    Kousis, P.4    Clements, J.5    Elliott, R.6
  • 79
    • 84055184842 scopus 로고    scopus 로고
    • Involvement of the nuclear proteasome activator PA28gamma in the cellular response to DNA double-strand breaks
    • Levy-Barda A, Lerenthal Y, Davis AJ, Chung YM, Essers J, Shao Z et al. Involvement of the nuclear proteasome activator PA28gamma in the cellular response to DNA double-strand breaks. Cell Cycle 2011; 10: 24.
    • (2011) Cell Cycle , vol.10 , pp. 24
    • Levy-Barda, A.1    Lerenthal, Y.2    Davis, A.J.3    Chung, Y.M.4    Essers, J.5    Shao, Z.6
  • 80
    • 84863299183 scopus 로고    scopus 로고
    • S5a/Rpn10, a UIM-protein, as a universal substrate for ubiquitination
    • Kim HT, Goldberg AL. S5a/Rpn10, a UIM-protein, as a universal substrate for ubiquitination. Methods Mol Biol 2012; 832: 653-660.
    • (2012) Methods Mol Biol , vol.832 , pp. 653-660
    • Kim, H.T.1    Goldberg, A.L.2
  • 81
    • 67650427174 scopus 로고    scopus 로고
    • S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains
    • Kim HT, Kim KP, Uchiki T, Gygi SP, Goldberg AL. S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains. EMBO J 2009; 28: 1867-1877.
    • (2009) EMBO J , vol.28 , pp. 1867-1877
    • Kim, H.T.1    Kim, K.P.2    Uchiki, T.3    Gygi, S.P.4    Goldberg, A.L.5
  • 82
    • 80053583606 scopus 로고    scopus 로고
    • A genome-wide screen identifies p97 as an essential regulator of DNA damage-dependent CDT1 destruction
    • Raman M, Havens CG, Walter JC, Harper JW. A genome-wide screen identifies p97 as an essential regulator of DNA damage-dependent CDT1 destruction. Mol Cell 2011; 44: 72-84.
    • (2011) Mol Cell , vol.44 , pp. 72-84
    • Raman, M.1    Havens, C.G.2    Walter, J.C.3    Harper, J.W.4
  • 83
    • 80053606383 scopus 로고    scopus 로고
    • CDC-48/p97 coordinates CDT-1 degradation with GINS chromatin dissociation to ensure faithful DNA replication
    • Franz A, Orth M, Pirson PA, Sonneville R, Blow JJ, Gartner A et al. CDC-48/p97 coordinates CDT-1 degradation with GINS chromatin dissociation to ensure faithful DNA replication. Mol Cell 2011; 44: 85-96.
    • (2011) Mol Cell , vol.44 , pp. 85-96
    • Franz, A.1    Orth, M.2    Pirson, P.A.3    Sonneville, R.4    Blow, J.J.5    Gartner, A.6
  • 84
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • Meyer H, Bug M, Bremer S. Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat Cell Biol 2012; 14: 117-123.
    • (2012) Nat Cell Biol , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 85
    • 84862777619 scopus 로고    scopus 로고
    • The E3 ligase RNF8 regulates KU80 removal and NHEJ repair
    • Feng L, Chen J. The E3 ligase RNF8 regulates KU80 removal and NHEJ repair. Nat Struct Mol Biol 2012; 19: 201-206.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 201-206
    • Feng, L.1    Chen, J.2
  • 86
    • 80052568653 scopus 로고    scopus 로고
    • SCF(FBXO22) regulates histone H3 lysine 9 and 36 methylation levels by targeting histone demethylase KDM4A for ubiquitinmediated proteasomal degradation
    • Tan MK, Lim HJ, Harper JW. SCF(FBXO22) regulates histone H3 lysine 9 and 36 methylation levels by targeting histone demethylase KDM4A for ubiquitinmediated proteasomal degradation. Mol Cell Biol 2011; 31: 3687-3699.
    • (2011) Mol Cell Biol , vol.31 , pp. 3687-3699
    • Tan, M.K.1    Lim, H.J.2    Harper, J.W.3
  • 87
    • 84865024389 scopus 로고    scopus 로고
    • K48-linked ubiquitination and protein degradation regulate 53BP1 recruitment at DNA damage sites
    • Mallette FA, Richard S. K48-linked ubiquitination and protein degradation regulate 53BP1 recruitment at DNA damage sites. Cell Res 2012; 22: 1221-1223.
    • (2012) Cell Res , vol.22 , pp. 1221-1223
    • Mallette, F.A.1    Richard, S.2
  • 89
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly H, Rape M, Braun S, Rumpf S, Hoege C, Jentsch S. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 2005; 120: 73-84.
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 90
    • 73349115264 scopus 로고    scopus 로고
    • A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor-promoter DNA complex
    • Wilcox AJ, Laney JD. A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor-promoter DNA complex. Nat Cell Biol 2009; 11: 1481-1486.
    • (2009) Nat Cell Biol , vol.11 , pp. 1481-1486
    • Wilcox, A.J.1    Laney, J.D.2
  • 91
    • 30744451400 scopus 로고    scopus 로고
    • Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone
    • Rumpf S, Jentsch S. Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone. Mol Cell 2006; 21: 261-269.
    • (2006) Mol Cell , vol.21 , pp. 261-269
    • Rumpf, S.1    Jentsch, S.2
  • 94
    • 24744434431 scopus 로고    scopus 로고
    • Valosin-containing protein phosphorylation at Ser784 in response to DNA damage
    • Livingstone M, Ruan H, Weiner J, Clauser KR, Strack P, Jin S et al. Valosin-containing protein phosphorylation at Ser784 in response to DNA damage. Cancer Res 2005; 65: 7533-7540.
    • (2005) Cancer Res , vol.65 , pp. 7533-7540
    • Livingstone, M.1    Ruan, H.2    Weiner, J.3    Clauser, K.R.4    Strack, P.5    Jin, S.6
  • 95
    • 0033855808 scopus 로고    scopus 로고
    • VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells
    • Zhang H, Wang Q, Kajino K, Greene MI. VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells. DNA Cell Biol 2000; 19: 253-263.
    • (2000) DNA Cell Biol , vol.19 , pp. 253-263
    • Zhang, H.1    Wang, Q.2    Kajino, K.3    Greene, M.I.4
  • 97
    • 0033959478 scopus 로고    scopus 로고
    • P97 ATPase, an ATPase involved in membrane fusion, interacts with DNA unwinding factor (DUF) that functions in DNA replication
    • Yamada T, Okuhara K, Iwamatsu A, Seo H, Ohta K, Shibata T et al. p97 ATPase, an ATPase involved in membrane fusion, interacts with DNA unwinding factor (DUF) that functions in DNA replication. FEBS Lett 2000; 466: 287-291.
    • (2000) FEBS Lett , vol.466 , pp. 287-291
    • Yamada, T.1    Okuhara, K.2    Iwamatsu, A.3    Seo, H.4    Ohta, K.5    Shibata, T.6
  • 99
    • 82955164827 scopus 로고    scopus 로고
    • Differential regulation of RNF8-mediated Lys48-and Lys63-based poly-ubiquitylation
    • Lok GT, Sy SM, Dong SS, Ching YP, Tsao SW, Thomson TM et al. Differential regulation of RNF8-mediated Lys48-and Lys63-based poly-ubiquitylation. Nucleic Acids Res 2011; 40: 196-205.
    • (2011) Nucleic Acids Res , vol.40 , pp. 196-205
    • Lok, G.T.1    Sy, S.M.2    Dong, S.S.3    Ching, Y.P.4    Tsao, S.W.5    Thomson, T.M.6
  • 100
    • 57049132043 scopus 로고    scopus 로고
    • 53BP1 promotes non-homologous end joining of telomeres by increasing chromatin mobility
    • Dimitrova N, Chen YC, Spector DL, de Lange T. 53BP1 promotes non-homologous end joining of telomeres by increasing chromatin mobility. Nature 2008; 456: 524-528.
    • (2008) Nature , vol.456 , pp. 524-528
    • Dimitrova, N.1    Chen, Y.C.2    Spector, D.L.3    De Lange, T.4
  • 101
    • 79955502009 scopus 로고    scopus 로고
    • Regulation of DNA end joining, resection, and immunoglobulin class switch recombination by 53BP1
    • Bothmer A, Robbiani DF, Di Virgilio M, Bunting SF, Klein IA, Feldhahn N et al. Regulation of DNA end joining, resection, and immunoglobulin class switch recombination by 53BP1. Mol Cell 2011; 42: 319-329.
    • (2011) Mol Cell , vol.42 , pp. 319-329
    • Bothmer, A.1    Robbiani, D.F.2    Di Virgilio, M.3    Bunting, S.F.4    Klein, I.A.5    Feldhahn, N.6
  • 102
    • 84864076551 scopus 로고    scopus 로고
    • Rap80 Recruitment to DNA double strand breaks requires binding to both sumo-and ubiquitin-conjugates
    • Hu X, Paul A, Wang B. Rap80 Recruitment to DNA double strand breaks requires binding to both sumo-and ubiquitin-conjugates. J Biol Chem 2012; 287: 25510-25519.
    • (2012) J Biol Chem , vol.287 , pp. 25510-25519
    • Hu, X.1    Paul, A.2    Wang, B.3
  • 103
    • 84870760201 scopus 로고    scopus 로고
    • RNF4-dependent hybrid SUMO-ubiquitin chains are signals for RAP80 and thereby mediate the recruitment of BRCA1 to sites of DNA damage
    • Guzzo CM, Berndsen CE, Zhu J, Gupta V, Datta A, Greenberg RA et al. RNF4-dependent hybrid SUMO-ubiquitin chains are signals for RAP80 and thereby mediate the recruitment of BRCA1 to sites of DNA damage. Sci Signal 2012; 5: 88.
    • (2012) Sci Signal , vol.5 , pp. 88
    • Guzzo, C.M.1    Berndsen, C.E.2    Zhu, J.3    Gupta, V.4    Datta, A.5    Greenberg, R.A.6
  • 104
    • 63049138322 scopus 로고    scopus 로고
    • NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control
    • Wang B, Hurov K, Hofmann K, Elledge SJ. NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control. Genes Dev 2009; 23: 729-739.
    • (2009) Genes Dev , vol.23 , pp. 729-739
    • Wang, B.1    Hurov, K.2    Hofmann, K.3    Elledge, S.J.4
  • 105
    • 70349982566 scopus 로고    scopus 로고
    • A comparison of BRCA1 nuclear localization with 14 DNA damage response proteins and domains: Identification of specific differences between BRCA1 and 53BP1 at DNA damage-induced foci
    • Mok MT, Henderson BR. A comparison of BRCA1 nuclear localization with 14 DNA damage response proteins and domains: identification of specific differences between BRCA1 and 53BP1 at DNA damage-induced foci. Cell Signal 2010; 22: 47-56.
    • (2010) Cell Signal , vol.22 , pp. 47-56
    • Mok, M.T.1    Henderson, B.R.2
  • 106
    • 84865386136 scopus 로고    scopus 로고
    • BRCA1-associated exclusion of 53BP1 from DNA damage sites underlies temporal control of DNA repair
    • Chapman JR, Sossick AJ, Boulton SJ, Jackson SP. BRCA1-associated exclusion of 53BP1 from DNA damage sites underlies temporal control of DNA repair. J Cell Sci 2012; 125(Pt 15): 3529-3534.
    • (2012) J Cell Sci , vol.125 , Issue.PART. 15 , pp. 3529-3534
    • Chapman, J.R.1    Sossick, A.J.2    Boulton, S.J.3    Jackson, S.P.4
  • 107
    • 77953291328 scopus 로고    scopus 로고
    • 53BP1 loss rescues BRCA1 deficiency and is associated with triple-negative and BRCA-mutated breast cancers.
    • Bouwman P, Aly A, Escandell JM, Pieterse M, Bartkova J, van der Gulden H et al. 53BP1 loss rescues BRCA1 deficiency and is associated with triple-negative and BRCA-mutated breast cancers. Nat Struct Mol Biol 2010; 17: 688-695.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 688-695
    • Bouwman, P.1    Aly, A.2    Escandell, J.M.3    Pieterse, M.4    Bartkova, J.5    Van Der Gulden, H.6
  • 108
    • 77950958141 scopus 로고    scopus 로고
    • 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks
    • Bunting SF, Callen E, Wong N, Chen HT, Polato F, Gunn A et al. 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks. Cell 2010; 141: 243-254.
    • (2010) Cell , vol.141 , pp. 243-254
    • Bunting, S.F.1    Callen, E.2    Wong, N.3    Chen, H.T.4    Polato, F.5    Gunn, A.6
  • 109
    • 68949221567 scopus 로고    scopus 로고
    • A selective requirement for 53BP1 in the biological response to genomic instability induced by Brca1 deficiency
    • Cao L, Xu X, Bunting SF, Liu J, Wang RH, Cao LL et al. A selective requirement for 53BP1 in the biological response to genomic instability induced by Brca1 deficiency. Mol Cell 2009; 35: 534-541.
    • (2009) Mol Cell , vol.35 , pp. 534-541
    • Cao, L.1    Xu, X.2    Bunting, S.F.3    Liu, J.4    Wang, R.H.5    Cao, L.L.6
  • 110
    • 84865232294 scopus 로고    scopus 로고
    • TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes
    • Gudjonsson T, Altmeyer M, Savic V, Toledo L, Dinant C, Grofte M et al. TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes. Cell 2012; 150: 697-709.
    • (2012) Cell , vol.150 , pp. 697-709
    • Gudjonsson, T.1    Altmeyer, M.2    Savic, V.3    Toledo, L.4    Dinant, C.5    Grofte, M.6
  • 111
    • 84857411692 scopus 로고    scopus 로고
    • Identification of mammalian protein quality control factors by high-throughput cellular imaging
    • Pegoraro G, Voss TC, Martin SE, Tuzmen P, Guha R, Misteli T. Identification of mammalian protein quality control factors by high-throughput cellular imaging. PLoS ONE 2012; 7: e31684.
    • (2012) PLoS ONE , vol.7
    • Pegoraro, G.1    Voss, T.C.2    Martin, S.E.3    Tuzmen, P.4    Guha, R.5    Misteli, T.6
  • 112
    • 78649433314 scopus 로고    scopus 로고
    • Depletion of DSS1 protein disables homologous recombinational repair in human cells
    • Kristensen CN, Bystol KM, Li B, Serrano L, Brenneman MA. Depletion of DSS1 protein disables homologous recombinational repair in human cells. Mutat Res 2010; 694: 60-64.
    • (2010) Mutat Res , vol.694 , pp. 60-64
    • Kristensen, C.N.1    Bystol, K.M.2    Li, B.3    Serrano, L.4    Brenneman, M.A.5
  • 113
    • 34147195807 scopus 로고    scopus 로고
    • Dss1 interaction with Brh2 as a regulatory mechanism for recombinational repair
    • Zhou Q, Kojic M, Cao Z, Lisby M, Mazloum NA, Holloman WK. Dss1 interaction with Brh2 as a regulatory mechanism for recombinational repair. Mol Cell Biol 2007; 27: 2512-2526.
    • (2007) Mol Cell Biol , vol.27 , pp. 2512-2526
    • Zhou, Q.1    Kojic, M.2    Cao, Z.3    Lisby, M.4    Mazloum, N.A.5    Holloman, W.K.6
  • 114
    • 15044340651 scopus 로고    scopus 로고
    • Brh2-Dss1 interplay enables properly controlled recombination in Ustilago maydis
    • Kojic M, Zhou Q, Lisby M, Holloman WK. Brh2-Dss1 interplay enables properly controlled recombination in Ustilago maydis. Mol Cell Biol 2005; 25: 2547-2557.
    • (2005) Mol Cell Biol , vol.25 , pp. 2547-2557
    • Kojic, M.1    Zhou, Q.2    Lisby, M.3    Holloman, W.K.4
  • 115
    • 77957804215 scopus 로고    scopus 로고
    • Human BRCA2 protein promotes RAD51 filament formation on RPA-covered single-stranded DNA
    • Liu J, Doty T, Gibson B, Heyer WD. Human BRCA2 protein promotes RAD51 filament formation on RPA-covered single-stranded DNA. Nat Struct Mol Biol 2010; 17: 1260-1262
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1260-1262
    • Liu, J.1    Doty, T.2    Gibson, B.3    Heyer, W.D.4
  • 116
    • 69049099939 scopus 로고    scopus 로고
    • Perturbation of DNA repair pathways by proteasome inhibitors corresponds to enhanced chemosensitivity of cells to DNA damage-inducing agents
    • Takeshita T, Wu W, Koike A, Fukuda M, Ohta T. Perturbation of DNA repair pathways by proteasome inhibitors corresponds to enhanced chemosensitivity of cells to DNA damage-inducing agents. Cancer Chemotherapy Pharmacol 2009; 64: 1039-1046.
    • (2009) Cancer Chemotherapy Pharmacol , vol.64 , pp. 1039-1046
    • Takeshita, T.1    Wu, W.2    Koike, A.3    Fukuda, M.4    Ohta, T.5
  • 117
    • 83455195500 scopus 로고    scopus 로고
    • Bortezomib-induced 'BRCAness' sensitizes multiple myeloma cells to PARP inhibitors
    • Neri P, Ren L, Gratton K, Stebner E, Johnson J, Klimowicz A et al. Bortezomib-induced 'BRCAness' sensitizes multiple myeloma cells to PARP inhibitors. Blood 2011; 118: 6368-6379.
    • (2011) Blood , vol.118 , pp. 6368-6379
    • Neri, P.1    Ren, L.2    Gratton, K.3    Stebner, E.4    Johnson, J.5    Klimowicz, A.6
  • 119
    • 22144466584 scopus 로고    scopus 로고
    • The FA/BRCA pathway is involved in melphalan-induced DNA interstrand cross-link repair and accounts for melphalan resistance in multiple myeloma cells
    • Chen Q, Van der Sluis PC, Boulware D, Hazlehurst LA, Dalton WS. The FA/BRCA pathway is involved in melphalan-induced DNA interstrand cross-link repair and accounts for melphalan resistance in multiple myeloma cells. Blood 2005; 106: 698-705.
    • (2005) Blood , vol.106 , pp. 698-705
    • Chen, Q.1    Van Der Sluis, P.C.2    Boulware, D.3    Hazlehurst, L.A.4    Dalton, W.S.5
  • 120
    • 84862908084 scopus 로고    scopus 로고
    • A phase i study evaluating ibritumomab tiuxetan (Zevalin(R)) in combination with bortezomib (Velcade(R)) in relapsed/refractory mantle cell and low grade B-cell non-Hodgkin lymphoma
    • Beaven AW, Shea TC, Moore DT, Feldman T, Ivanova A, Ferraro M et al. A phase I study evaluating ibritumomab tiuxetan (Zevalin(R)) in combination with bortezomib (Velcade(R)) in relapsed/refractory mantle cell and low grade B-cell non-Hodgkin lymphoma. Leukemia Lymphoma 2012; 53: 254-258.
    • (2012) Leukemia Lymphoma , vol.53 , pp. 254-258
    • Beaven, A.W.1    Shea, T.C.2    Moore, D.T.3    Feldman, T.4    Ivanova, A.5    Ferraro, M.6
  • 122
    • 84858683642 scopus 로고    scopus 로고
    • Targeting the ubiquitin-proteasome pathway with inorganic compounds to fight cancer: A challenge for the future
    • Dalla Via L, Nardon C, Fregona D. Targeting the ubiquitin-proteasome pathway with inorganic compounds to fight cancer: a challenge for the future. Future Med Chem 2012; 4: 525-543.
    • (2012) Future Med Chem , vol.4 , pp. 525-543
    • Dalla Via, L.1    Nardon, C.2    Fregona, D.3
  • 123
    • 84859395758 scopus 로고    scopus 로고
    • Advances in the treatment of relapsed or refractory Hodgkin's lymphoma
    • Ramchandren R. Advances in the treatment of relapsed or refractory Hodgkin's lymphoma. Oncol 2012; 17: 367-376.
    • (2012) Oncol , vol.17 , pp. 367-376
    • Ramchandren, R.1
  • 125
    • 84864448811 scopus 로고    scopus 로고
    • Proteasome deubiquitinases as novel targets for cancer therapy
    • D'Arcy P, Linder S. Proteasome deubiquitinases as novel targets for cancer therapy. Int J Biochem Cell Biol 2012; 44: 1729-1738.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1729-1738
    • D'Arcy, P.1    Linder, S.2
  • 126
    • 79951688311 scopus 로고    scopus 로고
    • Targeting malignancies with disulfiram (Antabuse): Multidrug resistance, angiogenesis, and proteasome
    • Cvek B. Targeting malignancies with disulfiram (Antabuse): multidrug resistance, angiogenesis, and proteasome. Curr Cancer Drug Targets 2011; 11: 332-337.
    • (2011) Curr Cancer Drug Targets , vol.11 , pp. 332-337
    • Cvek, B.1
  • 128
    • 84857134729 scopus 로고    scopus 로고
    • Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach
    • Lasker K, Forster F, Bohn S, Walzthoeni T, Villa E, Unverdorben P et al. Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach. Proc Natl Acad Sci USA 2012; 109: 1380-1387.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 1380-1387
    • Lasker, K.1    Forster, F.2    Bohn, S.3    Walzthoeni, T.4    Villa, E.5    Unverdorben, P.6
  • 131
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • Verma R, Aravind L, Oania R, McDonald WH, Yates 3rd JR, Koonin EV et al. Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 2002; 298: 611-615.
    • (2002) Science , vol.298 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4    Yates III, J.R.5    Koonin, E.V.6
  • 132
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao T, Cohen RE. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 2002; 419: 403-407.
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 133
    • 33744947551 scopus 로고    scopus 로고
    • The 19 S proteasomal subunit POH1 contributes to the regulation of c-Jun ubiquitination, stability, and subcellular localization
    • Nabhan JF, Ribeiro P. The 19 S proteasomal subunit POH1 contributes to the regulation of c-Jun ubiquitination, stability, and subcellular localization. J Biol Chem 2006; 281: 16099-16107.
    • (2006) J Biol Chem , vol.281 , pp. 16099-16107
    • Nabhan, J.F.1    Ribeiro, P.2
  • 134
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-[kappa] B signalling
    • Wertz IE, O'Rourke KM, Zhou H, Eby M, Aravind L, Seshagiri S et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-[kappa]B signalling. Nature 2004; 430: 694-699.
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1    O'Rourke, K.M.2    Zhou, H.3    Eby, M.4    Aravind, L.5    Seshagiri, S.6
  • 135
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • Burnett B, Li F, Pittman RN. The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Human Mol Genet 2003; 12: 3195-3205.
    • (2003) Human Mol Genet , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 136
    • 0242693202 scopus 로고    scopus 로고
    • Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics
    • Scheel H, Tomiuk S, Hofmann K. Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics. Human Mol Genet 2003; 12: 2845-2852.
    • (2003) Human Mol Genet , vol.12 , pp. 2845-2852
    • Scheel, H.1    Tomiuk, S.2    Hofmann, K.3
  • 137
    • 0037131567 scopus 로고    scopus 로고
    • The UCH-L1 gene encodes two opposing enzymatic activities that affect a-synuclein degradation and parkinson's disease susceptibility
    • Liu Y, Fallon L, Lashuel HA, Liu Z, Lansbury Jr PT. The UCH-L1 gene encodes two opposing enzymatic activities that affect a-synuclein degradation and parkinson's disease susceptibility. Cell 2002; 111: 209-218.
    • (2002) Cell , vol.111 , pp. 209-218
    • Liu, Y.1    Fallon, L.2    Lashuel, H.A.3    Liu, Z.4    Lansbury Jr., P.T.5
  • 138
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • Lam YA, Xu W, DeMartino GN, Cohen RE. Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 1997; 385: 737-740.
    • (1997) Nature , vol.385 , pp. 737-740
    • Lam, Y.A.1    Xu, W.2    Demartino, G.N.3    Cohen, R.E.4
  • 140
    • 4344717012 scopus 로고    scopus 로고
    • BRCA2 is ubiquitinated in vivo and interacts with USP11, a deubiquitinating enzyme that exhibits prosurvival function in the cellular response to DNA damage
    • Schoenfeld AR, Apgar S, Dolios G, Wang R, Aaronson SA. BRCA2 is ubiquitinated in vivo and interacts with USP11, a deubiquitinating enzyme that exhibits prosurvival function in the cellular response to DNA damage. Mol Cell Biol 2004; 24: 7444-7455.
    • (2004) Mol Cell Biol , vol.24 , pp. 7444-7455
    • Schoenfeld, A.R.1    Apgar, S.2    Dolios, G.3    Wang, R.4    Aaronson, S.A.5
  • 141
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-[kappa] B
    • Brummelkamp TR, Nijman SMB, Dirac AMG, Bernards R. Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-[kappa]B. Nature 2003; 424: 797-801.
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.B.2    Dirac, A.M.G.3    Bernards, R.4
  • 142
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-[kappa] B signalling by deubiquitination
    • Kovalenko A, Chable-Bessia C, Cantarella G, Israel A, Wallach D, Courtois G. The tumour suppressor CYLD negatively regulates NF-[kappa]B signalling by deubiquitination. Nature 2003; 424: 801-805.
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1    Chable-Bessia, C.2    Cantarella, G.3    Israel, A.4    Wallach, D.5    Courtois, G.6
  • 143
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-[kappa] B activation by TNFR family members
    • Trompouki E, Hatzivassiliou E, Tsichritzis T, Farmer H, Ashworth A, Mosialos G. CYLD is a deubiquitinating enzyme that negatively regulates NF-[kappa]B activation by TNFR family members. Nature 2003; 424: 793-796.
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 145
    • 1942470483 scopus 로고    scopus 로고
    • Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analoguesw,z
    • Russell NS, Wilkinson KD. Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analoguesw,z. Biochemistry 2004; 43: 4844-4854.
    • (2004) Biochemistry , vol.43 , pp. 4844-4854
    • Russell, N.S.1    Wilkinson, K.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.