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Volumn 14, Issue 9, 2015, Pages 1413-1425

USP7 deubiquitinase promotes ubiquitin-dependent DNA damage signaling by stabilizing RNF168

Author keywords

[No Author keywords available]

Indexed keywords

BMI1 PROTEIN; BRCA1 PROTEIN; DEUBIQUITINASE; HISTONE H2A; HISTONE H2AX; MUTANT PROTEIN; RNF168 PROTEIN; RNF8 PROTEIN; SMALL INTERFERING RNA; UBIQUITIN; UNCLASSIFIED DRUG; USP7 DEUBIQUITINASE; BRCA1 PROTEIN, HUMAN; DNA BINDING PROTEIN; H2AFX PROTEIN, HUMAN; HISTONE; PROTEIN BINDING; RNF168 PROTEIN, HUMAN; RNF8 PROTEIN, HUMAN; SIGNAL PEPTIDE; TP53BP1 PROTEIN, HUMAN; TUMOR SUPPRESSOR P53 BINDING PROTEIN 1; UBIQUITIN PROTEIN LIGASE; UBIQUITIN THIOLESTERASE; USP7 PROTEIN, HUMAN;

EID: 84983490951     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.1080/15384101.2015.1007785     Document Type: Article
Times cited : (67)

References (54)
  • 1
    • 70350504453 scopus 로고    scopus 로고
    • The DNA-damage response in human biology and disease
    • PMID:19847258
    • Jackson SP, Bartek J. The DNA-damage response in human biology and disease. Nature 2009; 461:1071-8; PMID:19847258; http://dx.doi.org/ 10.1038/nature08467
    • (2009) Nature , vol.461 , pp. 1071-1078
    • Jackson, S.P.1    Bartek, J.2
  • 2
    • 36749022214 scopus 로고    scopus 로고
    • The DNA damage response: Ten years after
    • PMID:18082599
    • Harper JW, Elledge SJ. The DNA damage response:ten years after. Mol Cell 2007; 28:739-45; PMID:18082599; http://dx.doi.org/10.1016/j. molcel.2007.11.015
    • (2007) Mol Cell , vol.28 , pp. 739-745
    • Harper, J.W.1    Elledge, S.J.2
  • 4
    • 29244434544 scopus 로고    scopus 로고
    • MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks
    • PMID:16377563
    • Stucki M, Clapperton JA, Mohammad D, Yaffe MB, Smerdon SJ and Jackson SP. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell 2005; 123:1213-26; PMID:16377563; http://dx.doi.org/ 10.1016/j.cell.2005.09.038
    • (2005) Cell , vol.123 , pp. 1213-1226
    • Stucki, M.1    Clapperton, J.A.2    Mohammad, D.3    Yaffe, M.B.4    Smerdon, S.J.5    Jackson, S.P.6
  • 5
    • 0037341599 scopus 로고    scopus 로고
    • Distinct spatiotemporal dynamics of mammalian checkpoint regulators induced by DNA damage
    • PMID:12598907
    • Lukas C, Falck J, Bartkova J, Bartek J, Lukas J. Distinct spatiotemporal dynamics of mammalian checkpoint regulators induced by DNA damage. Nat Cell Biol 2003; 5:255-60; PMID:12598907; http://dx.doi.org/ 10.1038/ncb945
    • (2003) Nat Cell Biol , vol.5 , pp. 255-260
    • Lukas, C.1    Falck, J.2    Bartkova, J.3    Bartek, J.4    Lukas, J.5
  • 6
    • 59049091728 scopus 로고    scopus 로고
    • RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins
    • PMID:19203579
    • Doil C, Mailand N, Bekker-Jensen S, Menard P, Larsen DH, Pepperkok R, Ellenberg J, Panier S, Durocher D, Bartek J, et al. RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell 2009; 136:435-46; PMID:19203579; http://dx.doi.org/ 10.1016/j.cell.2008.12.041
    • (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    Ellenberg, J.7    Panier, S.8    Durocher, D.9    Bartek, J.10
  • 7
    • 36249031962 scopus 로고    scopus 로고
    • RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly
    • PMID:18001825
    • Huen MS, Grant R, Manke I, Minn K, Yu X, Yaffe MB, Chen J. RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell 2007; 131:901-14; PMID:18001825; http://dx.doi.org/10.1016/j.cell. 2007.09.041
    • (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    Chen, J.7
  • 8
    • 36248966246 scopus 로고    scopus 로고
    • RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins
    • PMID:18001824
    • Mailand N, Bekker-Jensen S, Faustrup H, Melander F, Bartek J, Lukas C, Lukas J. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 2007; 131:887-900; PMID:18001824; http://dx.doi.org/10.1016/j.cell. 2007.09.040
    • (2007) Cell , vol.131 , pp. 887-900
    • Mailand, N.1    Bekker-Jensen, S.2    Faustrup, H.3    Melander, F.4    Bartek, J.5    Lukas, C.6    Lukas, J.7
  • 9
    • 36749025467 scopus 로고    scopus 로고
    • Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage
    • PMID:18077395
    • 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 U S A 2007; 104:20759-63; PMID:18077395; http://dx.doi.org/10.1073/pnas.0710061104
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 20759-20763
    • Wang, B.1    Elledge, S.J.2
  • 12
    • 63649144413 scopus 로고    scopus 로고
    • Principles of ubiquitin and SUMO modifications in DNA repair
    • PMID:19325626
    • Bergink S, Jentsch S. Principles of ubiquitin and SUMO modifications in DNA repair. Nature 2009; 458:461-7; PMID:19325626; http://dx.doi.org/ 10.1038/nature07963
    • (2009) Nature , vol.458 , pp. 461-467
    • Bergink, S.1    Jentsch, S.2
  • 13
    • 63849107089 scopus 로고    scopus 로고
    • DNA repair: New tales of an old tail
    • PMID:19340068
    • Lukas J, Bartek J. DNA repair: new tales of an old tail. Nature 2009; 458:581-3; PMID:19340068; http://dx. doi.org/10.1038/458581a
    • (2009) Nature , vol.458 , pp. 581-583
    • Lukas, J.1    Bartek, J.2
  • 14
    • 75549087964 scopus 로고    scopus 로고
    • The ubiquitin landscape at DNA double-strand breaks
    • PMID:19948475
    • Messick TE, Greenberg RA. The ubiquitin landscape at DNA double-strand breaks. J Cell Biol 2009; 187:319-26; PMID:19948475; http://dx.doi.org/10.1083/ jcb.200908074
    • (2009) J Cell Biol , vol.187 , pp. 319-326
    • Messick, T.E.1    Greenberg, R.A.2
  • 15
    • 77950958141 scopus 로고    scopus 로고
    • 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks
    • PMID:20362325
    • Bunting SF, Callen E, Wong N, Chen HT, Polato F, Gunn A, Bothmer A, Feldhahn N, Fernandez-Capetillo O, Cao L, et al. 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks. Cell 2010; 141:243-54; PMID:20362325; http://dx.doi.org/ 10.1016/j.cell.2010.03.012
    • (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    Bothmer, A.7    Feldhahn, N.8    Fernandez-Capetillo, O.9    Cao, L.10
  • 17
    • 68949221567 scopus 로고    scopus 로고
    • A selective requirement for 53BP1 in the biological response to genomic instability induced by Brca1 deficiency
    • PMID:19716796
    • Cao L, Xu X, Bunting SF, Liu J, Wang RH, Cao LL, Wu JJ, Peng TN, Chen J, Nussenzweig A, et al. A selective requirement for 53BP1 in the biological response to genomic instability induced by Brca1 deficiency. Mol Cell 2009; 35:534-41; PMID:19716796; http://dx.doi.org/10.1016/j.molcel.2009.06.037
    • (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    Wu, J.J.7    Peng, T.N.8    Chen, J.9    Nussenzweig, A.10
  • 18
    • 84869996067 scopus 로고    scopus 로고
    • RING finger nuclear factor RNF168 is important for defects in homologous recombination caused by loss of the breast cancer susceptibility factor BRCA1
    • PMID:23055523
    • Munoz MC, Laulier C, Gunn A, Cheng A, Robbiani DF, Nussenzweig A, Stark JM. RING finger nuclear factor RNF168 is important for defects in homologous recombination caused by loss of the breast cancer susceptibility factor BRCA1. J Biol Chem 2012; 287:40618-28; PMID:23055523; http://dx.doi.org/ 10.1074/jbc.M112.410951
    • (2012) J Biol Chem , vol.287 , pp. 40618-40628
    • Munoz, M.C.1    Laulier, C.2    Gunn, A.3    Cheng, A.4    Robbiani, D.F.5    Nussenzweig, A.6    Stark, J.M.7
  • 21
    • 33745753378 scopus 로고    scopus 로고
    • Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b
    • PMID:16710298
    • Buchwald G, van der Stoop P, Weichenrieder O, Perrakis A, van LM, Sixma TK. Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b. EMBO J 2006; 25:2465-74; PMID:16710298; http://dx.doi.org/10.1038/sj.emboj.7601144
    • (2006) EMBO J , vol.25 , pp. 2465-2474
    • Buchwald, G.1    van der Stoop, P.2    Weichenrieder, O.3    Perrakis, A.4    van, L.M.5    Sixma, T.K.6
  • 22
    • 29144487990 scopus 로고    scopus 로고
    • Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing
    • PMID:16359901
    • Cao R, Tsukada Y, Zhang Y. Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. Mol Cell 2005; 20:845-54; PMID:16359901; http:// dx.doi.org/10.1016/j.molcel.2005.12.002
    • (2005) Mol Cell , vol.20 , pp. 845-854
    • Cao, R.1    Tsukada, Y.2    Zhang, Y.3
  • 23
    • 7244234099 scopus 로고    scopus 로고
    • Role of histone H2A ubiquitination in Polycomb silencing
    • PMID:15386022
    • Wang H, Wang L, Erdjument-Bromage H, Vidal M, Tempst P, Jones RS, Zhang Y. Role of histone H2A ubiquitination in Polycomb silencing. Nature 2004; 431:873-8; PMID:15386022; http://dx.doi.org/10.1038/nature02985
    • (2004) Nature , vol.431 , pp. 873-878
    • Wang, H.1    Wang, L.2    Erdjument-Bromage, H.3    Vidal, M.4    Tempst, P.5    Jones, R.S.6    Zhang, Y.7
  • 25
    • 70349944658 scopus 로고    scopus 로고
    • Nucleotide excision repair-induced H2A ubiquitination is dependent on MDC1 and RNF8 and reveals a universal DNA damage response
    • PMID:19797077
    • Marteijn JA, Bekker-Jensen S, Mailand N, Lans H, Schwertman P, Gourdin AM, Dantuma NP, Lukas J, Vermeulen W. Nucleotide excision repair-induced H2A ubiquitination is dependent on MDC1 and RNF8 and reveals a universal DNA damage response. J Cell Biol 2009; 186:835-47; PMID:19797077; http:// dx.doi.org/10.1083/jcb.200902150
    • (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    Dantuma, N.P.7    Lukas, J.8    Vermeulen, W.9
  • 26
    • 59249095962 scopus 로고    scopus 로고
    • Histone ubiquitination associates with BRCA1-dependent DNA damage response
    • PMID:19015238
    • Wu J, Huen MS, Lu LY, Ye L, Dou Y, Ljungman M, Chen J, Yu X. Histone ubiquitination associates with BRCA1-dependent DNA damage response. Mol Cell Biol 2009; 29:849-60; PMID:19015238; http://dx.doi. org/10.1128/MCB.01302-08
    • (2009) Mol Cell Biol , vol.29 , pp. 849-860
    • Wu, J.1    Huen, M.S.2    Lu, L.Y.3    Ye, L.4    Dou, Y.5    Ljungman, M.6    Chen, J.7    Yu, X.8
  • 27
    • 58149159543 scopus 로고    scopus 로고
    • Chromatin restoration following nucleotide excision repair involves the incorporation of ubiquitinated H2A at damaged genomic sites
    • PMID:19059499
    • Zhu Q, Wani G, Arab HH, El-Mahdy MA, Ray A, Wani AA. Chromatin restoration following nucleotide excision repair involves the incorporation of ubiquitinated H2A at damaged genomic sites. DNA Repair (Amst) 2009; 8:262-73; PMID:19059499; http://dx. doi.org/10.1016/j.dnarep.2008.11.007
    • (2009) DNA Repair (Amst) , vol.8 , pp. 262-273
    • Zhu, Q.1    Wani, G.2    Arab, H.H.3    El-Mahdy, M.A.4    Ray, A.5    Wani, A.A.6
  • 28
    • 80051494784 scopus 로고    scopus 로고
    • Monoubiquitination of H2AX protein regulates DNA damage response signaling
    • PMID:21676867
    • Pan MR, Peng G, Hung WC, Lin SY. Monoubiquitination of H2AX protein regulates DNA damage response signaling. J Biol Chem 2011; 286:28599-607; PMID:21676867; http://dx.doi.org/10.1074/jbc. M111.256297
    • (2011) J Biol Chem , vol.286 , pp. 28599-28607
    • Pan, M.R.1    Peng, G.2    Hung, W.C.3    Lin, S.Y.4
  • 29
    • 84884201421 scopus 로고    scopus 로고
    • A small molecule inhibitor of polycomb repressive complex 1 inhibits ubiquitin signaling at DNA double-strand breaks
    • PMID:23902761
    • Ismail IH, McDonald D, Strickfaden H, Xu Z, Hendzel MJ. A small molecule inhibitor of polycomb repressive complex 1 inhibits ubiquitin signaling at DNA double-strand breaks. J Biol Chem 2013; 288:26944-54; PMID:23902761; http://dx.doi.org/10.1074/jbc. M113.461699
    • (2013) J Biol Chem , vol.288 , pp. 26944-26954
    • Ismail, I.H.1    McDonald, D.2    Strickfaden, H.3    Xu, Z.4    Hendzel, M.J.5
  • 30
    • 77957748289 scopus 로고    scopus 로고
    • BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair
    • PMID:20921134
    • Ismail IH, Andrin C, McDonald D, Hendzel MJ. BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair. J Cell Biol 2010; 191:45-60; PMID:20921134; http://dx.doi.org/10.1083/ jcb.201003034
    • (2010) J Cell Biol , vol.191 , pp. 45-60
    • Ismail, I.H.1    Andrin, C.2    McDonald, D.3    Hendzel, M.J.4
  • 31
    • 79956086415 scopus 로고    scopus 로고
    • BMI1 is recruited to DNA breaks and contributes to DNA damage- induced H2A ubiquitination and repair
    • PMID:21383063
    • Ginjala V, Nacerddine K, Kulkarni A, Oza J, Hill SJ, Yao M, Citterio E, van LM, Ganesan S. BMI1 is recruited to DNA breaks and contributes to DNA damage- induced H2A ubiquitination and repair. Mol Cell Biol 2011; 31:1972-82; PMID:21383063; http://dx. doi.org/10.1128/MCB.00981-10
    • (2011) Mol Cell Biol , vol.31 , pp. 1972-1982
    • Ginjala, V.1    Nacerddine, K.2    Kulkarni, A.3    Oza, J.4    Hill, S.J.5    Yao, M.6    Citterio, E.7    van, L.M.8    Ganesan, S.9
  • 33
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • PMID:11923872
    • Li M, Chen D, Shiloh A, Luo J, Nikolaev AY, Qin J, Gu W. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 2002; 416:648-53; PMID:11923872; http://dx.doi.org/10.1038/nature737
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 34
    • 1842431904 scopus 로고    scopus 로고
    • Tumour suppression: Disruption of HAUSP gene stabilizes p53
    • PMID:15058298
    • Cummins JM, Rago C, Kohli M, Kinzler KW, Lengauer C, Vogelstein B. Tumour suppression: disruption of HAUSP gene stabilizes p53. Nature 2004; 428:1; PMID:15058298; http://dx.doi.org/10.1038/ nature02501
    • (2004) Nature , vol.428 , pp. 1
    • Cummins, J.M.1    Rago, C.2    Kohli, M.3    Kinzler, K.W.4    Lengauer, C.5    Vogelstein, B.6
  • 35
    • 77956899405 scopus 로고    scopus 로고
    • Regulation of the Polycomb protein RING1B ubiquitination by USP7
    • PMID:20800574
    • de BP, Zaaroor-Regev D, Ciechanover A. Regulation of the Polycomb protein RING1B ubiquitination by USP7. Biochem Biophys Res Commun 2010; 400:389-95; PMID:20800574; http://dx.doi.org/10.1016/j.bbrc.2010.08.082
    • (2010) Biochem Biophys Res Commun , vol.400 , pp. 389-395
    • de, B.P.1    Zaaroor-Regev, D.2    Ciechanover, A.3
  • 36
    • 77955419051 scopus 로고    scopus 로고
    • Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor
    • PMID:20601937
    • Maertens GN, El Messaoudi-Aubert S, Elderkin S, Hiom K, Peters G. Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor. EMBO J 2010; 29:2553-65; PMID:20601937; http://dx.doi.org/10.1038/emboj.2010.129
    • (2010) EMBO J , vol.29 , pp. 2553-2565
    • Maertens, G.N.1    El Messaoudi-Aubert, S.2    Elderkin, S.3    Hiom, K.4    Peters, G.5
  • 37
    • 84855268679 scopus 로고    scopus 로고
    • Switches, excitable responses and oscillations in the Ring1B/Bmi1 ubiquitination system
    • PMID:22194680
    • Nguyen LK, Munoz-Garcia J, Maccario H, Ciechanover A, Kolch W, Kholodenko BN. Switches, excitable responses and oscillations in the Ring1B/Bmi1 ubiquitination system. PLoS Comput Biol 2011; 7:e1002317; PMID:22194680; http://dx.doi.org/10.1371/journal.pcbi.1002317
    • (2011) PLoS Comput Biol , vol.7 , pp. e1002317
    • Nguyen, L.K.1    Munoz-Garcia, J.2    Maccario, H.3    Ciechanover, A.4    Kolch, W.5    Kholodenko, B.N.6
  • 38
    • 84907478478 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 7 regulates nucleotide excision repair through deubiquitinating XPC protein and preventing XPC protein from undergoing ultraviolet light-induced and VCP/p97 protein-regulated proteolysis
    • PMID:25118285
    • He J, Zhu Q, Wani G, Sharma N, Han C, Qian J, Pentz K, Wang QE, Wani AA. Ubiquitin-specific protease 7 regulates nucleotide excision repair through deubiquitinating XPC protein and preventing XPC protein from undergoing ultraviolet light-induced and VCP/p97 protein-regulated proteolysis. J Biol Chem 2014; 289:27278-89; PMID:25118285; http://dx.doi. org/10.1074/jbc.M114.589812
    • (2014) J Biol Chem , vol.289 , pp. 27278-27289
    • He, J.1    Zhu, Q.2    Wani, G.3    Sharma, N.4    Han, C.5    Qian, J.6    Pentz, K.7    Wang, Q.E.8    Wani, A.A.9
  • 39
    • 7744228427 scopus 로고    scopus 로고
    • Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation
    • PMID:15525528
    • de Napoles M, Mermoud JE, Wakao R, Tang YA, Endoh M, Appanah R, Nesterova TB, Silva J, Otte AP, Vidal M, et al. Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation. Dev Cell 2004; 7:663-76; PMID:15525528; http://dx. doi.org/10.1016/j.devcel.2004.10.005
    • (2004) Dev Cell , vol.7 , pp. 663-676
    • de Napoles, M.1    Mermoud, J.E.2    Wakao, R.3    Tang, Y.A.4    Endoh, M.5    Appanah, R.6    Nesterova, T.B.7    Silva, J.8    Otte, A.P.9    Vidal, M.10
  • 42
    • 67649404816 scopus 로고    scopus 로고
    • RNF168, a new RING finger, MIU-containing protein that modifies chromatin by ubiquitination of histones H2A and H2AX
    • PMID:19500350
    • Pinato S, Scandiuzzi C, Arnaudo N, Citterio E, Gaudino G, Penengo L. RNF168, a new RING finger, MIU-containing protein that modifies chromatin by ubiquitination of histones H2A and H2AX. BMC Mol Biol 2009; 10:55; PMID:19500350; http://dx.doi.org/10.1186/1471-2199-10-55
    • (2009) BMC Mol Biol , vol.10 , pp. 55
    • Pinato, S.1    Scandiuzzi, C.2    Arnaudo, N.3    Citterio, E.4    Gaudino, G.5    Penengo, L.6
  • 43
    • 84859475181 scopus 로고    scopus 로고
    • M phase phosphorylation of the epigenetic regulator UHRF1 regulates its physical association with the deubiquitylase USP7 and stability
    • PMID:22411829
    • Ma H, Chen H, Guo X, Wang Z, Sowa ME, Zheng L, Hu S, Zeng P, Guo R, Diao J, et al. M phase phosphorylation of the epigenetic regulator UHRF1 regulates its physical association with the deubiquitylase USP7 and stability. Proc Natl Acad Sci U S A 2012; 109:4828-33; PMID:22411829; http://dx.doi.org/10.1073/pnas.1116349109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 4828-4833
    • Ma, H.1    Chen, H.2    Guo, X.3    Wang, Z.4    Sowa, M.E.5    Zheng, L.6    Hu, S.7    Zeng, P.8    Guo, R.9    Diao, J.10
  • 44
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • PMID:12507430
    • Hu M, Li P, Li M, Li W, Yao T, Wu JW, Gu W, Cohen RE, Shi Y. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 2002; 111:1041-54; PMID:12507430; http://dx.doi.org/10.1016/S0092-8674(02)01199-6
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9
  • 45
    • 80053594090 scopus 로고    scopus 로고
    • Mechanism of USP7/HAUSP activation by its C-terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase
    • PMID:21981925
    • Faesen AC, Dirac AM, Shanmugham A, Ovaa H, Perrakis A, Sixma TK. Mechanism of USP7/HAUSP activation by its C-terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase. Mol Cell 2011; 44:147-59; PMID:21981925; http://dx.doi.org/10.1016/j.molcel.2011.06.034
    • (2011) Mol Cell , vol.44 , pp. 147-159
    • Faesen, A.C.1    Dirac, A.M.2    Shanmugham, A.3    Ovaa, H.4    Perrakis, A.5    Sixma, T.K.6
  • 46
    • 84908282623 scopus 로고    scopus 로고
    • Regulation of 53BP1 protein stability by RNF8 and RNF168 is important for efficient DNA double-strand break repair
    • PMID:25337968
    • Hu Y, Wang C, Huang K, Xia F, Parvin JD, Mondal N. Regulation of 53BP1 protein stability by RNF8 and RNF168 is important for efficient DNA double-strand break repair. PLoS One 2014; 9:e110522; PMID:25337968; http://dx.doi.org/10.1371/journal. pone.0110522
    • (2014) PLoS One , vol.9 , pp. e110522
    • Hu, Y.1    Wang, C.2    Huang, K.3    Xia, F.4    Parvin, J.D.5    Mondal, N.6
  • 47
    • 84892562030 scopus 로고    scopus 로고
    • USP3 counteracts RNF168 via deubiquitinating H2A and gammaH2AX at lysine 13 and 15
    • PMID:24196443
    • Sharma N, Zhu Q, Wani G, He J, Wang QE, Wani AA. USP3 counteracts RNF168 via deubiquitinating H2A and gammaH2AX at lysine 13 and 15. Cell Cycle 2014; 13:106-14; PMID:24196443; http://dx.doi.org/10.4161/cc.26814
    • (2014) Cell Cycle , vol.13 , pp. 106-114
    • Sharma, N.1    Zhu, Q.2    Wani, G.3    He, J.4    Wang, Q.E.5    Wani, A.A.6
  • 48
    • 84878758649 scopus 로고    scopus 로고
    • The deubiquitylating enzyme USP44 counteracts the DNA double-strand break response mediated by the RNF8 and RNF168 ubiquitin ligases
    • PMID:23615962
    • 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 2013; 288:16579-87; PMID:23615962; http://dx.doi. org/10.1074/jbc.M113.459917
    • (2013) J Biol Chem , vol.288 , pp. 16579-16587
    • Mosbech, A.1    Lukas, C.2    Bekker-Jensen, S.3    Mailand, N.4
  • 50
    • 79251496438 scopus 로고    scopus 로고
    • Turnover of BRCA1 involves in radiationinduced apoptosis
    • PMID:21217819
    • LiuW, Zong W, Wu G, Fujita T, Li W, Wu J, Wan Y. Turnover of BRCA1 involves in radiationinduced apoptosis. PLoS One 2010; 5:e14484; PMID:21217819; http://dx.doi.org/10.1371/journal. pone.0014484
    • (2010) PLoS One , vol.5 , pp. e14484
    • Liu, W.1    Zong, W.2    Wu, G.3    Fujita, T.4    Li, W.5    Wu, J.6    Wan, Y.7
  • 51
    • 22244478319 scopus 로고    scopus 로고
    • DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation
    • PMID:16030353
    • Wang QE, Zhu Q,Wani G, El-Mahdy MA, Li J, Wani AA. DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation. Nucleic Acids Res 2005; 33:4023-34; PMID:16030353; http://dx. doi.org/10.1093/nar/gki684
    • (2005) Nucleic Acids Res , vol.33 , pp. 4023-4034
    • Wang, Q.E.1    Zhu, Q.2    Wani, G.3    El-Mahdy, M.A.4    Li, J.5    Wani, A.A.6
  • 52
    • 0023425741 scopus 로고
    • Quantitation of pyrimidine dimers by immunoslot blot following sublethal UV-irradiation of human cells
    • PMID:3423120
    • Wani AA, D’Ambrosio SM, Alvi NK. Quantitation of pyrimidine dimers by immunoslot blot following sublethal UV-irradiation of human cells. Photochem Photobiol 1987; 46:477-82; PMID:3423120; http:// dx.doi.org/10.1111/j.1751-1097.1987.tb04798.x
    • (1987) Photochem Photobiol , vol.46 , pp. 477-482
    • Wani, A.A.1    D’Ambrosio, S.M.2    Alvi, N.K.3
  • 53
    • 77955209543 scopus 로고    scopus 로고
    • Dissociation of CAK from core TFIIH reveals a functional link between XP-G/CS and the TFIIH disassembly state
    • PMID:20543986
    • Arab HH, Wani G, Ray A, Shah ZI, Zhu Q, Wani AA. Dissociation of CAK from core TFIIH reveals a functional link between XP-G/CS and the TFIIH disassembly state. PLoS One 2010; 5:e11007; PMID:20543986; http://dx.doi.org/10.1371/journal. pone.0011007
    • (2010) PLoS One , vol.5 , pp. e11007
    • Arab, H.H.1    Wani, G.2    Ray, A.3    Shah, Z.I.4    Zhu, Q.5    Wani, A.A.6
  • 54
    • 84869177693 scopus 로고    scopus 로고
    • Lack of CAK complex accumulation at DNA damage sites in XPB and XP-B/CS fibroblasts reveals differential regulation of CAK anchoring to core TFIIH by XPB and XPD helicases during nucleotide excision repair
    • PMID:23083890
    • Zhu Q, Wani G, Sharma N, Wani A. Lack of CAK complex accumulation at DNA damage sites in XPB and XP-B/CS fibroblasts reveals differential regulation of CAK anchoring to core TFIIH by XPB and XPD helicases during nucleotide excision repair. DNA Repair (Amst) 2012; 11:942-50; PMID:23083890; http://dx.doi.org/10.1016/j. dnarep.2012.09.003
    • (2012) DNA Repair (Amst) , vol.11 , pp. 942-950
    • Zhu, Q.1    Wani, G.2    Sharma, N.3    Wani, A.4


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