메뉴 건너뛰기




Volumn 6, Issue SEP, 2015, Pages

Fine-tuning the ubiquitin code at DNA double-strand breaks: Deubiquitinating enzymes at work

Author keywords

Cancer; Chromatin; Deubiquitinating enzymes (DUBs); DNA damage response (DDR); DNA double strand breaks (DSBs); Hematopoietic stem cell (HSC); Histone H2A; Ubiquitin

Indexed keywords

DEUBIQUITINASE; DOUBLE STRANDED DNA; METALLOPROTEINASE; PROTEIN P53; UBIQUITIN; UBIQUITIN THIOLESTERASE;

EID: 84944721504     PISSN: None     EISSN: 16648021     Source Type: Journal    
DOI: 10.3389/fgene.2015.00282     Document Type: Review
Times cited : (24)

References (173)
  • 1
    • 82955233157 scopus 로고    scopus 로고
    • The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks
    • Acs, K., Luijsterburg, M. S., Ackermann, L., Salomons, F. A., Hoppe, T., and Dantuma, N. P. (2011). The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks. Nat. Struct. Mol. Biol. 18, 1345-1350. doi: 10.1038/nsmb.2188
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 1345-1350
    • Acs, K.1    Luijsterburg, M.S.2    Ackermann, L.3    Salomons, F.A.4    Hoppe, T.5    Dantuma, N.P.6
  • 3
    • 84892910467 scopus 로고    scopus 로고
    • MYSM1 is mutated in a family with transient transfusion-dependent anemia, mild thrombocytopenia, and low NK-and B-cell counts
    • Alsultan, A., Shamseldin, H. E., Osman, M. E., Aljabri, M., and Alkuraya, F. S. (2013). MYSM1 is mutated in a family with transient transfusion-dependent anemia, mild thrombocytopenia, and low NK-and B-cell counts. Blood 122, 3844-3845. doi: 10.1182/blood-2013-09-527127
    • (2013) Blood , vol.122 , pp. 3844-3845
    • Alsultan, A.1    Shamseldin, H.E.2    Osman, M.E.3    Aljabri, M.4    Alkuraya, F.S.5
  • 4
    • 84873320525 scopus 로고    scopus 로고
    • Mechanisms of programmed DNA lesions and genomic instability in the immune system
    • Alt, F. W., Zhang, Y., Meng, F.-L., Guo, C., and Schwer, B. (2013). Mechanisms of programmed DNA lesions and genomic instability in the immune system. Cell 152, 417-429. doi: 10.1016/j.cell.2013.01.007
    • (2013) Cell , vol.152 , pp. 417-429
    • Alt, F.W.1    Zhang, Y.2    Meng, F.-L.3    Guo, C.4    Schwer, B.5
  • 5
    • 84897990643 scopus 로고    scopus 로고
    • Transcriptionally active chromatin recruits homologous recombination at DNA double-strand breaks
    • Aymard, F., Bugler, B., Schmidt, C. K., Guillou, E., Caron, P., Briois, S., et al. (2014). Transcriptionally active chromatin recruits homologous recombination at DNA double-strand breaks. Nat. Struct. Mol. Biol. 21, 366-374. doi: 10.1038/nsmb.2796
    • (2014) Nat. Struct. Mol. Biol , vol.21 , pp. 366-374
    • Aymard, F.1    Bugler, B.2    Schmidt, C.K.3    Guillou, E.4    Caron, P.5    Briois, S.6
  • 6
    • 84904043095 scopus 로고    scopus 로고
    • Quiescent hematopoietic stem cells accumulate DNA damage during aging that is repaired upon entry into cell cycle
    • Beerman, I., Seita, J., Inlay, M. A., Weissman, I. L., and Rossi, D. J. (2014). Quiescent hematopoietic stem cells accumulate DNA damage during aging that is repaired upon entry into cell cycle. Cell Stem Cell 15, 37-50. doi: 10.1016/j.stem.2014.04.016
    • (2014) Cell Stem Cell , vol.15 , pp. 37-50
    • Beerman, I.1    Seita, J.2    Inlay, M.A.3    Weissman, I.L.4    Rossi, D.J.5
  • 7
    • 84895497062 scopus 로고    scopus 로고
    • Impact of genomic damage and ageing on stem cell function
    • Behrens, A., Van Deursen, J. M., Rudolph, K. L., and Schumacher, B. (2014). Impact of genomic damage and ageing on stem cell function. Nat. Cell Biol. 16, 201-207. doi: 10.1038/ncb2928
    • (2014) Nat. Cell Biol , vol.16 , pp. 201-207
    • Behrens, A.1    Van Deursen, J.M.2    Rudolph, K.L.3    Schumacher, B.4
  • 8
    • 84862986431 scopus 로고    scopus 로고
    • HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes
    • Bekker-Jensen, S., Danielsen, J., Fugger, K., Gromova, I., Nerstedt, A., Bartek, J., et al. (2010). HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Nat. Cell Biol. 12, 80-86. doi: 10.1038/ncb2008
    • (2010) Nat. Cell Biol , vol.12 , pp. 80-86
    • Bekker-Jensen, S.1    Danielsen, J.2    Fugger, K.3    Gromova, I.4    Nerstedt, A.5    Bartek, J.6
  • 9
    • 84927663729 scopus 로고    scopus 로고
    • p53 mediates loss of hematopoietic stem cell function and lymphopenia in Mysm1 deficiency
    • Belle, J. I., Langlais, D., Petrov, J. C., Pardo, M., Jones, R. G., Gros, P., et al. (2015). p53 mediates loss of hematopoietic stem cell function and lymphopenia in Mysm1 deficiency. Blood 125, 2344-2348. doi: 10.1182/blood-2014-05-574111
    • (2015) Blood , vol.125 , pp. 2344-2348
    • Belle, J.I.1    Langlais, D.2    Petrov, J.C.3    Pardo, M.4    Jones, R.G.5    Gros, P.6
  • 10
    • 84899412770 scopus 로고    scopus 로고
    • H2A-DUBbing the mammalian epigenome: expanding frontiers for histone H2A deubiquitinating enzymes in cell biology and physiology
    • Belle, J. I., and Nijnik, A. (2014). H2A-DUBbing the mammalian epigenome: expanding frontiers for histone H2A deubiquitinating enzymes in cell biology and physiology. Int. J. Biochem. Cell Biol. 50C, 161-174. doi: 10.1016/j.biocel.2014.03.004
    • (2014) Int. J. Biochem. Cell Biol , vol.50C , pp. 161-174
    • Belle, J.I.1    Nijnik, A.2
  • 11
    • 0036713424 scopus 로고    scopus 로고
    • Cancer predisposition and hematopoietic failure in Rad50S/S mice
    • Bender, C. (2002). Cancer predisposition and hematopoietic failure in Rad50S/S mice. Genes Dev. 16, 2237-2251. doi: 10.1101/gad.1007902
    • (2002) Genes Dev , vol.16 , pp. 2237-2251
    • Bender, C.1
  • 12
    • 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., and Ciechanover, A. (2006). The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity. Mol. Cell 24, 701-711. doi: 10.1016/j.molcel.2006.10.022
    • (2006) Mol. Cell , vol.24 , pp. 701-711
    • Ben-Saadon, R.1    Zaaroor, D.2    Ziv, T.3    Ciechanover, A.4
  • 13
    • 78650979504 scopus 로고    scopus 로고
    • DNA-damage response in tissue-specific and cancer stem cells
    • Blanpain, C., Mohrin, M., Sotiropoulou, P. A., and Passegue, E. (2011). DNA-damage response in tissue-specific and cancer stem cells. Cell Stem Cell 8, 16-29. doi: 10.1016/j.stem.2010.12.012
    • (2011) Cell Stem Cell , vol.8 , pp. 16-29
    • Blanpain, C.1    Mohrin, M.2    Sotiropoulou, P.A.3    Passegue, E.4
  • 14
    • 79955627875 scopus 로고    scopus 로고
    • Genomic instability, defective spermatogenesis, immunodeficiency, and cancer in a mouse model of the RIDDLE syndrome
    • Bohgaki, T., Bohgaki, M., Cardoso, R., Panier, S., Zeegers, D., Li, L., et al. (2011). Genomic instability, defective spermatogenesis, immunodeficiency, and cancer in a mouse model of the RIDDLE syndrome. PLoS Genetics 7:e1001381. doi: 10.1371/journal.pgen.1001381
    • (2011) PLoS Genetics , vol.7
    • Bohgaki, T.1    Bohgaki, M.2    Cardoso, R.3    Panier, S.4    Zeegers, D.5    Li, L.6
  • 15
    • 79959694149 scopus 로고    scopus 로고
    • The nuclear deubiquitinase BAP1 is commonly inactivated by somatic mutations and 3p21.1 losses in malignant pleural mesothelioma
    • Bott, M., Brevet, M., Taylor, B. S., Shimizu, S., Ito, T., Wang, L., et al. (2011). The nuclear deubiquitinase BAP1 is commonly inactivated by somatic mutations and 3p21.1 losses in malignant pleural mesothelioma. Nat. Genet. 43, 668-672. doi: 10.1038/ng.855
    • (2011) Nat. Genet , vol.43 , pp. 668-672
    • Bott, M.1    Brevet, M.2    Taylor, B.S.3    Shimizu, S.4    Ito, T.5    Wang, L.6
  • 16
    • 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, J., Pieterse, M., Bartkova, J., Van Der Gulden, H., et al. (2010). 53BP1 loss rescues BRCA1 deficiency and is associated with triple-negative and BRCA-mutated breast cancers. Nat. Struct. Mol. Biol. 17, 688-695. doi: 10.1038/nsmb.1831
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 688-695
    • Bouwman, P.1    Aly, A.2    Escandell, J.3    Pieterse, M.4    Bartkova, J.5    Van Der Gulden, H.6
  • 17
    • 0742305878 scopus 로고    scopus 로고
    • The SANT domain: a unique histone-tail-binding module?
    • Boyer, L. A., Latek, R. R., and Peterson, C. L. (2004). The SANT domain: a unique histone-tail-binding module? Nat. Rev. Mol. Cell Biol. 5, 158-163. doi: 10.1038/nrm1314
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 158-163
    • Boyer, L.A.1    Latek, R.R.2    Peterson, C.L.3
  • 18
    • 84933073669 scopus 로고    scopus 로고
    • Ubiquitylation, neddylation and the DNA damage response
    • Brown, J. S., and Jackson, S. P. (2015). Ubiquitylation, neddylation and the DNA damage response. Open Biol. 5, 150018. doi: 10.1098/rsob.150018
    • (2015) Open Biol , vol.5
    • Brown, J.S.1    Jackson, S.P.2
  • 19
    • 77950958141 scopus 로고    scopus 로고
    • 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks
    • Bunting, S. F., Call�n, E., Wong, N., Chen, H., Polato, F., Gunn, A., et al. (2010). 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks. Cell 141, 243-254. doi: 10.1016/j.cell.2010.03.012
    • (2010) Cell , vol.141 , pp. 243-254
    • Bunting, S.F.1    Call�n, E.2    Wong, N.3    Chen, H.4    Polato, F.5    Gunn, A.6
  • 20
    • 84867101138 scopus 로고    scopus 로고
    • The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response
    • Butler, L. R., Densham, R. M., Jia, J., Garvin, A. J., Stone, H. R., Shah, V., et al. (2012). The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response. EMBO J. 31, 3918-3934. doi: 10.1038/emboj.2012.232
    • (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
  • 21
    • 69949173205 scopus 로고    scopus 로고
    • Deubiquitinase activities required for hepatocyte growth factor-induced scattering of epithelial cells
    • Buus, R., Faronato, M., Hammond, D. E., Urbe, S., and Clague, M. J. (2009). Deubiquitinase activities required for hepatocyte growth factor-induced scattering of epithelial cells. Curr. Biol. 19, 1463-1466. doi: 10.1016/j.cub.2009.07.040
    • (2009) Curr. Biol , vol.19 , pp. 1463-1466
    • Buus, R.1    Faronato, M.2    Hammond, D.E.3    Urbe, S.4    Clague, M.J.5
  • 22
    • 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, S. F., Liu, J., Wang, R., Cao, L. L., et al. (2009). A selective requirement for 53BP1 in the biological response to genomic instability induced by Brca1 deficiency. Mol. Cell 35, 534-541. doi: 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.5    Cao, L.L.6
  • 24
    • 84863625900 scopus 로고    scopus 로고
    • Bone marrow failure in Fanconi anemia is triggered by an exacerbated p53/p21 DNA damage response that impairs hematopoietic stem and progenitor cells
    • Ceccaldi, R., Parmar, K., Mouly, E., Delord, M., Kim, J. M., Regairaz, M., et al. (2012). Bone marrow failure in Fanconi anemia is triggered by an exacerbated p53/p21 DNA damage response that impairs hematopoietic stem and progenitor cells. Cell Stem Cell 11, 36-49. doi: 10.1016/j.stem.2012.05.013
    • (2012) Cell Stem Cell , vol.11 , pp. 36-49
    • Ceccaldi, R.1    Parmar, K.2    Mouly, E.3    Delord, M.4    Kim, J.M.5    Regairaz, M.6
  • 25
    • 84865386136 scopus 로고    scopus 로고
    • BRCA1-associated exclusion of 53BP1 from DNA damage sites underlies temporal control of DNA repair
    • Chapman, J. R., Sossick, A. J., Boulton, S. J., and Jackson, S. P. (2012). BRCA1-associated exclusion of 53BP1 from DNA damage sites underlies temporal control of DNA repair. J. Cell Sci. 125, 3529-3534. doi: 10.1242/jcs.105353
    • (2012) J. Cell Sci , vol.125 , pp. 3529-3534
    • Chapman, J.R.1    Sossick, A.J.2    Boulton, S.J.3    Jackson, S.P.4
  • 26
    • 78649349810 scopus 로고    scopus 로고
    • A chromatin localization screen reveals poly (ADP ribose)-regulated recruitment of the repressive polycomb and NuRD complexes to sites of DNA damage
    • Chou, D., Adamson, B., Dephoure, N., Tan, X., Nottke, A., Hurov, K., et al. (2010). A chromatin localization screen reveals poly (ADP ribose)-regulated recruitment of the repressive polycomb and NuRD complexes to sites of DNA damage. Proc. Natl. Acad. Sci. U.S.A. 107, 18475-18480. doi: 10.1073/pnas.1012946107
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 18475-18480
    • Chou, D.1    Adamson, B.2    Dephoure, N.3    Tan, X.4    Nottke, A.5    Hurov, K.6
  • 27
    • 78649336706 scopus 로고    scopus 로고
    • The DNA damage response: making it safe to play with knives
    • Ciccia, A., and Elledge, S. J. (2010). The DNA damage response: making it safe to play with knives. Mol. Cell 40, 179-204. doi: 10.1016/j.molcel.2010.09.019
    • (2010) Mol. Cell , vol.40 , pp. 179-204
    • Ciccia, A.1    Elledge, S.J.2
  • 28
    • 84858119736 scopus 로고    scopus 로고
    • Cellular functions of the DUBs
    • Clague, M. J., Coulson, J. M., and Urbe, S. (2012). Cellular functions of the DUBs. J. Cell Sci. 125, 277-286. doi: 10.1242/jcs.090985
    • (2012) J. Cell Sci , vol.125 , pp. 277-286
    • Clague, M.J.1    Coulson, J.M.2    Urbe, S.3
  • 29
    • 79953869356 scopus 로고    scopus 로고
    • The BRCA1-RAP80 complex regulates DNA repair mechanism utilization by restricting end resection
    • Coleman, K. A., and Greenberg, R. A. (2011). The BRCA1-RAP80 complex regulates DNA repair mechanism utilization by restricting end resection. J. Biol. Chem. 286, 13669-13680. doi: 10.1074/jbc.M110.213728
    • (2011) J. Biol. Chem , vol.286 , pp. 13669-13680
    • Coleman, K.A.1    Greenberg, R.A.2
  • 30
    • 62649104153 scopus 로고    scopus 로고
    • K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1
    • Cooper, E. M., Cutcliffe, C., Kristiansen, T. Z., Pandey, A., Pickart, C. M., and Cohen, R. E. (2009). K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1. EMBO J. 28, 621-631. doi: 10.1038/emboj.2009.27
    • (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
  • 31
    • 84898040489 scopus 로고    scopus 로고
    • USP3 inhibits type I interferon signaling by deubiquitinating RIG-I-like receptors
    • Cui, J., Song, Y., Li, Y., Zhu, Q., Tan, P., Qin, Y., et al. (2014). USP3 inhibits type I interferon signaling by deubiquitinating RIG-I-like receptors. Cell Res. 24, 400-416. doi: 10.1038/cr.2013.170
    • (2014) Cell Res , vol.24 , pp. 400-416
    • Cui, J.1    Song, Y.2    Li, Y.3    Zhu, Q.4    Tan, P.5    Qin, Y.6
  • 32
    • 84903536551 scopus 로고    scopus 로고
    • Dub3 controls DNA damage signalling by direct deubiquitination of H2AX
    • Delgado-Diaz, M. R., Martin, Y., Berg, A., Freire, R., and Smits, V. A. (2014). Dub3 controls DNA damage signalling by direct deubiquitination of H2AX. Mol. Oncol. 8, 884-893. doi: 10.1016/j.molonc.2014.03.003
    • (2014) Mol. Oncol , vol.8 , pp. 884-893
    • Delgado-Diaz, M.R.1    Martin, Y.2    Berg, A.3    Freire, R.4    Smits, V.A.5
  • 33
    • 84866467141 scopus 로고    scopus 로고
    • Loss of the tumor suppressor BAP1 causes myeloid transformation
    • Dey, A., Seshasayee, D., Noubade, R., French, D. M., Liu, J., Chaurushiya, M. S., et al. (2012). Loss of the tumor suppressor BAP1 causes myeloid transformation. Science 337, 1541-1546. doi: 10.1126/science.1221711
    • (2012) Science , vol.337 , pp. 1541-1546
    • Dey, A.1    Seshasayee, D.2    Noubade, R.3    French, D.M.4    Liu, J.5    Chaurushiya, M.S.6
  • 34
    • 84885393469 scopus 로고    scopus 로고
    • Transcriptional regulation by Polycomb group proteins
    • Di Croce, L., and Helin, K. (2013). Transcriptional regulation by Polycomb group proteins. Nat. Struct. Mol. Biol. 20, 1147-1155. doi: 10.1038/nsmb.2669
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 1147-1155
    • Di Croce, L.1    Helin, K.2
  • 35
    • 84908315165 scopus 로고    scopus 로고
    • Identification of genes important for cutaneous function revealed by a large scale reverse genetic screen in the mouse
    • DiTommaso, T., Jones, L. K., Cottle, D. L., Gerdin, A. K., Vancollie, V. E., Watt, F. M., et al. (2014). Identification of genes important for cutaneous function revealed by a large scale reverse genetic screen in the mouse. PLoS Genet. 10:e1004705. doi: 10.1371/journal.pgen.1004705
    • (2014) PLoS Genet , vol.10
    • DiTommaso, T.1    Jones, L.K.2    Cottle, D.L.3    Gerdin, A.K.4    Vancollie, V.E.5    Watt, F.M.6
  • 36
    • 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, D. H., Pepperkok, R., et al. (2009). RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell 136, 435-446. doi: 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
  • 37
    • 0345276495 scopus 로고    scopus 로고
    • Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair
    • Dong, Y., Hakimi, M., Chen, X., Kumaraswamy, E., Cooch, N., Godwin, A., et al. (2003). Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair. Mol. Cell 12, 1087-1099. doi: 10.1016/S1097-2765(03)00424-6
    • (2003) Mol. Cell , vol.12 , pp. 1087-1099
    • Dong, Y.1    Hakimi, M.2    Chen, X.3    Kumaraswamy, E.4    Cooch, N.5    Godwin, A.6
  • 38
    • 84888640837 scopus 로고    scopus 로고
    • BAP1 is phosphorylated at serine 592 in S-phase following DNA damage
    • Eletr, Z. M., Yin, L., and Wilkinson, K. D. (2013). BAP1 is phosphorylated at serine 592 in S-phase following DNA damage. FEBS Lett. 587, 3906-3911. doi: 10.1016/j.febslet.2013.10.035
    • (2013) FEBS Lett , vol.587 , pp. 3906-3911
    • Eletr, Z.M.1    Yin, L.2    Wilkinson, K.D.3
  • 39
    • 84873085753 scopus 로고    scopus 로고
    • A strategy for modulation of enzymes in the ubiquitin system
    • Ernst, A., Avvakumov, G., Tong, J., Fan, Y., Zhao, Y., Alberts, P., et al. (2013). A strategy for modulation of enzymes in the ubiquitin system. Science 339, 590-595. doi: 10.1126/science.1230161
    • (2013) Science , vol.339 , pp. 590-595
    • Ernst, A.1    Avvakumov, G.2    Tong, J.3    Fan, Y.4    Zhao, Y.5    Alberts, P.6
  • 40
    • 84555218153 scopus 로고    scopus 로고
    • The differential modulation of USP activity by internal regulatory domains, interactors and eight ubiquitin chain types
    • Faesen, A. C., Luna-Vargas, M. P., Geurink, P. P., Clerici, M., Merkx, R., Van Dijk, W. J., et al. (2011). The differential modulation of USP activity by internal regulatory domains, interactors and eight ubiquitin chain types. Chem. Biol. 18, 1550-1561. doi: 10.1016/j.chembiol.2011.10.017
    • (2011) Chem. Biol , vol.18 , pp. 1550-1561
    • Faesen, A.C.1    Luna-Vargas, M.P.2    Geurink, P.P.3    Clerici, M.4    Merkx, R.5    Van Dijk, W.J.6
  • 41
    • 84906254220 scopus 로고    scopus 로고
    • Replication stress is a potent driver of functional decline in ageing haematopoietic stem cells
    • Flach, J., Bakker, S. T., Mohrin, M., Conroy, P. C., Pietras, E. M., Reynaud, D., et al. (2014). Replication stress is a potent driver of functional decline in ageing haematopoietic stem cells. Nature 512, 198-202. doi: 10.1038/nature13619
    • (2014) Nature , vol.512 , pp. 198-202
    • Flach, J.1    Bakker, S.T.2    Mohrin, M.3    Conroy, P.C.4    Pietras, E.M.5    Reynaud, D.6
  • 43
    • 84883796667 scopus 로고    scopus 로고
    • The aurora B kinase and the polycomb protein ring1B combine to regulate active promoters in quiescent lymphocytes
    • Frangini, A., Sjoberg, M., Roman-Trufero, M., Dharmalingam, G., Haberle, V., Bartke, T., et al. (2013). The aurora B kinase and the polycomb protein ring1B combine to regulate active promoters in quiescent lymphocytes. Mol. Cell 51, 647-661. doi: 10.1016/j.molcel.2013.08.022
    • (2013) Mol. Cell , vol.51 , pp. 647-661
    • Frangini, A.1    Sjoberg, M.2    Roman-Trufero, M.3    Dharmalingam, G.4    Haberle, V.5    Bartke, T.6
  • 44
    • 84904036680 scopus 로고    scopus 로고
    • Writing and reading H2B monoubiquitylation
    • Fuchs, G., and Oren, M. (2014). Writing and reading H2B monoubiquitylation. Biochim. Biophys. Acta 1839, 694-701. doi: 10.1016/j.bbagrm.2014.01.002
    • (2014) Biochim. Biophys. Acta , vol.1839 , pp. 694-701
    • Fuchs, G.1    Oren, M.2
  • 45
    • 84861968321 scopus 로고    scopus 로고
    • RNF20 and USP44 regulate stem cell differentiation by modulating H2B monoubiquitylation
    • Fuchs, G., Shema, E., Vesterman, R., Kotler, E., Wolchinsky, Z., Wilder, S., et al. (2012). RNF20 and USP44 regulate stem cell differentiation by modulating H2B monoubiquitylation. Mol. Cell 46, 662-673. doi: 10.1016/j.molcel.2012.05.023
    • (2012) Mol. Cell , vol.46 , pp. 662-673
    • Fuchs, G.1    Shema, E.2    Vesterman, R.3    Kotler, E.4    Wolchinsky, Z.5    Wilder, S.6
  • 46
    • 84866952680 scopus 로고    scopus 로고
    • Genotoxic consequences of endogenous aldehydes on mouse haematopoietic stem cell function
    • Garaycoechea, J. I., Crossan, G. P., Langevin, F., Daly, M., Arends, M. J., and Patel, K. J. (2012). Genotoxic consequences of endogenous aldehydes on mouse haematopoietic stem cell function. Nature 489, 571-575. doi: 10.1038/nature11368
    • (2012) Nature , vol.489 , pp. 571-575
    • Garaycoechea, J.I.1    Crossan, G.P.2    Langevin, F.3    Daly, M.4    Arends, M.J.5    Patel, K.J.6
  • 47
    • 84920936909 scopus 로고    scopus 로고
    • RNF168 promotes noncanonical K27 ubiquitination to signal DNA damage
    • Gatti, M., Pinato, S., Maiolica, A., Rocchio, F., Prato, M. G., Aebersold, R., et al. (2015). RNF168 promotes noncanonical K27 ubiquitination to signal DNA damage. Cell Rep. 10, 226-238. doi: 10.1016/j.celrep.2014.12.021
    • (2015) Cell Rep , vol.10 , pp. 226-238
    • Gatti, M.1    Pinato, S.2    Maiolica, A.3    Rocchio, F.4    Prato, M.G.5    Aebersold, R.6
  • 48
    • 84863793933 scopus 로고    scopus 로고
    • A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase
    • Gatti, M., Pinato, S., Maspero, E., Soffientini, P., Polo, S., and Penengo, L. (2012). A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase. Cell cycle (Georgetown, Tex) 11, 2538-2544. doi: 10.4161/cc.20919
    • (2012) Cell cycle (Georgetown, Tex) , vol.11 , pp. 2538-2544
    • Gatti, M.1    Pinato, S.2    Maspero, E.3    Soffientini, P.4    Polo, S.5    Penengo, L.6
  • 49
    • 84938952451 scopus 로고    scopus 로고
    • Interplay of H2A deubiquitinase 2A-DUB/Mysm1 and the p19/p53 axis in hematopoiesis, early T-cell development and tissue differentiation
    • Gatzka, M., Tasdogan, A., Hainzl, A., Allies, G., Maity, P., Wilms, C., et al. (2015). Interplay of H2A deubiquitinase 2A-DUB/Mysm1 and the p19/p53 axis in hematopoiesis, early T-cell development and tissue differentiation. Cell Death Differ. 22, 1451-1462. doi: 10.1038/cdd.2014.231
    • (2015) Cell Death Differ , vol.22 , pp. 1451-1462
    • Gatzka, M.1    Tasdogan, A.2    Hainzl, A.3    Allies, G.4    Maity, P.5    Wilms, C.6
  • 50
    • 84876909069 scopus 로고    scopus 로고
    • The ageing haematopoietic stem cell compartment
    • Geiger, H., De Haan, G., and Florian, M. C. (2013). The ageing haematopoietic stem cell compartment. Nat. Rev. Immunol. 13, 376-389. doi: 10.1038/nri3433
    • (2013) Nat. Rev. Immunol , vol.13 , pp. 376-389
    • Geiger, H.1    De Haan, G.2    Florian, M.C.3
  • 51
    • 79952633107 scopus 로고    scopus 로고
    • Polycomb group proteins in the DNA damage response-A link between radiation resistance and "stemness."
    • Gieni, R. S., Ismail, I. H., Campbell, S., and Hendzel, M. J. (2011). Polycomb group proteins in the DNA damage response-A link between radiation resistance and "stemness." Cell Cycle 10, 883-894. doi: 10.4161/cc.10.6.14907
    • (2011) Cell Cycle , vol.10 , pp. 883-894
    • Gieni, R.S.1    Ismail, I.H.2    Campbell, S.3    Hendzel, M.J.4
  • 52
    • 79956086415 scopus 로고    scopus 로고
    • BMI1 is recruited to DNA breaks and contributes to DNA damage-induced H2A ubiquitination and repair
    • Ginjala, V., Nacerddine, K., Kulkarni, A., Oza, J., Hill, S., Yao, M., et al. (2011). BMI1 is recruited to DNA breaks and contributes to DNA damage-induced H2A ubiquitination and repair. Mol. Cell. Biol. 31, 1972-1982. doi: 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.5    Yao, M.6
  • 53
    • 0017601447 scopus 로고
    • Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24
    • Goldknopf, I., and Busch, H. (1977). Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24. Proc. Natl. Acad. Sci. U.S.A. 74, 864-868. doi: 10.1073/pnas.74.3.864
    • (1977) Proc. Natl. Acad. Sci. U.S.A , vol.74 , pp. 864-868
    • Goldknopf, I.1    Busch, H.2
  • 54
    • 84941969036 scopus 로고    scopus 로고
    • Repair versus checkpoint functions of Brca1 are differentially regulated by site of chromatin binding
    • Goldstein, M., and Kastan, M. B. (2015). Repair versus checkpoint functions of Brca1 are differentially regulated by site of chromatin binding. Cancer Res. 75, 2699-2707. doi: 10.1158/0008-5472.CAN-15-0400
    • (2015) Cancer Res , vol.75 , pp. 2699-2707
    • Goldstein, M.1    Kastan, M.B.2
  • 55
    • 84992005830 scopus 로고    scopus 로고
    • Screen identifies bromodomain protein ZMYND8 in chromatin recognition of transcription-associated DNA damage that promotes homologous recombination
    • Gong, F., Chiu, L. Y., Cox, B., Aymard, F., Clouaire, T., Leung, J. W., et al. (2015). Screen identifies bromodomain protein ZMYND8 in chromatin recognition of transcription-associated DNA damage that promotes homologous recombination. Genes Dev. 29, 197-211. doi: 10.1101/gad.252189.114
    • (2015) Genes Dev , vol.29 , pp. 197-211
    • Gong, F.1    Chiu, L.Y.2    Cox, B.3    Aymard, F.4    Clouaire, T.5    Leung, J.W.6
  • 56
    • 29944434644 scopus 로고    scopus 로고
    • Multifactorial contributions to an acute DNA damage response by BRCA1/BARD1-containing complexes
    • Greenberg, R. A., Sobhian, B., Pathania, S., Cantor, S. B., Nakatani, Y., and Livingston, D. M. (2006). Multifactorial contributions to an acute DNA damage response by BRCA1/BARD1-containing complexes. Genes Dev. 20, 34-46. doi: 10.1101/gad.1381306
    • (2006) Genes Dev , vol.20 , pp. 34-46
    • Greenberg, R.A.1    Sobhian, B.2    Pathania, S.3    Cantor, S.B.4    Nakatani, Y.5    Livingston, D.M.6
  • 57
    • 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., Gr�fte, M., et al. (2012). TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes. Cell 150, 697-709. doi: 10.1016/j.cell.2012.06.039
    • (2012) Cell , vol.150 , pp. 697-709
    • Gudjonsson, T.1    Altmeyer, M.2    Savic, V.3    Toledo, L.4    Dinant, C.5    Gr�fte, M.6
  • 58
    • 78649700287 scopus 로고    scopus 로고
    • Frequent mutation of BAP1 in metastasizing uveal melanomas
    • Harbour, J. W., Onken, M. D., Roberson, E. D., Duan, S., Cao, L., Worley, L. A., et al. (2010). Frequent mutation of BAP1 in metastasizing uveal melanomas. Science 330, 1410-1413. doi: 10.1126/science.1194472
    • (2010) Science , vol.330 , pp. 1410-1413
    • Harbour, J.W.1    Onken, M.D.2    Roberson, E.D.3    Duan, S.4    Cao, L.5    Worley, L.A.6
  • 59
    • 0242361623 scopus 로고    scopus 로고
    • Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8
    • Henry, K. W., Wyce, A., Lo, W. S., Duggan, L. J., Emre, N. C., Kao, C. F., et al. (2003). Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8. Genes Dev. 17, 2648-2663. doi: 10.1101/gad.1144003
    • (2003) Genes Dev , vol.17 , pp. 2648-2663
    • Henry, K.W.1    Wyce, A.2    Lo, W.S.3    Duggan, L.J.4    Emre, N.C.5    Kao, C.F.6
  • 60
    • 84885106833 scopus 로고    scopus 로고
    • OTUB1 enhances TGFbeta signalling by inhibiting the ubiquitylation and degradation of active SMAD2/3
    • Herhaus, L., Al-Salihi, M., Macartney, T., Weidlich, S., and Sapkota, G. P. (2013). OTUB1 enhances TGFbeta signalling by inhibiting the ubiquitylation and degradation of active SMAD2/3. Nat. Commun. 4, 2519. doi: 10.1038/ncomms3519
    • (2013) Nat. Commun , vol.4 , pp. 2519
    • Herhaus, L.1    Al-Salihi, M.2    Macartney, T.3    Weidlich, S.4    Sapkota, G.P.5
  • 61
    • 84896520139 scopus 로고    scopus 로고
    • Ubiquitin code assembly and disassembly
    • Heride, C., Urbe, S., and Clague, M. J. (2014). Ubiquitin code assembly and disassembly. Curr. Biol. 24, R215-R220. doi: 10.1016/j.cub.2014.02.002
    • (2014) Curr. Biol , vol.24 , pp. R215-R220
    • Heride, C.1    Urbe, S.2    Clague, M.J.3
  • 62
    • 79954528832 scopus 로고    scopus 로고
    • RAP80-directed tuning of BRCA1 homologous recombination function at ionizing radiation-induced nuclear foci
    • Hu, Y., Scully, R., Sobhian, B., Xie, A., Shestakova, E., and Livingston, D. (2011). RAP80-directed tuning of BRCA1 homologous recombination function at ionizing radiation-induced nuclear foci. Genes Dev. 25, 685-700. doi: 10.1101/gad.2011011
    • (2011) Genes Dev , vol.25 , pp. 685-700
    • Hu, Y.1    Scully, R.2    Sobhian, B.3    Xie, A.4    Shestakova, E.5    Livingston, D.6
  • 63
    • 36249031962 scopus 로고    scopus 로고
    • RNF8 Transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly
    • Huen, M., Grant, R., Manke, I., Minn, K., Yu, X., Yaffe, M., et al. (2007). RNF8 Transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell 131, 901-914. doi: 10.1016/j.cell.2007.09.041
    • (2007) Cell , vol.131 , pp. 901-914
    • Huen, M.1    Grant, R.2    Manke, I.3    Minn, K.4    Yu, X.5    Yaffe, M.6
  • 64
    • 77957748289 scopus 로고    scopus 로고
    • BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair
    • Ismail, I. H., Andrin, C., Mcdonald, D., and Hendzel, M. J. (2010). BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair. J. Cell Biol. 191, 45-60. doi: 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
  • 65
    • 84905995383 scopus 로고    scopus 로고
    • Germline mutations in BAP1 impair its function in DNA double-strand break repair
    • Ismail, I. H., Davidson, R., Gagne, J. P., Xu, Z. Z., Poirier, G. G., and Hendzel, M. J. (2014). Germline mutations in BAP1 impair its function in DNA double-strand break repair. Cancer Res. 74, 4282-4294. doi: 10.1158/0008-5472.CAN-13-3109
    • (2014) Cancer Res , vol.74 , pp. 4282-4294
    • Ismail, I.H.1    Davidson, R.2    Gagne, J.P.3    Xu, Z.Z.4    Poirier, G.G.5    Hendzel, M.J.6
  • 66
    • 7244250309 scopus 로고    scopus 로고
    • Regulation of oxidative stress by ATM is required for self-renewal of haematopoietic stem cells
    • Ito, K., Hirao, A., Arai, F., Matsuoka, S., Takubo, K., Hamaguchi, I., et al. (2004). Regulation of oxidative stress by ATM is required for self-renewal of haematopoietic stem cells. Nature 431, 997-1002. doi: 10.1038/nature02989
    • (2004) Nature , vol.431 , pp. 997-1002
    • Ito, K.1    Hirao, A.2    Arai, F.3    Matsuoka, S.4    Takubo, K.5    Hamaguchi, I.6
  • 67
    • 70350504453 scopus 로고    scopus 로고
    • The DNA-damage response in human biology and disease
    • Jackson, S. P., and Bartek, J. (2009). The DNA-damage response in human biology and disease. Nature 461, 1071-1078. doi: 10.1038/nature08467
    • (2009) Nature , vol.461 , pp. 1071-1078
    • Jackson, S.P.1    Bartek, J.2
  • 68
    • 84876886904 scopus 로고    scopus 로고
    • Regulation of DNA damage responses by ubiquitin and SUMO
    • Jackson, S. P., and Durocher, D. (2013). Regulation of DNA damage responses by ubiquitin and SUMO. Mol. Cell 49, 795-807. doi: 10.1016/j.molcel.2013.01.017
    • (2013) Mol. Cell , vol.49 , pp. 795-807
    • Jackson, S.P.1    Durocher, D.2
  • 69
    • 84883458147 scopus 로고    scopus 로고
    • Deubiquitylating enzymes and DNA damage response pathways
    • Jacq, X., Kemp, M., Martin, N. M., and Jackson, S. P. (2013). Deubiquitylating enzymes and DNA damage response pathways. Cell Biochem. Biophys. 67, 25-43. doi: 10.1007/s12013-013-9635-3
    • (2013) Cell Biochem. Biophys , vol.67 , pp. 25-43
    • Jacq, X.1    Kemp, M.2    Martin, N.M.3    Jackson, S.P.4
  • 70
    • 15144342687 scopus 로고    scopus 로고
    • BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression
    • Jensen, D. E., Proctor, M., Marquis, S. T., Gardner, H. P., Ha, S. I., Chodosh, L. A., et al. (1998). BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and enhances BRCA1-mediated cell growth suppression. Oncogene 16, 1097-1112. doi: 10.1038/sj.onc.1201861
    • (1998) Oncogene , vol.16 , pp. 1097-1112
    • Jensen, D.E.1    Proctor, M.2    Marquis, S.T.3    Gardner, H.P.4    Ha, S.I.5    Chodosh, L.A.6
  • 71
    • 84255174663 scopus 로고    scopus 로고
    • Control of B cell development by the histone H2A deubiquitinase MYSM1
    • Jiang, X.-X., Nguyen, Q., Chou, Y., Wang, T., Nandakumar, V., Yates, P., et al. (2011). Control of B cell development by the histone H2A deubiquitinase MYSM1. Immunity 35, 883-896. doi: 10.1016/j.immuni.2011.11.010
    • (2011) Immunity , vol.35 , pp. 883-896
    • Jiang, X.-X.1    Nguyen, Q.2    Chou, Y.3    Wang, T.4    Nandakumar, V.5    Yates, P.6
  • 72
    • 35548986309 scopus 로고    scopus 로고
    • Regulation of cell cycle progression and gene expression by H2A deubiquitination
    • Joo, H., Zhai, L., Yang, C., Nie, S., Erdjument-Bromage, H., Tempst, P., et al. (2007). Regulation of cell cycle progression and gene expression by H2A deubiquitination. Nature 449, 1068-1072. doi: 10.1038/nature06256
    • (2007) Nature , vol.449 , pp. 1068-1072
    • Joo, H.1    Zhai, L.2    Yang, C.3    Nie, S.4    Erdjument-Bromage, H.5    Tempst, P.6
  • 73
    • 84856801739 scopus 로고    scopus 로고
    • OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function
    • Juang, Y. C., Landry, M. C., Sanches, M., Vittal, V., Leung, C. C., Ceccarelli, D. F., et al. (2012). OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function. Mol. Cell 45, 384-397. doi: 10.1016/j.molcel.2012.01.011
    • (2012) Mol. Cell , vol.45 , pp. 384-397
    • Juang, Y.C.1    Landry, M.C.2    Sanches, M.3    Vittal, V.4    Leung, C.C.5    Ceccarelli, D.F.6
  • 74
    • 84919451538 scopus 로고    scopus 로고
    • Requirement for PBAF in transcriptional repression and repair at DNA breaks in actively transcribed regions of chromatin
    • Kakarougkas, A., Ismail, A., Chambers, A. L., Riballo, E., Herbert, A. D., Kunzel, J., et al. (2014). Requirement for PBAF in transcriptional repression and repair at DNA breaks in actively transcribed regions of chromatin. Mol. Cell 55, 723-732. doi: 10.1016/j.molcel.2014.06.028
    • (2014) Mol. Cell , vol.55 , pp. 723-732
    • Kakarougkas, A.1    Ismail, A.2    Chambers, A.L.3    Riballo, E.4    Herbert, A.D.5    Kunzel, J.6
  • 75
    • 84890324730 scopus 로고    scopus 로고
    • Co-operation of BRCA1 and POH1 relieves the barriers posed by 53BP1 and RAP80 to resection
    • Kakarougkas, A., Ismail, A., Katsuki, Y., Freire, R., Shibata, A., and Jeggo, P. A. (2013). Co-operation of BRCA1 and POH1 relieves the barriers posed by 53BP1 and RAP80 to resection. Nucleic Acids Res. 41, 10298-10311. doi: 10.1093/nar/gkt802
    • (2013) Nucleic Acids Res , vol.41 , pp. 10298-10311
    • Kakarougkas, A.1    Ismail, A.2    Katsuki, Y.3    Freire, R.4    Shibata, A.5    Jeggo, P.A.6
  • 76
    • 84908356633 scopus 로고    scopus 로고
    • BRCA1 is a histone-H2A-specific ubiquitin ligase
    • Kalb, R., Mallery, D. L., Larkin, C., Huang, J. T., and Hiom, K. (2014). BRCA1 is a histone-H2A-specific ubiquitin ligase. Cell Rep. 8, 999-1005. doi: 10.1016/j.celrep.2014.07.025
    • (2014) Cell Rep , vol.8 , pp. 999-1005
    • Kalb, R.1    Mallery, D.L.2    Larkin, C.3    Huang, J.T.4    Hiom, K.5
  • 77
    • 84894067659 scopus 로고    scopus 로고
    • Fine-tuning of DNA damage-dependent ubiquitination by OTUB2 supports the DNA repair pathway choice
    • Kato, K., Nakajima, K., Ui, A., Muto-Terao, Y., Ogiwara, H., and Nakada, S. (2014). Fine-tuning of DNA damage-dependent ubiquitination by OTUB2 supports the DNA repair pathway choice. Mol. Cell 53, 617-630. doi: 10.1016/j.molcel.2014.01.030
    • (2014) Mol. Cell , vol.53 , pp. 617-630
    • Kato, K.1    Nakajima, K.2    Ui, A.3    Muto-Terao, Y.4    Ogiwara, H.5    Nakada, S.6
  • 78
    • 59649114341 scopus 로고    scopus 로고
    • Inactivation of murine Usp1 results in genomic instability and a Fanconi anemia phenotype
    • Kim, J. M., Parmar, K., Huang, M., Weinstock, D. M., Ruit, C. A., Kutok, J. L., et al. (2010). Inactivation of murine Usp1 results in genomic instability and a Fanconi anemia phenotype. Dev. Cell 16, 314-320. doi: 10.1016/j.devcel.2009.01.001
    • (2010) Dev. Cell , vol.16 , pp. 314-320
    • Kim, J.M.1    Parmar, K.2    Huang, M.3    Weinstock, D.M.4    Ruit, C.A.5    Kutok, J.L.6
  • 79
    • 84899880562 scopus 로고    scopus 로고
    • USP28 is recruited to sites of DNA damage by the tandem BRCT domains of 53BP1 but plays a minor role in double-strand break metabolism
    • Knobel, P. A., Belotserkovskaya, R., Galanty, Y., Schmidt, C. K., Jackson, S. P., and Stracker, T. H. (2014). USP28 is recruited to sites of DNA damage by the tandem BRCT domains of 53BP1 but plays a minor role in double-strand break metabolism. Mol. Cell. Biol. 34, 2062-2074. doi: 10.1128/MCB.00197-14
    • (2014) Mol. Cell. Biol , vol.34 , pp. 2062-2074
    • Knobel, P.A.1    Belotserkovskaya, R.2    Galanty, Y.3    Schmidt, C.K.4    Jackson, S.P.5    Stracker, T.H.6
  • 80
    • 36749084931 scopus 로고    scopus 로고
    • Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase
    • Kolas, N., Chapman, J., Nakada, S., Ylanko, J., Chahwan, R., Sweeney, F., et al. (2007). Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase. Science 318, 1637-1640. doi: 10.1126/science.1150034
    • (2007) Science , vol.318 , pp. 1637-1640
    • Kolas, N.1    Chapman, J.2    Nakada, S.3    Ylanko, J.4    Chahwan, R.5    Sweeney, F.6
  • 81
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: structure and function of the deubiquitinases
    • Komander, D., Clague, M. J., and Urb�, S. (2009). Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol. 10, 550-563. doi: 10.1038/nrm2731
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urb�, S.3
  • 82
    • 84861877407 scopus 로고    scopus 로고
    • The ubiquitin code
    • Komander, D., and Rape, M. (2012). The ubiquitin code. Annu. Rev. Biochem. 81, 203-229. doi: 10.1146/annurev-biochem-060310-170328
    • (2012) Annu. Rev. Biochem , vol.81 , pp. 203-229
    • Komander, D.1    Rape, M.2
  • 83
    • 84864222562 scopus 로고    scopus 로고
    • Atypical ubiquitylation-the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
    • Kulathu, Y., and Komander, D. (2012). Atypical ubiquitylation-the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Nat. Rev. Mol. Cell Biol. 13, 508-523. doi: 10.1038/nrm3394
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 508-523
    • Kulathu, Y.1    Komander, D.2
  • 84
    • 84906552235 scopus 로고    scopus 로고
    • Tight regulation of ubiquitin-mediated DNA damage response by USP3 preserves the functional integrity of hematopoietic stem cells
    • Lancini, C., Van Den Berk, P. C., Vissers, J. H., Gargiulo, G., Song, J. Y., Hulsman, D., et al. (2014). Tight regulation of ubiquitin-mediated DNA damage response by USP3 preserves the functional integrity of hematopoietic stem cells. J. Exp. Med. 211, 1759-1777. doi: 10.1084/jem.20131436
    • (2014) J. Exp. Med , vol.211 , pp. 1759-1777
    • Lancini, C.1    Van Den Berk, P.C.2    Vissers, J.H.3    Gargiulo, G.4    Song, J.Y.5    Hulsman, D.6
  • 85
    • 0037673984 scopus 로고    scopus 로고
    • Bmi-1 determines the proliferative capacity of normal and leukaemic stem cells
    • Lessard, J., and Sauvageau, G. (2003). Bmi-1 determines the proliferative capacity of normal and leukaemic stem cells. Nature 423, 255-260. doi: 10.1038/nature01572
    • (2003) Nature , vol.423 , pp. 255-260
    • Lessard, J.1    Sauvageau, G.2
  • 86
    • 84897449829 scopus 로고    scopus 로고
    • Nucleosome acidic patch promotes RNF168-and RING1B/BMI1-dependent H2AX and H2A ubiquitination and DNA damage signaling
    • Leung, J. W., Agarwal, P., Canny, M. D., Gong, F., Robison, A. D., Finkelstein, I. J., et al. (2014). Nucleosome acidic patch promotes RNF168-and RING1B/BMI1-dependent H2AX and H2A ubiquitination and DNA damage signaling. PLoS Genet. 10:e1004178. doi: 10.1371/journal.pgen.1004178
    • (2014) PLoS Genet , vol.10
    • Leung, J.W.1    Agarwal, P.2    Canny, M.D.3    Gong, F.4    Robison, A.D.5    Finkelstein, I.J.6
  • 87
    • 77952318450 scopus 로고    scopus 로고
    • Rnf8 deficiency impairs class switch recombination, spermatogenesis, and genomic integrity and predisposes for cancer
    • Li, L., Halaby, M., Hakem, A., Cardoso, R., El Ghamrasni, S., Harding, S., et al. (2010). Rnf8 deficiency impairs class switch recombination, spermatogenesis, and genomic integrity and predisposes for cancer. J. Exp. Med. 207, 983-997. doi: 10.1084/jem.20092437
    • (2010) J. Exp. Med , vol.207 , pp. 983-997
    • Li, L.1    Halaby, M.2    Hakem, A.3    Cardoso, R.4    El Ghamrasni, S.5    Harding, S.6
  • 88
    • 84898669669 scopus 로고    scopus 로고
    • Novel skin phenotypes revealed by a genome-wide mouse reverse genetic screen
    • Liakath-Ali, K., Vancollie, V. E., Heath, E., Smedley, D. P., Estabel, J., Sunter, D., et al. (2014). Novel skin phenotypes revealed by a genome-wide mouse reverse genetic screen. Nat. Commun. 5, 3540. doi: 10.1038/ncomms4540
    • (2014) Nat. Commun , vol.5 , pp. 3540
    • Liakath-Ali, K.1    Vancollie, V.E.2    Heath, E.3    Smedley, D.P.4    Estabel, J.5    Sunter, D.6
  • 89
    • 84873631924 scopus 로고    scopus 로고
    • CHFR is important for the first wave of ubiquitination at DNA damage sites
    • Liu, C., Wu, J., Paudyal, S. C., You, Z., and Yu, X. (2013). CHFR is important for the first wave of ubiquitination at DNA damage sites. Nucleic Acids Res. 41, 1698-1710. doi: 10.1093/nar/gks1278
    • (2013) Nucleic Acids Res , vol.41 , pp. 1698-1710
    • Liu, C.1    Wu, J.2    Paudyal, S.C.3    You, Z.4    Yu, X.5
  • 90
    • 67349156082 scopus 로고    scopus 로고
    • Bmi1 regulates mitochondrial function and the DNA damage response pathway
    • Liu, J., Cao, L., Chen, J., Song, S., Lee, I. H., Quijano, C., et al. (2009). Bmi1 regulates mitochondrial function and the DNA damage response pathway. Nature 459, 387-392. doi: 10.1038/nature08040
    • (2009) Nature , vol.459 , pp. 387-392
    • Liu, J.1    Cao, L.2    Chen, J.3    Song, S.4    Lee, I.H.5    Quijano, C.6
  • 91
    • 80052606865 scopus 로고    scopus 로고
    • Defective hematopoietic stem cell and lymphoid progenitor development in the Ts65Dn mouse model of Down syndrome: potential role of oxidative stress
    • Lorenzo, L. P., Chen, H., Shatynski, K. E., Clark, S., Yuan, R., Harrison, D. E., et al. (2011). Defective hematopoietic stem cell and lymphoid progenitor development in the Ts65Dn mouse model of Down syndrome: potential role of oxidative stress. Antioxid. Redox Signal. 15, 2083-2094. doi: 10.1089/ars.2010.3798
    • (2011) Antioxid. Redox Signal , vol.15 , pp. 2083-2094
    • Lorenzo, L.P.1    Chen, H.2    Shatynski, K.E.3    Clark, S.4    Yuan, R.5    Harrison, D.E.6
  • 92
    • 79956128376 scopus 로고    scopus 로고
    • The ubiquitin-specific protease USP34 regulates axin stability and Wnt/beta-catenin signaling
    • Lui, T. T., Lacroix, C., Ahmed, S. M., Goldenberg, S. J., Leach, C. A., Daulat, A. M., et al. (2011). The ubiquitin-specific protease USP34 regulates axin stability and Wnt/beta-catenin signaling. Mol. Cell. Biol. 31, 2053-2065. doi: 10.1128/MCB.01094-10
    • (2011) Mol. Cell. Biol , vol.31 , pp. 2053-2065
    • Lui, T.T.1    Lacroix, C.2    Ahmed, S.M.3    Goldenberg, S.J.4    Leach, C.A.5    Daulat, A.M.6
  • 93
    • 80053555789 scopus 로고    scopus 로고
    • More than just a focus: the chromatin response to DNA damage and its role in genome integrity maintenance
    • Lukas, J., Lukas, C., and Bartek, J. (2011). More than just a focus: the chromatin response to DNA damage and its role in genome integrity maintenance. Nat. Cell Biol. 13, 1161-1169. doi: 10.1038/ncb2344
    • (2011) Nat. Cell Biol , vol.13 , pp. 1161-1169
    • Lukas, J.1    Lukas, C.2    Bartek, J.3
  • 94
    • 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. (2007). RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 131, 887-900. doi: 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
  • 95
    • 84859895529 scopus 로고    scopus 로고
    • RNF8-and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites
    • Mallette, F. A., Mattiroli, F., Cui, G., Young, L. C., Hendzel, M. J., Mer, G., et al. (2012). RNF8-and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites. EMBO J. 31, 1865-1878. doi: 10.1038/emboj.2012.47
    • (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
  • 96
    • 34249947699 scopus 로고    scopus 로고
    • ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage
    • Matsuoka, S., Ballif, B. A., Smogorzewska, A., Mcdonald, E. R. III, Hurov, K. E., Luo, J., et al. (2007). ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science 316, 1160-1166. doi: 10.1126/science.1140321
    • (2007) Science , vol.316 , pp. 1160-1166
    • Matsuoka, S.1    Ballif, B.A.2    Smogorzewska, A.3    Mcdonald, E.R.4    Hurov, K.E.5    Luo, J.6
  • 97
    • 84866388311 scopus 로고    scopus 로고
    • RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage signaling
    • Mattiroli, F., Vissers, J. H. A., Van Dijk, W. J., Ikpa, P., Citterio, E., Vermeulen, W., et al. (2012). RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage signaling. Cell 150, 1182-1195. doi: 10.1016/j.cell.2012.08.005
    • (2012) Cell , vol.150 , pp. 1182-1195
    • Mattiroli, F.1    Vissers, J.H.A.2    Van Dijk, W.J.3    Ikpa, P.4    Citterio, E.5    Vermeulen, W.6
  • 98
    • 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. (2011). The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA double-strand breaks. Nat. Cell Biol. 13, 1376-1382. doi: 10.1038/ncb2367
    • (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
  • 99
    • 84878832998 scopus 로고    scopus 로고
    • OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis
    • Mevissen, T. E., Hospenthal, M. K., Geurink, P. P., Elliott, P. R., Akutsu, M., Arnaudo, N., et al. (2013). OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis. Cell 154, 169-184. doi: 10.1016/j.cell.2013.05.046
    • (2013) Cell , vol.154 , pp. 169-184
    • Mevissen, T.E.1    Hospenthal, M.K.2    Geurink, P.P.3    Elliott, P.R.4    Akutsu, M.5    Arnaudo, N.6
  • 100
    • 1942517849 scopus 로고    scopus 로고
    • BRCA1: BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair
    • Morris, J. R., and Solomon, E. (2004). BRCA1: BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair. Hum. Mol. Genet. 13, 807-817. doi: 10.1093/hmg/ddh095
    • (2004) Hum. Mol. Genet , vol.13 , pp. 807-817
    • Morris, J.R.1    Solomon, E.2
  • 101
    • 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., and Mailand, N. (2013). 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. doi: 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
  • 102
    • 79951974992 scopus 로고    scopus 로고
    • Requirement of ATM-dependent monoubiquitylation of histone H2B for timely repair of DNA double-strand breaks
    • Moyal, L., Lerenthal, Y., Gana-Weisz, M., Mass, G., So, S., Wang, S.-Y., et al. (2011). Requirement of ATM-dependent monoubiquitylation of histone H2B for timely repair of DNA double-strand breaks. Mol. Cell 41, 529-542. doi: 10.1016/j.molcel.2011.02.015
    • (2011) Mol. Cell , vol.41 , pp. 529-542
    • Moyal, L.1    Lerenthal, Y.2    Gana-Weisz, M.3    Mass, G.4    So, S.5    Wang, S.-Y.6
  • 103
    • 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.-I., Juang, Y.-C., et al. (2010). Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1. Nature 466, 941-946. doi: 10.1038/nature09297
    • (2010) Nature , vol.466 , pp. 941-946
    • Nakada, S.1    Tai, I.2    Panier, S.3    Al-Hakim, A.4    Iemura, S.-I.5    Juang, Y.-C.6
  • 104
    • 79951971464 scopus 로고    scopus 로고
    • Regulation of homologous recombination by RNF20-dependent H2B ubiquitination
    • Nakamura, K., Kato, A., Kobayashi, J., Yanagihara, H., Sakamoto, S., Oliveira, D. V. N. P., et al. (2011). Regulation of homologous recombination by RNF20-dependent H2B ubiquitination. Mol. Cell 41, 515-528. doi: 10.1016/j.molcel.2011.02.002
    • (2011) Mol. Cell , vol.41 , pp. 515-528
    • Nakamura, K.1    Kato, A.2    Kobayashi, J.3    Yanagihara, H.4    Sakamoto, S.5    Oliveira, D.V.N.P.6
  • 105
    • 84885335074 scopus 로고    scopus 로고
    • Epigenetic control of natural killer cell maturation by histone H2A deubiquitinase, MYSM1
    • Nandakumar, V., Chou, Y., Zang, L., Huang, X. F., and Chen, S. Y. (2013). Epigenetic control of natural killer cell maturation by histone H2A deubiquitinase, MYSM1. Proc. Natl. Acad. Sci. U.S.A. 110, E3927-E3936. doi: 10.1073/pnas.1308888110
    • (2013) Proc. Natl. Acad. Sci. U.S.A , vol.110 , pp. E3927-E3936
    • Nandakumar, V.1    Chou, Y.2    Zang, L.3    Huang, X.F.4    Chen, S.Y.5
  • 106
    • 36049036216 scopus 로고    scopus 로고
    • Human USP3 is a chromatin modifier required for S phase progression and genome stability
    • Nicassio, F., Corrado, N., Vissers, J. H., Areces, L. B., Bergink, S., Marteijn, J. A., et al. (2007). Human USP3 is a chromatin modifier required for S phase progression and genome stability. Curr. Biol. 17, 1972-1977. doi: 10.1016/j.cub.2007.10.034
    • (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
  • 107
    • 39149133141 scopus 로고    scopus 로고
    • DNA repair is crucial for maintaining hematopoietic stem cell function
    • Niedernhofer, L. J. (2008). DNA repair is crucial for maintaining hematopoietic stem cell function. DNA Repair (Amst) 7, 523-529. doi: 10.1016/j.dnarep.2007.11.012
    • (2008) DNA Repair (Amst) , vol.7 , pp. 523-529
    • Niedernhofer, L.J.1
  • 108
    • 28344456279 scopus 로고    scopus 로고
    • A genomic and functional inventory of deubiquitinating enzymes
    • Nijman, S., Luna-Vargas, M., Velds, A., Brummelkamp, T., Dirac, A., Sixma, T., et al. (2005). A genomic and functional inventory of deubiquitinating enzymes. Cell 123, 773-786. doi: 10.1016/j.cell.2005.11.007
    • (2005) Cell , vol.123 , pp. 773-786
    • Nijman, S.1    Luna-Vargas, M.2    Velds, A.3    Brummelkamp, T.4    Dirac, A.5    Sixma, T.6
  • 109
    • 84863393730 scopus 로고    scopus 로고
    • The critical role of histone H2A-deubiquitinase Mysm1 in hematopoiesis and lymphocyte differentiation
    • Nijnik, A., Clare, S., Hale, C., Raisen, C., Mcintyre, R. E., Yusa, K., et al. (2012). The critical role of histone H2A-deubiquitinase Mysm1 in hematopoiesis and lymphocyte differentiation. Blood 119, 1370-1379. doi: 10.1182/blood-2011-05-352666
    • (2012) Blood , vol.119 , pp. 1370-1379
    • Nijnik, A.1    Clare, S.2    Hale, C.3    Raisen, C.4    Mcintyre, R.E.5    Yusa, K.6
  • 110
    • 34250001450 scopus 로고    scopus 로고
    • DNA repair is limiting for haematopoietic stem cells during ageing
    • Nijnik, A., Woodbine, L., Marchetti, C., Dawson, S., Lambe, T., Liu, C., et al. (2007). DNA repair is limiting for haematopoietic stem cells during ageing. Nature 447, 686-690. doi: 10.1038/nature05875
    • (2007) Nature , vol.447 , pp. 686-690
    • Nijnik, A.1    Woodbine, L.2    Marchetti, C.3    Dawson, S.4    Lambe, T.5    Liu, C.6
  • 111
    • 84922010371 scopus 로고    scopus 로고
    • Systematic characterization of deubiquitylating enzymes for roles in maintaining genome integrity
    • Nishi, R., Wijnhoven, P., Le Sage, C., Tjeertes, J., Galanty, Y., Forment, J. V., et al. (2014). Systematic characterization of deubiquitylating enzymes for roles in maintaining genome integrity. Nat. Cell Biol. 16, 1011-1018. doi: 10.1038/ncb3028
    • (2014) Nat. Cell Biol , vol.16 , pp. 1011-1018
    • Nishi, R.1    Wijnhoven, P.2    Le Sage, C.3    Tjeertes, J.4    Galanty, Y.5    Forment, J.V.6
  • 112
    • 58249095937 scopus 로고    scopus 로고
    • BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity
    • Nishikawa, H., Wu, W., Koike, A., Kojima, R., Gomi, H., Fukuda, M., et al. (2009). BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity. Cancer Res. 69, 111-119. doi: 10.1158/0008-5472.CAN-08-3355
    • (2009) Cancer Res , vol.69 , pp. 111-119
    • Nishikawa, H.1    Wu, W.2    Koike, A.3    Kojima, R.4    Gomi, H.5    Fukuda, M.6
  • 113
  • 114
    • 84898052474 scopus 로고    scopus 로고
    • Mitosis inhibits DNA double-strand break repair to guard against telomere fusions
    • Orthwein, A., Fradet-Turcotte, A., Noordermeer, S. M., Canny, M. D., Brun, C. M., Strecker, J., et al. (2014). Mitosis inhibits DNA double-strand break repair to guard against telomere fusions. Science 344, 189-193. doi: 10.1126/science.1248024
    • (2014) Science , vol.344 , pp. 189-193
    • Orthwein, A.1    Fradet-Turcotte, A.2    Noordermeer, S.M.3    Canny, M.D.4    Brun, C.M.5    Strecker, J.6
  • 115
    • 80051494784 scopus 로고    scopus 로고
    • Monoubiquitination of H2AX regulates DNA damage response signaling
    • Pan, M.-R., Peng, G., Hung, W.-C., and Lin, S.-Y. (2011). Monoubiquitination of H2AX regulates DNA damage response signaling. J. Biol. Chem. 286, 28599-28607. doi: 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
  • 116
    • 84891014338 scopus 로고    scopus 로고
    • Double-strand break repair: 53BP1 comes into focus
    • Panier, S., and Boulton, S. J. (2014). Double-strand break repair: 53BP1 comes into focus. Nat. Rev. Mol. Cell Biol. 15, 7-18. doi: 10.1038/nrm3719
    • (2014) Nat. Rev. Mol. Cell Biol , vol.15 , pp. 7-18
    • Panier, S.1    Boulton, S.J.2
  • 117
    • 84886429265 scopus 로고    scopus 로고
    • Push back to respond better: regulatory inhibition of the DNA double-strand break response
    • Panier, S., and Durocher, D. (2013). Push back to respond better: regulatory inhibition of the DNA double-strand break response. Nat. Rev. Mol. Cell Biol. 14, 661-672. doi: 10.1038/nrm3659
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 661-672
    • Panier, S.1    Durocher, D.2
  • 118
    • 84864919890 scopus 로고    scopus 로고
    • Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks
    • Panier, S., Ichijima, Y., Fradet-Turcotte, A., Leung, C. C., Kaustov, L., Arrowsmith, C. H., et al. (2012). Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks. Mol. Cell 47, 383-395. doi: 10.1016/j.molcel.2012.05.045
    • (2012) Mol. Cell , vol.47 , pp. 383-395
    • Panier, S.1    Ichijima, Y.2    Fradet-Turcotte, A.3    Leung, C.C.4    Kaustov, L.5    Arrowsmith, C.H.6
  • 119
    • 0038349957 scopus 로고    scopus 로고
    • Bmi-1 is required for maintenance of adult self-renewing haematopoietic stem cells
    • Park, I. K., Qian, D., Kiel, M., Becker, M. W., Pihalja, M., Weissman, I. L., et al. (2003). Bmi-1 is required for maintenance of adult self-renewing haematopoietic stem cells. Nature 423, 302-305. doi: 10.1038/nature01587
    • (2003) Nature , vol.423 , pp. 302-305
    • Park, I.K.1    Qian, D.2    Kiel, M.3    Becker, M.W.4    Pihalja, M.5    Weissman, I.L.6
  • 120
    • 77954821842 scopus 로고    scopus 로고
    • Hematopoietic stem cell defects in mice with deficiency of Fancd2 or Usp1
    • Parmar, K., Kim, J., Sykes, S., Shimamura, A., Stuckert, P., Zhu, K., et al. (2010). Hematopoietic stem cell defects in mice with deficiency of Fancd2 or Usp1. Stem Cells 28, 1186-1195. doi: 10.1002/stem.437
    • (2010) Stem Cells , vol.28 , pp. 1186-1195
    • Parmar, K.1    Kim, J.2    Sykes, S.3    Shimamura, A.4    Stuckert, P.5    Zhu, K.6
  • 122
    • 77950517895 scopus 로고    scopus 로고
    • Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A
    • Pereg, Y., Liu, B. Y., O'rourke, K. M., Sagolla, M., Dey, A., Komuves, L., et al. (2010). Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A. Nat. Cell Biol. 12, 400-406. doi: 10.1038/ncb2041
    • (2010) Nat. Cell Biol , vol.12 , pp. 400-406
    • Pereg, Y.1    Liu, B.Y.2    O'rourke, K.M.3    Sagolla, M.4    Dey, A.5    Komuves, L.6
  • 123
    • 80052491304 scopus 로고    scopus 로고
    • DNA-damage response and repair activities at uncapped telomeres depend on RNF8
    • Peuscher, M. H., and Jacobs, J. J. (2011). DNA-damage response and repair activities at uncapped telomeres depend on RNF8. Nat. Cell Biol. 13, 1139-1145. doi: 10.1038/ncb2326
    • (2011) Nat. Cell Biol , vol.13 , pp. 1139-1145
    • Peuscher, M.H.1    Jacobs, J.J.2
  • 124
    • 67649404816 scopus 로고    scopus 로고
    • RNF168, a new RING finger, MIU-containing protein that modifies chromatin by ubiquitination of histones H2A and H2AX
    • Pinato, S., Scandiuzzi, C., Arnaudo, N., Citterio, E., Gaudino, G., and Penengo, L. (2009). RNF168, a new RING finger, MIU-containing protein that modifies chromatin by ubiquitination of histones H2A and H2AX. BMC Mol. Biol. 10:55. doi: 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
  • 125
    • 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., and Mailand, N. (2012). Human RNF169 is a negative regulator of the ubiquitin-dependent response to DNA double-strand breaks. J. Cell Biol. 197, 189-199. doi: 10.1083/jcb.201109100
    • (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
  • 126
    • 34250007142 scopus 로고    scopus 로고
    • Deficiencies in DNA damage repair limit the function of haematopoietic stem cells with age
    • Rossi, D. J., Bryder, D., Seita, J., Nussenzweig, A., Hoeijmakers, J., and Weissman, I. L. (2007). Deficiencies in DNA damage repair limit the function of haematopoietic stem cells with age. Nature 447, 725-729. doi: 10.1038/nature05862
    • (2007) Nature , vol.447 , pp. 725-729
    • Rossi, D.J.1    Bryder, D.2    Seita, J.3    Nussenzweig, A.4    Hoeijmakers, J.5    Weissman, I.L.6
  • 127
    • 79952338609 scopus 로고    scopus 로고
    • Accumulation of DNA damage in hematopoietic stem and progenitor cells during human aging
    • R�be, C., Fricke, A., Widmann, T., F�rst, T., Madry, H., Pfreundschuh, M., et al. (2011). Accumulation of DNA damage in hematopoietic stem and progenitor cells during human aging. PLoS ONE 6:e17487. doi: 10.1371/journal.pone.0017487
    • (2011) PLoS ONE , vol.6
    • R�be, C.1    Fricke, A.2    Widmann, T.3    F�rst, T.4    Madry, H.5    Pfreundschuh, M.6
  • 128
    • 84937518319 scopus 로고    scopus 로고
    • Layers of DUB regulation
    • Sahtoe, D. D., and Sixma, T. K. (2015). Layers of DUB regulation. Trends Biochem. Sci. 40, 456-467. doi: 10.1016/j.tibs.2015.05.002
    • (2015) Trends Biochem. Sci , vol.40 , pp. 456-467
    • Sahtoe, D.D.1    Sixma, T.K.2
  • 129
    • 77952294873 scopus 로고    scopus 로고
    • Class switching and meiotic defects in mice lacking the E3 ubiquitin ligase RNF8
    • Santos, M., Huen, M., Jankovic, M., Chen, H., Lopez-Contreras, A., Klein, I., et al. (2010). Class switching and meiotic defects in mice lacking the E3 ubiquitin ligase RNF8. J. Exp. Med. 207, 973-981. doi: 10.1084/jem.20092308
    • (2010) J. Exp. Med , vol.207 , pp. 973-981
    • Santos, M.1    Huen, M.2    Jankovic, M.3    Chen, H.4    Lopez-Contreras, A.5    Klein, I.6
  • 130
  • 131
    • 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., and Greenberg, R. A. (2010). ATM-dependent chromatin changes silence transcription in cis to DNA double-strand breaks. Cell 141, 970-981. doi: 10.1016/j.cell.2010.04.038
    • (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
  • 132
    • 62549140202 scopus 로고    scopus 로고
    • The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks
    • Shao, G., Lilli, D. R., Patterson-Fortin, J., Coleman, K. A., Morrissey, D. E., and Greenberg, R. A. (2009). The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks. Proc. Natl. Acad. Sci. U.S.A. 106, 3166-3171. doi: 10.1073/pnas.0807485106
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 3166-3171
    • Shao, G.1    Lilli, D.R.2    Patterson-Fortin, J.3    Coleman, K.A.4    Morrissey, D.E.5    Greenberg, R.A.6
  • 133
    • 84892562030 scopus 로고    scopus 로고
    • USP3 counteracts RNF168 via deubiquitinating H2A and gammaH2AX at lysine 13 and 15
    • Sharma, N., Zhu, Q., Wani, G., He, J., Wang, Q. E., and Wani, A. A. (2014). USP3 counteracts RNF168 via deubiquitinating H2A and gammaH2AX at lysine 13 and 15. Cell Cycle 13, 106-114. doi: 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
  • 134
    • 80052779612 scopus 로고    scopus 로고
    • RNF20-RNF40: a ubiquitin-driven link between gene expression and the DNA damage response
    • Shiloh, Y., Shema, E., Moyal, L., and Oren, M. (2011). RNF20-RNF40: a ubiquitin-driven link between gene expression and the DNA damage response. FEBS Lett. 585, 2795-2802. doi: 10.1016/j.febslet.2011.07.034
    • (2011) FEBS Lett , vol.585 , pp. 2795-2802
    • Shiloh, Y.1    Shema, E.2    Moyal, L.3    Oren, M.4
  • 135
    • 0033578890 scopus 로고    scopus 로고
    • Characterization and chromosomal localization of USP3, a novel human ubiquitin-specific protease
    • Sloper-Mould, K. E., Eyre, H. J., Wang, X.-W., Sutherland, G. R., and Baker, R. T. (1999). Characterization and chromosomal localization of USP3, a novel human ubiquitin-specific protease. J. Biol. Chem. 274, 26878-26884. doi: 10.1074/jbc.274.38.26878
    • (1999) J. Biol. Chem , vol.274 , pp. 26878-26884
    • Sloper-Mould, K.E.1    Eyre, H.J.2    Wang, X.-W.3    Sutherland, G.R.4    Baker, R.T.5
  • 136
    • 84876328368 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation links the chromatin remodeler SMARCA5/SNF2H to RNF168-dependent DNA damage signaling
    • Smeenk, G., Wiegant, W. W., Marteijn, J. A., Luijsterburg, M. S., Sroczynski, N., Costelloe, T., et al. (2013). Poly(ADP-ribosyl)ation links the chromatin remodeler SMARCA5/SNF2H to RNF168-dependent DNA damage signaling. J. Cell Sci. 126, 889-903. doi: 10.1242/jcs.109413
    • (2013) J. Cell Sci , vol.126 , pp. 889-903
    • Smeenk, G.1    Wiegant, W.W.2    Marteijn, J.A.3    Luijsterburg, M.S.4    Sroczynski, N.5    Costelloe, T.6
  • 137
    • 34249949779 scopus 로고    scopus 로고
    • RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites
    • Sobhian, B., Shao, G., Lilli, D. R., Culhane, A. C., Moreau, L. A., Xia, B., et al. (2007). RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites. Science 316, 1198-1202. doi: 10.1126/science.1139516
    • (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
  • 138
    • 77954523079 scopus 로고    scopus 로고
    • The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control reversible ubiquitination at the spliceosome
    • Song, E. J., Werner, S. L., Neubauer, J., Stegmeier, F., Aspden, J., Rio, D., et al. (2010). The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control reversible ubiquitination at the spliceosome. Genes Dev. 24, 1434-1447. doi: 10.1101/gad.1925010
    • (2010) Genes Dev , vol.24 , pp. 1434-1447
    • Song, E.J.1    Werner, S.L.2    Neubauer, J.3    Stegmeier, F.4    Aspden, J.5    Rio, D.6
  • 139
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E., Bennett, E. J., Gygi, S. P., and Harper, J. (2009). Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389-403. doi: 10.1016/j.cell.2009.04.042
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.4
  • 140
    • 33750379420 scopus 로고    scopus 로고
    • Polycomb silencers control cell fate, development and cancer
    • Sparmann, A., and van Lohuizen, M. (2006). Polycomb silencers control cell fate, development and cancer. Nat. Rev. Cancer 6, 846-856. doi: 10.1038/nrc1991
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 846-856
    • Sparmann, A.1    van Lohuizen, M.2
  • 141
    • 34247376926 scopus 로고    scopus 로고
    • Anaphase initiation is regulated by antagonistic ubiquitination and deubiquitination activities
    • Stegmeier, F., Rape, M., Draviam, V., Nalepa, G., Sowa, M., Ang, X., et al. (2007). Anaphase initiation is regulated by antagonistic ubiquitination and deubiquitination activities. Nature 446, 876-881. doi: 10.1038/nature05694
    • (2007) Nature , vol.446 , pp. 876-881
    • Stegmeier, F.1    Rape, M.2    Draviam, V.3    Nalepa, G.4    Sowa, M.5    Ang, X.6
  • 142
    • 59049103900 scopus 로고    scopus 로고
    • The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage
    • Stewart, G. S., Panier, S., Townsend, K., Al-Hakim, A. K., Kolas, N. K., Miller, E. S., et al. (2009). The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell 136, 420-434. doi: 10.1016/j.cell.2008.12.042
    • (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
  • 143
    • 84856415004 scopus 로고    scopus 로고
    • Positive regulation of p53 stability and activity by the deubiquitinating enzyme Otubain 1
    • Sun, X. X., Challagundla, K. B., and Dai, M. S. (2012). Positive regulation of p53 stability and activity by the deubiquitinating enzyme Otubain 1. EMBO J. 31, 576-592. doi: 10.1038/emboj.2011.434
    • (2012) EMBO J , vol.31 , pp. 576-592
    • Sun, X.X.1    Challagundla, K.B.2    Dai, M.S.3
  • 144
    • 84885940995 scopus 로고    scopus 로고
    • The ubiquitin specific protease USP34 promotes ubiquitin signaling at DNA double-strand breaks
    • Sy, S. M., Jiang, J., O, Ws., Deng, Y., and Huen, M. S. (2013). The ubiquitin specific protease USP34 promotes ubiquitin signaling at DNA double-strand breaks. Nucleic Acids Res. 41, 8572-8580. doi: 10.1093/nar/gkt622
    • (2013) Nucleic Acids Res , vol.41 , pp. 8572-8580
    • Sy, S.M.1    Jiang, J.2    Ws, O.3    Deng, Y.4    Huen, M.S.5
  • 145
    • 84866894408 scopus 로고    scopus 로고
    • Comprehensive genomic characterization of squamous cell lung cancers
    • TCGA. (2012). Comprehensive genomic characterization of squamous cell lung cancers. Nature 489, 519-525. doi: 10.1038/nature11404
    • (2012) Nature , vol.489 , pp. 519-525
  • 146
    • 74549158762 scopus 로고    scopus 로고
    • Genome-wide loss-of-function analysis of deubiquitylating enzymes for zebrafish development
    • Tse, W. K., Eisenhaber, B., Ho, S. H., Ng, Q., Eisenhaber, F., and Jiang, Y.-J. (2009). Genome-wide loss-of-function analysis of deubiquitylating enzymes for zebrafish development. BMC Genomics 10:637. doi: 10.1186/1471-2164-10-637
    • (2009) BMC Genomics , vol.10 , pp. 637
    • Tse, W.K.1    Eisenhaber, B.2    Ho, S.H.3    Ng, Q.4    Eisenhaber, F.5    Jiang, Y.-J.6
  • 147
    • 84865289865 scopus 로고    scopus 로고
    • Systematic analysis of the physiological importance of deubiquitinating enzymes
    • Tsou, W. L., Sheedlo, M. J., Morrow, M. E., Blount, J. R., Mcgregor, K. M., Das, C., et al. (2012). Systematic analysis of the physiological importance of deubiquitinating enzymes. PLoS ONE 7:e43112. doi: 10.1371/journal.pone.0043112
    • (2012) PLoS ONE , vol.7
    • Tsou, W.L.1    Sheedlo, M.J.2    Morrow, M.E.3    Blount, J.R.4    Mcgregor, K.M.5    Das, C.6
  • 148
    • 84928907539 scopus 로고    scopus 로고
    • Transcriptional elongation factor ENL phosphorylated by ATM recruits polycomb and switches off transcription for DSB repair
    • Ui, A., Nagaura, Y., and Yasui, A. (2015). Transcriptional elongation factor ENL phosphorylated by ATM recruits polycomb and switches off transcription for DSB repair. Mol. Cell 58, 468-482. doi: 10.1016/j.molcel.2015.03.023
    • (2015) Mol. Cell , vol.58 , pp. 468-482
    • Ui, A.1    Nagaura, Y.2    Yasui, A.3
  • 149
    • 84858147489 scopus 로고    scopus 로고
    • Ubiquitin and SUMO in DNA repair at a glance
    • Ulrich, H. D. (2012). Ubiquitin and SUMO in DNA repair at a glance. J. Cell Sci. 125, 249-254. doi: 10.1242/jcs.091801
    • (2012) J. Cell Sci , vol.125 , pp. 249-254
    • Ulrich, H.D.1
  • 150
    • 84887195033 scopus 로고    scopus 로고
    • High Dub3 expression in mouse ESCs couples the G1/S checkpoint to pluripotency
    • van der Laan, S., Tsanov, N., Crozet, C., and Maiorano, D. (2013). High Dub3 expression in mouse ESCs couples the G1/S checkpoint to pluripotency. Mol. Cell 52, 366-379. doi: 10.1016/j.molcel.2013.10.003
    • (2013) Mol. Cell , vol.52 , pp. 366-379
    • van der Laan, S.1    Tsanov, N.2    Crozet, C.3    Maiorano, D.4
  • 151
    • 84869102655 scopus 로고    scopus 로고
    • The emerging role of Polycomb repressors in the response to DNA damage
    • Vissers, J. H., Van Lohuizen, M., and Citterio, E. (2012). The emerging role of Polycomb repressors in the response to DNA damage. J. Cell Sci. 125, 3939-3948. doi: 10.1242/jcs.107375
    • (2012) J. Cell Sci , vol.125 , pp. 3939-3948
    • Vissers, J.H.1    Van Lohuizen, M.2    Citterio, E.3
  • 152
    • 84928569602 scopus 로고    scopus 로고
    • Exit from dormancy provokes DNA-damage-induced attrition in haematopoietic stem cells
    • Walter, D., Lier, A., Geiselhart, A., Thalheimer, F. B., Huntscha, S., Sobotta, M. C., et al. (2015). Exit from dormancy provokes DNA-damage-induced attrition in haematopoietic stem cells. Nature 520, 549-552. doi: 10.1038/nature14131
    • (2015) Nature , vol.520 , pp. 549-552
    • Walter, D.1    Lier, A.2    Geiselhart, A.3    Thalheimer, F.B.4    Huntscha, S.5    Sobotta, M.C.6
  • 153
    • 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., and Elledge, S. (2007). 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. 104, 20759-20763. doi: 10.1073/pnas.0710061104
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 20759-20763
    • Wang, B.1    Elledge, S.2
  • 154
    • 34249946686 scopus 로고    scopus 로고
    • Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response
    • Wang, B., Matsuoka, S., Ballif, B. A., Zhang, D., Smogorzewska, A., Gygi, S. P., et al. (2007). Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response. Science 316, 1194-1198. doi: 10.1126/science.1139476
    • (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
  • 155
    • 7244234099 scopus 로고    scopus 로고
    • Role of histone H2A ubiquitination in Polycomb silencing
    • Wang, H., Wang, L., Erdjument-Bromage, H., Vidal, M., Tempst, P., Jones, R., et al. (2004). Role of histone H2A ubiquitination in Polycomb silencing. Nature 431, 873-878. doi: 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.6
  • 156
    • 84863229585 scopus 로고    scopus 로고
    • A differentiation checkpoint limits hematopoietic stem cell self-renewal in response to DNA damage
    • Wang, J., Sun, Q., Morita, Y., Jiang, H., Gro�, A., Lechel, A., et al. (2012). A differentiation checkpoint limits hematopoietic stem cell self-renewal in response to DNA damage. Cell 148, 1001-1014. doi: 10.1016/j.cell.2012.01.040
    • (2012) Cell , vol.148 , pp. 1001-1014
    • Wang, J.1    Sun, Q.2    Morita, Y.3    Jiang, H.4    Gro�, A.5    Lechel, A.6
  • 157
    • 84891546394 scopus 로고    scopus 로고
    • The control of hematopoietic stem cell maintenance, self-renewal, and differentiation by Mysm1-mediated epigenetic regulation
    • Wang, T., Nandakumar, V., Jiang, X. X., Jones, L., Yang, A. G., Huang, X. F., et al. (2013). The control of hematopoietic stem cell maintenance, self-renewal, and differentiation by Mysm1-mediated epigenetic regulation. Blood 122, 2812-2822. doi: 10.1182/blood-2013-03-489641
    • (2013) Blood , vol.122 , pp. 2812-2822
    • Wang, T.1    Nandakumar, V.2    Jiang, X.X.3    Jones, L.4    Yang, A.G.5    Huang, X.F.6
  • 158
    • 84862806447 scopus 로고    scopus 로고
    • The mechanism of OTUB1-mediated inhibition of ubiquitination
    • Wiener, R., Zhang, X., Wang, T., and Wolberger, C. (2012). The mechanism of OTUB1-mediated inhibition of ubiquitination. Nature 483, 618-622. doi: 10.1038/nature10911
    • (2012) Nature , vol.483 , pp. 618-622
    • Wiener, R.1    Zhang, X.2    Wang, T.3    Wolberger, C.4
  • 159
    • 77951985779 scopus 로고    scopus 로고
    • Sensitivity to poly(ADP-ribose) polymerase (PARP) inhibition identifies ubiquitin-specific peptidase 11 (USP11) as a regulator of DNA double-strand break repair
    • Wiltshire, T., Lovejoy, C., Wang, T., Xia, F., O'connor, M., and Cortez, D. (2010). Sensitivity to poly(ADP-ribose) polymerase (PARP) inhibition identifies ubiquitin-specific peptidase 11 (USP11) as a regulator of DNA double-strand break repair. J. Biol. Chem. 285, 14565-14571. doi: 10.1074/jbc.M110.104745
    • (2010) J. Biol. Chem , vol.285 , pp. 14565-14571
    • Wiltshire, T.1    Lovejoy, C.2    Wang, T.3    Xia, F.4    O'connor, M.5    Cortez, D.6
  • 160
    • 84908245248 scopus 로고    scopus 로고
    • Epigenetic control of dendritic cell development and fate determination of common myeloid progenitor by Mysm1
    • Won, H., Nandakumar, V., Yates, P., Sanchez, S., Jones, L., Huang, X. F., et al. (2014). Epigenetic control of dendritic cell development and fate determination of common myeloid progenitor by Mysm1. Blood 124, 2647-2656. doi: 10.1182/blood-2013-10-534313
    • (2014) Blood , vol.124 , pp. 2647-2656
    • Won, H.1    Nandakumar, V.2    Yates, P.3    Sanchez, S.4    Jones, L.5    Huang, X.F.6
  • 161
    • 80052238249 scopus 로고    scopus 로고
    • The critical role of monoubiquitination of Histone H2AX in Histone H2AX phosphorylation and DNA damage response
    • Wu, C., Kang, H., Yang, W., Wu, J., Jeong, Y., Wang, J., et al. (2011a). The critical role of monoubiquitination of Histone H2AX in Histone H2AX phosphorylation and DNA damage response. J. Biol. Chem. 286, 30806-30815. doi: 10.1074/jbc.M111.257469
    • (2011) J. Biol. Chem , vol.286 , pp. 30806-30815
    • Wu, C.1    Kang, H.2    Yang, W.3    Wu, J.4    Jeong, Y.5    Wang, J.6
  • 162
  • 163
    • 84899820221 scopus 로고    scopus 로고
    • The histone H2A deubiquitinase Usp16 regulates embryonic stem cell gene expression and lineage commitment
    • Yang, W., Lee, Y. H., Jones, A. E., Woolnough, J. L., Zhou, D., Dai, Q., et al. (2014). The histone H2A deubiquitinase Usp16 regulates embryonic stem cell gene expression and lineage commitment. Nat. Commun. 5, 3818. doi: 10.1038/ncomms4818
    • (2014) Nat. Commun , vol.5 , pp. 3818
    • Yang, W.1    Lee, Y.H.2    Jones, A.E.3    Woolnough, J.L.4    Zhou, D.5    Dai, Q.6
  • 164
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao, T., and Cohen, R. E. (2002). A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419, 403-407. doi: 10.1038/nature01071
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 165
    • 84867119889 scopus 로고    scopus 로고
    • RAP80 is critical in maintaining genomic stability and suppressing tumor development
    • Yin, Z., Menendez, D., Resnick, M. A., French, J. E., Janardhan, K. S., and Jetten, A. M. (2012). RAP80 is critical in maintaining genomic stability and suppressing tumor development. Cancer Res. 72, 5080-5090. doi: 10.1158/0008-5472.CAN-12-1484
    • (2012) Cancer Res , vol.72 , pp. 5080-5090
    • Yin, Z.1    Menendez, D.2    Resnick, M.A.3    French, J.E.4    Janardhan, K.S.5    Jetten, A.M.6
  • 166
    • 34247390658 scopus 로고    scopus 로고
    • Structural and functional differences of SWIRM domain subtypes
    • Yoneyama, M., Tochio, N., Umehara, T., Koshiba, S., Inoue, M., Yabuki, T., et al. (2007). Structural and functional differences of SWIRM domain subtypes. J. Mol. Biol. 369, 222-238. doi: 10.1016/j.jmb.2007.03.027
    • (2007) J. Mol. Biol , vol.369 , pp. 222-238
    • Yoneyama, M.1    Tochio, N.2    Umehara, T.3    Koshiba, S.4    Inoue, M.5    Yabuki, T.6
  • 167
    • 84891912266 scopus 로고    scopus 로고
    • Tumor suppressor and deubiquitinase BAP1 promotes DNA double-strand break repair
    • Yu, H., Pak, H., Hammond-Martel, I., Ghram, M., Rodrigue, A., Daou, S., et al. (2014). Tumor suppressor and deubiquitinase BAP1 promotes DNA double-strand break repair. Proc. Natl. Acad. Sci. U.S.A. 111, 285-290. doi: 10.1073/pnas.1309085110
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111 , pp. 285-290
    • Yu, H.1    Pak, H.2    Hammond-Martel, I.3    Ghram, M.4    Rodrigue, A.5    Daou, S.6
  • 168
    • 84892365810 scopus 로고    scopus 로고
    • Development of inhibitors in the ubiquitination cascade
    • Zhang, W., and Sidhu, S. S. (2014). Development of inhibitors in the ubiquitination cascade. FEBS Lett. 588, 356-367. doi: 10.1016/j.febslet.2013.11.003
    • (2014) FEBS Lett , vol.588 , pp. 356-367
    • Zhang, W.1    Sidhu, S.S.2
  • 169
    • 84870562210 scopus 로고    scopus 로고
    • USP44 regulates centrosome positioning to prevent aneuploidy and suppress tumorigenesis
    • Zhang, Y., Foreman, O., Wigle, D. A., Kosari, F., Vasmatzis, G., Salisbury, J. L., et al. (2012). USP44 regulates centrosome positioning to prevent aneuploidy and suppress tumorigenesis. J. Clin. Invest. 122, 4362-4374. doi: 10.1172/JCI63084
    • (2012) J. Clin. Invest , vol.122 , pp. 4362-4374
    • Zhang, Y.1    Foreman, O.2    Wigle, D.A.3    Kosari, F.4    Vasmatzis, G.5    Salisbury, J.L.6
  • 170
    • 80051654271 scopus 로고    scopus 로고
    • Overexpression of ubiquitin specific protease 44 (USP44) induces chromosomal instability and is frequently observed in human T-cell leukemia
    • Zhang, Y., Van Deursen, J., and Galardy, P. J. (2011). Overexpression of ubiquitin specific protease 44 (USP44) induces chromosomal instability and is frequently observed in human T-cell leukemia. PLoS ONE 6:e23389. doi: 10.1371/journal.pone.0023389
    • (2011) PLoS ONE , vol.6
    • Zhang, Y.1    Van Deursen, J.2    Galardy, P.J.3
  • 171
    • 84911895779 scopus 로고    scopus 로고
    • The histone H2A deubiquitinase USP16 interacts with HERC2 and fine-tunes cellular response to DNA damage
    • Zhang, Z., Yang, H., and Wang, H. (2014). The histone H2A deubiquitinase USP16 interacts with HERC2 and fine-tunes cellular response to DNA damage. J. Biol. Chem. 289, 32883-32894. doi: 10.1074/jbc.M114.599605
    • (2014) J. Biol. Chem , vol.289 , pp. 32883-32894
    • Zhang, Z.1    Yang, H.2    Wang, H.3
  • 172
    • 84885852890 scopus 로고    scopus 로고
    • A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon responses
    • Zheng, H., Gupta, V., Patterson-Fortin, J., Bhattacharya, S., Katlinski, K., Wu, J., et al. (2013). A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon responses. Cell Rep. 5, 180-193. doi: 10.1016/j.celrep.2013.08.025
    • (2013) Cell Rep , vol.5 , pp. 180-193
    • Zheng, H.1    Gupta, V.2    Patterson-Fortin, J.3    Bhattacharya, S.4    Katlinski, K.5    Wu, J.6
  • 173
    • 34547730282 scopus 로고    scopus 로고
    • A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation
    • Zhu, P., Zhou, W., Wang, J., Puc, J., Ohgi, K., Erdjument-Bromage, H., et al. (2007). A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation. Mol. Cell 27, 609-621. doi: 10.1016/j.molcel.2007.07.024
    • (2007) Mol. Cell , vol.27 , pp. 609-621
    • Zhu, P.1    Zhou, W.2    Wang, J.3    Puc, J.4    Ohgi, K.5    Erdjument-Bromage, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.