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Volumn 8, Issue 7, 2013, Pages

Msl2 Is a Novel Component of the Vertebrate DNA Damage Response

Author keywords

[No Author keywords available]

Indexed keywords

DNA; LYSINE; MALE SPECIFIC LETHAL 2 PROTEIN; MALES ABSENT OF THE FIRST PROTEIN; RING FINGER PROTEIN; UNCLASSIFIED DRUG;

EID: 84879991661     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0068549     Document Type: Article
Times cited : (7)

References (57)
  • 1
    • 84873440196 scopus 로고    scopus 로고
    • Pathway choice in DNA double strand break repair: observations of a balancing act
    • Brandsma I, Gent DC, (2012) Pathway choice in DNA double strand break repair: observations of a balancing act. Genome Integr 3: 9.
    • (2012) Genome Integr , vol.3 , pp. 9
    • Brandsma, I.1    Gent, D.C.2
  • 2
    • 33845604556 scopus 로고    scopus 로고
    • DNA double-strand break repair: all's well that ends well
    • Wyman C, Kanaar R, (2006) DNA double-strand break repair: all's well that ends well. Annu Rev Genet 40: 363-383.
    • (2006) Annu Rev Genet , vol.40 , pp. 363-383
    • Wyman, C.1    Kanaar, R.2
  • 3
    • 78649336706 scopus 로고    scopus 로고
    • The DNA damage response: making it safe to play with knives
    • Ciccia A, Elledge SJ, (2010) The DNA damage response: making it safe to play with knives. Mol Cell 40: 179-204.
    • (2010) Mol Cell , vol.40 , pp. 179-204
    • Ciccia, A.1    Elledge, S.J.2
  • 4
    • 79952235291 scopus 로고    scopus 로고
    • Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications
    • Polo SE, Jackson SP, (2011) Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications. Genes Dev 25: 409-433.
    • (2011) Genes Dev , vol.25 , pp. 409-433
    • Polo, S.E.1    Jackson, S.P.2
  • 5
    • 77950958141 scopus 로고    scopus 로고
    • 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks
    • Bunting SF, Callen E, Wong N, Chen HT, Polato F, et al. (2010) 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks. Cell 141: 243-254.
    • (2010) Cell , vol.141 , pp. 243-254
    • Bunting, S.F.1    Callen, E.2    Wong, N.3    Chen, H.T.4    Polato, F.5
  • 7
    • 84860389035 scopus 로고    scopus 로고
    • 53BP1-mediated DNA double strand break repair: insert bad pun here
    • Noon AT, Goodarzi AA, (2011) 53BP1-mediated DNA double strand break repair: insert bad pun here. DNA Repair (Amst) 10: 1071-1076.
    • (2011) DNA Repair (Amst) , vol.10 , pp. 1071-1076
    • Noon, A.T.1    Goodarzi, A.A.2
  • 8
    • 9244252580 scopus 로고    scopus 로고
    • Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
    • Huyen Y, Zgheib O, Ditullio RA Jr, Gorgoulis VG, Zacharatos P, et al. (2004) Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks. Nature 432: 406-411.
    • (2004) Nature , vol.432 , pp. 406-411
    • Huyen, Y.1    Zgheib, O.2    Ditullio Jr., R.A.3    Gorgoulis, V.G.4    Zacharatos, P.5
  • 9
    • 79551665780 scopus 로고    scopus 로고
    • MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites
    • Pei H, Zhang L, Luo K, Qin Y, Chesi M, et al. (2011) MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites. Nature 470: 124-128.
    • (2011) Nature , vol.470 , pp. 124-128
    • Pei, H.1    Zhang, L.2    Luo, K.3    Qin, Y.4    Chesi, M.5
  • 10
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan MV, Lee J, Ward IM, Kim JE, Thompson JR, et al. (2006) Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 127: 1361-1373.
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3    Kim, J.E.4    Thompson, J.R.5
  • 11
    • 84862829634 scopus 로고    scopus 로고
    • Bat3 facilitates H3K79 dimethylation by DOT1L and promotes DNA damage-induced 53BP1 foci at G1/G2 cell-cycle phases
    • Wakeman TP, Wang Q, Feng J, Wang XF, (2012) Bat3 facilitates H3K79 dimethylation by DOT1L and promotes DNA damage-induced 53BP1 foci at G1/G2 cell-cycle phases. EMBO J 31: 2169-2181.
    • (2012) EMBO J , vol.31 , pp. 2169-2181
    • Wakeman, T.P.1    Wang, Q.2    Feng, J.3    Wang, X.F.4
  • 12
    • 77949708459 scopus 로고    scopus 로고
    • Regulation of chromatin architecture by the PWWP domain-containing DNA damage-responsive factor EXPAND1/MUM1
    • Huen MS, Huang J, Leung JW, Sy SM, Leung KM, et al. (2010) Regulation of chromatin architecture by the PWWP domain-containing DNA damage-responsive factor EXPAND1/MUM1. Mol Cell 37: 854-864.
    • (2010) Mol Cell , vol.37 , pp. 854-864
    • Huen, M.S.1    Huang, J.2    Leung, J.W.3    Sy, S.M.4    Leung, K.M.5
  • 13
    • 80052320737 scopus 로고    scopus 로고
    • Drosophila dosage compensation: males are from Mars, females are from Venus
    • Georgiev P, Chlamydas S, Akhtar A, (2011) Drosophila dosage compensation: males are from Mars, females are from Venus. Fly (Austin) 5: 147-154.
    • (2011) Fly (Austin) , vol.5 , pp. 147-154
    • Georgiev, P.1    Chlamydas, S.2    Akhtar, A.3
  • 14
    • 33947156677 scopus 로고    scopus 로고
    • The right dose for every sex
    • Mendjan S, Akhtar A, (2007) The right dose for every sex. Chromosoma 116: 95-106.
    • (2007) Chromosoma , vol.116 , pp. 95-106
    • Mendjan, S.1    Akhtar, A.2
  • 15
    • 0029063585 scopus 로고
    • Expression of msl-2 causes assembly of dosage compensation regulators on the X chromosomes and female lethality in Drosophila
    • Kelley RL, Solovyeva I, Lyman LM, Richman R, Solovyev V, et al. (1995) Expression of msl-2 causes assembly of dosage compensation regulators on the X chromosomes and female lethality in Drosophila. Cell 81: 867-877.
    • (1995) Cell , vol.81 , pp. 867-877
    • Kelley, R.L.1    Solovyeva, I.2    Lyman, L.M.3    Richman, R.4    Solovyev, V.5
  • 16
    • 84894895524 scopus 로고    scopus 로고
    • Different chromatin interfaces of the Drosophila dosage compensation complex revealed by high-shear ChIP-seq
    • Straub T, Zabel A, Gilfillan GD, Feller C, Becker PB (2012) Different chromatin interfaces of the Drosophila dosage compensation complex revealed by high-shear ChIP-seq. Genome Res.
    • (2012) Genome Res
    • Straub, T.1    Zabel, A.2    Gilfillan, G.D.3    Feller, C.4    Becker, P.B.5
  • 17
    • 84870391874 scopus 로고    scopus 로고
    • Msl1-mediated dimerization of the dosage compensation complex is essential for male x-chromosome regulation in Drosophila
    • Hallacli E, Lipp M, Georgiev P, Spielman C, Cusack S, et al. (2012) Msl1-mediated dimerization of the dosage compensation complex is essential for male x-chromosome regulation in Drosophila. Mol Cell 48: 587-600.
    • (2012) Mol Cell , vol.48 , pp. 587-600
    • Hallacli, E.1    Lipp, M.2    Georgiev, P.3    Spielman, C.4    Cusack, S.5
  • 18
    • 84870391617 scopus 로고    scopus 로고
    • MSL2 Combines Sensor and Effector Functions in Homeostatic Control of the Drosophila Dosage Compensation Machinery
    • Villa R, Forne I, Muller M, Imhof A, Straub T, et al. (2012) MSL2 Combines Sensor and Effector Functions in Homeostatic Control of the Drosophila Dosage Compensation Machinery. Mol Cell.
    • (2012) Mol Cell
    • Villa, R.1    Forne, I.2    Muller, M.3    Imhof, A.4    Straub, T.5
  • 19
    • 70350012477 scopus 로고    scopus 로고
    • Two mammalian MOF complexes regulate transcription activation by distinct mechanisms
    • Li X, Wu L, Corsa CA, Kunkel S, Dou Y, (2009) Two mammalian MOF complexes regulate transcription activation by distinct mechanisms. Mol Cell 36: 290-301.
    • (2009) Mol Cell , vol.36 , pp. 290-301
    • Li, X.1    Wu, L.2    Corsa, C.A.3    Kunkel, S.4    Dou, Y.5
  • 20
    • 33644870525 scopus 로고    scopus 로고
    • Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila
    • Mendjan S, Taipale M, Kind J, Holz H, Gebhardt P, et al. (2006) Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila. Mol Cell 21: 811-823.
    • (2006) Mol Cell , vol.21 , pp. 811-823
    • Mendjan, S.1    Taipale, M.2    Kind, J.3    Holz, H.4    Gebhardt, P.5
  • 21
    • 27144546434 scopus 로고    scopus 로고
    • A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16
    • Smith ER, Cayrou C, Huang R, Lane WS, Cote J, et al. (2005) A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. Mol Cell Biol 25: 9175-9188.
    • (2005) Mol Cell Biol , vol.25 , pp. 9175-9188
    • Smith, E.R.1    Cayrou, C.2    Huang, R.3    Lane, W.S.4    Cote, J.5
  • 22
    • 59149085299 scopus 로고    scopus 로고
    • MSL2 promotes Mdm2-independent cytoplasmic localization of p53
    • Kruse JP, Gu W, (2009) MSL2 promotes Mdm2-independent cytoplasmic localization of p53. J Biol Chem 284: 3250-3263.
    • (2009) J Biol Chem , vol.284 , pp. 3250-3263
    • Kruse, J.P.1    Gu, W.2
  • 23
    • 81155154333 scopus 로고    scopus 로고
    • The cancer-associated K351N mutation affects the ubiquitination and the translocation to mitochondria of p53 protein
    • Muscolini M, Montagni E, Palermo V, Di Agostino S, Gu W, et al. (2011) The cancer-associated K351N mutation affects the ubiquitination and the translocation to mitochondria of p53 protein. J Biol Chem 286: 39693-39702.
    • (2011) J Biol Chem , vol.286 , pp. 39693-39702
    • Muscolini, M.1    Montagni, E.2    Palermo, V.3    Di Agostino, S.4    Gu, W.5
  • 24
    • 79959864524 scopus 로고    scopus 로고
    • The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation
    • Wu L, Zee BM, Wang Y, Garcia BA, Dou Y, (2011) The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation. Mol Cell 43: 132-144.
    • (2011) Mol Cell , vol.43 , pp. 132-144
    • Wu, L.1    Zee, B.M.2    Wang, Y.3    Garcia, B.A.4    Dou, Y.5
  • 25
    • 79953131815 scopus 로고    scopus 로고
    • SUV420H2-mediated H4K20 trimethylation enforces RNA polymerase II promoter-proximal pausing by blocking hMOF-dependent H4K16 acetylation
    • Kapoor-Vazirani P, Kagey JD, Vertino PM, (2011) SUV420H2-mediated H4K20 trimethylation enforces RNA polymerase II promoter-proximal pausing by blocking hMOF-dependent H4K16 acetylation. Mol Cell Biol 31: 1594-1609.
    • (2011) Mol Cell Biol , vol.31 , pp. 1594-1609
    • Kapoor-Vazirani, P.1    Kagey, J.D.2    Vertino, P.M.3
  • 26
    • 37549014206 scopus 로고    scopus 로고
    • The mammalian ortholog of Drosophila MOF that acetylates histone H4 lysine 16 is essential for embryogenesis and oncogenesis
    • Gupta A, Guerin-Peyrou TG, Sharma GG, Park C, Agarwal M, et al. (2008) The mammalian ortholog of Drosophila MOF that acetylates histone H4 lysine 16 is essential for embryogenesis and oncogenesis. Mol Cell Biol 28: 397-409.
    • (2008) Mol Cell Biol , vol.28 , pp. 397-409
    • Gupta, A.1    Guerin-Peyrou, T.G.2    Sharma, G.G.3    Park, C.4    Agarwal, M.5
  • 27
    • 39649119288 scopus 로고    scopus 로고
    • The histone acetyltransferase hMOF is frequently downregulated in primary breast carcinoma and medulloblastoma and constitutes a biomarker for clinical outcome in medulloblastoma
    • Pfister S, Rea S, Taipale M, Mendrzyk F, Straub B, et al. (2008) The histone acetyltransferase hMOF is frequently downregulated in primary breast carcinoma and medulloblastoma and constitutes a biomarker for clinical outcome in medulloblastoma. Int J Cancer 122: 1207-1213.
    • (2008) Int J Cancer , vol.122 , pp. 1207-1213
    • Pfister, S.1    Rea, S.2    Taipale, M.3    Mendrzyk, F.4    Straub, B.5
  • 28
    • 78649533191 scopus 로고    scopus 로고
    • MOF and H4 K16 acetylation play important roles in DNA damage repair by modulating recruitment of DNA damage repair protein Mdc1
    • Li X, Corsa CA, Pan PW, Wu L, Ferguson D, et al. (2010) MOF and H4 K16 acetylation play important roles in DNA damage repair by modulating recruitment of DNA damage repair protein Mdc1. Mol Cell Biol 30: 5335-5347.
    • (2010) Mol Cell Biol , vol.30 , pp. 5335-5347
    • Li, X.1    Corsa, C.A.2    Pan, P.W.3    Wu, L.4    Ferguson, D.5
  • 29
    • 77954360144 scopus 로고    scopus 로고
    • MOF and histone H4 acetylation at lysine 16 are critical for DNA damage response and double-strand break repair
    • Sharma GG, So S, Gupta A, Kumar R, Cayrou C, et al. (2010) MOF and histone H4 acetylation at lysine 16 are critical for DNA damage response and double-strand break repair. Mol Cell Biol 30: 3582-3595.
    • (2010) Mol Cell Biol , vol.30 , pp. 3582-3595
    • Sharma, G.G.1    So, S.2    Gupta, A.3    Kumar, R.4    Cayrou, C.5
  • 30
    • 22544480772 scopus 로고    scopus 로고
    • hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells
    • Taipale M, Rea S, Richter K, Vilar A, Lichter P, et al. (2005) hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells. Mol Cell Biol 25: 6798-6810.
    • (2005) Mol Cell Biol , vol.25 , pp. 6798-6810
    • Taipale, M.1    Rea, S.2    Richter, K.3    Vilar, A.4    Lichter, P.5
  • 32
    • 33845656738 scopus 로고    scopus 로고
    • Acetylation of the p53 DNA-binding domain regulates apoptosis induction
    • Sykes SM, Mellert HS, Holbert MA, Li K, Marmorstein R, et al. (2006) Acetylation of the p53 DNA-binding domain regulates apoptosis induction. Mol Cell 24: 841-851.
    • (2006) Mol Cell , vol.24 , pp. 841-851
    • Sykes, S.M.1    Mellert, H.S.2    Holbert, M.A.3    Li, K.4    Marmorstein, R.5
  • 33
    • 70449717068 scopus 로고    scopus 로고
    • p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage
    • Gironella M, Malicet C, Cano C, Sandi MJ, Hamidi T, et al. (2009) p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage. J Cell Physiol 221: 594-602.
    • (2009) J Cell Physiol , vol.221 , pp. 594-602
    • Gironella, M.1    Malicet, C.2    Cano, C.3    Sandi, M.J.4    Hamidi, T.5
  • 34
    • 0033866836 scopus 로고    scopus 로고
    • Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila
    • Akhtar A, Becker PB, (2000) Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila. Mol Cell 5: 367-375.
    • (2000) Mol Cell , vol.5 , pp. 367-375
    • Akhtar, A.1    Becker, P.B.2
  • 35
    • 34547913733 scopus 로고    scopus 로고
    • Males absent on the first (MOF): from flies to humans
    • Rea S, Xouri G, Akhtar A, (2007) Males absent on the first (MOF): from flies to humans. Oncogene 26: 5385-5394.
    • (2007) Oncogene , vol.26 , pp. 5385-5394
    • Rea, S.1    Xouri, G.2    Akhtar, A.3
  • 36
    • 79961083402 scopus 로고    scopus 로고
    • Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice
    • Krishnan V, Chow MZ, Wang Z, Zhang L, Liu B, et al. (2011) Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice. Proc Natl Acad Sci U S A 108: 12325-12330.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12325-12330
    • Krishnan, V.1    Chow, M.Z.2    Wang, Z.3    Zhang, L.4    Liu, B.5
  • 37
    • 57749086992 scopus 로고    scopus 로고
    • Di-methyl H4 lysine 20 targets the checkpoint protein Crb2 to sites of DNA damage
    • Greeson NT, Sengupta R, Arida AR, Jenuwein T, Sanders SL, (2008) Di-methyl H4 lysine 20 targets the checkpoint protein Crb2 to sites of DNA damage. J Biol Chem 283: 33168-33174.
    • (2008) J Biol Chem , vol.283 , pp. 33168-33174
    • Greeson, N.T.1    Sengupta, R.2    Arida, A.R.3    Jenuwein, T.4    Sanders, S.L.5
  • 38
    • 3242887420 scopus 로고    scopus 로고
    • The role of the non-homologous end-joining pathway in lymphocyte development
    • Rooney S, Chaudhuri J, Alt FW, (2004) The role of the non-homologous end-joining pathway in lymphocyte development. Immunol Rev 200: 115-131.
    • (2004) Immunol Rev , vol.200 , pp. 115-131
    • Rooney, S.1    Chaudhuri, J.2    Alt, F.W.3
  • 39
    • 0035977007 scopus 로고    scopus 로고
    • Genetic analysis of the DNA-dependent protein kinase reveals an inhibitory role of Ku in late S-G2 phase DNA double-strand break repair
    • Fukushima T, Takata M, Morrison C, Araki R, Fujimori A, et al. (2001) Genetic analysis of the DNA-dependent protein kinase reveals an inhibitory role of Ku in late S-G2 phase DNA double-strand break repair. J Biol Chem 276: 44413-44418.
    • (2001) J Biol Chem , vol.276 , pp. 44413-44418
    • Fukushima, T.1    Takata, M.2    Morrison, C.3    Araki, R.4    Fujimori, A.5
  • 40
    • 78649446475 scopus 로고    scopus 로고
    • A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation
    • Dobbs TA, Tainer JA, Lees-Miller SP, (2010) A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation. DNA Repair (Amst) 9: 1307-1314.
    • (2010) DNA Repair (Amst) , vol.9 , pp. 1307-1314
    • Dobbs, T.A.1    Tainer, J.A.2    Lees-Miller, S.P.3
  • 41
    • 68249138694 scopus 로고    scopus 로고
    • Role of Mre11 in chromosomal nonhomologous end joining in mammalian cells
    • Rass E, Grabarz A, Plo I, Gautier J, Bertrand P, et al. (2009) Role of Mre11 in chromosomal nonhomologous end joining in mammalian cells. Nat Struct Mol Biol 16: 819-824.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 819-824
    • Rass, E.1    Grabarz, A.2    Plo, I.3    Gautier, J.4    Bertrand, P.5
  • 42
    • 59449094470 scopus 로고    scopus 로고
    • An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks
    • Zgheib O, Pataky K, Brugger J, Halazonetis TD, (2009) An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks. Mol Cell Biol 29: 1050-1058.
    • (2009) Mol Cell Biol , vol.29 , pp. 1050-1058
    • Zgheib, O.1    Pataky, K.2    Brugger, J.3    Halazonetis, T.D.4
  • 43
    • 65549143757 scopus 로고    scopus 로고
    • RAD18 promotes DNA double-strand break repair during G1 phase through chromatin retention of 53BP1
    • Watanabe K, Iwabuchi K, Sun J, Tsuji Y, Tani T, et al. (2009) RAD18 promotes DNA double-strand break repair during G1 phase through chromatin retention of 53BP1. Nucleic Acids Res 37: 2176-2193.
    • (2009) Nucleic Acids Res , vol.37 , pp. 2176-2193
    • Watanabe, K.1    Iwabuchi, K.2    Sun, J.3    Tsuji, Y.4    Tani, T.5
  • 44
    • 79960953769 scopus 로고    scopus 로고
    • The demoiselle of X-inactivation: 50 years old and as trendy and mesmerising as ever
    • Morey C, Avner P, (2011) The demoiselle of X-inactivation: 50 years old and as trendy and mesmerising as ever. PLoS Genet 7: e1002212.
    • (2011) PLoS Genet , vol.7
    • Morey, C.1    Avner, P.2
  • 45
    • 0032530393 scopus 로고    scopus 로고
    • Complex formation by the Drosophila MSL proteins: role of the MSL2 RING finger in protein complex assembly
    • Copps K, Richman R, Lyman LM, Chang KA, Rampersad-Ammons J, et al. (1998) Complex formation by the Drosophila MSL proteins: role of the MSL2 RING finger in protein complex assembly. EMBO J 17: 5409-5417.
    • (1998) EMBO J , vol.17 , pp. 5409-5417
    • Copps, K.1    Richman, R.2    Lyman, L.M.3    Chang, K.A.4    Rampersad-Ammons, J.5
  • 46
    • 84870391617 scopus 로고    scopus 로고
    • MSL2 Combines Sensor and Effector Functions in Homeostatic Control of the Drosophila Dosage Compensation Machinery
    • Villa R, Forne I, Muller M, Imhof A, Straub T, et al. (2012) MSL2 Combines Sensor and Effector Functions in Homeostatic Control of the Drosophila Dosage Compensation Machinery. Mol Cell 48: 647-654.
    • (2012) Mol Cell , vol.48 , pp. 647-654
    • Villa, R.1    Forne, I.2    Muller, M.3    Imhof, A.4    Straub, T.5
  • 47
    • 77957354585 scopus 로고    scopus 로고
    • Methylated H3K4, a transcription-associated histone modification, is involved in the DNA damage response pathway
    • Faucher D, Wellinger RJ (2010) Methylated H3K4, a transcription-associated histone modification, is involved in the DNA damage response pathway. PLoS Genet 6.
    • (2010) PLoS Genet , vol.6
    • Faucher, D.1    Wellinger, R.J.2
  • 48
    • 58649094213 scopus 로고    scopus 로고
    • The direct interaction between 53BP1 and MDC1 is required for the recruitment of 53BP1 to sites of damage
    • Eliezer Y, Argaman L, Rhie A, Doherty AJ, Goldberg M, (2009) The direct interaction between 53BP1 and MDC1 is required for the recruitment of 53BP1 to sites of damage. J Biol Chem 284: 426-435.
    • (2009) J Biol Chem , vol.284 , pp. 426-435
    • Eliezer, Y.1    Argaman, L.2    Rhie, A.3    Doherty, A.J.4    Goldberg, M.5
  • 49
    • 84862771956 scopus 로고    scopus 로고
    • The in vivo dynamic interplay of MDC1 and 53BP1 at DNA damage-induced nuclear foci
    • Mok MT, Henderson BR, (2012) The in vivo dynamic interplay of MDC1 and 53BP1 at DNA damage-induced nuclear foci. Int J Biochem Cell Biol 44: 1398-1409.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1398-1409
    • Mok, M.T.1    Henderson, B.R.2
  • 50
    • 0027458374 scopus 로고
    • A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm
    • Sukegawa J, Blobel G, (1993) A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm. Cell 72: 29-38.
    • (1993) Cell , vol.72 , pp. 29-38
    • Sukegawa, J.1    Blobel, G.2
  • 51
    • 84859596654 scopus 로고    scopus 로고
    • Nucleoporin NUP153 guards genome integrity by promoting nuclear import of 53BP1
    • Moudry P, Lukas C, Macurek L, Neumann B, Heriche JK, et al. (2012) Nucleoporin NUP153 guards genome integrity by promoting nuclear import of 53BP1. Cell Death Differ 19: 798-807.
    • (2012) Cell Death Differ , vol.19 , pp. 798-807
    • Moudry, P.1    Lukas, C.2    Macurek, L.3    Neumann, B.4    Heriche, J.K.5
  • 52
    • 84871547322 scopus 로고    scopus 로고
    • Multiple facets of the DNA damage response contribute to the radioresistance of mouse mesenchymal stromal cell lines
    • Sugrue T, Brown JA, Lowndes NF, Ceredig R, (2013) Multiple facets of the DNA damage response contribute to the radioresistance of mouse mesenchymal stromal cell lines. Stem Cells 31: 137-145.
    • (2013) Stem Cells , vol.31 , pp. 137-145
    • Sugrue, T.1    Brown, J.A.2    Lowndes, N.F.3    Ceredig, R.4
  • 53
    • 34547436174 scopus 로고    scopus 로고
    • Isolation of nuclear and cytoplasmic proteins from DT40 cells
    • Wang YD, Caldwell RB, (2006) Isolation of nuclear and cytoplasmic proteins from DT40 cells. Subcell Biochem 40: 439-440.
    • (2006) Subcell Biochem , vol.40 , pp. 439-440
    • Wang, Y.D.1    Caldwell, R.B.2
  • 54
    • 79953803643 scopus 로고    scopus 로고
    • Roles of vertebrate Smc5 in sister chromatid cohesion and homologous recombinational repair
    • Stephan AK, Kliszczak M, Dodson H, Cooley C, Morrison CG, (2011) Roles of vertebrate Smc5 in sister chromatid cohesion and homologous recombinational repair. Mol Cell Biol 31: 1369-1381.
    • (2011) Mol Cell Biol , vol.31 , pp. 1369-1381
    • Stephan, A.K.1    Kliszczak, M.2    Dodson, H.3    Cooley, C.4    Morrison, C.G.5
  • 55
    • 33745182540 scopus 로고    scopus 로고
    • The DNA polymerase lambda is required for the repair of non-compatible DNA double strand breaks by NHEJ in mammalian cells
    • Capp JP, Boudsocq F, Bertrand P, Laroche-Clary A, Pourquier P, et al. (2006) The DNA polymerase lambda is required for the repair of non-compatible DNA double strand breaks by NHEJ in mammalian cells. Nucleic Acids Res 34: 2998-3007.
    • (2006) Nucleic Acids Res , vol.34 , pp. 2998-3007
    • Capp, J.P.1    Boudsocq, F.2    Bertrand, P.3    Laroche-Clary, A.4    Pourquier, P.5
  • 57
    • 76249090489 scopus 로고    scopus 로고
    • BioGPS: an extensible and customizable portal for querying and organizing gene annotation resources
    • Wu C, Orozco C, Boyer J, Leglise M, Goodale J, et al. (2009) BioGPS: an extensible and customizable portal for querying and organizing gene annotation resources. Genome Biol 10: R130.
    • (2009) Genome Biol , vol.10
    • Wu, C.1    Orozco, C.2    Boyer, J.3    Leglise, M.4    Goodale, J.5


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