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Volumn 5, Issue 10, 2013, Pages

Nucleotide excision repair in Eukaryotes

Author keywords

[No Author keywords available]

Indexed keywords

DNA;

EID: 84870751887     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a012609     Document Type: Review
Times cited : (587)

References (166)
  • 2
    • 0242605710 scopus 로고    scopus 로고
    • Nucleotide excision repair of DNA with recombinant human proteins: Definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK
    • Araujo SJ, Tirode F, Coin F, Pospiech H, Syvaoja JE, Stucki M, Hubscher U, Egly JM, Wood RD. 2000. Nucleotide excision repair of DNA with recombinant human proteins: Definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK. Genes Dev 14: 349-359.
    • (2000) Genes Dev , vol.14 , pp. 349-359
    • Araujo, S.J.1    Tirode, F.2    Coin, F.3    Pospiech, H.4    Syvaoja, J.E.5    Stucki, M.6    Hubscher, U.7    Egly, J.M.8    Wood, R.D.9
  • 3
    • 0035102950 scopus 로고    scopus 로고
    • Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled re-pairosome
    • Araujo SJ, Nigg EA, Wood RD. 2001. Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled re-pairosome. Mol Cell Biol 21: 2281-2291.
    • (2001) Mol Cell Biol , vol.21 , pp. 2281-2291
    • Araujo, S.J.1    Nigg, E.A.2    Wood, R.D.3
  • 6
    • 0001408659 scopus 로고
    • Release of ultraviolet light-induced thymine dimers from DNA in E coli K-12
    • Boyce RP, Howard-Flanders P. 1964. Release of ultraviolet light-induced thymine dimers from DNA in E. coli K-12. Proc Natl Acad Sci 51: 293-300.
    • (1964) Proc Natl Acad Sci , vol.51 , pp. 293-300
    • Boyce, R.P.1    Howard-Flanders, P.2
  • 7
    • 33845575990 scopus 로고    scopus 로고
    • Biochemical and structural domain analysis of xe-roderma pigmentosum complementation group C protein
    • Bunick CG, Miller MR, Fuller BE, Fanning E, Chazin WJ. 2006. Biochemical and structural domain analysis of xe-roderma pigmentosum complementation group C protein. Biochemistry 45: 14965-14979.
    • (2006) Biochemistry , vol.45 , pp. 14965-14979
    • Bunick, C.G.1    Miller, M.R.2    Fuller, B.E.3    Fanning, E.4    Chazin, W.J.5
  • 8
    • 23944515285 scopus 로고    scopus 로고
    • DNA quality control by conformational readout on the undamaged strand of the double helix
    • Buterin T, Meyer C, Giese B, Naegeli H. 2005. DNA quality control by conformational readout on the undamaged strand of the double helix. Chem Biol 12: 913-922.
    • (2005) Chem Biol , vol.12 , pp. 913-922
    • Buterin, T.1    Meyer, C.2    Giese, B.3    Naegeli, H.4
  • 10
    • 33644812489 scopus 로고    scopus 로고
    • Recognition of helical kinks by xeroderma pigmen-tosum group A protein triggers DNA excision repair
    • Camenisch U, Dip R, Schumacher SB, Schuler B, Naegeli H. 2006. Recognition of helical kinks by xeroderma pigmen-tosum group A protein triggers DNA excision repair. Nat Struct Mol Biol 13: 278-284.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 278-284
    • Camenisch, U.1    Dip, R.2    Schumacher, S.B.3    Schuler, B.4    Naegeli, H.5
  • 12
    • 0014421995 scopus 로고
    • Defective repair replication of DNA in xeroderma pigmentosum
    • Cleaver JE. 1968. Defective repair replication of DNA in xeroderma pigmentosum. Nature 218: 652-656.
    • (1968) Nature , vol.218 , pp. 652-656
    • Cleaver, J.E.1
  • 14
    • 34247513888 scopus 로고    scopus 로고
    • Distinct roles for the XPB/p52 and XPD/p44 sub complexes of TFIIH in damaged DNA opening during nucleotide excision repair
    • Coin F, Oksenych V, Egly JM. 2007. Distinct roles for the XPB/p52 and XPD/p44 sub complexes of TFIIH in damaged DNA opening during nucleotide excision repair. Mol Cell 26: 245-256.
    • (2007) Mol Cell , vol.26 , pp. 245-256
    • Coin, F.1    Oksenych, V.2    Egly, J.M.3
  • 15
  • 16
    • 84861457511 scopus 로고    scopus 로고
    • TFIIH: When transcription met DNA repair
    • Compe E, Egly JM. 2012. TFIIH: When transcription met DNA repair. Nat Rev Mol Cell Biol 13: 343-354.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 343-354
    • Compe, E.1    Egly, J.M.2
  • 17
    • 0033605159 scopus 로고    scopus 로고
    • Conserved residues of human XPG protein important for nuclease activity and func-tioninnucleotide excision repair
    • Constantinou A, Gunz D, Evans E, Lalle P, Bates PA, Wood RD, Clarkson SG. 1999. Conserved residues of human XPG protein important for nuclease activity and func-tioninnucleotide excision repair. J Biol Chem 274: 5637-5648.
    • (1999) J Biol Chem , vol.274 , pp. 5637-5648
    • Constantinou, A.1    Gunz, D.2    Evans, E.3    Lalle, P.4    Bates, P.A.5    Wood, R.D.6    Clarkson, S.G.7
  • 18
  • 19
    • 0015516045 scopus 로고
    • Genetic heterogeneity of xeroderma pigmentosum demonstrated by somatic cell hybridization
    • De Weerd-Kastelein EA, Keijzer W, Bootsma D. 1972. Genetic heterogeneity of xeroderma pigmentosum demonstrated by somatic cell hybridization. Nat New Biol 238: 80-83.
    • (1972) Nat New Biol , vol.238 , pp. 80-83
    • De Weerd-Kastelein, E.A.1    Keijzer, W.2    Bootsma, D.3
  • 20
    • 84857041145 scopus 로고    scopus 로고
    • Shining a light on xero-derma pigmentosum
    • Di Giovanna JJ, Kraemer KH. 2012. Shining a light on xero-derma pigmentosum. J Invest Dermatol 132: 785-796.
    • (2012) J Invest Dermatol , vol.132 , pp. 785-796
    • Di Giovanna, J.J.1    Kraemer, K.H.2
  • 21
    • 14844300809 scopus 로고    scopus 로고
    • The spacer region of XPG mediates recruitment to nucleotide excision repair complexes and determines substrate specificity
    • Dunand-Sauthier I, Hohl M, Thorel F, Jaquier-Gubler P, Clarkson SG, Schärer OD. 2005. The spacer region of XPG mediates recruitment to nucleotide excision repair complexes and determines substrate specificity. J Biol Chem 280: 7030-7037.
    • (2005) J Biol Chem , vol.280 , pp. 7030-7037
    • Dunand-Sauthier, I.1    Hohl, M.2    Thorel, F.3    Jaquier-Gubler, P.4    Clarkson, S.G.5    Schärer, O.D.6
  • 22
    • 0031013308 scopus 로고    scopus 로고
    • Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein
    • Evans E, Fellows J, Coffer A, Wood RD. 1997a. Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein. Embo J 16: 625-638.
    • (1997) Embo J , vol.16 , pp. 625-638
    • Evans, E.1    Fellows, J.2    Coffer, A.3    Wood, R.D.4
  • 23
    • 0030732132 scopus 로고    scopus 로고
    • Mechanism of open complex and dual incision formation by human nucleotide excision repair factors
    • Evans E, Moggs JG, Hwang JR, Egly JM, Wood RD. 1997b. Mechanism of open complex and dual incision formation by human nucleotide excision repair factors. Embo J 16: 6559-6573.
    • (1997) Embo J , vol.16 , pp. 6559-6573
    • Evans, E.1    Moggs, J.G.2    Hwang, J.R.3    Egly, J.M.4    Wood, R.D.5
  • 24
    • 79960343567 scopus 로고    scopus 로고
    • Regulation of en-donuclease activity in human nucleotide excision repair
    • Fagbemi AF, Orelli B, Schärer OD. 2011. Regulation of en-donuclease activity in human nucleotide excision repair. DNA Repair (Amst) 10: 722-729.
    • (2011) DNA Repair (Amst) , vol.10 , pp. 722-729
    • Fagbemi, A.F.1    Orelli, B.2    Schärer, O.D.3
  • 25
    • 77955501963 scopus 로고    scopus 로고
    • SIRT1 regulates UV-induced DNA repair through deacetylating XPA
    • Fan W, Luo J. 2010. SIRT1 regulates UV-induced DNA repair through deacetylating XPA. Mol Cell 39: 247-258.
    • (2010) Mol Cell , vol.39 , pp. 247-258
    • Fan, W.1    Luo, J.2
  • 26
    • 84867693856 scopus 로고    scopus 로고
    • Structure and conformational change of a replication protein A heterotrimer bound to ssDNA
    • Fan J, Pavletich NP. 2012. Structure and conformational change of a replication protein A heterotrimer bound to ssDNA. Genes Dev 26: 2337-2347.
    • (2012) Genes Dev , vol.26 , pp. 2337-2347
    • Fan, J.1    Pavletich, N.P.2
  • 27
    • 33645988522 scopus 로고    scopus 로고
    • Conserved XPB core structure and motifs for DNA unwinding: Implications for pathway selection of transcription or excision repair
    • Fan L, Arvai AS, Cooper PK, Iwai S, Hanaoka F, Tainer JA. 2006. Conserved XPB core structure and motifs for DNA unwinding: Implications for pathway selection of transcription or excision repair. Mol Cell 22: 27-37.
    • (2006) Mol Cell , vol.22 , pp. 27-37
    • Fan, L.1    Arvai, A.S.2    Cooper, P.K.3    Iwai, S.4    Hanaoka, F.5    Tainer, J.A.6
  • 28
    • 44149094083 scopus 로고    scopus 로고
    • XPD helicase structures and activities: Insights into the cancer and aging phenotypes from XPD mutations
    • Fan L, Fuss JO, Cheng QJ, Arvai AS, Hammel M, Roberts VA, Cooper PK, Tainer JA. 2008. XPD helicase structures and activities: Insights into the cancer and aging phenotypes from XPD mutations. Cell 133: 789-800.
    • (2008) Cell , vol.133 , pp. 789-800
    • Fan, L.1    Fuss, J.O.2    Cheng, Q.J.3    Arvai, A.S.4    Hammel, M.5    Roberts, V.A.6    Cooper, P.K.7    Tainer, J.A.8
  • 29
    • 80055046325 scopus 로고    scopus 로고
    • Regulation of nucleotide excision repair by UV-DDB: Prioritization of damage recognition to internu-cleosomal DNA
    • Fei J, Kaczmarek N, Luch A, Glas A, Carell T, Naegeli H. 2011. Regulation of nucleotide excision repair by UV-DDB: Prioritization of damage recognition to internu-cleosomal DNA. PLoS Biol 9: e1001183.
    • (2011) PLoS Biol , vol.9
    • Fei, J.1    Kaczmarek, N.2    Luch, A.3    Glas, A.4    Carell, T.5    Naegeli, H.6
  • 31
    • 0345306615 scopus 로고    scopus 로고
    • In vivo recruitment of XPC to UV-induced cyclobutane pyrim-idine dimers by the DDB2 gene product
    • Fitch ME, Nakajima S, Yasui A, Ford JM. 2003. In vivo recruitment of XPC to UV-induced cyclobutane pyrim-idine dimers by the DDB2 gene product. J Biol Chem 278: 46906-46910.
    • (2003) J Biol Chem , vol.278 , pp. 46906-46910
    • Fitch, M.E.1    Nakajima, S.2    Yasui, A.3    Ford, J.M.4
  • 32
    • 34247482968 scopus 로고    scopus 로고
    • DNA repair and transcriptional deficiencies caused by mutations in the Drosophila p52 subunit of TFIIH generate developmental defects and chromosome fragility
    • Fregoso M, Laine JP, Aguilar-Fuentes J, Mocquet V, Reynaud E, Coin F, Egly JM, Zurita M. 2007. DNA repair and transcriptional deficiencies caused by mutations in the Drosophila p52 subunit of TFIIH generate developmental defects and chromosome fragility. Mol Cell Biol 27: 3640-3650.
    • (2007) Mol Cell Biol , vol.27 , pp. 3640-3650
    • Fregoso, M.1    Laine, J.P.2    Aguilar-Fuentes, J.3    Mocquet, V.4    Reynaud, E.5    Coin, F.6    Egly, J.M.7    Zurita, M.8
  • 35
    • 0030710190 scopus 로고    scopus 로고
    • Initiation and bidirectional propagation of chromatin assembly from a target site for nucleotide excision repair
    • Gaillard PH, Moggs JG, Roche DM, Quivy JP, Becker PB, Wood RD, Almouzni G. 1997. Initiation and bidirectional propagation of chromatin assembly from a target site for nucleotide excision repair. EMBO J 16: 6281-6289.
    • (1997) EMBO J , vol.16 , pp. 6281-6289
    • Gaillard, P.H.1    Moggs, J.G.2    Roche, D.M.3    Quivy, J.P.4    Becker, P.B.5    Wood, R.D.6    Almouzni, G.7
  • 36
    • 1542320702 scopus 로고    scopus 로고
    • Physical and functional interactions between nucleotide excision repair and DNA damage checkpoint
    • Giannattasio M, Lazzaro F, Longhese MP, Plevani P, Muzi-Falconi M. 2004. Physical and functional interactions between nucleotide excision repair and DNA damage checkpoint. EMBO J 23: 429-438.
    • (2004) EMBO J , vol.23 , pp. 429-438
    • Giannattasio, M.1    Lazzaro, F.2    Longhese, M.P.3    Plevani, P.4    Muzi-Falconi, M.5
  • 40
    • 32644450616 scopus 로고    scopus 로고
    • Molecular mechanisms of mammalian global genome nucleotide excision repair
    • Gillet LC, Schärer OD. 2006. Molecular mechanisms of mammalian global genome nucleotide excision repair. Chem Rev 106: 253-276.
    • (2006) Chem Rev , vol.106 , pp. 253-276
    • Gillet, L.C.1    Schärer, O.D.2
  • 41
    • 84869077981 scopus 로고    scopus 로고
    • Nu-cleotide excision repair is associated with the replisome and its efficiency depends on adirect interaction between XPA and PCNA
    • Gilljam KM, Muller R, Liabakk NB, Otterlei M. 2012. Nu-cleotide excision repair is associated with the replisome and its efficiency depends on adirect interaction between XPA and PCNA. PloS ONE 7: e49199.
    • (2012) PloS ONE , vol.7
    • Gilljam, K.M.1    Muller, R.2    Liabakk, N.B.3    Otterlei, M.4
  • 42
    • 33749520485 scopus 로고    scopus 로고
    • Rad4-Rad23 interaction with SWI/SNF links ATP-dependent chromatin remodeling with nucleotide excision repair
    • Gong F, Fahy D, Smerdon MJ. 2006. Rad4-Rad23 interaction with SWI/SNF links ATP-dependent chromatin remodeling with nucleotide excision repair. Nat Struct Mol Biol 13: 902-907.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 902-907
    • Gong, F.1    Fahy, D.2    Smerdon, M.J.3
  • 43
    • 84856699863 scopus 로고    scopus 로고
    • Unpairing and gating: Sequence-independent substrate recognition by FEN superfamily nucleases
    • Grasby JA, Finger LD, Tsutakawa SE, Atack JM, Tainer JA. 2012. Unpairing and gating: Sequence-independent substrate recognition by FEN superfamily nucleases. Trends Biochem Sci 37: 74-84.
    • (2012) Trends Biochem Sci , vol.37 , pp. 74-84
    • Grasby, J.A.1    Finger, L.D.2    Tsutakawa, S.E.3    Atack, J.M.4    Tainer, J.A.5
  • 44
    • 0141530885 scopus 로고    scopus 로고
    • Local action of the chroma-tin assembly factor CAF-1 at sites of nucleotide excision repair in vivo
    • Green CM, Almouzni G. 2003. Local action of the chroma-tin assembly factor CAF-1 at sites of nucleotide excision repair in vivo. EMBO J 22: 5163-5174.
    • (2003) EMBO J , vol.22 , pp. 5163-5174
    • Green, C.M.1    Almouzni, G.2
  • 45
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage
    • Groisman R, Polanowska J, Kuraoka I, Sawada J, Saijo M, Drapkin R, Kisselev AF, Tanaka K, Nakatani Y. 2003. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell 113: 357-367.
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3    Sawada, J.4    Saijo, M.5    Drapkin, R.6    Kisselev, A.F.7    Tanaka, K.8    Nakatani, Y.9
  • 46
    • 48549085044 scopus 로고    scopus 로고
    • The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A
    • Guerrero-Santoro J, Kapetanaki MG, Hsieh CL, Gorbachin-sky I, Levine AS, Rapic-Otrin V. 2008. The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A. Cancer Res 68: 5014-5022.
    • (2008) Cancer Res , vol.68 , pp. 5014-5022
    • Guerrero-Santoro, J.1    Kapetanaki, M.G.2    Hsieh, C.L.3    Gorbachin-Sky, I.4    Levine, A.S.5    Rapic-Otrin, V.6
  • 47
    • 0029840823 scopus 로고    scopus 로고
    • Recognition of DNA adducts by human nucleotide excision repair. Evidence for a thermodynamic probing mechanism
    • Gunz D, Hess MT, Naegeli H. 1996. Recognition of DNA adducts by human nucleotide excision repair. Evidence for a thermodynamic probing mechanism. J Biol Chem 271: 25089-25098.
    • (1996) J Biol Chem , vol.271 , pp. 25089-25098
    • Gunz, D.1    Hess, M.T.2    Naegeli, H.3
  • 48
    • 36148951013 scopus 로고    scopus 로고
    • H2AX phosphorylation after UV irradiation is triggered by DNA repair intermediates and is mediated by the ATR kinase
    • Hanasoge S, Ljungman M. 2007. H2AX phosphorylation after UV irradiation is triggered by DNA repair intermediates and is mediated by the ATR kinase. Carcinogenesis 28: 2298-2304.
    • (2007) Carcinogenesis , vol.28 , pp. 2298-2304
    • Hanasoge, S.1    Ljungman, M.2
  • 49
    • 56749157389 scopus 로고    scopus 로고
    • Transcription-coupled DNA repair: Two decades of progress and surprises
    • Hanawalt PC, Spivak G. 2008. Transcription-coupled DNA repair: Two decades of progress and surprises. Nat Rev Mol Cell Biol 9: 958-970.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 958-970
    • Hanawalt, P.C.1    Spivak, G.2
  • 50
    • 0036785614 scopus 로고    scopus 로고
    • The SWI/SNF chromatin-remod-eling factor stimulates repair by human excision nuclease in the mononucleosome core particle
    • Hara R, Sancar A. 2002. The SWI/SNF chromatin-remod-eling factor stimulates repair by human excision nuclease in the mononucleosome core particle. Mol Cell Biol 22: 6779-6787.
    • (2002) Mol Cell Biol , vol.22 , pp. 6779-6787
    • Hara, R.1    Sancar, A.2
  • 51
    • 0034461931 scopus 로고    scopus 로고
    • DNA damage in the nucleo-some core is refractory to repair by human excision nu-clease
    • Hara R, Mo J, Sancar A. 2000. DNA damage in the nucleo-some core is refractory to repair by human excision nu-clease. Mol Cell Biol 20: 9173-9181.
    • (2000) Mol Cell Biol , vol.20 , pp. 9173-9181
    • Hara, R.1    Mo, J.2    Sancar, A.3
  • 53
    • 0037628995 scopus 로고    scopus 로고
    • Structural determinants for substrate binding and catalysis by the structure-specific endonuclease XPG
    • Hohl M, Thorel F, Clarkson SG, Schärer OD. 2003. Structural determinants for substrate binding and catalysis by the structure-specific endonuclease XPG. J Biol Chem 278: 19500-19508.
    • (2003) J Biol Chem , vol.278 , pp. 19500-19508
    • Hohl, M.1    Thorel, F.2    Clarkson, S.G.3    Schärer, O.D.4
  • 58
    • 0027944087 scopus 로고
    • Substrate spectrum of human excinuclease: Repair of abasic sites, methylated bases, mismatches, and bulky adducts
    • Huang JC, Hsu DS, Kazantsev A, Sancar A. 1994. Substrate spectrum of human excinuclease: Repair of abasic sites, methylated bases, mismatches, and bulky adducts. Proc Natl Acad Sci 91: 12213-12217.
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 12213-12217
    • Huang, J.C.1    Hsu, D.S.2    Kazantsev, A.3    Sancar, A.4
  • 59
    • 34247256517 scopus 로고    scopus 로고
    • XPG stabilizes TFIIH, allowing transactivationofnuclear receptors: Implications for Cockayne syndrome in XP-G/CS patients
    • Ito S, Kuraoka I, Chymkowitch P, Compe E, Takedachi A, Ishigami C, Coin F, Egly JM, Tanaka K. 2007. XPG stabilizes TFIIH, allowing transactivationofnuclear receptors: Implications for Cockayne syndrome in XP-G/CS patients. Mol Cell 26: 231-243.
    • (2007) Mol Cell , vol.26 , pp. 231-243
    • Ito, S.1    Kuraoka, I.2    Chymkowitch, P.3    Compe, E.4    Takedachi, A.5    Ishigami, C.6    Coin, F.7    Egly, J.M.8    Tanaka, K.9
  • 60
    • 78049241459 scopus 로고    scopus 로고
    • INO80 chromatin remodeling complex promotes the removal of UV lesions by the nucleotide excision repair pathway
    • Jiang Y, Wang X, Bao S, Guo R, Johnson DG, Shen X, Li L. 2010. INO80 chromatin remodeling complex promotes the removal of UV lesions by the nucleotide excision repair pathway. Proc Natl Acad Sci 107: 17274-17279.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 17274-17279
    • Jiang, Y.1    Wang, X.2    Bao, S.3    Guo, R.4    Johnson, D.G.5    Shen, X.6    Li, L.7
  • 61
    • 77950422142 scopus 로고    scopus 로고
    • Circadian control of XPA and excision repairof cisplatin-DNA damage by cryptochrome and HERC2 ubiquitin ligase
    • Kang TH, Lindsey-Boltz LA, Reardon JT, Sancar A. 2010. Circadian control of XPA and excision repairof cisplatin-DNA damage by cryptochrome and HERC2 ubiquitin ligase. Proc Natl Acad Sci 107: 4890-4895.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 4890-4895
    • Kang, T.H.1    Lindsey-Boltz, L.A.2    Reardon, J.T.3    Sancar, A.4
  • 62
    • 79955606995 scopus 로고    scopus 로고
    • Regulation of nucle-otide excision repair activity by transcriptional and post-transcriptional control of the XPA protein
    • Kang TH, Reardon JT, Sancar A. 2011. Regulation of nucle-otide excision repair activity by transcriptional and post-transcriptional control of the XPA protein. Nucleic Acids Res 39: 3176-3187.
    • (2011) Nucleic Acids Res , vol.39 , pp. 3176-3187
    • Kang, T.H.1    Reardon, J.T.2    Sancar, A.3
  • 63
    • 33644536070 scopus 로고    scopus 로고
    • The DDB1-CU-L4ADDB2 ubiquitin ligase is deficient in xeroderma pig-mentosum group E and targets histone H2A at UV-dam-aged DNA sites
    • Kapetanaki MG, Guerrero-Santoro J, Bisi DC, Hsieh CL, Rapic-Otrin V, Levine AS. 2006. The DDB1-CU-L4ADDB2 ubiquitin ligase is deficient in xeroderma pig-mentosum group E and targets histone H2A at UV-dam-aged DNA sites. Proc Natl Acad Sci 103: 2588-2593.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 2588-2593
    • Kapetanaki, M.G.1    Guerrero-Santoro, J.2    Bisi, D.C.3    Hsieh, C.L.4    Rapic-Otrin, V.5    Levine, A.S.6
  • 64
    • 84863306922 scopus 로고    scopus 로고
    • Mechanism ofrelease and fate ofexcised oligonucleotides during nucleotide excision repair
    • Kemp MG, Reardon JT, Lindsey-Boltz LA, Sancar A. 2012. Mechanism ofrelease and fate ofexcised oligonucleotides during nucleotide excision repair. J Biol Chem 287: 22889-22899.
    • (2012) J Biol Chem , vol.287 , pp. 22889-22899
    • Kemp, M.G.1    Reardon, J.T.2    Lindsey-Boltz, L.A.3    Sancar, A.4
  • 65
    • 84869218112 scopus 로고    scopus 로고
    • Poly(ADP-ribose) contributes to an association between poly-(ADP-ribose) polymerase-1 and xeroderma pigmento-sum complementation group A in nucleotide excision repair
    • King BS, Cooper KL, Liu KJ, Hudson LG. 2012. Poly(ADP-ribose) contributes to an association between poly-(ADP-ribose) polymerase-1 and xeroderma pigmento-sum complementation group A in nucleotide excision repair. J Biol Chem 287: 39824-39833.
    • (2012) J Biol Chem , vol.287 , pp. 39824-39833
    • King, B.S.1    Cooper, K.L.2    Liu, K.J.3    Hudson, L.G.4
  • 67
    • 78650435945 scopus 로고    scopus 로고
    • Localization of xeroderma pigmento-sum group A protein and replication protein A on damaged DNA in nucleotide excision repair
    • Krasikova YS, Rechkunova NI, Maltseva EA, Petruseva IO, Lavrik OI. 2010. Localization of xeroderma pigmento-sum group A protein and replication protein A on damaged DNA in nucleotide excision repair. Nucleic Acids Res 38: 8083-8094.
    • (2010) Nucleic Acids Res , vol.38 , pp. 8083-8094
    • Krasikova, Y.S.1    Rechkunova, N.I.2    Maltseva, E.A.3    Petruseva, I.O.4    Lavrik, O.I.5
  • 68
    • 84857195289 scopus 로고    scopus 로고
    • Functional and structural studies of the nucleotide excision repair helicase XPD suggest a polarity for DNA translocation
    • Kuper J, Wolski SC, Michels G, Kisker C. 2012. Functional and structural studies of the nucleotide excision repair helicase XPD suggest a polarity for DNA translocation. EMBO J 31: 494-502.
    • (2012) EMBO J , vol.31 , pp. 494-502
    • Kuper, J.1    Wolski, S.C.2    Michels, G.3    Kisker, C.4
  • 69
    • 84856278412 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling in the DNA-damage response
    • Lans H, Marteijn JA, Vermeulen W. 2012. ATP-dependent chromatin remodeling in the DNA-damage response. Epigenetics Chromatin 5: 4.
    • (2012) Epigenetics Chromatin , vol.5 , pp. 4
    • Lans, H.1    Marteijn, J.A.2    Vermeulen, W.3
  • 71
    • 0942268166 scopus 로고    scopus 로고
    • DNA repair-deficient diseases, xeroder-ma pigmentosum, Cockayne syndrome and trichothio-dystrophy
    • Lehmann AR. 2003. DNA repair-deficient diseases, xeroder-ma pigmentosum, Cockayne syndrome and trichothio-dystrophy. Biochimie 85: 1101-1111.
    • (2003) Biochimie , vol.85 , pp. 1101-1111
    • Lehmann, A.R.1
  • 72
    • 79960347948 scopus 로고    scopus 로고
    • DNA polymerases and repair synthesis in NER in human cells
    • Lehmann AR. 2011. DNA polymerases and repair synthesis in NER in human cells. DNA Repair 10: 730-733.
    • (2011) DNA Repair , vol.10 , pp. 730-733
    • Lehmann, A.R.1
  • 74
    • 0029129283 scopus 로고
    • An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair
    • Li L, Lu X, Peterson CA, Legerski RJ. 1995a. An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair. Mol Cell Biol 15: 5396-5402.
    • (1995) Mol Cell Biol , vol.15 , pp. 5396-5402
    • Li, L.1    Lu, X.2    Peterson, C.A.3    Legerski, R.J.4
  • 75
    • 0028934368 scopus 로고
    • Mutations in XPA that prevent association with ERCC1 are defective in nucleotide excision repair
    • Li L, Peterson CA, Lu X, Legerski RJ. 1995b. Mutations in XPA that prevent association with ERCC1 are defective in nucleotide excision repair. Mol Cell Biol 15: 1993-1998.
    • (1995) Mol Cell Biol , vol.15 , pp. 1993-1998
    • Li, L.1    Peterson, C.A.2    Lu, X.3    Legerski, R.J.4
  • 77
    • 79960372834 scopus 로고    scopus 로고
    • Probing for DNA damage with beta-hairpins: Similarities in incision efficiencies of bulky DNA adducts by prokaryotic and human nucleotide excision repair systems in vitro
    • Liu Y, Reeves D, Kropachev K, Cai Y, Ding S, Kolbanovskiy M, Kolbanovskiy A, Bolton JL, Broyde S, Van Houten B, et al. 2011. Probing for DNA damage with beta-hairpins: Similarities in incision efficiencies of bulky DNA adducts by prokaryotic and human nucleotide excision repair systems in vitro. DNA Repair (Amst) 10: 684-696.
    • (2011) DNA Repair (Amst) , vol.10 , pp. 684-696
    • Liu, Y.1    Reeves, D.2    Kropachev, K.3    Cai, Y.4    Ding, S.5    Kolbanovskiy, M.6    Kolbanovskiy, A.7    Bolton, J.L.8    Broyde, S.9    van Houten, B.10
  • 79
    • 34247381126 scopus 로고    scopus 로고
    • An aromatic sensor with aversion to damaged strands confers versatility to DNA repair
    • Maillard O, Solyom S, Naegeli H. 2007. An aromatic sensor with aversion to damaged strands confers versatility to DNA repair. PLoS Biol 5: e79.
    • (2007) PLoS Biol , vol.5
    • Maillard, O.1    Solyom, S.2    Naegeli, H.3
  • 82
    • 33745607326 scopus 로고    scopus 로고
    • H2AX phosphorylation within the G1 phase after UV irradiation depends on nucleotide excision repair and not DNA double-strand breaks
    • Marti TM, Hefner E, Feeney L, Natale V, Cleaver JE. 2006. H2AX phosphorylation within the G1 phase after UV irradiation depends on nucleotide excision repair and not DNA double-strand breaks. Proc Natl Acad Sci 103: 9891-9896.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 9891-9896
    • Marti, T.M.1    Hefner, E.2    Feeney, L.3    Natale, V.4    Cleaver, J.E.5
  • 83
    • 78049274322 scopus 로고    scopus 로고
    • Strand- and site-specific DNA lesion demarcation by the xeroderma pigmentosum group D helicase
    • Mathieu N, Kaczmarek N, Naegeli H. 2010. Strand- and site-specific DNA lesion demarcation by the xeroderma pigmentosum group D helicase. Proc Natl Acad Sci 107: 17545-17550.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 17545-17550
    • Mathieu, N.1    Kaczmarek, N.2    Naegeli, H.3
  • 84
    • 84873408109 scopus 로고    scopus 로고
    • DNA quality control by a lesion sensor pocket of the xeroderma pigmentosum group Dhelicase subunit of TFIIH
    • Mathieu N, Kaczmarek N, Ruthemann P, Luch A, Naegeli H. 2013. DNA quality control by a lesion sensor pocket of the xeroderma pigmentosum group Dhelicase subunit of TFIIH. Curr Biol 23: 204-212.
    • (2013) Curr Biol , vol.23 , pp. 204-212
    • Mathieu, N.1    Kaczmarek, N.2    Ruthemann, P.3    Luch, A.4    Naegeli, H.5
  • 87
    • 34948892722 scopus 로고    scopus 로고
    • Recognition of DNA damage by the Rad4 nucleotide excision repair protein
    • Min JH, Pavletich NP. 2007. Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature 449: 570-575.
    • (2007) Nature , vol.449 , pp. 570-575
    • Min, J.H.1    Pavletich, N.P.2
  • 88
    • 0035796455 scopus 로고    scopus 로고
    • Double-check probing of DNA bending and unwinding by XPA-RPA: An architectural function in DNA repair
    • Missura M, Buterin T, Hindges R, Hubscher U, Kasparkova J, Brabec V, Naegeli H. 2001. Double-check probing of DNA bending and unwinding by XPA-RPA: An architectural function in DNA repair. Embo J 20: 3554-3564.
    • (2001) Embo J , vol.20 , pp. 3554-3564
    • Missura, M.1    Buterin, T.2    Hindges, R.3    Hubscher, U.4    Kasparkova, J.5    Brabec, V.6    Naegeli, H.7
  • 90
    • 38049000832 scopus 로고    scopus 로고
    • Sequential recruitment of the repair factors during NER: The role of XPG in initiating the resynthesis step
    • Mocquet V, Laine JP, Riedl T, Yajin Z, Lee MY, Egly JM. 2008. Sequential recruitment of the repair factors during NER: The role of XPG in initiating the resynthesis step. EMBO J 27: 155-167.
    • (2008) EMBO J , vol.27 , pp. 155-167
    • Mocquet, V.1    Laine, J.P.2    Riedl, T.3    Yajin, Z.4    Lee, M.Y.5    Egly, J.M.6
  • 91
    • 34447302016 scopus 로고    scopus 로고
    • Sealing of chromosomal DNA nicks during nucleotide excision repair requires XRCC1 and DNA ligase III a in a cell-cycle-specific manner
    • Moser J, Kool H, Giakzidis I, Caldecott K, Mullenders LH, Fousteri MI. 2007. Sealing of chromosomal DNA nicks during nucleotide excision repair requires XRCC1 and DNA ligase III a in a cell-cycle-specific manner. Mol Cell 27: 311-323.
    • (2007) Mol Cell , vol.27 , pp. 311-323
    • Moser, J.1    Kool, H.2    Giakzidis, I.3    Caldecott, K.4    Mullenders, L.H.5    Fousteri, M.I.6
  • 92
    • 0028896837 scopus 로고
    • Reconstitution of human DNA repair excision nuclease in a highly defined system
    • Mu D, Park CH, Matsunaga T, Hsu DS, Reardon JT, Sancar A. 1995. Reconstitution of human DNA repair excision nuclease in a highly defined system. J Biol Chem 270: 2415-2418.
    • (1995) J Biol Chem , vol.270 , pp. 2415-2418
    • Mu, D.1    Park, C.H.2    Matsunaga, T.3    Hsu, D.S.4    Reardon, J.T.5    Sancar, A.6
  • 93
    • 84868133144 scopus 로고    scopus 로고
    • Nucle-otide excision repair of 2-acetylaminofluorene- and 2-aminofluorene-(C8)-guanine adducts: Molecular dynamics simulations elucidate how lesion structure and base sequence context impact repair efficiencies
    • Mu H, Kropachev K, Wang L, Zhang L, Kolbanovskiy A, Kolbanovskiy M, Geacintov NE, Broyde S. 2012. Nucle-otide excision repair of 2-acetylaminofluorene- and 2-aminofluorene-(C8)-guanine adducts: Molecular dynamics simulations elucidate how lesion structure and base sequence context impact repair efficiencies. Nucleic Acids Res 40: 9675-9690.
    • (2012) Nucleic Acids Res , vol.40 , pp. 9675-9690
    • Mu, H.1    Kropachev, K.2    Wang, L.3    Zhang, L.4    Kolbanovskiy, A.5    Kolbanovskiy, M.6    Geacintov, N.E.7    Broyde, S.8
  • 94
    • 0026536763 scopus 로고
    • The DNA heli-case and adenosine triphosphatase activities of yeast Rad3 protein are inhibited by DNA damage. A potential mechanism for damage-specific recognition
    • Naegeli H, Bardwell L, Friedberg EC. 1992. The DNA heli-case and adenosine triphosphatase activities of yeast Rad3 protein are inhibited by DNA damage. A potential mechanism for damage-specific recognition. J Biol Chem 267: 392-398.
    • (1992) J Biol Chem , vol.267 , pp. 392-398
    • Naegeli, H.1    Bardwell, L.2    Friedberg, E.C.3
  • 95
    • 0038339144 scopus 로고    scopus 로고
    • A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pig-mentosum group C protein
    • Ng JM, Vermeulen W, van der Horst GT, Bergink S, Suga-sawa K, Vrieling H, Hoeijmakers JH. 2003. A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pig-mentosum group C protein. Genes Dev 17: 1630-1645.
    • (2003) Genes Dev , vol.17 , pp. 1630-1645
    • Ng, J.M.1    Vermeulen, W.2    van der Horst, G.T.3    Bergink, S.4    Suga-Sawa, K.5    Vrieling, H.6    Hoeijmakers, J.H.7
  • 96
    • 20744446570 scopus 로고    scopus 로고
    • Centrin 2 stimulates nu-cleotide excision repair by interacting with xeroderma pigmentosum group C protein
    • Nishi R, Okuda Y, Watanabe E, Mori T, Iwai S, Masutani C, Sugasawa K, Hanaoka F. 2005. Centrin 2 stimulates nu-cleotide excision repair by interacting with xeroderma pigmentosum group C protein. Mol Cell Biol 25: 5664-5674.
    • (2005) Mol Cell Biol , vol.25 , pp. 5664-5674
    • Nishi, R.1    Okuda, Y.2    Watanabe, E.3    Mori, T.4    Iwai, S.5    Masutani, C.6    Sugasawa, K.7    Hanaoka, F.8
  • 98
    • 0030817140 scopus 로고    scopus 로고
    • DNA damage recognition by XPA protein promotes efficient recruitment of transcription factor II H
    • Nocentini S, Coin F, Saijo M, Tanaka K, Egly JM. 1997. DNA damage recognition by XPA protein promotes efficient recruitment of transcription factor II H. J Biol Chem 272: 22991-22994.
    • (1997) J Biol Chem , vol.272 , pp. 22991-22994
    • Nocentini, S.1    Coin, F.2    Saijo, M.3    Tanaka, K.4    Egly, J.M.5
  • 100
    • 33744789415 scopus 로고    scopus 로고
    • The Y-family DNA polymerase kappa (pol k) functions in mammalian nucleotide-exci-sion repair
    • Ogi T, Lehmann AR. 2006. The Y-family DNA polymerase kappa (pol k) functions in mammalian nucleotide-exci-sion repair. Nat Cell Biol 8: 640-642.
    • (2006) Nat Cell Biol , vol.8 , pp. 640-642
    • Ogi, T.1    Lehmann, A.R.2
  • 102
    • 70350566800 scopus 로고    scopus 로고
    • Molecular insights into the recruitment of TFIIH to sites of DNA damage
    • Oksenych V, de Jesus BB, Zhovmer A, Egly JM, Coin F. 2009. Molecular insights into the recruitment of TFIIH to sites of DNA damage. EMBO J 28: 2971-2980.
    • (2009) EMBO J , vol.28 , pp. 2971-2980
    • Oksenych, V.1    de Jesus, B.B.2    Zhovmer, A.3    Egly, J.M.4    Coin, F.5
  • 103
    • 79953838905 scopus 로고    scopus 로고
    • Structures of human exonu-clease 1 DNA complexes suggest a unified mechanism for nuclease family
    • Orans J, McSweeney EA, Iyer RR, Hast MA, Hellinga HW, Modrich P, Beese LS. 2011. Structures of human exonu-clease 1 DNA complexes suggest a unified mechanism for nuclease family. Cell 145: 212-223.
    • (2011) Cell , vol.145 , pp. 212-223
    • Orans, J.1    McSweeney, E.A.2    Iyer, R.R.3    Hast, M.A.4    Hellinga, H.W.5    Modrich, P.6    Beese, L.S.7
  • 106
    • 0028932889 scopus 로고
    • The general transcription-repair factor TFIIH is recruited to the excision repair complex by the XPA protein independent of the TFIIE transcription factor
    • Park CH, Mu D, Reardon JT, Sancar A. 1995. The general transcription-repair factor TFIIH is recruited to the excision repair complex by the XPA protein independent of the TFIIE transcription factor. J Biol Chem 270: 4896-4902.
    • (1995) J Biol Chem , vol.270 , pp. 4896-4902
    • Park, C.H.1    Mu, D.2    Reardon, J.T.3    Sancar, A.4
  • 107
    • 0037013193 scopus 로고    scopus 로고
    • Xeroderma pigmentosum complementation group A protein (XPA) modulates RPA-DNA interactions via enhanced complex stability and inhibition of strand separation activity
    • Patrick SM, Turchi JJ. 2002. Xeroderma pigmentosum complementation group A protein (XPA) modulates RPA-DNA interactions via enhanced complex stability and inhibition of strand separation activity. J Biol Chem 277: 16096-16101.
    • (2002) J Biol Chem , vol.277 , pp. 16096-16101
    • Patrick, S.M.1    Turchi, J.J.2
  • 108
    • 84883797029 scopus 로고    scopus 로고
    • Nucleosome dynamics as modular systems that integrate DNA damage and repair
    • doi: 10.1101/cshper-spect.a012658
    • Peterson CL, Almouzni G. 2013. Nucleosome dynamics as modular systems that integrate DNA damage and repair. Cold Spring Harb Perspect Biol doi: 10.1101/cshper-spect.a012658.
    • (2013) Cold Spring Harb Perspect Biol
    • Peterson, C.L.1    Almouzni, G.2
  • 109
    • 0000830740 scopus 로고
    • Evidence for repair-replication of ultraviolet damaged DNA in bacteria
    • Pettijohn D, Hanawalt P. 1964. Evidence for repair-replication of ultraviolet damaged DNA in bacteria. J Mol Biol 9: 395-410.
    • (1964) J Mol Biol , vol.9 , pp. 395-410
    • Pettijohn, D.1    Hanawalt, P.2
  • 111
    • 33750449326 scopus 로고    scopus 로고
    • New histone incorporation marks sites of UV repair in human cells
    • Polo SE, Roche D, Almouzni G. 2006. New histone incorporation marks sites of UV repair in human cells. Cell 127: 481-493.
    • (2006) Cell , vol.127 , pp. 481-493
    • Polo, S.E.1    Roche, D.2    Almouzni, G.3
  • 112
    • 0034733496 scopus 로고    scopus 로고
    • Nucleotide excision repair in yeast
    • Prakash S, Prakash L. 2000. Nucleotide excision repair in yeast. Mutat Res 451: 13-24.
    • (2000) Mutat Res , vol.451 , pp. 13-24
    • Prakash, S.1    Prakash, L.2
  • 113
    • 84857194573 scopus 로고    scopus 로고
    • Regulation of transloca-tion polarity by helicase domain 1 in SF2B helicases
    • Pugh RA, Wu CG, Spies M. 2012. Regulation of transloca-tion polarity by helicase domain 1 in SF2B helicases. EMBO J 31: 503-514.
    • (2012) EMBO J , vol.31 , pp. 503-514
    • Pugh, R.A.1    Wu, C.G.2    Spies, M.3
  • 115
    • 3042703022 scopus 로고    scopus 로고
    • Identification ofTFB5,anew componentof general transcription and DNA repair factor IIH
    • Ranish JA, Hahn S, Lu Y, Yi EC, Li XJ, Eng J, Aebersold R. 2004. Identification ofTFB5,anew componentof general transcription and DNA repair factor IIH. Nat Genet 36: 707-713.
    • (2004) Nat Genet , vol.36 , pp. 707-713
    • Ranish, J.A.1    Hahn, S.2    Lu, Y.3    Yi, E.C.4    Li, X.J.5    Eng, J.6    Aebersold, R.7
  • 116
    • 0001186415 scopus 로고
    • Evidence for repair of ultra-violet damaged deoxyribonucleic acid in cultured mammalian cells
    • Rasmussen RE, Painter RB. 1964. Evidence for repair of ultra-violet damaged deoxyribonucleic acid in cultured mammalian cells. Nature 203: 1360-1362.
    • (1964) Nature , vol.203 , pp. 1360-1362
    • Rasmussen, R.E.1    Painter, R.B.2
  • 117
    • 71949103959 scopus 로고    scopus 로고
    • Human SNF5/INI1, acomponent of the human SWI/SNF chromatin remodeling complex, promotes nucleotide excision repair by influencing ATM recruitment and downstream H2AX phosphorylation
    • Ray A, Mir SN, Wani G, Zhao Q, Battu A, Zhu Q, Wang QE, Wani AA. 2009. Human SNF5/INI1, acomponent of the human SWI/SNF chromatin remodeling complex, promotes nucleotide excision repair by influencing ATM recruitment and downstream H2AX phosphorylation. Mol Cell Biol 29: 6206-6219.
    • (2009) Mol Cell Biol , vol.29 , pp. 6206-6219
    • Ray, A.1    Mir, S.N.2    Wani, G.3    Zhao, Q.4    Battu, A.5    Zhu, Q.6    Wang, Q.E.7    Wani, A.A.8
  • 118
    • 0142059994 scopus 로고    scopus 로고
    • Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease
    • Reardon JT, Sancar A. 2003. Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease. Genes Dev 17: 2539-2551.
    • (2003) Genes Dev , vol.17 , pp. 2539-2551
    • Reardon, J.T.1    Sancar, A.2
  • 119
    • 0141753120 scopus 로고    scopus 로고
    • The comings and goings of nucleotide excision repair factors on damaged DNA
    • Riedl T, Hanaoka F, Egly JM. 2003. The comings and goings of nucleotide excision repair factors on damaged DNA. Embo J 22: 5293-5303.
    • (2003) Embo J , vol.22 , pp. 5293-5303
    • Riedl, T.1    Hanaoka, F.2    Egly, J.M.3
  • 120
    • 84873130772 scopus 로고    scopus 로고
    • Role of poly(ADP-ribose) polymerase-1in the removal of UV-induced DNA lesions by nucleotide excision repair
    • Robu M, Shah RG, Petitclerc N, Brind'Amour J, Kandan-Kulangara F, Shah GM. 2013. Role of poly(ADP-ribose) polymerase-1in the removal of UV-induced DNA lesions by nucleotide excision repair. Proc Natl Acad Sci 110: 1658-1663.
    • (2013) Proc Natl Acad Sci , vol.110 , pp. 1658-1663
    • Robu, M.1    Shah, R.G.2    Petitclerc, N.3    Brind'Amour, J.4    Kandan-Kulangara, F.5    Shah, G.M.6
  • 121
    • 79953153739 scopus 로고    scopus 로고
    • Nucleotide excision repair by mutant xeroderma pigmentosum group A (XPA) proteins with deficiency in interaction with RPA
    • Saijo M, Takedachi A, Tanaka K. 2011. Nucleotide excision repair by mutant xeroderma pigmentosum group A (XPA) proteins with deficiency in interaction with RPA. J Biol Chem 286: 5476-5483.
    • (2011) J Biol Chem , vol.286 , pp. 5476-5483
    • Saijo, M.1    Takedachi, A.2    Tanaka, K.3
  • 122
    • 78650089978 scopus 로고    scopus 로고
    • The Ino80 chromatin-remodeling complex restores chromatin structure during UV DNA damage repair
    • Sarkar S, Kiely R, McHugh PJ. 2010. The Ino80 chromatin-remodeling complex restores chromatin structure during UV DNA damage repair. J Cell Biol 191: 1061-1068.
    • (2010) J Cell Biol , vol.191 , pp. 1061-1068
    • Sarkar, S.1    Kiely, R.2    McHugh, P.J.3
  • 125
    • 80051961183 scopus 로고    scopus 로고
    • Human exonuclease 1 connects nucleotide excision repair (NER) processing with checkpoint activation in response to UV irradiation
    • Sertic S, Pizzi S, Cloney R, Lehmann AR, Marini F, Plevani P, Muzi-Falconi M. 2011. Human exonuclease 1 connects nucleotide excision repair (NER) processing with checkpoint activation in response to UV irradiation. Proc Natl Acad Sci 108: 13647-13652.
    • (2011) Proc Natl Acad Sci , vol.108 , pp. 13647-13652
    • Sertic, S.1    Pizzi, S.2    Cloney, R.3    Lehmann, A.R.4    Marini, F.5    Plevani, P.6    Muzi-Falconi, M.7
  • 126
    • 78651191735 scopus 로고
    • The disappearanceof thymine dimers from DNA: An error-correcting mechanism
    • Setlow RB, Carrier WL. 1964. The disappearanceof thymine dimers from DNA: An error-correcting mechanism. Proc Natl Acad Sci 51: 226-231.
    • (1964) Proc Natl Acad Sci , vol.51 , pp. 226-231
    • Setlow, R.B.1    Carrier, W.L.2
  • 127
    • 0028965151 scopus 로고
    • Nu-cleotide excision repair DNA synthesis by DNA polymer-ase epsilon in the presence of PCNA, RFC, and RPA
    • Shivji MK, Podust VN, Hubscher U, Wood RD. 1995. Nu-cleotide excision repair DNA synthesis by DNA polymer-ase epsilon in the presence of PCNA, RFC, and RPA. Biochemistry 34: 5011-5017.
    • (1995) Biochemistry , vol.34 , pp. 5011-5017
    • Shivji, M.K.1    Podust, V.N.2    Hubscher, U.3    Wood, R.D.4
  • 128
    • 0018125018 scopus 로고
    • Nucleosome rearrangement in human chromatin during UV-induced DNA-reapir [sic] synthesis
    • Smerdon MJ, Lieberman MW. 1978. Nucleosome rearrangement in human chromatin during UV-induced DNA-reapir [sic] synthesis. Proc Natl Acad Sci 75: 4238-4241.
    • (1978) Proc Natl Acad Sci , vol.75 , pp. 4238-4241
    • Smerdon, M.J.1    Lieberman, M.W.2
  • 132
    • 0035282109 scopus 로고    scopus 로고
    • A multistep damage recognition mechanism for global genomic nucleotide excision repair
    • Sugasawa K, Okamoto T, Shimizu Y, Masutani C, Iwai S, Hanaoka F. 2001. A multistep damage recognition mechanism for global genomic nucleotide excision repair. Genes Dev 15: 507-521.
    • (2001) Genes Dev , vol.15 , pp. 507-521
    • Sugasawa, K.1    Okamoto, T.2    Shimizu, Y.3    Masutani, C.4    Iwai, S.5    Hanaoka, F.6
  • 133
    • 0036012799 scopus 로고    scopus 로고
    • A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex
    • Sugasawa K, Shimizu Y, Iwai S, Hanaoka F. 2002. A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex. DNA Repair (Amst) 1: 95-107.
    • (2002) DNA Repair (Amst) , vol.1 , pp. 95-107
    • Sugasawa, K.1    Shimizu, Y.2    Iwai, S.3    Hanaoka, F.4
  • 135
    • 70449717367 scopus 로고    scopus 로고
    • Two-step recognition of DNA damage for mammalian nucle-otide excision repair: Directional binding of the XPC complex and DNA strand scanning
    • Sugasawa K, Akagi J, Nishi R, Iwai S, Hanaoka F. 2009. Two-step recognition of DNA damage for mammalian nucle-otide excision repair: Directional binding of the XPC complex and DNA strand scanning. Mol Cell 36: 642-653.
    • (2009) Mol Cell , vol.36 , pp. 642-653
    • Sugasawa, K.1    Akagi, J.2    Nishi, R.3    Iwai, S.4    Hanaoka, F.5
  • 137
    • 0033636515 scopus 로고    scopus 로고
    • Xeroderma pigmentosum p48 gene enhances global ge-nomic repair and suppresses UV-induced mutagenesis
    • Tang JY, Hwang BJ, Ford JM, Hanawalt PC, Chu G. 2000. Xeroderma pigmentosum p48 gene enhances global ge-nomic repair and suppresses UV-induced mutagenesis. Mol Cell 5: 737-744.
    • (2000) Mol Cell , vol.5 , pp. 737-744
    • Tang, J.Y.1    Hwang, B.J.2    Ford, J.M.3    Hanawalt, P.C.4    Chu, G.5
  • 139
    • 80052320934 scopus 로고    scopus 로고
    • Slowly progressing nucleotide excision repair in trichothiodystrophy group A patient fibroblasts
    • Theil AF, Nonnekens J, Wijgers N, Vermeulen W, Giglia-Mari G. 2011. Slowly progressing nucleotide excision repair in trichothiodystrophy group A patient fibroblasts. Mol Cell Biol 31: 3630-3638.
    • (2011) Mol Cell Biol , vol.31 , pp. 3630-3638
    • Theil, A.F.1    Nonnekens, J.2    Wijgers, N.3    Vermeulen, W.4    Giglia-Mari, G.5
  • 141
    • 0032128265 scopus 로고    scopus 로고
    • Chinese hamster cells meet DNA repair: An entirely acceptable affair
    • Thompson LH. 1998. Chinese hamster cells meet DNA repair: An entirely acceptable affair. Bioessays 20: 589-597.
    • (1998) Bioessays , vol.20 , pp. 589-597
    • Thompson, L.H.1
  • 142
    • 34848864364 scopus 로고    scopus 로고
    • Analysis of the XPA and ssDNA-binding surfaceson the central domain ofhuman ERCC1 reveals evidence for subfunctionalization
    • Tripsianes K, Folkers GE, Zheng C, Das D, Grinstead JS, Kaptein R, Boelens R. 2007. Analysis of the XPA and ssDNA-binding surfaceson the central domain ofhuman ERCC1 reveals evidence for subfunctionalization. Nucleic Acids Res 35: 5789-5798.
    • (2007) Nucleic Acids Res , vol.35 , pp. 5789-5798
    • Tripsianes, K.1    Folkers, G.E.2    Zheng, C.3    Das, D.4    Grinstead, J.S.5    Kaptein, R.6    Boelens, R.7
  • 146
    • 0035901558 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling facilitates nucleotide excision repair of UV-induced DNA lesions in synthetic dinucleo-somes
    • Ura K, Araki M, Saeki H, Masutani C, Ito T, Iwai S, Mizu-koshi T, Kaneda Y, Hanaoka F. 2001. ATP-dependent chromatin remodeling facilitates nucleotide excision repair of UV-induced DNA lesions in synthetic dinucleo-somes. EMBO J 20: 2004-2014.
    • (2001) EMBO J , vol.20 , pp. 2004-2014
    • Ura, K.1    Araki, M.2    Saeki, H.3    Masutani, C.4    Ito, T.5    Iwai, S.6    Mizu-Koshi, T.7    Kaneda, Y.8    Hanaoka, F.9
  • 150
    • 0032499719 scopus 로고    scopus 로고
    • Assembly, subunit composition, and footprint of human DNA repair excision nu-clease
    • Wakasugi M, Sancar A. 1998. Assembly, subunit composition, and footprint of human DNA repair excision nu-clease. Proc Natl Acad Sci 95: 6669-6674.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 6669-6674
    • Wakasugi, M.1    Sancar, A.2
  • 151
    • 0030941340 scopus 로고    scopus 로고
    • The non-catalytic function of XPG protein during dual incision in human nucleotide excision repair
    • Wakasugi M, Reardon JT, Sancar A. 1997. The non-catalytic function of XPG protein during dual incision in human nucleotide excision repair. J Biol Chem 272: 16030-16034.
    • (1997) J Biol Chem , vol.272 , pp. 16030-16034
    • Wakasugi, M.1    Reardon, J.T.2    Sancar, A.3
  • 152
    • 0035805554 scopus 로고    scopus 로고
    • Damaged DNA-binding protein DDB stimulates the excision of cyclobutane pyrimidine dimers in vitro in concert with XPA and replication protein A
    • Wakasugi M, Shimizu M, Morioka H, Linn S, Nikaido O, Matsunaga T. 2001. Damaged DNA-binding protein DDB stimulates the excision of cyclobutane pyrimidine dimers in vitro in concert with XPA and replication protein A. J Biol Chem 276: 15434-15440.
    • (2001) J Biol Chem , vol.276 , pp. 15434-15440
    • Wakasugi, M.1    Shimizu, M.2    Morioka, H.3    Linn, S.4    Nikaido, O.5    Matsunaga, T.6
  • 153
    • 0037127293 scopus 로고    scopus 로고
    • DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair
    • Wakasugi M, Kawashima A, Morioka H, Linn S, Sancar A, Mori T, Nikaido O, Matsunaga T.2002. DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair. J Biol Chem 277: 1637-1640.
    • (2002) J Biol Chem , vol.277 , pp. 1637-1640
    • Wakasugi, M.1    Kawashima, A.2    Morioka, H.3    Linn, S.4    Sancar, A.5    Mori, T.6    Nikaido, O.7    Matsunaga, T.8
  • 155
    • 33744781568 scopus 로고    scopus 로고
    • Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage
    • Wang H, Zhai L, Xu J, Joo HY, Jackson S, Erdjument-Brom-age H, Tempst P, Xiong Y, Zhang Y. 2006. Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol Cell 22: 383-394.
    • (2006) Mol Cell , vol.22 , pp. 383-394
    • Wang, H.1    Zhai, L.2    Xu, J.3    Joo, H.Y.4    Jackson, S.5    Erdjument-Brom-age, H.6    Tempst, P.7    Xiong, Y.8    Zhang, Y.9
  • 157
    • 28944440380 scopus 로고    scopus 로고
    • DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane py-rimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA
    • Winkler GS, Araujo SJ, Fiedler U, Vermeulen W, Coin F, Egly JM, Hoeijmakers JH, Wittschieben BO, Iwai S, Wood RD. 2005. DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane py-rimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA. J Biol Chem 280: 39982-39989.
    • (2005) J Biol Chem , vol.280 , pp. 39982-39989
    • Winkler, G.S.1    Araujo, S.J.2    Fiedler, U.3    Vermeulen, W.4    Coin, F.5    Egly, J.M.6    Hoeijmakers, J.H.7    Wittschieben, B.O.8    Iwai, S.9    Wood, R.D.10
  • 159
    • 0023878893 scopus 로고
    • Complementation of the xeroderma pigmentosum DNA repair defect in cell-free extracts
    • Wood RD, Robins P, Lindahl T. 1988. Complementation of the xeroderma pigmentosum DNA repair defect in cell-free extracts. Cell 53: 97-106.
    • (1988) Cell , vol.53 , pp. 97-106
    • Wood, R.D.1    Robins, P.2    Lindahl, T.3
  • 161
    • 84869407113 scopus 로고    scopus 로고
    • The efficiencies of damage recognition and excision correlate with duplex destabilization induced by acetylamino-fluorene adducts in human nucleotide excision repair
    • Yeo JE, Khoo A, Fagbemi AF, Scharer OD. 2012. The efficiencies of damage recognition and excision correlate with duplex destabilization induced by acetylamino-fluorene adducts in human nucleotide excision repair. Chem Res Toxicol 25: 2462-2468.
    • (2012) Chem Res Toxicol , vol.25 , pp. 2462-2468
    • Yeo, J.E.1    Khoo, A.2    Fagbemi, A.F.3    Scharer, O.D.4
  • 162
    • 0034737426 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA
    • Yokoi M, Masutani C, Maekawa T, Sugasawa K, Ohkuma Y, Hanaoka F. 2000. The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA. J Biol Chem 275: 9870-9875.
    • (2000) J Biol Chem , vol.275 , pp. 9870-9875
    • Yokoi, M.1    Masutani, C.2    Maekawa, T.3    Sugasawa, K.4    Ohkuma, Y.5    Hanaoka, F.6
  • 163
    • 0037470239 scopus 로고    scopus 로고
    • Biochemical analysis of the damage recognition process in nucleotide excision repair
    • You JS, Wang M, Lee SH. 2003. Biochemical analysis of the damage recognition process in nucleotide excision repair. J Biol Chem 278: 7476-7485.
    • (2003) J Biol Chem , vol.278 , pp. 7476-7485
    • You, J.S.1    Wang, M.2    Lee, S.H.3
  • 164
    • 71049159100 scopus 로고    scopus 로고
    • Modulation of nucleotide excision repair by mammalian SWI/SNF chromatin-remodeling complex
    • Zhao Q, Wang QE, Ray A, Wani G, Han C, Milum K, Wani AA. 2009. Modulation of nucleotide excision repair by mammalian SWI/SNF chromatin-remodeling complex. J Biol Chem 284: 30424-30432.
    • (2009) J Biol Chem , vol.284 , pp. 30424-30432
    • Zhao, Q.1    Wang, Q.E.2    Ray, A.3    Wani, G.4    Han, C.5    Milum, K.6    Wani, A.A.7
  • 166
    • 0037567268 scopus 로고    scopus 로고
    • Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
    • Zou L, Elledge SJ. 2003. Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes. Science 300: 1542-1548.
    • (2003) Science , vol.300 , pp. 1542-1548
    • Zou, L.1    Elledge, S.J.2


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