메뉴 건너뛰기




Volumn 72, Issue 11, 2015, Pages 2177-2186

Orchestral maneuvers at the damaged sites in nucleotide excision repair

Author keywords

DDB2; TFIIH; XPA; XPC

Indexed keywords

DNA; DNA BINDING PROTEIN; TRANSCRIPTION FACTOR IIH; XERODERMA PIGMENTOSUM GROUP A PROTEIN; XPA PROTEIN, HUMAN; XPC PROTEIN, HUMAN;

EID: 84938089003     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-015-1859-5     Document Type: Article
Times cited : (30)

References (94)
  • 1
    • 84904642416 scopus 로고    scopus 로고
    • Understanding nucleotide excision repair and its roles in cancer and ageing
    • 1:CAS:528:DC%2BC2cXhtVaisL7I 24954209
    • Marteijn JA, Lans H, Vermeulen W, Hoeijmakers JH (2014) Understanding nucleotide excision repair and its roles in cancer and ageing. Nat Rev Mol Cell Biol 15:465-481
    • (2014) Nat Rev Mol Cell Biol , vol.15 , pp. 465-481
    • Marteijn, J.A.1    Lans, H.2    Vermeulen, W.3    Hoeijmakers, J.H.4
  • 3
    • 0035804828 scopus 로고    scopus 로고
    • Diversity of the damage recognition step in the global genomic nucleotide excision repair in vitro
    • 1:CAS:528:DC%2BD3MXitVOksLY%3D 11267833
    • Kusumoto R et al (2001) Diversity of the damage recognition step in the global genomic nucleotide excision repair in vitro. Mutat Res 485:219-227
    • (2001) Mutat Res , vol.485 , pp. 219-227
    • Kusumoto, R.1
  • 4
    • 0035282109 scopus 로고    scopus 로고
    • A multistep damage recognition mechanism for global genomic nucleotide excision repair
    • 312644 1:CAS:528:DC%2BD3MXhvVChsrc%3D 11238373
    • Sugasawa K et al (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
  • 5
    • 75149126423 scopus 로고    scopus 로고
    • Photo-cross-linking of XPC-Rad23B to cisplatin-damaged DNA reveals contacts with both strands of the DNA duplex and spans the DNA adduct
    • 2811759 1:CAS:528:DC%2BC3cXhtFGhsw%3D%3D 20028083
    • Neher TM, Rechkunova NI, Lavrik OI, Turchi JJ (2010) Photo-cross-linking of XPC-Rad23B to cisplatin-damaged DNA reveals contacts with both strands of the DNA duplex and spans the DNA adduct. Biochemistry 49:669-678
    • (2010) Biochemistry , vol.49 , pp. 669-678
    • Neher, T.M.1    Rechkunova, N.I.2    Lavrik, O.I.3    Turchi, J.J.4
  • 6
    • 84902103235 scopus 로고    scopus 로고
    • The relationships between XPC binding to conformationally diverse DNA adducts and their excision by the human NER system: Is there a correlation?
    • 1:CAS:528:DC%2BC2cXntFGhur8%3D
    • Lee YC et al (2014) The relationships between XPC binding to conformationally diverse DNA adducts and their excision by the human NER system: is there a correlation? DNA Repair (Amst) 19:55-63
    • (2014) DNA Repair (Amst) , vol.19 , pp. 55-63
    • Lee, Y.C.1
  • 7
    • 84899802515 scopus 로고    scopus 로고
    • Structural basis for the recognition of diastereomeric 5′,8-cyclo-2′-deoxypurine lesions by the human nucleotide excision repair system
    • 4041128 1:CAS:528:DC%2BC2cXntlyksLg%3D 24615810
    • Kropachev K et al (2014) Structural basis for the recognition of diastereomeric 5′,8-cyclo-2′-deoxypurine lesions by the human nucleotide excision repair system. Nucleic Acids Res 42:5020-5032
    • (2014) Nucleic Acids Res , vol.42 , pp. 5020-5032
    • Kropachev, K.1
  • 8
    • 0942268166 scopus 로고    scopus 로고
    • DNA repair-deficient diseases, xeroderma pigmentosum. Cockayne syndrome and trichothiodystrophy
    • 1:CAS:528:DC%2BD2cXjsVyrtA%3D%3D 14726016
    • Lehmann AR (2003) DNA repair-deficient diseases, xeroderma pigmentosum. Cockayne syndrome and trichothiodystrophy. Biochimie 85:1101-1111
    • (2003) Biochimie , vol.85 , pp. 1101-1111
    • Lehmann, A.R.1
  • 10
    • 34247256517 scopus 로고    scopus 로고
    • XPG stabilizes TFIIH, allowing transactivation of nuclear receptors: Implications for cockayne syndrome in XP-G/CS patients
    • 1:CAS:528:DC%2BD2sXltFCqur8%3D 17466625
    • Ito S et al (2007) XPG stabilizes TFIIH, allowing transactivation of nuclear 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
  • 11
    • 77649242633 scopus 로고    scopus 로고
    • Three DNA polymerases, recruited by different mechanisms, carry out NER repair synthesis in human cells
    • 1:CAS:528:DC%2BC3cXlt1KrsLY%3D 20227374
    • Ogi T et al (2010) Three DNA polymerases, recruited by different mechanisms, carry out NER repair synthesis in human cells. Mol Cell 37:714-727
    • (2010) Mol Cell , vol.37 , pp. 714-727
    • Ogi, T.1
  • 12
    • 84902081701 scopus 로고    scopus 로고
    • The complex choreography of transcription-coupled repair
    • 1:CAS:528:DC%2BC2cXmsFCmsbw%3D
    • Spivak G, Ganesan AK (2014) The complex choreography of transcription-coupled repair. DNA Repair (Amst) 19:64-70
    • (2014) DNA Repair (Amst) , vol.19 , pp. 64-70
    • Spivak, G.1    Ganesan, A.K.2
  • 13
    • 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
    • 1:CAS:528:DC%2BD3sXjslOlur0%3D 12732143
    • Groisman R et al (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
  • 14
    • 0028948394 scopus 로고
    • Mammalian DNA nucleotide excision repair reconstituted with purified protein components
    • 1:CAS:528:DyaK2MXkslOmtbo%3D 7697716
    • Aboussekhra A et al (1995) Mammalian DNA nucleotide excision repair reconstituted with purified protein components. Cell 80:859-868
    • (1995) Cell , vol.80 , pp. 859-868
    • Aboussekhra, A.1
  • 15
    • 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
    • 316364 1:CAS:528:DC%2BD3cXhsVKhsrc%3D 10673506
    • Araujo SJ et al (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
  • 16
    • 0037127293 scopus 로고    scopus 로고
    • DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair
    • 1:CAS:528:DC%2BD38XosFaqug%3D%3D 11705987
    • Wakasugi M et al (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
  • 17
    • 0033538572 scopus 로고    scopus 로고
    • Characterization of DNA recognition by the human UV-damaged DNA-binding protein
    • 1:CAS:528:DyaK1MXksFKlsro%3D 10391953
    • Fujiwara Y et al (1999) Characterization of DNA recognition by the human UV-damaged DNA-binding protein. J Biol Chem 274:20027-20033
    • (1999) J Biol Chem , vol.274 , pp. 20027-20033
    • Fujiwara, Y.1
  • 18
    • 28944440380 scopus 로고    scopus 로고
    • DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA
    • 1:CAS:528:DC%2BD2MXht1Gjs7%2FK 16223728
    • Wittschieben BO, Iwai S, Wood RD (2005) DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine 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
    • Wittschieben, B.O.1    Iwai, S.2    Wood, R.D.3
  • 19
    • 0029768095 scopus 로고    scopus 로고
    • Mutations specific to the xeroderma pigmentosum group e Ddb- phenotype
    • 1:CAS:528:DyaK28XmtFeisLY%3D 8798680
    • Nichols AF, Ong P, Linn S (1996) Mutations specific to the xeroderma pigmentosum group E Ddb- phenotype. J Biol Chem 271:24317-24320
    • (1996) J Biol Chem , vol.271 , pp. 24317-24320
    • Nichols, A.F.1    Ong, P.2    Linn, S.3
  • 20
    • 1242296809 scopus 로고    scopus 로고
    • DDB2 gene disruption leads to skin tumors and resistance to apoptosis after exposure to ultraviolet light but not a chemical carcinogen
    • 357050 1:CAS:528:DC%2BD2cXhs1Sku7c%3D 14769931
    • Itoh T, Cado D, Kamide R, Linn S (2004) DDB2 gene disruption leads to skin tumors and resistance to apoptosis after exposure to ultraviolet light but not a chemical carcinogen. Proc Natl Acad Sci USA 101:2052-2057
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2052-2057
    • Itoh, T.1    Cado, D.2    Kamide, R.3    Linn, S.4
  • 21
    • 37549061452 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group e gene product DDB2 activates nucleotide excision repair by regulating the level of p21Waf1/Cip1
    • 2223305 1:CAS:528:DC%2BD1cXktValtg%3D%3D 17967871
    • Stoyanova T, Yoon T, Kopanja D, Mokyr MB, Raychaudhuri P (2008) The xeroderma pigmentosum group E gene product DDB2 activates nucleotide excision repair by regulating the level of p21Waf1/Cip1. Mol Cell Biol 28:177-187
    • (2008) Mol Cell Biol , vol.28 , pp. 177-187
    • Stoyanova, T.1    Yoon, T.2    Kopanja, D.3    Mokyr, M.B.4    Raychaudhuri, P.5
  • 22
    • 16244423719 scopus 로고    scopus 로고
    • The UV-damaged DNA binding protein mediates efficient targeting of the nucleotide excision repair complex to UV-induced photo lesions
    • 1:CAS:528:DC%2BD2MXjt1Kit7g%3D
    • Moser J et al (2005) The UV-damaged DNA binding protein mediates efficient targeting of the nucleotide excision repair complex to UV-induced photo lesions. DNA Repair (Amst) 4:571-582
    • (2005) DNA Repair (Amst) , vol.4 , pp. 571-582
    • Moser, J.1
  • 23
    • 3042780229 scopus 로고    scopus 로고
    • UV radiation-induced XPC translocation within chromatin is mediated by damaged-DNA binding protein, DDB2
    • 1:CAS:528:DC%2BD2cXksVaht7w%3D 14742321
    • Wang QE, Zhu Q, Wani G, Chen J, Wani AA (2004) UV radiation-induced XPC translocation within chromatin is mediated by damaged-DNA binding protein, DDB2. Carcinogenesis 25:1033-1043
    • (2004) Carcinogenesis , vol.25 , pp. 1033-1043
    • Wang, Q.E.1    Zhu, Q.2    Wani, G.3    Chen, J.4    Wani, A.A.5
  • 24
    • 0038771963 scopus 로고    scopus 로고
    • The DDB2 nucleotide excision repair gene product p48 enhances global genomic repair in p53 deficient human fibroblasts
    • 1:CAS:528:DC%2BD3sXkvVWjs70%3D
    • Fitch ME et al (2003) The DDB2 nucleotide excision repair gene product p48 enhances global genomic repair in p53 deficient human fibroblasts. DNA Repair (Amst) 2:819-826
    • (2003) DNA Repair (Amst) , vol.2 , pp. 819-826
    • Fitch, M.E.1
  • 25
    • 79955369234 scopus 로고    scopus 로고
    • Nucleotide excision repair proteins rapidly accumulate but fail to persist in human XP-E (DDB2 mutant) cells
    • 3082610 1:CAS:528:DC%2BC3MXmvFert7s%3D 21388382
    • Oh KS et al (2011) Nucleotide excision repair proteins rapidly accumulate but fail to persist in human XP-E (DDB2 mutant) cells. Photochem Photobiol 87:729-733
    • (2011) Photochem Photobiol , vol.87 , pp. 729-733
    • Oh, K.S.1
  • 26
    • 84906881097 scopus 로고    scopus 로고
    • Sequential and ordered assembly of a large DNA repair complex on undamaged chromatin
    • 4151144 1:CAS:528:DC%2BC2cXhsFantb%2FP 25154395
    • Ziani S et al (2014) Sequential and ordered assembly of a large DNA repair complex on undamaged chromatin. J Cell Biol 206:589-598
    • (2014) J Cell Biol , vol.206 , pp. 589-598
    • Ziani, S.1
  • 27
    • 0033636515 scopus 로고    scopus 로고
    • Xeroderma pigmentosum p48 gene enhances global genomic repair and suppresses UV-induced mutagenesis
    • 2894271 1:CAS:528:DC%2BD3cXjtFSqtL4%3D 10882109
    • Tang JY, Hwang BJ, Ford JM, Hanawalt PC, Chu G (2000) Xeroderma pigmentosum p48 gene enhances global genomic 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
  • 28
    • 28544434877 scopus 로고    scopus 로고
    • Enhanced DDB2 expression protects mice from carcinogenic effects of chronic UV-B irradiation
    • 1:CAS:528:DC%2BD2MXht1WgurfI 16288018
    • Alekseev S et al (2005) Enhanced DDB2 expression protects mice from carcinogenic effects of chronic UV-B irradiation. Cancer Res 65:10298-10306
    • (2005) Cancer Res , vol.65 , pp. 10298-10306
    • Alekseev, S.1
  • 29
    • 0000516293 scopus 로고    scopus 로고
    • Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair
    • 15152 1:CAS:528:DyaK1MXmtlCgtA%3D%3D 9892649
    • Hwang BJ, Ford JM, Hanawalt PC, Chu G (1999) Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair. Proc Natl Acad Sci USA 96:424-428
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 424-428
    • Hwang, B.J.1    Ford, J.M.2    Hanawalt, P.C.3    Chu, G.4
  • 30
    • 0033176104 scopus 로고    scopus 로고
    • A newly identified patient with clinical xeroderma pigmentosum phenotype has a non-sense mutation in the DDB2 gene and incomplete repair in (6-4) photoproducts
    • 1:CAS:528:DyaK1MXlt1Khsr8%3D 10469312
    • Itoh T, Mori T, Ohkubo H, Yamaizumi M (1999) A newly identified patient with clinical xeroderma pigmentosum phenotype has a non-sense mutation in the DDB2 gene and incomplete repair in (6-4) photoproducts. J Invest Dermatol 113:251-257
    • (1999) J Invest Dermatol , vol.113 , pp. 251-257
    • Itoh, T.1    Mori, T.2    Ohkubo, H.3    Yamaizumi, M.4
  • 31
    • 33748987094 scopus 로고    scopus 로고
    • DNA Damage Binding Protein Component DDB1 Participates in Nucleotide Excision Repair through DDB2 DNA-binding and Cullin 4A Ubiquitin Ligase Activity
    • 1:CAS:528:DC%2BD28XovF2itLY%3D 16951172
    • Li J et al (2006) DNA Damage Binding Protein Component DDB1 Participates in Nucleotide Excision Repair through DDB2 DNA-binding and Cullin 4A Ubiquitin Ligase Activity. Cancer Res 66:8590-8597
    • (2006) Cancer Res , vol.66 , pp. 8590-8597
    • Li, J.1
  • 32
    • 19944431173 scopus 로고    scopus 로고
    • Powerful skin cancer protection by a CPD-photolyase transgene
    • 1:CAS:528:DC%2BD2MXmvFemtQ%3D%3D 15668165
    • Jans J et al (2005) Powerful skin cancer protection by a CPD-photolyase transgene. Curr Biol 15:105-115
    • (2005) Curr Biol , vol.15 , pp. 105-115
    • Jans, J.1
  • 33
    • 33751112293 scopus 로고    scopus 로고
    • DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-ROC1 ubiquitin ligases
    • 1620025 1:CAS:528:DC%2BD28XhtFynu7bF 17079684
    • He YJ, McCall CM, Hu J, Zeng Y, Xiong Y (2006) DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-ROC1 ubiquitin ligases. Genes Dev 20:2949-2954
    • (2006) Genes Dev , vol.20 , pp. 2949-2954
    • He, Y.J.1    McCall, C.M.2    Hu, J.3    Zeng, Y.4    Xiong, Y.5
  • 34
    • 33744958177 scopus 로고    scopus 로고
    • Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites regulates in vivo lesion recognition by XPC
    • 1:CAS:528:DC%2BD28Xkt1ymtrw%3D 16527807
    • El-Mahdy MA et al (2006) Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites regulates in vivo lesion recognition by XPC. J Biol Chem 281:13404-13411
    • (2006) J Biol Chem , vol.281 , pp. 13404-13411
    • El-Mahdy, M.A.1
  • 35
    • 57349187165 scopus 로고    scopus 로고
    • Cellular concentrations of DDB2 regulate dynamic binding of DDB1 at UV-induced DNA damage
    • 2593426 1:CAS:528:DC%2BD1cXhsV2mtLnP 18936169
    • Alekseev S et al (2008) Cellular concentrations of DDB2 regulate dynamic binding of DDB1 at UV-induced DNA damage. Mol Cell Biol 28:7402-7413
    • (2008) Mol Cell Biol , vol.28 , pp. 7402-7413
    • Alekseev, S.1
  • 36
    • 57749198023 scopus 로고    scopus 로고
    • Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex
    • 2676164 1:CAS:528:DC%2BD1MXisFyjtA%3D%3D 19109893
    • Scrima A et al (2008) Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex. Cell 135:1213-1223
    • (2008) Cell , vol.135 , pp. 1213-1223
    • Scrima, A.1
  • 37
    • 81855227619 scopus 로고    scopus 로고
    • The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation
    • 1:CAS:528:DC%2BC3MXhsFeisrjM 22118460
    • Fischer ES et al (2011) The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation. Cell 147:1024-1039
    • (2011) Cell , vol.147 , pp. 1024-1039
    • Fischer, E.S.1
  • 38
    • 0034813575 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group e gene product DDB2 is a specific target of cullin 4A in mammalian cells
    • 99852 1:CAS:528:DC%2BD3MXntFChsb8%3D 11564859
    • Nag A, Bondar T, Shiv S, Raychaudhuri P (2001) The xeroderma pigmentosum group E gene product DDB2 is a specific target of cullin 4A in mammalian cells. Mol Cell Biol 21:6738-6747
    • (2001) Mol Cell Biol , vol.21 , pp. 6738-6747
    • Nag, A.1    Bondar, T.2    Shiv, S.3    Raychaudhuri, P.4
  • 39
    • 0036606551 scopus 로고    scopus 로고
    • Sequential binding of UV DNA damage binding factor and degradation of the p48 subunit as early events after UV irradiation
    • 1:CAS:528:DC%2BD38XkvV2hsLk%3D 12034848
    • Rapic-Otrin V, McLenigan MP, Bisi DC, Gonzalez M, Levine AS (2002) Sequential binding of UV DNA damage binding factor and degradation of the p48 subunit as early events after UV irradiation. Nucleic Acids Res 30:2588-2598
    • (2002) Nucleic Acids Res , vol.30 , pp. 2588-2598
    • Rapic-Otrin, V.1    McLenigan, M.P.2    Bisi, D.C.3    Gonzalez, M.4    Levine, A.S.5
  • 40
    • 34548266764 scopus 로고    scopus 로고
    • Dynamic in vivo interaction of DDB2 E3 ubiquitin ligase with UV-damaged DNA is independent of damage-recognition protein XPC
    • 1:CAS:528:DC%2BD2sXhtVelsrfK 17635991
    • Luijsterburg MS et al (2007) Dynamic in vivo interaction of DDB2 E3 ubiquitin ligase with UV-damaged DNA is independent of damage-recognition protein XPC. J Cell Sci 120:2706-2716
    • (2007) J Cell Sci , vol.120 , pp. 2706-2716
    • Luijsterburg, M.S.1
  • 41
    • 65649105790 scopus 로고    scopus 로고
    • CUL4A abrogation augments DNA damage response and protection against skin carcinogenesis
    • 2722740 1:CAS:528:DC%2BD1MXosVCktr4%3D 19481525
    • Liu L et al (2009) CUL4A abrogation augments DNA damage response and protection against skin carcinogenesis. Mol Cell 34:451-460
    • (2009) Mol Cell , vol.34 , pp. 451-460
    • Liu, L.1
  • 42
    • 33644536070 scopus 로고    scopus 로고
    • The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group e and targets histone H2A at UV-damaged DNA sites
    • 1:CAS:528:DC%2BD28XksF2rsLg%3D 16473935
    • Kapetanaki MG et al (2006) The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites. Proc Natl Acad Sci USA 103:2588-2593
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2588-2593
    • Kapetanaki, M.G.1
  • 43
    • 33744781568 scopus 로고    scopus 로고
    • Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage
    • 16678110
    • Wang H et al (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
  • 44
    • 84861939507 scopus 로고    scopus 로고
    • DDB2 promotes chromatin decondensation at UV-induced DNA damage
    • 3328393 1:CAS:528:DC%2BC38XmtFGksrc%3D 22492724
    • Luijsterburg MS et al (2012) DDB2 promotes chromatin decondensation at UV-induced DNA damage. J Cell Biol 197:267-281
    • (2012) J Cell Biol , vol.197 , pp. 267-281
    • Luijsterburg, M.S.1
  • 45
    • 84869111403 scopus 로고    scopus 로고
    • PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1
    • 3471223 1:CAS:528:DC%2BC38XhsFKmtrvL 23045548
    • Pines A et al (2012) PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1. J Cell Biol 199:235-249
    • (2012) J Cell Biol , vol.199 , pp. 235-249
    • Pines, A.1
  • 46
    • 0032134423 scopus 로고    scopus 로고
    • Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair
    • 1:CAS:528:DyaK1cXmtVyisrw%3D 9734359
    • Sugasawa K et al (1998) Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair. Mol Cell 2:223-232
    • (1998) Mol Cell , vol.2 , pp. 223-232
    • Sugasawa, K.1
  • 47
    • 17944361949 scopus 로고    scopus 로고
    • Sequential assembly of the nucleotide excision repair factors in vivo
    • 1:CAS:528:DC%2BD3MXls1Wmsro%3D 11511374
    • Volker M et al (2001) Sequential assembly of the nucleotide excision repair factors in vivo. Mol Cell 8:213-224
    • (2001) Mol Cell , vol.8 , pp. 213-224
    • Volker, M.1
  • 48
    • 0141753120 scopus 로고    scopus 로고
    • The comings and goings of nucleotide excision repair factors on damaged DNA
    • 204472 1:CAS:528:DC%2BD3sXnvVeqtb4%3D 14517266
    • 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
  • 49
    • 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
    • 1:CAS:528:DC%2BD3cXitlCqtr4%3D 10734143
    • Yokoi M et al (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
  • 50
    • 0028269240 scopus 로고
    • Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23
    • 395023 1:CAS:528:DyaK2cXltVGrsLg%3D 8168482
    • Masutani C et al (1994) Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23. EMBO J 13:1831-1843
    • (1994) EMBO J , vol.13 , pp. 1831-1843
    • Masutani, C.1
  • 51
    • 0035374836 scopus 로고    scopus 로고
    • Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair
    • 1:CAS:528:DC%2BD3MXkt12ktrg%3D 11279143
    • Araki M et al (2001) Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair. J Biol Chem 276:18665-18672
    • (2001) J Biol Chem , vol.276 , pp. 18665-18672
    • Araki, M.1
  • 52
    • 0029742577 scopus 로고    scopus 로고
    • HHR23B, a human Rad23 homolog, stimulates XPC protein in nucleotide excision repair in vitro
    • 231487 1:CAS:528:DyaK28XltFKjsbY%3D 8756644
    • Sugasawa K et al (1996) HHR23B, a human Rad23 homolog, stimulates XPC protein in nucleotide excision repair in vitro. Mol Cell Biol 16:4852-4861
    • (1996) Mol Cell Biol , vol.16 , pp. 4852-4861
    • Sugasawa, K.1
  • 53
    • 0030688064 scopus 로고    scopus 로고
    • Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity
    • 232549 1:CAS:528:DyaK2sXnsFWhu7s%3D 9372924
    • Sugasawa K et al (1997) Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity. Mol Cell Biol 17:6924-6931
    • (1997) Mol Cell Biol , vol.17 , pp. 6924-6931
    • Sugasawa, K.1
  • 54
    • 0038339144 scopus 로고    scopus 로고
    • A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein
    • 196135 1:CAS:528:DC%2BD3sXlsV2ru7o%3D 12815074
    • Ng JM et al (2003) A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein. Genes Dev 17:1630-1645
    • (2003) Genes Dev , vol.17 , pp. 1630-1645
    • Ng, J.M.1
  • 55
    • 0029885890 scopus 로고    scopus 로고
    • XPC and human homologs of RAD23: Intracellular localization and relationship to other nucleotide excision repair complexes
    • 145966 8692695
    • van der Spek PJ et al (1996) XPC and human homologs of RAD23: intracellular localization and relationship to other nucleotide excision repair complexes. Nucleic Acids Res 24:2551-2559
    • (1996) Nucleic Acids Res , vol.24 , pp. 2551-2559
    • Van Der Spek, P.J.1
  • 56
    • 4444371794 scopus 로고    scopus 로고
    • Relative levels of the two mammalian Rad23 homologs determine composition and stability of the xeroderma pigmentosum group C protein complex
    • 1:CAS:528:DC%2BD2cXntFSmsrw%3D
    • Okuda Y et al (2004) Relative levels of the two mammalian Rad23 homologs determine composition and stability of the xeroderma pigmentosum group C protein complex. DNA Repair (Amst) 3:1285-1295
    • (2004) DNA Repair (Amst) , vol.3 , pp. 1285-1295
    • Okuda, Y.1
  • 57
    • 11344250554 scopus 로고    scopus 로고
    • Roles of Rad23 protein in yeast nucleotide excision repair
    • 534619 1:CAS:528:DC%2BD2cXhtVanurvP 15545636
    • Xie Z, Liu S, Zhang Y, Wang Z (2004) Roles of Rad23 protein in yeast nucleotide excision repair. Nucleic Acids Res 32:5981-5990
    • (2004) Nucleic Acids Res , vol.32 , pp. 5981-5990
    • Xie, Z.1    Liu, S.2    Zhang, Y.3    Wang, Z.4
  • 58
    • 84860339685 scopus 로고    scopus 로고
    • Recognition of DNA damage by XPC coincides with disruption of the XPC-RAD23 complex
    • 3308700 1:CAS:528:DC%2BC38XksFCmsb4%3D 22431748
    • Bergink S et al (2012) Recognition of DNA damage by XPC coincides with disruption of the XPC-RAD23 complex. J Cell Biol 196:681-688
    • (2012) J Cell Biol , vol.196 , pp. 681-688
    • Bergink, S.1
  • 59
    • 20744446570 scopus 로고    scopus 로고
    • Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein
    • 1156980 1:CAS:528:DC%2BD2MXlslCjt7k%3D 15964821
    • Nishi R et al (2005) Centrin 2 stimulates nucleotide 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
  • 60
    • 84887151305 scopus 로고    scopus 로고
    • The intertwined roles of transcription and repair proteins
    • 3919531 1:CAS:528:DC%2BC3sXhvVSlurrE 24207023
    • Fong YW, Cattoglio C, Tjian R (2013) The intertwined roles of transcription and repair proteins. Mol Cell 52:291-302
    • (2013) Mol Cell , vol.52 , pp. 291-302
    • Fong, Y.W.1    Cattoglio, C.2    Tjian, R.3
  • 61
    • 34948892722 scopus 로고    scopus 로고
    • Recognition of DNA damage by the Rad4 nucleotide excision repair protein
    • 1:CAS:528:DC%2BD2sXhtFagt7fL 17882165
    • 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
  • 62
    • 69249202311 scopus 로고    scopus 로고
    • Two-stage dynamic DNA quality check by xeroderma pigmentosum group C protein
    • 2735174 1:CAS:528:DC%2BD1MXotlSgt7g%3D 19609301
    • Camenisch U et al (2009) Two-stage dynamic DNA quality check by xeroderma pigmentosum group C protein. EMBO J 28:2387-2399
    • (2009) EMBO J , vol.28 , pp. 2387-2399
    • Camenisch, U.1
  • 63
    • 84881496811 scopus 로고    scopus 로고
    • Structure-function analysis of the EF-hand protein centrin-2 for its intracellular localization and nucleotide excision repair
    • 3737541 1:CAS:528:DC%2BC3sXht1Cktb7P 23716636
    • Nishi R, Sakai W, Tone D, Hanaoka F, Sugasawa K (2013) Structure-function analysis of the EF-hand protein centrin-2 for its intracellular localization and nucleotide excision repair. Nucleic Acids Res 41:6917-6929
    • (2013) Nucleic Acids Res , vol.41 , pp. 6917-6929
    • Nishi, R.1    Sakai, W.2    Tone, D.3    Hanaoka, F.4    Sugasawa, K.5
  • 64
    • 11144263684 scopus 로고    scopus 로고
    • Cellular ubiquitination and proteasomal functions positively modulate mammalian nucleotide excision repair
    • 15547920
    • Wang QE et al (2005) Cellular ubiquitination and proteasomal functions positively modulate mammalian nucleotide excision repair. Mol Carcinog 42:53-64
    • (2005) Mol Carcinog , vol.42 , pp. 53-64
    • Wang, Q.E.1
  • 65
    • 34548790663 scopus 로고    scopus 로고
    • Ubiquitylation-independent degradation of Xeroderma pigmentosum group C protein is required for efficient nucleotide excision repair
    • 2018625 1:CAS:528:DC%2BD2sXht1ygtLfF 17693435
    • Wang QE et al (2007) Ubiquitylation-independent degradation of Xeroderma pigmentosum group C protein is required for efficient nucleotide excision repair. Nucleic Acids Res 35:5338-5350
    • (2007) Nucleic Acids Res , vol.35 , pp. 5338-5350
    • Wang, Q.E.1
  • 66
    • 21044442126 scopus 로고    scopus 로고
    • UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex
    • 1:CAS:528:DC%2BD2MXktlSiu7g%3D 15882621
    • Sugasawa K et al (2005) UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex. Cell 121:387-400
    • (2005) Cell , vol.121 , pp. 387-400
    • Sugasawa, K.1
  • 67
    • 22244478319 scopus 로고    scopus 로고
    • DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation
    • 1178000 1:CAS:528:DC%2BD2MXpslOnsbs%3D 16030353
    • Wang QE et al (2005) DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation. Nucleic Acids Res 33:4023-4034
    • (2005) Nucleic Acids Res , vol.33 , pp. 4023-4034
    • Wang, Q.E.1
  • 68
    • 84907478478 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 7 regulates nucleotide excision repair through deubiquitinating XPC protein and preventing XPC protein from undergoing ultraviolet light-induced and VCP/p97 protein-regulated proteolysis
    • 1:CAS:528:DC%2BC2cXhs1eiurjF 25118285
    • He J et al (2014) Ubiquitin-specific protease 7 regulates nucleotide excision repair through deubiquitinating XPC protein and preventing XPC protein from undergoing ultraviolet light-induced and VCP/p97 protein-regulated proteolysis. J Biol Chem 289:27278-27289
    • (2014) J Biol Chem , vol.289 , pp. 27278-27289
    • He, J.1
  • 69
    • 84880032059 scopus 로고    scopus 로고
    • RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response
    • 3678163 1:CAS:528:DC%2BC3sXpsVaqtr4%3D 23751493
    • Poulsen SL et al (2013) RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response. J Cell Biol 201:797-807
    • (2013) J Cell Biol , vol.201 , pp. 797-807
    • Poulsen, S.L.1
  • 70
    • 53349128176 scopus 로고    scopus 로고
    • Versatile DNA damage detection by the global genome nucleotide excision repair protein XPC
    • 1:CAS:528:DC%2BD1cXht1SrsrbI 18682493
    • Hoogstraten D et al (2008) Versatile DNA damage detection by the global genome nucleotide excision repair protein XPC. J Cell Sci 121:2850-2859
    • (2008) J Cell Sci , vol.121 , pp. 2850-2859
    • Hoogstraten, D.1
  • 71
    • 84887164461 scopus 로고    scopus 로고
    • Xeroderma pigmentosum complementation group C protein (XPC) serves as a general sensor of damaged DNA
    • 1:CAS:528:DC%2BC3sXhsVOnu7nP
    • Shell SM et al (2013) Xeroderma pigmentosum complementation group C protein (XPC) serves as a general sensor of damaged DNA. DNA Repair (Amst) 12:947-953
    • (2013) DNA Repair (Amst) , vol.12 , pp. 947-953
    • Shell, S.M.1
  • 72
    • 70350566800 scopus 로고    scopus 로고
    • Molecular insights into the recruitment of TFIIH to sites of DNA damage
    • 2760107 1:CAS:528:DC%2BD1MXhtVKhs7%2FI 19713942
    • 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
  • 73
    • 0035929594 scopus 로고    scopus 로고
    • A yeast four-hybrid system identifies Cdk-activating kinase as a regulator of the XPD helicase, a subunit of transcription factor IIH
    • 1:CAS:528:DC%2BD3MXntFaiurk%3D 11445587
    • Sandrock B, Egly JM (2001) A yeast four-hybrid system identifies Cdk-activating kinase as a regulator of the XPD helicase, a subunit of transcription factor IIH. J Biol Chem 276:35328-35333
    • (2001) J Biol Chem , vol.276 , pp. 35328-35333
    • Sandrock, B.1    Egly, J.M.2
  • 74
    • 46349091030 scopus 로고    scopus 로고
    • Nucleotide excision repair driven by the dissociation of CAK from TFIIH
    • 1:CAS:528:DC%2BD1cXovFWgu7Y%3D 18614043
    • Coin F et al (2008) Nucleotide excision repair driven by the dissociation of CAK from TFIIH. Mol Cell 31:9-20
    • (2008) Mol Cell , vol.31 , pp. 9-20
    • Coin, F.1
  • 75
    • 70449717367 scopus 로고    scopus 로고
    • Two-step recognition of DNA damage for mammalian nucleotide excision repair: Directional binding of the XPC complex and DNA strand scanning
    • 1:CAS:528:DC%2BC3cXksFWmsg%3D%3D 19941824
    • Sugasawa K, Akagi J, Nishi R, Iwai S, Hanaoka F (2009) Two-step recognition of DNA damage for mammalian nucleotide 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
  • 76
    • 84873408109 scopus 로고    scopus 로고
    • DNA quality control by a lesion sensor pocket of the xeroderma pigmentosum group D helicase subunit of TFIIH
    • 1:CAS:528:DC%2BC3sXhsFCks78%3D 23352696
    • Mathieu N, Kaczmarek N, Ruthemann P, Luch A, Naegeli H (2013) DNA quality control by a lesion sensor pocket of the xeroderma pigmentosum group D helicase 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
  • 77
    • 45849119445 scopus 로고    scopus 로고
    • Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD
    • 2435149 18578568
    • Wolski SC et al (2008) Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD. PLoS Biol 6:e149
    • (2008) PLoS Biol , vol.6 , pp. 149
    • Wolski, S.C.1
  • 78
    • 44149094083 scopus 로고    scopus 로고
    • XPD helicase structures and activities: Insights into the cancer and aging phenotypes from XPD mutations
    • 3055247 1:CAS:528:DC%2BD1cXntFaltrk%3D 18510924
    • Fan L et al (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
  • 79
    • 43949110271 scopus 로고    scopus 로고
    • Structure of the DNA repair helicase XPD
    • 3326533 1:CAS:528:DC%2BD1cXntFaltrY%3D 18510925
    • Liu H et al (2008) Structure of the DNA repair helicase XPD. Cell 133:801-812
    • (2008) Cell , vol.133 , pp. 801-812
    • Liu, H.1
  • 80
    • 0027483739 scopus 로고
    • Preferential binding of the Xeroderma Pigmentosum group A complementing protein to damaged DNA
    • 1:CAS:528:DyaK3sXmsVars7w%3D 8218288
    • Jones CJ, Wood RD (1993) Preferential binding of the Xeroderma Pigmentosum group A complementing protein to damaged DNA. Biochemistry 32:12096-12104
    • (1993) Biochemistry , vol.32 , pp. 12096-12104
    • Jones, C.J.1    Wood, R.D.2
  • 81
    • 0033603338 scopus 로고    scopus 로고
    • Order of assembly of human DNA repair excision nuclease
    • 1:CAS:528:DyaK1MXkt1SitL8%3D 10373492
    • Wakasugi M, Sancar A (1999) Order of assembly of human DNA repair excision nuclease. J Biol Chem 274:18759-18768
    • (1999) J Biol Chem , vol.274 , pp. 18759-18768
    • Wakasugi, M.1    Sancar, A.2
  • 82
    • 0032102927 scopus 로고    scopus 로고
    • Structural features of the minimal DNA binding domain (M98-F219) of human nucleotide excision repair protein XPA
    • 147584 1:CAS:528:DyaK1cXktFalu7c%3D 9592168
    • Buchko GW, Ni S, Thrall BD, Kennedy MA (1998) Structural features of the minimal DNA binding domain (M98-F219) of human nucleotide excision repair protein XPA. Nucleic Acids Res 26:2779-2788
    • (1998) Nucleic Acids Res , vol.26 , pp. 2779-2788
    • Buchko, G.W.1    Ni, S.2    Thrall, B.D.3    Kennedy, M.A.4
  • 83
    • 0030039031 scopus 로고    scopus 로고
    • Identification of a damaged-DNA binding domain of the XPA protein
    • 8538652
    • Kuraoka I et al (1996) Identification of a damaged-DNA binding domain of the XPA protein. Mutat Res 362:87-95
    • (1996) Mutat Res , vol.362 , pp. 87-95
    • Kuraoka, I.1
  • 84
    • 0029131609 scopus 로고
    • Human xeroderma pigmentosum group A protein interacts with human replication protein A and inhibits DNA replication
    • 1:CAS:528:DyaK2MXotFaisLo%3D 7665601
    • Lee SH, Kim DK, Drissi R (1995) Human xeroderma pigmentosum group A protein interacts with human replication protein A and inhibits DNA replication. J Biol Chem 270:21800-21805
    • (1995) J Biol Chem , vol.270 , pp. 21800-21805
    • Lee, S.H.1    Kim, D.K.2    Drissi, R.3
  • 85
    • 0029129283 scopus 로고
    • An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair
    • 230789 1:STN:280:DyaK28%2FgvFGltA%3D%3D 7565690
    • Li L, Lu X, Peterson CA, Legerski RJ (1995) 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
  • 86
    • 0030817140 scopus 로고    scopus 로고
    • DNA damage recognition by XPA protein promotes efficient recruitment of transcription factor II H
    • 1:CAS:528:DyaK2sXmt1WjtLo%3D
    • Nocentini S, Coin F, Saijo M, Tanaka K, Egly J-M (1997) DNA damage recognition by XPA protein promotes efficient recruitment of transcription factor II H. J Biol Sci 272:22991-22994
    • (1997) J Biol Sci , vol.272 , pp. 22991-22994
    • Nocentini, S.1    Coin, F.2    Saijo, M.3    Tanaka, K.4    Egly, J.-M.5
  • 87
    • 36249002305 scopus 로고    scopus 로고
    • Structural basis for the recruitment of ERCC1-XPF to nucleotide excision repair complexes by XPA
    • 2080803 1:CAS:528:DC%2BD2sXht12gtbbL 17948053
    • Tsodikov OV et al (2007) Structural basis for the recruitment of ERCC1-XPF to nucleotide excision repair complexes by XPA. EMBO J 26:4768-4776
    • (2007) EMBO J , vol.26 , pp. 4768-4776
    • Tsodikov, O.V.1
  • 88
    • 33846849467 scopus 로고    scopus 로고
    • ATR-dependent checkpoint modulates XPA nuclear import in response to UV irradiation
    • 3106104 1:CAS:528:DC%2BD2sXhtFGmu7o%3D 16862173
    • Wu X, Shell SM, Liu Y, Zou Y (2007) ATR-dependent checkpoint modulates XPA nuclear import in response to UV irradiation. Oncogene 26:757-764
    • (2007) Oncogene , vol.26 , pp. 757-764
    • Wu, X.1    Shell, S.M.2    Liu, Y.3    Zou, Y.4
  • 89
    • 77955501963 scopus 로고    scopus 로고
    • SIRT1 regulates UV-induced DNA repair through deacetylating XPA
    • 1:CAS:528:DC%2BC3cXpsVCnsbo%3D 20670893
    • 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
  • 90
    • 84902650127 scopus 로고    scopus 로고
    • PKA-mediated phosphorylation of ATR promotes recruitment of XPA to UV-induced DNA damage
    • 1:CAS:528:DC%2BC2cXhtVamtLfK 24950377
    • Jarrett SG et al (2014) PKA-mediated phosphorylation of ATR promotes recruitment of XPA to UV-induced DNA damage. Mol Cell 54:999-1011
    • (2014) Mol Cell , vol.54 , pp. 999-1011
    • Jarrett, S.G.1
  • 91
    • 84891736600 scopus 로고    scopus 로고
    • Coordinated regulation of XPA stability by ATR and HERC2 during nucleotide excision repair
    • 1:CAS:528:DC%2BC38XhslagsL3N 23178497
    • Lee TH, Park JM, Leem SH, Kang TH (2014) Coordinated regulation of XPA stability by ATR and HERC2 during nucleotide excision repair. Oncogene 33:19-25
    • (2014) Oncogene , vol.33 , pp. 19-25
    • Lee, T.H.1    Park, J.M.2    Leem, S.H.3    Kang, T.H.4
  • 92
    • 84869218112 scopus 로고    scopus 로고
    • Poly(ADP-ribose) contributes to an association between poly(ADP-ribose) polymerase-1 and xeroderma pigmentosum complementation group A in nucleotide excision repair
    • 3501068 1:CAS:528:DC%2BC38Xhs12ksrzF 23038248
    • King BS, Cooper KL, Liu KJ, Hudson LG (2012) Poly(ADP-ribose) contributes to an association between poly(ADP-ribose) polymerase-1 and xeroderma pigmentosum 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
  • 93
    • 84906791678 scopus 로고    scopus 로고
    • Poly(ADP-ribose)-mediated interplay of XPA and PARP1 leads to reciprocal regulation of protein function
    • 4160017 1:CAS:528:DC%2BC2cXhtlKksr3E 24953096
    • Fischer JM et al (2014) Poly(ADP-ribose)-mediated interplay of XPA and PARP1 leads to reciprocal regulation of protein function. FEBS J 281:3625-3641
    • (2014) FEBS J , vol.281 , pp. 3625-3641
    • Fischer, J.M.1
  • 94
    • 84858758050 scopus 로고    scopus 로고
    • Stimulation of DNA glycosylase activities by XPC protein complex: Roles of protein-protein interactions
    • Article ID 805698
    • Shimizu Y et al (2010) Stimulation of DNA glycosylase activities by XPC protein complex: roles of protein-protein interactions. J Nucleic Acids 2010. Article ID 805698
    • (2010) J Nucleic Acids 2010
    • Shimizu, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.