메뉴 건너뛰기




Volumn 637, Issue , 2008, Pages 103-112

Other proteins interacting with XP proteins

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL AGENT; DEOXYRIBONUCLEOPROTEIN; DNA DIRECTED DNA POLYMERASE ETA; ENDONUCLEASE; HELICASE; NUCLEASE; TRANSCRIPTION FACTOR IIH; UNCLASSIFIED DRUG; XERODERMA PIGMENTOSUM GROUP A PROTEIN; XERODERMA PIGMENTOSUM GROUP B PROTEIN; XERODERMA PIGMENTOSUM GROUP C PROTEIN; XERODERMA PIGMENTOSUM GROUP D PROTEIN; XERODERMA PIGMENTOSUM GROUP E PROTEIN; XERODERMA PIGMENTOSUM GROUP F PROTEIN; XERODERMA PIGMENTOSUM GROUP G PROTEIN; XERODERMA PIGMENTOSUM GROUP V PROTEIN; XERODERMA PIGMENTOSUM PROTEIN; Y BOX BINDING PROTEIN 1; DDB2 PROTEIN, HUMAN; DNA BINDING PROTEIN; DNA DIRECTED DNA POLYMERASE; DNA EXCISION REPAIR PROTEIN ERCC 5; DNA EXCISION REPAIR PROTEIN ERCC-5; NUCLEAR PROTEIN; PROTEIN; TRANSCRIPTION FACTOR; XPA PROTEIN, HUMAN;

EID: 60549117349     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-0-387-09599-8_11     Document Type: Review
Times cited : (17)

References (97)
  • 1
    • 0028110878 scopus 로고    scopus 로고
    • Kraemer KH, Lee MM, Andrews AD ct al. The role of sunlight and DNA repair in melanoma and nonmelanoma skin cancer. The Xeroderma pigmentosum paradigm. Arch Dermatol 1994; 130:1018-1021.
    • Kraemer KH, Lee MM, Andrews AD ct al. The role of sunlight and DNA repair in melanoma and nonmelanoma skin cancer. The Xeroderma pigmentosum paradigm. Arch Dermatol 1994; 130:1018-1021.
  • 2
    • 0023130695 scopus 로고
    • Xeroderma pigmentosum. Cutaneous, ocular and neurologic abnormalities in 830 published cases
    • Kraemer KH, Lee MM, Scotto J. Xeroderma pigmentosum. Cutaneous, ocular and neurologic abnormalities in 830 published cases. Arch Dermato 1987; 123:241-250.
    • (1987) Arch Dermato , vol.123 , pp. 241-250
    • Kraemer, K.H.1    Lee, M.M.2    Scotto, J.3
  • 3
    • 0942268166 scopus 로고    scopus 로고
    • DNA repair-deficient diseases. Xeroderma pigmentosum, Cockayne syndrome and trichothiodystrophy
    • Lehmann AR. DNA repair-deficient diseases. Xeroderma pigmentosum, Cockayne syndrome and trichothiodystrophy. Biochimie 2003; 85:1101-1111.
    • (2003) Biochimie , vol.85 , pp. 1101-1111
    • Lehmann, A.R.1
  • 4
    • 33646865105 scopus 로고    scopus 로고
    • The protein shuffle. Sequential interactions among components of the human nucleotide excision repair pathway
    • Park CJ and Choi BS. The protein shuffle. Sequential interactions among components of the human nucleotide excision repair pathway. FEBS J 2006; 273:1600-1608.
    • (2006) FEBS J , vol.273 , pp. 1600-1608
    • Park, C.J.1    Choi, B.S.2
  • 5
    • 0141753120 scopus 로고    scopus 로고
    • The comings and goings of nucleotide excision repair factors on damaged DNA
    • Riedl T, Hanaoka F and Egly JM. The comings and goings of nucleotide excision repair factors on damaged DNA. EMBO J 2003; 22:5293-5303.
    • (2003) EMBO J , vol.22 , pp. 5293-5303
    • Riedl, T.1    Hanaoka, F.2    Egly, J.M.3
  • 6
    • 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
    • Masutani C, Sugasawa K, Yanagisawa J et al. Purification and cloning of a nucleotide excision repair complex involving the Xeroderma pigmentosum group C protein and a human homologue of yeast RAD23. EMBOJ 1994; 13:1831-1843.
    • (1994) EMBOJ , vol.13 , pp. 1831-1843
    • Masutani, C.1    Sugasawa, K.2    Yanagisawa, J.3
  • 7
    • 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, Mackawa T et al. 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 2000; 275:9870-9875.
    • (2000) J Biol Chem , vol.275 , pp. 9870-9875
    • Yokoi, M.1    Masutani, C.2    Mackawa, T.3
  • 8
    • 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
    • Araki M, Masutani C, Takcmura M et al. 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 2001; 276:18665-18672.
    • (2001) J Biol Chem , vol.276 , pp. 18665-18672
    • Araki, M.1    Masutani, C.2    Takcmura, M.3
  • 9
    • 0141924869 scopus 로고    scopus 로고
    • Xeroderma pigmentosum group C protein possesses a high affinity binding site to human centrin 2 and calmodulin
    • Popescu A, Miron S, Blouquit Y et al. Xeroderma pigmentosum group C protein possesses a high affinity binding site to human centrin 2 and calmodulin. J Biol Chem 2003; 278:40252-40261.
    • (2003) J Biol Chem , vol.278 , pp. 40252-40261
    • Popescu, A.1    Miron, S.2    Blouquit, Y.3
  • 10
    • 33845417285 scopus 로고    scopus 로고
    • Tissue specific mutagenic and carcinogenic responses in NER defective mouse models
    • Wijnhoven SW, Hoogervorst EM, de Waard H et al. Tissue specific mutagenic and carcinogenic responses in NER defective mouse models. Mut Res 2006; 614:77-94.
    • (2006) Mut Res , vol.614 , pp. 77-94
    • Wijnhoven, S.W.1    Hoogervorst, E.M.2    de Waard, H.3
  • 11
    • 21044442126 scopus 로고    scopus 로고
    • UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex
    • Sugasawa K, Okuda Y, Saijo M et al. UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex. Cell 2005; 121:387-400.
    • (2005) Cell , vol.121 , pp. 387-400
    • Sugasawa, K.1    Okuda, Y.2    Saijo, M.3
  • 12
    • 0033600798 scopus 로고    scopus 로고
    • Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome
    • Hiyama H, Yokoi M, Masutani C et al. Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome. J Biol Chem 1999; 274:28019-28025.
    • (1999) J Biol Chem , vol.274 , pp. 28019-28025
    • Hiyama, H.1    Yokoi, M.2    Masutani, C.3
  • 13
    • 22244478319 scopus 로고    scopus 로고
    • Wang QE, Zhu Q, Wani G ct al. DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation. Nucleic Acids Research 2005; 33:4023-4034.
    • Wang QE, Zhu Q, Wani G ct al. DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation. Nucleic Acids Research 2005; 33:4023-4034.
  • 14
    • 33748754078 scopus 로고    scopus 로고
    • The involvement of ataxia-telangiectasia mutated protein activation in nucleotide excision repair-facilitated cell survival with cisplatin treatment
    • Colton SL, Xu XS, Wang YA et al. The involvement of ataxia-telangiectasia mutated protein activation in nucleotide excision repair-facilitated cell survival with cisplatin treatment. J Biol Chem 2006; 281:27117-27125.
    • (2006) J Biol Chem , vol.281 , pp. 27117-27125
    • Colton, S.L.1    Xu, X.S.2    Wang, Y.A.3
  • 15
    • 0037413689 scopus 로고    scopus 로고
    • Shimizu Y, Iwai S, Hanaoka F ct al. Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase. EMBO J 2003; 22:164-173.
    • Shimizu Y, Iwai S, Hanaoka F ct al. Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase. EMBO J 2003; 22:164-173.
  • 16
    • 0024378645 scopus 로고
    • Evidence that Xeroderma pigmentosum cells firom complementation group E arc deficient in a homolog of yeast photolyase
    • Patterson M, Chu G. Evidence that Xeroderma pigmentosum cells firom complementation group E arc deficient in a homolog of yeast photolyase. Mol Cell Biol 1989; 9:5105-5112.
    • (1989) Mol Cell Biol , vol.9 , pp. 5105-5112
    • Patterson, M.1    Chu, G.2
  • 17
    • 0035850238 scopus 로고    scopus 로고
    • The p48 subunit of the damagcd-DNA binding protein DDB associates with the CBP/p300 family of histonc acetyltransfcrase
    • Datta A, Bagchi S, Nag A et al. The p48 subunit of the damagcd-DNA binding protein DDB associates with the CBP/p300 family of histonc acetyltransfcrase. Mutat Res 2001; 486:89-97.
    • (2001) Mutat Res , vol.486 , pp. 89-97
    • Datta, A.1    Bagchi, S.2    Nag, A.3
  • 18
    • 27644510072 scopus 로고    scopus 로고
    • Xeroderma pigmentosum complementation group E protein (XPE/DDB2):purification of various complexes of XPE and analyses of their damaged DNA binding and putative DNA repair properties
    • Kulaksiz G, Rcardon JT, Sancar A. Xeroderma pigmentosum complementation group E protein (XPE/DDB2):purification of various complexes of XPE and analyses of their damaged DNA binding and putative DNA repair properties. Mol Cell Biol 2005; 25:9784-9792.
    • (2005) Mol Cell Biol , vol.25 , pp. 9784-9792
    • Kulaksiz, G.1    Rcardon, J.T.2    Sancar, A.3
  • 19
    • 0034812915 scopus 로고    scopus 로고
    • Human STAGA complex is a chromatin-acctylating transcription coactivator that interacts with prcmRNA splicing and DNA damage-binding factors in vivo
    • Martinez E, Palhan VB, Tjcrnbcrg A et al. Human STAGA complex is a chromatin-acctylating transcription coactivator that interacts with prcmRNA splicing and DNA damage-binding factors in vivo. Mol Cell Biol 2001; 21:6782-6795.
    • (2001) Mol Cell Biol , vol.21 , pp. 6782-6795
    • Martinez, E.1    Palhan, V.B.2    Tjcrnbcrg, A.3
  • 20
    • 33644536070 scopus 로고    scopus 로고
    • The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in Xeroderma pigmentosum group E and targets histone H2A at UV-damagcd DNA sites
    • Kapetanaki MG, Guerrero-Santoro J, Bisi DC et al. The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in Xeroderma pigmentosum group E and targets histone H2A at UV-damagcd DNA sites. PNAS 2006; 103:2588-2593.
    • (2006) PNAS , vol.103 , pp. 2588-2593
    • Kapetanaki, M.G.1    Guerrero-Santoro, J.2    Bisi, D.C.3
  • 21
    • 0031962186 scopus 로고    scopus 로고
    • Hayes S, Shiyanov P, Chen X ct al. DDB, a putative DNA repair protein, can function as a transcriptional partner of E2F1. Mol Cell Biol 1998; 18:240-249.
    • Hayes S, Shiyanov P, Chen X ct al. DDB, a putative DNA repair protein, can function as a transcriptional partner of E2F1. Mol Cell Biol 1998; 18:240-249.
  • 22
    • 33646685947 scopus 로고    scopus 로고
    • A kinasc-independent function of c-Abl in promoting proteolytic destruction of damaged DNA binding proteins
    • Chen X, Zhang J, Lee J et al. A kinasc-independent function of c-Abl in promoting proteolytic destruction of damaged DNA binding proteins. Mol Cell 2006; 22:489-499.
    • (2006) Mol Cell , vol.22 , pp. 489-499
    • Chen, X.1    Zhang, J.2    Lee, J.3
  • 23
    • 0035930582 scopus 로고    scopus 로고
    • UV-damagcd DNA-binding proteins are targets of CUL-4A-mediatcd ubiquitination and degradation
    • Chen X, Zhang Y, Douglas L et al. (2001) UV-damagcd DNA-binding proteins are targets of CUL-4A-mediatcd ubiquitination and degradation. J Biol Chem 2001; 276:48175-48182.
    • (2001) J Biol Chem 2001 , vol.276 , pp. 48175-48182
    • Chen, X.1    Zhang, Y.2    Douglas, L.3
  • 24
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DDB2 and CSA complexes is diflPercntially regulated by the COP9 signalosome in response to DNA damage
    • Groisman R, Polanowska J, Kuraoka I et al. The ubiquitin ligase activity in the DDB2 and CSA complexes is diflPercntially regulated by the COP9 signalosome in response to DNA damage. Cell 2003; 113:357-367.
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3
  • 25
    • 0033988552 scopus 로고    scopus 로고
    • Damage recognition in nucleotide excision repair of DNA
    • Batty DP, Wood RD. Damage recognition in nucleotide excision repair of DNA. Gene 2000; 41:193-204.
    • (2000) Gene , vol.41 , pp. 193-204
    • Batty, D.P.1    Wood, R.D.2
  • 26
    • 0030723714 scopus 로고    scopus 로고
    • Cleaver JE, States JC. The DNA damage-recognition problem in human and other eukaryotic cells:the XPA damage binding protein. Biochem J 1997; 328:1-12.
    • Cleaver JE, States JC. The DNA damage-recognition problem in human and other eukaryotic cells:the XPA damage binding protein. Biochem J 1997; 328:1-12.
  • 27
    • 0029131609 scopus 로고
    • Human Xeroderma pigmentosum group A protein interacts with human replication protein A and inhibits DNA replication
    • Lee SH, Kim DK, Drissi R. Human Xeroderma pigmentosum group A protein interacts with human replication protein A and inhibits DNA replication. J Biol Chem 1995; 270:21800-21805.
    • (1995) J Biol Chem , vol.270 , pp. 21800-21805
    • Lee, S.H.1    Kim, D.K.2    Drissi, R.3
  • 28
    • 0034721654 scopus 로고    scopus 로고
    • Structural basis for the recognition of DNA repair proteins UNG2, XPA and RAD52 by replication factor RPA
    • Mer G, Bochkarev A, Gupta R et al. Structural basis for the recognition of DNA repair proteins UNG2, XPA and RAD52 by replication factor RPA. Cell 2000; 103:449-456.
    • (2000) Cell , vol.103 , pp. 449-456
    • Mer, G.1    Bochkarev, A.2    Gupta, R.3
  • 29
    • 33745607897 scopus 로고    scopus 로고
    • Functions of human replication protein A (RPA):from DNA replication to DNA damage and stress responses
    • Zou Y, Liu Y, Wu X et al. Functions of human replication protein A (RPA):from DNA replication to DNA damage and stress responses. J Cell Physiol 2006; 208:267-273.
    • (2006) J Cell Physiol , vol.208 , pp. 267-273
    • Zou, Y.1    Liu, Y.2    Wu, X.3
  • 30
    • 31344443061 scopus 로고    scopus 로고
    • Complex formation with damage recognition protein Radl4 is essential for Saccharomyces cerevisiae Radl-RadlO nuclease to perform its function in nucleotide excision repair in vivo
    • Guzder SN, Sommers CH, Prakash L et al. Complex formation with damage recognition protein Radl4 is essential for Saccharomyces cerevisiae Radl-RadlO nuclease to perform its function in nucleotide excision repair in vivo. Mol Cell Biol 2006; 26:1135-1141.
    • (2006) Mol Cell Biol , vol.26 , pp. 1135-1141
    • Guzder, S.N.1    Sommers, C.H.2    Prakash, L.3
  • 31
    • 33845925343 scopus 로고    scopus 로고
    • Specific and Efficient Binding of Xeroderma Pigmentosum Complementation Group A to Double-Strand/Single-Strand DNA Junctions with 3'- and/or 5'-ssDNA Branches
    • Yang Z, Roginskaya M, Colis LC et al. Specific and Efficient Binding of Xeroderma Pigmentosum Complementation Group A to Double-Strand/Single-Strand DNA Junctions with 3'- and/or 5'-ssDNA Branches. Biochemistry 2006; 45:15921-15930.
    • (2006) Biochemistry , vol.45 , pp. 15921-15930
    • Yang, Z.1    Roginskaya, M.2    Colis, L.C.3
  • 32
    • 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 et al. Double-check probing of DNA bending and unwinding by XPA-RPA: an architectural function in DNA repair. EMBO J 2001; 20:3554-3564.
    • (2001) EMBO J , vol.20 , pp. 3554-3564
    • Missura, M.1    Buterin, T.2    Hindges, R.3
  • 33
    • 33645513410 scopus 로고    scopus 로고
    • Phosphorylation of nucleotide excision repair factor Xeroderma pigmentosum group A by ataxia telangiectasia mutated and Rad3-related-dependent checkpoint pathway promotes cell survival in response to UV irradiation
    • Wii X, Shell SM, Yang Z et al. Phosphorylation of nucleotide excision repair factor Xeroderma pigmentosum group A by ataxia telangiectasia mutated and Rad3-related-dependent checkpoint pathway promotes cell survival in response to UV irradiation. Cancer Res 2006; 66:2997-3005.
    • (2006) Cancer Res , vol.66 , pp. 2997-3005
    • Wii, X.1    Shell, S.M.2    Yang, Z.3
  • 34
    • 0037370035 scopus 로고    scopus 로고
    • MBDin, a novel MBD2-interacting protein, relieves MBD2 repression potential and reactivates transcription from methylated promoters
    • Lcmbo F, Pero R, Angrisano T et al. MBDin, a novel MBD2-interacting protein, relieves MBD2 repression potential and reactivates transcription from methylated promoters. Mol Cell Biol 2003; 23:1656-1665.
    • (2003) Mol Cell Biol , vol.23 , pp. 1656-1665
    • Lcmbo, F.1    Pero, R.2    Angrisano, T.3
  • 35
    • 0034326862 scopus 로고    scopus 로고
    • A novel cytoplasmic GTPase XABl interacts with DNA repair protein XPA
    • Nitta M, Saijo M, Kodo N et al. A novel cytoplasmic GTPase XABl interacts with DNA repair protein XPA. Nucleic Acids Res 2000; 28:4212-4218.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4212-4218
    • Nitta, M.1    Saijo, M.2    Kodo, N.3
  • 36
    • 0034634570 scopus 로고    scopus 로고
    • XAB2, a novel tetratricopeptide repeat protein involved in transcription-coupled DNA repair and transcription
    • Nakatsu Y, Asahina H, Citterio E et al. XAB2, a novel tetratricopeptide repeat protein involved in transcription-coupled DNA repair and transcription. J Biol Chem 2000; 275:34931-34937.
    • (2000) J Biol Chem , vol.275 , pp. 34931-34937
    • Nakatsu, Y.1    Asahina, H.2    Citterio, E.3
  • 37
    • 13844321120 scopus 로고    scopus 로고
    • Disruption of mouse XAB2 gene involved in premRNA splicing, transcription and transcription-coupled DNA repair results in preimplantation lethality
    • Yonemasu R, Minami M, Nakatsu Y et al. Disruption of mouse XAB2 gene involved in premRNA splicing, transcription and transcription-coupled DNA repair results in preimplantation lethality. DNA Repair 2005; 4:479-491.
    • (2005) DNA Repair , vol.4 , pp. 479-491
    • Yonemasu, R.1    Minami, M.2    Nakatsu, Y.3
  • 38
    • 33846849467 scopus 로고    scopus 로고
    • ATR-dependent checkpoint modulates XPA nuclear import in response to UV irradiation
    • Wu X, Shell SM, Liu Y et al. ATR-dependent checkpoint modulates XPA nuclear import in response to UV irradiation. Oncogene 2007; 26:757-764.
    • (2007) Oncogene , vol.26 , pp. 757-764
    • Wu, X.1    Shell, S.M.2    Liu, Y.3
  • 39
    • 4544242205 scopus 로고    scopus 로고
    • Mechanisms of DNA damage recognition and strand discrimination in human nucleotide excision repair
    • Dip R, Camenisch U, Naegcli H. Mechanisms of DNA damage recognition and strand discrimination in human nucleotide excision repair. DNA Repair 2004; 3:1409-1423.
    • (2004) DNA Repair , vol.3 , pp. 1409-1423
    • Dip, R.1    Camenisch, U.2    Naegcli, H.3
  • 40
    • 0035929594 scopus 로고    scopus 로고
    • A yeast four-hybrid system identifies Cdk-activating kinase as a regulator of the XPD hehcase, a subunit of transcription factor IIH
    • Sandrock B, Egly JM. A yeast four-hybrid system identifies Cdk-activating kinase as a regulator of the XPD hehcase, a subunit of transcription factor IIH. J Biol Chem 2001; 276:35328-35333.
    • (2001) J Biol Chem , vol.276 , pp. 35328-35333
    • Sandrock, B.1    Egly, J.M.2
  • 41
    • 0031666241 scopus 로고    scopus 로고
    • Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH
    • Coin F, Marinoni JC, Rodolfo C et al. Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH. Nat Genet 1998; 20:184-188.
    • (1998) Nat Genet , vol.20 , pp. 184-188
    • Coin, F.1    Marinoni, J.C.2    Rodolfo, C.3
  • 42
    • 19544366827 scopus 로고    scopus 로고
    • Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions
    • Kellenberger E, Dominguez C, Fribourg S et al. Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions. J Biol Chem 2005; 280:20785-20792.
    • (2005) J Biol Chem , vol.280 , pp. 20785-20792
    • Kellenberger, E.1    Dominguez, C.2    Fribourg, S.3
  • 43
    • 0034669496 scopus 로고    scopus 로고
    • Cloning of a human homolog of the yeast nucleotide excision repair gene MMS19 and interaction with transcription repair factor TFIIH via the XPB and XPD hclicases
    • Seroz T, Winkler GS, Auriol J et al. Cloning of a human homolog of the yeast nucleotide excision repair gene MMS19 and interaction with transcription repair factor TFIIH via the XPB and XPD hclicases. Nucleic Acids Res 2000; 28:4506-4513.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4506-4513
    • Seroz, T.1    Winkler, G.S.2    Auriol, J.3
  • 44
    • 0035968284 scopus 로고    scopus 로고
    • The human homologue of the yeast DNA repair and T F I IH regulator MMS19 is an AF-1-specific coactivator of estrogen receptor
    • Wu X, Li H, Chen JD. The human homologue of the yeast DNA repair and T F I IH regulator MMS19 is an AF-1-specific coactivator of estrogen receptor. J Biol Chem 2001; 276:23962-23968.
    • (2001) J Biol Chem , vol.276 , pp. 23962-23968
    • Wu, X.1    Li, H.2    Chen, J.D.3
  • 45
    • 0035190540 scopus 로고    scopus 로고
    • Robles Al, Harris CC. p53-mediated apoptosis and genomic instability diseases. Acta oncologica (Stockholm, Sweden) 2001; 40:696-701.
    • Robles Al, Harris CC. p53-mediated apoptosis and genomic instability diseases. Acta oncologica (Stockholm, Sweden) 2001; 40:696-701.
  • 46
    • 33645501206 scopus 로고    scopus 로고
    • Redundancy of DNA helicases in p53-mediated apoptosis
    • Spillare EA, Wang XW, von Kobbe C et al. Redundancy of DNA helicases in p53-mediated apoptosis. Oncogene 2006; 25:2119-2123.
    • (2006) Oncogene , vol.25 , pp. 2119-2123
    • Spillare, E.A.1    Wang, X.W.2    von Kobbe, C.3
  • 47
    • 0035957917 scopus 로고    scopus 로고
    • Transcriptional regulation of the TFIIH transcription repair components XPB and XPD by the hepatitis B virus x protein in liver cells and transgenic liver tissue
    • Jaitovich-Groisman I, Benlimame N, Slagle BL et al. Transcriptional regulation of the TFIIH transcription repair components XPB and XPD by the hepatitis B virus x protein in liver cells and transgenic liver tissue. J Biol Chem 2001; 276:14124-14132.
    • (2001) J Biol Chem , vol.276 , pp. 14124-14132
    • Jaitovich-Groisman, I.1    Benlimame, N.2    Slagle, B.L.3
  • 48
    • 0029880959 scopus 로고    scopus 로고
    • Functional interactions between p53 and the TFIIH complex are affected by tumour-associated mutations
    • Leveillard T, Andera L, Bissonnctte N et al. Functional interactions between p53 and the TFIIH complex are affected by tumour-associated mutations. EMBO J 1996; 15:1615-1624.
    • (1996) EMBO J , vol.15 , pp. 1615-1624
    • Leveillard, T.1    Andera, L.2    Bissonnctte, N.3
  • 49
    • 0001655748 scopus 로고
    • Hepatitis B virus X protein inhibits p53 sequence-specific DNA binding, transcriptional activity and association with transcription factor ERCC3
    • Wang XW, Forrester K, Yeh H et al. Hepatitis B virus X protein inhibits p53 sequence-specific DNA binding, transcriptional activity and association with transcription factor ERCC3. PNAS 1994; 91:2230-2234.
    • (1994) PNAS , vol.91 , pp. 2230-2234
    • Wang, X.W.1    Forrester, K.2    Yeh, H.3
  • 50
    • 30744438055 scopus 로고    scopus 로고
    • p8/TTD-A as a repair-specific TFIIH subunit
    • Coin F, Proietti De Santis L, Nardo T et al. p8/TTD-A as a repair-specific TFIIH subunit. Mol Cell 2006; 21:215-226.
    • (2006) Mol Cell , vol.21 , pp. 215-226
    • Coin, F.1    Proietti, D.2    Santis, L.3    Nardo, T.4
  • 51
    • 30944453283 scopus 로고    scopus 로고
    • Characterization of ERCC3 mutations in the Chinese hamster ovary 27-1, UV24 and MMC-2 cell lines
    • Hall H, Gursky J, Nicodcmou A et al. Characterization of ERCC3 mutations in the Chinese hamster ovary 27-1, UV24 and MMC-2 cell lines. Mutat Res 2006; 593:177-186.
    • (2006) Mutat Res , vol.593 , pp. 177-186
    • Hall, H.1    Gursky, J.2    Nicodcmou, A.3
  • 52
    • 0037200120 scopus 로고    scopus 로고
    • p52 Mediates XPB function within the transcription/repair factor TFIIH
    • Jawhari A, Laine JP, Dubaele S et al. p52 Mediates XPB function within the transcription/repair factor TFIIH. J Biol Chem 2002; 277:31761-31767.
    • (2002) J Biol Chem , vol.277 , pp. 31761-31767
    • Jawhari, A.1    Laine, J.P.2    Dubaele, S.3
  • 53
    • 20044387094 scopus 로고    scopus 로고
    • Stimulation of the XPB ATP-dependent helicase by the beta subunit of TFIIE
    • Lin YC, Gralla JD. Stimulation of the XPB ATP-dependent helicase by the beta subunit of TFIIE. Nucleic Acids Res 2005; 33:3072-3081.
    • (2005) Nucleic Acids Res , vol.33 , pp. 3072-3081
    • Lin, Y.C.1    Gralla, J.D.2
  • 54
    • 11244296193 scopus 로고    scopus 로고
    • Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity
    • Coin F, Auriol J, Tapias A et al. Phosphorylation of XPB helicase regulates TFIIH nucleotide excision repair activity. EMBO J 2004; 23:4835-4846.
    • (2004) EMBO J , vol.23 , pp. 4835-4846
    • Coin, F.1    Auriol, J.2    Tapias, A.3
  • 55
    • 0034671692 scopus 로고    scopus 로고
    • The 26S proteasome negatively regulates the level of overall genomic nucleotide excision repair
    • Lommel L, Chen L, Madura K et al. The 26S proteasome negatively regulates the level of overall genomic nucleotide excision repair. Nucleic Acids Res 2000; 28:4839-4845.
    • (2000) Nucleic Acids Res , vol.28 , pp. 4839-4845
    • Lommel, L.1    Chen, L.2    Madura, K.3
  • 56
    • 0030739911 scopus 로고    scopus 로고
    • The XPB subunit of repair/transcription factor TFIIH directly interacts with SUGl, a subunit of the 26S proteasome and putative transcription factor
    • Weeda G, Rossignol M, Eraser RA et al. The XPB subunit of repair/transcription factor TFIIH directly interacts with SUGl, a subunit of the 26S proteasome and putative transcription factor. Nucleic Acids Res 1997; 25:2274-2283.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2274-2283
    • Weeda, G.1    Rossignol, M.2    Eraser, R.A.3
  • 57
    • 0036399626 scopus 로고    scopus 로고
    • Liu J, Meng X and Shen Z. Association of human RAD52 protein with transcription factors. Biochem Biophys Res Commun 2002; 297:1191-1196.\
    • Liu J, Meng X and Shen Z. Association of human RAD52 protein with transcription factors. Biochem Biophys Res Commun 2002; 297:1191-1196.\
  • 58
    • 0141816691 scopus 로고    scopus 로고
    • p210 BCR/ABL kinase regulates nucleotide excision repair (NER) and resistance to UV radiation
    • Canitrot Y, FaUnski R, Louat T et al. p210 BCR/ABL kinase regulates nucleotide excision repair (NER) and resistance to UV radiation. Blood 2003; 102:2632-2637.
    • (2003) Blood , vol.102 , pp. 2632-2637
    • Canitrot, Y.1    FaUnski, R.2    Louat, T.3
  • 59
    • 14844300809 scopus 로고    scopus 로고
    • The spacer region of XPG mediates recruitment to nucleotide excision repair complexes and determines substrate specificity
    • Dimand-Sauthier I, Hohl M, Thorel F et al. The spacer region of XPG mediates recruitment to nucleotide excision repair complexes and determines substrate specificity. J Biol Chem 2005; 280:7030-7037.
    • (2005) J Biol Chem , vol.280 , pp. 7030-7037
    • Dimand-Sauthier, I.1    Hohl, M.2    Thorel, F.3
  • 60
    • 0031104841 scopus 로고    scopus 로고
    • Lieber MR. I h e FEN-1 family of structure-specific nucleases in eukaryotic DNA replication, recombination and repair. Bioessays 1997; 19:233-240.
    • Lieber MR. I h e FEN-1 family of structure-specific nucleases in eukaryotic DNA replication, recombination and repair. Bioessays 1997; 19:233-240.
  • 61
    • 10044268665 scopus 로고    scopus 로고
    • Definition of a short region of XPG necessary for TFIIH interaction and stable recruitment to sites of UV damage
    • Thorel F, Constantinou A, Dunand-Sauthier I et al. Definition of a short region of XPG necessary for TFIIH interaction and stable recruitment to sites of UV damage. Mol Cell Biol 2004; 24:10670-10680.
    • (2004) Mol Cell Biol , vol.24 , pp. 10670-10680
    • Thorel, F.1    Constantinou, A.2    Dunand-Sauthier, I.3
  • 62
    • 0030025947 scopus 로고    scopus 로고
    • Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG and Cockayne syndrome group B (CSB) protein
    • Iyer N, Reagan MS, Wii KJ et al. Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG and Cockayne syndrome group B (CSB) protein. Biochemistry 1996; 35:2157-2167.
    • (1996) Biochemistry , vol.35 , pp. 2157-2167
    • Iyer, N.1    Reagan, M.S.2    Wii, K.J.3
  • 63
    • 33845232596 scopus 로고    scopus 로고
    • Recruitment of the nucleotide excision repair endonuclease XPG to sites of UV-induced dna damage depends on functional TFIIH
    • Zotter A, Luijsterburg MS, Warmerdam DO et al. Recruitment of the nucleotide excision repair endonuclease XPG to sites of UV-induced dna damage depends on functional TFIIH. Mol Cell Biol 2006; 26:8868-8879.
    • (2006) Mol Cell Biol , vol.26 , pp. 8868-8879
    • Zotter, A.1    Luijsterburg, M.S.2    Warmerdam, D.O.3
  • 64
    • 3042547173 scopus 로고    scopus 로고
    • TFIIH contains a PH domain involved in DNA nucleotide excision repair
    • Gervais V, Lamour V, Jawhari A et al. TFIIH contains a PH domain involved in DNA nucleotide excision repair. Nat Struct Mol Biol 2004; 11:616-622.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 616-622
    • Gervais, V.1    Lamour, V.2    Jawhari, A.3
  • 65
    • 0030767281 scopus 로고    scopus 로고
    • The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21
    • Gary R, Ludwig DL, Cornelius HL et al. The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21. J Biol Chem 1997; 272:24522-24529.
    • (1997) J Biol Chem , vol.272 , pp. 24522-24529
    • Gary, R.1    Ludwig, D.L.2    Cornelius, H.L.3
  • 66
    • 26944448202 scopus 로고    scopus 로고
    • Recognition of RNA polymerase II and transcription bubbles by XPG, CSB and TFIIH: Insights for transcription-coupled repair and Cockayne Syndrome
    • Sarker AH, Tsutakawa SE, Kostek S et al. Recognition of RNA polymerase II and transcription bubbles by XPG, CSB and TFIIH: insights for transcription-coupled repair and Cockayne Syndrome. Mol Cell 2005; 20:187-198.
    • (2005) Mol Cell , vol.20 , pp. 187-198
    • Sarker, A.H.1    Tsutakawa, S.E.2    Kostek, S.3
  • 67
    • 0033557139 scopus 로고    scopus 로고
    • Nucleotide excision repair 3' endonuclease XPG stimulates the activity of base excision repair enzyme thymine glycol DNA glycosylase
    • Bessho T. Nucleotide excision repair 3' endonuclease XPG stimulates the activity of base excision repair enzyme thymine glycol DNA glycosylase. Nucleic Acids Res 1999; 27:979-983.
    • (1999) Nucleic Acids Res , vol.27 , pp. 979-983
    • Bessho, T.1
  • 68
    • 0032973211 scopus 로고    scopus 로고
    • Base excision repair of oxidative DNA damage activated by XPG protein
    • Klungland A, Hoss M, Gunz D et al. Base excision repair of oxidative DNA damage activated by XPG protein. Mol Cell 1999; 3:33-42.
    • (1999) Mol Cell , vol.3 , pp. 33-42
    • Klungland, A.1    Hoss, M.2    Gunz, D.3
  • 69
    • 3543003499 scopus 로고    scopus 로고
    • Human N T H l physically interacts with p53 and proliferating cell nuclear antigen
    • Oyama M, Wakasugi M, Hama T et al. Human N T H l physically interacts with p53 and proliferating cell nuclear antigen. Biochem Biophys Res Commun 2004; 321:183-191.
    • (2004) Biochem Biophys Res Commun , vol.321 , pp. 183-191
    • Oyama, M.1    Wakasugi, M.2    Hama, T.3
  • 70
    • 0029095693 scopus 로고
    • Purification and characterization of the XPF-ERCCl complex of human DNA repair excision nuclease
    • Park CH, Bessho T, Matsunaga T et al. Purification and characterization of the XPF-ERCCl complex of human DNA repair excision nuclease. J Biol Chem 1995; 270:22657-22660.
    • (1995) J Biol Chem , vol.270 , pp. 22657-22660
    • Park, C.H.1    Bessho, T.2    Matsunaga, T.3
  • 71
    • 17944361949 scopus 로고    scopus 로고
    • Sequential assembly of the nucleotide excision repair factors in vivo
    • Volker M, Mone MJ, Karmakar P et al. Sequential assembly of the nucleotide excision repair factors in vivo. Mol Cell 2001; 8:213-224.
    • (2001) Mol Cell , vol.8 , pp. 213-224
    • Volker, M.1    Mone, M.J.2    Karmakar, P.3
  • 72
    • 0032529167 scopus 로고    scopus 로고
    • DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair
    • de Laat WL, Appeldoorn E, Sugasawa K et al. DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair. Genes Dev 1998; 12:2598-2609.
    • (1998) Genes Dev , vol.12 , pp. 2598-2609
    • de Laat, W.L.1    Appeldoorn, E.2    Sugasawa, K.3
  • 73
    • 33745033996 scopus 로고    scopus 로고
    • XPA versus ERCCl as chemosensitising agents to cisplatin and mitomycin C in prostate cancer cells: Role of ERCCl in homologous recombination repair
    • Cummings M, Higginbottom K, McGurk CJ et al. XPA versus ERCCl as chemosensitising agents to cisplatin and mitomycin C in prostate cancer cells: role of ERCCl in homologous recombination repair. Biochem Pharmacol 2006; 72:166-175.
    • (2006) Biochem Pharmacol , vol.72 , pp. 166-175
    • Cummings, M.1    Higginbottom, K.2    McGurk, C.J.3
  • 74
    • 1842690842 scopus 로고    scopus 로고
    • Physical and functional interaction between the XPF/ERCCl endonuclease and hRad,52
    • Motycka TA, Bessho T, Post SM et al. Physical and functional interaction between the XPF/ERCCl endonuclease and hRad,52. J Biol Chem 2004; 279:13634-13639.
    • (2004) J Biol Chem , vol.279 , pp. 13634-13639
    • Motycka, T.A.1    Bessho, T.2    Post, S.M.3
  • 75
    • 0347360230 scopus 로고    scopus 로고
    • Functional and physical interactions between ERCCl and MSH2 complexes for resistance to cis- diamminedichloroplatinum(II) in mammaUan cells
    • Lan L, Hayashi T, Rabeya RM et al. Functional and physical interactions between ERCCl and MSH2 complexes for resistance to cis- diamminedichloroplatinum(II) in mammaUan cells. DNA Repair 2004; 3:135-143.
    • (2004) DNA Repair , vol.3 , pp. 135-143
    • Lan, L.1    Hayashi, T.2    Rabeya, R.M.3
  • 76
    • 0037350437 scopus 로고    scopus 로고
    • Nonerythroid alphall spectrin is required for recruitment of FANCA and XPF to nuclear foci induced by DNA interstrand cross-links
    • Sridharan D, Brown M, Lambert WC et al. Nonerythroid alphall spectrin is required for recruitment of FANCA and XPF to nuclear foci induced by DNA interstrand cross-links. J Cell Sci 2003; 116:823-835.
    • (2003) J Cell Sci , vol.116 , pp. 823-835
    • Sridharan, D.1    Brown, M.2    Lambert, W.C.3
  • 77
    • 13444250245 scopus 로고    scopus 로고
    • Thompson LH, Hinz JM, Yamada, N. A et al. How Fanconi anemia proteins promote the four Rs: rephcation, recombination, repair and recovery. Environ Mol Mutagen 2005; 45:128-142.
    • Thompson LH, Hinz JM, Yamada, N. A et al. How Fanconi anemia proteins promote the four Rs: rephcation, recombination, repair and recovery. Environ Mol Mutagen 2005; 45:128-142.
  • 78
    • 28844509443 scopus 로고    scopus 로고
    • The Pso4 mRNA splicing and DNA repair complex interacts with WRN for processing of DNA interstrand cross-links
    • Zhang N, Kaur R, Lu X et al. The Pso4 mRNA splicing and DNA repair complex interacts with WRN for processing of DNA interstrand cross-links. J Biol Chem 2005; 280:40559-40567.
    • (2005) J Biol Chem , vol.280 , pp. 40559-40567
    • Zhang, N.1    Kaur, R.2    Lu, X.3
  • 79
    • 13944263628 scopus 로고    scopus 로고
    • Human telomeric proetin TRF2 associates with genomic double-strand breaks as an early response to DNA damage
    • Bradshaw PS, Stavropoulos DJ and Meyn MS. Human telomeric proetin TRF2 associates with genomic double-strand breaks as an early response to DNA damage. Nat Gen 2005; 37:193-197.
    • (2005) Nat Gen , vol.37 , pp. 193-197
    • Bradshaw, P.S.1    Stavropoulos, D.J.2    Meyn, M.S.3
  • 80
    • 33745288539 scopus 로고    scopus 로고
    • TERF2-XPF: Caught in the middle; beginnings from the end
    • McDaniel LD, Schultz RA and Friedberg EC. TERF2-XPF: caught in the middle; beginnings from the end. DNA Repair 2006; 5:868-872.
    • (2006) DNA Repair , vol.5 , pp. 868-872
    • McDaniel, L.D.1    Schultz, R.A.2    Friedberg, E.C.3
  • 81
    • 27144515686 scopus 로고    scopus 로고
    • XPF nuclease-dependent telomere loss and increased DNA damage in mice overexprcssing TRF2 result in premature aging and cancer
    • Munoz P, Blanco R, Flores JM et al. XPF nuclease-dependent telomere loss and increased DNA damage in mice overexprcssing TRF2 result in premature aging and cancer. Nat Genet 2005; 37:1063-1071.
    • (2005) Nat Genet , vol.37 , pp. 1063-1071
    • Munoz, P.1    Blanco, R.2    Flores, J.M.3
  • 82
    • 0033578040 scopus 로고    scopus 로고
    • The XPV (Xeroderma pigmentosum variant) gene encodes human DNA polymerase eta
    • Masutani C, Kusumoto R, Yamada A et al. The XPV (Xeroderma pigmentosum variant) gene encodes human DNA polymerase eta. Nature 1999; 399:700-704.
    • (1999) Nature , vol.399 , pp. 700-704
    • Masutani, C.1    Kusumoto, R.2    Yamada, A.3
  • 83
    • 0000242262 scopus 로고
    • Xeroderma pigmentosum cells with normal levels of excision repair have a defect in DNA synthesis after UV-irradiation
    • Lehmann AR, Kirk-Bell S, Arlett CF et al. Xeroderma pigmentosum cells with normal levels of excision repair have a defect in DNA synthesis after UV-irradiation. PNAS 1975; 72:219-223.
    • (1975) PNAS , vol.72 , pp. 219-223
    • Lehmann, A.R.1    Kirk-Bell, S.2    Arlett, C.F.3
  • 84
    • 0033548231 scopus 로고    scopus 로고
    • Efficient Bypass of a Thymine-Thymine Dimer by Yeast DNA Polymerase, Poleta
    • Johnson RE, Prakash S and Prakash L. Efficient Bypass of a Thymine-Thymine Dimer by Yeast DNA Polymerase, Poleta. Science 1999; 283:1001-1004.
    • (1999) Science , vol.283 , pp. 1001-1004
    • Johnson, R.E.1    Prakash, S.2    Prakash, L.3
  • 85
    • 18744413609 scopus 로고    scopus 로고
    • Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells
    • Kannouche P, Fernandez de Henestrosa AR, Coull B et al. Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells. EMBO J 2002; 21:6246-6256.
    • (2002) EMBO J , vol.21 , pp. 6246-6256
    • Kannouche, P.1    Fernandez de Henestrosa, A.R.2    Coull, B.3
  • 86
    • 2442417331 scopus 로고    scopus 로고
    • Interaction of human DNA polymerase eta with monoubiquitinated PGNA: A possible mechanism for the polymerase switch in response to DNA damage
    • Kannouche PL, Wing J and Lehmann AR. Interaction of human DNA polymerase eta with monoubiquitinated PGNA: a possible mechanism for the polymerase switch in response to DNA damage. Mol CeU 2004; 14:491-500.
    • (2004) Mol CeU , vol.14 , pp. 491-500
    • Kannouche, P.L.1    Wing, J.2    Lehmann, A.R.3
  • 87
    • 29144499065 scopus 로고    scopus 로고
    • Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis
    • Bienko M, Green CM, Crosetto N et al. Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis. Science 2005; 310:1821-1824.
    • (2005) Science , vol.310 , pp. 1821-1824
    • Bienko, M.1    Green, C.M.2    Crosetto, N.3
  • 88
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen(PCNA): A dancer with many partners
    • Maga G and Hubscher U. Proliferating cell nuclear antigen(PCNA): a dancer with many partners. J Cell Sci 2003; 116:3051-3060.
    • (2003) J Cell Sci , vol.116 , pp. 3051-3060
    • Maga, G.1    Hubscher, U.2
  • 89
    • 9144258471 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen-dependent coordination of the biological functions of human DNA polymerase iota
    • Vidal AE, Kannouche P, Podust VN et al. Proliferating cell nuclear antigen-dependent coordination of the biological functions of human DNA polymerase iota. J Biol Chem 2004; 279:48360-48368.
    • (2004) J Biol Chem , vol.279 , pp. 48360-48368
    • Vidal, A.E.1    Kannouche, P.2    Podust, V.N.3
  • 90
    • 6344288785 scopus 로고    scopus 로고
    • Radl8 guides pol eta to replication stalling sites through physical interaction and PCNA monoubiquitination
    • Watanabe K, Tateishi S, Kawasuji M et al. Radl8 guides pol eta to replication stalling sites through physical interaction and PCNA monoubiquitination. EMBO J 2004; 23:3886-3896.
    • (2004) EMBO J , vol.23 , pp. 3886-3896
    • Watanabe, K.1    Tateishi, S.2    Kawasuji, M.3
  • 91
    • 0034437638 scopus 로고    scopus 로고
    • Roles of DNA polymerase zeta and Revl protein in eukaryotic mutagenesis and translesion replication
    • Lawrence CW, Gibbs PE, Murante RS et al. Roles of DNA polymerase zeta and Revl protein in eukaryotic mutagenesis and translesion replication. Cold Spring Harb Symp Quant Biol 2000; 65:61-69.
    • (2000) Cold Spring Harb Symp Quant Biol , vol.65 , pp. 61-69
    • Lawrence, C.W.1    Gibbs, P.E.2    Murante, R.S.3
  • 92
    • 4544251295 scopus 로고    scopus 로고
    • colocalization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein
    • Tissier A, Kannouche P, Reck MP et al. colocalization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein. DNA Repair 2004; 3:1503-1514.
    • (2004) DNA Repair , vol.3 , pp. 1503-1514
    • Tissier, A.1    Kannouche, P.2    Reck, M.P.3
  • 93
    • 28444470501 scopus 로고    scopus 로고
    • Human DNA polymerase eta promotes DNA synthesis from strand invasion intermediates of homologous recombination
    • Mcllwraith MJ, Vaisman A, Liu Y et al. Human DNA polymerase eta promotes DNA synthesis from strand invasion intermediates of homologous recombination. Mol Cell 2005; 20:783-792.
    • (2005) Mol Cell , vol.20 , pp. 783-792
    • Mcllwraith, M.J.1    Vaisman, A.2    Liu, Y.3
  • 94
    • 0042632884 scopus 로고    scopus 로고
    • Rademakers S, Volker M, Hoogstraten D et al. Xeroderma pigmentosum group A protein loads as a separate factor onto DNA lesions. Mol Ceil Biol 2003; 23:57555767.
    • Rademakers S, Volker M, Hoogstraten D et al. Xeroderma pigmentosum group A protein loads as a separate factor onto DNA lesions. Mol Ceil Biol 2003; 23:57555767.
  • 95
    • 20744446570 scopus 로고    scopus 로고
    • Centrin 2 stimulates nucleotide excision repair by interacting with Xeroderma pigmentosum group C protein
    • Nishi R, Okuda Y, Watanabe E et al. Centrin 2 stimulates nucleotide excision repair by interacting with Xeroderma pigmentosum group C protein. Mol Cell Biol 2005; 25:5664-5674.
    • (2005) Mol Cell Biol , vol.25 , pp. 5664-5674
    • Nishi, R.1    Okuda, Y.2    Watanabe, E.3
  • 96
    • 0035102950 scopus 로고    scopus 로고
    • Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome
    • Araujo SJ, Nigg EA, Wood RD. Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome. Mol Cell Biol 2001; 21:2281-2291.
    • (2001) Mol Cell Biol , vol.21 , pp. 2281-2291
    • Araujo, S.J.1    Nigg, E.A.2    Wood, R.D.3
  • 97
    • 0034721776 scopus 로고    scopus 로고
    • p44/SSLl, the regulatory subunit of the XPD/RAD3 helicase, plays a crucial role in the transcriptional activity of TFIIH
    • Seroz T, Perez C, Bergmann E et al. p44/SSLl, the regulatory subunit of the XPD/RAD3 helicase, plays a crucial role in the transcriptional activity of TFIIH. J Biol Chem 2000; 275:33260-33266.
    • (2000) J Biol Chem , vol.275 , pp. 33260-33266
    • Seroz, T.1    Perez, C.2    Bergmann, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.