메뉴 건너뛰기




Volumn 38, Issue 1, 2003, Pages 1-13

Critical DNA damage recognition functions of XPC-hHR23B and XPA-RPA in nucleotide excision repair

Author keywords

DNA repair; Global genome repair; Transcription coupled repair

Indexed keywords

BINDING PROTEIN; DNA; REPLICATION PROTEIN A; UNCLASSIFIED DRUG; XERODERMA PIGMENTOSUM PROTEIN A REPLICATION PROTEIN A; XERODERMA PIGMENTOSUM PROTEIN C HOMOLOG OF RAD23B;

EID: 0141567801     PISSN: 08991987     EISSN: None     Source Type: Journal    
DOI: 10.1002/mc.10143     Document Type: Review
Times cited : (111)

References (126)
  • 1
    • 0000184202 scopus 로고
    • Effect of monochromatic UV on macromolecular synthesis in E. coli
    • Hanawalt PC, Setlow RB. Effect of monochromatic UV on macromolecular synthesis in E. coli. Biochim Biophys Acta 1960;41:283-294.
    • (1960) Biochim Biophys Acta , vol.41 , pp. 283-294
    • Hanawalt, P.C.1    Setlow, R.B.2
  • 2
    • 0035946009 scopus 로고    scopus 로고
    • Controlling the efficiency of excision repair
    • Hanawalt PC. Controlling the efficiency of excision repair. Mutat Res 2001;485:3-13.
    • (2001) Mutat Res , vol.485 , pp. 3-13
    • Hanawalt, P.C.1
  • 3
    • 0035163025 scopus 로고    scopus 로고
    • Revisiting the rodent repairadox
    • Hanawalt PC. Revisiting the rodent repairadox. Environ Mol Mutagen 2001;38:89-96.
    • (2001) Environ Mol Mutagen , vol.38 , pp. 89-96
    • Hanawalt, P.C.1
  • 4
    • 0001347975 scopus 로고
    • Isolation and identification of the irradiation product of thymine
    • Beukers R, Berends W. Isolation and identification of the irradiation product of thymine. Biochim Biophys Acta 1960;41:550-551.
    • (1960) Biochim Biophys Acta , vol.41 , pp. 550-551
    • Beukers, R.1    Berends, W.2
  • 5
    • 0001388115 scopus 로고
    • Nature of the photoreactivable ultraviolet lesion in DNA
    • Setlow JK, Setlow RB. Nature of the photoreactivable ultraviolet lesion in DNA. Nature 1963;197:560-562.
    • (1963) Nature , vol.197 , pp. 560-562
    • Setlow, J.K.1    Setlow, R.B.2
  • 6
    • 0001526576 scopus 로고
    • Deoxyribonucleic acid replication in bacteria following ultraviolet irradiation
    • Pettijohn D, Hanawalt PC. Deoxyribonucleic acid replication in bacteria following ultraviolet irradiation. Biochim Biophys Acta 1963;72:127-129.
    • (1963) Biochim Biophys Acta , vol.72 , pp. 127-129
    • Pettijohn, D.1    Hanawalt, P.C.2
  • 7
    • 0000830740 scopus 로고
    • Evidence for repair-replication of ultraviolet damaged DNA in bacteria
    • Pettijohn D, Hanawalt PC. Evidence for repair-replication of ultraviolet damaged DNA in bacteria. J Mol Biol 1964;9:395-410.
    • (1964) J Mol Biol , vol.9 , pp. 395-410
    • Pettijohn, D.1    Hanawalt, P.C.2
  • 8
    • 78651191735 scopus 로고
    • The disappearance of thymine dimers from DNA: An error-correcting mechanism
    • Setlow RB, Carrier WL. The disappearance of thymine dimers from DNA: An error-correcting mechanism. Proc Natl Acad Sci USA 1964;51:226-231.
    • (1964) Proc Natl Acad Sci USA , vol.51 , pp. 226-231
    • Setlow, R.B.1    Carrier, W.L.2
  • 9
    • 0001408659 scopus 로고
    • Release of ultraviolet light-induced thymine dimers from DNA in E. coli K-12
    • Boyce R, Howard-Flanders P. Release of ultraviolet light-induced thymine dimers from DNA in E. coli K-12. Proc Natl Acad Sci USA 1964;51:293-300.
    • (1964) Proc Natl Acad Sci USA , vol.51 , pp. 293-300
    • Boyce, R.1    Howard-Flanders, P.2
  • 10
    • 0000781937 scopus 로고
    • Repair replication of DNA in bacteria: Irrelevance of chemical nature of base defect
    • Hanawalt PC, Haynes R. Repair replication of DNA in bacteria: Irrelevance of chemical nature of base defect. Biochem Biophys Res Comm 1965;19:462-467.
    • (1965) Biochem Biophys Res Comm , vol.19 , pp. 462-467
    • Hanawalt, P.C.1    Haynes, R.2
  • 11
    • 0013579690 scopus 로고
    • Repair tracts in mismatched DNA heteroduplexes
    • Wagner R, Jr., Meselson M. Repair tracts in mismatched DNA heteroduplexes. Proc Natl Acad Sci USA 1976;73:4135-4139.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 4135-4139
    • Wagner R., Jr.1    Meselson, M.2
  • 12
    • 0001186415 scopus 로고
    • Evidence for repair of ultra-violet damaged deoxyribonucleic acid in cultured mammalian cells
    • Rasmussen RE, Painter RB. Evidence for repair of ultra-violet damaged deoxyribonucleic acid in cultured mammalian cells. Nature 1964;203:1360-1362.
    • (1964) Nature , vol.203 , pp. 1360-1362
    • Rasmussen, R.E.1    Painter, R.B.2
  • 13
    • 0013898642 scopus 로고
    • Radiation-stimulated DNA synthesis in cultured mammalian cells
    • Rasmussen RE, Painter RB. Radiation-stimulated DNA synthesis in cultured mammalian cells. J Cell Biol 1966;29:11-19.
    • (1966) J Cell Biol , vol.29 , pp. 11-19
    • Rasmussen, R.E.1    Painter, R.B.2
  • 14
    • 0014421995 scopus 로고
    • Defective repair replication of DNA in xeroderma pigmentosum
    • Cleaver JE. Defective repair replication of DNA in xeroderma pigmentosum. Nature 1968;218:652-656.
    • (1968) Nature , vol.218 , pp. 652-656
    • Cleaver, J.E.1
  • 16
    • 0019829568 scopus 로고
    • The causes of cancer: Quantitative estimates of avoidable risks of cancer in the United States today
    • Doll R, Peto R. The causes of cancer: Quantitative estimates of avoidable risks of cancer in the United States today. J Natl Cancer Inst 1981;66:1191-1308.
    • (1981) J Natl Cancer Inst , vol.66 , pp. 1191-1308
    • Doll, R.1    Peto, R.2
  • 18
    • 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, et al. 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 2000;14:349-359.
    • (2000) Genes Dev , vol.14 , pp. 349-359
    • Araujo, S.J.1    Tirode, F.2    Coin, F.3
  • 19
    • 0028948394 scopus 로고
    • Mammalian DNA nucleotide excision repair reconstituted with purified protein components
    • Aboussekhra A, Biggerstaff M, Shivji MK, et al. Mammalian DNA nucleotide excision repair reconstituted with purified protein components. Cell 1995;80:859-868.
    • (1995) Cell , vol.80 , pp. 859-868
    • Aboussekhra, A.1    Biggerstaff, M.2    Shivji, M.K.3
  • 20
    • 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. Reconstitution of human DNA repair excision nuclease in a highly defined system. J Biol Chem 1995;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
  • 21
    • 0030723714 scopus 로고    scopus 로고
    • The DNA damage-recognition problem in human and other eukaryotic cells: The XPA damage binding protein
    • 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.
    • (1997) Biochem J , vol.328 , pp. 1-12
    • Cleaver, J.E.1    States, J.C.2
  • 22
    • 0033538572 scopus 로고    scopus 로고
    • Characterization of DNA recognition by the human UV-damaged DNA-binding protein
    • Fujiwara Y, Masutani C, Mizukoshi T, Kondo J, Hanaoka F, Iwai S. Characterization of DNA recognition by the human UV-damaged DNA-binding protein. J Biol Chem 1999;274:20027-20033.
    • (1999) J Biol Chem , vol.274 , pp. 20027-20033
    • Fujiwara, Y.1    Masutani, C.2    Mizukoshi, T.3    Kondo, J.4    Hanaoka, F.5    Iwai, S.6
  • 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. Mechanism of open complex and dual incision formation by human nucleotide excision repair factors. EMBO J 1997;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
  • 25
    • 0032561318 scopus 로고    scopus 로고
    • Stereoselectivity of human nucleotide excision repair promoted by defective hybridization
    • Hess MT, Naegeli H, Capobianco M. Stereoselectivity of human nucleotide excision repair promoted by defective hybridization. J Biol Chem 1998;273:27867-27872.
    • (1998) J Biol Chem , vol.273 , pp. 27867-27872
    • Hess, M.T.1    Naegeli, H.2    Capobianco, M.3
  • 27
    • 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. A multistep damage recognition mechanism for global genomic nucleotide excision repair. Genes Dev 2001;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
  • 28
    • 0032134423 scopus 로고    scopus 로고
    • Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair
    • Sugasawa K, Ng JM, Masutani C, et al. Xeroderma pigmentosum group C protein complex is the initiator of global genome nucleotide excision repair. Mol Cell 1998;2:223-232.
    • (1998) Mol Cell , vol.2 , pp. 223-232
    • Sugasawa, K.1    Ng, J.M.2    Masutani, C.3
  • 29
    • 0034620554 scopus 로고    scopus 로고
    • Replication protein A interactions with DNA. III. Molecular basis of recognition of damaged DNA
    • Lao Y, Gomes XV, Ren Y, Taylor JS, Wold MS. Replication protein A interactions with DNA. III. Molecular basis of recognition of damaged DNA. Biochemistry 2000;39:850-859.
    • (2000) Biochemistry , vol.39 , pp. 850-859
    • Lao, Y.1    Gomes, X.V.2    Ren, Y.3    Taylor, J.S.4    Wold, M.S.5
  • 30
    • 0029741027 scopus 로고    scopus 로고
    • Overproduction, purification, and characterization of the XPC subunit of the human DNA repair excision nuclease
    • Reardon JT, Mu D, Sancar A. Overproduction, purification, and characterization of the XPC subunit of the human DNA repair excision nuclease. J Biol Chem 1996;271:19451-19456.
    • (1996) J Biol Chem , vol.271 , pp. 19451-19456
    • Reardon, J.T.1    Mu, D.2    Sancar, A.3
  • 31
    • 0035814930 scopus 로고    scopus 로고
    • Binding of XPA and RPA to damaged DNA investigated by fluorescence anisotropy
    • Hey T, Lipps G, Krauss G. Binding of XPA and RPA to damaged DNA investigated by fluorescence anisotropy. Biochemistry 2001;40:2901-2910.
    • (2001) Biochemistry , vol.40 , pp. 2901-2910
    • Hey, T.1    Lipps, G.2    Krauss, G.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
    • 0037195277 scopus 로고    scopus 로고
    • Dimerization of human XPA and formation of XPA2-RPA protein complex
    • Yang ZG, Liu Y, Mao LY, Zhang JT, Zou Y. Dimerization of human XPA and formation of XPA2-RPA protein complex. Biochemistry 2002;41:13012-13020.
    • (2002) Biochemistry , vol.41 , pp. 13012-13020
    • Yang, Z.G.1    Liu, Y.2    Mao, L.Y.3    Zhang, J.T.4    Zou, Y.5
  • 34
    • 0037197844 scopus 로고    scopus 로고
    • Human XPA and RPA DNA repair proteins participate in specific recognition of triplex-induced helical distortions
    • Vasquez KM, Christensen J, Li L, Finch RA, Glazer PM. Human XPA and RPA DNA repair proteins participate in specific recognition of triplex-induced helical distortions. Proc Natl Acad Sci USA 2002;99:5848-5853.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5848-5853
    • Vasquez, K.M.1    Christensen, J.2    Li, L.3    Finch, R.A.4    Glazer, P.M.5
  • 35
    • 0027483739 scopus 로고
    • Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA
    • Jones CJ, Wood RD. Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA. Biochemistry 1993;32:12096-12104.
    • (1993) Biochemistry , vol.32 , pp. 12096-12104
    • Jones, C.J.1    Wood, R.D.2
  • 36
    • 0028089652 scopus 로고
    • The XPA protein is a zinc metalloprotein with an ability to recognize various kinds of DNA damage
    • Asahina H, Kuraoka I, Shirakawa M, et al. The XPA protein is a zinc metalloprotein with an ability to recognize various kinds of DNA damage. Mutat Res 1994;315:229-237.
    • (1994) Mutat Res , vol.315 , pp. 229-237
    • Asahina, H.1    Kuraoka, I.2    Shirakawa, M.3
  • 37
    • 0026076553 scopus 로고
    • Complementation of DNA repair in xeroderma pigmentosum group A cell extracts by a protein with affinity for damaged DNA
    • Robins P, Jones CJ, Biggerstaff M, Lindahl T, Wood RD. Complementation of DNA repair in xeroderma pigmentosum group A cell extracts by a protein with affinity for damaged DNA. EMBO J 1991;10:3913-3921.
    • (1991) EMBO J , vol.10 , pp. 3913-3921
    • Robins, P.1    Jones, C.J.2    Biggerstaff, M.3    Lindahl, T.4    Wood, R.D.5
  • 38
    • 0033603338 scopus 로고    scopus 로고
    • Order of assembly of human DNA repair excision nuclease
    • Wakasugi M, Sancar A. Order of assembly of human DNA repair excision nuclease. J Biol Chem 1999;274:18759-18768.
    • (1999) J Biol Chem , vol.274 , pp. 18759-18768
    • Wakasugi, M.1    Sancar, A.2
  • 39
    • 0028929611 scopus 로고
    • RPA involvement in the damage-recognition and incision steps of nucleotide excision repair
    • He Z, Henricksen LA, Wold MS, Ingles CJ. RPA involvement in the damage-recognition and incision steps of nucleotide excision repair. Nature 1995;374:566-569.
    • (1995) Nature , vol.374 , pp. 566-569
    • He, Z.1    Henricksen, L.A.2    Wold, M.S.3    Ingles, C.J.4
  • 40
    • 0034616963 scopus 로고    scopus 로고
    • Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites
    • Batty D, Rapic'-Otrin V, Levine AS, Wood RD. Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites. J Mol Biol 2000;300:275-290.
    • (2000) J Mol Biol , vol.300 , pp. 275-290
    • Batty, D.1    Rapic'-Otrin, V.2    Levine, A.S.3    Wood, R.D.4
  • 41
    • 0035804828 scopus 로고    scopus 로고
    • Diversity of the damage recognition step in the global genomic nucleotide excision repair in vitro
    • Kusumoto R, Masutani C, Sugasawa K, et al. Diversity of the damage recognition step in the global genomic nucleotide excision repair in vitro. Mutat Res 2001;485:219-227.
    • (2001) Mutat Res , vol.485 , pp. 219-227
    • Kusumoto, R.1    Masutani, C.2    Sugasawa, K.3
  • 42
    • 0025168640 scopus 로고
    • Analysis of a human DNA excision repair gene involved in group A xeroderma pigmentosum and containing a zinc-finger domain
    • Tanaka K, Miura N, Satokata I, et al. Analysis of a human DNA excision repair gene involved in group A xeroderma pigmentosum and containing a zinc-finger domain. Nature 1990;348:73-76.
    • (1990) Nature , vol.348 , pp. 73-76
    • Tanaka, K.1    Miura, N.2    Satokata, I.3
  • 43
    • 0032531868 scopus 로고    scopus 로고
    • Mutational analysis of a function of xeroderma pigmentosum group A (XPA) protein in strand-specific DNA repair
    • Kobayashi T, Takeuchi S, Saijo M, et al. Mutational analysis of a function of xeroderma pigmentosum group A (XPA) protein in strand-specific DNA repair. Nucleic Acids Res 1998;26:4662-4668.
    • (1998) Nucleic Acids Res , vol.26 , pp. 4662-4668
    • Kobayashi, T.1    Takeuchi, S.2    Saijo, M.3
  • 44
    • 0030716255 scopus 로고    scopus 로고
    • Characterization of reaction intermediates of human excision repair nuclease
    • Mu D, Wakasugi M, Hsu DS, Sancar A. Characterization of reaction intermediates of human excision repair nuclease. J Biol Chem 1997;272:28971-28979.
    • (1997) J Biol Chem , vol.272 , pp. 28971-28979
    • Mu, D.1    Wakasugi, M.2    Hsu, D.S.3    Sancar, A.4
  • 45
    • 0029870677 scopus 로고    scopus 로고
    • Reaction mechanism of human DNA repair excision nuclease
    • Mu D, Hsu DS, Sancar A. Reaction mechanism of human DNA repair excision nuclease. J Biol Chem 1996;271:8285-8294.
    • (1996) J Biol Chem , vol.271 , pp. 8285-8294
    • Mu, D.1    Hsu, D.S.2    Sancar, A.3
  • 46
    • 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. An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair. Mol Cell Biol 1995;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
  • 47
    • 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. A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex. DNA Repair (Amst) 2002;1:95-107.
    • (2002) DNA Repair (Amst) , vol.1 , pp. 95-107
    • Sugasawa, K.1    Shimizu, Y.2    Iwai, S.3    Hanaoka, F.4
  • 48
    • 0031053575 scopus 로고    scopus 로고
    • Recognition and repair of compound DNA lesions (base damage and mismatch) by human mismatch repair and excision repair systems
    • Mu D, Tursun M, Duckett DR, Drummond JT, Modrich P, Sancar A. Recognition and repair of compound DNA lesions (base damage and mismatch) by human mismatch repair and excision repair systems. Mol Cell Biol 1997;17:760-769.
    • (1997) Mol Cell Biol , vol.17 , pp. 760-769
    • Mu, D.1    Tursun, M.2    Duckett, D.R.3    Drummond, J.T.4    Modrich, P.5    Sancar, A.6
  • 49
    • 0030751955 scopus 로고    scopus 로고
    • Differential human nucleotide excision repair of paired and mispaired cisplatin-DNA adducts
    • Moggs JG, Szymkowski DE, Yamada M, Karran P, Wood RD. Differential human nucleotide excision repair of paired and mispaired cisplatin-DNA adducts. Nucleic Acids Res 1997;25:480-491.
    • (1997) Nucleic Acids Res , vol.25 , pp. 480-491
    • Moggs, J.G.1    Szymkowski, D.E.2    Yamada, M.3    Karran, P.4    Wood, R.D.5
  • 50
    • 0030944206 scopus 로고    scopus 로고
    • Model for XPC-independent transcription-coupled repair of pyrimidine dimers in humans
    • Mu D, Sancar A. Model for XPC-independent transcription-coupled repair of pyrimidine dimers in humans. J Biol Chem 1997;272:7570-7573.
    • (1997) J Biol Chem , vol.272 , pp. 7570-7573
    • Mu, D.1    Sancar, A.2
  • 51
    • 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. 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    Maekawa, T.3    Sugasawa, K.4    Ohkuma, Y.5    Hanaoka, F.6
  • 52
    • 0032516786 scopus 로고    scopus 로고
    • Interactions of the transcription/DNA repair factor TFIIH and XP repair proteins with DNA lesions in a cell-free repair assay
    • Li RY, Calsou P, Jones CJ, Salles B. Interactions of the transcription/DNA repair factor TFIIH and XP repair proteins with DNA lesions in a cell-free repair assay. J Mol Biol 1998;281:211-218.
    • (1998) J Mol Biol , vol.281 , pp. 211-218
    • Li, R.Y.1    Calsou, P.2    Jones, C.J.3    Salles, B.4
  • 53
    • 0037150494 scopus 로고    scopus 로고
    • The carboxy-terminal domain of the XPC protein plays a crucial role in nucleotide excision repair through interactions with transcription factor IIH
    • Uchida A, Sugasawa K, Masutani C, et al. The carboxy-terminal domain of the XPC protein plays a crucial role in nucleotide excision repair through interactions with transcription factor IIH. DNA Repair (Amst) 2002;1:449-461.
    • (2002) DNA Repair (Amst) , vol.1 , pp. 449-461
    • Uchida, A.1    Sugasawa, K.2    Masutani, C.3
  • 54
    • 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. 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 1995;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
  • 55
    • 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. DNA damage recognition by XPA protein promotes efficient recruitment of transcription factor II H. J Biol Chem 1997;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
  • 56
    • 0035830457 scopus 로고    scopus 로고
    • Novel functional interactions between nucleotide excision DNA repair proteins influencing the enzymatic activities of TFIIH, XPG, and ERCC1-XPF
    • Winkler GS, Sugasawa K, Eker AP, de Laat WL, Hoeijmakers JH. Novel functional interactions between nucleotide excision DNA repair proteins influencing the enzymatic activities of TFIIH, XPG, and ERCC1-XPF. Biochemistry 2001;40:160-165.
    • (2001) Biochemistry , vol.40 , pp. 160-165
    • Winkler, G.S.1    Sugasawa, K.2    Eker, A.P.3    De Laat, W.L.4    Hoeijmakers, J.H.5
  • 57
    • 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
  • 58
    • 0028360068 scopus 로고
    • Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II
    • Drapkin R, Reardon JT, Ansari A, et al. Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II. Nature 1994;368:769-772.
    • (1994) Nature , vol.368 , pp. 769-772
    • Drapkin, R.1    Reardon, J.T.2    Ansari, A.3
  • 59
    • 0027760994 scopus 로고
    • Dual roles of a multiprotein complex from S. cerevisiae in transcription and DNA repair
    • Feaver WJ, Svejstrup JQ, Bardwell L, et al. Dual roles of a multiprotein complex from S. cerevisiae in transcription and DNA repair. Cell 1993;75:1379-1387.
    • (1993) Cell , vol.75 , pp. 1379-1387
    • Feaver, W.J.1    Svejstrup, J.Q.2    Bardwell, L.3
  • 60
    • 0027905008 scopus 로고
    • DNA repair helicase: A component of BTF2 (TFIIH) basic transcription factor
    • Schaeffer L, Roy R, Humbert S, et al. DNA repair helicase: A component of BTF2 (TFIIH) basic transcription factor. Science 1993;260:58-63.
    • (1993) Science , vol.260 , pp. 58-63
    • Schaeffer, L.1    Roy, R.2    Humbert, S.3
  • 62
    • 0023218009 scopus 로고
    • Evidence for two independent pathways of biologically effective excision repair from its rate and extent in cells cultured from sun-sensitive humans
    • Tyrrell RM, Amaudruz F. Evidence for two independent pathways of biologically effective excision repair from its rate and extent in cells cultured from sun-sensitive humans. Cancer Res 1987;47:3725-3728.
    • (1987) Cancer Res , vol.47 , pp. 3725-3728
    • Tyrrell, R.M.1    Amaudruz, F.2
  • 63
    • 0021132406 scopus 로고
    • The rate of removal of pyrimidine dimers in quiescent cultures of normal human and xeroderma pigmentosum cells
    • Kantor GJ, Hull DR. The rate of removal of pyrimidine dimers in quiescent cultures of normal human and xeroderma pigmentosum cells. Mutat Res 1984;132:21-31.
    • (1984) Mutat Res , vol.132 , pp. 21-31
    • Kantor, G.J.1    Hull, D.R.2
  • 64
    • 0025775473 scopus 로고
    • Xeroderma pigmentosum complementation group C cells remove pyrimidine dimers selectively from the transcribed strand of active genes
    • Venema J, van Hoffen A, Karcagi V, Natarajan AT, van Zeeland AA, Mullenders LH. Xeroderma pigmentosum complementation group C cells remove pyrimidine dimers selectively from the transcribed strand of active genes. Mol Cell Biol 1991;11:4128-4134.
    • (1991) Mol Cell Biol , vol.11 , pp. 4128-4134
    • Venema, J.1    Van Hoffen, A.2    Karcagi, V.3    Natarajan, A.T.4    Van Zeeland, A.A.5    Mullenders, L.H.6
  • 65
    • 0023663101 scopus 로고
    • Selective removal of transcription-blocking DNA damage from the transcribed strand of the mammalian DHFR gene
    • Mellon I, Spivak G, Hanawalt PC. Selective removal of transcription-blocking DNA damage from the transcribed strand of the mammalian DHFR gene. Cell 1987;51:241-249.
    • (1987) Cell , vol.51 , pp. 241-249
    • Mellon, I.1    Spivak, G.2    Hanawalt, P.C.3
  • 66
    • 0024426244 scopus 로고
    • Induction of the Escherichia coli lactose operon selectively increases repair of its transcribed DNA strand
    • Mellon I, Hanawalt PC. Induction of the Escherichia coli lactose operon selectively increases repair of its transcribed DNA strand. Nature 1989;342:95-98.
    • (1989) Nature , vol.342 , pp. 95-98
    • Mellon, I.1    Hanawalt, P.C.2
  • 67
    • 0028596398 scopus 로고
    • Transcription-coupled repair and human disease
    • Hanawalt PC. Transcription-coupled repair and human disease. Science 1994;266:1957-1958.
    • (1994) Science , vol.266 , pp. 1957-1958
    • Hanawalt, P.C.1
  • 68
    • 0002225411 scopus 로고
    • Stranded in an active gene
    • Hanawalt PC, Mellon I. Stranded in an active gene. Curr Biol 1993;3:67-69.
    • (1993) Curr Biol , vol.3 , pp. 67-69
    • Hanawalt, P.C.1    Mellon, I.2
  • 69
    • 0028106162 scopus 로고
    • Transcript cleavage by RNA polymerase II arrested by a cyclobutane pyrimidine dimer in the DNA template
    • Donahue BA, Yin S, Taylor JS, Reines D, Hanawalt PC. Transcript cleavage by RNA polymerase II arrested by a cyclobutane pyrimidine dimer in the DNA template. Proc Natl Acad Sci USA 1994;91:8502-8506.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8502-8506
    • Donahue, B.A.1    Yin, S.2    Taylor, J.S.3    Reines, D.4    Hanawalt, P.C.5
  • 70
    • 0034646516 scopus 로고    scopus 로고
    • Transcription-coupled repair of 8-oxoguanine: Requirement for XPG, TFIIH, and CSB and implications for Cockayne syndrome
    • Le Page F, Kwoh EE, Avrutskaya A, et al. Transcription-coupled repair of 8-oxoguanine: Requirement for XPG, TFIIH, and CSB and implications for Cockayne syndrome. Cell 2000;101:159-171.
    • (2000) Cell , vol.101 , pp. 159-171
    • Le Page, F.1    Kwoh, E.E.2    Avrutskaya, A.3
  • 71
    • 0032742715 scopus 로고    scopus 로고
    • DNA damage recognition during nucleotide excision repair in mammalian cells
    • Wood RD. DNA damage recognition during nucleotide excision repair in mammalian cells. Biochimie 1999;81:39-44.
    • (1999) Biochimie , vol.81 , pp. 39-44
    • Wood, R.D.1
  • 72
    • 0020066520 scopus 로고
    • Failure of RNA synthesis to recover after UV irradiation: An early defect in cells from individuals with Cockayne's syndrome and xeroderma pigmentosum
    • Mayne LV, Lehmann AR. Failure of RNA synthesis to recover after UV irradiation: An early defect in cells from individuals with Cockayne's syndrome and xeroderma pigmentosum. Cancer Res 1982;42:1473-1478.
    • (1982) Cancer Res , vol.42 , pp. 1473-1478
    • Mayne, L.V.1    Lehmann, A.R.2
  • 73
    • 0029941444 scopus 로고    scopus 로고
    • The sensitivity of Cockayne's syndrome cells to DNA-damaging agents is not due to defective transcription-coupled repair of active genes
    • van Oosterwijk MF, Versteeg A, Filon R, van Zeeland AA, Mullenders LH. The sensitivity of Cockayne's syndrome cells to DNA-damaging agents is not due to defective transcription-coupled repair of active genes. Mol Cell Biol 1996;16:4436-4444.
    • (1996) Mol Cell Biol , vol.16 , pp. 4436-4444
    • Van Oosterwijk, M.F.1    Versteeg, A.2    Filon, R.3    Van Zeeland, A.A.4    Mullenders, L.H.5
  • 74
    • 0032561475 scopus 로고    scopus 로고
    • RNA polymerase II elongation complexes containing the Cockayne syndrome group B protein interact with a molecular complex containing the transcription factor IIH components xeroderma pigmentosum B and p62
    • Tantin D. RNA polymerase II elongation complexes containing the Cockayne syndrome group B protein interact with a molecular complex containing the transcription factor IIH components xeroderma pigmentosum B and p62. J Biol Chem 1998;273:27794-27799.
    • (1998) J Biol Chem , vol.273 , pp. 27794-27799
    • Tantin, D.1
  • 75
    • 0033358652 scopus 로고    scopus 로고
    • Transcription-coupled repair of DNA damage: Unanticipated players, unexpected complexities
    • Leadon SA. Transcription-coupled repair of DNA damage: Unanticipated players, unexpected complexities. Am J Hum Genet 1999;64:1259-1263.
    • (1999) Am J Hum Genet , vol.64 , pp. 1259-1263
    • Leadon, S.A.1
  • 76
    • 0031020871 scopus 로고    scopus 로고
    • Human transcription-repair coupling factor CSB/ERCC6 is a DNA-stimulated ATPase but is not a helicase and does not disrupt the ternary transcription complex of stalled RNA polymerase II
    • Selby CP, Sancar A. Human transcription-repair coupling factor CSB/ERCC6 is a DNA-stimulated ATPase but is not a helicase and does not disrupt the ternary transcription complex of stalled RNA polymerase II. J Biol Chem 1997;272:1885-1890.
    • (1997) J Biol Chem , vol.272 , pp. 1885-1890
    • Selby, C.P.1    Sancar, A.2
  • 77
    • 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, Wu KJ, Canagarajah B, Friedberg EC. 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    Wu, K.J.3    Canagarajah, B.4    Friedberg, E.C.5
  • 78
    • 0027939024 scopus 로고
    • Interactions of human replication protein A with oligonucleotides
    • Kim C, Paulus BF, Wold MS. Interactions of human replication protein A with oligonucleotides. Biochemistry 1994;33:14197-14206.
    • (1994) Biochemistry , vol.33 , pp. 14197-14206
    • Kim, C.1    Paulus, B.F.2    Wold, M.S.3
  • 79
    • 0026772415 scopus 로고
    • Binding properties of replication protein A from human and yeast cells
    • Kim C, Snyder RO, Wold MS. Binding properties of replication protein A from human and yeast cells. Mol Cell Biol 1992;12:3050-3059.
    • (1992) Mol Cell Biol , vol.12 , pp. 3050-3059
    • Kim, C.1    Snyder, R.O.2    Wold, M.S.3
  • 80
    • 0023140133 scopus 로고
    • Replication of simian virus 40 origin-containing DNA in vitro with purified proteins
    • Wobbe CR, Weissbach L, Borowiec JA, et al. Replication of simian virus 40 origin-containing DNA in vitro with purified proteins. Proc Natl Acad Sci USA 1987;84:1834-1838.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1834-1838
    • Wobbe, C.R.1    Weissbach, L.2    Borowiec, J.A.3
  • 81
    • 0023992803 scopus 로고
    • Purification and characterization of replication protein A, a cellular protein required for in vitro replication of simian virus 40 DNA
    • Wold MS, Kelly T. Purification and characterization of replication protein A, a cellular protein required for in vitro replication of simian virus 40 DNA. Proc Natl Acad Sci USA 1988;85:2523-2527.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2523-2527
    • Wold, M.S.1    Kelly, T.2
  • 82
    • 1842311742 scopus 로고
    • Cellular factors required for multiple stages of SV40 DNA replication in vitro
    • Fairman MP, Stillman B. Cellular factors required for multiple stages of SV40 DNA replication in vitro. EMBO J 1988;7:1211-1218.
    • (1988) EMBO J , vol.7 , pp. 1211-1218
    • Fairman, M.P.1    Stillman, B.2
  • 83
  • 84
    • 0027964775 scopus 로고
    • DNA repair defect in xeroderma pigmentosum group C and complementing factor from HeLa cells
    • Shivji MK, Eker AP, Wood RD. DNA repair defect in xeroderma pigmentosum group C and complementing factor from HeLa cells. J Biol Chem 1994;269:22749-22757.
    • (1994) J Biol Chem , vol.269 , pp. 22749-22757
    • Shivji, M.K.1    Eker, A.P.2    Wood, R.D.3
  • 85
    • 0029019788 scopus 로고
    • Reconstitution of yeast nucleotide excision repair with purified Rad proteins, replication protein A, and transcription factor TFIIH
    • Guzder SN, Habraken Y, Sung P, Prakash L, Prakash S. Reconstitution of yeast nucleotide excision repair with purified Rad proteins, replication protein A, and transcription factor TFIIH. J Biol Chem 1995;270:12973-12976.
    • (1995) J Biol Chem , vol.270 , pp. 12973-12976
    • Guzder, S.N.1    Habraken, Y.2    Sung, P.3    Prakash, L.4    Prakash, S.5
  • 86
    • 0021905437 scopus 로고
    • DNA repair in an active gene: Removal of pyrimidine dimers from the DHFR gene of CHO cells is much more efficient than in the genome overall
    • Bohr VA, Smith CA, Okumoto DS, Hanawalt PC. DNA repair in an active gene: Removal of pyrimidine dimers from the DHFR gene of CHO cells is much more efficient than in the genome overall. Cell 1985;40:359-369.
    • (1985) Cell , vol.40 , pp. 359-369
    • Bohr, V.A.1    Smith, C.A.2    Okumoto, D.S.3    Hanawalt, P.C.4
  • 87
  • 88
    • 0028985014 scopus 로고
    • Transcription-coupled repair removes both cyclobutane pyrimidine dimers and 6-4 photoproducts with equal efficiency and in a sequential way from transcribed DNA in xeroderma pigmentosum group C fibroblasts
    • van Hoffen A, Venema J, Meschini R, van Zeeland AA, Mullenders LH. Transcription-coupled repair removes both cyclobutane pyrimidine dimers and 6-4 photoproducts with equal efficiency and in a sequential way from transcribed DNA in xeroderma pigmentosum group C fibroblasts Embo J 1995;14:360-367.
    • (1995) Embo J , vol.14 , pp. 360-367
    • Van Hoffen, A.1    Venema, J.2    Meschini, R.3    Van Zeeland, A.A.4    Mullenders, L.H.5
  • 89
    • 0034007866 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group C gene leads to selective repair of cyclobutane pyrimidine dimers rather than 6-4 photoproducts
    • Emmert S, Kobayashi N, Khan SG, Kraemer KH. The xeroderma pigmentosum group C gene leads to selective repair of cyclobutane pyrimidine dimers rather than 6-4 photoproducts. Proc Natl Acad Sci USA 2000;97:2151-2156.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2151-2156
    • Emmert, S.1    Kobayashi, N.2    Khan, S.G.3    Kraemer, K.H.4
  • 90
    • 0027408241 scopus 로고
    • Purification and characterization of a human protein that binds to damaged DNA
    • Hwang BJ, Chu G. Purification and characterization of a human protein that binds to damaged DNA. Biochemistry 1993;32:1657-1666.
    • (1993) Biochemistry , vol.32 , pp. 1657-1666
    • Hwang, B.J.1    Chu, G.2
  • 91
    • 0031023182 scopus 로고    scopus 로고
    • Reconstitution of human excision nuclease with recombinant XPF-ERCC1 complex
    • Bessho T, Sancar A, Thompson LH, Thelen MP. Reconstitution of human excision nuclease with recombinant XPF-ERCC1 complex. J Biol Chem 1997;272:3833-3837.
    • (1997) J Biol Chem , vol.272 , pp. 3833-3837
    • Bessho, T.1    Sancar, A.2    Thompson, L.H.3    Thelen, M.P.4
  • 92
    • 0033636515 scopus 로고    scopus 로고
    • Xeroderma pigmentosum p48 gene enhances global genomic repair and suppresses UV-induced mutagenesis
    • Tang JY, Hwang BJ, Ford JM, Hanawalt PC, Chu G. Xeroderma pigmentosum p48 gene enhances global genomic repair and suppresses UV-induced mutagenesis. Mol Cell 2000;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
  • 93
    • 0000516293 scopus 로고    scopus 로고
    • Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair
    • Hwang BJ, Ford JM, Hanawalt PC, Chu G. Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair. Proc Natl Acad Sci USA 1999;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
  • 94
    • 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. 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 2001;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
  • 95
    • 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, et al. DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair. J Biol Chem 2002;277:1637-1640.
    • (2002) J Biol Chem , vol.277 , pp. 1637-1640
    • Wakasugi, M.1    Kawashima, A.2    Morioka, H.3
  • 96
    • 0026480243 scopus 로고
    • Binding of human single-stranded DNA binding protein to DNA damaged by the anticancer drug cis-diamminedichloroplatinum (11)
    • Clugston CK, McLaughlin K, Kenny MK, Brown R. Binding of human single-stranded DNA binding protein to DNA damaged by the anticancer drug cis-diamminedichloroplatinum (11). Cancer Res 1992;52:6375-6379.
    • (1992) Cancer Res , vol.52 , pp. 6375-6379
    • Clugston, C.K.1    McLaughlin, K.2    Kenny, M.K.3    Brown, R.4
  • 97
    • 0032537491 scopus 로고    scopus 로고
    • Human replication protein A preferentially binds cisplatin-damaged duplex DNA in vitro
    • Patrick SM, Turchi JJ. Human replication protein A preferentially binds cisplatin-damaged duplex DNA in vitro. Biochemistry 1998;37:8808-8815.
    • (1998) Biochemistry , vol.37 , pp. 8808-8815
    • Patrick, S.M.1    Turchi, J.J.2
  • 98
    • 0033179499 scopus 로고    scopus 로고
    • Photocrosslinking locates a binding site for the large subunit of human replication protein A to the damaged strand of cisplatin-modified DNA
    • Schweizer U, Hey T, Lipps G, Krauss G. Photocrosslinking locates a binding site for the large subunit of human replication protein A to the damaged strand of cisplatin-modified DNA. Nucleic Acids Res 1999;27:3183-3189.
    • (1999) Nucleic Acids Res , vol.27 , pp. 3183-3189
    • Schweizer, U.1    Hey, T.2    Lipps, G.3    Krauss, G.4
  • 99
    • 0036318818 scopus 로고    scopus 로고
    • Molecular anatomy of the human excision nuclease assembled at sites of DNA damage
    • Reardon JT, Sancar A. Molecular anatomy of the human excision nuclease assembled at sites of DNA damage. Mol Cell Biol 2002;22:5938-5945.
    • (2002) Mol Cell Biol , vol.22 , pp. 5938-5945
    • Reardon, J.T.1    Sancar, A.2
  • 100
    • 0030908093 scopus 로고    scopus 로고
    • Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
    • Wold MS. Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism. Annu Rev Biochem 1997;66:61-92.
    • (1997) Annu Rev Biochem , vol.66 , pp. 61-92
    • Wold, M.S.1
  • 101
    • 0031893854 scopus 로고    scopus 로고
    • Triplex-directed modification of genes and gene activity
    • Vasquez KM, Wilson JH. Triplex-directed modification of genes and gene activity. Trends Biochem Sci 1998;23:4-9.
    • (1998) Trends Biochem Sci , vol.23 , pp. 4-9
    • Vasquez, K.M.1    Wilson, J.H.2
  • 102
    • 0036120314 scopus 로고    scopus 로고
    • Triplex-forming oligonucleotides: Principles and applications
    • Vasquez KM, Glazer PM. Triplex-forming oligonucleotides: Principles and applications. Q Rev Biophys 2002;35:89-107.
    • (2002) Q Rev Biophys , vol.35 , pp. 89-107
    • Vasquez, K.M.1    Glazer, P.M.2
  • 103
    • 0034724438 scopus 로고    scopus 로고
    • Unambiguous demonstration of triple-helix-directed gene modification
    • Barre FX, Ait-Si-Ali S, Giovannangeli C, et al. Unambiguous demonstration of triple-helix-directed gene modification. Proc Natl Acad Sci USA 2000;97:3084-3088.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3084-3088
    • Barre, F.X.1    Ait-Si-Ali, S.2    Giovannangeli, C.3
  • 104
    • 0033766239 scopus 로고    scopus 로고
    • Specific mutations induced by triplex-forming oligonucleotides in mice
    • Vasquez KM, Narayanan L, Glazer PM. Specific mutations induced by triplex-forming oligonucleotides in mice. Science 2000;290:530-533.
    • (2000) Science , vol.290 , pp. 530-533
    • Vasquez, K.M.1    Narayanan, L.2    Glazer, P.M.3
  • 105
    • 0033981578 scopus 로고    scopus 로고
    • Triple-helix formation induces recombination in mammalian cells via a nucleotide excision repair-dependent pathway
    • Faruqi AF, Datta HJ, Carroll D, Seidman MM, Glazer PM. Triple-helix formation induces recombination in mammalian cells via a nucleotide excision repair-dependent pathway. Mol Cell Biol 2000;20:990-1000.
    • (2000) Mol Cell Biol , vol.20 , pp. 990-1000
    • Faruqi, A.F.1    Datta, H.J.2    Carroll, D.3    Seidman, M.M.4    Glazer, P.M.5
  • 106
    • 0035947657 scopus 로고    scopus 로고
    • Triplex-induced recombination in human cell-free extracts. Dependence on XPA and HsRad51
    • Datta HJ, Chan PP, Vasquez KM, Gupta RC, Glazer PM. Triplex-induced recombination in human cell-free extracts. Dependence on XPA and HsRad51. J Biol Chem 2001;276:18018-18023.
    • (2001) J Biol Chem , vol.276 , pp. 18018-18023
    • Datta, H.J.1    Chan, P.P.2    Vasquez, K.M.3    Gupta, R.C.4    Glazer, P.M.5
  • 107
    • 0033557144 scopus 로고    scopus 로고
    • Chromosomal mutations induced by triplex-forming oligonucleotides in mammalian cells
    • Vasquez KM, Wang G, Havre PA, Glazer PM. Chromosomal mutations induced by triplex-forming oligonucleotides in mammalian cells. Nucleic Acids Res 1999;27:1176-1181.
    • (1999) Nucleic Acids Res , vol.27 , pp. 1176-1181
    • Vasquez, K.M.1    Wang, G.2    Havre, P.A.3    Glazer, P.M.4
  • 108
    • 0030059301 scopus 로고    scopus 로고
    • Mutagenesis in mammalian cells induced by triple helix formation and transcription-coupled repair
    • Wang G, Seidman MM, Glazer PM. Mutagenesis in mammalian cells induced by triple helix formation and transcription-coupled repair. Science 1996;271:802-805.
    • (1996) Science , vol.271 , pp. 802-805
    • Wang, G.1    Seidman, M.M.2    Glazer, P.M.3
  • 109
    • 0030801529 scopus 로고    scopus 로고
    • Isolation of human complexes proficient in nucleotide excision repair
    • He Z, Ingles CJ. Isolation of human complexes proficient in nucleotide excision repair. Nucleic Acids Res 1997;25:1136-1141.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1136-1141
    • He, Z.1    Ingles, C.J.2
  • 110
    • 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
  • 111
    • 0034732890 scopus 로고    scopus 로고
    • Genomic heterogeneity of nucleotide excision repair
    • Balajee AS, Bohr VA. Genomic heterogeneity of nucleotide excision repair. Gene 2000;250:15-30.
    • (2000) Gene , vol.250 , pp. 15-30
    • Balajee, A.S.1    Bohr, V.A.2
  • 112
    • 0031743602 scopus 로고    scopus 로고
    • Efficient PCNA complex formation is dependent upon both transcription coupled repair and genome overall repair
    • Balajee AS, May A, Dianova I, Bohr VA. Efficient PCNA complex formation is dependent upon both transcription coupled repair and genome overall repair. Mutat Res 1998;409:135-146.
    • (1998) Mutat Res , vol.409 , pp. 135-146
    • Balajee, A.S.1    May, A.2    Dianova, I.3    Bohr, V.A.4
  • 113
    • 0032480043 scopus 로고    scopus 로고
    • Fine structural analysis of DNA repair in mammalian cells
    • Balajee AS, May A, Bohr VA. Fine structural analysis of DNA repair in mammalian cells. Mutat Res 1998;404:3-11.
    • (1998) Mutat Res , vol.404 , pp. 3-11
    • Balajee, A.S.1    May, A.2    Bohr, V.A.3
  • 114
    • 0032480021 scopus 로고    scopus 로고
    • UV-induced alterations in the spatial distribution of the basal transcription factor TFIIH: An early event in nucleotide excision repair
    • Karmarkar P, Leer-van Hoffen A, Natarajan AT, van Zeeland AA, Mullenders LH. UV-induced alterations in the spatial distribution of the basal transcription factor TFIIH: An early event in nucleotide excision repair. Mutat Res 1998;404:129-131.
    • (1998) Mutat Res , vol.404 , pp. 129-131
    • Karmarkar, P.1    Leer-van Hoffen, A.2    Natarajan, A.T.3    Van Zeeland, A.A.4    Mullenders, L.H.5
  • 115
    • 0028823744 scopus 로고
    • Detection of nucleotide excision repair incisions in human fibroblasts by immunostaining for PCNA
    • Aboussekhra A, Wood RD. Detection of nucleotide excision repair incisions in human fibroblasts by immunostaining for PCNA. Exp Cell Res 1995;221:326-332.
    • (1995) Exp Cell Res , vol.221 , pp. 326-332
    • Aboussekhra, A.1    Wood, R.D.2
  • 116
    • 0030578442 scopus 로고    scopus 로고
    • Roles of XPG and XPF/ERCC1 endonucleases in UV-induced immunostaining of PCNA in fibroblasts
    • Miura M, Nakamura S, Sasaki T, Takasaki Y, Shiomi T, Yamaizumi M. Roles of XPG and XPF/ERCC1 endonucleases in UV-induced immunostaining of PCNA in fibroblasts. Exp Cell Res 1996;226:126-132.
    • (1996) Exp Cell Res , vol.226 , pp. 126-132
    • Miura, M.1    Nakamura, S.2    Sasaki, T.3    Takasaki, Y.4    Shiomi, T.5    Yamaizumi, M.6
  • 117
    • 0030971289 scopus 로고    scopus 로고
    • Translocation of a UV-damaged DNA binding protein into a tight association with chromatin after treatment of mammalian cells with UV light
    • Otrin VR, McLenigan M, Takao M, Levine AS, Protic M. Translocation of a UV-damaged DNA binding protein into a tight association with chromatin after treatment of mammalian cells with UV light. J Cell Sci 1997;110(Pt 10): 159-1168.
    • (1997) J Cell Sci , vol.110 , Issue.PART 10 , pp. 1159-1168
    • Otrin, V.R.1    McLenigan, M.2    Takao, M.3    Levine, A.S.4    Protic, M.5
  • 118
    • 0029738720 scopus 로고    scopus 로고
    • Ultraviolet-induced movement of the human DNA repair protein, Xeroderma pigmentosum type G, in the nucleus
    • Park MS, Knauf JA, Pendergrass SH, et al. Ultraviolet-induced movement of the human DNA repair protein, Xeroderma pigmentosum type G, in the nucleus. Proc Natl Acad Sci USA 1996;93:8368-8373.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8368-8373
    • Park, M.S.1    Knauf, J.A.2    Pendergrass, S.H.3
  • 120
    • 0035816649 scopus 로고    scopus 로고
    • DNA repair excision nuclease attacks undamaged DNA. A potential source of spontaneous mutations
    • Branum ME, Reardon JT, Sancar A. DNA repair excision nuclease attacks undamaged DNA. A potential source of spontaneous mutations. J Biol Chem 2001;276:25421-25426.
    • (2001) J Biol Chem , vol.276 , pp. 25421-25426
    • Branum, M.E.1    Reardon, J.T.2    Sancar, A.3
  • 121
    • 0037188408 scopus 로고    scopus 로고
    • The XPC-HR23B complex displays high affinity and specificity for damaged DNA in a true-equilibrium fluorescence assay
    • Hey T, Lipps G, Sugasawa K, Iwai S, Hanaoka F, Krauss G. The XPC-HR23B complex displays high affinity and specificity for damaged DNA in a true-equilibrium fluorescence assay. Biochemistry 2002;41:6583-6587.
    • (2002) Biochemistry , vol.41 , pp. 6583-6587
    • Hey, T.1    Lipps, G.2    Sugasawa, K.3    Iwai, S.4    Hanaoka, F.5    Krauss, G.6
  • 122
    • 0037133229 scopus 로고    scopus 로고
    • Strand-specific binding of RPA and XPA to damaged duplex DNA
    • Hermanson-Miller IL, Turchi JJ. Strand-specific binding of RPA and XPA to damaged duplex DNA. Biochemistry 2002;41:2402-2408.
    • (2002) Biochemistry , vol.41 , pp. 2402-2408
    • Hermanson-Miller, I.L.1    Turchi, J.J.2
  • 123
    • 0036732039 scopus 로고    scopus 로고
    • Transcription-coupled nucleotide excision repair as a determinant of cisplatin sensitivity of human cells
    • Furuta T, Ueda T, Aune G, Sarasin A, Kraemer KH, Pommier Y. Transcription-coupled nucleotide excision repair as a determinant of cisplatin sensitivity of human cells. Cancer Res 2002;62:4899-4902.
    • (2002) Cancer Res , vol.62 , pp. 4899-4902
    • Furuta, T.1    Ueda, T.2    Aune, G.3    Sarasin, A.4    Kraemer, K.H.5    Pommier, Y.6
  • 124
    • 0029742577 scopus 로고    scopus 로고
    • HHR23B, a human Rad23 homolog, stimulates XPC protein in nucleotide excision repair in vitro
    • Sugasawa K, Masutani C, Uchida A, et al. HHR23B, a human Rad23 homolog, stimulates XPC protein in nucleotide excision repair in vitro. Mol Cell Biol 1996;16:4852-4861.
    • (1996) Mol Cell Biol , vol.16 , pp. 4852-4861
    • Sugasawa, K.1    Masutani, C.2    Uchida, A.3
  • 125
    • 0030688064 scopus 로고    scopus 로고
    • Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity
    • Sugasawa K, Ng JM, Masutani C, et al. Two human homologs of Rad23 are functionally interchangeable in complex formation and stimulation of XPC repair activity. Mol Cell Biol 1997;17:6924-6931.
    • (1997) Mol Cell Biol , vol.17 , pp. 6924-6931
    • Sugasawa, K.1    Ng, J.M.2    Masutani, C.3
  • 126
    • 0029911744 scopus 로고    scopus 로고
    • Analysis of incision sites produced by human cell extracts and purified proteins during nucleotide excision repair of a 1,3-intrastrand d(GpTpG)-cisplatin adduct
    • Moggs JG, Yarema KJ, Essigmann JM, Wood RD. Analysis of incision sites produced by human cell extracts and purified proteins during nucleotide excision repair of a 1,3-intrastrand d(GpTpG)-cisplatin adduct. J Biol Chem 1996;271:7177-7186.
    • (1996) J Biol Chem , vol.271 , pp. 7177-7186
    • Moggs, J.G.1    Yarema, K.J.2    Essigmann, J.M.3    Wood, R.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.