메뉴 건너뛰기




Volumn 85, Issue 11, 2003, Pages 1083-1099

The eukaryotic nucleotide excision repair pathway

Author keywords

Apoptosis; DNA lesions; DNA repair; Evolution; Ultraviolet

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CSB PROTEIN; DNA REPAIR PROTEIN; ENDONUCLEASE; HELICASE; PROTEIN; PROTEIN P48; PROTEIN P53; RNA POLYMERASE; RPA PROTEIN; UNCLASSIFIED DRUG; XERODERMA PIGMENTOSUM GROUP C PROTEIN; XPA PROTEIN; XPE PROTEIN; XPF PROTEIN;

EID: 0942278966     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2003.10.017     Document Type: Short Survey
Times cited : (296)

References (165)
  • 1
    • 0035495386 scopus 로고    scopus 로고
    • How nucleotide excision repair protects against cancer
    • Friedberg E.C. How nucleotide excision repair protects against cancer. Nat. Rev. Cancer. 1:2001;22-33.
    • (2001) Nat. Rev. Cancer , vol.1 , pp. 22-33
    • Friedberg, E.C.1
  • 2
    • 0035234162 scopus 로고    scopus 로고
    • Xeroderma pigmentosum and related disorders: Defects in DNA repair and transcription
    • Berneburg M., Lehmann A.R. Xeroderma pigmentosum and related disorders: defects in DNA repair and transcription. Adv. Genet. 43:2001;71-102.
    • (2001) Adv. Genet , vol.43 , pp. 71-102
    • Berneburg, M.1    Lehmann, A.R.2
  • 6
    • 0037115936 scopus 로고    scopus 로고
    • Subpathways of nucleotide excision repair and their regulation
    • Hanawalt P.C. Subpathways of nucleotide excision repair and their regulation. Oncogene. 21:2002;8949-8956.
    • (2002) Oncogene , vol.21 , pp. 8949-8956
    • Hanawalt, P.C.1
  • 7
    • 0032738023 scopus 로고    scopus 로고
    • Effect of DNA lesions on transcription elongation
    • Tornaletti S., Hanawalt P.C. Effect of DNA lesions on transcription elongation. Biochimie. 81:1999;139-146.
    • (1999) Biochimie , vol.81 , pp. 139-146
    • Tornaletti, S.1    Hanawalt, P.C.2
  • 8
    • 0032740449 scopus 로고    scopus 로고
    • Chromatin rearrangements during nucleotide excision repair
    • Moggs J.G., Almouzni G. Chromatin rearrangements during nucleotide excision repair. Biochimie. 81:1999;45-52.
    • (1999) Biochimie , vol.81 , pp. 45-52
    • Moggs, J.G.1    Almouzni, G.2
  • 10
    • 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. 275:2000;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
  • 12
    • 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. 15:2001;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
  • 13
    • 0026697582 scopus 로고
    • Expression cloning of a human DNA repair gene involved in xeroderma pigmentosum group C
    • Legerski R., Peterson C. Expression cloning of a human DNA repair gene involved in xeroderma pigmentosum group C. Nature. 359:1992;70-73.
    • (1992) Nature , vol.359 , pp. 70-73
    • Legerski, R.1    Peterson, C.2
  • 15
    • 0035374836 scopus 로고    scopus 로고
    • Centrosome protein cetrin2/caltractin1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair
    • Araki M., Masutani C., Takemura M., Uchida A., Sugasawa K., Kondoh J., Ohkuma Y., Hanaoka F. Centrosome protein cetrin2/caltractin1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair. J. Biol. Chem. 276:2001;18665-18672.
    • (2001) J. Biol. Chem , vol.276 , pp. 18665-18672
    • Araki, M.1    Masutani, C.2    Takemura, M.3    Uchida, A.4    Sugasawa, K.5    Kondoh, J.6    Ohkuma, Y.7    Hanaoka, F.8
  • 18
    • 0038339144 scopus 로고    scopus 로고
    • A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein
    • Ng J.M., Vermeulen W., van der Horst G.T., Bergink S., Sugasawa K., Vrieling H., Hoeijmakers J.H. A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein. Genes Dev. 17:2003;1630-1645.
    • (2003) Genes Dev , vol.17 , pp. 1630-1645
    • Ng, J.M.1    Vermeulen, W.2    Van Der Horst, G.T.3    Bergink, S.4    Sugasawa, K.5    Vrieling, H.6    Hoeijmakers, J.H.7
  • 19
    • 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., Dohmae N., Araki M., Yokoi M., Ohkuma Y., Hanaoka F. The carboxy-terminal domain of the XPC protein plays a crucial role in nucleotide excision repair through interactions with transcription factor IIH. DNA Repair. 1:2002;449-461.
    • (2002) DNA Repair , vol.1 , pp. 449-461
    • Uchida, A.1    Sugasawa, K.2    Masutani, C.3    Dohmae, N.4    Araki, M.5    Yokoi, M.6    Ohkuma, Y.7    Hanaoka, F.8
  • 21
    • 0033636515 scopus 로고    scopus 로고
    • Xeroderma pigmentosum p48 gene enhances global genomic repair and suppresses UV-induced mutagenesis
    • Tang J.Y., Hwang B.J., Ford J.M., Hanawalt P.C., Chu G. Xeroderma pigmentosum p48 gene enhances global genomic repair and suppresses UV-induced mutagenesis. Mol. Cell. 5:2000;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
  • 22
    • 0027408241 scopus 로고
    • Purification and characterization of a human protein that binds to damaged DNA
    • Hwang B.J., Chu G. Purification and characterization of a human protein that binds to damaged DNA. Biochemistry. 32:1993;1657-1666.
    • (1993) Biochemistry , vol.32 , pp. 1657-1666
    • Hwang, B.J.1    Chu, G.2
  • 23
    • 0029768095 scopus 로고    scopus 로고
    • Mutations specific to the xeroderma pigmentosum group e DDB-phenotype
    • Nichols A.F., Ong P., Linn S. Mutations specific to the xeroderma pigmentosum group E DDB-phenotype. J. Biol. Chem. 271:1996;24317-24320.
    • (1996) J. Biol. Chem , vol.271 , pp. 24317-24320
    • Nichols, A.F.1    Ong, P.2    Linn, S.3
  • 24
    • 0038105065 scopus 로고    scopus 로고
    • True XP group e patients have a defective UV-damaged DNA binding protein complex and mutations in DDB2 which reveal the functional domains of its p48 product
    • Rapic-Otrin V., Navazza V., Nardo T., Botta E., McLenigan M., Bisi D.C., Levine A.S., Stefanini M. True XP group E patients have a defective UV-damaged DNA binding protein complex and mutations in DDB2 which reveal the functional domains of its p48 product. Hum. Mol. Genet. 12:2003;1507-1522.
    • (2003) Hum. Mol. Genet , vol.12 , pp. 1507-1522
    • Rapic-Otrin, V.1    Navazza, V.2    Nardo, T.3    Botta, E.4    McLenigan, M.5    Bisi, D.C.6    Levine, A.S.7    Stefanini, M.8
  • 25
    • 0345306615 scopus 로고    scopus 로고
    • In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by the DDB2 gene product
    • Fitch M.E., Nakajima S., Yasui A., Ford J.M. In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by the DDB2 gene product. J. Biol. Chem. 278:2003;46906-46910.
    • (2003) J. Biol. Chem , vol.278 , pp. 46906-46910
    • Fitch, M.E.1    Nakajima, S.2    Yasui, A.3    Ford, J.M.4
  • 26
    • 0000516293 scopus 로고    scopus 로고
    • Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair
    • Hwang B.J., Ford J.M., Hanawalt P.C., Chu G. Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair. Proc. Natl. Acad. Sci. USA. 96:1999;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
  • 27
    • 0035930582 scopus 로고    scopus 로고
    • UV-damaged DNA-binding proteins are targets of CUL-4A-mediated ubiquitination and degradation
    • Chen X., Zhang Y., Douglas L., Zhou P. UV-damaged DNA-binding proteins are targets of CUL-4A-mediated ubiquitination and degradation. J. Biol. Chem. 276:2001;48175-48182.
    • (2001) J. Biol. Chem , vol.276 , pp. 48175-48182
    • Chen, X.1    Zhang, Y.2    Douglas, L.3    Zhou, P.4
  • 30
    • 0037039443 scopus 로고    scopus 로고
    • Translocation of Cockayne's syndrome group a protein to the nuclear matrix: Possible relevance to transcription-coupled DNA repair
    • Kamiuchi S., Saijo M., Citterio E., de Jager M., Hoeijmakers J.H.J., Tanaka K. Translocation of Cockayne's syndrome group A protein to the nuclear matrix: possible relevance to transcription-coupled DNA repair. Proc. Natl. Acad. Sci. USA. 99:2002;201-206.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 201-206
    • Kamiuchi, S.1    Saijo, M.2    Citterio, E.3    De Jager, M.4    Hoeijmakers, J.H.J.5    Tanaka, K.6
  • 32
    • 0030667078 scopus 로고    scopus 로고
    • Recruitment of the putative transcription-repair coupling factor CSB/ERCC6 to RNA polymerase II elongation complexes
    • Tantin D., Kansal A., Carey M. Recruitment of the putative transcription-repair coupling factor CSB/ERCC6 to RNA polymerase II elongation complexes. Mol. Cell. Biol. 17:1997;6803-6814.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 6803-6814
    • Tantin, D.1    Kansal, A.2    Carey, M.3
  • 33
    • 0032561475 scopus 로고    scopus 로고
    • RNA polymerase II elongation complexes containing the Cockayne's 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's syndrome group B protein interact with a molecular complex containing the transcription factor IIH components xeroderma pigmentosum B and p62. J. Biol. Chem. 273:1998;27794-27799.
    • (1998) J. Biol. Chem , vol.273 , pp. 27794-27799
    • Tantin, D.1
  • 34
    • 0030902253 scopus 로고    scopus 로고
    • Reduced RNA polymerase II transcription in intact and permeabilized Cockayne's syndrome group B cells
    • Balajee A.S., May A., Dianov G.L., Friedberg E.C., Bohr V.A. Reduced RNA polymerase II transcription in intact and permeabilized Cockayne's syndrome group B cells. Proc. Natl. Acad. Sci. USA. 94:1997;4306-4311.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4306-4311
    • Balajee, A.S.1    May, A.2    Dianov, G.L.3    Friedberg, E.C.4    Bohr, V.A.5
  • 35
    • 0030862095 scopus 로고    scopus 로고
    • Reduced RNA polymerase II transcription in extracts of Cockayne's syndrome and xeroderma pigmentosum/Cockayne's syndrome cells
    • Dianov G.L., Houle J.F., Iyer N., Bohr V.A., Friedberg E.C. Reduced RNA polymerase II transcription in extracts of Cockayne's syndrome and xeroderma pigmentosum/Cockayne's syndrome cells. Nucleic Acids Res. 25:1997;3636-3642.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3636-3642
    • Dianov, G.L.1    Houle, J.F.2    Iyer, N.3    Bohr, V.A.4    Friedberg, E.C.5
  • 36
    • 0030822591 scopus 로고    scopus 로고
    • Cockayne's syndrome group B protein enhances elongation by RNA polymerase II
    • Selby C.P., Sancar A. Cockayne's syndrome group B protein enhances elongation by RNA polymerase II. Proc. Natl. Acad. Sci. USA. 94:1997;11205-11209.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11205-11209
    • Selby, C.P.1    Sancar, A.2
  • 39
    • 0037154203 scopus 로고    scopus 로고
    • Transcription-coupled repair in RNA polymerase I-transcribed genes of yeast
    • Conconi A., Bespalov V.A., Smerdon M.J. Transcription-coupled repair in RNA polymerase I-transcribed genes of yeast. Proc. Natl. Acad. Sci. USA. 99:2002;649-654.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 649-654
    • Conconi, A.1    Bespalov, V.A.2    Smerdon, M.J.3
  • 40
    • 0027370604 scopus 로고
    • Lack of transcription-coupled repair in mammalian ribosomal RNA genes
    • Christians F.C., Hanawalt P.C. Lack of transcription-coupled repair in mammalian ribosomal RNA genes. Biochemistry. 32:1993;10512-10518.
    • (1993) Biochemistry , vol.32 , pp. 10512-10518
    • Christians, F.C.1    Hanawalt, P.C.2
  • 41
    • 0031014596 scopus 로고    scopus 로고
    • Lack of gene- and strand-specific DNA repair in RNA polymerase III-transcribed human tRNA genes
    • Dammann R., Pfeifer G.P. Lack of gene- and strand-specific DNA repair in RNA polymerase III-transcribed human tRNA genes. Mol. Cell. Biol. 17:1997;219-229.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 219-229
    • Dammann, R.1    Pfeifer, G.P.2
  • 42
    • 0033806183 scopus 로고    scopus 로고
    • RNA polymerase II elongation complexes containing the Cockayne's syndrome group B protein interacts with a molecular complex containing the transcription factor IIH component xeroderma pigmentosum B and p62
    • Citterio E., van den Boom V., Schnitzler G., Kanaar R., Bonte E., Kingston R.E., Hoeijmakers J.H.J. RNA polymerase II elongation complexes containing the Cockayne's syndrome group B protein interacts with a molecular complex containing the transcription factor IIH component xeroderma pigmentosum B and p62. Mol. Cell. Biol. 20:2000;7643-7653.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 7643-7653
    • Citterio, E.1    Van Den Boom, V.2    Schnitzler, G.3    Kanaar, R.4    Bonte, E.5    Kingston, R.E.6    Hoeijmakers, J.H.J.7
  • 45
    • 0030732132 scopus 로고    scopus 로고
    • Mechanism of open complex and dual incision formation by human nucleotide excision repair factors
    • Evans E., Moggs J., Hwang J., Egly J., Wood R.D. Mechanism of open complex and dual incision formation by human nucleotide excision repair factors. EMBO J. 16:1997;6559-6573.
    • (1997) EMBO J , vol.16 , pp. 6559-6573
    • Evans, E.1    Moggs, J.2    Hwang, J.3    Egly, J.4    Wood, R.D.5
  • 46
    • 0031013308 scopus 로고    scopus 로고
    • Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein
    • Evans E., Fellows J., Coffer A., Wood R.D. Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein. EMBO J. 16:1997;625-638.
    • (1997) EMBO J , vol.16 , pp. 625-638
    • Evans, E.1    Fellows, J.2    Coffer, A.3    Wood, R.D.4
  • 47
    • 0031975207 scopus 로고    scopus 로고
    • Affinity purification of human DNA repair/transcription factor TFIIH using epitope-tagged xeroderma pigmentosum B protein
    • Winkler G.S., Vermeulen W., Coin F., Egly J.M., Hoeijmakers J.H., Weeda G. Affinity purification of human DNA repair/transcription factor TFIIH using epitope-tagged xeroderma pigmentosum B protein. J. Biol. Chem. 273:1998;1092-1098.
    • (1998) J. Biol. Chem , vol.273 , pp. 1092-1098
    • Winkler, G.S.1    Vermeulen, W.2    Coin, F.3    Egly, J.M.4    Hoeijmakers, J.H.5    Weeda, G.6
  • 48
    • 0033104514 scopus 로고    scopus 로고
    • Mutations in XPB and XPD helicases found in xeroderma pigmentosum patients impair the transcription function of TFII-H
    • Coin F., Bergmann E., Bravard A.T., Egly J.M. Mutations in XPB and XPD helicases found in xeroderma pigmentosum patients impair the transcription function of TFII-H. EMBO J. 18:1999;1357-1366.
    • (1999) EMBO J , vol.18 , pp. 1357-1366
    • Coin, F.1    Bergmann, E.2    Bravard, A.T.3    Egly, J.M.4
  • 50
    • 0038157142 scopus 로고    scopus 로고
    • XPD/ERCC2 regulates CAK activity and mitotic progression
    • Chen J., Larochelle S., Li X., Suter B. XPD/ERCC2 regulates CAK activity and mitotic progression. Nature. 424:2003;228-232.
    • (2003) Nature , vol.424 , pp. 228-232
    • Chen, J.1    Larochelle, S.2    Li, X.3    Suter, B.4
  • 51
    • 0030998712 scopus 로고    scopus 로고
    • Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH
    • Rossignol M., Kolb-Cheynel I., Egly J.M. Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH. EMBO J. 16:1997;1628-1637.
    • (1997) EMBO J , vol.16 , pp. 1628-1637
    • Rossignol, M.1    Kolb-Cheynel, I.2    Egly, J.M.3
  • 53
    • 0029870677 scopus 로고    scopus 로고
    • Reaction mechanism of human DNA repair excision nuclease
    • Mu D., Hsu D.S., Sancar A. Reaction mechanism of human DNA repair excision nuclease. J. Biol. Chem. 271:1996;8285-8294.
    • (1996) J. Biol. Chem , vol.271 , pp. 8285-8294
    • Mu, D.1    Hsu, D.S.2    Sancar, A.3
  • 54
    • 0025158110 scopus 로고
    • A presumed DNA helicase encoded by ERCC-3 is involved in the human repair disorders xeroderma pigmentosum and Cockayne's syndrome
    • Weeda G., van Ham R.C., Vermeulen W., Bootsma D., van der Eb A.J., Hoeijmakers J.H. A presumed DNA helicase encoded by ERCC-3 is involved in the human repair disorders xeroderma pigmentosum and Cockayne's syndrome. Cell. 62:1990;777-791.
    • (1990) Cell , vol.62 , pp. 777-791
    • Weeda, G.1    Van Ham, R.C.2    Vermeulen, W.3    Bootsma, D.4    Van Der Eb, A.J.5    Hoeijmakers, J.H.6
  • 55
    • 0025250069 scopus 로고
    • ERCC2: CDNA cloning and molecular characterization of a human nucleotide excision repair gene with high homology to yeast RAD3
    • Weber C.A., Salazar E.P., Stewart S.A., Thompson L.H. ERCC2: cDNA cloning and molecular characterization of a human nucleotide excision repair gene with high homology to yeast RAD3. EMBO J. 9:1990;1437-1447.
    • (1990) EMBO J. , vol.9 , pp. 1437-1447
    • Weber, C.A.1    Salazar, E.P.2    Stewart, S.A.3    Thompson, L.H.4
  • 58
    • 0028180697 scopus 로고
    • P44 and p34 subunits of the BTF2/TFIIH transcription factor have homologies with SSL1, a yeast protein involved in DNA repair
    • Humbert S., van Vuuren H., Lutz Y., Hoeijmakers J.H., Egly J.M., Moncollin V. p44 and p34 subunits of the BTF2/TFIIH transcription factor have homologies with SSL1, a yeast protein involved in DNA repair. EMBO J. 13:1994;2393-2398.
    • (1994) EMBO J , vol.13 , pp. 2393-2398
    • Humbert, S.1    Van Vuuren, H.2    Lutz, Y.3    Hoeijmakers, J.H.4    Egly, J.M.5    Moncollin, V.6
  • 59
    • 0035920181 scopus 로고    scopus 로고
    • A role of the C-terminal part of p44 in the promoter escape activity of transcription factor IIH
    • Tremeau-Bravard A., Perez C., Egly J.M. A role of the C-terminal part of p44 in the promoter escape activity of transcription factor IIH. J. Biol. Chem. 276:2001;27693-27697.
    • (2001) J. Biol. Chem , vol.276 , pp. 27693-27697
    • Tremeau-Bravard, A.1    Perez, C.2    Egly, J.M.3
  • 66
    • 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 J.M. DNA damage recognition by XPA protein promotes efficient recruitment of transcription factor II H. J. Biol. Chem. 272:1997;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
  • 67
    • 0032502760 scopus 로고    scopus 로고
    • Functional analysis of human replication protein a in nucleotide excision repair
    • Stigger E., Drissi R., Lee S.H. Functional analysis of human replication protein A in nucleotide excision repair. J. Biol. Chem. 273:1998;9337-9343.
    • (1998) J. Biol. Chem , vol.273 , pp. 9337-9343
    • Stigger, E.1    Drissi, R.2    Lee, S.H.3
  • 68
    • 0023992803 scopus 로고
    • Purification and characterization of replication protein A, a cellular protein required for in vitro replication of simian virus 40 DNA
    • Wold M.S., 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. 85:1988;2523-2527.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2523-2527
    • Wold, M.S.1    Kelly, T.2
  • 69
    • 0030908093 scopus 로고    scopus 로고
    • Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
    • Wold M.S. Replication protein A: a heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism. Annu. Rev. Biochem. 66:1997;61-92.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 61-92
    • Wold, M.S.1
  • 70
    • 0032529167 scopus 로고    scopus 로고
    • DNA-binding polarity of human replication protein a positions nucleases in nucleotide excision repair
    • de Laat W.L., Appeldoorn E., Sugasawa K., Weterings E., Jaspers N.G., Hoeijmakers J.H. DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair. Genes Dev. 12:1998;2598-2609.
    • (1998) Genes Dev , vol.12 , pp. 2598-2609
    • De Laat, W.L.1    Appeldoorn, E.2    Sugasawa, K.3    Weterings, E.4    Jaspers, N.G.5    Hoeijmakers, J.H.6
  • 72
    • 0037197844 scopus 로고    scopus 로고
    • Human XPA and RPA DNA repair proteins participate in specific recognition of triplex-induced helical distortions
    • Vasquez K.M., Christensen J., Li L., Finch R.A., Glazer P.M. Human XPA and RPA DNA repair proteins participate in specific recognition of triplex-induced helical distortions. Proc. Natl. Acad. Sci. USA. 99:2002;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
  • 73
    • 0037195277 scopus 로고    scopus 로고
    • Dimerization of human XPA and formation of XPA2-RPA protein complex
    • Yang Z.G., Liu Y., Mao L.Y., Zhang J.T., Zhou Y. Dimerization of human XPA and formation of XPA2-RPA protein complex. Biochemistry. 41:2002;13012-13020.
    • (2002) Biochemistry , vol.41 , pp. 13012-13020
    • Yang, Z.G.1    Liu, Y.2    Mao, L.Y.3    Zhang, J.T.4    Zhou, Y.5
  • 74
    • 0035796455 scopus 로고    scopus 로고
    • Double-check probing of DNA bending and unwinding by XPA-RPA: An architectural function in DNA repair
    • Missura M., Buterin T., Hindges R., Hubscher U., Kasparkova J., Brabec V., Naegeli H. Double-check probing of DNA bending and unwinding by XPA-RPA: an architectural function in DNA repair. EMBO J. 20:2001;3554-3564.
    • (2001) EMBO J , vol.20 , pp. 3554-3564
    • Missura, M.1    Buterin, T.2    Hindges, R.3    Hubscher, U.4    Kasparkova, J.5    Brabec, V.6    Naegeli, H.7
  • 75
    • 0025687972 scopus 로고
    • Isolation of the functional human excision repair gene ERCC5 by intercosmid recombination
    • Mudgett J.S., MacInnes M.A. Isolation of the functional human excision repair gene ERCC5 by intercosmid recombination. Genomics. 8:1990;623-633.
    • (1990) Genomics , vol.8 , pp. 623-633
    • Mudgett, J.S.1    MacInnes, M.A.2
  • 76
    • 0037188888 scopus 로고    scopus 로고
    • Requirement of yeast RAD2, a homolog of human XPG gene, for efficient RNA polymerase II transcription: Implications for Cockayne's syndrome
    • Lee S.K., Yu S.L., Prakash L., Prakash S. Requirement of yeast RAD2, a homolog of human XPG gene, for efficient RNA polymerase II transcription: implications for Cockayne's syndrome. Cell. 109:2002;823-834.
    • (2002) Cell , vol.109 , pp. 823-834
    • Lee, S.K.1    Yu, S.L.2    Prakash, L.3    Prakash, S.4
  • 78
    • 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. 275:2000;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
  • 80
    • 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 S.J., Nigg E.A., Wood R.D. Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome. Mol. Cell. Biol. 21:2001;2281-2291.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 2281-2291
    • Araujo, S.J.1    Nigg, E.A.2    Wood, R.D.3
  • 84
    • 0031027248 scopus 로고    scopus 로고
    • A low content of ERCC1 and a 120 kDa protein is a frequent feature of group F xeroderma pigmentosum fibroblast cell
    • Yagi T., Wood R.D., Takebe H. A low content of ERCC1 and a 120 kDa protein is a frequent feature of group F xeroderma pigmentosum fibroblast cell. Mutagenesis. 12:1997;41-44.
    • (1997) Mutagenesis , vol.12 , pp. 41-44
    • Yagi, T.1    Wood, R.D.2    Takebe, H.3
  • 87
    • 0029828941 scopus 로고    scopus 로고
    • Sequential binding of DNA repair proteins RPA and ERCC1 to XPA in vitro
    • Saijo M., Kuraoka I., Masutani C., Hanaoka F., Tanaka K. Sequential binding of DNA repair proteins RPA and ERCC1 to XPA in vitro. Nucleic Acids Res. 24:1996;4719-4724.
    • (1996) Nucleic Acids Res , vol.24 , pp. 4719-4724
    • Saijo, M.1    Kuraoka, I.2    Masutani, C.3    Hanaoka, F.4    Tanaka, K.5
  • 88
    • 0033118354 scopus 로고    scopus 로고
    • Molecular mechanism of nucleotide excision repair
    • de Laat W.L., Jaspers N.G., Hoeijmakers J.H. Molecular mechanism of nucleotide excision repair. Genes Dev. 13:1999;768-785.
    • (1999) Genes Dev , vol.13 , pp. 768-785
    • De Laat, W.L.1    Jaspers, N.G.2    Hoeijmakers, J.H.3
  • 89
    • 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 G.S., Sugasawa K., Eker A.P., de Laat W.L., Hoeijmakers J.H.J. Novel functional interactions between nucleotide excision DNA repair proteins influencing the enzymatic activities of TFIIH, XPG and ERCC1-XPF. Biochemistry. 40:2001;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.J.5
  • 90
    • 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 J.G., Yarema K.J., Essigmann J.M., Wood R.D. 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. 271:1996;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
  • 91
    • 0030716255 scopus 로고    scopus 로고
    • Characterization of reaction intermediates of human excision repair nuclease
    • Mu D., Wakasugi M., Hsu D.S., Sancar A. Characterization of reaction intermediates of human excision repair nuclease. J. Biol. Chem. 272:1997;28971-28979.
    • (1997) J. Biol. Chem , vol.272 , pp. 28971-28979
    • Mu, D.1    Wakasugi, M.2    Hsu, D.S.3    Sancar, A.4
  • 92
    • 0030941340 scopus 로고    scopus 로고
    • The non-catalytic function of XPG protein during dual incision in human nucleotide excision repair
    • Wakasugi M., Reardon J.T., Sancar A. The non-catalytic function of XPG protein during dual incision in human nucleotide excision repair. J. Biol. Chem. 272:1997;16030-16034.
    • (1997) J. Biol. Chem , vol.272 , pp. 16030-16034
    • Wakasugi, M.1    Reardon, J.T.2    Sancar, A.3
  • 93
    • 0026149320 scopus 로고
    • DNA polymerase delta mediates excision repair in growing cells damaged with ultraviolet radiation
    • Hunting D.J., Gowans B.J., Dresler S.L. DNA polymerase delta mediates excision repair in growing cells damaged with ultraviolet radiation. Biochem. Cell Biol. 69:1991;303-308.
    • (1991) Biochem. Cell Biol , vol.69 , pp. 303-308
    • Hunting, D.J.1    Gowans, B.J.2    Dresler, S.L.3
  • 94
    • 0026670370 scopus 로고
    • A role for the human single-stranded DNA binding protein HSSB/RPA in an early stage of nucleotide excision repair
    • Coverley D., Kenny M.K., Lane D.P., Wood R.D. A role for the human single-stranded DNA binding protein HSSB/RPA in an early stage of nucleotide excision repair. Nucleic Acids Res. 20:1992;3873-3880.
    • (1992) Nucleic Acids Res , vol.20 , pp. 3873-3880
    • Coverley, D.1    Kenny, M.K.2    Lane, D.P.3    Wood, R.D.4
  • 95
    • 0026546407 scopus 로고
    • Proliferating cell nuclear antigen is required for DNA excision repair
    • Shivji K.K., Kenny M.K., Wood R.D. Proliferating cell nuclear antigen is required for DNA excision repair. Cell. 69:1992;367-374.
    • (1992) Cell , vol.69 , pp. 367-374
    • Shivji, K.K.1    Kenny, M.K.2    Wood, R.D.3
  • 96
    • 0031416756 scopus 로고    scopus 로고
    • Which DNA polymerases are used for DNA repair in eukaryotes?
    • Wood R.D., Shivji M.K.K. Which DNA polymerases are used for DNA repair in eukaryotes? Carcinogenesis. 18:1997;605-610.
    • (1997) Carcinogenesis , vol.18 , pp. 605-610
    • Wood, R.D.1    Shivji, M.K.K.2
  • 97
    • 0028965151 scopus 로고
    • Nucleotide excision repair DNA synthesis by DNA polymerase epsilon in the presence of PCNA, RFC, and RPA
    • Shivji M.K., Podust V.N., Hubscher U., Wood R.D. Nucleotide excision repair DNA synthesis by DNA polymerase epsilon in the presence of PCNA, RFC, and RPA. Biochemistry. 34:1995;5011-5017.
    • (1995) Biochemistry , vol.34 , pp. 5011-5017
    • Shivji, M.K.1    Podust, V.N.2    Hubscher, U.3    Wood, R.D.4
  • 98
  • 99
    • 0037435411 scopus 로고    scopus 로고
    • Tumor suppressor p53 dependent recruitment of nucleotide excision repair factors XPC and TFIIH to DNA damage
    • Wang Q., Zhu Q., Wani M.A., Wani G., Chen J., Wani A.A. Tumor suppressor p53 dependent recruitment of nucleotide excision repair factors XPC and TFIIH to DNA damage. DNA Repair. 2:2003;483-499.
    • (2003) DNA Repair , vol.2 , pp. 483-499
    • Wang, Q.1    Zhu, Q.2    Wani, M.A.3    Wani, G.4    Chen, J.5    Wani, A.A.6
  • 101
    • 0033010376 scopus 로고    scopus 로고
    • The relative expression of mutated XPB genes results in xeroderma pigmentosum/Cockayne's syndrome or trichothiodystrophy cellular phenotypes
    • Riou L., Zeng L., Chevalier-Lagente O., Stary A., Nikaido O., Taïeb A., Mezzina M., Sarasin A. The relative expression of mutated XPB genes results in xeroderma pigmentosum/Cockayne's syndrome or trichothiodystrophy cellular phenotypes. Hum. Mol. Genet. 8:1999;1125-1133.
    • (1999) Hum. Mol. Genet , vol.8 , pp. 1125-1133
    • Riou, L.1    Zeng, L.2    Chevalier-Lagente, O.3    Stary, A.4    Nikaido, O.5    Taïeb, A.6    Mezzina, M.7    Sarasin, A.8
  • 102
    • 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 M.F., Versteeg A., Filon R., van Zeeland A.A., Mullenders L.H.F. 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. 16:1996;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.F.5
  • 103
    • 0032577452 scopus 로고    scopus 로고
    • Lack of transcription-coupled repair of acetylaminofluorene DNA adducts in human fibroblasts contrasts their efficient inhibition of transcription
    • van Oosterwijk M.F., Filon R., de Groot A.J.L., van Zeeland A.A., Mullenders L.H.F. Lack of transcription-coupled repair of acetylaminofluorene DNA adducts in human fibroblasts contrasts their efficient inhibition of transcription. J. Biol. Chem. 273:1998;13599-13604.
    • (1998) J. Biol. Chem , vol.273 , pp. 13599-13604
    • Van Oosterwijk, M.F.1    Filon, R.2    De Groot, A.J.L.3    Van Zeeland, A.A.4    Mullenders, L.H.F.5
  • 104
    • 0023663101 scopus 로고
    • Selective removal of transcription-blocking DNA damage from the transcribed strand of the mammalian DHFR gene
    • Mellon I., Spivak G., Hanawalt P.C. Selective removal of transcription-blocking DNA damage from the transcribed strand of the mammalian DHFR gene. Cell. 51:1987;241-249.
    • (1987) Cell , vol.51 , pp. 241-249
    • Mellon, I.1    Spivak, G.2    Hanawalt, P.C.3
  • 105
    • 0942275657 scopus 로고    scopus 로고
    • DNA replication in the face of (In)surmountable odds
    • Cleaver J.E., Laposa R.R., Limoli C.L. DNA replication in the face of (In)surmountable odds. Cell Cycle. 2:2003;310-315.
    • (2003) Cell Cycle , vol.2 , pp. 310-315
    • Cleaver, J.E.1    Laposa, R.R.2    Limoli, C.L.3
  • 106
    • 0029785723 scopus 로고    scopus 로고
    • Blockage of RNA polymerase as a possible trigger for UV light-induced apoptosis
    • Ljungman M., Zhang F. Blockage of RNA polymerase as a possible trigger for UV light-induced apoptosis. Oncogene. 13:1996;823-831.
    • (1996) Oncogene , vol.13 , pp. 823-831
    • Ljungman, M.1    Zhang, F.2
  • 107
    • 0642317018 scopus 로고    scopus 로고
    • The role of ATM and ATR in DNA damaged-induced cell cycle control
    • Goodarzi A.A., Block W.D., Lees-Miller S.P. The role of ATM and ATR in DNA damaged-induced cell cycle control. Progr. Cell Cycle Res. 5:2003;393-411.
    • (2003) Progr. Cell Cycle Res , vol.5 , pp. 393-411
    • Goodarzi, A.A.1    Block, W.D.2    Lees-Miller, S.P.3
  • 108
    • 0035449355 scopus 로고    scopus 로고
    • Cell cycle checkpoint signaling through the ATM and ATR kinases
    • Abraham R.T. Cell cycle checkpoint signaling through the ATM and ATR kinases. Genes Dev. 15:2001;2177-2196.
    • (2001) Genes Dev , vol.15 , pp. 2177-2196
    • Abraham, R.T.1
  • 109
    • 0037365789 scopus 로고    scopus 로고
    • ATM and related protein kinases: Safeguarding genome integrity
    • Shiloh Y. ATM and related protein kinases: safeguarding genome integrity. Nat. Rev. Cancer. 3:2003;155-168.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 155-168
    • Shiloh, Y.1
  • 111
    • 0035960723 scopus 로고    scopus 로고
    • DNA replication: Stable driving prevents fatal smashes
    • Donaldson A.D., Blow J.J. DNA replication: stable driving prevents fatal smashes. Curr. Biol. 11:2001;R979-R982.
    • (2001) Curr. Biol , vol.11
    • Donaldson, A.D.1    Blow, J.J.2
  • 112
    • 0037312317 scopus 로고    scopus 로고
    • Molecular anatomy of the DNA damage and replication checkpoints
    • Qin J., Li L. Molecular anatomy of the DNA damage and replication checkpoints. Radiat. Res. 159:2003;139-148.
    • (2003) Radiat. Res , vol.159 , pp. 139-148
    • Qin, J.1    Li, L.2
  • 113
    • 0000502113 scopus 로고    scopus 로고
    • DNA replication checkpoint
    • Boddy M.N., Russell P. DNA replication checkpoint. Curr. Biol. 11:2001;R953-R956.
    • (2001) Curr. Biol , vol.11
    • Boddy, M.N.1    Russell, P.2
  • 114
    • 0037027880 scopus 로고    scopus 로고
    • DNA structure dependent checkpoints as regulators of DNA repair
    • Carr A.M. DNA structure dependent checkpoints as regulators of DNA repair. DNA Repair. 1:2002;983-994.
    • (2002) DNA Repair , vol.1 , pp. 983-994
    • Carr, A.M.1
  • 115
    • 0037106186 scopus 로고    scopus 로고
    • A requirement for replication in activation of the ATR-dependent DNA damage checkpoint
    • Lupardus P.J., Byun T., Yee M.C., Hekmat-Nejad M., Cimprich K.A. A requirement for replication in activation of the ATR-dependent DNA damage checkpoint. Genes Dev. 16:2002;2327-2332.
    • (2002) Genes Dev , vol.16 , pp. 2327-2332
    • Lupardus, P.J.1    Byun, T.2    Yee, M.C.3    Hekmat-Nejad, M.4    Cimprich, K.A.5
  • 116
    • 0036790477 scopus 로고    scopus 로고
    • Photorepair of RNA polymerase arrest and apoptosis after ultraviolet irradiation in normal and XPB deficient rodent cells
    • Chiganças V., Batista L.F.Z., Brumatti G., Amarante-Mendes G.P., Yassui A., Menck C.F.M. Photorepair of RNA polymerase arrest and apoptosis after ultraviolet irradiation in normal and XPB deficient rodent cells. Cell Death Differ. 9:2002;1099-1107.
    • (2002) Cell Death Differ , vol.9 , pp. 1099-1107
    • Chiganças, V.1    Batista, L.F.Z.2    Brumatti, G.3    Amarante-Mendes, G.P.4    Yassui, A.5    Menck, C.F.M.6
  • 117
    • 0032501965 scopus 로고    scopus 로고
    • A novel function of poly(ADP-ribosyl)ation: Silencing of RNA polymerase II-dependent transcription
    • Öei S.L., Griesenbeck J., Ziegler M., Schweiger M. A novel function of poly(ADP-ribosyl)ation: silencing of RNA polymerase II-dependent transcription. Biochemistry. 37:1998;1465-1469.
    • (1998) Biochemistry , vol.37 , pp. 1465-1469
    • Öei, S.L.1    Griesenbeck, J.2    Ziegler, M.3    Schweiger, M.4
  • 118
    • 0034985121 scopus 로고    scopus 로고
    • A cellular survival switch: Poly(ADP-ribosyl)ation stimulates DNA repair and silences transcription
    • Ziegler M., Öei S.L. A cellular survival switch: poly(ADP-ribosyl)ation stimulates DNA repair and silences transcription. Bioessays. 23:2001;543-548.
    • (2001) Bioessays , vol.23 , pp. 543-548
    • Ziegler, M.1    Öei, S.L.2
  • 119
    • 0028865245 scopus 로고
    • Post-translational modification of poly(ADP-ribose)polymerase induced by DNA strand breaks
    • Lindahl T., Satoh M.S., Poirier G.G., Klungland A. Post-translational modification of poly(ADP-ribose)polymerase induced by DNA strand breaks. Trends Biochem. Sci. 20:1995;405-411.
    • (1995) Trends Biochem. Sci , vol.20 , pp. 405-411
    • Lindahl, T.1    Satoh, M.S.2    Poirier, G.G.3    Klungland, A.4
  • 120
    • 0034730190 scopus 로고    scopus 로고
    • A cellular defense pathway regulating transcription through poly(ADP-ribosyl)ation in response to DNA damage
    • Vispé S., Yung T.M., Ritchot J., Serizawa H., Satoh M.S. A cellular defense pathway regulating transcription through poly(ADP-ribosyl) ation in response to DNA damage. Proc. Natl. Acad. Sci. USA. 97:2000;9886-9891.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9886-9891
    • Vispé, S.1    Yung, T.M.2    Ritchot, J.3    Serizawa, H.4    Satoh, M.S.5
  • 121
    • 0035921686 scopus 로고    scopus 로고
    • Ultraviolet light-induced DNA damage triggers apoptosis in nucleotide excision repair-deficient cells via Bcl-2 decline and caspase-3/-8 activation
    • Dunkern T.R., Fritz G., Kaina B. Ultraviolet light-induced DNA damage triggers apoptosis in nucleotide excision repair-deficient cells via Bcl-2 decline and caspase-3/-8 activation. Oncogene. 20:2001;6026-6038.
    • (2001) Oncogene , vol.20 , pp. 6026-6038
    • Dunkern, T.R.1    Fritz, G.2    Kaina, B.3
  • 122
    • 0034111148 scopus 로고    scopus 로고
    • DNA-binding activity of the N-terminal cleavage product of poly(ADP-ribose) polymerase is required for UV mediated apoptosis
    • Kim J.W., Won J., Sohn S., Joe C.O. DNA-binding activity of the N-terminal cleavage product of poly(ADP-ribose) polymerase is required for UV mediated apoptosis. J. Cell Sci. 113:2000;955-961.
    • (2000) J. Cell Sci , vol.113 , pp. 955-961
    • Kim, J.W.1    Won, J.2    Sohn, S.3    Joe, C.O.4
  • 123
    • 0035807072 scopus 로고    scopus 로고
    • Ultraviolet irradiation alters the phosphorylation of RNA polymerase II large subunit and accelerates its proteasome-dependent degradation
    • Luo Z., Zheng J., Lu Y., Bregman D.B. Ultraviolet irradiation alters the phosphorylation of RNA polymerase II large subunit and accelerates its proteasome-dependent degradation. Mutat. Res. 486:2001;259-274.
    • (2001) Mutat. Res , vol.486 , pp. 259-274
    • Luo, Z.1    Zheng, J.2    Lu, Y.3    Bregman, D.B.4
  • 125
    • 0031818021 scopus 로고    scopus 로고
    • P53-dependent DNA repair and apoptosis respond differently to high- and low-dose ultraviolet radiation
    • Li G., Ho V.C. p53-dependent DNA repair and apoptosis respond differently to high- and low-dose ultraviolet radiation. Br. J. Dermatol. 139:1998;3-10.
    • (1998) Br. J. Dermatol , vol.139 , pp. 3-10
    • Li, G.1    Ho, V.C.2
  • 126
    • 0141916811 scopus 로고    scopus 로고
    • Cell cycle arrest and apoptosis provoked by UV radiation-induced DNA damage are transcriptionally highly divergent responses
    • Gentile M., Latonen L., Laiho M. Cell cycle arrest and apoptosis provoked by UV radiation-induced DNA damage are transcriptionally highly divergent responses. Nucleic Acids Res. 31:2003;4779-4790.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4779-4790
    • Gentile, M.1    Latonen, L.2    Laiho, M.3
  • 127
    • 0033032157 scopus 로고    scopus 로고
    • Recovery of RNA synthesis from the DHFR gene following UV-irradiation precedes the removal of photolesions from the transcribed strand
    • Ljungman M. Recovery of RNA synthesis from the DHFR gene following UV-irradiation precedes the removal of photolesions from the transcribed strand. Carcinogenesis. 20:1999;395-399.
    • (1999) Carcinogenesis , vol.20 , pp. 395-399
    • Ljungman, M.1
  • 130
    • 0034665461 scopus 로고    scopus 로고
    • P53 transcriptional activity is essential for p53-dependent apoptosis following DNA damage
    • Chao C., Saito S., Kang J., Anderson C.W., Apella E., Xu Y. p53 transcriptional activity is essential for p53-dependent apoptosis following DNA damage. EMBO J. 19:2000;4967-4975.
    • (2000) EMBO J , vol.19 , pp. 4967-4975
    • Chao, C.1    Saito, S.2    Kang, J.3    Anderson, C.W.4    Apella, E.5    Xu, Y.6
  • 131
    • 0036791008 scopus 로고    scopus 로고
    • P53 and DNA damage-inducible expression of the xeroderma pigmentosum group C gene
    • Adimoolam S., Ford J.M. p53 and DNA damage-inducible expression of the xeroderma pigmentosum group C gene. Proc. Natl. Acad. Sci. USA. 99:2002;12985-12990.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12985-12990
    • Adimoolam, S.1    Ford, J.M.2
  • 132
    • 0036490207 scopus 로고    scopus 로고
    • A nucleotide excision repair master-switch: P53 regulated coordinate induction of global genomic repair genes
    • Amundson S.A., Patterson A., Do K.T., Fornace A.J. Jr. A nucleotide excision repair master-switch: p53 regulated coordinate induction of global genomic repair genes. Cancer Biol. Ther. 1:2002;145-149.
    • (2002) Cancer Biol. Ther , vol.1 , pp. 145-149
    • Amundson, S.A.1    Patterson, A.2    Do, K.T.3    Fornace Jr., A.J.4
  • 133
    • 0037450761 scopus 로고    scopus 로고
    • P53 is a chromatin accessibility factor for nucleotide excision repair of DNA damage
    • Rubbi C.P., Miner J. p53 is a chromatin accessibility factor for nucleotide excision repair of DNA damage. EMBO J. 22:2003;975-986.
    • (2003) EMBO J , vol.22 , pp. 975-986
    • Rubbi, C.P.1    Miner, J.2
  • 134
    • 0029029741 scopus 로고
    • Li-Fraumeni syndrome fibroblasts homozygous for p53 mutations are deficient in global DNA repair but exhibit normal transcription-coupled repair and enhanced UV resistance
    • Ford J.M., Hanawalt P.C. Li-Fraumeni syndrome fibroblasts homozygous for p53 mutations are deficient in global DNA repair but exhibit normal transcription-coupled repair and enhanced UV resistance. Proc. Natl. Acad. Sci. USA. 92:1995;8876-8880.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8876-8880
    • Ford, J.M.1    Hanawalt, P.C.2
  • 135
    • 0030853074 scopus 로고    scopus 로고
    • Expression of wild-type p53 is required for efficient global genomic nucleotide excision repair in UV-irradiated human fibroblasts
    • Ford J.M., Hanawalt P.C. Expression of wild-type p53 is required for efficient global genomic nucleotide excision repair in UV-irradiated human fibroblasts. J. Biol. Chem. 272:1997;28073-28080.
    • (1997) J. Biol. Chem , vol.272 , pp. 28073-28080
    • Ford, J.M.1    Hanawalt, P.C.2
  • 137
    • 0038809820 scopus 로고    scopus 로고
    • UV wavelength-dependent regulation of transcription-coupled nucleotide excision repair in p53-deficient human cells
    • Mathonnet G., Leger C., Desnoyers J., Drouin R., Therrien J.P., Drobetsky E.A. UV wavelength-dependent regulation of transcription-coupled nucleotide excision repair in p53-deficient human cells. Proc. Natl. Acad. Sci. USA. 100:2003;7219-7224.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7219-7224
    • Mathonnet, G.1    Leger, C.2    Desnoyers, J.3    Drouin, R.4    Therrien, J.P.5    Drobetsky, E.A.6
  • 139
    • 0037022654 scopus 로고    scopus 로고
    • A cut above: Discovery of an alternative excision repair pathway in bacteria
    • van Houten B., Eisen J.A., Hanawalt P.C. A cut above: discovery of an alternative excision repair pathway in bacteria. Proc. Natl. Acad. Sci. USA. 99:2002;2581-2583.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2581-2583
    • Van Houten, B.1    Eisen, J.A.2    Hanawalt, P.C.3
  • 141
    • 0037206310 scopus 로고    scopus 로고
    • The Caenorhabditis elegans XPA homolog of human XPA
    • Park H.K., Yook J.S., Koo H.S., Choi I.S., Ahn B. The Caenorhabditis elegans XPA homolog of human XPA. Mol. Cell. 14:2002;50-55.
    • (2002) Mol. Cell , vol.14 , pp. 50-55
    • Park, H.K.1    Yook, J.S.2    Koo, H.S.3    Choi, I.S.4    Ahn, B.5
  • 142
    • 0037014596 scopus 로고    scopus 로고
    • The gene expression and deficiency phenotypes of Cockayne's syndrome B protein in Caenorhabditis elegans
    • Lee M.H., Ahn B., Choi I.S., Koo H.S. The gene expression and deficiency phenotypes of Cockayne's syndrome B protein in Caenorhabditis elegans. FEBS Lett. 522:2002;47-51.
    • (2002) FEBS Lett , vol.522 , pp. 47-51
    • Lee, M.H.1    Ahn, B.2    Choi, I.S.3    Koo, H.S.4
  • 145
    • 0032908820 scopus 로고    scopus 로고
    • The Drosophila melanogaster homologue of the xeroderma pigmentosum D gene product is located in euchromatic regions and has a dynamic response to UV light-induced lesions in polytene chromosomes
    • Reynaud E., Lomeli H., Vazquez M., Zurita M. The Drosophila melanogaster homologue of the xeroderma pigmentosum D gene product is located in euchromatic regions and has a dynamic response to UV light-induced lesions in polytene chromosomes. Mol. Biol. Cell. 10:1999;1191-1203.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1191-1203
    • Reynaud, E.1    Lomeli, H.2    Vazquez, M.3    Zurita, M.4
  • 146
    • 0029082115 scopus 로고
    • The Drosophila meiotic recombination gene mei-9 encodes a homologue of the yeast excision repair protein Rad1
    • Sekelsky J.J., McKim K.S., Chin G.M., Hawley R.S. The Drosophila meiotic recombination gene mei-9 encodes a homologue of the yeast excision repair protein Rad1. Genetics. 141:1995;619-627.
    • (1995) Genetics , vol.141 , pp. 619-627
    • Sekelsky, J.J.1    McKim, K.S.2    Chin, G.M.3    Hawley, R.S.4
  • 147
    • 0032989562 scopus 로고    scopus 로고
    • The Drosophila ortholog of the human XPG gene
    • Houle J.F., Friedberg E.C. The Drosophila ortholog of the human XPG gene. Gene. 234:1999;353-360.
    • (1999) Gene , vol.234 , pp. 353-360
    • Houle, J.F.1    Friedberg, E.C.2
  • 148
    • 0034724939 scopus 로고    scopus 로고
    • Nucleotide excision repair endonuclease genes in Drosophila melanogaster
    • Sekelsky J.J., Hollis K.J., Eimerl A.I., Burtis K.C., Hawley R.S. Nucleotide excision repair endonuclease genes in Drosophila melanogaster. Mutat. Res. 459:2000;219-228.
    • (2000) Mutat. Res , vol.459 , pp. 219-228
    • Sekelsky, J.J.1    Hollis, K.J.2    Eimerl, A.I.3    Burtis, K.C.4    Hawley, R.S.5
  • 151
    • 0038376763 scopus 로고    scopus 로고
    • Arabidopsis UVH6, a homolog of human XPD and yeast RAD3 DNA repair genes, functions in DNA repair and is essential for plant growth
    • Liu Z., Hong S.W., Escobar M., Vierling E., Mitchell D.L., Mount D.W., Hall J.D. Arabidopsis UVH6, a homolog of human XPD and yeast RAD3 DNA repair genes, functions in DNA repair and is essential for plant growth. Plant Physiol. 132:2003;1405-1414.
    • (2003) Plant Physiol , vol.132 , pp. 1405-1414
    • Liu, Z.1    Hong, S.W.2    Escobar, M.3    Vierling, E.4    Mitchell, D.L.5    Mount, D.W.6    Hall, J.D.7
  • 152
    • 0034000524 scopus 로고    scopus 로고
    • Repair of UV damage in plants by nucleotide excision repair: Arabidopsis UVH1 DNA repair gene is a homolog of Saccharomyces cerevisiae Rad1
    • Liu Z., Hossain G.S., Islas-Osuna M.A., Mitchell D.L., Mount D.W. Repair of UV damage in plants by nucleotide excision repair: Arabidopsis UVH1 DNA repair gene is a homolog of Saccharomyces cerevisiae Rad1. Plant J. 21:2000;519-528.
    • (2000) Plant J , vol.21 , pp. 519-528
    • Liu, Z.1    Hossain, G.S.2    Islas-Osuna, M.A.3    Mitchell, D.L.4    Mount, D.W.5
  • 153
    • 0034002935 scopus 로고    scopus 로고
    • AtRAD1, a plant homologue of human and yeast nucleotide excision repair endonucleases, is involved in dark repair of UV damages and recombination
    • Gallego F., Fleck O., Li A., Wyrzykowska J., Tinland B. AtRAD1, a plant homologue of human and yeast nucleotide excision repair endonucleases, is involved in dark repair of UV damages and recombination. Plant J. 21:2000;507-518.
    • (2000) Plant J , vol.21 , pp. 507-518
    • Gallego, F.1    Fleck, O.2    Li, A.3    Wyrzykowska, J.4    Tinland, B.5
  • 154
    • 0034937767 scopus 로고    scopus 로고
    • Arabidopsis UVH3 gene is a homolog of the Saccharomyces cerevisiae RAD2 and human XPG DNA repair genes
    • Liu Z., Hall J.D., Mount D.W. Arabidopsis UVH3 gene is a homolog of the Saccharomyces cerevisiae RAD2 and human XPG DNA repair genes. Plant J. 26:2001;329-338.
    • (2001) Plant J , vol.26 , pp. 329-338
    • Liu, Z.1    Hall, J.D.2    Mount, D.W.3
  • 155
    • 0034733496 scopus 로고    scopus 로고
    • Nucleotide excision repair in yeast
    • Prakash S., Prakash L. Nucleotide excision repair in yeast. Mutat. Res. 451:2000;13-24.
    • (2000) Mutat. Res , vol.451 , pp. 13-24
    • Prakash, S.1    Prakash, L.2
  • 157
    • 0034175750 scopus 로고    scopus 로고
    • The question of DNA repair in hyperthermophilic archaea
    • Grogan D.W. The question of DNA repair in hyperthermophilic archaea. Trends Microbiol. 8:2000;180-185.
    • (2000) Trends Microbiol , vol.8 , pp. 180-185
    • Grogan, D.W.1
  • 158
    • 0038202108 scopus 로고    scopus 로고
    • Archaeal DNA repair: Paradigms and puzzles
    • White M.F. Archaeal DNA repair: paradigms and puzzles. Biochem. Soc. Trans. 31:2003;690-693.
    • (2003) Biochem. Soc. Trans , vol.31 , pp. 690-693
    • White, M.F.1
  • 159
    • 0036698611 scopus 로고    scopus 로고
    • Novel endonuclease in archaea cleaving DNA with various branched structure
    • Komori K., Fujikane R., Shinagawa H., Ishino Y. Novel endonuclease in archaea cleaving DNA with various branched structure. Genes Genet. Syst. 77:2002;227-241.
    • (2002) Genes Genet. Syst , vol.77 , pp. 227-241
    • Komori, K.1    Fujikane, R.2    Shinagawa, H.3    Ishino, Y.4
  • 160
    • 0037772376 scopus 로고    scopus 로고
    • An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA
    • Roberts J.A., Bell S.D., White M.F. An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA. Mol. Microbiol. 48:2003;361-371.
    • (2003) Mol. Microbiol , vol.48 , pp. 361-371
    • Roberts, J.A.1    Bell, S.D.2    White, M.F.3
  • 161
    • 0038557114 scopus 로고    scopus 로고
    • Who's on first in the cellular response to DNA damage?
    • Cline S.D., Hanawalt P.C. Who's on first in the cellular response to DNA damage? Nat. Rev. Mol. Cell. Biol. 4:2003;361-372.
    • (2003) Nat. Rev. Mol. Cell. Biol , vol.4 , pp. 361-372
    • Cline, S.D.1    Hanawalt, P.C.2
  • 163
    • 0041928171 scopus 로고    scopus 로고
    • Potential role of MLH1 in the induction of p53 and apoptosis by blocking transcription on damaged DNA templates
    • Yanamadala S., Ljungman M. Potential role of MLH1 in the induction of p53 and apoptosis by blocking transcription on damaged DNA templates. Mol. Cancer Res. 1:2003;747-754.
    • (2003) Mol. Cancer Res , vol.1 , pp. 747-754
    • Yanamadala, S.1    Ljungman, M.2
  • 164
    • 0942268172 scopus 로고    scopus 로고
    • Transcription-coupled repair of δ-oxoguanine in human cells and its deficiency in some DNA repair diseases
    • (in press)
    • Gallego M.P., Sarasin A. Transcription-coupled repair of δ-oxoguanine in human cells and its deficiency in some DNA repair diseases. Biochimie. 85:2003;. (in press).
    • (2003) Biochimie , vol.85
    • Gallego, M.P.1    Sarasin, A.2
  • 165
    • 0037174945 scopus 로고    scopus 로고
    • Characterization of a Schizosaccharomyces pombe strain deleted for a sequence homologue of the human DDB1 gene
    • Zolezzi F., Fuss J., Uzawa S., Linn S. Characterization of a Schizosaccharomyces pombe strain deleted for a sequence homologue of the human DDB1 gene. J. Biol. Chem. 277:2002;41183-41191.
    • (2002) J. Biol. Chem , vol.277 , pp. 41183-41191
    • Zolezzi, F.1    Fuss, J.2    Uzawa, S.3    Linn, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.