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Volumn 509, Issue 1-2, 2002, Pages 23-34

Replication of damaged DNA in mammalian cells: New solutions to an old problem

Author keywords

DNA polymerase; Translesion synthesis; Ultraviolet light; Xeroderma pigmentosum variants

Indexed keywords

CYCLOBUTANE DERIVATIVE; DIMER; DNA; DNA DIRECTED DNA POLYMERASE BETA; DNA POLYMERASE; PYRIMIDINE DERIVATIVE; REV PROTEIN; UBIQUITIN CONJUGATING ENZYME;

EID: 0037202616     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0027-5107(02)00227-0     Document Type: Article
Times cited : (104)

References (96)
  • 2
    • 0034705095 scopus 로고    scopus 로고
    • The many faces of DNA polymerases: Strategies for mutagenesis and for mutational avoidance
    • Friedberg E.C., Feaver W.J., Gerlach V.L. The many faces of DNA polymerases: strategies for mutagenesis and for mutational avoidance. Proc. Natl. Acad. Sci. U.S.A. 97:2000;5681-5683.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5681-5683
    • Friedberg, E.C.1    Feaver, W.J.2    Gerlach, V.L.3
  • 3
    • 0034026051 scopus 로고    scopus 로고
    • Sloppier copier DNA polymerases involved in genome repair
    • Goodman M.F., Tippin B. Sloppier copier DNA polymerases involved in genome repair. Curr. Opin. Genet. Dev. 10:2000;162-168.
    • (2000) Curr. Opin. Genet. Dev. , vol.10 , pp. 162-168
    • Goodman, M.F.1    Tippin, B.2
  • 4
    • 0034713899 scopus 로고    scopus 로고
    • Replication of UV-damaged DNA new insights into links betweeen DNA polymerases
    • Lehmann A.R. Replication of UV-damaged DNA new insights into links betweeen DNA polymerases. Gene. 253:2000;1-12.
    • (2000) Gene , vol.253 , pp. 1-12
    • Lehmann, A.R.1
  • 5
    • 0035854676 scopus 로고    scopus 로고
    • DNA damage control by novel DNA polymerases: Translesion replication and mutagenesis
    • Livneh Z. DNA damage control by novel DNA polymerases: translesion replication and mutagenesis. J. Biol. Chem. 276:2001;25639-25642.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25639-25642
    • Livneh, Z.1
  • 6
    • 0015527017 scopus 로고
    • Postreplication repair of DNA in ultraviolet-irradiated mammalian cells
    • Lehmann A.R. Postreplication repair of DNA in ultraviolet-irradiated mammalian cells. J. Mol. Biol. 66:1972;319-337.
    • (1972) J. Mol. Biol. , vol.66 , pp. 319-337
    • Lehmann, A.R.1
  • 7
    • 0016727657 scopus 로고
    • The influence of caffeine on cell survival in excision-proficient and excision-deficient xeroderma pigmentosum and normal human cell strains following ultraviolet light irradiation
    • Arlett C.F., Harcourt S.A., Broughton B.C. The influence of caffeine on cell survival in excision-proficient and excision-deficient xeroderma pigmentosum and normal human cell strains following ultraviolet light irradiation. Mut. Res. 33:1975;341-346.
    • (1975) Mut. Res. , vol.33 , pp. 341-346
    • Arlett, C.F.1    Harcourt, S.A.2    Broughton, B.C.3
  • 9
    • 0017309743 scopus 로고
    • Frequency of ultraviolet light-induced mutations is higher in xeroderma pigmentosum variant cells than in normal human cells
    • Maher V.M., Ouellette L.M., Curren R.D., McCormick J.J. Frequency of ultraviolet light-induced mutations is higher in xeroderma pigmentosum variant cells than in normal human cells. Nature. 261:1976;593-595.
    • (1976) Nature , vol.261 , pp. 593-595
    • Maher, V.M.1    Ouellette, L.M.2    Curren, R.D.3    McCormick, J.J.4
  • 10
    • 0018290105 scopus 로고
    • Ultraviolet mutagenesis of normal and xeroderma pigmentosum variant human fibroblasts
    • Myhr B.C., Turnbull D., DiPaolo J.A. Ultraviolet mutagenesis of normal and xeroderma pigmentosum variant human fibroblasts. Mut. Res. 62:1979;341-353.
    • (1979) Mut. Res. , vol.62 , pp. 341-353
    • Myhr, B.C.1    Turnbull, D.2    DiPaolo, J.A.3
  • 11
    • 0002573572 scopus 로고
    • Mutagenesis in repair-deficient human cell strains
    • M. Alacevic (Ed.), Elsevier, Amsterdam
    • C.F. Arlett, 1980. Mutagenesis in repair-deficient human cell strains, in: M. Alacevic (Ed.), Progress in Environmental Mutagenesis, Elsevier, Amsterdam, pp. 161-174.
    • (1980) Progress in Environmental Mutagenesis , pp. 161-174
    • Arlett, C.F.1
  • 12
    • 0030925436 scopus 로고    scopus 로고
    • Replication fork bypass of a pyrimidine dimer blocking leading strand DNA synthesis
    • Cordeiro-Stone M., Zaritskaya L.S., Price L.K., Kaufmann W.K. Replication fork bypass of a pyrimidine dimer blocking leading strand DNA synthesis. J. Biol. Chem. 272:1997;13945-13954.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13945-13954
    • Cordeiro-Stone, M.1    Zaritskaya, L.S.2    Price, L.K.3    Kaufmann, W.K.4
  • 13
    • 0032474431 scopus 로고    scopus 로고
    • Bypass of a site-specific cis-syn thymine dimer in an SV40 vector during in vitro replication by HeLa and XP-V cell-free extracts
    • Ensch-Simon I., Burgers P.M., Taylor J.S. Bypass of a site-specific cis-syn thymine dimer in an SV40 vector during in vitro replication by HeLa and XP-V cell-free extracts. Biochemistry. 37:1998;8218-8226.
    • (1998) Biochemistry , vol.37 , pp. 8218-8226
    • Ensch-Simon, I.1    Burgers, P.M.2    Taylor, J.S.3
  • 14
    • 0032101146 scopus 로고    scopus 로고
    • Defective bypass replication of a leading strand cyclobutane thymine dimer in xeroderma pigmentosum variant cell extracts
    • Svoboda D.L., Briley L.P., Vos J.M. Defective bypass replication of a leading strand cyclobutane thymine dimer in xeroderma pigmentosum variant cell extracts. Cancer Res. 58:1998;2445-2448.
    • (1998) Cancer Res. , vol.58 , pp. 2445-2448
    • Svoboda, D.L.1    Briley, L.P.2    Vos, J.M.3
  • 15
    • 0033020150 scopus 로고    scopus 로고
    • Impaired translesion synthesis in xeroderma pigmentosum extracts
    • Cordonnier A.M., Lehmann A.R., Fuchs R.P.P. Impaired translesion synthesis in xeroderma pigmentosum extracts. Mol. Cell. Biol. 19:1999;2206-2211.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2206-2211
    • Cordonnier, A.M.1    Lehmann, A.R.2    Fuchs, R.P.P.3
  • 16
    • 0033564917 scopus 로고    scopus 로고
    • Xeroderma pigmentosum variant (XP-V) correcting protein from HeLa cells has a thymine dimer bypass DNA polymerase activity
    • Masutani C., Araki M., Yamada A., Kusumoto R., Nogimori T., Maekawa T., Iwai S., Hanaoka F. Xeroderma pigmentosum variant (XP-V) correcting protein from HeLa cells has a thymine dimer bypass DNA polymerase activity. EMBO J. 18:1999;3491-3501.
    • (1999) EMBO J. , vol.18 , pp. 3491-3501
    • Masutani, C.1    Araki, M.2    Yamada, A.3    Kusumoto, R.4    Nogimori, T.5    Maekawa, T.6    Iwai, S.7    Hanaoka, F.8
  • 18
    • 0033538470 scopus 로고    scopus 로고
    • HRAD30 mutations in the variant form of xeroderma pigmentosum
    • Johnson R.E., Kondratick C.M., Prakash S., Prakash L. hRAD30 mutations in the variant form of xeroderma pigmentosum. Science. 285:1999;263-265.
    • (1999) Science , vol.285 , pp. 263-265
    • Johnson, R.E.1    Kondratick, C.M.2    Prakash, S.3    Prakash, L.4
  • 21
    • 0033387531 scopus 로고    scopus 로고
    • Mutation enhancement by DINB1: A mammalian homologue of the Escherichia coli mutagenesis protein dinB
    • Ogi T., Kato T., Ohmori H. Mutation enhancement by DINB1: a mammalian homologue of the Escherichia coli mutagenesis protein dinB. Genes Cells. 4:1999;607-618.
    • (1999) Genes Cells , vol.4 , pp. 607-618
    • Ogi, T.1    Kato, T.2    Ohmori, H.3
  • 22
    • 0034660259 scopus 로고    scopus 로고
    • Accurate translesion synthesis by human DNA polymerase η
    • Masutani C., Kusumoto R., Iwai S., Hanaoka F. Accurate translesion synthesis by human DNA polymerase η EMBO J. 19:2000;3100-3109.
    • (2000) EMBO J. , vol.19 , pp. 3100-3109
    • Masutani, C.1    Kusumoto, R.2    Iwai, S.3    Hanaoka, F.4
  • 23
  • 26
    • 0034425754 scopus 로고    scopus 로고
    • Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase eta
    • Haracska L., Yu S.L., Johnson R.E., Prakash L., Prakash S. Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase eta. Nat. Genet. 25:2000;458-461.
    • (2000) Nat. Genet , vol.25 , pp. 458-461
    • Haracska, L.1    Yu, S.L.2    Johnson, R.E.3    Prakash, L.4    Prakash, S.5
  • 28
    • 0035034974 scopus 로고    scopus 로고
    • Role of DNA polymerase eta in the bypass of a (6-4) TT photoproduct
    • Johnson R.E., Haracska L., Prakash S., Prakash L. Role of DNA polymerase eta in the bypass of a (6-4) TT photoproduct. Mol. Cell Biol. 21:2001;3558-3563.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 3558-3563
    • Johnson, R.E.1    Haracska, L.2    Prakash, S.3    Prakash, L.4
  • 29
    • 0037099578 scopus 로고    scopus 로고
    • Lesion bypass in yeast cells: Pol eta participates in a multi-DNA polymerase process
    • Bresson A., Fuchs R.P. Lesion bypass in yeast cells: Pol eta participates in a multi-DNA polymerase process. EMBO J. 21:2002;3881-3887.
    • (2002) EMBO J. , vol.21 , pp. 3881-3887
    • Bresson, A.1    Fuchs, R.P.2
  • 30
    • 0035012235 scopus 로고    scopus 로고
    • Acidic residues critical for the activity and biological function of yeast DNA polymerase eta
    • Kondratick C.M., Washington M.T., Prakash S., Prakash L. Acidic residues critical for the activity and biological function of yeast DNA polymerase eta. Mol. Cell. Biol. 21:2001;2018-2025.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2018-2025
    • Kondratick, C.M.1    Washington, M.T.2    Prakash, S.3    Prakash, L.4
  • 31
    • 0034847259 scopus 로고    scopus 로고
    • Structure of the catalytic core of S. cerevisiae DNA polymerase η: Implications for translesion DNA synthesis
    • Trincao J., Johnson R.E., Escalante C.R., Prakash S., Prakash L., Aggarwal A.K. Structure of the catalytic core of S. cerevisiae DNA polymerase η: implications for translesion DNA synthesis. Mol. Cell. 8:2001;417-426.
    • (2001) Mol. Cell. , vol.8 , pp. 417-426
    • Trincao, J.1    Johnson, R.E.2    Escalante, C.R.3    Prakash, S.4    Prakash, L.5    Aggarwal, A.K.6
  • 32
    • 0035812849 scopus 로고    scopus 로고
    • Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication
    • Ling H., Boudsocq F., Woodgate R., Yang W. Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication. Cell. 107:2001;91-102.
    • (2001) Cell , vol.107 , pp. 91-102
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 33
    • 0034857266 scopus 로고    scopus 로고
    • Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain
    • Zhou B.L., Pata J.D., Steitz T.A. Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain. Mol. Cell. 8:2001;427-437.
    • (2001) Mol. Cell. , vol.8 , pp. 427-437
    • Zhou, B.L.1    Pata, J.D.2    Steitz, T.A.3
  • 34
    • 0035812844 scopus 로고    scopus 로고
    • Error-prone DNA polymerases: Novel structures and the benefits of infidelity
    • Friedberg E.C., Fischhaber P.L., Kisker C. Error-prone DNA polymerases: novel structures and the benefits of infidelity. Cell. 107:2001;9-12.
    • (2001) Cell , vol.107 , pp. 9-12
    • Friedberg, E.C.1    Fischhaber, P.L.2    Kisker, C.3
  • 35
    • 0037126608 scopus 로고    scopus 로고
    • Mutations in human DNA polymerase eta motif II alter bypass of DNA lesions
    • Glick E., Vigna K.L., Loeb L.A. Mutations in human DNA polymerase eta motif II alter bypass of DNA lesions. EMBO J. 20:2001;7303-7312.
    • (2001) EMBO J. , vol.20 , pp. 7303-7312
    • Glick, E.1    Vigna, K.L.2    Loeb, L.A.3
  • 36
    • 0035862988 scopus 로고    scopus 로고
    • Domain structure, localization and function of DNA polymerase η, defective in xeroderma pigmentosum variant cells
    • Kannouche P., Broughton B.C., Volker M., Hanaoka F., Mullenders L.H.F., Lehmann A.R. Domain structure, localization and function of DNA polymerase η, defective in xeroderma pigmentosum variant cells. Genes Dev. 15:2001;158-172.
    • (2001) Genes Dev. , vol.15 , pp. 158-172
    • Kannouche, P.1    Broughton, B.C.2    Volker, M.3    Hanaoka, F.4    Mullenders, L.H.F.5    Lehmann, A.R.6
  • 40
    • 0037039463 scopus 로고    scopus 로고
    • UV-induced replication arrest in the xeroderma pigmentosum variant leads to DNA double-strand breaks, gamma-H2AX formation, and Mre11 relocalization
    • Limoli C.L., Giedzinski E., Bonner W.M., Cleaver J.E. UV-induced replication arrest in the xeroderma pigmentosum variant leads to DNA double-strand breaks, gamma-H2AX formation, and Mre11 relocalization. Proc. Natl. Acad. Sci. U.S.A. 99:2002;233-238.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 233-238
    • Limoli, C.L.1    Giedzinski, E.2    Bonner, W.M.3    Cleaver, J.E.4
  • 41
    • 0034214838 scopus 로고    scopus 로고
    • Polι: A remarkably error-prone human DNA polymerase
    • Tissier A., McDonald J.P., Frank E.G., Woodgate R. Polι: a remarkably error-prone human DNA polymerase. Genes Dev. 14:2000;1642-1650.
    • (2000) Genes Dev. , vol.14 , pp. 1642-1650
    • Tissier, A.1    McDonald, J.P.2    Frank, E.G.3    Woodgate, R.4
  • 42
    • 0033830464 scopus 로고    scopus 로고
    • Preferential incorporation of G opposite template T by the low-fidelity human DNA polymerase ι
    • Zhang Y., Yuan F., Wu X., Wang Z. Preferential incorporation of G opposite template T by the low-fidelity human DNA polymerase ι Mol. Cell. Biol. 20:2000;7099-7108.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7099-7108
    • Zhang, Y.1    Yuan, F.2    Wu, X.3    Wang, Z.4
  • 43
    • 0034738983 scopus 로고    scopus 로고
    • Eukaryotic polymerases ι and ζ act sequentially to bypass DNA lesions
    • Johnson R.E., Washington M.T., Haracska L., Prakash S., Prakash L. Eukaryotic polymerases ι and ζ act sequentially to bypass DNA lesions. Nature. 406:2000;1015-1019.
    • (2000) Nature , vol.406 , pp. 1015-1019
    • Johnson, R.E.1    Washington, M.T.2    Haracska, L.3    Prakash, S.4    Prakash, L.5
  • 44
    • 0034596992 scopus 로고    scopus 로고
    • Mis-insertion and bypass of thymine-thymine dimers by human DNA polymerase ι
    • Tissier A., Frank E.G., McDonald J.P., Iwai S., Hanaoka F., Woodgate R. Mis-insertion and bypass of thymine-thymine dimers by human DNA polymerase ι EMBO J. 19:2000;5259-5266.
    • (2000) EMBO J. , vol.19 , pp. 5259-5266
    • Tissier, A.1    Frank, E.G.2    McDonald, J.P.3    Iwai, S.4    Hanaoka, F.5    Woodgate, R.6
  • 49
  • 51
    • 0035808417 scopus 로고    scopus 로고
    • Purification and characterization of polκ: A DNA polymerase encoded by the human DINB1 gene
    • Gerlach V.L., Feaver W.J., Fischhaber P.L., Friedberg E.C. Purification and characterization of polκ: a DNA polymerase encoded by the human DINB1 gene. J. Biol. Chem. 276:2001;92-98.
    • (2001) J. Biol. Chem. , vol.276 , pp. 92-98
    • Gerlach, V.L.1    Feaver, W.J.2    Fischhaber, P.L.3    Friedberg, E.C.4
  • 53
    • 0035179083 scopus 로고    scopus 로고
    • Expression of human and mouse genes encoding pol Kappa: Testis-specific developmental regulation and AhR-dependent inducible transcription
    • Ogi T., Mimura J., Hikida M., Fujimoto H., Fujii-Kuriyama Y., Ohmori H. Expression of human and mouse genes encoding pol Kappa: testis-specific developmental regulation and AhR-dependent inducible transcription. Genes Cells. 6:2001;943-953.
    • (2001) Genes Cells , vol.6 , pp. 943-953
    • Ogi, T.1    Mimura, J.2    Hikida, M.3    Fujimoto, H.4    Fujii-Kuriyama, Y.5    Ohmori, H.6
  • 54
    • 0001908121 scopus 로고
    • Mutants of yeast defective in mutation induced by ultraviolet light
    • Lemontt J.F. Mutants of yeast defective in mutation induced by ultraviolet light. Adv. Genet. 68:1971;21-33.
    • (1971) Adv. Genet. , vol.68 , pp. 21-33
    • Lemontt, J.F.1
  • 55
    • 0024461293 scopus 로고
    • REV3: A Saccharomyces cerevisiae gene whose function is required for induced mutagenesis, is predicted to encode a non-essential DNA polymerase
    • Morrison A., Christensen R.B., Alley J., Beck A.K., Bernstine E.G., Lemontt J.F., Lawrence C.W. REV3: a Saccharomyces cerevisiae gene whose function is required for induced mutagenesis, is predicted to encode a non-essential DNA polymerase. J. Bacteriol. 171:1989;5659-5667.
    • (1989) J. Bacteriol. , vol.171 , pp. 5659-5667
    • Morrison, A.1    Christensen, R.B.2    Alley, J.3    Beck, A.K.4    Bernstine, E.G.5    Lemontt, J.F.6    Lawrence, C.W.7
  • 56
    • 0029952294 scopus 로고    scopus 로고
    • Thymine-thymine dimer bypass by yeast DNA polymerase ζ
    • Nelson J.R., Lawrence C.W., Hinkle D.C. Thymine-thymine dimer bypass by yeast DNA polymerase ζ Science. 272:1996;1646-1649.
    • (1996) Science , vol.272 , pp. 1646-1649
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 57
    • 0032499748 scopus 로고    scopus 로고
    • A human homologue of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase ζ
    • Gibbs P.E.M., McGregor W.G., Maher V.M., Nisson P., Lawrence C.W. A human homologue of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase ζ Proc. Natl. Acad. Sci. U.S.A. 95:1998;6876-6880.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6876-6880
    • Gibbs, P.E.M.1    McGregor, W.G.2    Maher, V.M.3    Nisson, P.4    Lawrence, C.W.5
  • 59
    • 0032994152 scopus 로고    scopus 로고
    • A full-length cDNA of hREV3 is predicted to encode DNA polymerase ζ for damage-induced mutagenesis in humans
    • Lin W., Wu X., Wang Z. A full-length cDNA of hREV3 is predicted to encode DNA polymerase ζ for damage-induced mutagenesis in humans. Mut. Res. 433:1999;89-98.
    • (1999) Mut. Res. , vol.433 , pp. 89-98
    • Lin, W.1    Wu, X.2    Wang, Z.3
  • 60
    • 0034609744 scopus 로고    scopus 로고
    • Disruption of mouse polymerase zeta (Rev3) leads to embryonic lethality and impairs blastocyst development in vitro
    • Bemark M., Khamlichi A.A., Davies S.L., Neuberger M.S. Disruption of mouse polymerase zeta (Rev3) leads to embryonic lethality and impairs blastocyst development in vitro. Curr. Biol. 10:2000;1213-1216.
    • (2000) Curr. Biol. , vol.10 , pp. 1213-1216
    • Bemark, M.1    Khamlichi, A.A.2    Davies, S.L.3    Neuberger, M.S.4
  • 61
    • 0034609725 scopus 로고    scopus 로고
    • Disruption of the Rev3l-encoded catalytic subunit of polymerase zeta in mice results in early embryonic lethality
    • Esposito G., Godindagger I., Klein U., Yaspo M.L., Cumano A., Rajewsky K. Disruption of the Rev3l-encoded catalytic subunit of polymerase zeta in mice results in early embryonic lethality. Curr. Biol. 10:2000;1221-1224.
    • (2000) Curr. Biol. , vol.10 , pp. 1221-1224
    • Esposito, G.1    Godindagger, I.2    Klein, U.3    Yaspo, M.L.4    Cumano, A.5    Rajewsky, K.6
  • 64
    • 0034635445 scopus 로고    scopus 로고
    • A human REV7 homologue that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2
    • Murakumo Y., Roth T., Ishii H., Rasio D., Numata S., Croce C.M., Fishel R. A human REV7 homologue that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2. J. Biol. Chem. 275:2000;4391-4397.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4391-4397
    • Murakumo, Y.1    Roth, T.2    Ishii, H.3    Rasio, D.4    Numata, S.5    Croce, C.M.6    Fishel, R.7
  • 65
    • 0035394142 scopus 로고    scopus 로고
    • Translesion synthesis by yeast DNA polymerase zeta from templates containing lesions of ultraviolet radiation and acetylaminofluorene
    • Guo D., Wu X., Rajpal D.K., Taylor J.S., Wang Z. Translesion synthesis by yeast DNA polymerase zeta from templates containing lesions of ultraviolet radiation and acetylaminofluorene. Nucleic Acids Res. 29:2001;2875-2883.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2875-2883
    • Guo, D.1    Wu, X.2    Rajpal, D.K.3    Taylor, J.S.4    Wang, Z.5
  • 67
    • 0029787108 scopus 로고    scopus 로고
    • Deoxycytidyl transferase activity of yeast REV1 protein
    • Nelson J.R., Lawrence C.W., Hinkle D.C. Deoxycytidyl transferase activity of yeast REV1 protein. Nature. 382:1996;729-731.
    • (1996) Nature , vol.382 , pp. 729-731
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 68
    • 0011444181 scopus 로고    scopus 로고
    • Yeast Rev1 protein is a G template specific DNA polymerase
    • Haracska L., Prakash S., Prakash L. Yeast Rev1 protein is a G template specific DNA polymerase. J. Biol. Chem. 15:2002;15.
    • (2002) J. Biol. Chem. , vol.15 , pp. 15
    • Haracska, L.1    Prakash, S.2    Prakash, L.3
  • 70
    • 0033571521 scopus 로고    scopus 로고
    • The human REV1 gene codes for a DNA template-dependent dCMP transferase
    • Lin W., Xin H., Zhang Y., Wu X., Yuan F., Wang Z. The human REV1 gene codes for a DNA template-dependent dCMP transferase. Nucleic Acids Res. 27:1999;4468-4475.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4468-4475
    • Lin, W.1    Xin, H.2    Zhang, Y.3    Wu, X.4    Yuan, F.5    Wang, Z.6
  • 72
    • 0036529562 scopus 로고    scopus 로고
    • Response of human REV1 to different DNA damage: Preferential dCMP insertion opposite the lesion
    • Zhang Y., Wu X., Rechkoblit O., Geacintov N.E., Taylor J.S., Wang Z. Response of human REV1 to different DNA damage: preferential dCMP insertion opposite the lesion. Nucleic Acids Res. 30:2002;1630-1638.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1630-1638
    • Zhang, Y.1    Wu, X.2    Rechkoblit, O.3    Geacintov, N.E.4    Taylor, J.S.5    Wang, Z.6
  • 74
    • 0029995908 scopus 로고    scopus 로고
    • In vitro bypass replication of the cisplatin-d(GpG) lesion by calf thymus DNA polymerase beta and human immunodeficiency virus type I reverse transcriptase is highly mutagenic
    • Hoffmann J.S., Pillaire M.J., Garcia-Estefania D., Lapalu S., Villani G. In vitro bypass replication of the cisplatin-d(GpG) lesion by calf thymus DNA polymerase beta and human immunodeficiency virus type I reverse transcriptase is highly mutagenic. J. Biol. Chem. 271:1996;15386-15392.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15386-15392
    • Hoffmann, J.S.1    Pillaire, M.J.2    Garcia-Estefania, D.3    Lapalu, S.4    Villani, G.5
  • 75
    • 0029661257 scopus 로고    scopus 로고
    • Replication across O-6-methylguanine by human DNA polymerase beta in vitro: Insights into the futile cytotoxic repair and mutagenesis of O-6-methylguanine
    • Singh J., Su L., Snow E.T. Replication across O-6-methylguanine by human DNA polymerase beta in vitro: insights into the futile cytotoxic repair and mutagenesis of O-6-methylguanine. J. Biol. Chem. 271:1996;28391-28398.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28391-28398
    • Singh, J.1    Su, L.2    Snow, E.T.3
  • 76
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani S., Takeshita M., Grollman A.P. Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature. 349:1991;431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 77
    • 0031038053 scopus 로고    scopus 로고
    • Abasic translesion synthesis by DNA polymerase beta violates the A-rule: Novel types of nucleotide incorporation by human DNA polymerase beta at an abasic lesion in different sequence contexts
    • Efrati E., Tocco G., Eritja R., Wilson S.H., Goodman M.F. Abasic translesion synthesis by DNA polymerase beta violates the A-rule: novel types of nucleotide incorporation by human DNA polymerase beta at an abasic lesion in different sequence contexts. J. Biol. Chem. 272:1997;2559-2569.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2559-2569
    • Efrati, E.1    Tocco, G.2    Eritja, R.3    Wilson, S.H.4    Goodman, M.F.5
  • 78
    • 0032514636 scopus 로고    scopus 로고
    • Overexpression of DNA polymerase beta in cell results in a mutator phenotype and a decreased sensitivity to anticancer drugs
    • Canitrot Y., Cazaux C., Frechet M., Bouayadi K., Lesca C., Salles B., Hoffmann J.S. Overexpression of DNA polymerase beta in cell results in a mutator phenotype and a decreased sensitivity to anticancer drugs. Proc. Natl. Acad. Sci. U.S.A. 95:1998;12586-12590.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 12586-12590
    • Canitrot, Y.1    Cazaux, C.2    Frechet, M.3    Bouayadi, K.4    Lesca, C.5    Salles, B.6    Hoffmann, J.S.7
  • 79
    • 0019770524 scopus 로고
    • Characterization of postreplication repair in Saccharomyces cerevisiae and effects of rad6, rad18, rev3 and rad52 mutations
    • Prakash L. Characterization of postreplication repair in Saccharomyces cerevisiae and effects of rad6, rad18, rev3 and rad52 mutations. Mol. Gen. Genet. 184:1981;471-478.
    • (1981) Mol. Gen. Genet. , vol.184 , pp. 471-478
    • Prakash, L.1
  • 80
    • 0033525582 scopus 로고    scopus 로고
    • Non-canonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann R.M., Pickart C.M. Non-canonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell. 96:1999;645-653.
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 81
    • 0034600851 scopus 로고    scopus 로고
    • Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair
    • Ulrich H.D., Jentsch S. Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. EMBO J. 19:2000;3388-3397.
    • (2000) EMBO J. , vol.19 , pp. 3388-3397
    • Ulrich, H.D.1    Jentsch, S.2
  • 83
    • 0032169004 scopus 로고    scopus 로고
    • The products of the yeast MMS2 and two human homologues (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family
    • Xiao W., Lin S.L., Broomfield S., Chow B.L., Wei Y.F. The products of the yeast MMS2 and two human homologues (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family. Nucleic Acids Res. 26:1998;3908-3914.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3908-3914
    • Xiao, W.1    Lin, S.L.2    Broomfield, S.3    Chow, B.L.4    Wei, Y.F.5
  • 84
    • 0034608876 scopus 로고    scopus 로고
    • Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens
    • Tateishi S., Sakuraba Y., Masuyama S., Inoue H., Yamaizumi M. Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens. Proc. Natl. Acad. Sci. U.S.A. 97:2000;7927-7932.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 7927-7932
    • Tateishi, S.1    Sakuraba, Y.2    Masuyama, S.3    Inoue, H.4    Yamaizumi, M.5
  • 86
    • 0037007015 scopus 로고    scopus 로고
    • Identification of a protein essential for a major pathway used by human cells to avoid UV-induced DNA damage
    • Li Z., Xiao W., McCormick J.J., Maher V.M. Identification of a protein essential for a major pathway used by human cells to avoid UV-induced DNA damage. Proc. Natl. Acad. Sci. U.S.A. 99:2002;4459-4464.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 4459-4464
    • Li, Z.1    Xiao, W.2    McCormick, J.J.3    Maher, V.M.4
  • 87
    • 0035902615 scopus 로고    scopus 로고
    • Managing DNA polymerases: Coordinating DNA replication, DNA repair, and DNA recombination
    • Sutton M.D., Walker G.C. Managing DNA polymerases: coordinating DNA replication, DNA repair, and DNA recombination. Proc. Natl. Acad. Sci. U.S.A. 98:2001;8342-8349.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8342-8349
    • Sutton, M.D.1    Walker, G.C.2
  • 88
    • 0037076519 scopus 로고    scopus 로고
    • Translesion synthesis by human DNA polymerase eta across thymine glycol lesions
    • Kusumoto R., Masutani C., Iwai S., Hanaoka F. Translesion synthesis by human DNA polymerase eta across thymine glycol lesions. Biochemistry. 41:2002;6090-6099.
    • (2002) Biochemistry , vol.41 , pp. 6090-6099
    • Kusumoto, R.1    Masutani, C.2    Iwai, S.3    Hanaoka, F.4
  • 89
    • 0035909805 scopus 로고    scopus 로고
    • Translesional synthesis past acetylaminofluorene-derived DNA adducts catalyzed by human DNA polymerase Kappa and Escherichia coli DNA polymerase IV
    • Suzuki N., Ohashi E., Hayashi K., Ohmori H., Grollman A.P., Shibutani S. Translesional synthesis past acetylaminofluorene-derived DNA adducts catalyzed by human DNA polymerase Kappa and Escherichia coli DNA polymerase IV. Biochemistry. 40:2001;15176-15183.
    • (2001) Biochemistry , vol.40 , pp. 15176-15183
    • Suzuki, N.1    Ohashi, E.2    Hayashi, K.3    Ohmori, H.4    Grollman, A.P.5    Shibutani, S.6
  • 90
    • 0034712656 scopus 로고    scopus 로고
    • Efficient translesion replication past oxaliplatin and cisplatin GpG adducts by human DNA polymerase eta
    • Vaisman A., Masutani C., Hanaoka F., Chaney S.G. Efficient translesion replication past oxaliplatin and cisplatin GpG adducts by human DNA polymerase eta. Biochemistry. 39:2000;4575-4580.
    • (2000) Biochemistry , vol.39 , pp. 4575-4580
    • Vaisman, A.1    Masutani, C.2    Hanaoka, F.3    Chaney, S.G.4
  • 91
    • 0033772926 scopus 로고    scopus 로고
    • Replication past O-(6)-methylguanine by yeast and human DNA polymerase eta
    • Haracska L., Prakash S., Prakash L. Replication past O-(6)-methylguanine by yeast and human DNA polymerase eta. Mol. Cell. Biol. 20:2000;8001-8007.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8001-8007
    • Haracska, L.1    Prakash, S.2    Prakash, L.3
  • 92
    • 0037023677 scopus 로고    scopus 로고
    • Preferential misincorporation of purine nucleotides by human DNA polymerase eta opposite benzo[a]pyrene 7,8-diol 9,10-epoxide deoxyguanosine adducts
    • Chiapperino D., Kroth H., Kramarczuk I.H., Sayer J.M., Masutani C., Hanaovcka F., Jerina D.M., Cheh A.M. Preferential misincorporation of purine nucleotides by human DNA polymerase eta opposite benzo[a]pyrene 7,8-diol 9,10-epoxide deoxyguanosine adducts. J. Biol. Chem. 277:2002;11765-11771.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11765-11771
    • Chiapperino, D.1    Kroth, H.2    Kramarczuk, I.H.3    Sayer, J.M.4    Masutani, C.5    Hanaovcka, F.6    Jerina, D.M.7    Cheh, A.M.8
  • 93
    • 0037125136 scopus 로고    scopus 로고
    • Activities of human DNA polymerase k in response to the major benzo[a]pyrene DNA adduct: Error-free lesion bypass and extension synthesis from opposite the lesion
    • Zhang Y., Wu X., Guo D., Rechkoblit O., Wang Z. Activities of human DNA polymerase k in response to the major benzo[a]pyrene DNA adduct: error-free lesion bypass and extension synthesis from opposite the lesion. DNA Repair. 1:2002;559-569.
    • (2002) DNA Repair , vol.1 , pp. 559-569
    • Zhang, Y.1    Wu, X.2    Guo, D.3    Rechkoblit, O.4    Wang, Z.5
  • 94
    • 0037076538 scopus 로고    scopus 로고
    • Translesion synthesis by human DNA polymerase Kappa on a DNA template containing a single stereoisomer of dG-(+)- or dG-(-)-anti-N(2)-BPDE (7,8-dihydroxy-anti-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene)
    • Suzuki N., Ohashi E., Kolbanovskiy A., Geacintov N.E., Grollman A.P., Ohmori H., Shibutani S. Translesion synthesis by human DNA polymerase Kappa on a DNA template containing a single stereoisomer of dG-(+)- or dG-(-)-anti-N(2)-BPDE (7,8-dihydroxy-anti-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene). Biochemistry. 41:2002;6100-6106.
    • (2002) Biochemistry , vol.41 , pp. 6100-6106
    • Suzuki, N.1    Ohashi, E.2    Kolbanovskiy, A.3    Geacintov, N.E.4    Grollman, A.P.5    Ohmori, H.6    Shibutani, S.7
  • 95
    • 0035966003 scopus 로고    scopus 로고
    • Oxygen free radical damage to DNA: Translesion synthesis by human DNA polymerase eta and resistance to exonuclease action at cyclopurine deoxynucleoside residues
    • Kuraoka I., Robins P., Masutani C., Hanaoka F., Gasparutto D., Cadet J., Wood R.D., Lindahl T. Oxygen free radical damage to DNA: translesion synthesis by human DNA polymerase eta and resistance to exonuclease action at cyclopurine deoxynucleoside residues. J. Biol. Chem. 276:2001;49283-49288.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49283-49288
    • Kuraoka, I.1    Robins, P.2    Masutani, C.3    Hanaoka, F.4    Gasparutto, D.5    Cadet, J.6    Wood, R.D.7    Lindahl, T.8


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