메뉴 건너뛰기




Volumn , Issue , 2005, Pages 507-528

Mechanism of Bypass Polymerases in Eukaryotes

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77956116645     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9780849352683-32     Document Type: Chapter
Times cited : (3)

References (142)
  • 1
    • 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 1981; 184:471-478.
    • (1981) Mol Gen Genet , vol.184 , pp. 471-478
    • Prakash, L.1
  • 2
    • 0019429333 scopus 로고
    • Dna synthesis in uv-irradiated yeast
    • di Caprio L, Cox BS. DNA synthesis in UV-irradiated yeast. Mutat Res 1981; 82:69-85.
    • (1981) Mutat Res , vol.82 , pp. 69-85
    • Di Caprio, L.1    Cox, B.S.2
  • 3
    • 0035833662 scopus 로고    scopus 로고
    • Dna postreplication repair and mutagenesis in saccharomyces cerevisiae
    • Broomfield S, Hryciw T, Xiao W. DNA postreplication repair and mutagenesis in Saccharomyces cerevisiae. Mutat Res 2001; 486:167-184.
    • (2001) Mutat Res , vol.486 , pp. 167-184
    • Broomfield, S.1    Hryciw, T.2    Xiao, W.3
  • 4
    • 0017298802 scopus 로고
    • A model for replication repair in mammalian cells
    • Higgins NP, Kato K, Strauss B. A model for replication repair in mammalian cells. J Mol Biol 1976; 101:417-425.
    • (1976) J Mol Biol , vol.101 , pp. 417-425
    • Higgins, N.P.1    Kato, K.2    Strauss, B.3
  • 5
    • 0037196077 scopus 로고    scopus 로고
    • Two-step error-prone bypass of the (+)- and (—)-trans-anti-bpde-n2-dg adducts by human dna polymerases z and k
    • Zhang Y, Wu X, Guo D, Rechkoblit O, Geacintov NE, Wang Z. Two-step error-prone bypass of the (+)- and (—)-trans-anti-BPDE-N2-dG adducts by human DNA polymerases z and k. Mutat Res 2002; 510:23-35.
    • (2002) Mutat Res , vol.510 , pp. 23-35
    • Zhang, Y.1    Wu, X.2    Guo, D.3    Rechkoblit, O.4    Geacintov, N.E.5    Wang, Z.6
  • 6
    • 0001908121 scopus 로고
    • Mutants of yeast defective in mutation induction by ultraviolet light
    • Lemontt JF. Mutants of yeast defective in mutation induction by ultraviolet light. Genetics 1971; 68:21-33.
    • (1971) Genetics , vol.68 , pp. 21-33
    • Lemontt, J.F.1
  • 7
    • 0014303905 scopus 로고
    • The isolation, genetics and survival characteristics of ultraviolet light-sensitive mutants in yeast
    • Cox BS, Parry JM. The isolation, genetics and survival characteristics of ultraviolet light-sensitive mutants in yeast. Mutat Res 1968; 6:37-55.
    • (1968) Mutat Res , vol.6 , pp. 37-55
    • Cox, B.S.1    Parry, J.M.2
  • 8
    • 0016252465 scopus 로고
    • Specificity and frequency of ultraviolet-induced reversion of an iso-1-cytochrome c ochre mutant in radiationsensitive strains of yeast
    • Lawrence CW, Stewart JW, Sherman F, Christensen R. Specificity and frequency of ultraviolet-induced reversion of an iso-1-cytochrome c ochre mutant in radiationsensitive strains of yeast. J Mol Biol 1974; 85:137-162.
    • (1974) J Mol Biol , vol.85 , pp. 137-162
    • Lawrence, C.W.1    Stewart, J.W.2    Sherman, F.3    Christensen, R.4
  • 9
    • 0017288156 scopus 로고
    • Uv mutagenesis in radiation-sensitive strains of yeast
    • Lawrence CW, Christensen R. UV mutagenesis in radiation-sensitive strains of yeast. Genetics 1976; 82:207-232.
    • (1976) Genetics , vol.82 , pp. 207-232
    • Lawrence, C.W.1    Christensen, R.2
  • 10
    • 0025872504 scopus 로고
    • A similar defect in uv-induced mutagenesis conferred by the rad6 and rad18 mutations of saccharomyces cerevisiae
    • Cassier-Chauvat C, Fabre F. A similar defect in UV-induced mutagenesis conferred by the rad6 and rad18 mutations of Saccharomyces cerevisiae. Mutat Res 1991; 254: 247-253.
    • (1991) Mutat Res , vol.254 , pp. 247-253
    • Cassier-Chauvat, C.1    Fabre, F.2
  • 11
    • 0021971687 scopus 로고
    • New mutations affecting induced mutagenesis in yeast
    • Lawrence CW, Krauss BR, Christensen RB. New mutations affecting induced mutagenesis in yeast. Mutat Res 1985; 150:211-216.
    • (1985) Mutat Res , vol.150 , pp. 211-216
    • Lawrence, C.W.1    Krauss, B.R.2    Christensen, R.B.3
  • 12
    • 0021869226 scopus 로고
    • Rev7, a new gene concerned with uv mutagenesis in yeast
    • Lawrence CW, Das G, Christensen RB. REV7, a new gene concerned with UV mutagenesis in yeast. Mol Gen Genet 1985; 200:80-85.
    • (1985) Mol Gen Genet , vol.200 , pp. 80-85
    • Lawrence, C.W.1    Das, G.2    Christensen, R.B.3
  • 13
    • 0024461293 scopus 로고
    • Rev3, a saccharomyces cerevisiae gene whose function is required for induced mutagenesis, is predicted to encode a nonessential dna polymerase
    • Morrison A, Christensen RB, Alley J, Beck AK, Bernstine EG, Lemontt JF, Lawrence CW. REV3, a Saccharomyces cerevisiae gene whose function is required for induced mutagenesis, is predicted to encode a nonessential DNA polymerase. J Bacteriol 1989; 171:5659-5667.
    • (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
  • 15
    • 0029952294 scopus 로고    scopus 로고
    • Thymine-thymine dimer bypass by yeast dna polymerase z
    • Nelson JR, Lawrence CW, Hinkle DC. Thymine-thymine dimer bypass by yeast DNA polymerase Z. Science 1996; 272:1646-1649.
    • (1996) Science , vol.272 , pp. 1646-1649
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 16
    • 0035394142 scopus 로고    scopus 로고
    • Translesion synthesis by yeast dna polymerase z from templates containing lesions of ultraviolet radiation and acetylamino-fluorene
    • Guo D, Wu X, Rajpal DK, Taylor J-S, Wang Z. Translesion synthesis by yeast DNA polymerase Z from templates containing lesions of ultraviolet radiation and acetylamino-fluorene. Nucleic Acids Res 2001; 29:2875-2883.
    • (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
  • 17
    • 0141567937 scopus 로고    scopus 로고
    • Mutagenesis of benzo[a]-pyrene diol epoxide in yeast: Requirement for dna polymerase z and involvement of dna polymerase z
    • Xie Z, Braithwaite E, Guo D, Bo Z, Geacintov NE, Wang Z. Mutagenesis of benzo[a]-pyrene diol epoxide in yeast: Requirement for DNA polymerase Z and involvement of DNA polymerase z. Biochemistry 2003; 42:11253-11262.
    • (2003) Biochemistry , vol.42 , pp. 11253-11262
    • Xie, Z.1    Braithwaite, E.2    Guo, D.3    Bo, Z.4    Geacintov, N.E.5    Wang, Z.6
  • 18
    • 0029787108 scopus 로고    scopus 로고
    • Deoxycytidyl transferase activity of yeast rev1 protein
    • Nelson JR, Lawrence CW, Hinkle DC. Deoxycytidyl transferase activity of yeast REV1 protein. Nature 1996; 382:729-731.
    • (1996) Nature , vol.382 , pp. 729-731
    • Nelson, J.R.1    Lawrence, C.W.2    Hinkle, D.C.3
  • 20
  • 21
    • 0038529609 scopus 로고    scopus 로고
    • Synthesis across an acrolein-derived deoxyguanosine adduct. Participation of dna polymerase z in error- prone synthesis in human cells
    • Yang IY, Miller H, Wang Z, Frank EG, Ohmori H, Hanaoka F, Moriya M. Mammalian translesion DNA synthesis across an acrolein-derived deoxyguanosine adduct. Participation of DNA polymerase z in error- prone synthesis in human cells. J Biol Chem 2003; 278:13989-13994.
    • (2003) J Biol Chem , vol.278 , pp. 13989-13994
    • Yang, I.Y.1    Miller, H.2    Wang, Z.3    Frank, E.G.4    Ohmori, H.5    Hanaoka, F.6    Moriya, M.7    Mammalian Translesion, D.8
  • 23
    • 0032499748 scopus 로고    scopus 로고
    • A human homolog of the saccharomyces cerevisiae rev3 gene, which encodes the catalytic subunit of dna polymerase z
    • Gibbs PE, McGregor WG, Maher VM, Nisson P, Lawrence CW. A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase Z. Proc Natl Acad Sci USA 1998; 95:6876-6880.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6876-6880
    • Gibbs, P.E.1    McGregor, W.G.2    Maher, V.M.3    Nisson, P.4    Lawrence, C.W.5
  • 24
    • 0032994152 scopus 로고    scopus 로고
    • A full-length cdna of hrev3 is predicted to encode dna polymerase z for damage-induced mutagenesis is humans
    • Lin W, Wu X, Wang Z. A full-length cDNA of hREV3 is predicted to encode DNA polymerase Z for damage-induced mutagenesis is humans. Mutat Res 1999; 433:89-98.
    • (1999) Mutat Res , vol.433 , pp. 89-98
    • Lin, W.1    Wu, X.2    Wang, Z.3
  • 25
    • 0034635445 scopus 로고    scopus 로고
    • A human rev7 homolog that interacts with the polymerase z catalytic subunit hrev3 and the spindle assembly checkpoint protein hmad2
    • Murakumo Y, Roth T, Ishii H, Rasio D, Numata S, Croce CM, Fishel R. A human REV7 homolog that interacts with the polymerase Z catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD2. J Biol Chem 2000; 275:4391-4397.
    • (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
  • 26
    • 0141542616 scopus 로고    scopus 로고
    • Decreased frequency and highly aberrant spectrum of ultraviolet-induced mutations in the hprt gene of mouse fibroblasts expressing antisense rna to dna polymerase z
    • Diaz M, Watson NB, Turkington G, Verkoczy LK, Klinman NR, McGregor WG. Decreased frequency and highly aberrant spectrum of ultraviolet-induced mutations in the hprt gene of mouse fibroblasts expressing antisense RNA to DNA polymerase Z. Mol Cancer Res 2003; 1:836-847.
    • (2003) Mol Cancer Res , vol.1 , pp. 836-847
    • Diaz, M.1    Watson, N.B.2    Turkington, G.3    Verkoczy, L.K.4    Klinman, N.R.5    McGregor, W.G.6
  • 28
    • 0034609744 scopus 로고    scopus 로고
    • Disruption of mouse polymerase z (Rev3) leads to embryonic lethality and impairs blastocyst development in vitro
    • Bemark M, Khamlichi AA, Davies SL, Neuberger MS. Disruption of mouse polymerase Z (Rev3) leads to embryonic lethality and impairs blastocyst development in vitro. Curr Biol 2000; 10:1213-1216.
    • (2000) Curr Biol , vol.10 , pp. 1213-1216
    • Bemark, M.1    Khamlichi, A.A.2    Davies, S.L.3    Neuberger, M.S.4
  • 29
    • 0034609725 scopus 로고    scopus 로고
    • Disruption of the rev3l-encoded catalytic subunit of polymerase z in mice results in early embryonic lethality
    • Esposito G, Godindagger I, Klein U, Yaspo M, Cumano A, Rajewsky K. Disruption of the REv3l -encoded catalytic subunit of polymerase Z in mice results in early embryonic lethality. Curr Biol 2000; 10:1221-1224.
    • (2000) Curr Biol , vol.10 , pp. 1221-1224
    • Esposito, G.1    Godindagger, I.2    Klein, U.3    Yaspo, M.4    Cumano, A.5    Rajewsky, K.6
  • 32
    • 0021925909 scopus 로고
    • Rad6 gene of saccharomyces cerevisiae encodes a protein containing a tract of 13 consecutive asparatates
    • Reynolds P, Weber S, Prakash L. RAD6 gene of Saccharomyces cerevisiae encodes a protein containing a tract of 13 consecutive asparatates. Proc Natl Acad Sci USA 1985; 82:168-172.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 168-172
    • Reynolds, P.1    Weber, S.2    Prakash, L.3
  • 33
    • 0024236309 scopus 로고
    • Potential dna-binding domains in the rad18 gene product of saccharomyces cerevisiae
    • Chanet R, Magana-Schwencke N, Fabre F. Potential DNA-binding domains in the RAD18 gene product of Saccharomyces cerevisiae. Gene 1988; 74:543-547.
    • (1988) Gene , vol.74 , pp. 543-547
    • Chanet, R.1    Magana-Schwencke, N.2    Fabre, F.3
  • 34
    • 0024297027 scopus 로고
    • The saccharomyces cerevisiae rad18 gene encodes a protein that contains potential zinc finger domains for nucleic acid binding and a putative nucleotide binding sequence
    • Jones JS, Weber S, Prakash L. The Saccharomyces cerevisiae RAD18 gene encodes a protein that contains potential zinc finger domains for nucleic acid binding and a putative nucleotide binding sequence. Nucleic Acids Res 1988; 16:7119-7131.
    • (1988) Nucleic Acids Res , vol.16 , pp. 7119-7131
    • Jones, J.S.1    Weber, S.2    Prakash, L.3
  • 35
    • 0024526246 scopus 로고
    • The rev1 gene of saccharomyces cerevisiae: Isolation, sequence, and functional analysis
    • Larimer FW, Perry JR, Hardigree AA. The REV1 gene of Saccharomyces cerevisiae: isolation, sequence, and functional analysis. J Bacteriol 1989; 171:230-237.
    • (1989) J Bacteriol , vol.171 , pp. 230-237
    • Larimer, F.W.1    Perry, J.R.2    Hardigree, A.A.3
  • 36
    • 0033729983 scopus 로고    scopus 로고
    • Pol32, a subunit of the saccharomyces cerevisiae dna polymerase d, defines a link between dna replication and the mutagenic bypass repair pathway
    • Huang ME, de Calignon A, Nicolas A, Galibert F. POL32, a subunit of the Saccharomyces cerevisiae DNA polymerase d, defines a link between DNA replication and the mutagenic bypass repair pathway. Curr Genet 2000; 38:178-187.
    • (2000) Curr Genet , vol.38 , pp. 178-187
    • Huang, M.E.1    De Calignon, A.2    Nicolas, A.3    Galibert, F.4
  • 37
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by sumo and ubiquitin conjugation
    • Stelter P, Ulrich HD. Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature 2003; 425:188-191.
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 39
    • 0028314007 scopus 로고
    • Specific complex formation between yeast rad6 and rad18 proteins: A potential mechanism for targeting rad6 ubiqui-tin-conjugating activity to dna damage sites
    • Bailly V, Lamb J, Sung P, Prakash S, Prakash L. Specific complex formation between yeast RAD6 and RAD18 proteins: a potential mechanism for targeting RAD6 ubiqui-tin-conjugating activity to DNA damage sites. Genes Dev 1994; 8:811-820.
    • (1994) Genes Dev , vol.8 , pp. 811-820
    • Bailly, V.1    Lamb, J.2    Sung, P.3    Prakash, S.4    Prakash, L.5
  • 40
    • 0030800865 scopus 로고    scopus 로고
    • Yeast dna repair proteins rad6 and rad18 form a heterodimer that has ubiquitin conjugating, dna binding, and atp hydrolytic activities
    • Bailly V, Lauder S, Prakash S, Prakash L. Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities. J Biol Chem 1997; 272:23360-23365.
    • (1997) J Biol Chem , vol.272 , pp. 23360-23365
    • Bailly, V.1    Lauder, S.2    Prakash, S.3    Prakash, L.4
  • 43
    • 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 USA 2000; 97:7927-7932.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7927-7932
    • Tateishi, S.1    Sakuraba, Y.2    Masuyama, S.3    Inoue, H.4    Yamaizumi, M.5
  • 44
    • 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 1999; 27:4468-4475.
    • (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
  • 46
    • 0030735538 scopus 로고    scopus 로고
    • The saccharomyces cerevisiae rad30 gene, a homologue of escherichia coli din b and umuc, is dna damage inducible and functions in a novel error-free postreplication repair mechanism
    • McDonald JP, Levine AS, Woodgate R. The Saccharomyces cerevisiae RAD30 gene, a homologue of Escherichia coli din B and umuC, is DNA damage inducible and functions in a novel error-free postreplication repair mechanism. Genetics 1997; 147:1557-1568.
    • (1997) Genetics , vol.147 , pp. 1557-1568
    • McDonald, J.P.1    Levine, A.S.2    Woodgate, R.3
  • 47
    • 0031921639 scopus 로고    scopus 로고
    • Deletion of the saccharomyces cerevisiae gene rad30 encoding an escherichia coli dinb homolog confers uv radiation sensitivity and altered mutability
    • Roush AA, Suarez M, Friedberg EC, Radman M, Siede W. Deletion of the Saccharomyces cerevisiae gene RAD30 encoding an Escherichia coli DinB homolog confers UV radiation sensitivity and altered mutability. Mol Gen Genet 1998; 257:686-692.
    • (1998) Mol Gen Genet , vol.257 , pp. 686-692
    • Roush, A.A.1    Suarez, M.2    Friedberg, E.C.3    Radman, M.4    Siede, W.5
  • 48
    • 0033548231 scopus 로고    scopus 로고
    • Efficient bypass of a thymine-thymine dimer by yeast dna polymerase, polp
    • Johnson RE, Prakash S, Prakash L. Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Polp. Science 1999; 283:1001-1004.
    • (1999) Science , vol.283 , pp. 1001-1004
    • Johnson, R.E.1    Prakash, S.2    Prakash, L.3
  • 49
    • 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 1999; 18: 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
  • 51
    • 0033538470 scopus 로고    scopus 로고
    • Hrad30 mutations in the variant form of xeroderma pigmentosum
    • Johnson RE, Kondratick CM, Prakash S, Prakash L. hRAD30 mutations in the variant form of xeroderma pigmentosum. Science 1999; 285:263-265.
    • (1999) Science , vol.285 , pp. 263-265
    • Johnson, R.E.1    Kondratick, C.M.2    Prakash, S.3    Prakash, L.4
  • 52
  • 55
    • 0033601194 scopus 로고    scopus 로고
    • Fidelity and processivity of saccharomyces cerevisiae dna polymerase z
    • Washington MT, Johnson RE, Prakash S, Prakash L. Fidelity and processivity of Saccharomyces cerevisiae DNA polymerase z. J Biol Chem 1999; 274:36835-36838.
    • (1999) J Biol Chem , vol.274 , pp. 36835-36838
    • Washington, M.T.1    Johnson, R.E.2    Prakash, S.3    Prakash, L.4
  • 58
    • 0034847259 scopus 로고    scopus 로고
    • Structure of the catalytic core of s. Cerevisiae dna polymerase z: Implications for translesion dna synthesis
    • Trincao J, Johnson RE, Escalante CR, Prakash S, Prakash L, Aggarwal AK. Structure of the catalytic core of S. cerevisiae DNA polymerase z: implications for translesion DNA synthesis. Mol Cell 2001; 8:417-426.
    • (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
  • 59
    • 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 2001; 107:91-102.
    • (2001) Cell , vol.107 , pp. 91-102
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 60
    • 0041864009 scopus 로고    scopus 로고
    • Replication of a cis-syn thymine dimer at atomic resolution
    • Ling H, Boudsocq F, Plosky BS, Woodgate R, Yang W. Replication of a cis-syn thymine dimer at atomic resolution. Nature 2003; 424:1083-1087.
    • (2003) Nature , vol.424 , pp. 1083-1087
    • Ling, H.1    Boudsocq, F.2    Plosky, B.S.3    Woodgate, R.4    Yang, W.5
  • 61
    • 0033830464 scopus 로고    scopus 로고
    • Preferential incorporation of g opposite template t by the low fidelity human dna polymerase i
    • Zhang Y, Yuan F, Wu X, Wang Z. Preferential incorporation of G opposite template T by the low fidelity human DNA polymerase i. Mol Cell Biol 2000; 20:7099-7108.
    • (2000) Mol Cell Biol , vol.20 , pp. 7099-7108
    • Zhang, Y.1    Yuan, F.2    Wu, X.3    Wang, Z.4
  • 62
  • 63
    • 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 NE, Taylor JS, Wang Z. Response of human REV1 to different DNA damage: preferential dCMP insertion opposite the lesion. Nucleic Acids Res 2002; 30:1630-1638.
    • (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
  • 64
    • 0037169495 scopus 로고    scopus 로고
    • Mechanisms of dcmp transferase reactions catalyzed by mouse rev1 protein
    • Masuda Y, Takahashi M, Fukuda S, Sumii M, Kamiya K. Mechanisms of dCMP transferase reactions catalyzed by mouse Rev1 protein. J Biol Chem 2001; 277:3040-3046.
    • (2001) J Biol Chem , vol.277 , pp. 3040-3046
    • Masuda, Y.1    Takahashi, M.2    Fukuda, S.3    Sumii, M.4    Kamiya, K.5
  • 65
    • 0037013287 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 2002; 277:15546-15551.
    • (2002) J Biol Chem , vol.277 , pp. 15546-15551
    • Haracska, L.1    Prakash, S.2    Prakash, L.3
  • 66
    • 0035862988 scopus 로고    scopus 로고
    • Domain structure, localization, and function of dna polymerase z, defective in xeroderma pigmentosum variant cells
    • Kannouche P, Broughton BC, Volker M, Hanaoka F, Mullenders LH, Lehmann AR. Domain structure, localization, and function of DNA polymerase z, defective in xeroderma pigmentosum variant cells. Genes Dev 2001; 15:158-172.
    • (2001) Genes Dev , vol.15 , pp. 158-172
    • Kannouche, P.1    Broughton, B.C.2    Volker, M.3    Hanaoka, F.4    Mullenders, L.H.5    Lehmann, A.R.6
  • 67
    • 0035012235 scopus 로고    scopus 로고
    • Acidic resudues critical for the activity and biological function of yeast dna polymerase z
    • Kondratick CM, Washington MT, Prakash S, Prakash L. Acidic resudues critical for the activity and biological function of yeast DNA polymerase z. Mol Cell Biol 2001; 21: 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
  • 70
    • 0035158355 scopus 로고    scopus 로고
    • Highly frequent frameshift dna synthesis by human dna polymerase m
    • Zhang Y, Wu X, Yuan F, Xie Z, Wang Z. Highly frequent frameshift DNA synthesis by human DNA polymerase m. Mol Cell Biol 2001; 21:7995-8006.
    • (2001) Mol Cell Biol , vol.21 , pp. 7995-8006
    • Zhang, Y.1    Wu, X.2    Yuan, F.3    Xie, Z.4    Wang, Z.5
  • 71
    • 0036293744 scopus 로고    scopus 로고
    • Association of dna polymerase m (Pol m) with ku and ligase iv: Role for pol m in end-joining double-strand break repair
    • Mahajan KN, Nick McElhinny SA, Mitchell BS, Ramsden DA. Association of DNA polymerase m (pol m) with Ku and ligase IV: role for pol m in end-joining double-strand break repair. Mol Cell Biol 2002; 22:5194-5202.
    • (2002) Mol Cell Biol , vol.22 , pp. 5194-5202
    • Mahajan, K.N.1    Nick McElhinny, S.A.2    Mitchell, B.S.3    Ramsden, D.A.4
  • 74
    • 0037133339 scopus 로고    scopus 로고
    • Human dinb1 -encoded dna polymerase k is a promiscuous extender of mispaired primer termini
    • Washington MT, Johnson RE, Prakash L, Prakash S. Human DINB1 -encoded DNA polymerase k is a promiscuous extender of mispaired primer termini. Proc Natl Acad Sci USA 2002; 99:1910-1914.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1910-1914
    • Washington, M.T.1    Johnson, R.E.2    Prakash, L.3    Prakash, S.4
  • 75
    • 0037125136 scopus 로고    scopus 로고
    • Activities of human dna polyemrase k in response to the major benzo[a]pyrene dna adduct: Error-free bypass and extension synthesis from opposite the lesion
    • Zhang Y, Wu X, Guo D, Rechkoblit O, Wang Z. Activities of human DNA polyemrase k in response to the major benzo[a]pyrene DNA adduct: error-free bypass and extension synthesis from opposite the lesion. DNA Repair 2002; 1:559-569.
    • (2002) DNA Repair , vol.1 , pp. 559-569
    • Zhang, Y.1    Wu, X.2    Guo, D.3    Rechkoblit, O.4    Wang, Z.5
  • 76
    • 0036493157 scopus 로고    scopus 로고
    • Uv-induced t- > c transition at a tt photoproduct site is dependent on saccharomyces cerevisiae polymerase z in vivo
    • Zhang H, Siede W. UV-induced T- > C transition at a TT photoproduct site is dependent on Saccharomyces cerevisiae polymerase z in vivo. Nucleic Acids Res 2002; 30:1262-1267.
    • (2002) Nucleic Acids Res , vol.30 , pp. 1262-1267
    • Zhang, H.1    Siede, W.2
  • 77
    • 0037099578 scopus 로고    scopus 로고
    • Lesion bypass in yeast cells: Pol z participates in a multi-dna polymerase process
    • Bresson A, Fuchs RP. Lesion bypass in yeast cells: Pol z participates in a multi-DNA polymerase process. EMBO J 2002; 21:3881-3887.
    • (2002) EMBO J , vol.21 , pp. 3881-3887
    • Bresson, A.1    Fuchs, R.P.2
  • 79
    • 0017309743 scopus 로고
    • Frequency of ultraviolet light-induced mutations is higher in exeroderma pimentosum variant cells than in normal human cells
    • Maher VM, Ouellette LM, Curren RD, McCormick JJ. Frequency of ultraviolet light-induced mutations is higher in exeroderma pimentosum variant cells than in normal human cells. Nature 1976; 261:593-595.
    • (1976) Nature , vol.261 , pp. 593-595
    • Maher, V.M.1    Ouellette, L.M.2    Curren, R.D.3    McCormick, J.J.4
  • 80
    • 0025858252 scopus 로고
    • Xeroderma pigmentosum variant cells are less likely than normal cells to incorporate damp opposite photoproducts during replication of uv-irradiated plasmids
    • Wang YC, Maher VM, McCormick JJ. Xeroderma pigmentosum variant cells are less likely than normal cells to incorporate dAMP opposite photoproducts during replication of UV-irradiated plasmids. Proc Natl Acad Sci USA 1991; 88:7810-7814.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7810-7814
    • Wang, Y.C.1    Maher, V.M.2    McCormick, J.J.3
  • 81
    • 0032938853 scopus 로고    scopus 로고
    • Abnormal, error-prone bypass of photoproducts by xeroderma pigmentosum variant cell extracts results in extreme strand bias for the kinds of mutations induced by uv light
    • McGregor WG, Wei D, Maher VM, McCormick JJ. Abnormal, error-prone bypass of photoproducts by xeroderma pigmentosum variant cell extracts results in extreme strand bias for the kinds of mutations induced by UV light. Mol Cell Biol 1999; 19:147-154.
    • (1999) Mol Cell Biol , vol.19 , pp. 147-154
    • McGregor, W.G.1    Wei, D.2    Maher, V.M.3    McCormick, J.J.4
  • 84
    • 0034596992 scopus 로고    scopus 로고
    • Misinsertion and bypass of thymine-thymine dimers by human dna polymerase i
    • Tissier A, Frank EG, McDonald JP, Iwai S, Hanaoka F, Woodgate R. Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase i. EMBO J 2000; 19:5259-5266.
    • (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
  • 85
    • 0037180343 scopus 로고    scopus 로고
    • Polk protects mammalian cells against the lethal and mutagenic effects of benzo[a]pyrene
    • Ogi T, Shinkai Y, Tanaka K, Ohmori H. Polk protects mammalian cells against the lethal and mutagenic effects of benzo[a]pyrene. Proc Natl Acad Sci USA 2002; 99: 15548-15553.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15548-15553
    • Ogi, T.1    Shinkai, Y.2    Tanaka, K.3    Ohmori, H.4
  • 88
    • 0032102944 scopus 로고    scopus 로고
    • The (6-4) photoproduct of thymine-thymine induces targeted substitution mutations in mammalian cells
    • Kamiya H, Iwai S, Kasai H. The (6-4) photoproduct of thymine-thymine induces targeted substitution mutations in mammalian cells. Nucleic Acids Res 1998; 26: 2611-2617.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2611-2617
    • Kamiya, H.1    Iwai, S.2    Kasai, H.3
  • 89
    • 0025305574 scopus 로고
    • Rapid repair kinetics of pyrimidine(6-4)pyrimidone photoproducts in human cells are due to excision rather than conformational change
    • Mitchell DL, Brash DE, Nairn RS. Rapid repair kinetics of pyrimidine(6-4)pyrimidone photoproducts in human cells are due to excision rather than conformational change. Nucleic Acids Res 1990; 18:963-971.
    • (1990) Nucleic Acids Res , vol.18 , pp. 963-971
    • Mitchell, D.L.1    Brash, D.E.2    Nairn, R.S.3
  • 90
    • 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, Okomuto 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    Okomuto, D.S.3    Hanawalt, P.C.4
  • 91
    • 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
  • 93
    • 0034676229 scopus 로고    scopus 로고
    • Alteration of ultraviolet-induced mutagenesis in yeast though molecular modulation of the rev3 and rev7 gene expression
    • Rajpal DK, Wu X, Wang Z. Alteration of ultraviolet-induced mutagenesis in yeast though molecular modulation of the REV3 and REV7 gene expression. Mutat Res 2000; 461:133-143.
    • (2000) Mutat Res , vol.461 , pp. 133-143
    • Rajpal, D.K.1    Wu, X.2    Wang, Z.3
  • 94
    • 0026111317 scopus 로고
    • The ‘a rule’ of mutagen specificity: A consequence of dna polymerase bypass of non-instructional lesions?
    • Strauss BS. The ‘A rule’ of mutagen specificity: a consequence of DNA polymerase bypass of non-instructional lesions? Bioessays 1991; 13:79-84.
    • (1991) Bioessays , vol.13 , pp. 79-84
    • Strauss, B.S.1
  • 97
    • 0026775189 scopus 로고
    • Mutation spectrum of heat-induced abasic sites on a single-stranded shuttle vector replicated in mammalian cells
    • Neto JB, Gentil A, Cabral RE, Sarasin A. Mutation spectrum of heat-induced abasic sites on a single-stranded shuttle vector replicated in mammalian cells. J Biol Chem 1992; 267:19718-19723.
    • (1992) J Biol Chem , vol.267 , pp. 19718-19723
    • Neto, J.B.1    Gentil, A.2    Cabral, R.E.3    Sarasin, A.4
  • 99
    • 0028292587 scopus 로고
    • Mechanism of mutation on dna templates containing synthetic abasic sites: Study with a double strand vector
    • Takeshita M, Eisenberg W. Mechanism of mutation on DNA templates containing synthetic abasic sites: study with a double strand vector. Nucleic Acids Res 1994; 22: 1897-1902.
    • (1994) Nucleic Acids Res , vol.22 , pp. 1897-1902
    • Takeshita, M.1    Eisenberg, W.2
  • 100
    • 0026727768 scopus 로고
    • Mutagenesis by apurinic sites in normal and ataxia telangiectasia human lymphoblastoid cells
    • Klinedinst DK, Drinkwater NR. Mutagenesis by apurinic sites in normal and ataxia telangiectasia human lymphoblastoid cells. Mol Carcinog 1992; 6:32-42.
    • (1992) Mol Carcinog , vol.6 , pp. 32-42
    • Klinedinst, D.K.1    Drinkwater, N.R.2
  • 101
    • 0029100516 scopus 로고
    • Novel mutagenic properties of abasic sites in saccharomyces cerevisiae
    • Gibbs PE, Lawrence CW. Novel mutagenic properties of abasic sites in Saccharomyces cerevisiae. J Mol Biol 1995; 251:229-236.
    • (1995) J Mol Biol , vol.251 , pp. 229-236
    • Gibbs, P.E.1    Lawrence, C.W.2
  • 103
    • 0034660259 scopus 로고    scopus 로고
    • Mechanisms of accurate translesion synthesis by human dna polymerase z
    • Masutani C, Kusumoto R, Iwai S, Hanaoka F. Mechanisms of accurate translesion synthesis by human DNA polymerase z. EMBO J 2000; 19:3100-3109.
    • (2000) EMBO J , vol.19 , pp. 3100-3109
    • Masutani, C.1    Kusumoto, R.2    Iwai, S.3    Hanaoka, F.4
  • 104
    • 0025981359 scopus 로고
    • Insertion of specific bases during dna synthesis past the oxidation- damaged base 8-oxodg
    • Shibutani S, Takeshita M, Grollman AP. Insertion of specific bases during DNA synthesis past the oxidation- damaged base 8-oxodG. Nature 1991; 349:431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 105
    • 0034425754 scopus 로고    scopus 로고
    • Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by dna polymerase z
    • Haracska L, Yu SL, Johnson RE, Prakash L, Prakash S. Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase z. Nat Genet 2000; 25:458-461.
    • (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
  • 106
    • 0037313816 scopus 로고    scopus 로고
    • Yeast dna polymerase z is an efficient extender of primer ends opposite from 7,8-dihydro-8-oxoguanine and o6-methylguanine
    • 6-methylguanine. Mol Cell Biol 2003; 23:1453-1459.
    • (2003) Mol Cell Biol , vol.23 , pp. 1453-1459
    • Haracska, L.1    Prakash, S.2    Prakash, L.3
  • 108
    • 0028089887 scopus 로고
    • Mutational spectrum induced in saccharomyces cerevisiae by the carcinogen n-2-acetylaminofluorene
    • Roy A, Fuchs RP. Mutational spectrum induced in Saccharomyces cerevisiae by the carcinogen N-2-acetylaminofluorene. Mol Gen Genet 1994; 245:69-77.
    • (1994) Mol Gen Genet , vol.245 , pp. 69-77
    • Roy, A.1    Fuchs, R.P.2
  • 109
    • 0027436351 scopus 로고
    • Kato t. n-acetoxy-n-acetyl-2-aminofluor-ene-induced mutation spectrum in a human hprt cdna shuttle vector integrated into mammalian cells
    • Ogawa HI, Kimura H, Koya M, Higuchi H, Kato T. N -acetoxy- N -acetyl-2-aminofluor-ene-induced mutation spectrum in a human hprt cDNA shuttle vector integrated into mammalian cells. Carcinogenesis 1993; 14:2245-2250.
    • (1993) Carcinogenesis , vol.14 , pp. 2245-2250
    • Ogawa, H.I.1    Kimura, H.2    Koya, M.3    Higuchi, H.4
  • 110
    • 0032821162 scopus 로고    scopus 로고
    • Distinct roles for rev1p and rev7p during translesion synthesis in saccharomyces cerevisiae
    • Baynton K, Bresson-Roy A, Fuchs RP. Distinct roles for Rev1p and Rev7p during translesion synthesis in Saccharomyces cerevisiae. Mol Microbiol 1999; 34:124-133.
    • (1999) Mol Microbiol , vol.34 , pp. 124-133
    • Baynton, K.1    Bresson-Roy, A.2    Fuchs, R.P.3
  • 111
    • 0031907155 scopus 로고    scopus 로고
    • Analysis of damage tolerance pathways in saccharomyces cerevisiae: A requirement for rev3 dna polymerase in translesion synthesis
    • Baynton K, Bresson-Roy A, Fuchs RP. Analysis of damage tolerance pathways in Saccharomyces cerevisiae : a requirement for Rev3 DNA polymerase in translesion synthesis. Mol Cell biol 1998; 18:960-966.
    • (1998) Mol Cell Biol , vol.18 , pp. 960-966
    • Baynton, K.1    Bresson-Roy, A.2    Fuchs, R.P.3
  • 112
    • 2342635739 scopus 로고    scopus 로고
    • Translesion synthesis of acetylaminofluorene-dg adducts by dna polymerase z is stimulated by yeast revl protein
    • Guo D, Xie Z, Shen H, Bo Z, Wang Z. Translesion synthesis of acetylaminofluorene-dG adducts by DNA polymerase Z is stimulated by yeast Revl protein. Nucleic Acids Res 2004; 32:1122-1130.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1122-1130
    • Guo, D.1    Xie, Z.2    Shen, H.3    Bo, Z.4    Wang, Z.5
  • 113
    • 0035808417 scopus 로고    scopus 로고
    • Purification and characterization of polk, a dna polymerase encoded by the human dinb1 gene
    • Gerlach VL, Feaver WJ, Fischhaber PL, Friedberg EC. Purification and characterization of polk, a DNA polymerase encoded by the human DINB1 gene. J Biol CheDINB1m 2001; 276:92-98.
    • (2001) J Biol Chedinb1m , vol.276 , pp. 92-98
    • Gerlach, V.L.1    Feaver, W.J.2    Fischhaber, P.L.3    Friedberg, E.C.4
  • 114
    • 0028285404 scopus 로고
    • Polycyclic hydrocarbon activation: Bay regions and beyond
    • Phillips DH, Grover PL. Polycyclic hydrocarbon activation: bay regions and beyond. Drug Metab Rev 1994; 26:443-467.
    • (1994) Drug Metab Rev , vol.26 , pp. 443-467
    • Phillips, D.H.1    Grover, P.L.2
  • 115
    • 0028897519 scopus 로고
    • Polycyclic aromatic hydrocarbons: Chemistry of dna adduct formation
    • Peltonen K, Dipple A. Polycyclic aromatic hydrocarbons: chemistry of DNA adduct formation. J Occup Environ Med 1995; 37:52-58.
    • (1995) J Occup Environ Med , vol.37 , pp. 52-58
    • Peltonen, K.1    Dipple, A.2
  • 116
    • 0024442239 scopus 로고
    • Dna adducts from carcinogenic and noncarcinogenic enantiomers of benzo[a]pyrene dihydrodiol epoxide
    • Cheng SC, Hilton BD, Roman JM, Dipple A. DNA adducts from carcinogenic and noncarcinogenic enantiomers of benzo[a]pyrene dihydrodiol epoxide. Chem Res Toxicol 1989; 2:334-340.
    • (1989) Chem Res Toxicol , vol.2 , pp. 334-340
    • Cheng, S.C.1    Hilton, B.D.2    Roman, J.M.3    Dipple, A.4
  • 118
    • 0037023677 scopus 로고    scopus 로고
    • Preferential misincorporation of purine nucleotides by human dna polymerase z opposite benzo[a]pyrene 7,8-diol 9,10-epoxide deoxyguanosine adducts
    • Chiapperino D, Kroth H, Kramarczuk IH, Sayer JM, Masutani C, Hanaoka F, Jerina DM, Cheh AM. Preferential misincorporation of purine nucleotides by human DNA polymerase z opposite benzo[a]pyrene 7,8-diol 9,10-epoxide deoxyguanosine adducts. J Biol Chem 2002; 277:11765-11771.
    • (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    Hanaoka, F.6    Jerina, D.M.7    Cheh, A.M.8
  • 119
    • 0037196075 scopus 로고    scopus 로고
    • Hrev3 is essential for error-prone translesion synthesis past uv or benzo[a]pyrene diol epoxide-induced dna lesions in human fibroblasts
    • Li Z, Zhang H, McManus TP, McCormick JJ, Lawrence CW, Maher VM. hREV3 is essential for error-prone translesion synthesis past UV or benzo[a]pyrene diol epoxide-induced DNA lesions in human fibroblasts. Mutat Res 2002; 510:71-80.
    • (2002) Mutat Res , vol.510 , pp. 71-80
    • Li, Z.1    Zhang, H.2    McManus, T.P.3    McCormick, J.J.4    Lawrence, C.W.5    Maher, V.M.6
  • 120
    • 0000011428 scopus 로고    scopus 로고
    • Holland JF, Bast RC Jr, Morton DL, Frei E III, Kufe DW, Weichselbaum RR eds, 4th ed. Baltimore: Williams & Wilkins
    • Colvin OM. In: Holland JF, Bast RC Jr, Morton DL, Frei E III, Kufe DW, Weichselbaum RR eds. Cancer Medicine. 4th ed. Baltimore: Williams & Wilkins, 1997; 1:949-975.
    • (1997) Cancer Medicine , vol.1 , pp. 949-975
    • Colvin, O.M.1
  • 122
    • 0025071833 scopus 로고
    • Single d(Apg)/cis-diamminedichlor-oplatinum(ii) adduct-induced mutagenesis in escherichia coli
    • Burnouf D, Gauthier C, Chottard JC, Fuchs RP. Single d(ApG)/cis-diamminedichlor-oplatinum(II) adduct-induced mutagenesis in Escherichia coli. Proc Natl Acad Sci USA 1990; 87:6087-6091.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6087-6091
    • Burnouf, D.1    Gauthier, C.2    Chottard, J.C.3    Fuchs, R.P.4
  • 123
    • 0027058626 scopus 로고
    • Characterization and localization of cis-diamminedichloro-platinum(Ii) adducts on a purified oligonucleotide containing the codons 12 and 13 of h-ras proto-oncogene
    • Pillaire MJ, Villani G, Hoffmann JS, Mazard AM, Defais M. Characterization and localization of cis -diamminedichloro-platinum(II) adducts on a purified oligonucleotide containing the codons 12 and 13 of H-ras proto-oncogene. Nucleic Acids Res 1992; 20:6473-6479.
    • (1992) Nucleic Acids Res , vol.20 , pp. 6473-6479
    • Pillaire, M.J.1    Villani, G.2    Hoffmann, J.S.3    Mazard, A.M.4    Defais, M.5
  • 124
    • 0029620990 scopus 로고
    • Replication of dna containing cisplatin lesions and its mutagenic consequences
    • Pillaire MJ, Hoffmann JS, Defais M, Villani G. Replication of DNA containing cisplatin lesions and its mutagenic consequences. Biochimie 1995; 77:803-807.
    • (1995) Biochimie , vol.77 , pp. 803-807
    • Pillaire, M.J.1    Hoffmann, J.S.2    Defais, M.3    Villani, G.4
  • 125
    • 0027478962 scopus 로고
    • Mutagenicity and genotoxicity of the major dna adduct of the antitumor drug cis-diamminedichloroplatinum(ii)
    • Bradley LJ, Yarema KJ, Lippard SJ, Essigmann JM. Mutagenicity and genotoxicity of the major DNA adduct of the antitumor drug cis-diamminedichloroplatinum(II). Biochemistry 1993; 32:982-988.
    • (1993) Biochemistry , vol.32 , pp. 982-988
    • Bradley, L.J.1    Yarema, K.J.2    Lippard, S.J.3    Essigmann, J.M.4
  • 126
    • 0032580979 scopus 로고    scopus 로고
    • Nmr solution structure of a dna dodecamer duplex containing a cis-diammineplatinum(Ii) d(gpg) intrastrand cross-link, the major adduct of the anticancer drug cisplatin
    • Gelasco A, Lippard SJ. NMR solution structure of a DNA dodecamer duplex containing a cis -diammineplatinum(II) d(GpG) intrastrand cross-link, the major adduct of the anticancer drug cisplatin. Biochemistry 1998; 37:9230-9239.
    • (1998) Biochemistry , vol.37 , pp. 9230-9239
    • Gelasco, A.1    Lippard, S.J.2
  • 127
    • 0034712656 scopus 로고    scopus 로고
    • Efficient translesion replication past oxaliplatin and cisplatin gpg adducts by human dna polymerase z
    • Vaisman A, Masutani C, Hanaoka F, Chaney SG. Efficient translesion replication past oxaliplatin and cisplatin GpG adducts by human DNA polymerase z. Biochemistry 2000; 39:4575-4580.
    • (2000) Biochemistry , vol.39 , pp. 4575-4580
    • Vaisman, A.1    Masutani, C.2    Hanaoka, F.3    Chaney, S.G.4
  • 128
    • 0345060496 scopus 로고    scopus 로고
    • Efficiency of extension of mismatched primer termini across from cisplatin and oxaliplatin adducts by human dna polymerases ß and z in vitro
    • Bassett E, Vaisman A, Havener JM, Masutani C, Hanaoka F, Chaney SG. Efficiency of extension of mismatched primer termini across from cisplatin and oxaliplatin adducts by human DNA polymerases ß and z in vitro. Biochemistry 2003; 42:14197-14206.
    • (2003) Biochemistry , vol.42 , pp. 14197-14206
    • Bassett, E.1    Vaisman, A.2    Havener, J.M.3    Masutani, C.4    Hanaoka, F.5    Chaney, S.G.6
  • 129
    • 0037027854 scopus 로고    scopus 로고
    • Frameshifts and deletions during in vitro translesion synthesis past pt-dna adducts by dna polymerases ß and z
    • Bassett E, Vaisman A, Tropea KA, McCall CM, Masutani C, Hanaoka F, Chaney SG. Frameshifts and deletions during in vitro translesion synthesis past Pt-DNA adducts by DNA polymerases ß and z. DNA Repair 2002; 1:1003-1016.
    • (2002) DNA Repair , vol.1 , pp. 1003-1016
    • Bassett, E.1    Vaisman, A.2    Tropea, K.A.3    McCall, C.M.4    Masutani, C.5    Hanaoka, F.6    Chaney, S.G.7
  • 130
    • 0030443024 scopus 로고    scopus 로고
    • Dna z and the control of dna damage induced mutagenesis in eukaryotes
    • Lawrence CW, Hinkle DC. DNA Z and the control of DNA damage induced mutagenesis in eukaryotes. Cancer Surv 1996; 28:21-31.
    • (1996) Cancer Surv , vol.28 , pp. 21-31
    • Lawrence, C.W.1    Hinkle, D.C.2
  • 131
    • 0001427251 scopus 로고    scopus 로고
    • Dna damage-induced mutagenesis: A novel target for cancer prevention
    • Wang Z. DNA damage-induced mutagenesis: a novel target for cancer prevention. Mol Interv 2001; 1:269-281.
    • (2001) Mol Interv , vol.1 , pp. 269-281
    • Wang, Z.1
  • 132
    • 0029872907 scopus 로고    scopus 로고
    • Somatic hypermutation of immunoglobulin genes
    • Wagner SD, Neuberger MS. Somatic hypermutation of immunoglobulin genes. Annu Rev Immunol 1996; 14:441-457.
    • (1996) Annu Rev Immunol , vol.14 , pp. 441-457
    • Wagner, S.D.1    Neuberger, M.S.2
  • 133
    • 0037388165 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded dna but requires the action of rnase
    • Bransteitter R, Pham P, Scharff MD, Goodman MF. Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. Proc Natl Acad Sci USA 2003; 100:4102-4107.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4102-4107
    • Bransteitter, R.1    Pham, P.2    Scharff, M.D.3    Goodman, M.F.4
  • 134
    • 0037926476 scopus 로고    scopus 로고
    • Processive aid-catalysed cytosine deamination on single-stranded dna simulates somatic hypermutation
    • Pham P, Bransteitter R, Petruska J, Goodman MF. Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutation. Nature 2003; 424:103-107.
    • (2003) Nature , vol.424 , pp. 103-107
    • Pham, P.1    Bransteitter, R.2    Petruska, J.3    Goodman, M.F.4
  • 136
    • 0035399804 scopus 로고    scopus 로고
    • Decreased frequency of somatic hypermutation and impaired affinity maturation but intact germinal center formation in mice expressing antisense rna to dna polymerase z
    • Diaz M, Verkoczy LK, Flajnik MF, Klinman NR. Decreased frequency of somatic hypermutation and impaired affinity maturation but intact germinal center formation in mice expressing antisense RNA to DNA polymerase Z. J Immunol 2001; 167:327-335.
    • (2001) J Immunol , vol.167 , pp. 327-335
    • Diaz, M.1    Verkoczy, L.K.2    Flajnik, M.F.3    Klinman, N.R.4
  • 137
    • 0037388452 scopus 로고    scopus 로고
    • Rev1 is essential for dna damage tolerance and non-templated immunoglobulin gene mutation in a vertebrate cell line
    • Simpson LJ, Sale JE. Rev1 is essential for DNA damage tolerance and non-templated immunoglobulin gene mutation in a vertebrate cell line. EMBO J 2003; 22:1654-1664.
    • (2003) EMBO J , vol.22 , pp. 1654-1664
    • Simpson, L.J.1    Sale, J.E.2
  • 138
    • 0037206851 scopus 로고    scopus 로고
    • Induction of somatic hypermutation in immunoglubulin genes is dependent on dna polymerase;
    • Faili A, Aoufouchi S, Flatter E, Gueranger Q, Reynaud CA, Weill JC. Induction of somatic hypermutation in immunoglubulin genes is dependent on DNA polymerase;. Nature 2002; 419:944-947.
    • (2002) Nature , vol.419 , pp. 944-947
    • Faili, A.1    Aoufouchi, S.2    Flatter, E.3    Gueranger, Q.4    Reynaud, C.A.5    Weill, J.C.6
  • 139
    • 0035377269 scopus 로고    scopus 로고
    • Dna polymerase z is an a-t mutator in somatic hypermutation of immunoglubulin variable genes
    • Zeng X, Winter DB, Kasmer C, Kraemer KH, Lehmann AR, Gearhart PJ. DNA polymerase z is an A-T mutator in somatic hypermutation of immunoglubulin variable genes. Nat Immunol 2001; 2:537-541.
    • (2001) Nat Immunol , vol.2 , pp. 537-541
    • Zeng, X.1    Winter, D.B.2    Kasmer, C.3    Kraemer, K.H.4    Lehmann, A.R.5    Gearhart, P.J.6
  • 141
    • 0037162552 scopus 로고    scopus 로고
    • Correlation of somatic hypermutation specificity and a-t base pair substitution errors by dna polymerase z during copying of a mouse immunoglobulin k light chain transgene
    • Pavlov YI, Rogozin IB, Galkin AP, Aksenova AY, Hanaoka F, Rada C, Kunkel TA. Correlation of somatic hypermutation specificity and A-T base pair substitution errors by DNA polymerase z during copying of a mouse immunoglobulin k light chain transgene. Proc Natl Acad Sci USA 2002; 99:9954-9959.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9954-9959
    • Pavlov, Y.I.1    Rogozin, I.B.2    Galkin, A.P.3    Aksenova, A.Y.4    Hanaoka, F.5    Rada, C.6    Kunkel, T.A.7
  • 142
    • 0042422042 scopus 로고    scopus 로고
    • Gearhart pj. 129-derived strains of mice are deficient in dna polymerase; and have normal immunoglubulin hypermutation
    • McDonald JP, Frank EG, Plosky BS, Rogozin IB, Masutani C, Hanaoka F, Woodgate R, Gearhart PJ. 129-derived strains of mice are deficient in DNA polymerase; and have normal immunoglubulin hypermutation. J Exp Med 2003; 198:635-643.
    • (2003) J Exp Med , vol.198 , pp. 635-643
    • McDonald, J.P.1    Frank, E.G.2    Plosky, B.S.3    Rogozin, I.B.4    Masutani, C.5    Hanaoka, F.6    Woodgate, R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.