메뉴 건너뛰기




Volumn 290, Issue 2, 2015, Pages 775-787

Error-prone translesion synthesis past DNA-peptide cross-links conjugated to the major groove of DNA via C5 of thymidine

Author keywords

[No Author keywords available]

Indexed keywords

IONIZING RADIATION; OXYGEN; PEPTIDES; POLYMERS; PROTEINS; REPAIR;

EID: 84920973951     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.613638     Document Type: Article
Times cited : (31)

References (74)
  • 1
    • 15944429355 scopus 로고    scopus 로고
    • DNA-protein cross-links: Their induction, repair, and biological consequences
    • Barker, S., Weinfeld, M., and Murray, D. (2005) DNA-protein cross-links: their induction, repair, and biological consequences. Mutat. Res. 589, 111-135
    • (2005) Mutat. Res. , vol.589 , pp. 111-135
    • Barker, S.1    Weinfeld, M.2    Murray, D.3
  • 2
    • 23944471409 scopus 로고    scopus 로고
    • A method for the isolation of covalent DNA-protein cross-links suitable for proteomics analysis
    • Barker, S., Murray, D., Zheng, J., Li, L., and Weinfeld, M. (2005) A method for the isolation of covalent DNA-protein cross-links suitable for proteomics analysis. Anal. Biochem. 344, 204-215
    • (2005) Anal. Biochem. , vol.344 , pp. 204-215
    • Barker, S.1    Murray, D.2    Zheng, J.3    Li, L.4    Weinfeld, M.5
  • 6
    • 84877110276 scopus 로고    scopus 로고
    • 1,2,3,4-Diepoxybutane-induced DNA-protein crosslinking in human fibrosarcoma (HT1080) cells
    • Gherezghiher, T. B., Ming, X., Villalta, P. W., Campbell, C., and Tretyakova, N. Y. (2013) 1,2,3,4-Diepoxybutane-induced DNA-protein crosslinking in human fibrosarcoma (HT1080) cells. J. Proteome Res. 12, 2151-2164
    • (2013) J. Proteome Res. , vol.12 , pp. 2151-2164
    • Gherezghiher, T.B.1    Ming, X.2    Villalta, P.W.3    Campbell, C.4    Tretyakova, N.Y.5
  • 8
    • 84866952680 scopus 로고    scopus 로고
    • Genotoxic consequences of endogenous aldehydes on mouse haematopoietic stem cell function
    • Garaycoechea, J. I., Crossan, G. P., Langevin, F., Daly, M., Arends, M. J., and Patel, K. J. (2012) Genotoxic consequences of endogenous aldehydes on mouse haematopoietic stem cell function. Nature 489, 571-575
    • (2012) Nature , vol.489 , pp. 571-575
    • Garaycoechea, J.I.1    Crossan, G.P.2    Langevin, F.3    Daly, M.4    Arends, M.J.5    Patel, K.J.6
  • 9
    • 79960037006 scopus 로고    scopus 로고
    • Fancd2 counteracts the toxic effects of naturally produced aldehydes in mice
    • Langevin, F., Crossan, G. P., Rosado, I. V., Arends, M. J., and Patel, K. J. (2011) Fancd2 counteracts the toxic effects of naturally produced aldehydes in mice. Nature 475, 53-58
    • (2011) Nature , vol.475 , pp. 53-58
    • Langevin, F.1    Crossan, G.P.2    Rosado, I.V.3    Arends, M.J.4    Patel, K.J.5
  • 10
    • 34548598331 scopus 로고    scopus 로고
    • 5-Azacytidine-induced methyltransferase-DNA adducts block DNA replication in vivo
    • Kuo, H. K., Griffith, J. D., and Kreuzer, K. N. (2007) 5-Azacytidine-induced methyltransferase-DNA adducts block DNA replication in vivo. Cancer Res. 67, 8248-8254
    • (2007) Cancer Res. , vol.67 , pp. 8248-8254
    • Kuo, H.K.1    Griffith, J.D.2    Kreuzer, K.N.3
  • 11
    • 0033200360 scopus 로고    scopus 로고
    • A plethora of lesion-replicating DNA polymerases
    • Woodgate, R. (1999) A plethora of lesion-replicating DNA polymerases. Genes Dev. 13, 2191-2195
    • (1999) Genes Dev. , vol.13 , pp. 2191-2195
    • Woodgate, R.1
  • 12
    • 19444383801 scopus 로고    scopus 로고
    • Trading places: How doDNApolymerases switch during translesionDNAsyn
    • thesis?
    • Friedberg, E. C., Lehmann, A. R., and Fuchs, R. P. (2005) Trading places: how doDNApolymerases switch during translesionDNAsynthesis? Mol. Cell 18, 499-505
    • (2005) Mol. Cell , vol.18 , pp. 499-505
    • Friedberg, E.C.1    Lehmann, A.R.2    Fuchs, R.P.3
  • 17
    • 0042357095 scopus 로고    scopus 로고
    • POLN, a nuclear PolA family DNA polymerase homologous to the DNA cross-link sensitivity protein Mus308
    • Marini, F., Kim, N., Schuffert, A., and Wood, R. D. (2003) POLN, a nuclear PolA family DNA polymerase homologous to the DNA cross-link sensitivity protein Mus308. J. Biol. Chem. 278, 32014-32019
    • (2003) J. Biol. Chem. , vol.278 , pp. 32014-32019
    • Marini, F.1    Kim, N.2    Schuffert, A.3    Wood, R.D.4
  • 18
    • 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., and Kaufmann, W. K. (1997) Replication fork bypass of a pyrimidine dimer blocking leading strand DNA synthesis. J. Biol. Chem. 272, 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
  • 20
    • 0034720285 scopus 로고    scopus 로고
    • Low fidelity DNA synthesis by human DNA polymerase η
    • Matsuda, T., Bebenek, K., Masutani, C., Hanaoka, F., and Kunkel, T. A. (2000) Low fidelity DNA synthesis by human DNA polymerase η. Nature 404, 1011-1013
    • (2000) Nature , vol.404 , pp. 1011-1013
    • Matsuda, T.1    Bebenek, K.2    Masutani, C.3    Hanaoka, F.4    Kunkel, T.A.5
  • 21
    • 0344237408 scopus 로고    scopus 로고
    • 2]. A concept for activation of the trans geometry in platinum antitumor complex
    • Novakova, O., Kasparkova, J., Malina, J., Natile, G., and Brabec, V. (2003) DNA-protein cross-linking by trans-[PtCl2(E-iminoether)2]. A concept for activation of the trans geometry in platinum antitumor complex. Nucleic Acids Res. 31, 6450-6460
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6450-6460
    • Novakova, O.1    Kasparkova, J.2    Malina, J.3    Natile, G.4    Brabec, V.5
  • 22
    • 0028278039 scopus 로고
    • Aldehyde-induced protein-DNA crosslinks disrupt specific stages of SV40 DNA replication
    • Permana, P. A., and Snapka, R. M. (1994) Aldehyde-induced protein-DNA crosslinks disrupt specific stages of SV40 DNA replication. Carcinigenesis 15, 1031-1036
    • (1994) Carcinigenesis , vol.15 , pp. 1031-1036
    • Permana, P.A.1    Snapka, R.M.2
  • 23
    • 84916942962 scopus 로고    scopus 로고
    • Repair of a DNA-protein crosslink by replication-coupled proteolysis
    • Duxin, J. P., Dewar, J. M., Yardimci, H., and Walter, J. C. (2014) Repair of a DNA-protein crosslink by replication-coupled proteolysis. Cell 159, 346-357
    • (2014) Cell , vol.159 , pp. 346-357
    • Duxin, J.P.1    Dewar, J.M.2    Yardimci, H.3    Walter, J.C.4
  • 25
    • 79960420861 scopus 로고    scopus 로고
    • Role of high-fidelity Escherichia coli DNA polymerase i in replication bypass of a deoxyadenosine DNA-peptide cross-link
    • Yamanaka, K., Minko, I. G., Finkel, S. E., Goodman, M. F., and Lloyd, R. S. (2011) Role of high-fidelity Escherichia coli DNA polymerase I in replication bypass of a deoxyadenosine DNA-peptide cross-link. J. Bacteriol. 193, 3815-3821
    • (2011) J. Bacteriol. , vol.193 , pp. 3815-3821
    • Yamanaka, K.1    Minko, I.G.2    Finkel, S.E.3    Goodman, M.F.4    Lloyd, R.S.5
  • 27
  • 28
    • 34247614959 scopus 로고    scopus 로고
    • Mechanism of the formation of DNA-protein cross-links by antitumor cisplatin
    • Chválová, K., Brabec, V., and Kaspárková, J. (2007) Mechanism of the formation of DNA-protein cross-links by antitumor cisplatin. Nucleic Acids Res. 35, 1812-1821
    • (2007) Nucleic Acids Res. , vol.35 , pp. 1812-1821
    • Chválová, K.1    Brabec, V.2    Kaspárková, J.3
  • 29
    • 84879179094 scopus 로고    scopus 로고
    • 6-deoxyadenosinyl)-2,3-dihydroxybutyl] glutathione by DNA polymerases
    • Cho, S. H., and Guengerich, F. P. (2013) Replication past the butadiene diepoxide-derived DNA adduct S-[4-(N6-deoxyadenosinyl)-2,3-dihydroxybutyl] glutathione by DNA polymerases. Chem. Res. Toxicol. 26, 1005-1013
    • (2013) Chem. Res. Toxicol. , vol.26 , pp. 1005-1013
    • Cho, S.H.1    Guengerich, F.P.2
  • 30
    • 0026523796 scopus 로고
    • Mechanism of human methyl-directed DNA methyltransferase and the fidelity of cytosine methylation
    • Smith, S. S., Kaplan, B. E., Sowers, L. C., and Newman, E. M. (1992) Mechanism of human methyl-directed DNA methyltransferase and the fidelity of cytosine methylation. Proc. Natl. Acad. Sci. U.S.A. 89, 4744-4748
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4744-4748
    • Smith, S.S.1    Kaplan, B.E.2    Sowers, L.C.3    Newman, E.M.4
  • 31
    • 15744401773 scopus 로고    scopus 로고
    • Eukaryotic cytosine methyltransferases
    • Goll, M. G., and Bestor, T. H. (2005) Eukaryotic cytosine methyltransferases. Annu. Rev. Biochem. 74, 481-514
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 481-514
    • Goll, M.G.1    Bestor, T.H.2
  • 32
    • 84858133452 scopus 로고    scopus 로고
    • Mechanisms of free radical-induced damage to DNA
    • Dizdaroglu, M., and Jaruga, P. (2012) Mechanisms of free radical-induced damage to DNA. Free Radic. Res. 46, 382-419
    • (2012) Free Radic. Res. , vol.46 , pp. 382-419
    • Dizdaroglu, M.1    Jaruga, P.2
  • 33
    • 0036801404 scopus 로고    scopus 로고
    • Oxidative DNA adducts and DNA-protein cross-links are the major DNA lesions induced by arsenite
    • Bau, D. T., Wang, T. S., Chung, C. H., Wang, A. S., Wang, A. S., and Jan, K. Y. (2002) Oxidative DNA adducts and DNA-protein cross-links are the major DNA lesions induced by arsenite. Environ. Health Perspect. 110, 753-756
    • (2002) Environ. Health Perspect. , vol.110 , pp. 753-756
    • Bau, D.T.1    Wang, T.S.2    Chung, C.H.3    Wang, A.S.4    Wang, A.S.5    Jan, K.Y.6
  • 34
    • 0032492727 scopus 로고    scopus 로고
    • Hydroxyl radical-induced cross-linking of thymine and lysine: Identification of the primary structure and mechanism
    • Morimoto, S., Hatta, H., Fujita, S., Matsuyama, T., Ueno, T., and Nishimoto, S. (1998) Hydroxyl radical-induced cross-linking of thymine and lysine: identification of the primary structure and mechanism. Bioorg. Med. Chem. Lett. 8, 865-870
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 865-870
    • Morimoto, S.1    Hatta, H.2    Fujita, S.3    Matsuyama, T.4    Ueno, T.5    Nishimoto, S.6
  • 35
    • 0024399817 scopus 로고
    • Structure and mechanism of hydroxyl radical-induced formation of a DNA-protein cross-link involving thymine and lysine in nucleohistone
    • Dizdaroglu, M., and Gajewski, E. (1989) Structure and mechanism of hydroxyl radical-induced formation of a DNA-protein cross-link involving thymine and lysine in nucleohistone. Cancer Res. 49, 3463-3467
    • (1989) Cancer Res. , vol.49 , pp. 3463-3467
    • Dizdaroglu, M.1    Gajewski, E.2
  • 36
    • 0032839258 scopus 로고    scopus 로고
    • A covalent thymine-tyrosine adduct involved in DNA-protein cross-links: Synthesis, characterization and quantification
    • Charlton, T. S., Ingelse, B. A., Black, D. S., Craig, D. C., Mason, K. E., and Duncan, M. W. (1999) A covalent thymine-tyrosine adduct involved in DNA-protein cross-links: synthesis, characterization and quantification. Free Radic. Biol Med. 27, 254-261
    • (1999) Free Radic. Biol Med. , vol.27 , pp. 254-261
    • Charlton, T.S.1    Ingelse, B.A.2    Black, D.S.3    Craig, D.C.4    Mason, K.E.5    Duncan, M.W.6
  • 38
    • 0037458649 scopus 로고    scopus 로고
    • 2-Deoxyguanosine adducts of acrolein, crotonaldehyde, and trans-4-hydroxynonenal cross-link to peptides via Schiff base linkage
    • Kurtz, A. J., and Lloyd, R. S. (2003) 1,N2-Deoxyguanosine adducts of acrolein, crotonaldehyde, and trans-4-hydroxynonenal cross-link to peptides via Schiff base linkage. J. Biol. Chem. 278, 5970-5976
    • (2003) J. Biol. Chem. , vol.278 , pp. 5970-5976
    • Kurtz, A.J.1    Lloyd, R.S.2
  • 39
    • 23944449018 scopus 로고    scopus 로고
    • 2-guanine DNA lesions by human DNA polymerase η
    • Choi, J. Y., and Guengerich, F. P. (2005) Adduct size limits efficient and error-free bypass across bulky N2-guanine DNA lesions by human DNA polymerase η. J. Mol. Biol. 352, 72-90
    • (2005) J. Mol. Biol. , vol.352 , pp. 72-90
    • Choi, J.Y.1    Guengerich, F.P.2
  • 41
    • 84858642631 scopus 로고    scopus 로고
    • 2-deoxyguanosine interstrand cross-links by human DNA polymerases η and ι
    • Klug, A. R., Harbut, M. B., Lloyd, R. S., and Minko, I. G. (2012) Replication bypass of N2-deoxyguanosine interstrand cross-links by human DNA polymerases η and ι. Chem. Res. Toxicol. 25, 755-762
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 755-762
    • Klug, A.R.1    Harbut, M.B.2    Lloyd, R.S.3    Minko, I.G.4
  • 42
    • 0344154365 scopus 로고    scopus 로고
    • Miscoding properties of 1,N6-ethanoadenine, a DNA adduct derived from reaction with the antitumor agent 1,3-bis(2-chloroethyl)-1-nitrosourea
    • Hang, B., Chenna, A., Guliaev, A. B., and Singer, B. (2003) Miscoding properties of 1,N6-ethanoadenine, a DNA adduct derived from reaction with the antitumor agent 1,3-bis(2-chloroethyl)-1-nitrosourea. Mutat. Res. 531, 191-203
    • (2003) Mutat. Res. , vol.531 , pp. 191-203
    • Hang, B.1    Chenna, A.2    Guliaev, A.B.3    Singer, B.4
  • 44
  • 45
    • 67449103244 scopus 로고    scopus 로고
    • Replication past the N5-methyl-formamidopyrimidine lesion of deoxyguanosine by DNA polymerases and an improved procedure for sequence analysis of in vitro bypass products by mass spectrometry
    • Christov, P. P., Angel, K. C., Guengerich, F. P., and Rizzo, C. J. (2009) Replication past the N5-methyl-formamidopyrimidine lesion of deoxyguanosine by DNA polymerases and an improved procedure for sequence analysis of in vitro bypass products by mass spectrometry. Chem. Res. Toxicol. 22, 1086-1095
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 1086-1095
    • Christov, P.P.1    Angel, K.C.2    Guengerich, F.P.3    Rizzo, C.J.4
  • 47
    • 33845270444 scopus 로고    scopus 로고
    • 2-deoxyguanosine adducts of the dietary mutagen 2-amino-3-methylimidazo[4,5-f]quinoline in the NarI recognition sequence by prokaryotic DNA polymerases
    • Stover, J. S., Chowdhury, G., Zang, H., Guengerich, F. P., and Rizzo, C. J. (2006) Translesion synthesis past the C8- and N2-deoxyguanosine adducts of the dietary mutagen 2-amino-3-methylimidazo[4,5-f]quinoline in the NarI recognition sequence by prokaryotic DNA polymerases. Chem. Res. Toxicol. 19, 1506-1517
    • (2006) Chem. Res. Toxicol. , vol.19 , pp. 1506-1517
    • Stover, J.S.1    Chowdhury, G.2    Zang, H.3    Guengerich, F.P.4    Rizzo, C.J.5
  • 48
    • 0035902484 scopus 로고    scopus 로고
    • Mechanism of DNA polymerase II-mediated frameshift mutagenesis
    • Becherel, O. J., and Fuchs, R. P. (2001) Mechanism of DNA polymerase II-mediated frameshift mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 98, 8566-8571
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8566-8571
    • Becherel, O.J.1    Fuchs, R.P.2
  • 50
    • 0031038053 scopus 로고    scopus 로고
    • Abasic translesion synthesis by DNA polymerase β violates the "a-rule". Novel types of nucleotide incorporation by human DNA polymerase β at an abasic lesion in different sequence contexts
    • Efrati, E., Tocco, G., Eritja, R., Wilson, S. H., and Goodman, M. F. (1997) Abasic translesion synthesis by DNA polymerase β violates the "A-rule". Novel types of nucleotide incorporation by human DNA polymerase β at an abasic lesion in different sequence contexts. J. Biol. Chem. 272, 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
  • 51
    • 0027171266 scopus 로고
    • Oxidants, antioxidants, and the degenerative diseases of aging
    • Ames, B. N., Shigenaga, M. K., and Hagen, T. M. (1993) Oxidants, antioxidants, and the degenerative diseases of aging. Proc. Natl. Acad. Sci. U.S.A. 90, 7915-7922
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7915-7922
    • Ames, B.N.1    Shigenaga, M.K.2    Hagen, T.M.3
  • 52
    • 43249118458 scopus 로고    scopus 로고
    • DNA damage and repair: Relevance to mechanisms of neurodegeneration
    • Martin, L. J. (2008) DNA damage and repair: relevance to mechanisms of neurodegeneration. J. Neuropathol. Exp. Neurol. 67, 377-387
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 377-387
    • Martin, L.J.1
  • 53
    • 0033519450 scopus 로고    scopus 로고
    • Assessment of DNA-protein cross-links in the course of aging in two mouse strains by use of a modified alkaline filter elution applied to whole tissue samples
    • Zahn, R. K., Zahn-Daimler, G., Ax, S., Hosokawa, M., and Takeda, T. (1999) Assessment of DNA-protein cross-links in the course of aging in two mouse strains by use of a modified alkaline filter elution applied to whole tissue samples. Mech. Ageing Dev. 108, 99-112
    • (1999) Mech. Ageing Dev. , vol.108 , pp. 99-112
    • Zahn, R.K.1    Zahn-Daimler, G.2    Ax, S.3    Hosokawa, M.4    Takeda, T.5
  • 54
    • 67649678412 scopus 로고    scopus 로고
    • Oxidative stress in diabetes and Alzheimer's disease
    • Reddy, V. P., Zhu, X., Perry, G., and Smith, M. A. (2009) Oxidative stress in diabetes and Alzheimer's disease. J. Alzheimers. Dis. 16, 763-774
    • (2009) J. Alzheimers. Dis. , vol.16 , pp. 763-774
    • Reddy, V.P.1    Zhu, X.2    Perry, G.3    Smith, M.A.4
  • 56
    • 38049010515 scopus 로고    scopus 로고
    • Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer's disease
    • Lovell, M. A., and Markesbery, W. R. (2007) Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer's disease. Nucleic Acids Res. 35, 7497-7504
    • (2007) Nucleic Acids Res. , vol.35 , pp. 7497-7504
    • Lovell, M.A.1    Markesbery, W.R.2
  • 57
    • 0037133210 scopus 로고    scopus 로고
    • Incision of DNA-protein cross-links by UvrABC nuclease suggests a potential repair pathway involving nucleotide excision repair
    • Minko, I. G., Zou, Y., and Lloyd, R. S. (2002) Incision of DNA-protein cross-links by UvrABC nuclease suggests a potential repair pathway involving nucleotide excision repair. Proc. Natl. Acad. Sci. U.S.A. 99, 1905-1909
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1905-1909
    • Minko, I.G.1    Zou, Y.2    Lloyd, R.S.3
  • 58
    • 34547945474 scopus 로고    scopus 로고
    • Nucleotide excision repair eliminates unique DNA-protein cross-links from mammalian cells
    • Baker, D. J., Wuenschell, G., Xia, L., Termini, J., Bates, S. E., Riggs, A. D., and O'Connor, T. R. (2007) Nucleotide excision repair eliminates unique DNA-protein cross-links from mammalian cells. J. Biol. Chem. 282, 22592-22604
    • (2007) J. Biol. Chem. , vol.282 , pp. 22592-22604
    • Baker, D.J.1    Wuenschell, G.2    Xia, L.3    Termini, J.4    Bates, S.E.5    Riggs, A.D.6    O'connor, T.R.7
  • 59
    • 33746606573 scopus 로고    scopus 로고
    • Repair of DNA-protein cross-links in mammalian cells
    • Reardon, J. T., Cheng, Y., and Sancar, A. (2006) Repair of DNA-protein cross-links in mammalian cells. Cell Cycle 5, 1366-1370
    • (2006) Cell Cycle , vol.5 , pp. 1366-1370
    • Reardon, J.T.1    Cheng, Y.2    Sancar, A.3
  • 60
    • 33645210785 scopus 로고    scopus 로고
    • Repair of DNA-polypeptide crosslinks by human excision nuclease
    • Reardon, J. T., and Sancar, A. (2006) Repair of DNA-polypeptide crosslinks by human excision nuclease. Proc. Natl. Acad. Sci. U.S.A. 103, 4056-4061
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 4056-4061
    • Reardon, J.T.1    Sancar, A.2
  • 62
    • 0033852536 scopus 로고    scopus 로고
    • Loss of DNA-protein cross-links from formaldehyde-exposed cells occurs through spontaneous hydrolysis and an active repair process linked to proteosome function
    • Quievryn, G., and Zhitkovich, A. (2000) Loss of DNA-protein cross-links from formaldehyde-exposed cells occurs through spontaneous hydrolysis and an active repair process linked to proteosome function. Carcinogenesis 21, 1573-1580
    • (2000) Carcinogenesis , vol.21 , pp. 1573-1580
    • Quievryn, G.1    Zhitkovich, A.2
  • 63
    • 77954820678 scopus 로고    scopus 로고
    • 2γhydroxypropanodeoxyguanosine lesion with a trimethylene linkage
    • Huang, H., Kozekov, I. D., Kozekova, A., Rizzo, C. J., McCullough, A. K., Lloyd, R. S., and Stone, M. P. (2010) Minor groove orientation of the KWKK peptide tethered via the N-terminal amine to the acrolein-derived 1,N2-γ-hydroxypropanodeoxyguanosine lesion with a trimethylene linkage. Biochemistry 49, 6155-6164
    • (2010) Biochemistry , vol.49 , pp. 6155-6164
    • Huang, H.1    Kozekov, I.D.2    Kozekova, A.3    Rizzo, C.J.4    McCullough, A.K.5    Lloyd, R.S.6    Stone, M.P.7
  • 64
    • 84859171807 scopus 로고    scopus 로고
    • MYC on the path to cancer
    • Dang, C. V. (2012) MYC on the path to cancer. Cell 149, 22-35
    • (2012) Cell , vol.149 , pp. 22-35
    • Dang, C.V.1
  • 65
    • 84893233590 scopus 로고    scopus 로고
    • Genome recognition by MYC
    • 4, 2014 Feb
    • Sabo, A., and Amati, B. (2014) Genome recognition by MYC. Cold Spring Harb. Perspect. Med. 4, 2014 Feb 1;4(2). pii: a014191
    • (2014) Cold Spring Harb. Perspect. Med , vol.1-4 , Issue.2
    • Sabo, A.1    Amati, B.2
  • 68
    • 38049125552 scopus 로고    scopus 로고
    • The fidelity of DNA synthesis by eukaryotic replicative and translesion synthesis polymerases
    • McCulloch, S. D., and Kunkel, T. A. (2008) The fidelity of DNA synthesis by eukaryotic replicative and translesion synthesis polymerases. Cell Res. 18, 148-161
    • (2008) Cell Res. , vol.18 , pp. 148-161
    • McCulloch, S.D.1    Kunkel, T.A.2
  • 69
    • 0034327552 scopus 로고    scopus 로고
    • Human DNA polymerase κ synthesizes DNA with extraordinarily low fidelity
    • Zhang, Y., Yuan, F., Xin, H., Wu, X., Rajpal, D. K., Yang, D., and Wang, Z. (2000) Human DNA polymerase κ synthesizes DNA with extraordinarily low fidelity. Nucleic Acids Res. 28, 4147-4156
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4147-4156
    • Zhang, Y.1    Yuan, F.2    Xin, H.3    Wu, X.4    Rajpal, D.K.5    Yang, D.6    Wang, Z.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.