메뉴 건너뛰기




Volumn 34, Issue 11, 2006, Pages 3326-3337

Mutagenic nucleotide incorporation and hindered translocation by a food carcinogen C8-dG adduct in Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): Modeling and dynamics studies

Author keywords

[No Author keywords available]

Indexed keywords

2'-DEOXYADENOSINE TRIPHOSPHATE; 2'-DEOXYCYTIDINE 5'-TRIPHOSPHATE; CARCINOGEN; DEOXYADENOSINE PHOSPHATE; DEOXYADENOSINE TRIPHOSPHATE; DEOXYCYTIDINE PHOSPHATE; DEOXYCYTIDINE TRIPHOSPHATE; DEOXYGUANOSINE; DEOXYGUANOSINE PHOSPHATE; DEOXYGUANOSINE TRIPHOSPHATE; DEOXYRIBONUCLEOTIDE; DNA; DNA DIRECTED DNA POLYMERASE BETA; DRUG DERIVATIVE; IMIDAZOLE DERIVATIVE; N (DEOXYGUANOSIN 8 YL) 2 AMINO 1 METHYL 6 PHENYLIMIDAZO(4,5 B)PYRIDINE; N-(DEOXYGUANOSIN-8-YL)-2-AMINO-1-METHYL-6-PHENYLIMIDAZO(4,5-B)PYRIDINE; PYRIMIDINE NUCLEOTIDE; THYMIDINE 5'-TRIPHOSPHATE; THYMIDINE TRIPHOSPHATE;

EID: 33746269679     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkl425     Document Type: Article
Times cited : (19)

References (73)
  • 3
    • 14544287434 scopus 로고    scopus 로고
    • Replication of damaged DNA by translesion synthesis in human cells
    • Lehmann,A.R. (2005) Replication of damaged DNA by translesion synthesis in human cells. FEBS Lett., 579, 873-876.
    • (2005) FEBS Lett. , vol.579 , pp. 873-876
    • Lehmann, A.R.1
  • 4
    • 21244506437 scopus 로고    scopus 로고
    • Eukaryotic translesion synthesis DNA polymerases: Specificity of structure and function
    • DOI 10.1146/annurev.biochem.74.082803.133250
    • Prakash,S., Johnson,R.E. and Prakash,L. (2005) Eukaryotic translesion synthesis DNA polymerases: specificity of structure and function. Annu. Rev. Biochem., 74, 317-353. (Pubitemid 40995510)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 317-353
    • Prakash, S.1    Johnson, R.E.2    Prakash, L.3
  • 5
    • 0000918686 scopus 로고    scopus 로고
    • The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis
    • DOI 10.1016/S1097-2765(00)80376-7
    • Wagner,J., Gruz,P., Kim,S.R., Yamada,M., Matsui,K., Fuchs,R.P. and Nohmi,T. (1999) The dinB gene encodes a novel E.coli DNA polymerase, DNA pol IV, involved in mutagenesis. Mol. Cell, 4, 281-286. (Pubitemid 29456897)
    • (1999) Molecular Cell , vol.4 , Issue.2 , pp. 281-286
    • Wagner, J.1    Gruz, P.2    Kim, S.-R.3    Yamada, M.4    Matsui, K.5    Fuchs, R.P.P.6    Nohmi, T.7
  • 6
    • 0032703301 scopus 로고    scopus 로고
    • Replication of damaged DNA: Molecular defect in Xeroderma pigmentosum variant cells
    • DOI 10.1016/S0921-8777(99)00047-6, PII S0921877799000476
    • Cordonnier,A.M. and Fuchs,R.P. (1999) Replication of damaged DNA: molecular defect in Xeroderma pigmentosum variant cells. Mutat. Res., 435, 111-119. (Pubitemid 29518299)
    • (1999) Mutation Research - DNA Repair , vol.435 , Issue.2 , pp. 111-119
    • Cordonnier, A.M.1    Fuchs, R.P.P.2
  • 7
    • 0037115955 scopus 로고    scopus 로고
    • How DNA lesions are turned into mutations within cells?
    • DOI 10.1038/sj.onc.1206006
    • Pagès,V. and Fuchs,R.P. (2002) How DNA lesions are turned into mutations within cells? Oncogene, 21, 8957-8966. (Pubitemid 36110825)
    • (2002) Oncogene , vol.21 , Issue.58 REV. ISS. 8 , pp. 8957-8966
    • Pages, V.1    Fuchs, R.P.P.2
  • 9
    • 0034669125 scopus 로고    scopus 로고
    • All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V) are involved in induced mutagenesis
    • Napolitano,R., Janel-Bintz,R., Wagner,J. and Fuchs,R.P. (2000) All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V) are involved in induced mutagenesis. EMBO J., 19, 6259-6265.
    • (2000) EMBO J. , vol.19 , pp. 6259-6265
    • Napolitano, R.1    Janel-Bintz, R.2    Wagner, J.3    Fuchs, R.P.4
  • 11
    • 19444383801 scopus 로고    scopus 로고
    • Trading Places: How do DNA polymerases switch during translesion DNA synthesis?
    • DOI 10.1016/j.molcel.2005.03.032, PII S1097276505012761
    • Friedberg,E.C., Lehmann,A.R. and Fuchs,R.P. (2005) Trading places: how do DNA polymerases switch during translesion DNA synthesis? Mol. Cell, 18, 499-505. (Pubitemid 40726227)
    • (2005) Molecular Cell , vol.18 , Issue.5 , pp. 499-505
    • Friedberg, E.C.1    Lehmann, A.R.2    Fuchs, R.P.P.3
  • 12
    • 0035890599 scopus 로고    scopus 로고
    • Sulfolobus solfataricus P2 DNA polymerase IV (Dp04): An archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic poleta
    • Boudsocq,F., Iwai,S., Hanaoka,F. and Woodgate,R. (2001) Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): an archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic polη. Nucleic Acids Res., 29, 4607-4616. (Pubitemid 33095021)
    • (2001) Nucleic Acids Research , vol.29 , Issue.22 , pp. 4607-4616
    • Boudsocq, F.1    Iwai, S.2    Hanaoka, F.3    Woodgate, R.4
  • 14
    • 1642382214 scopus 로고    scopus 로고
    • Snapshots of replication through an abasic lesion: Structural basis for base substitutions and frameshifts
    • DOI 10.1016/S1097-2765(04)00101-7, PII S1097276504001017
    • Ling,H., Boudsocq,F., Woodgate,R. and Yang,W. (2004) Snapshots of replication through an abasic lesion; structural basis for base substitutions and frameshifts. Mol. Cell, 13, 751-762. (Pubitemid 38368130)
    • (2004) Molecular Cell , vol.13 , Issue.5 , pp. 751-762
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 15
    • 0035812849 scopus 로고    scopus 로고
    • Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication
    • DOI 10.1016/S0092-8674(01)00515-3
    • Ling,H., Boudsocq,F., Woodgate,R. and Yang,W. (2001) Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication. Cell, 107, 91-102. (Pubitemid 32972040)
    • (2001) Cell , vol.107 , Issue.1 , pp. 91-102
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 17
    • 0041864009 scopus 로고    scopus 로고
    • Replication of a cis-syn thymine dimer at atomic resolution
    • DOI 10.1038/nature01919
    • Ling,H., Boudsocq,F., Plosky,B.S., Woodgate,R. and Yang,W. (2003) Replication of a cis-syn thymine dimer at atomic resolution. Nature, 424, 1083-1087. (Pubitemid 37064312)
    • (2003) Nature , vol.424 , Issue.6952 , pp. 1083-1087
    • Ling, H.1    Boudsocq, F.2    Plosky, B.S.3    Woodgate, R.4    Yang, W.5
  • 18
    • 27144542782 scopus 로고    scopus 로고
    • Fidelity of Dpo4: Effect of metal ions, nucleotide selection and pyrophosphorolysis
    • DOI 10.1038/sj.emboj.7600786, PII 7600786
    • Vaisman,A., Ling,H., Woodgate,R. and Yang,W. (2005) Fidelity of Dpo4: effect of metal ions, nucleotide selection and pyrophosphorolysis. EMBO. J., 24, 2957-2967. (Pubitemid 41486333)
    • (2005) EMBO Journal , vol.24 , Issue.17 , pp. 2957-2967
    • Vaisman, A.1    Ling, H.2    Woodgate, R.3    Yang, W.4
  • 21
    • 3543028588 scopus 로고    scopus 로고
    • Investigating the role of the little finger domain of Y-family DNA polymerases in low fidelity synthesis and translesion replication
    • DOI 10.1074/jbc.M405249200
    • Boudsocq,F., Kokoska,R.J., Plosky,B.S., Vaisman,A., Ling,H., Kunkel,T.A., Yang,W. and Woodgate,R. (2004) Investigating the role of the little finger domain of Y-family DNA polymerases in low fidelity synthesis and translesion replication. J. Biol. Chem., 279, 32932-32940. (Pubitemid 39014753)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 32932-32940
    • Boudsocq, F.1    Kokoska, R.J.2    Plosky, B.B.3    Vaisman, A.4    Ling, H.5    Kunkel, T.A.6    Yang, W.7    Woodgate, R.8
  • 22
    • 33644866040 scopus 로고    scopus 로고
    • Efficient and high fidelity incorporation of dCTP opposite 7,8-dihydro-8-oxodeoxyguanosine by Sulfolobus solfataricus DNA polymerase Dpo4
    • DOI 10.1074/jbc.M510889200
    • Zang,H., Irimia,A., Choi,J.Y., Angel,K.C., Loukachevitch,L.V., Egli,M. and Guengerich,F.P. (2006) Efficient and high fidelity incorporation of dCTP opposite 7,8-dihydro-8-oxodeoxyguanosine by Sulfolobus solfataricus DNA polymerase Dpo4. J. Biol. Chem., 281, 2358-2372. (Pubitemid 43845827)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.4 , pp. 2358-2372
    • Zang, H.1    Irimia, A.2    Choi, J.-Y.3    Angel, K.C.4    Loukachevitch, L.V.5    Egli, M.6    Guengerich, F.P.7
  • 24
    • 26844566830 scopus 로고    scopus 로고
    • Structure and mechanism of DNA polymerases
    • DOI 10.1016/S0065-3233(04)71011-6, PII S0065323304710116
    • Rothwell,P.J. and Waksman,G. (2005) Structure and mechanism of DNA polymerases. Adv. Protein Chem., 71, 401-440. (Pubitemid 41446935)
    • (2005) Advances in Protein Chemistry , vol.71 , pp. 401-440
    • Rothwell, P.J.1    Waksman, G.2
  • 25
    • 0035997351 scopus 로고    scopus 로고
    • Active site tightness and substrate fit in DNA replication
    • Kool,E.T. (2002) Active site tightness and substrate fit in DNA replication. Annu. Rev. Biochem., 71, 191-219.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 191-219
    • Kool, E.T.1
  • 26
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz,T.A. (1999) DNA polymerases: structural diversity and common mechanisms. J. Biol. Chem., 274, 17395-17398.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 27
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol alpha family DNA polymerase
    • DOI 10.1016/S0092-8674(01)00367-1
    • Franklin,M.C., Wang,J. and Steitz,T.A. (2001) Structure of the replicating complex of a pol a family DNA polymerase. Cell, 105, 657-667. (Pubitemid 32524118)
    • (2001) Cell , vol.105 , Issue.5 , pp. 657-667
    • Franklin, M.C.1    Wang, J.2    Steitz, T.A.3
  • 28
    • 0034711010 scopus 로고    scopus 로고
    • Functional hydrogen-bonding map of the minor groove binding tracks of six DNA polymerases
    • Morales,J.C. and Kool,E.T. (2000) Functional hydrogen-bonding map of the minor groove binding tracks of six DNA polymerases. Biochemistry, 39, 12979-12988.
    • (2000) Biochemistry , vol.39 , pp. 12979-12988
    • Morales, J.C.1    Kool, E.T.2
  • 29
    • 2342419732 scopus 로고    scopus 로고
    • DNA replication fidelity
    • Kunkel,T.A. (2004) DNA replication fidelity. J. Biol. Chem., 279, 16895-16898.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16895-16898
    • Kunkel, T.A.1
  • 30
    • 0034762679 scopus 로고    scopus 로고
    • Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus
    • DOI 10.1038/nsb1101-984
    • Silvian,L.F., Toth,E.A., Pham,P., Goodman,M.F. and Ellenberger,T. (2001) Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus. Nature Struct. Biol., 8, 984-989. (Pubitemid 33032369)
    • (2001) Nature Structural Biology , vol.8 , Issue.11 , pp. 984-989
    • Silvian, L.F.1    Toth, E.A.2    Pham, P.3    Goodman, M.F.4    Ellenberger, T.5
  • 31
    • 0034847259 scopus 로고    scopus 로고
    • Structure of the Catalytic Core of S. cerevisiae DNA polymerase eta: Implications for translesion DNA synthesis
    • DOI 10.1016/S1097-2765(01)00306-9
    • Trincao,J., Johnson,R.E., Escalante,C.R., Prakash,S., Prakash,L. and Aggarwal,A.K. (2001) Structure of the catalytic core of S.cerevisiae DNA polymerase h: implications for translesion DNA synthesis. Mol. Cell, 8, 417-426. (Pubitemid 32831558)
    • (2001) Molecular Cell , vol.8 , Issue.2 , 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
    • 30544445218 scopus 로고    scopus 로고
    • A single amino acid governs enhanced activity of DinB DNA polymerases on damaged templates
    • DOI 10.1038/nature04318, PII NATURE04318
    • Jarosz,D.F., Godoy,V.G., Delaney,J.C., Essigmann,J.M. and Walker,G.C. (2006) A single amino acid governs enhanced activity of DinB DNA polymerases on damaged templates. Nature, 439, 225-228. (Pubitemid 43083146)
    • (2006) Nature , vol.439 , Issue.7073 , pp. 225-228
    • Jarosz, D.F.1    Godoy, V.G.2    Delaney, J.C.3    Essigmann, J.M.4    Walker, G.C.5
  • 33
    • 0035909805 scopus 로고    scopus 로고
    • Translesional synthesis past acetylaminofluorene-derived DNA adducts catalyzed by human DNA polymerase kappa and Escherichia coli DNA polymerase IV
    • DOI 10.1021/bi010702g
    • Suzuki,N., Ohashi,E., Hayashi,K., Ohmori,H., Grollman,A.P. and Shibutani,S. (2001) Translesional synthesis past acetylaminofluorene-derived DNA adducts catalyzed by human DNA polymerase κ and Escherichia coli DNA polymerase IV. Biochemistry, 40, 15176-15183. (Pubitemid 33151932)
    • (2001) Biochemistry , vol.40 , Issue.50 , pp. 15176-15183
    • Suzuki, N.1    Ohashi, E.2    Hayashi, K.3    Ohmori, H.4    Grollman, A.P.5    Shibutani, S.6
  • 34
    • 33644859916 scopus 로고    scopus 로고
    • A new anti conformation for N-(deoxyguanosin-8-yl)-2-acetylaminofluorene (AAF-dG) allows Watson-Crick pairing in the Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4)
    • DOI 10.1093/nar/gkj479
    • Wang,L. and Broyde,S. (2006) A new anti conformation for N-(deoxyguanosin-8-yl)-2-acetylaminofluorene (AAF-dG) allows Watson-Crick pairing in the Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4). Nucleic Acids Res., 34, 785-795. (Pubitemid 43380664)
    • (2006) Nucleic Acids Research , vol.34 , Issue.3 , pp. 785-795
    • Wang, L.1    Broyde, S.2
  • 36
    • 0034674913 scopus 로고    scopus 로고
    • 2-Amino-1-methyl-6-phenylimidazo[4,5-b]pyridine, a carcinogen in high-temperature-cooked meat, and breast cancer risk
    • Sinha,R., Gustafson,D.R., Kulldorff,M., Wen,W.Q., Cerhan,J.R. and Zheng,W. (2000) 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine, a carcinogen in high-temperature-cooked meat, and breast cancer risk. J. Natl. Cancer Inst., 92, 1352-1354. (Pubitemid 30660596)
    • (2000) Journal of the National Cancer Institute , vol.92 , Issue.16 , pp. 1352-1354
    • Sinha, R.1    Gustafson, D.R.2    Kulldorff, M.3    Wen, W.-Q.4    Cerhan, J.R.5    Zheng, W.6
  • 37
    • 0032543359 scopus 로고    scopus 로고
    • The role of DNA adducts in chemical carcinogenesis
    • Garner,R.C. (1998) The role of DNA adducts in chemical carcinogenesis. Mutat. Res., 402, 67-75.
    • (1998) Mutat. Res. , vol.402 , pp. 67-75
    • Garner, R.C.1
  • 39
    • 0028069430 scopus 로고
    • CYP1A2-catalyzed conversion of dietary heterocyclic amines to their proximate carcinogens is their major route of metabolism in humans
    • Boobis,A.R., Lynch,A.M., Murray,S., de la Torre,R., Solans,A., Farre,M., Segura,J., Gooderham,N.J. and Davies,D.S. (1994) CYP1A2-catalyzed conversion of dietary heterocyclic amines to their proximate carcinogens is their major route of metabolism in humans. Cancer Res., 54, 89-94. (Pubitemid 24042093)
    • (1994) Cancer Research , vol.54 , Issue.1 , pp. 89-94
    • Boobis, A.R.1    Lynch, A.M.2    Murray, S.3    De La, T.R.4    Solans, A.5    Farre, M.6    Segura, J.7    Gooderham, N.J.8    Davies, D.S.9
  • 41
    • 0025013470 scopus 로고
    • Role of sulfation and acetylation in the activation of 2-hydroxyamino-1-methyl-6-phenylimidazo[4,5-b]pyridine to intermediates which bind DNA
    • Buonarati,M.H., Turteltaub,K.W., Shen,N.H. and Felton,J.S. (1990) Role of sulfation and acetylation in the activation of 2-hydroxyamino-1-methyl-6- phenylimidazo[4,5-b]pyridine to intermediates which bind DNA. Mutat. Res., 245, 185-190. (Pubitemid 20368892)
    • (1990) Mutation Research , vol.245 , Issue.3 , pp. 185-190
    • Buonarati, M.H.1    Turteltaub, K.W.2    Shen, N.H.3    Felton, J.S.4
  • 43
    • 0026783540 scopus 로고
    • Identification of N-(Deoxyguanosin-8-yl)-2-amino-1-methyl-6-phenylimidazo [4,5-b]pyridine as the major adduct formed by the food-borne carcinogen, 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine, with DNA
    • Lin,D., Kaderlik,K.R., Turesky,R.J., Miller,D.W., Lay,J.O.,Jr and Kadlubar,F.F. (1992) Identification of N-(Deoxyguanosin-8-yl)-2-amino-1-methyl- 6-phenylimidazo [4,5-b]pyridine as the major adduct formed by the food-borne carcinogen, 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine, with DNA. Chem. Res. Toxicol., 5, 691-697.
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 691-697
    • Lin, D.1    Kaderlik, K.R.2    Turesky, R.J.3    Miller, D.W.4    Lay Jr., J.O.5    Kadlubar, F.F.6
  • 44
    • 0028329729 scopus 로고
    • Mutation and repair induced by the carcinogen 2-(hydroxyamino)-1-methyl- 6-phenylimidazo[4,5-b]pyridine (N-OH-PhIP) in the dihydrofolate reductase gene of Chinese hamster ovary cells and conformational modeling of the dG- C8-PhIP adduct in DNA
    • Carothers,A.M., Yuan,W., Hingerty,B.E., Broyde,S., Grunberger,D. and Snyderwine,E.G. (1994) Mutation and repair induced by the carcinogen 2-(hydroxyamino)-1-methyl-6-phenylimidazo[4,5-b] pyridine (N-OH-PhIP) in the dihydrofolate reductase gene of Chinese hamster ovary cells and conformational modeling of the dG-C8-PhIP adduct in DNA. Chem. Res. Toxicol., 7, 209-218. (Pubitemid 24105354)
    • (1994) Chemical Research in Toxicology , vol.7 , Issue.2 , pp. 209-218
    • Carothers, A.M.1    Yuan, W.2    Hingerty, B.E.3    Broyde, S.4    Grunberger, D.5    Snyderwine, E.G.6
  • 46
    • 0035115614 scopus 로고    scopus 로고
    • Early detection of 2-amino-1-methyl-6-phenylimidazo (4,5-b)pyridine(PhIP) -induced mutations within the Apc gene of rat colon
    • Burnouf,D., Miturski,R., Nagao,M., Nakagama,H., Nothisen,M., Wagner,J. and Fuchs,R.P. (2001) Early detection of 2-amino-1-methyl-6-phenylimidazo (4,5-b)pyridine(PhIP)-induced mutations within the Apc gene of rat colon. Carcinogenesis, 22, 329-335. (Pubitemid 32175523)
    • (2001) Carcinogenesis , vol.22 , Issue.2 , pp. 329-335
    • Burnouf, D.Y.1    Miturski, R.2    Nagao, M.3    Nakagama, H.4    Nothisen, M.5    Wagner, J.6    Fuchs, R.P.P.7
  • 47
    • 0028944521 scopus 로고
    • Analysis of mutations induced by 2-amino-1-methyl-6-phenylimidazo[4,5-b] pyridine (PhIP) in human lymphoblastoid cells
    • Morgenthaler,P.M. and Holzhauser,D. (1995) Analysis of mutations induced by 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) in human lymphoblastoid cells. Carcinogenesis, 16, 713-718.
    • (1995) Carcinogenesis , vol.16 , pp. 713-718
    • Morgenthaler, P.M.1    Holzhauser, D.2
  • 48
    • 0029970360 scopus 로고    scopus 로고
    • Mutational spectra of the dietary carcinogen 2-amino-1-methyl-6- phenylimidazo[4,5-b]pyridine (PhIP) at the Chinese hamster hprt locus
    • DOI 10.1093/carcin/17.4.617
    • Yadollahi-Farsani,M., Gooderham,N., Davies,D. and Boobis,A. (1996) Mutational spectra of the dietary carcinogen 2-amino-1-methyl-6-phenylimidazo[4, 5-b]pyridine(PhIP) at the Chinese hamsters hprt locus. Carcinogenesis, 17, 617-624. (Pubitemid 26129670)
    • (1996) Carcinogenesis , vol.17 , Issue.4 , pp. 617-624
    • Yadollahi-Farsani, M.1    Gooderham, N.J.2    Davies, D.S.3    Boobis, A.R.4
  • 49
    • 6844261154 scopus 로고    scopus 로고
    • Agreement of mutational characteristics of heterocyclic amines in lacI of the Big Blue mouse with those in tumor related genes in rodents
    • DOI 10.1093/carcin/18.4.745
    • Okonogi,H., Ushijima,T., Zhang,X., Heddle,J., Suzuki,T., Sofuni,T., Felton,J., Tucker,J., Sugimura,T. and Nagao,M. (1997) Agreement of mutational characteristics of heterocyclic amines in lacI of the Big Blue mouse with those in tumor related genes in rodents. Carcinogenesis, 18, 745-748. (Pubitemid 28132462)
    • (1997) Carcinogenesis , vol.18 , Issue.4 , pp. 745-748
    • Okonogi, H.1    Ushijima, T.2    Zhang, X.B.3    Heddle, J.A.4    Suzuki, T.5    Sofuni, T.6    Felton, J.S.7    Tucker, J.D.8    Sugimura, T.9    Nagao, M.10
  • 51
    • 0033600909 scopus 로고    scopus 로고
    • Mutagenesis of the N-(deoxyguanosin-8-yl)-2-amino-1-methyl-6- phenylimidazo[4,5-b]pyridine DNA adduct in mammalian cells. Sequence context effects
    • Shibutani,S., Fernandes,A., Suzuki,N., Zhou,L., Johnson,F. and Grollman,A.P. (1999) Mutagenesis of the N-(deoxyguanosin-8-yl)-2-amino-1-methyl- 6-phenylimidazo[4,5-b]pyridine DNA adduct in mammalian cells. Sequence context effects. J. Biol. Chem., 274, 27433-27438.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27433-27438
    • Shibutani, S.1    Fernandes, A.2    Suzuki, N.3    Zhou, L.4    Johnson, F.5    Grollman, A.P.6
  • 52
    • 0036265736 scopus 로고    scopus 로고
    • Mutagenicity of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) in the mammary gland of big blue rats on high- and low- fat diets
    • Yu,M., Jones,M.L., Gong,M., Sinha,R., Schut,H.A. and Snyderwine,E.G. (2002) Mutagenicity of 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) in the mammary gland of Big Blue rats on high-and low-fat diets. Carcinogenesis, 23, 877-884. (Pubitemid 34567529)
    • (2002) Carcinogenesis , vol.23 , Issue.5 , pp. 877-884
    • Yu, M.1    Jones, M.L.2    Gong, M.3    Sinha, R.4    Schut, H.A.J.5    Snyderwine, E.G.6
  • 53
    • 25444458311 scopus 로고    scopus 로고
    • Molecular dynamics of a food carcinogen-DNA adduct in a replicative DNA polymerase suggest hindered nucleotide incorporation and extension
    • DOI 10.1021/tx050132b
    • Zhang,L., Shapiro,R. and Broyde,S. (2005) Molecular dynamics of a food carcinogen-DNA adduct in a replicative DNA polymerase suggest hindered nucleotide incorporation and extension. Chem. Res. Toxicol., 18, 1347-1363. (Pubitemid 41361708)
    • (2005) Chemical Research in Toxicology , vol.18 , Issue.9 , pp. 1347-1363
    • Zhang, L.1    Shapiro, R.2    Broyde, S.3
  • 54
    • 4344596952 scopus 로고    scopus 로고
    • The spacious active site of a Y-family DNA polymerase facilitates promiscuous nucleotide incorporation opposite a bulky carcinogen-DNA adduct: Elucidating the structure-function relationship through experimental and computational approaches
    • DOI 10.1074/jbc.M404332200
    • Perlow-Poehnelt,R.A., Likhterov,I., Scicchitano,D.A., Geacintov,N.E. and Broyde,S. (2004) The spacious active site of a Y-family DNA polymerase facilitates promiscuous nucleotide incorporation opposite a bulky carcinogen-DNA adduct: elucidating the structure-function relationship through experimental and computational approaches. J. Biol. Chem., 279, 36951-36961. (Pubitemid 39129045)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36951-36961
    • Perlow-Poehnelt, R.A.1    Likhterov, I.2    Scicchitano, D.A.3    Geacintov, N.E.4    Broyde, S.5
  • 57
    • 33644687408 scopus 로고    scopus 로고
    • Varying DNA base-pair size in subangstrom increments: Evidence for a loose, not large, active site in low-fidelity Dpo4 polymerase
    • DOI 10.1021/bi051961z
    • Mizukami,S., Kim,T.W., Helquist,S.A. and Kool,E.T. (2006) Varying DNA base-pair size in subangstrom increments: evidence for a loose, not large, active site in low-fidelity dpo4 polymerase. Biochemistry, 45, 2772-2778. (Pubitemid 43334526)
    • (2006) Biochemistry , vol.45 , Issue.9 , pp. 2772-2778
    • Mizukami, S.1    Kim, T.W.2    Helquist, S.A.3    Kool, E.T.4
  • 58
    • 31044454139 scopus 로고    scopus 로고
    • DNA polymerase catalysis in the absence of Watson-Crick hydrogen bonds: Analysis by single-turnover kinetics
    • DOI 10.1021/bi051792i
    • Potapova,O., Chan,C., Delucia,A.M., Helquist,S.A., Kool,E.T., Grindley,N.D. and Joyce,C.M. (2006) DNA polymerase catalysis in the absence of Watson-Crick hydrogen bonds: analysis by single-turnover kinetics. Biochemistry, 45, 890-898. (Pubitemid 43122253)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 890-898
    • Potapova, O.1    Chan, C.2    DeLucia, A.M.3    Helquist, S.A.4    Kool, E.T.5    Grindley, N.D.F.6    Joyce, C.M.7
  • 61
    • 0032922174 scopus 로고    scopus 로고
    • A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat
    • Cheatham,T.E.,III, Cieplak,P. and Kollman,P.A. (1999) A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat. J. Biomol. Struct. Dyn., 16, 845-862.
    • (1999) J. Biomol. Struct. Dyn. , vol.16 , pp. 845-862
    • Cheatham III, T.E.1    Cieplak, P.2    Kollman, P.A.3
  • 62
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An Nxlog(N) method for Ewald sums in large systems
    • Darden,T., York,D. and Pedersen,L. (1993) Particle mesh Ewald: an Nxlog(N) method for Ewald sums in large systems. J. Phys. Chem., 98, 10089-10092.
    • (1993) J. Phys. Chem. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 63
    • 33646940952 scopus 로고
    • Numerical integration of cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert,J.P., Ciccotti,G. and Berendsen,H.J.C. (1977) Numerical integration of cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys., 23, 327-341.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 64
    • 0001430231 scopus 로고    scopus 로고
    • The flying ice cube: Velocity rescaling in molecular dynamics leads to violation of energy equipartition
    • Harvey,S.C., Tan,R.K.Z. and Cheatham,T.E. (1998) The flying ice cube: velocity rescaling in molecular dynamics leads to violation of energy equipartition. J. Comput. Chem., 19, 726-740.
    • (1998) J. Comput. Chem. , vol.19 , pp. 726-740
    • Harvey, S.C.1    Tan, R.K.Z.2    Cheatham, T.E.3
  • 65
    • 84962339749 scopus 로고    scopus 로고
    • Interaction and solvation energies of nonpolar DNA base analogues and their role in polymerase insertion fidelity
    • Barsky,D., Kool,E.T. and Colvin,M.E. (1999) Interaction and solvation energies of nonpolar DNA base analogues and their role in polymerase insertion fidelity. J. Biomol. Struct. Dyn., 16, 1119-1134. (Pubitemid 29299427)
    • (1999) Journal of Biomolecular Structure and Dynamics , vol.16 , Issue.6 , pp. 1119-1134
    • Barsky, D.1    Kool, E.T.2    Colvin, M.E.3
  • 66
    • 0032005866 scopus 로고    scopus 로고
    • Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes
    • DOI 10.1016/S0959-440X(98)80010-9
    • Brautigam,C.A. and Steitz,T.A. (1998) Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes. Curr. Opin. Struct. Biol., 8, 54-63. (Pubitemid 28107916)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.1 , pp. 54-63
    • Brautigam, C.A.1    Steitz, T.A.2
  • 67
    • 0032425080 scopus 로고    scopus 로고
    • The mechanism of action of T7 DNA polymerase
    • DOI 10.1016/S0959-440X(98)80089-4
    • Doublie,S. and Ellenberger,T. (1998) The mechanism of action of T7 DNA polymerase. Curr. Opin. Struct. Biol., 8, 704-712. (Pubitemid 29004667)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.6 , pp. 704-712
    • Doublie, S.1    Ellenberger, T.2
  • 69
    • 0242317682 scopus 로고    scopus 로고
    • An error-prone family Y DNA polymerase (DinB homolog from Sulfolobus solfataricus) uses a 'steric gate' residue for discrimination against ribonucleotides
    • DOI 10.1093/nar/gkg417
    • DeLucia,A.M., Grindley,N.D. and Joyce,C.M. (2003) An error-prone family Y DNA polymerase (DinB homolog from Sulfolobus solfataricus) uses a 'steric gate' residue for discrimination against ribonucleotides. Nucleic Acids Res., 31, 4129-4137. (Pubitemid 37442292)
    • (2003) Nucleic Acids Research , vol.31 , Issue.14 , pp. 4129-4137
    • DeLucia, A.M.1    Grindley, N.D.F.2    Joyce, C.M.3
  • 70
    • 9744237198 scopus 로고    scopus 로고
    • 2-yl)-2- acetylaminofluorene, a persistent acetylaminofluorene-derived DNA adduct in mammalian cells
    • DOI 10.1021/bi048279+
    • Yasui,M., Dong,H., Bonala,R.R., Suzuki,N., Ohmori,H., Hanaoka,F., Johnson,F., Grollman,A.P. and Shibutani,S. (2004) Mutagenic properties of 3-(deoxyguanosin-N2-yl)-2-acetylaminofluorene, a persistent acetylaminofluorene- derived DNA adduct in mammalian cells. Biochemistry, 43, 15005-15013. (Pubitemid 39587477)
    • (2004) Biochemistry , vol.43 , Issue.47 , pp. 15005-15013
    • Yasui, M.1    Dong, H.2    Bonala, R.R.3    Suzuki, N.4    Ohmori, H.5    Hanaoka, F.6    Johnson, F.7    Grollman, A.P.8    Shibutani, S.9
  • 71
    • 4143116647 scopus 로고    scopus 로고
    • Crystal structure of the catalytic core of human DNA polymerase kappa
    • DOI 10.1016/j.str.2004.05.011, PII S0969212604002138
    • Uljon,S.N., Johnson,R.E., Edwards,T.A., Prakash,S., Prakash,L. and Aggarwal,A.K. (2004) Crystal structure of the catalytic core of human DNA polymerase k. Structure (Camb), 12, 1395-1404. (Pubitemid 39092084)
    • (2004) Structure , vol.12 , Issue.8 , pp. 1395-1404
    • Uljon, S.N.1    Johnson, R.E.2    Edwards, T.A.3    Prakash, S.4    Prakash, L.5    Aggarwal, A.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.