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Volumn 26, Issue 5, 2013, Pages 803-816

Modeling the conformational preference of the carbon-bonded covalent adduct formed upon exposure of 2′-deoxyguanosine to ochratoxin A

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; DEOXYGUANOSINE; GUANINE; HYDROGEN; NUCLEIC ACID BASE; NUCLEOSIDE; NUCLEOTIDE; OCHRATOXIN; PHOSPHATE; POLYCYCLIC AROMATIC HYDROCARBON; SUGAR; DNA ADDUCT;

EID: 84877956877     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx4000864     Document Type: Article
Times cited : (24)

References (76)
  • 3
    • 79952045213 scopus 로고    scopus 로고
    • Ochratoxin A producing species in the genus Penicillium
    • Cabañes, F. J., Bragulat, M. R., and Castellá, G. (2010) Ochratoxin A producing species in the genus Penicillium Toxins 2, 1111-1120
    • (2010) Toxins , vol.2 , pp. 1111-1120
    • Cabañes, F.J.1    Bragulat, M.R.2    Castellá, G.3
  • 4
    • 33646257329 scopus 로고    scopus 로고
    • Fusarium mycotoxins and ochratoxin A in cereals and cereal products
    • Engelhardt, G., Barthel, J., and Sparrer, D. (2006) Fusarium mycotoxins and ochratoxin A in cereals and cereal products Mol. Nutr. Food Res. 50, 401-405
    • (2006) Mol. Nutr. Food Res. , vol.50 , pp. 401-405
    • Engelhardt, G.1    Barthel, J.2    Sparrer, D.3
  • 6
    • 0031864523 scopus 로고    scopus 로고
    • Survey of pork, poultry, coffee, beer and pulses for ochratoxin A
    • Jörgensen, K. (1998) Survey of pork, poultry, coffee, beer and pulses for ochratoxin A Food Addit. Contam. 15, 550-554
    • (1998) Food Addit. Contam. , vol.15 , pp. 550-554
    • Jörgensen, K.1
  • 7
    • 0038059315 scopus 로고    scopus 로고
    • Review: Ochratoxin A (OTA) in wines, musts and grape juices: Occurrence, regulations and methods of analysis
    • Bellí, N., Marín, S., Sanchis, V., and Ramos, A. J. (2002) Review: ochratoxin A (OTA) in wines, musts and grape juices: occurrence, regulations and methods of analysis Food Sci. Technol. Int. 8, 325-335
    • (2002) Food Sci. Technol. Int. , vol.8 , pp. 325-335
    • Bellí, N.1    Marín, S.2    Sanchis, V.3    Ramos, A.J.4
  • 8
    • 0016262531 scopus 로고
    • Acute intraperitoneal toxicity of ochratoxin a and B derivatives in rainbow trout (Salmo gairdneri)
    • Doster, R. C., Sinnhuber, R. O., and Pawlowski, N. E. (1974) Acute intraperitoneal toxicity of ochratoxin a and B derivatives in rainbow trout (Salmo gairdneri) Food Cosmet. Toxicol. 12, 499-505
    • (1974) Food Cosmet. Toxicol. , vol.12 , pp. 499-505
    • Doster, R.C.1    Sinnhuber, R.O.2    Pawlowski, N.E.3
  • 9
    • 33748292907 scopus 로고    scopus 로고
    • Ochratoxins: A global perspective
    • Bayman, P. and Baker, J. (2006) Ochratoxins: a global perspective Mycopathologia 162, 215-223
    • (2006) Mycopathologia , vol.162 , pp. 215-223
    • Bayman, P.1    Baker, J.2
  • 10
    • 78649357553 scopus 로고    scopus 로고
    • Ochratoxin A: General overview and actual molecular status
    • El Khoury, A. and Atoui, A. (2010) Ochratoxin A: general overview and actual molecular status Toxins 2, 461-493
    • (2010) Toxins , vol.2 , pp. 461-493
    • El Khoury, A.1    Atoui, A.2
  • 11
    • 65749089980 scopus 로고    scopus 로고
    • Mycotoxins and the kidney: Modes of action for renal tumor formation by ochratoxin A in rodents
    • Mally, A. and Dekant, W. (2009) Mycotoxins and the kidney: Modes of action for renal tumor formation by ochratoxin A in rodents Mol. Nutr. Food Res. 53, 467-478
    • (2009) Mol. Nutr. Food Res. , vol.53 , pp. 467-478
    • Mally, A.1    Dekant, W.2
  • 12
    • 0016789988 scopus 로고
    • Nephrotoxicity of dietary ochratoxin A in broiler chickens
    • Huff, W. E., Wyatt, R. D., and Hamilton, P. B. (1975) Nephrotoxicity of dietary ochratoxin A in broiler chickens Appl. Microbiol. 30, 48-51
    • (1975) Appl. Microbiol. , vol.30 , pp. 48-51
    • Huff, W.E.1    Wyatt, R.D.2    Hamilton, P.B.3
  • 13
    • 0036171917 scopus 로고    scopus 로고
    • Hypothesis: Does ochratoxin A cause testicular cancer?
    • Schwartz, G. G. (2002) Hypothesis: does ochratoxin A cause testicular cancer? Cancer Causes Control 13, 91-100
    • (2002) Cancer Causes Control , vol.13 , pp. 91-100
    • Schwartz, G.G.1
  • 14
    • 0023917438 scopus 로고
    • Ochratoxin A in human blood in relation to Balkan endemic nephropathy and urinary system tumours in Bulgaria
    • Petkova-Bocharova, T., Chernozemsky, I. N., and Castegnaro, M. (1988) Ochratoxin A in human blood in relation to Balkan endemic nephropathy and urinary system tumours in Bulgaria Food Addit. Contam. 5, 299-301
    • (1988) Food Addit. Contam. , vol.5 , pp. 299-301
    • Petkova-Bocharova, T.1    Chernozemsky, I.N.2    Castegnaro, M.3
  • 15
    • 0026272252 scopus 로고
    • Ochratoxin A in human blood in relation to Balkan endemic nephropathy and urinary tract tumours in Bulgaria
    • Petkova-Bocharova, T. and Castegnaro, M. (1991) Ochratoxin A in human blood in relation to Balkan endemic nephropathy and urinary tract tumours in Bulgaria IARC scientific publications 135-137
    • (1991) IARC Scientific Publications , pp. 135-137
    • Petkova-Bocharova, T.1    Castegnaro, M.2
  • 17
    • 13144293044 scopus 로고    scopus 로고
    • Ochratoxin A: The continuing enigma
    • O'Brien, E. and Dietrich, D. R. (2005) Ochratoxin A: the continuing enigma Crit. Rev. Toxicol. 35, 33-60
    • (2005) Crit. Rev. Toxicol. , vol.35 , pp. 33-60
    • O'Brien, E.1    Dietrich, D.R.2
  • 18
    • 80052669892 scopus 로고    scopus 로고
    • Evidence for a role of oxidative stress in the carcinogenicity of ochratoxin A
    • Marin-Kuan, M., Ehrlich, V., Delatour, T., Cavin, C., and Schilter, B. (2011) Evidence for a role of oxidative stress in the carcinogenicity of ochratoxin A J. Toxicol. 2011, 645361
    • (2011) J. Toxicol. , vol.2011 , pp. 645361
    • Marin-Kuan, M.1    Ehrlich, V.2    Delatour, T.3    Cavin, C.4    Schilter, B.5
  • 20
    • 79960700316 scopus 로고    scopus 로고
    • Perturbation of mitosis through inhibition of histone acetyltransferases: The key to ochratoxin A toxicity and carcinogenicity?
    • Czakai, K., Müller, K., Mosesso, P., Pepe, G., Schulze, M., Gohla, A., Patnaik, D., Dekant, W., Higgins, J. M. G., and Mally, A. (2011) Perturbation of mitosis through inhibition of histone acetyltransferases: the key to ochratoxin A toxicity and carcinogenicity? Toxicol. Sci. 122, 317-329
    • (2011) Toxicol. Sci. , vol.122 , pp. 317-329
    • Czakai, K.1    Müller, K.2    Mosesso, P.3    Pepe, G.4    Schulze, M.5    Gohla, A.6    Patnaik, D.7    Dekant, W.8    Higgins, J.M.G.9    Mally, A.10
  • 21
    • 84859785087 scopus 로고    scopus 로고
    • An update on direct genotoxicity as a molecular mechanism of ochratoxin A carcinogenicity
    • Pfohl-Leszkowicz, A. and Manderville, R. A. (2011) An update on direct genotoxicity as a molecular mechanism of ochratoxin A carcinogenicity Chem. Res. Toxicol. 25, 252-262
    • (2011) Chem. Res. Toxicol. , vol.25 , pp. 252-262
    • Pfohl-Leszkowicz, A.1    Manderville, R.A.2
  • 23
    • 33847112240 scopus 로고    scopus 로고
    • Opinion of the scientific panel on contaminants in the food chain on a request from the commission related to ochratoxin A in food, EFSA-Q-2005-154
    • EFSA ()
    • EFSA (2006) Opinion of the scientific panel on contaminants in the food chain on a request from the commission related to ochratoxin A in food, EFSA-Q-2005-154 EFSA J. 365, 1-56
    • (2006) EFSA J. , vol.365 , pp. 1-56
  • 24
    • 75149113718 scopus 로고    scopus 로고
    • Structures of covalent adducts between DNA and ochratoxin A: A new factor in debate about genotoxicity and human risk assessment
    • Mantle, P. G., Faucet-Marquis, V., Manderville, R. A., Squillaci, B., and Pfohl-Leszkowicz, A. (2009) Structures of covalent adducts between DNA and ochratoxin A: a new factor in debate about genotoxicity and human risk assessment Chem. Res. Toxicol. 23, 89-98
    • (2009) Chem. Res. Toxicol. , vol.23 , pp. 89-98
    • Mantle, P.G.1    Faucet-Marquis, V.2    Manderville, R.A.3    Squillaci, B.4    Pfohl-Leszkowicz, A.5
  • 25
    • 0034659115 scopus 로고    scopus 로고
    • In vitro DNA and dGMP adducts formation caused by ochratoxin A
    • Obrecht-Pflumio, S. and Dirheimer, G. (2000) In vitro DNA and dGMP adducts formation caused by ochratoxin A Chem.-Biol. Interact. 127, 29-44
    • (2000) Chem.-Biol. Interact. , vol.127 , pp. 29-44
    • Obrecht-Pflumio, S.1    Dirheimer, G.2
  • 26
    • 0035659452 scopus 로고    scopus 로고
    • Horseradish peroxidase mediates DNA and deoxyguanosine 3′-monophosphate adduct formation in the presence of ochratoxin A
    • Obrecht-Pflumio, S. and Dirheimer, G. (2001) Horseradish peroxidase mediates DNA and deoxyguanosine 3′-monophosphate adduct formation in the presence of ochratoxin A Arch. Toxicol. 75, 583-590
    • (2001) Arch. Toxicol. , vol.75 , pp. 583-590
    • Obrecht-Pflumio, S.1    Dirheimer, G.2
  • 27
    • 0037414317 scopus 로고    scopus 로고
    • Ochratoxin A forms a carbon-bonded C8-deoxyguanosine nucleoside adduct: Implications for C8 reactivity by a phenolic radical
    • Dai, J., Wright, M. W., and Manderville, R. A. (2003) Ochratoxin A forms a carbon-bonded C8-deoxyguanosine nucleoside adduct: implications for C8 reactivity by a phenolic radical J. Am. Chem. Soc. 125, 3716-3717
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3716-3717
    • Dai, J.1    Wright, M.W.2    Manderville, R.A.3
  • 28
    • 4644268330 scopus 로고    scopus 로고
    • Evidence for covalent DNA adduction by ochratoxin A following chronic exposure to rat and subacute exposure to pig
    • Faucet, V., Pfohl-Leszkowicz, A., Dai, J., Castegnaro, M., and Manderville, R. A. (2004) Evidence for covalent DNA adduction by ochratoxin A following chronic exposure to rat and subacute exposure to pig Chem. Res. Toxicol. 17, 1289-1296
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 1289-1296
    • Faucet, V.1    Pfohl-Leszkowicz, A.2    Dai, J.3    Castegnaro, M.4    Manderville, R.A.5
  • 29
    • 33746874095 scopus 로고    scopus 로고
    • Base-displaced intercalated structure of the food mutagen 2-amino-3-methylimidazo[4,5-f]quinoline in the recognition sequence of the NarI restriction enzyme, a hotspot for -2 bp deletions
    • Wang, F., DeMuro, N. E., Elmquist, C. E., Stover, J. S., Rizzo, C. J., and Stone, M. P. (2006) Base-displaced intercalated structure of the food mutagen 2-amino-3-methylimidazo[4,5-f]quinoline in the recognition sequence of the NarI restriction enzyme, a hotspot for -2 bp deletions J. Am. Chem. Soc. 128, 10085-10095
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 10085-10095
    • Wang, F.1    Demuro, N.E.2    Elmquist, C.E.3    Stover, J.S.4    Rizzo, C.J.5    Stone, M.P.6
  • 30
    • 0033578397 scopus 로고    scopus 로고
    • Solution structures of aminofluorene [AF]-stacked conformers of the syn [AF]-C8-dG adduct positioned opposite dC or da at a template-primer junction
    • Gu, Z., Gorin, A., Hingerty, B. E., Broyde, S., and Patel, D. J. (1999) Solution structures of aminofluorene [AF]-stacked conformers of the syn [AF]-C8-dG adduct positioned opposite dC or dA at a template-primer junction Biochemistry 38, 10855-10870
    • (1999) Biochemistry , vol.38 , pp. 10855-10870
    • Gu, Z.1    Gorin, A.2    Hingerty, B.E.3    Broyde, S.4    Patel, D.J.5
  • 31
    • 0032488634 scopus 로고    scopus 로고
    • Solution structure of the aminofluorene [AF]-intercalated conformer of the syn-[AF]-C8-dG adduct opposite dC in a DNA duplex
    • Mao, B., Hingerty, B. E., Broyde, S., and Patel, D. J. (1998) Solution structure of the aminofluorene [AF]-intercalated conformer of the syn-[AF]-C8-dG adduct opposite dC in a DNA duplex Biochemistry 37, 81-94
    • (1998) Biochemistry , vol.37 , pp. 81-94
    • Mao, B.1    Hingerty, B.E.2    Broyde, S.3    Patel, D.J.4
  • 32
    • 0032488597 scopus 로고    scopus 로고
    • Solution structure of the aminofluorene [AF]-external conformer of the anti-[AF]-C8-dG adduct opposite dC in a DNA duplex
    • Mao, B., Hingerty, B. E., Broyde, S., and Patel, D. J. (1998) Solution structure of the aminofluorene [AF]-external conformer of the anti-[AF]-C8-dG adduct opposite dC in a DNA duplex Biochemistry 37, 95-106
    • (1998) Biochemistry , vol.37 , pp. 95-106
    • Mao, B.1    Hingerty, B.E.2    Broyde, S.3    Patel, D.J.4
  • 34
    • 33644584203 scopus 로고    scopus 로고
    • Ambident reactivity of phenoxyl radicals in DNA adduction
    • Manderville, R. A. (2005) Ambident reactivity of phenoxyl radicals in DNA adduction Can. J. Chem. 83, 1261-1267
    • (2005) Can. J. Chem. , vol.83 , pp. 1261-1267
    • Manderville, R.A.1
  • 35
    • 34250841151 scopus 로고    scopus 로고
    • Efficient syntheses of C8-aryl adducts of adenine and guanine formed by reaction of radical cation metabolites of carcinogenic polycyclic aromatic hydrocarbons with DNA
    • Dai, Q., Xu, D., Lim, K., and Harvey, R. G. (2007) Efficient syntheses of C8-aryl adducts of adenine and guanine formed by reaction of radical cation metabolites of carcinogenic polycyclic aromatic hydrocarbons with DNA J. Org. Chem. 72, 4856-4863
    • (2007) J. Org. Chem. , vol.72 , pp. 4856-4863
    • Dai, Q.1    Xu, D.2    Lim, K.3    Harvey, R.G.4
  • 36
    • 80054770333 scopus 로고    scopus 로고
    • Fluorescent properties and conformational preferences of C-linked phenolic-DNA adducts
    • Omumi, A., Millen, A. L., Wetmore, S. D., and Manderville, R. A. (2011) Fluorescent properties and conformational preferences of C-linked phenolic-DNA adducts Chem. Res. Toxicol. 24, 1694-1709
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 1694-1709
    • Omumi, A.1    Millen, A.L.2    Wetmore, S.D.3    Manderville, R.A.4
  • 37
    • 78649295926 scopus 로고    scopus 로고
    • Structure-Function Characteristics of Aromatic Amine-DNA Adducts
    • in, pp, Wiley-VCH Verlag GmbH & Co KGaA, Weinheim, Germany
    • Cho, B. (2010) Structure-Function Characteristics of Aromatic Amine-DNA Adducts, in The Chemical Biology of DNA Damage, pp 217-238, Wiley-VCH Verlag GmbH & Co KGaA, Weinheim, Germany.
    • (2010) The Chemical Biology of DNA Damage , pp. 217-238
    • Cho, B.1
  • 38
    • 58549109864 scopus 로고    scopus 로고
    • Accommodation of an N-(deoxyguanosin-8-yl)-2-acetylaminofluorene adduct in the active site of human DNA polymerase ι: Hoogsteen or Watson-Crick base pairing?
    • Donny-Clark, K., Shapiro, R., and Broyde, S. (2008) Accommodation of an N-(deoxyguanosin-8-yl)-2-acetylaminofluorene adduct in the active site of human DNA polymerase ι: Hoogsteen or Watson-Crick base pairing? Biochemistry 48, 7-18
    • (2008) Biochemistry , vol.48 , pp. 7-18
    • Donny-Clark, K.1    Shapiro, R.2    Broyde, S.3
  • 39
    • 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)
    • 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
    • (2006) Nucleic Acids Res. , vol.34 , pp. 785-795
    • Wang, L.1    Broyde, S.2
  • 40
    • 9244229513 scopus 로고    scopus 로고
    • Crystal structures of 2-acetylaminofluorene and 2-aminofluorene in complex with T7 DNA polymerase reveal mechanisms of mutagenesis
    • Dutta, S., Li, Y., Johnson, D., Dzantiev, L., Richardson, C. C., Romano, L. J., and Ellenberger, T. (2004) Crystal structures of 2-acetylaminofluorene and 2-aminofluorene in complex with T7 DNA polymerase reveal mechanisms of mutagenesis Proc. Natl. Acad. Sci. U.S.A. 101, 16186-16191
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16186-16191
    • Dutta, S.1    Li, Y.2    Johnson, D.3    Dzantiev, L.4    Richardson, C.C.5    Romano, L.J.6    Ellenberger, T.7
  • 41
    • 0020055717 scopus 로고
    • Force field conformational analysis of aminofluorene and acetylaminofluorene substituted deoxyguanosine
    • Lipkowitz, K. B., Chevalier, T., Widdifield, M., and Beland, F. A. (1982) Force field conformational analysis of aminofluorene and acetylaminofluorene substituted deoxyguanosine Chem.-Biol. Interact. 40, 57-76
    • (1982) Chem.-Biol. Interact. , vol.40 , pp. 57-76
    • Lipkowitz, K.B.1    Chevalier, T.2    Widdifield, M.3    Beland, F.A.4
  • 42
    • 84867967079 scopus 로고    scopus 로고
    • C8-linked bulky guanosine DNA adducts: Experimental and computational insights into adduct conformational preferences and resulting mutagenicity
    • Millen, A. L., Sharma, P., and Wetmore, S. D. (2012) C8-linked bulky guanosine DNA adducts: experimental and computational insights into adduct conformational preferences and resulting mutagenicity Future Med. Chem. 4, 1981-2007
    • (2012) Future Med. Chem. , vol.4 , pp. 1981-2007
    • Millen, A.L.1    Sharma, P.2    Wetmore, S.D.3
  • 43
    • 0028039973 scopus 로고
    • Use of single-turnover kinetics to study bulky adduct bypass by T7 DNA polymerase
    • Lindsley, J. E. and Fuchs, R. P. P. (1994) Use of single-turnover kinetics to study bulky adduct bypass by T7 DNA polymerase Biochemistry 33, 764-772
    • (1994) Biochemistry , vol.33 , pp. 764-772
    • Lindsley, J.E.1    Fuchs, R.P.P.2
  • 44
    • 78649981502 scopus 로고    scopus 로고
    • Mechanism of acetylaminofluorene-dG induced frameshifting by polymerase eta
    • Schorr, S. and Carell, T. (2010) Mechanism of acetylaminofluorene-dG induced frameshifting by polymerase eta ChemBioChem 11, 2534-2537
    • (2010) ChemBioChem , vol.11 , pp. 2534-2537
    • Schorr, S.1    Carell, T.2
  • 45
    • 44949231330 scopus 로고    scopus 로고
    • Computational and experimental evidence for the structural preference of phenolic C-8 purine adducts
    • Millen, A. L., McLaughlin, C. K., Sun, K. M., Manderville, R. A., and Wetmore, S. D. (2008) Computational and experimental evidence for the structural preference of phenolic C-8 purine adducts J. Phys. Chem. A 112, 3742-3753
    • (2008) J. Phys. Chem. A , vol.112 , pp. 3742-3753
    • Millen, A.L.1    McLaughlin, C.K.2    Sun, K.M.3    Manderville, R.A.4    Wetmore, S.D.5
  • 46
    • 77950250407 scopus 로고    scopus 로고
    • Conformational flexibility of C8-phenoxyl-2′-deoxyguanosine nucleotide adduct
    • Millen, A. L., Manderville, R. A., and Wetmore, S. D. (2010) Conformational flexibility of C8-phenoxyl-2′-deoxyguanosine nucleotide adduct J. Phys. Chem. B 114, 4373-4382
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4373-4382
    • Millen, A.L.1    Manderville, R.A.2    Wetmore, S.D.3
  • 47
    • 37049089507 scopus 로고
    • Crystal structures and conformational analysis of ochratoxin A and B: Probing the chemical structure causing toxicity
    • Bredenkamp, M. W., Dillen, J. L. M., van Rooyen, P. H., and Steyn, P. S. (1989) Crystal structures and conformational analysis of ochratoxin A and B: probing the chemical structure causing toxicity J. Chem. Soc., Perkin Trans. 1835-1839
    • (1989) J. Chem. Soc., Perkin Trans. , pp. 1835-1839
    • Bredenkamp, M.W.1    Dillen, J.L.M.2    Van Rooyen, P.H.3    Steyn, P.S.4
  • 48
    • 25444526160 scopus 로고    scopus 로고
    • Conformational analysis of ochratoxin A by NMR spectroscopy and computational molecular modeling
    • Dais, P., Stefanaki, I., Fragaki, G., and Mikros, E. (2005) Conformational analysis of ochratoxin A by NMR spectroscopy and computational molecular modeling J. Phys. Chem. B 109, 16926-16936
    • (2005) J. Phys. Chem. B , vol.109 , pp. 16926-16936
    • Dais, P.1    Stefanaki, I.2    Fragaki, G.3    Mikros, E.4
  • 51
    • 0019834780 scopus 로고
    • Hot spots of frameshift mutations induced by the ultimate carcinogen N- acetoxy-N-2-acetylaminofluorene
    • Fuchs, R. P. P., Schwartz, N., and Daune, M. P. (1981) Hot spots of frameshift mutations induced by the ultimate carcinogen N- acetoxy-N-2- acetylaminofluorene Nature 294, 657-659
    • (1981) Nature , vol.294 , pp. 657-659
    • Fuchs, R.P.P.1    Schwartz, N.2    Daune, M.P.3
  • 52
    • 0039547559 scopus 로고
    • Single adduct mutagenesis: Strong effect of the position of a single acetylaminofluorene adduct within a mutation hot spot
    • Burnouf, D., Koehl, P., and Fuchs, R. P. (1989) Single adduct mutagenesis: strong effect of the position of a single acetylaminofluorene adduct within a mutation hot spot Proc. Natl. Acad. Sci. U.S.A. 86, 4147-4151
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 4147-4151
    • Burnouf, D.1    Koehl, P.2    Fuchs, R.P.3
  • 55
    • 34250318638 scopus 로고    scopus 로고
    • Refinement of the AMBER force field for nucleic acids: Improving the description of α/γ conformers
    • Pérez, A., Marchán, I., Svozil, D., Sponer, J., Cheatham Iii, T. E., Laughton, C. A., and Orozco, M. (2007) Refinement of the AMBER force field for nucleic acids: improving the description of α/γ conformers Biophys. J. 92, 3817-3829
    • (2007) Biophys. J. , vol.92 , pp. 3817-3829
    • Pérez, A.1    Marchán, I.2    Svozil, D.3    Sponer, J.4    Cheatham Iii, T.E.5    Laughton, C.A.6    Orozco, M.7
  • 56
    • 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., 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, T.E.1    Cieplak, P.2    Kollman, P.A.3
  • 58
    • 33748538349 scopus 로고    scopus 로고
    • Automatic atom type and bond type perception in molecular mechanical calculations
    • Wang, J., Wang, W., Kollman, P. A., and Case, D. A. (2006) Automatic atom type and bond type perception in molecular mechanical calculations J. Mol. Graphics Modell. 25, 247-260
    • (2006) J. Mol. Graphics Modell. , vol.25 , pp. 247-260
    • Wang, J.1    Wang, W.2    Kollman, P.A.3    Case, D.A.4
  • 60
    • 3042729705 scopus 로고    scopus 로고
    • Conformational properties of shape modified nucleosides - Fleximers
    • Polak, M., Seley, K. L., and Plavec, J. (2004) Conformational properties of shape modified nucleosides-fleximers J. Am. Chem. Soc. 126, 8159-8166
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8159-8166
    • Polak, M.1    Seley, K.L.2    Plavec, J.3
  • 61
    • 0027425942 scopus 로고
    • Base pairing of 8-oxoguanosine and 8-oxo-2′-deoxyguanosine with 2′-deoxyadenosine, 2′-deoxycytosine, 2′-deoxyguanosine, and thymidine
    • Gannett, P. M. and Sura, T. P. (1993) Base pairing of 8-oxoguanosine and 8-oxo-2′-deoxyguanosine with 2′-deoxyadenosine, 2′- deoxycytosine, 2′-deoxyguanosine, and thymidine Chem. Res. Toxicol. 6, 690-700
    • (1993) Chem. Res. Toxicol. , vol.6 , pp. 690-700
    • Gannett, P.M.1    Sura, T.P.2
  • 62
    • 0029928273 scopus 로고    scopus 로고
    • Synthesis and characterization of 8-methoxy-2′-deoxyadenosine- containing oligonucleotides to probe the syn glycosidic conformation of 2′-deoxyadenosine within DNA
    • Eason, R. G., Burkhardt, D. M., Phillips, S. J., Smith, D. P., and David, S. S. (1996) Synthesis and characterization of 8-methoxy-2′- deoxyadenosine-containing oligonucleotides to probe the syn glycosidic conformation of 2′-deoxyadenosine within DNA Nucleic Acids Res. 24, 890-897
    • (1996) Nucleic Acids Res. , vol.24 , pp. 890-897
    • Eason, R.G.1    Burkhardt, D.M.2    Phillips, S.J.3    Smith, D.P.4    David, S.S.5
  • 63
    • 0038463891 scopus 로고    scopus 로고
    • Ab initio conformational analysis of nucleic acid components: Intrinsic energetic contributions to nucleic acid structure and dynamics
    • Foloppe, N., Nilsson, L., and MacKerell, A. D. (2001) Ab initio conformational analysis of nucleic acid components: intrinsic energetic contributions to nucleic acid structure and dynamics Biopolymers 61, 61-76
    • (2001) Biopolymers , vol.61 , pp. 61-76
    • Foloppe, N.1    Nilsson, L.2    MacKerell, A.D.3
  • 64
    • 0036192864 scopus 로고    scopus 로고
    • Intrinsic conformational energetics associated with the glycosyl torsion in DNA: A quantum mechanical study
    • Foloppe, N., Hartmann, B., Nilsson, L., and MacKerell, A. D. (2002) Intrinsic conformational energetics associated with the glycosyl torsion in DNA: a quantum mechanical study Biophys. J. 82, 1554-1569
    • (2002) Biophys. J. , vol.82 , pp. 1554-1569
    • Foloppe, N.1    Hartmann, B.2    Nilsson, L.3    MacKerell, A.D.4
  • 66
    • 0014965547 scopus 로고
    • Crystal and molecular structure of 8-bromoguanosine and 8-bromoadenosine, two purine nucleosides in the syn conformation
    • Tavale, S. S. and Sobell, H. M. (1970) Crystal and molecular structure of 8-bromoguanosine and 8-bromoadenosine, two purine nucleosides in the syn conformation J. Mol. Biol. 48, 109-123
    • (1970) J. Mol. Biol. , vol.48 , pp. 109-123
    • Tavale, S.S.1    Sobell, H.M.2
  • 67
    • 0018794763 scopus 로고
    • 9-β-d-Arabinofuranosyl-8-n-butylaminoadenine, a C-8 substituted nucleoside in the anti conformation: Crystallographic and NMR studies
    • Neidle, S., Sanderson, M. R., Subbiah, A., Chattopadhyaya, J. B., Kuroda, R., and Reese, C. B. (1979) 9-β-d-Arabinofuranosyl-8-n-butylaminoadenine, a C-8 substituted nucleoside in the anti conformation: crystallographic and NMR studies Biochim. Biophys. Acta 565, 379-386
    • (1979) Biochim. Biophys. Acta , vol.565 , pp. 379-386
    • Neidle, S.1    Sanderson, M.R.2    Subbiah, A.3    Chattopadhyaya, J.B.4    Kuroda, R.5    Reese, C.B.6
  • 68
    • 0016355917 scopus 로고
    • Molecular and crystal structure of deoxyguanosine 5[prime]-phosphat
    • Viswamitra, M. A. and Seshadri, T. P. (1974) Molecular and crystal structure of deoxyguanosine 5[prime]-phosphat Nature 252, 176-177
    • (1974) Nature , vol.252 , pp. 176-177
    • Viswamitra, M.A.1    Seshadri, T.P.2
  • 69
    • 0019318942 scopus 로고
    • High-salt d(CpGpCpG), a left-handed Z[prime] DNA double helix
    • Drew, H., Takano, T., Tanaka, S., Itakura, K., and Dickerson, R. E. (1980) High-salt d(CpGpCpG), a left-handed Z[prime] DNA double helix Nature 286, 567-573
    • (1980) Nature , vol.286 , pp. 567-573
    • Drew, H.1    Takano, T.2    Tanaka, S.3    Itakura, K.4    Dickerson, R.E.5
  • 71
    • 0015817210 scopus 로고
    • Conformational studies on guanosine nucleotides and polynucleotides. The effect of the base on the glycosyl and backbone conformations
    • Yathindra, N. and Sundaralingam, M. (1973) Conformational studies on guanosine nucleotides and polynucleotides. The effect of the base on the glycosyl and backbone conformations Biopolymers 12, 2075-2082
    • (1973) Biopolymers , vol.12 , pp. 2075-2082
    • Yathindra, N.1    Sundaralingam, M.2
  • 72
    • 0015899139 scopus 로고
    • Syn-Anti effects on the spatial configuration of polynucleotide chains
    • Olson, W. K. (1973) Syn-Anti effects on the spatial configuration of polynucleotide chains Biopolymers 12, 1787-1814
    • (1973) Biopolymers , vol.12 , pp. 1787-1814
    • Olson, W.K.1
  • 73
    • 0017180164 scopus 로고
    • Flexibility of deoxyguanosine 5′monophosphate (5′dGMP): An E.H.T. conformational analysis
    • Lespinasse, J.-N., Broch, H., Cornillon, R., and Vasilescu, D. (1976) Flexibility of deoxyguanosine 5′monophosphate (5′dGMP): an E.H.T. conformational analysis J. Theor. Biol. 57, 225-230
    • (1976) J. Theor. Biol. , vol.57 , pp. 225-230
    • Lespinasse, J.-N.1    Broch, H.2    Cornillon, R.3    Vasilescu, D.4
  • 74
    • 0024428898 scopus 로고
    • NMR and computational characterization of the N-(deoxyguanosin-8-yl) aminofluorene adduct [(AF)G] opposite adenosine in DNA: (AF)G[syn].A[anti] pair formation and its pH dependence
    • Norman, D., Abuaf, P., Hingerty, B. E., Live, D., Grunberger, D., Broyde, S., and Patel, D. J. (1989) NMR and computational characterization of the N-(deoxyguanosin-8-yl)aminofluorene adduct [(AF)G] opposite adenosine in DNA: (AF)G[syn].A[anti] pair formation and its pH dependence Biochemistry 28, 7462-7476
    • (1989) Biochemistry , vol.28 , pp. 7462-7476
    • Norman, D.1    Abuaf, P.2    Hingerty, B.E.3    Live, D.4    Grunberger, D.5    Broyde, S.6    Patel, D.J.7
  • 75
    • 0031472574 scopus 로고    scopus 로고
    • Synthesis and miscoding specificity of oligodeoxynucleotide containing 8-phenyl-2 ′-deoxyguanosine
    • Kohda, K., Tsunomoto, H., Kasamatsu, T., Sawamura, F., Terashima, I., and Shibutani, S. (1997) Synthesis and miscoding specificity of oligodeoxynucleotide containing 8-phenyl-2 ′-deoxyguanosine Chem. Res. Toxicol. 10, 1351-1358
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 1351-1358
    • Kohda, K.1    Tsunomoto, H.2    Kasamatsu, T.3    Sawamura, F.4    Terashima, I.5    Shibutani, S.6


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