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Volumn 10, Issue 9, 2003, Pages 827-835

How do DNA repair proteins locate potential base lesions? A chemical crosslinking method to investigate O6-alkylguanine-DNA alkyltransferases

Author keywords

[No Author keywords available]

Indexed keywords

ADA; ESCHERICHIA COLI;

EID: 0141676627     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2003.08.007     Document Type: Article
Times cited : (26)

References (43)
  • 5
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • Bruner S.D., Norman D.P.G., Verdine G.L. Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature. 403:2000;859-866.
    • (2000) Nature , vol.403 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.G.2    Verdine, G.L.3
  • 6
    • 0037068446 scopus 로고    scopus 로고
    • Oxidative demethylation by Escherichia coli AlkB directly reverts DNA damage
    • Trewick S., Henshaw T.F., Hausinger R.P., Lindahl T., Sedgwick B. Oxidative demethylation by Escherichia coli AlkB directly reverts DNA damage. Nature. 419:2002;174-178.
    • (2002) Nature , vol.419 , pp. 174-178
    • Trewick, S.1    Henshaw, T.F.2    Hausinger, R.P.3    Lindahl, T.4    Sedgwick, B.5
  • 7
    • 0037068433 scopus 로고    scopus 로고
    • AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
    • Falnes P.O., Johansen R.F., Seeberg E. AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli. Nature. 419:2002;178-182.
    • (2002) Nature , vol.419 , pp. 178-182
    • Falnes, P.O.1    Johansen, R.F.2    Seeberg, E.3
  • 10
    • 0021894988 scopus 로고
    • 6-methylguanine-DNA methyltransferase in cell survivial, mutagenesis, and carcinogenesis
    • 6-methylguanine-DNA methyltransferase in cell survivial, mutagenesis, and carcinogenesis. Mutat. Res. 145:1985;1-16.
    • (1985) Mutat. Res. , vol.145 , pp. 1-16
    • Yarosh, D.B.1
  • 11
    • 0023919219 scopus 로고
    • Regulation and expression of the adaptive response to alkylating agents
    • Lindahl T., Sedgewick B., Sekiguchi M., Nakabeppu Y. Regulation and expression of the adaptive response to alkylating agents. Annu. Rev. Biochem. 57:1988;133-157.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 133-157
    • Lindahl, T.1    Sedgewick, B.2    Sekiguchi, M.3    Nakabeppu, Y.4
  • 12
    • 0002427798 scopus 로고
    • Self-methylation by suicide DNA repair enzymes
    • W.K. Pair, & S. Kim. Boca Raton, FL: CRC Press. 285-304.pp
    • Demple B. Self-methylation by suicide DNA repair enzymes. Pair W.K., Kim S. Protein Methylation. 1990;CRC Press, Boca Raton, FL. 285-304.pp.
    • (1990) Protein Methylation
    • Demple, B.1
  • 13
    • 0025195404 scopus 로고
    • 6-alkylguanine-DNA alkyltransferase: Regulation and importance in response to alkylating carcinogenic and therapeutic agents
    • 6-alkylguanine-DNA alkyltransferase. regulation and importance in response to alkylating carcinogenic and therapeutic agents Cancer Res. 50:1990;6119-6129.
    • (1990) Cancer Res. , vol.50 , pp. 6119-6129
    • Pegg, A.E.1
  • 14
    • 0027351670 scopus 로고
    • Regulation of repair of alkylation damage in mammalian genomes
    • Mitra S., Kaina B. Regulation of repair of alkylation damage in mammalian genomes. Prog. Nucleic Acid Res. Mol. Biol. 44:1993;109-142.
    • (1993) Prog. Nucleic Acid Res. Mol. Biol. , vol.44 , pp. 109-142
    • Mitra, S.1    Kaina, B.2
  • 17
    • 0022064910 scopus 로고
    • 6-alkylguanine-DNA alkyltransferase activity correlates with the therapeutic response of human rhabdomyosarcoma xenografts to 1-(2-chloroethyl)-3-(trans-4-methylcyclohexyl)-1-nitrosourea
    • 6-alkylguanine-DNA alkyltransferase activity correlates with the therapeutic response of human rhabdomyosarcoma xenografts to 1-(2-chloroethyl)-3-(trans-4-methylcyclohexyl)-1-nitrosourea. Proc. Natl. Acad. Sci. USA. 82:1985;2985-2989.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 2985-2989
    • Brent, T.P.1    Houghton, P.J.2    Houghton, J.A.3
  • 18
    • 0031594831 scopus 로고    scopus 로고
    • 6-methylguanine-DNA methyltransferase activity and sensitivity to cyclophosphamide and cisplatin in human lung tumor xenografts
    • 6-methylguanine-DNA methyltransferase activity and sensitivity to cyclophosphamide and cisplatin in human lung tumor xenografts. Int. J. Cancer. 77:1998;919-922.
    • (1998) Int. J. Cancer , vol.77 , pp. 919-922
    • Mattern, J.1    Eichhorn, U.2    Kaina, B.3    Volm, M.4
  • 19
    • 0025941670 scopus 로고
    • 6-methylguanine-DNA methyltransferase (MGMT) cDNA in Chinese hamster cells: The role of MGMT in protection against the genotoxic effects of alkylating agents
    • 6-methylguanine-DNA methyltransferase (MGMT) cDNA in Chinese hamster cells. the role of MGMT in protection against the genotoxic effects of alkylating agents Carcinogenesis. 12:1991;1857-1867.
    • (1991) Carcinogenesis , vol.12 , pp. 1857-1867
    • Kaina, B.1    Fritz, G.2    Mitra, S.3    Coquerelle, T.4
  • 21
    • 0034599723 scopus 로고    scopus 로고
    • Active and alkylated human AGT structures: A novel zinc site, inhibitor and extrahelical base binding
    • Daniels D.S., Mol C.D., Arvai A.S., Kanugula S., Pegg A.E., Tainer J.A. Active and alkylated human AGT structures. a novel zinc site, inhibitor and extrahelical base binding EMBO J. 19:2000;1719-1730.
    • (2000) EMBO J. , vol.19 , pp. 1719-1730
    • Daniels, D.S.1    Mol, C.D.2    Arvai, A.S.3    Kanugula, S.4    Pegg, A.E.5    Tainer, J.A.6
  • 23
    • 0031149139 scopus 로고    scopus 로고
    • How do DNA repair proteins locate damaged bases in the genome?
    • Verdine G.L., Bruner S.D. How do DNA repair proteins locate damaged bases in the genome? Chem. Biol. 4:1997;329-334.
    • (1997) Chem. Biol. , vol.4 , pp. 329-334
    • Verdine, G.L.1    Bruner, S.D.2
  • 24
    • 0028013240 scopus 로고
    • The flip side of DNA methylation
    • Verdine G.L. The flip side of DNA methylation. Cell. 76:1994;197-200.
    • (1994) Cell , vol.76 , pp. 197-200
    • Verdine, G.L.1
  • 27
    • 0028010888 scopus 로고
    • HhaI methyltransferase flips its target base out of the DNA helix
    • Klimasauskas S., Kumar S., Roberts S.J., Cheng X. HhaI methyltransferase flips its target base out of the DNA helix. Cell. 76:1994;357-369.
    • (1994) Cell , vol.76 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, S.J.3    Cheng, X.4
  • 28
    • 0029068629 scopus 로고
    • The crystal structure of HaeIII methyltransferase covalently complexed to DNA: An extrahelical cytosine and rearranged base pairing
    • Reinisch K.M., Chen L., Verdine G.L., Lipscomb W.N. The crystal structure of HaeIII methyltransferase covalently complexed to DNA. an extrahelical cytosine and rearranged base pairing Cell. 82:1995;143-153.
    • (1995) Cell , vol.82 , pp. 143-153
    • Reinisch, K.M.1    Chen, L.2    Verdine, G.L.3    Lipscomb, W.N.4
  • 29
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil DNA glycosylase bound to DNA
    • Slupphaug G., Mol C.D., Kavil B., Arvai A.S., Krokan H.E., Tainer J.A. A nucleotide-flipping mechanism from the structure of human uracil DNA glycosylase bound to DNA. Nature. 384:1996;87-92.
    • (1996) Nature , vol.384 , pp. 87-92
    • Slupphaug, G.1    Mol, C.D.2    Kavil, B.3    Arvai, A.S.4    Krokan, H.E.5    Tainer, J.A.6
  • 30
    • 0000742057 scopus 로고
    • Active site and complete sequence of the suicidal methyltransferase that counters alkylation mutagenesis
    • Demple B., Sedgwick B., Robin P., Totty N., Waterfield M.D., Lindahl T. Active site and complete sequence of the suicidal methyltransferase that counters alkylation mutagenesis. Proc. Natl. Acad. Sci. USA. 82:1985;2688-2692.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 2688-2692
    • Demple, B.1    Sedgwick, B.2    Robin, P.3    Totty, N.4    Waterfield, M.D.5    Lindahl, T.6
  • 31
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase at 2.7 Å resolution: Implications of comformational changes for polymerization and inhibition mechanism
    • Huang H., Chopra R., Verdine G.L., Harrison S.C. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase at 2.7 Å resolution. implications of comformational changes for polymerization and inhibition mechanism Science. 282:1998;1669-1675.
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 32
    • 0034111063 scopus 로고    scopus 로고
    • Trapping of a catalytic HIV reverse transcriptase-template:primer complex through a disulfide bond
    • Huang H., Harrison S.C., Verdine G.L. Trapping of a catalytic HIV reverse transcriptase-template:primer complex through a disulfide bond. Chem. Biol. 7:2000;355-364.
    • (2000) Chem. Biol. , vol.7 , pp. 355-364
    • Huang, H.1    Harrison, S.C.2    Verdine, G.L.3
  • 33
    • 12244275699 scopus 로고    scopus 로고
    • Trapping distinct structural states of a protein/DNA interaction through disulfide crosslinking
    • He C., Verdine G.L. Trapping distinct structural states of a protein/DNA interaction through disulfide crosslinking. Chem. Biol. 9:2002;1297-1303.
    • (2002) Chem. Biol. , vol.9 , pp. 1297-1303
    • He, C.1    Verdine, G.L.2
  • 34
    • 0001599016 scopus 로고
    • 4-(dimethylamino)-5-methylcytosine and 4-thiothymine
    • 4-(dimethylamino)-5-methylcytosine and 4-thiothymine J. Org. Chem. 57:1992;3839-3845.
    • (1992) J. Org. Chem. , vol.57 , pp. 3839-3845
    • Xu, Y.Z.1    Zheng, Q.2    Swann, P.F.3
  • 35
    • 0025650326 scopus 로고
    • Synthesis of functionally tethered oligonucleotides by the convertible nucleoside approach
    • MacMillan A.M., Verdine G.L. Synthesis of functionally tethered oligonucleotides by the convertible nucleoside approach. J. Org. Chem. 55:1990;5931-5933.
    • (1990) J. Org. Chem. , vol.55 , pp. 5931-5933
    • MacMillan, A.M.1    Verdine, G.L.2
  • 36
    • 0025969972 scopus 로고
    • Engineering tethered DNA molecules by the convertible nucleoside approach
    • MacMillan A.M., Verdine G.L. Engineering tethered DNA molecules by the convertible nucleoside approach. Tetrahedron. 14:1991;2603-2616.
    • (1991) Tetrahedron , vol.14 , pp. 2603-2616
    • MacMillan, A.M.1    Verdine, G.L.2
  • 37
    • 0032581024 scopus 로고    scopus 로고
    • Nearest-neighbor thermodynamics of internal A:C mismatches in DNA: Sequence dependence and pH effects
    • Allawi H.T., SantaLucia J. Jr. Nearest-neighbor thermodynamics of internal A:C mismatches in DNA. sequence dependence and pH effects Biochemistry. 37:1998;9435-9444.
    • (1998) Biochemistry , vol.37 , pp. 9435-9444
    • Allawi, H.T.1    SantaLucia J., Jr.2
  • 38
    • 0032102940 scopus 로고    scopus 로고
    • Thermodynamics of internal C:T mismatches in DNA
    • Allawi H.T., SantaLucia J. Jr. Thermodynamics of internal C:T mismatches in DNA. Nucleic Acids Res. 26:1998;2694-2701.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2694-2701
    • Allawi, H.T.1    SantaLucia J., Jr.2
  • 41
    • 0035501334 scopus 로고    scopus 로고
    • 6-methylguanine is not affected by thymine base pairing and the presence of MMR proteins
    • 6-methylguanine is not affected by thymine base pairing and the presence of MMR proteins. Mutat. Res. 487:2001;59-66.
    • (2001) Mutat. Res. , vol.487 , pp. 59-66
    • Lips, J.1    Kaina, B.2
  • 42
    • 0026611836 scopus 로고
    • 6-methylguanine:thymine mispairs in DNA by extracts of human cells
    • 6-methylguanine:thymine mispairs in DNA by extracts of human cells. Biochemistry. 31:1992;7998-8008.
    • (1992) Biochemistry , vol.31 , pp. 7998-8008
    • Ullah, S.1    Day R.S. III2
  • 43


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