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Volumn 330, Issue 5, 2003, Pages 1027-1037

Properties of and substrate determinants for the exonuclease activity of human apurinic endonuclease Ape1

Author keywords

Abasic (AP) endonuclease; Ape1; Mismatch DNA; Polymerase ; Proofreading exonuclease

Indexed keywords

APURINIC ACID; DNA DIRECTED DNA POLYMERASE BETA; DNA TOPOISOMERASE; EXONUCLEASE; EXONUCLEASE APE1; OLIGONUCLEOTIDE; PHOSPHATE; SINGLE STRANDED DNA; THYMINE; UNCLASSIFIED DRUG;

EID: 0038690166     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00712-5     Document Type: Article
Times cited : (85)

References (67)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T. Instability and decay of the primary structure of DNA. Nature. 362:1993;709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 2
    • 0035111895 scopus 로고    scopus 로고
    • Recent progress in the biology, chemistry and structural biology of DNA glycosylases
    • Scharer O.D., Jiricny J. Recent progress in the biology, chemistry and structural biology of DNA glycosylases. Bioessays. 23:2001;270-281.
    • (2001) Bioessays , vol.23 , pp. 270-281
    • Scharer, O.D.1    Jiricny, J.2
  • 3
    • 0023015325 scopus 로고
    • Mutagenesis by apurinic/apyrimidinic sites
    • Loeb L.A., Preston B.D. Mutagenesis by apurinic/apyrimidinic sites. Annu. Rev. Genet. 20:1986;201-230.
    • (1986) Annu. Rev. Genet. , vol.20 , pp. 201-230
    • Loeb, L.A.1    Preston, B.D.2
  • 4
    • 0035837587 scopus 로고    scopus 로고
    • The major human abasic endonuclease: Formation, consequences and repair of abasic lesions in DNA
    • Wilson D.M. III, Barsky D. The major human abasic endonuclease: formation, consequences and repair of abasic lesions in DNA. Mutat. Res. 485:2001;283-307.
    • (2001) Mutat. Res. , vol.485 , pp. 283-307
    • Wilson D.M. III1    Barsky, D.2
  • 5
    • 0026004662 scopus 로고
    • Two distinct human DNA diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidized DNA
    • Chen D.S., Herman T., Demple B. Two distinct human DNA diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidized DNA. Nucl. Acids Res. 19:1991;5907-5914.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 5907-5914
    • Chen, D.S.1    Herman, T.2    Demple, B.3
  • 6
    • 0029829265 scopus 로고    scopus 로고
    • The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice
    • Xanthoudakis S., Smeyne R.J., Wallace J.D., Curran T. The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice. Proc. Natl Acad. Sci. USA. 93:1996;8919-8923.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8919-8923
    • Xanthoudakis, S.1    Smeyne, R.J.2    Wallace, J.D.3    Curran, T.4
  • 7
    • 0031720426 scopus 로고    scopus 로고
    • A murine AP-endonuclease gene-targeted deficiency with post-implantation embryonic progression and ionizing radiation sensitivity
    • Ludwig D.L., MacInnes M.A., Takiguchi Y., Purtymun P.E., Henrie M., Flannery M., et al. A murine AP-endonuclease gene-targeted deficiency with post-implantation embryonic progression and ionizing radiation sensitivity. Mutat. Res. 409:1998;17-29.
    • (1998) Mutat. Res. , vol.409 , pp. 17-29
    • Ludwig, D.L.1    MacInnes, M.A.2    Takiguchi, Y.3    Purtymun, P.E.4    Henrie, M.5    Flannery, M.6
  • 9
    • 0032100860 scopus 로고    scopus 로고
    • Mammalian base excision repair and DNA polymerase beta
    • Wilson S.H. Mammalian base excision repair and DNA polymerase beta. Mutat. Res. 407:1998;203-215.
    • (1998) Mutat. Res. , vol.407 , pp. 203-215
    • Wilson, S.H.1
  • 10
    • 0034113805 scopus 로고    scopus 로고
    • Suppression of spontaneous mutagenesis in human cells by DNA base excision-repair
    • Lindahl T. Suppression of spontaneous mutagenesis in human cells by DNA base excision-repair. Mutat. Res. 462:2000;129-135.
    • (2000) Mutat. Res. , vol.462 , pp. 129-135
    • Lindahl, T.1
  • 11
    • 0031972353 scopus 로고    scopus 로고
    • Structure and function of mammalian DNA ligases
    • Tomkinson A.E., Mackey Z.B. Structure and function of mammalian DNA ligases. Mutat. Res. 407:1998;1-9.
    • (1998) Mutat. Res. , vol.407 , pp. 1-9
    • Tomkinson, A.E.1    Mackey, Z.B.2
  • 12
    • 0033955346 scopus 로고    scopus 로고
    • XRCC1 keeps DNA from getting stranded
    • Thompson L.H., West M.G. XRCC1 keeps DNA from getting stranded. Mutat. Res. 459:2000;1-18.
    • (2000) Mutat. Res. , vol.459 , pp. 1-18
    • Thompson, L.H.1    West, M.G.2
  • 13
    • 0024195429 scopus 로고
    • DNA damage produced by ionizing radiation in mammalian cells: Identities, mechanisms of formation, and reparability
    • Ward J.F. DNA damage produced by ionizing radiation in mammalian cells: identities, mechanisms of formation, and reparability. Prog. Nucl. Acid Res. Mol. Biol. 35:1988;95-125.
    • (1988) Prog. Nucl. Acid Res. Mol. Biol. , vol.35 , pp. 95-125
    • Ward, J.F.1
  • 14
    • 0030591651 scopus 로고    scopus 로고
    • DNA damage and mutagenesis by radiomimetic DNA-cleaving agents: Bleomycin, neocarzinostatin and other enediynes
    • Povirk L.F. DNA damage and mutagenesis by radiomimetic DNA-cleaving agents: bleomycin, neocarzinostatin and other enediynes. Mutat. Res. 355:1996;71-89.
    • (1996) Mutat. Res. , vol.355 , pp. 71-89
    • Povirk, L.F.1
  • 15
    • 0026323008 scopus 로고
    • Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: Definition of a family of DNA repair enzymes
    • Demple B., Herman T., Chen D.S. Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes. Proc. Natl Acad. Sci. USA. 88:1991;11450-11454.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 16
    • 0026683715 scopus 로고
    • CDNA cloning, sequencing, expression and possible domain structure of human APEX nuclease homologous to Escherichia coli exonuclease III
    • Seki S., Hatsushika M., Watanabe S., Akiyama K., Nagao K., Tsutsui K. cDNA cloning, sequencing, expression and possible domain structure of human APEX nuclease homologous to Escherichia coli exonuclease III. Biochim. Biophys. Acta. 1131:1992;287-299.
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 287-299
    • Seki, S.1    Hatsushika, M.2    Watanabe, S.3    Akiyama, K.4    Nagao, K.5    Tsutsui, K.6
  • 17
    • 0028245076 scopus 로고
    • Removal of 3′-phosphoglycolate from DNA strand-break damage in an oligonucleotide substrate by recombinant human apurinic/apyrimidinic endonuclease 1
    • Winters T.A., Henner W.D., Russell P.S., McCullough A., Jorgensen T.J. Removal of 3′-phosphoglycolate from DNA strand-break damage in an oligonucleotide substrate by recombinant human apurinic/apyrimidinic endonuclease 1. Nucl. Acids Res. 22:1994;1866-1873.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 1866-1873
    • Winters, T.A.1    Henner, W.D.2    Russell, P.S.3    McCullough, A.4    Jorgensen, T.J.5
  • 18
    • 0030788621 scopus 로고    scopus 로고
    • 3′-phosphodiesterase activity of human apurinic/apyrimidinic endonuclease at DNA double-strand break ends
    • Suh D., Wilson D.M. III, Povirk L.F. 3′-phosphodiesterase activity of human apurinic/apyrimidinic endonuclease at DNA double-strand break ends. Nucl. Acids Res. 25:1997;2495-2500.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 2495-2500
    • Suh, D.1    Wilson D.M. III2    Povirk, L.F.3
  • 19
    • 0029001186 scopus 로고
    • Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA
    • Wilson D.M. III, Takeshita M., Grollman A.P., Demple B. Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA. J. Biol. Chem. 270:1995;16002-16007.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16002-16007
    • Wilson D.M. III1    Takeshita, M.2    Grollman, A.P.3    Demple, B.4
  • 20
    • 0034613195 scopus 로고    scopus 로고
    • A novel action of human apurinic/apyrimidinic endonuclease: Excision of L-configuration deoxyribonucleoside analogs from the 3′ termini of DNA
    • Chou K.M., Kukhanova M., Cheng Y.C. A novel action of human apurinic/apyrimidinic endonuclease: excision of L-configuration deoxyribonucleoside analogs from the 3′ termini of DNA. J. Biol. Chem. 275:2000;31009-31015.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31009-31015
    • Chou, K.M.1    Kukhanova, M.2    Cheng, Y.C.3
  • 21
    • 0037034035 scopus 로고    scopus 로고
    • An exonucleolytic activity of human apurinic/apyrimidinic endonuclease on 3′ mispaired DNA
    • Chou K.M., Cheng Y.C. An exonucleolytic activity of human apurinic/apyrimidinic endonuclease on 3′ mispaired DNA. Nature. 415:2002;655-659.
    • (2002) Nature , vol.415 , pp. 655-659
    • Chou, K.M.1    Cheng, Y.C.2
  • 22
    • 0036303482 scopus 로고    scopus 로고
    • Determinants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III
    • Hadi M.Z., Ginalski K., Nguyen L.H., Wilson D.M. III. Determinants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III. J. Mol. Biol. 316:2002;853-866.
    • (2002) J. Mol. Biol. , vol.316 , pp. 853-866
    • Hadi, M.Z.1    Ginalski, K.2    Nguyen, L.H.3    Wilson D.M. III4
  • 23
    • 0033232311 scopus 로고    scopus 로고
    • III Effects of Ape1 overexpression on cellular resistance to DNA-damaging and anti-cancer agents
    • Schild L.J., Brookman K.W., Thompson L.H., Wilson D.M. III Effects of Ape1 overexpression on cellular resistance to DNA-damaging and anti-cancer agents. Som. Cell Mol. Genet. 25:2002;253-262.
    • (2002) Som. Cell Mol. Genet. , vol.25 , pp. 253-262
    • Schild, L.J.1    Brookman, K.W.2    Thompson, L.H.3    Wilson, D.M.4
  • 24
    • 0037034306 scopus 로고    scopus 로고
    • An APE that proofreads
    • Jiricny J. An APE that proofreads. Nature. 415:2002;593-594.
    • (2002) Nature , vol.415 , pp. 593-594
    • Jiricny, J.1
  • 27
    • 84961981834 scopus 로고    scopus 로고
    • Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases
    • Erzberger J.P., Barsky D., Scharer O.D., Colvin M.E., Wilson D.M. III. Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases. Nucl. Acids Res. 26:1998;2771-2778.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 2771-2778
    • Erzberger, J.P.1    Barsky, D.2    Scharer, O.D.3    Colvin, M.E.4    Wilson D.M. III5
  • 28
    • 0033538343 scopus 로고    scopus 로고
    • 2+ and specific amino acid residues in the catalytic reaction of the major human abasic endonuclease: New insights from EDTA-resistant incision of acyclic abasic site analogs and site-directed mutagenesis
    • 2+ and specific amino acid residues in the catalytic reaction of the major human abasic endonuclease: new insights from EDTA-resistant incision of acyclic abasic site analogs and site-directed mutagenesis. J. Mol. Biol. 290:1999;447-457.
    • (1999) J. Mol. Biol. , vol.290 , pp. 447-457
    • Erzberger, J.P.1    Wilson D.M. III2
  • 29
    • 0037089147 scopus 로고    scopus 로고
    • A quantitative model of human DNA base excision repair. I. Mechanistic insights
    • Sokhansanj B.A., Rodrigue G.R., Fitch J.P., Wilson D.M. III. A quantitative model of human DNA base excision repair. I. Mechanistic insights. Nucl. Acids Res. 30:2002;1817-1825.
    • (2002) Nucl. Acids Res. , vol.30 , pp. 1817-1825
    • Sokhansanj, B.A.1    Rodrigue, G.R.2    Fitch, J.P.3    Wilson D.M. III4
  • 30
    • 0033554862 scopus 로고    scopus 로고
    • Human apurinic/apyrimidinic endonuclease is processive
    • Carey D.C., Strauss P.R. Human apurinic/apyrimidinic endonuclease is processive. Biochemistry. 38:1999;16553-16560.
    • (1999) Biochemistry , vol.38 , pp. 16553-16560
    • Carey, D.C.1    Strauss, P.R.2
  • 31
    • 0031021533 scopus 로고    scopus 로고
    • Substrate binding by human apurinic/apyrimidinic endonuclease indicates a Briggs-Haldane mechanism
    • Strauss P.R., Beard W.A., Patterson T.A., Wilson S.H. Substrate binding by human apurinic/apyrimidinic endonuclease indicates a Briggs-Haldane mechanism. J. Biol. Chem. 272:1997;1302-1307.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1302-1307
    • Strauss, P.R.1    Beard, W.A.2    Patterson, T.A.3    Wilson, S.H.4
  • 33
    • 0034734377 scopus 로고    scopus 로고
    • Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: The 3′ ends justify the means
    • Mol C.D., Hosfield D.J., Tainer J.A. Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: the 3′ ends justify the means. Mutat. Res. 460:2000;211-229.
    • (2000) Mutat. Res. , vol.460 , pp. 211-229
    • Mol, C.D.1    Hosfield, D.J.2    Tainer, J.A.3
  • 34
    • 0029794521 scopus 로고    scopus 로고
    • Kinetic mechanism of the 3′→5′ proofreading exonuclease of DNA polymerase III. Analysis by steady state and pre-steady state methods
    • Miller H., Perrino F.W. Kinetic mechanism of the 3′→5′ proofreading exonuclease of DNA polymerase III. Analysis by steady state and pre-steady state methods. Biochemistry. 35:1996;12919-12925.
    • (1996) Biochemistry , vol.35 , pp. 12919-12925
    • Miller, H.1    Perrino, F.W.2
  • 35
    • 0031773901 scopus 로고    scopus 로고
    • Enzymatic processing of radiation-induced free radical damage in DNA
    • Wallace S.S. Enzymatic processing of radiation-induced free radical damage in DNA. Radiat. Res. 150:1998;S60-S79.
    • (1998) Radiat. Res. , vol.150
    • Wallace, S.S.1
  • 36
    • 0035163137 scopus 로고    scopus 로고
    • Complexities of the DNA base excision repair pathway for repair of oxidative DNA damage
    • Mitra S., Boldogh I., Izumi T., Hazra T.K. Complexities of the DNA base excision repair pathway for repair of oxidative DNA damage. Environ. Mol. Mutagen. 38:2001;180-190.
    • (2001) Environ. Mol. Mutagen. , vol.38 , pp. 180-190
    • Mitra, S.1    Boldogh, I.2    Izumi, T.3    Hazra, T.K.4
  • 37
    • 0037228625 scopus 로고    scopus 로고
    • AP endonuclease 1 has no biologically significant 3(′)→5(′)-exonuclease activity
    • Lebedeva N.A., Khodyreva S.N., Favre A., Lavrik O.I. AP endonuclease 1 has no biologically significant 3(′)→5(′)-exonuclease activity. Biochem. Biophys. Res. Commun. 300:2003;182-187.
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 182-187
    • Lebedeva, N.A.1    Khodyreva, S.N.2    Favre, A.3    Lavrik, O.I.4
  • 38
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway
    • Bennett R.A., Wilson D.M. III, Wong D., Demple B. Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway. Proc. Natl Acad. Sci. USA. 94:1997;7166-7169.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7166-7169
    • Bennett, R.A.1    Wilson D.M. III2    Wong, D.3    Demple, B.4
  • 39
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: A molecular perspective
    • Wang J.C. Cellular roles of DNA topoisomerases: a molecular perspective. Nature Rev. Mol. Cell Biol. 3:2002;430-440.
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 40
    • 0033605675 scopus 로고    scopus 로고
    • Induction of reversible complexes between eukaryotic DNA topoisomerase I and DNA-containing oxidative base damages. 7,8-Dihydro-8-oxoguanine and 5-hydroxycytosine
    • Pourquier P., Ueng L.M., Fertala J., Wang D., Park H.J., Essigmann J.M., et al. Induction of reversible complexes between eukaryotic DNA topoisomerase I and DNA-containing oxidative base damages. 7,8-Dihydro-8-oxoguanine and 5-hydroxycytosine. J. Biol. Chem. 274:1999;8516-8523.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8516-8523
    • Pourquier, P.1    Ueng, L.M.2    Fertala, J.3    Wang, D.4    Park, H.J.5    Essigmann, J.M.6
  • 41
    • 0034513226 scopus 로고    scopus 로고
    • Molecular and biological determinants of the cytotoxic actions of camptothecins. Perspective for the development of new topoisomerase I inhibitors
    • Kohn K.W., Pommier Y. Molecular and biological determinants of the cytotoxic actions of camptothecins. Perspective for the development of new topoisomerase I inhibitors. Ann. NY Acad. Sci. 922:2000;11-26.
    • (2000) Ann. NY Acad. Sci. , vol.922 , pp. 11-26
    • Kohn, K.W.1    Pommier, Y.2
  • 42
    • 0037069381 scopus 로고    scopus 로고
    • Repair of topoisomerase I covalent complexes in the absence of the tyrosyl-DNA phosphodiesterase Tdp1
    • Liu C., Pouliot J.J., Nash H.A. Repair of topoisomerase I covalent complexes in the absence of the tyrosyl-DNA phosphodiesterase Tdp1. Proc. Natl Acad. Sci. USA. 99:2002;14970-14975.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 14970-14975
    • Liu, C.1    Pouliot, J.J.2    Nash, H.A.3
  • 43
    • 0037108948 scopus 로고    scopus 로고
    • Yeast Tdp1 and Rad1-Rad10 function as redundant pathways for repairing Top1 replicative damage
    • Vance J.R., Wilson T.E. Yeast Tdp1 and Rad1-Rad10 function as redundant pathways for repairing Top1 replicative damage. Proc. Natl Acad. Sci. USA. 99:2002;13669-13674.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 13669-13674
    • Vance, J.R.1    Wilson, T.E.2
  • 44
    • 0033569666 scopus 로고    scopus 로고
    • Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes
    • Pouliot J.J., Yao K.C., Robertson C.A., Nash H.A. Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes. Science. 286:1999;552-555.
    • (1999) Science , vol.286 , pp. 552-555
    • Pouliot, J.J.1    Yao, K.C.2    Robertson, C.A.3    Nash, H.A.4
  • 45
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • Demple B., Harrison L. Repair of oxidative damage to DNA: enzymology and biology. Annu. Rev. Biochem. 63:1994;915-948.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 46
    • 0029347105 scopus 로고
    • Structure and function of apurinic/apyrimidinic endonucleases
    • Barzilay G., Hickson I.D. Structure and function of apurinic/apyrimidinic endonucleases. Bioessays. 17:1995;713-719.
    • (1995) Bioessays , vol.17 , pp. 713-719
    • Barzilay, G.1    Hickson, I.D.2
  • 47
    • 0001885914 scopus 로고    scopus 로고
    • Prokaryotic base excision repair
    • J.A. Nickoloff, & M.F. Hoekstra. Totowa, NJ: Humana Press
    • Wilson D.M. III, Engelward B.P., Samson L. Prokaryotic base excision repair. Nickoloff J.A., Hoekstra M.F. DNA Damage and Repair. 1998;29-64 Humana Press, Totowa, NJ.
    • (1998) DNA Damage and Repair , pp. 29-64
    • Wilson D.M. III1    Engelward, B.P.2    Samson, L.3
  • 48
    • 0030839750 scopus 로고    scopus 로고
    • Abasic site binding by the human apurinic endonuclease, Ape, and determination of the DNA contact sites
    • Wilson D.M. III, Takeshita M., Demple B. Abasic site binding by the human apurinic endonuclease, Ape, and determination of the DNA contact sites. Nucl. Acids Res. 25:1997;933-939.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 933-939
    • Wilson D.M. III1    Takeshita, M.2    Demple, B.3
  • 49
    • 0034607548 scopus 로고    scopus 로고
    • Mapping the protein-DNA interface and the metal-binding site of the major human apurinic/apyrimidinic endonuclease
    • Nguyen L.H., Barsky D., Erzberger J.P., Wilson D.M. III. Mapping the protein-DNA interface and the metal-binding site of the major human apurinic/apyrimidinic endonuclease. J. Mol. Biol. 298:2000;447-459.
    • (2000) J. Mol. Biol. , vol.298 , pp. 447-459
    • Nguyen, L.H.1    Barsky, D.2    Erzberger, J.P.3    Wilson D.M. III4
  • 50
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination
    • Mol C.D., Izumi T., Mitra S., Tainer J.A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination. Nature. 403:2000;451-456.
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 51
    • 0032515143 scopus 로고    scopus 로고
    • Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product
    • Masuda Y., Bennett R.A., Demple B. Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product. J. Biol. Chem. 273:1998;30352-30359.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30352-30359
    • Masuda, Y.1    Bennett, R.A.2    Demple, B.3
  • 52
    • 0035098395 scopus 로고    scopus 로고
    • Rates of base excision repair are not solely dependent on levels of initiating enzymes
    • Cappelli E., Hazra T., Hill J.W., Slupphaug G., Bogliolo M., Frosina G. Rates of base excision repair are not solely dependent on levels of initiating enzymes. Carcinogenesis. 22:2001;387-393.
    • (2001) Carcinogenesis , vol.22 , pp. 387-393
    • Cappelli, E.1    Hazra, T.2    Hill, J.W.3    Slupphaug, G.4    Bogliolo, M.5    Frosina, G.6
  • 53
    • 0037178839 scopus 로고    scopus 로고
    • Conversion of phosphoglycolate to phosphate termini on 3′ overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1
    • Inamdar K.V., Pouliot J.J., Zhou T., Lees-Miller S.P., Rasouli-Nia A., Povirk L.F. Conversion of phosphoglycolate to phosphate termini on 3′ overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1. J. Biol. Chem. 277:2002;27162-27168.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27162-27168
    • Inamdar, K.V.1    Pouliot, J.J.2    Zhou, T.3    Lees-Miller, S.P.4    Rasouli-Nia, A.5    Povirk, L.F.6
  • 54
    • 0036373079 scopus 로고    scopus 로고
    • Kinetic studies of human tyrosyl-DNA phosphodiesterase, an enzyme in the topoisomerase I DNA repair pathway
    • Cheng T.J., Rey P.G., Poon T., Kan C.C. Kinetic studies of human tyrosyl-DNA phosphodiesterase, an enzyme in the topoisomerase I DNA repair pathway. Eur. J. Biochem. 269:2002;3697-3704.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3697-3704
    • Cheng, T.J.1    Rey, P.G.2    Poon, T.3    Kan, C.C.4
  • 55
    • 0037786682 scopus 로고    scopus 로고
    • A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein
    • Hoss M., Robins P., Naven T.J., Pappin D.J., Sgouros J., Lindahl T. A human DNA editing enzyme homologous to the Escherichia coli DnaQ/MutD protein. EMBO J. 18:1999;3868-3875.
    • (1999) EMBO J. , vol.18 , pp. 3868-3875
    • Hoss, M.1    Robins, P.2    Naven, T.J.3    Pappin, D.J.4    Sgouros, J.5    Lindahl, T.6
  • 56
    • 0035907239 scopus 로고    scopus 로고
    • Excision of 3′ termini by the Trex1 and TREX2 3′→5′ exonucleases. Characterization of the recombinant proteins
    • Mazur D.J., Perrino F.W. Excision of 3′ termini by the Trex1 and TREX2 3′→5′ exonucleases. Characterization of the recombinant proteins. J. Biol. Chem. 276:2001;17022-17029.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17022-17029
    • Mazur, D.J.1    Perrino, F.W.2
  • 57
    • 0034612585 scopus 로고    scopus 로고
    • Substrate specificity of the p53-associated 3′-5′ exonuclease
    • Skalski V., Lin Z.Y., Choi B.Y., Brown K.R. Substrate specificity of the p53-associated 3′-5′ exonuclease. Oncogene. 19:2000;3321-3329.
    • (2000) Oncogene , vol.19 , pp. 3321-3329
    • Skalski, V.1    Lin, Z.Y.2    Choi, B.Y.3    Brown, K.R.4
  • 58
    • 0034850266 scopus 로고    scopus 로고
    • Exonucleolytic proofreading by p53 protein
    • Bakhanashvili M. Exonucleolytic proofreading by p53 protein. Eur. J. Biochem. 268:2001;2047-2054.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2047-2054
    • Bakhanashvili, M.1
  • 59
    • 0032545423 scopus 로고    scopus 로고
    • Werner syndrome protein. II. Characterization of the integral 3′→5′ DNA exonuclease
    • Kamath-Loeb A.S., Shen J.C., Loeb L.A., Fry M. Werner syndrome protein. II. Characterization of the integral 3′→5′ DNA exonuclease. J. Biol. Chem. 273:1998;34145-34150.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34145-34150
    • Kamath-Loeb, A.S.1    Shen, J.C.2    Loeb, L.A.3    Fry, M.4
  • 61
    • 0032560817 scopus 로고    scopus 로고
    • Excision of mismatched nucleotides from DNA: A potential mechanism for enhancing DNA replication fidelity by the wild-type p53 protein
    • Huang P. Excision of mismatched nucleotides from DNA: a potential mechanism for enhancing DNA replication fidelity by the wild-type p53 protein. Oncogene. 17:1998;261-270.
    • (1998) Oncogene , vol.17 , pp. 261-270
    • Huang, P.1
  • 62
    • 0036529624 scopus 로고    scopus 로고
    • Physical and functional interactions of the tumor suppressor protein p53 and DNA polymerase alpha-primase
    • Melle C., Nasheuer H.P. Physical and functional interactions of the tumor suppressor protein p53 and DNA polymerase alpha-primase. Nucl. Acids Res. 30:2002;1493-1499.
    • (2002) Nucl. Acids Res. , vol.30 , pp. 1493-1499
    • Melle, C.1    Nasheuer, H.P.2
  • 63
    • 0019876798 scopus 로고
    • Purification and characterization of an apurinic/apyrimidinic endonuclease from HeLa cells
    • Kane C.M., Linn S. Purification and characterization of an apurinic/apyrimidinic endonuclease from HeLa cells. J. Biol. Chem. 256:1981;3405-3414.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3405-3414
    • Kane, C.M.1    Linn, S.2
  • 65
    • 0037052948 scopus 로고    scopus 로고
    • Reconstitution of the base excision repair pathway for 7,8-dihydro-8-oxoguanine with purified human proteins
    • Pascucci B., Maga G., Hubscher U., Bjoras M., Seeberg E., Hickson I.D., et al. Reconstitution of the base excision repair pathway for 7,8-dihydro-8-oxoguanine with purified human proteins. Nucl. Acids Res. 30:2002;2124-2130.
    • (2002) Nucl. Acids Res. , vol.30 , pp. 2124-2130
    • Pascucci, B.1    Maga, G.2    Hubscher, U.3    Bjoras, M.4    Seeberg, E.5    Hickson, I.D.6
  • 66
    • 0035846899 scopus 로고    scopus 로고
    • XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair
    • Whitehouse C.J., Taylor R.M., Thistlethwaite A., Zhang H., Karimi-Busheri F., Lasko D.D., et al. XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair. Cell. 104:2001;107-117.
    • (2001) Cell , vol.104 , pp. 107-117
    • Whitehouse, C.J.1    Taylor, R.M.2    Thistlethwaite, A.3    Zhang, H.4    Karimi-Busheri, F.5    Lasko, D.D.6
  • 67
    • 0023664684 scopus 로고
    • Oligodeoxynucleotides containing synthetic abasic sites. Model substrates for DNA polymerases and apurinic/apyrimidinic endonucleases
    • Takeshita M., Chang C.N., Johnson F., Will S., Grollman A.P. Oligodeoxynucleotides containing synthetic abasic sites. Model substrates for DNA polymerases and apurinic/apyrimidinic endonucleases. J. Biol. Chem. 262:1987;10171-10179.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10171-10179
    • Takeshita, M.1    Chang, C.N.2    Johnson, F.3    Will, S.4    Grollman, A.P.5


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