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Volumn 41, Issue 10, 2005, Pages 1301-1309

Base excision repair: AP endonucleases and DNA polymerases

Author keywords

[No Author keywords available]

Indexed keywords

DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA POLYMERASE; DNA DIRECTED DNA POLYMERASE; ESCHERICHIA COLI PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 33644800486     PISSN: 00166758     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (3)

References (98)
  • 1
    • 33748696391 scopus 로고    scopus 로고
    • Russian source
  • 2
    • 23744443374 scopus 로고    scopus 로고
    • Base excision repair of DNA: Glycosylases
    • (Korolev V.G. Base Excision Repair of DNA: Glycosylases // Rus. J. Genetics. 2005. V. 41. No 6. P. 583-592.)
    • (2005) Rus. J. Genetics , vol.41 , Issue.6 , pp. 583-592
    • Korolev, V.G.1
  • 3
    • 0025342965 scopus 로고
    • Repair of intrinsic DNA lesions
    • Lindahl T. Repair of intrinsic DNA lesions // Mutat. Res. 1990. V. 238. P. 305-311.
    • (1990) Mutat. Res. , vol.238 , pp. 305-311
    • Lindahl, T.1
  • 4
    • 0025120572 scopus 로고
    • Enzymology of AP endonucleases
    • Doetsch P., Cunningham R. Enzymology of AP endonucleases // Mutat. Res. 1990. V. 236. P. 173-201.
    • (1990) Mutat. Res. , vol.236 , pp. 173-201
    • Doetsch, P.1    Cunningham, R.2
  • 5
    • 0034675927 scopus 로고    scopus 로고
    • Repair of chromosomal abasic sites in vivo involves at least three different repair pathways
    • Otterlei M., Kavli B., Standal R. et al. Repair of chromosomal abasic sites in vivo involves at least three different repair pathways // EMBO J. 2000. V. 19. P. 5542-5551.
    • (2000) EMBO J. , vol.19 , pp. 5542-5551
    • Otterlei, M.1    Kavli, B.2    Standal, R.3
  • 6
    • 0019955287 scopus 로고
    • An enzyme activity from Escherichia coli that attacks single-stranded deoxyribopolymers and single-stranded deoxyribonucleic acid containing apyrimidine sites
    • Bonura T., Schultz R., Friedberg E.C. An enzyme activity from Escherichia coli that attacks single-stranded deoxyribopolymers and single-stranded deoxyribonucleic acid containing apyrimidine sites // Biochem. 1982. V. 21. P. 2548-2556.
    • (1982) Biochem. , vol.21 , pp. 2548-2556
    • Bonura, T.1    Schultz, R.2    Friedberg, E.C.3
  • 7
    • 0018241635 scopus 로고
    • Purification and properties of a Bacillus subtilis endonuclease specific for apurinic sites in DNA
    • Inone T., Kada T. Purification and properties of a Bacillus subtilis endonuclease specific for apurinic sites in DNA // J. Biol. Chem. 1978. V. 253. P. 8559-8563.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8559-8563
    • Inone, T.1    Kada, T.2
  • 8
    • 0017701231 scopus 로고
    • A new endonuclease from Escherichia coli acting at apurinic sites in DNA
    • Ljungquist S. A new endonuclease from Escherichia coli acting at apurinic sites in DNA // J. Biol. Chem. 1977. V. 252. P. 2808-2814.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2808-2814
    • Ljungquist, S.1
  • 9
    • 0024094108 scopus 로고
    • Nucleotide sequence of the xth gene of Escherichia coli K-12
    • Saporito S.M., Smith-White B.J., Cunningham R.P. Nucleotide sequence of the xth gene of Escherichia coli K-12 // J. Bacteriol. 1988. V. 170. P. 4542-4547.
    • (1988) J. Bacteriol. , vol.170 , pp. 4542-4547
    • Saporito, S.M.1    Smith-White, B.J.2    Cunningham, R.P.3
  • 10
    • 0016651743 scopus 로고
    • Mutations simultaneously affecting endonuclease II and exonuclease III in Escherichia coli
    • Yajko D.M., Weiss B. Mutations simultaneously affecting endonuclease II and exonuclease III in Escherichia coli // Proc. Natl Acad. Sci. USA. 1975. V. 72. P. 688-692.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 688-692
    • Yajko, D.M.1    Weiss, B.2
  • 11
    • 0017161630 scopus 로고
    • Methyl methane sulfonate-sensitive mutant of Escherichia coli deficient in an endonuclease specific for apurinic sites in deoxyribonucleic acid
    • Ljungquist S., Lindahl T., Howard-Flanders P. Methyl methane sulfonate-sensitive mutant of Escherichia coli deficient in an endonuclease specific for apurinic sites in deoxyribonucleic acid // J. Bacteriol. 1976. V. 126. P. 646-653.
    • (1976) J. Bacteriol. , vol.126 , pp. 646-653
    • Ljungquist, S.1    Lindahl, T.2    Howard-Flanders, P.3
  • 12
    • 0020693158 scopus 로고
    • Escherichia coli xth mutants are hypersensitive to hydrogen peroxide
    • Demple B., Halbrook J., Linn S. Escherichia coli xth mutants are hypersensitive to hydrogen peroxide // J. Bacteriol. 1983. V. 153. P. 1079-1082.
    • (1983) J. Bacteriol. , vol.153 , pp. 1079-1082
    • Demple, B.1    Halbrook, J.2    Linn, S.3
  • 13
    • 0345709944 scopus 로고
    • Loss of an apurinic/apyrimidinic site endonuclease increases the mutagenicity of N-methyl-N′-nitro-nitrosoguanidine to Escherichia coli
    • Foster P.L., Davis E.F. Loss of an apurinic/apyrimidinic site endonuclease increases the mutagenicity of N-methyl-N′-nitro- nitrosoguanidine to Escherichia coli // Proc. Natl Acad. Sci. USA. 1987. V. 84. P. 2891-2895.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2891-2895
    • Foster, P.L.1    Davis, E.F.2
  • 14
    • 0017255036 scopus 로고
    • Endonuclease II of Escherichia coli is exonuclease III
    • Weiss B. Endonuclease II of Escherichia coli is exonuclease III // J. Biol. Chem. 1976. V. 251. P. 1896-1901.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1896-1901
    • Weiss, B.1
  • 15
    • 0021045679 scopus 로고
    • Enzyme action at 3′ termini of ionizing radiation-induced DNA strand breaks
    • Henner W.D., Grunberg S.M., Haseltine W.A. Enzyme action at 3′ termini of ionizing radiation-induced DNA strand breaks // J. Biol. Chem. 1983. V. 258. P. 15198-15205.
    • (1983) J. Biol. Chem. , vol.258 , pp. 15198-15205
    • Henner, W.D.1    Grunberg, S.M.2    Haseltine, W.A.3
  • 17
    • 0006639728 scopus 로고
    • Endonuclease IV of Escherichia coli is induced by paraquat
    • Chan E., Weiss B. Endonuclease IV of Escherichia coli is induced by paraquat // Proc. Natl Acad. Sci. USA. 1987. V. 84. P. 3189-3193.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3189-3193
    • Chan, E.1    Weiss, B.2
  • 19
    • 0028144992 scopus 로고
    • Interactions of Escherichia coli endonuclease IV and exonuclease III with abasic sites in DNA
    • Takeuchi M., Lillis R., Demple B., Takeshita M. Interactions of Escherichia coli endonuclease IV and exonuclease III with abasic sites in DNA // J. Biol. Chem. 1994. V. 269. P. 21907-21914.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21907-21914
    • Takeuchi, M.1    Lillis, R.2    Demple, B.3    Takeshita, M.4
  • 20
    • 0024279593 scopus 로고
    • Yeast DNA diesterase for 3′-fragments of deoxyribose: Purification and physical properties of a repair enzyme for oxidative DNA damage
    • Johnson A.W., Demple B. Yeast DNA diesterase for 3′-fragments of deoxyribose: Purification and physical properties of a repair enzyme for oxidative DNA damage // J. Biol. Chem. 1988. V. 263. P. 18009-18016.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18009-18016
    • Johnson, A.W.1    Demple, B.2
  • 21
    • 0024279616 scopus 로고
    • Yeast DNA 3′-repair diesterase is the major cellular apurinic/apyrimidinic endonuclease: Substrate specificity and kinetics
    • Johnson A.W., Demple B. Yeast DNA 3′-repair diesterase is the major cellular apurinic/apyrimidinic endonuclease: Substrate specificity and kinetics // J. Biol. Chem. 1988. V. 263. P. 18017-18022.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18017-18022
    • Johnson, A.W.1    Demple, B.2
  • 22
    • 0025324303 scopus 로고
    • Yeast structural gene (APN1) for the major apurinic endonuclease: Homology to Escherichia coli endonuclease IV
    • Popoff C., Spira A.I., Johnson A.W., Demple B. Yeast structural gene (APN1) for the major apurinic endonuclease: Homology to Escherichia coli endonuclease IV // Proc. Natl Acad. Sci. USA. 1990. V. 87. P. 4193-4197.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4193-4197
    • Popoff, C.1    Spira, A.I.2    Johnson, A.W.3    Demple, B.4
  • 23
    • 0025864553 scopus 로고
    • Cellular role of yeast Apn1 apurinic endonuclease/3′-diesterase: Repair of oxidative and alkylation DNA damage and control of spontaneous mutation
    • Ramotar D., Popoff S.C., Gralla E.B., Demple B. Cellular role of yeast Apn1 apurinic endonuclease/3′-diesterase: Repair of oxidative and alkylation DNA damage and control of spontaneous mutation // Mol. Cell. Biol. 1991. V. 11. P. 4537-4544.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4537-4544
    • Ramotar, D.1    Popoff, S.C.2    Gralla, E.B.3    Demple, B.4
  • 24
    • 0028133245 scopus 로고
    • Specificity of the mutator caused of deletion of the yeast structural gene (APN1) for the major apurinic endonuclease
    • Kunz B.A., Henson E.S., Roche H. et al. Specificity of the mutator caused of deletion of the yeast structural gene (APN1) for the major apurinic endonuclease // Proc. Natl Acad. Sci. USA. 1994. V. 91. P. 8165-8169.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8165-8169
    • Kunz, B.A.1    Henson, E.S.2    Roche, H.3
  • 25
    • 0025975106 scopus 로고
    • Complementation of DNA repair-deficient Escherichia coli by the yeast Apn1 apurinic/apyrimidinic endonuclease gene
    • Ramotar D., Popoff S.C., Demple B. Complementation of DNA repair-deficient Escherichia coli by the yeast Apn1 apurinic/apyrimidinic endonuclease gene // Mol. Microbiol. 1993. V. 5. P. 149-155.
    • (1993) Mol. Microbiol. , vol.5 , pp. 149-155
    • Ramotar, D.1    Popoff, S.C.2    Demple, B.3
  • 26
    • 0032190633 scopus 로고    scopus 로고
    • Identification of APN2, the Saccharomyces cerevisiae homolog of the major human AP endonuclease HAP1, and its role in the repair of abasic sites
    • Johnson R.E., Torres-Ramos C.A., Izumi T. et al. Identification of APN2, the Saccharomyces cerevisiae homolog of the major human AP endonuclease HAP1, and its role in the repair of abasic sites // Genes Dev. 1998. V. 12. P. 3137-3143.
    • (1998) Genes Dev. , vol.12 , pp. 3137-3143
    • Johnson, R.E.1    Torres-Ramos, C.A.2    Izumi, T.3
  • 27
    • 0032980426 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae ETH1 gene, an inducible homolog of exonuclease III that provides resistance to DNA-damaging agents and limits spontaneous mutagenesis
    • Bennett R.A. The Saccharomyces cerevisiae ETH1 gene, an inducible homolog of exonuclease III that provides resistance to DNA-damaging agents and limits spontaneous mutagenesis // Mol. Cell. Biol. 1999. V. 19. P. 1800-1809.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1800-1809
    • Bennett, R.A.1
  • 28
    • 0034698089 scopus 로고    scopus 로고
    • Apurinic endonuclease activity of yeast Apn2 protein
    • Unk I., Haracska L., Johnson R. E. et al. Apurinic endonuclease activity of yeast Apn2 protein // J. Biol. Chem. 2000. V. 275. P. 22427-22434.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22427-22434
    • Unk, I.1    Haracska, L.2    Johnson, R.E.3
  • 29
    • 0034746231 scopus 로고    scopus 로고
    • 3′-phosphodiesterase and 3′ → 5′ exonuclease activities of yeast Apn2 protein and requirement of these activities for repair of oxidative DNA damage
    • Unk I., Haracska L., Prakash S., Prakash L. 3′-phosphodiesterase and 3′ → 5′ exonuclease activities of yeast Apn2 protein and requirement of these activities for repair of oxidative DNA damage // Mol. Cell. Biol. 2001. V. 21. P. 1656-1661.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1656-1661
    • Unk, I.1    Haracska, L.2    Prakash, S.3    Prakash, L.4
  • 30
    • 1242331845 scopus 로고    scopus 로고
    • The major role of human AP-endonuclease homolog Apn2 in repair of abasic sites in Schizosaccharomyces pombe
    • Ribar B., Izumi T., Mitra S. The major role of human AP-endonuclease homolog Apn2 in repair of abasic sites in Schizosaccharomyces pombe // Nucl. Acids Res. 2004. V. 32. P. 115-126.
    • (2004) Nucl. Acids Res. , vol.32 , pp. 115-126
    • Ribar, B.1    Izumi, T.2    Mitra, S.3
  • 31
    • 0026323008 scopus 로고
    • Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: Definition of 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 family of DNA repair enzymes // Proc. Natl Acad. Sci. USA. 1991. V. 88. P. 11450-11454.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 32
    • 0025936119 scopus 로고
    • Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants
    • Robson C.N., Hickson I.D. Isolation of cDNA clones encoding a human apurinic / apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants // Nucl. Acids Res. 1991. V. 19. P. 5519-5523.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 5519-5523
    • Robson, C.N.1    Hickson, I.D.2
  • 33
    • 0027032179 scopus 로고
    • Human apurinic/apyrimidinic endonuclease gene (APE): Structure and genomic mapping (chromosome 14q 11.2-12)
    • Harrison L., Ascione L., Menninger G. et al. Human apurinic/apyrimidinic endonuclease gene (APE): Structure and genomic mapping (chromosome 14q 11.2-12) // Hum. Mol. Genet. 1992. V. 1. P. 677-680.
    • (1992) Hum. Mol. Genet. , vol.1 , pp. 677-680
    • Harrison, L.1    Ascione, L.2    Menninger, G.3
  • 34
    • 0028596574 scopus 로고
    • A role for the human DNA repair enzyme HAP1 in cellular protection against DNA damaging and hypoxic stress
    • Walker L. J., Graig R.B., Harris A.L., Hickson I.D. A role for the human DNA repair enzyme HAP1 in cellular protection against DNA damaging and hypoxic stress // Nucl. Acids Res. 1994. V. 22. P. 4884-4889.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4884-4889
    • Walker, L.J.1    Graig, R.B.2    Harris, A.L.3    Hickson, I.D.4
  • 35
    • 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. 1991. V. 19. P. 5907-5914.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 5907-5914
    • Chen, D.S.1    Herman, T.2    Demple, B.3
  • 36
    • 0032973211 scopus 로고    scopus 로고
    • Base excision repair of oxidative DNA damage activated by XPG protein
    • Klungland A., Hoss M., Gunz D. et al. Base excision repair of oxidative DNA damage activated by XPG protein // Mol. Cell. 1999. V. 3. P. 33-42.
    • (1999) Mol. Cell. , vol.3 , pp. 33-42
    • Klungland, A.1    Hoss, M.2    Gunz, D.3
  • 37
    • 0029347105 scopus 로고
    • Structure and function of apurinic/apyrimidinic endonucleases
    • Barzilay G., Hickson I.D. Structure and function of apurinic / apyrimidinic endonucleases // BioEssays. 1995. V. 17. P. 713-719.
    • (1995) BioEssays , vol.17 , pp. 713-719
    • Barzilay, G.1    Hickson, I.D.2
  • 38
    • 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. 2002. V. 415. P. 655-659.
    • (2002) Nature , vol.415 , pp. 655-659
    • Chou, K.-M.1    Cheng, Y.-C.2
  • 39
    • 14444274333 scopus 로고    scopus 로고
    • Excision of C-4′-oxidized deoxyribose lesions from double-stranded DNA by human apurinic/apyrimidinic endonuclease (Ape1 protein) and DNA polymerase β
    • Xu Y.-J., Kim E.Y., Demple B. Excision of C-4′-oxidized deoxyribose lesions from double-stranded DNA by human apurinic/apyrimidinic endonuclease (Ape1 protein) and DNA polymerase β // J. Biol. Chem. 1998. V. 273. P. 28837-28844.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28837-28844
    • Xu, Y.-J.1    Kim, E.Y.2    Demple, B.3
  • 40
    • 0030474259 scopus 로고    scopus 로고
    • A unusual mechanism for the major human apurinic/apyrimidinic (AP) endonuclease involving 5′ cleavage of DNA containing a benzene-derived exocyclic adduct in the absence of an AP site
    • Hang B., Chenna A., Fraenkel-Conrat H., Singer B. A unusual mechanism for the major human apurinic/apyrimidinic (AP) endonuclease involving 5′ cleavage of DNA containing a benzene-derived exocyclic adduct in the absence of an AP site // Proc. Natl Acad. Sci. USA. 1996. V. 93. P. 13737-13741.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13737-13741
    • Hang, B.1    Chenna, A.2    Fraenkel-Conrat, H.3    Singer, B.4
  • 41
    • 3142770341 scopus 로고    scopus 로고
    • APE1 is the major 3′-phosphoglycolate activity in human cell extracts
    • Parsons J.L., Dianova I.I., Dianov G.L. APE1 is the major 3′-phosphoglycolate activity in human cell extracts // Nucl. Acids Res. 2004. V. 32. P. 3531-3536.
    • (2004) Nucl. Acids Res. , vol.32 , pp. 3531-3536
    • Parsons, J.L.1    Dianova, I.I.2    Dianov, G.L.3
  • 42
    • 0035837587 scopus 로고    scopus 로고
    • The major human abasic endonuclease: Formation, consequences and repair of abasic lesions in DNA
    • Wilson III D.M., Barsky D. The major human abasic endonuclease: Formation, consequences and repair of abasic lesions in DNA // Mutat. Res. 2001. V. 485. P. 283-307.
    • (2001) Mutat. Res. , vol.485 , pp. 283-307
    • Wilson III, D.M.1    Barsky, D.2
  • 43
    • 0034531986 scopus 로고    scopus 로고
    • A second human protein with homology to the Escherichia coli abasic endonuclease exonuclease III
    • Hadi M.Z., Wilson III D.M. A second human protein with homology to the Escherichia coli abasic endonuclease exonuclease III // Environ. Mol. Mutagen. 2000. V. 36. P. 312-324.
    • (2000) Environ. Mol. Mutagen , vol.36 , pp. 312-324
    • Hadi, M.Z.1    Wilson III, D.M.2
  • 44
    • 0030728449 scopus 로고    scopus 로고
    • The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites
    • Gorman M.A., Morera S., Rothwell D.G. et al. The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites // EMBO J. 1997. V. 16. P. 6548-6558.
    • (1997) EMBO J. , vol.16 , pp. 6548-6558
    • Gorman, M.A.1    Morera, S.2    Rothwell, D.G.3
  • 45
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 DNA repair and coordination
    • Mol C.D., Izumi T., Mitra S., Tainer J.A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 DNA repair and coordination // Nature. 2000. V. 403. P. 451-455.
    • (2000) Nature , vol.403 , pp. 451-455
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 46
    • 0035253515 scopus 로고    scopus 로고
    • Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Ape1) in mammalian base excision repair of an A/GO mismatch
    • Yang H., Clendenin W.M., Wang D. et al. Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic / apyrimidinic endonuclease (Ape1) in mammalian base excision repair of an A/GO mismatch // Nucl. Acids Res. 2001. V. 29. P. 743-752.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 743-752
    • Yang, H.1    Clendenin, W.M.2    Wang, D.3
  • 47
    • 0035869114 scopus 로고    scopus 로고
    • Mechanism of stimulation of the DNA glycosylase activity of hOGG1 by the major human AP endonuclease: Bypass of the AP lyase activity step
    • Vidal A.E., Hikson I.D., Boiteux S., Radicella J.P. Mechanism of stimulation of the DNA glycosylase activity of hOGG1 by the major human AP endonuclease: Bypass of the AP lyase activity step // Nucl. Acids Res. 2001. V. 29. P. 1285-1292.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 1285-1292
    • Vidal, A.E.1    Hikson, I.D.2    Boiteux, S.3    Radicella, J.P.4
  • 48
    • 0035863739 scopus 로고    scopus 로고
    • Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: Potential coordination of the initial steps in base excision repair
    • Hill J.W., Hazra T.K., Izumi T., Mitra S. Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: Potential coordination of the initial steps in base excision repair // Nucl. Acids Res. 2001. V. 29. P. 430-438.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 430-438
    • Hill, J.W.1    Hazra, T.K.2    Izumi, T.3    Mitra, S.4
  • 49
    • 0037049975 scopus 로고    scopus 로고
    • Alternative nucleotide incision repair pathway for oxidative DNA damage
    • Ischenko A.A., Saparbaev M.R. Alternative nucleotide incision repair pathway for oxidative DNA damage // Nature. 2002. V. 415. P. 183-187.
    • (2002) Nature , vol.415 , pp. 183-187
    • Ischenko, A.A.1    Saparbaev, M.R.2
  • 50
    • 1242320312 scopus 로고    scopus 로고
    • The major human endonuclease (Ape1) is involved in the nucleotide incision repair pathway
    • Gros L., Ishchenko A.A., Ide H. et al. The major human endonuclease (Ape1) is involved in the nucleotide incision repair pathway // Nucl. Acids Res. 2004. V. 32. P. 73-81.
    • (2004) Nucl. Acids Res. , vol.32 , pp. 73-81
    • Gros, L.1    Ishchenko, A.A.2    Ide, H.3
  • 51
    • 0027475974 scopus 로고
    • DNA repair synthesis during base excision repair in vitro is catalyzed by DNA polymerase ε and is influenced by DNA polymerases α and δ in Saccharomyces cerevisiae
    • Wang Z., Wu X., Friedberg E.C. DNA repair synthesis during base excision repair in vitro is catalyzed by DNA polymerase ε and is influenced by DNA polymerases α and δ in Saccharomyces cerevisiae // Mol. Cell. Biol. 1993. V. 13. P. 1051-1058.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1051-1058
    • Wang, Z.1    Wu, X.2    Friedberg, E.C.3
  • 52
    • 0028608961 scopus 로고
    • DNA polymerase δ is required for base excision repair of DNA methylation damage in Saccharomyces cerevisiae
    • Blank A., Kim B., Loeb LA. DNA polymerase δ is required for base excision repair of DNA methylation damage in Saccharomyces cerevisiae // Proc. Natl Acad. Sci. USA. 1994. V. 91. P. 9047-9051.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9047-9051
    • Blank, A.1    Kim, B.2    Loeb, L.A.3
  • 53
    • 0027489726 scopus 로고
    • DNA polymerase III is required for DNA repair in Saccharomyces cerevisiae
    • Suszek W., Baranowska H., Zuk J., Jachymczyk W.J. DNA polymerase III is required for DNA repair in Saccharomyces cerevisiae // Curr. Genet. 1993. V. 24. P. 200-204.
    • (1993) Curr. Genet. , vol.24 , pp. 200-204
    • Suszek, W.1    Baranowska, H.2    Zuk, J.3    Jachymczyk, W.J.4
  • 54
    • 0027937623 scopus 로고
    • The yeast Saccharomyces cerevisiae DNA polymerase IV: Possible involvement in double strand breek DNA repair
    • Leem S.-H., Ropp P.A., Sugino A. The yeast Saccharomyces cerevisiae DNA polymerase IV: Possible involvement in double strand breek DNA repair // Nucl. Acids Res. 1994. V. 22. P. 3011-3017.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 3011-3017
    • Leem, S.-H.1    Ropp, P.A.2    Sugino, A.3
  • 55
    • 0027444778 scopus 로고
    • Yeast open reading frame YCR14C encodes a DNA β-polymerase-like enzyme
    • Prasad R., Widen S.G., Singhal R.K. et al. Yeast open reading frame YCR14C encodes a DNA β-polymerase-like enzyme // Nucl. Acids Res. 1994. V. 21. P. 5301-5307.
    • (1994) Nucl. Acids Res. , vol.21 , pp. 5301-5307
    • Prasad, R.1    Widen, S.G.2    Singhal, R.K.3
  • 56
    • 0037193544 scopus 로고    scopus 로고
    • Epistatic analysis of the roles of the RAD27 and POLA gene products in DNA base excision repair in S. cerevisiae
    • McInnis M., O'Neill G., Fossum K., Reagan M.S. Epistatic analysis of the roles of the RAD27 and POLA gene products in DNA base excision repair in S. cerevisiae // DNA Repair. 2002. V. 1. P. 311-315.
    • (2002) DNA Repair. , vol.1 , pp. 311-315
    • McInnis, M.1    O'Neill, G.2    Fossum, K.3    Reagan, M.S.4
  • 57
    • 0033557310 scopus 로고    scopus 로고
    • Relationships between yeast Rad27 and Apn1 in response to apurinic/apyrimidinic (AP) sites in DNA
    • Wu X., Wang Z. Relationships between yeast Rad27 and Apn1 in response to apurinic/apyrimidinic (AP) sites in DNA // Nucl. Acids Res. 1999. V. 27. P. 956-962.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 956-962
    • Wu, X.1    Wang, Z.2
  • 58
    • 0028335180 scopus 로고
    • Functional domains within FEN-1 and RAD2 define a family of structure-specific endonucleases: Implications for nucleotide excision repair
    • Harrington J.J., Lieber M.R. Functional domains within FEN-1 and RAD2 define a family of structure-specific endonucleases: Implications for nucleotide excision repair // Genes Dev. 1994. V. 8. P. 1344-1355.
    • (1994) Genes Dev. , vol.8 , pp. 1344-1355
    • Harrington, J.J.1    Lieber, M.R.2
  • 59
    • 0001160962 scopus 로고    scopus 로고
    • Purification and characterization of the DNA polymerase alpha associated exonuclease: The RTH1 gene product
    • Zhu F.X., Biswas E.E., Biswas S.B. Purification and characterization of the DNA polymerase alpha associated exonuclease: the RTH1 gene product // Biochemistry. 1997. V. 36. P. 5947-5954.
    • (1997) Biochemistry , vol.36 , pp. 5947-5954
    • Zhu, F.X.1    Biswas, E.E.2    Biswas, S.B.3
  • 60
    • 33748703441 scopus 로고    scopus 로고
    • Russian source
  • 61
    • 0034201604 scopus 로고    scopus 로고
    • RAD29 and RAD31, new genes of yeast Saccharomyces cerevisiae involved in DNA repair control: Isolation and genetic characterization of mutants
    • (Kozhina T.N., Kozhin S.A., Latypov V.F., Korolev V.G. RAD29 and RAD31, new genes of yeast Saccharomyces cerevisiae involved in DNA repair control: Isolation and genetic characterization of mutants // Rus. J. Genetics. 2000. V. 36. No 6. P. 627-633.)
    • (2000) Rus. J. Genetics , vol.36 , Issue.6 , pp. 627-633
    • Kozhina, T.N.1    Kozhin, S.A.2    Latypov, V.F.3    Korolev, V.G.4
  • 62
    • 33748700641 scopus 로고    scopus 로고
    • Russian source
  • 63
    • 22244457728 scopus 로고    scopus 로고
    • RAD29 and RAD31, new genes of the yeast Saccharomyces cerevisiae involved in DNA repair control: Determining possible functions of these genes
    • (Kozhin S.A., Kozhina T.N., Latypov V.F., Korolev V.G. RAD29 and RAD31, new genes of the yeast Saccharomyces cerevisiae involved in DNA repair control: Determining possible functions of these genes // Rus. J. Genetics. 2000. V. 36. No 8. P. 845-852.)
    • (2000) Rus. J. Genetics , vol.36 , Issue.8 , pp. 845-852
    • Kozhin, S.A.1    Kozhina, T.N.2    Latypov, V.F.3    Korolev, V.G.4
  • 64
    • 0036707526 scopus 로고    scopus 로고
    • Stimulation of 3′ → 5′ exonuclease and 3′-phosphodiesterase activities of yeast Apn2 by proliferating cell nuclear antigen
    • Unk I., Haracska L., Gomes X.V. et al. Stimulation of 3′ → 5′ exonuclease and 3′-phosphodiesterase activities of yeast Apn2 by proliferating cell nuclear antigen // Mol. Cell. Biol. 2002. V. 22. P. 6480-6486.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6480-6486
    • Unk, I.1    Haracska, L.2    Gomes, X.V.3
  • 65
    • 0030030379 scopus 로고    scopus 로고
    • Requirement of mammalian DNA polymerase beta in base excision repair
    • Sobol R.W., Horton J.K., Kuh R. et al. Requirement of mammalian DNA polymerase beta in base excision repair // Nature. 1996. V. 379. P. 183-186.
    • (1996) Nature , vol.379 , pp. 183-186
    • Sobol, R.W.1    Horton, J.K.2    Kuh, R.3
  • 66
    • 0026589375 scopus 로고
    • Generation of single-nucleotide repair patches following excision of uracil residues from DNA
    • Dianov G., Price A., Lindahl T. Generation of single-nucleotide repair patches following excision of uracil residues from DNA // Mol. Cell. Biol. 1992. V. 12. P. 1605-1612.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1605-1612
    • Dianov, G.1    Price, A.2    Lindahl, T.3
  • 67
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision repair: Reconstitution with purified proteins and requirement for DNAase IV (FEN1)
    • Klungland A., Lindahl T. Second pathway for completion of human DNA base excision repair: Reconstitution with purified proteins and requirement for DNAase IV (FEN1) // EMBO J. 1997. V. 16. P. 3341-3348.
    • (1997) EMBO J. , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 68
    • 0029873178 scopus 로고    scopus 로고
    • Two pathways for base excision repair in mammalian cells
    • Frosina G., Fortini P., Rossi O. et al. Two pathways for base excision repair in mammalian cells // J. Biol. Chem. 1996. V. 271. P. 9573-9578.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9573-9578
    • Frosina, G.1    Fortini, P.2    Rossi, O.3
  • 69
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair
    • Matsumoto Y., Kim K. Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair // Science. 1995. V. 269. P. 699-702.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 70
    • 0025088519 scopus 로고
    • Studies of the domain structure of mammalian DNA polymerase β: Identification of a discrete template binding domain
    • Kumar A., Widen S.G., Williams K.R. et al. Studies of the domain structure of mammalian DNA polymerase β: Identification of a discrete template binding domain // J. Biol. Chem. 1990. V. 265. P. 2124-2131.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2124-2131
    • Kumar, A.1    Widen, S.G.2    Williams, K.R.3
  • 71
    • 0025333457 scopus 로고
    • Identification and properties of the catalitic domain of mammalian DNA polymerase beta
    • Kumar A., Abbotts J., Karawya E., Wilson S.H. Identification and properties of the catalitic domain of mammalian DNA polymerase beta // Biochemistry. 1990. V. 29. P. 7156-7159.
    • (1990) Biochemistry , vol.29 , pp. 7156-7159
    • Kumar, A.1    Abbotts, J.2    Karawya, E.3    Wilson, S.H.4
  • 72
    • 0034654379 scopus 로고    scopus 로고
    • Neonatal lethality with abnormal neurogenesis in mice deficient in DNA polymerase
    • Sugo N., Aratani Y., Nagashima Y. et al. Neonatal lethality with abnormal neurogenesis in mice deficient in DNA polymerase // EMBO J. 2000. V. 19. P. 1397-1404.
    • (2000) EMBO J. , vol.19 , pp. 1397-1404
    • Sugo, N.1    Aratani, Y.2    Nagashima, Y.3
  • 73
    • 0034663530 scopus 로고    scopus 로고
    • DNA polymerase β is required for efficient DNA strand break repair induced by methyl methanesulfonate but not by hydrogen peroxide
    • Fortini P., Pascucci B., Belisario F., Dogliotti E. DNA polymerase β is required for efficient DNA strand break repair induced by methyl methanesulfonate but not by hydrogen peroxide // Nucl. Acids Res. 2000. V. 28. P. 3040-3046.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 3040-3046
    • Fortini, P.1    Pascucci, B.2    Belisario, F.3    Dogliotti, E.4
  • 74
    • 0037076434 scopus 로고    scopus 로고
    • Mutations associated with base excision repair deficiency and methylation-induced genotoxic strass
    • Sobol R.W., Watson D.E., Nakamura J. et al. Mutations associated with base excision repair deficiency and methylation-induced genotoxic strass // Proc. Natl Acad. Sci. USA. 2002. V. 99. P. 6860-6865.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6860-6865
    • Sobol, R.W.1    Watson, D.E.2    Nakamura, J.3
  • 75
    • 0028966181 scopus 로고
    • DNA polymerase β conducts the gap-filling step in uracil-initiated base excision repair in a bovin testis nuclear extract
    • Singhal R.K., Prasad R., Wilson S.H. DNA polymerase β conducts the gap-filling step in uracil-initiated base excision repair in a bovin testis nuclear extract // J. Biol. Chem. 1995. V. 270. P. 949-957.
    • (1995) J. Biol. Chem. , vol.270 , pp. 949-957
    • Singhal, R.K.1    Prasad, R.2    Wilson, S.H.3
  • 76
    • 0030018848 scopus 로고    scopus 로고
    • Specific interaction of DNA polymerase beta and DNA ligase 1 in a multiprotein base excision repair complex from bovine testis
    • Prasad R., Singhal R.K., Srivastava D.K. et al. Specific interaction of DNA polymerase beta and DNA ligase 1 in a multiprotein base excision repair complex from bovine testis // J. Biol. Chem. 1996. V. 271. P. 16000-16007.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16000-16007
    • Prasad, R.1    Singhal, R.K.2    Srivastava, D.K.3
  • 77
    • 0035803497 scopus 로고    scopus 로고
    • DNA polymerase β is the major dRP lyase involved in repair of oxidative base lesions in DNA by mammalian cell extracts
    • Allison S.L., Dianova I.I., Dianov G.L. DNA polymerase β is the major dRP lyase involved in repair of oxidative base lesions in DNA by mammalian cell extracts // EMBO J. 2001. V. 20. P. 6919-6926.
    • (2001) EMBO J. , vol.20 , pp. 6919-6926
    • Allison, S.L.1    Dianova, I.I.2    Dianov, G.L.3
  • 78
    • 0034697012 scopus 로고    scopus 로고
    • Single nucleotide patch base excision repair is the major pathway for removal of thymine glycol from DNA in human cell extracts
    • Dianov G.L., Thybo T., Dianova I.I. et al. Single nucleotide patch base excision repair is the major pathway for removal of thymine glycol from DNA in human cell extracts // J. Biol. Chem. 2000. V. 275. P. 11809-11813.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11809-11813
    • Dianov, G.L.1    Thybo, T.2    Dianova, I.I.3
  • 79
    • 0035811262 scopus 로고    scopus 로고
    • Enhancement of OGG1 protein AP lyase activity by increase of APEX protein
    • Saitoh T., Shinmura K., Yamaguchi S. et al. Enhancement of OGG1 protein AP lyase activity by increase of APEX protein // Mutat. Res. 2001. V. 486. P. 31-40.
    • (2001) Mutat. Res. , vol.486 , pp. 31-40
    • Saitoh, T.1    Shinmura, K.2    Yamaguchi, S.3
  • 80
    • 0035869014 scopus 로고    scopus 로고
    • Human DNA polymerase β initiates DNA synthesis during long-patch repair of reduced AP sites in DNA
    • Podlucsky A.J., Dianova I.I., Podust V.N. et al. Human DNA polymerase β initiates DNA synthesis during long-patch repair of reduced AP sites in DNA // EMBO J. 2001. V. 20. P. 1477-1482.
    • (2001) EMBO J. , vol.20 , pp. 1477-1482
    • Podlucsky, A.J.1    Dianova, I.I.2    Podust, V.N.3
  • 81
    • 0033553510 scopus 로고    scopus 로고
    • Role of DNA polymerase β in the excision step of long patch mammalian base excision repair
    • Dianov G. L., Prasad R., Willson S.H., Bohr V.A. Role of DNA polymerase β in the excision step of long patch mammalian base excision repair // J. Biol. Chem. 1999. V. 274. P. 13741-13743.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13741-13743
    • Dianov, G.L.1    Prasad, R.2    Willson, S.H.3    Bohr, V.A.4
  • 82
    • 0032539979 scopus 로고    scopus 로고
    • Different DNA polymerazes are involved in the short- and long-patch base excision repair in mammalian cells
    • Fortini P., Pascucci B., Parlanti E. et al. Different DNA polymerazes are involved in the short- and long-patch base excision repair in mammalian cells // Biochemistry. 1998. V. 37. P. 3575-3580.
    • (1998) Biochemistry , vol.37 , pp. 3575-3580
    • Fortini, P.1    Pascucci, B.2    Parlanti, E.3
  • 83
    • 0342787062 scopus 로고    scopus 로고
    • Base-excision repair initiation revealed by crystal structures and DNA-binding kinetics of human uracil-DNA glycosylase bound to DNA
    • Parikh S.S., Mol C.D., Slupphang G. et al. Base-excision repair initiation revealed by crystal structures and DNA-binding kinetics of human uracil-DNA glycosylase bound to DNA // EMBO J. 1998. V. 17. P. 5414-5426.
    • (1998) EMBO J. , vol.17 , pp. 5414-5426
    • Parikh, S.S.1    Mol, C.D.2    Slupphang, G.3
  • 84
    • 0032951710 scopus 로고    scopus 로고
    • Human thymine DNA glycosylase binds to apurinic sites in DNA but its displaced by human apurinic endonuclease 1
    • Waters T.R., Gallinari P., Jiricny J., Swann P.F. Human thymine DNA glycosylase binds to apurinic sites in DNA but its displaced by human apurinic endonuclease 1 // J. Biol. Chem. 1999. V. 274. P. 67-74.
    • (1999) J. Biol. Chem. , vol.274 , pp. 67-74
    • Waters, T.R.1    Gallinari, P.2    Jiricny, J.3    Swann, P.F.4
  • 85
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathways
    • Bennett R.A.O., Willson III D.M., Wong D., Demple B. Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathways // Proc. Natl Acad. Sci. USA. 1997. V. 94. P. 7166-7169.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7166-7169
    • Bennett, R.A.O.1    Willson III, D.M.2    Wong, D.3    Demple, B.4
  • 86
    • 0036828697 scopus 로고    scopus 로고
    • AP endonuclease 1 coordinates flap endonuclease 1 and DNA ligase 1 activity in long patch base excision repair
    • Ranalli T.A., Tom S., Bambara R.A. AP endonuclease 1 coordinates flap endonuclease 1 and DNA ligase 1 activity in long patch base excision repair // J. Biol. Chem. 2002. V. 277. P. 41715-41724.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41715-41724
    • Ranalli, T.A.1    Tom, S.2    Bambara, R.A.3
  • 87
    • 0035940441 scopus 로고    scopus 로고
    • Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair
    • Dianova I.I., Bohr V.A., Dianov G.L. Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair // Biochemistry. 2001. V. 40. P. 12639-12644.
    • (2001) Biochemistry , vol.40 , pp. 12639-12644
    • Dianova, I.I.1    Bohr, V.A.2    Dianov, G.L.3
  • 88
    • 0032538561 scopus 로고    scopus 로고
    • Replication protein a stimulates long patch DNA base excision repair
    • DeMott M.S., Zigman S., Bambara R.A. Replication protein A stimulates long patch DNA base excision repair // J. Biol. Chem. 1998. V. 273. P. 27492-27498.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27492-27498
    • DeMott, M.S.1    Zigman, S.2    Bambara, R.A.3
  • 89
    • 0034635403 scopus 로고    scopus 로고
    • FEN1 stimulation of DNA polymerase β an excision step in mammalian long patch base excision repair
    • Prasad R., Dianov G.L., Bohr V.A., Wilson S.H. FEN1 stimulation of DNA polymerase β an excision step in mammalian long patch base excision repair // J. Biol. Chem. 2000. V. 275. P. 4460-4466.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4460-4466
    • Prasad, R.1    Dianov, G.L.2    Bohr, V.A.3    Wilson, S.H.4
  • 90
    • 0035009313 scopus 로고    scopus 로고
    • Mammalian DNA single-strand break repair: An X-ra(y)ted affair
    • Caldecott K.W. Mammalian DNA single-strand break repair: an X-ra(y)ted affair // Bioessays. 2001. V. 23. P. 447-455.
    • (2001) Bioessays , vol.23 , pp. 447-455
    • Caldecott, K.W.1
  • 91
    • 0242582870 scopus 로고    scopus 로고
    • Role of XRCC1 in the coordination and stimulation of oxidative DNA damage repair initiated by the DNA glycosylase hOGG1
    • Marsin S., Vidal A.E., Sossou M. et al. Role of XRCC1 in the coordination and stimulation of oxidative DNA damage repair initiated by the DNA glycosylase hOGG1 // J. Biol. Chem. 2003. V. 278. P. 44068-44074.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44068-44074
    • Marsin, S.1    Vidal, A.E.2    Sossou, M.3
  • 92
    • 0035890069 scopus 로고    scopus 로고
    • XRCC1 coordinates the initial and late stages of DNA abasic site repair throuth protein-protein interactions
    • Vidal A.E., Boiteux S., Hickson I.D., Radicella J.P. XRCC1 coordinates the initial and late stages of DNA abasic site repair throuth protein-protein interactions // EMBO J. 2001. V. 20. P. 6530-6539.
    • (2001) EMBO J. , vol.20 , pp. 6530-6539
    • Vidal, A.E.1    Boiteux, S.2    Hickson, I.D.3    Radicella, J.P.4
  • 93
    • 0034656991 scopus 로고    scopus 로고
    • Domain specific interaction in the XRCC1-DNA polymerase β complex
    • Marintchev A., Robertson A., Dimitriadis E.K. et al. Domain specific interaction in the XRCC1-DNA polymerase β complex // Nucl. Acids Res. 2000. V. 28. P. 2049-2059.
    • (2000) Nucl. Acids Res. , vol.28 , pp. 2049-2059
    • Marintchev, A.1    Robertson, A.2    Dimitriadis, E.K.3
  • 94
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase β and the XRCC1 protein
    • Kubata Y., Nash R.A., Klungland A. et al. Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase β and the XRCC1 protein // EMBO J. 1996. V. 15. P. 6662-6670.
    • (1996) EMBO J. , vol.15 , pp. 6662-6670
    • Kubata, Y.1    Nash, R.A.2    Klungland, A.3
  • 95
    • 0030863307 scopus 로고    scopus 로고
    • Involvement of XPCC1 and DNA ligase III gene products in DNA base excision repair
    • Cappelli E., Taylor R., Cevasco M. et al. Involvement of XPCC1 and DNA ligase III gene products in DNA base excision repair // J. Biol. Chem. 1997. V. 272. P. 23970-23975.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23970-23975
    • Cappelli, E.1    Taylor, R.2    Cevasco, M.3
  • 96
    • 0034720734 scopus 로고    scopus 로고
    • Base excision repair is impaired in mammalian cells lacking poly(ADP-ribose) polymerase-1
    • Dantzer F., de la Rubia G., Menissier-de Murcia J. et al. Base excision repair is impaired in mammalian cells lacking poly(ADP-ribose) polymerase-1 // Biochemistry. 1999. V. 39. P. 7559-7569.
    • (1999) Biochemistry , vol.39 , pp. 7559-7569
    • Dantzer, F.1    De La Rubia, G.2    Menissier-De Murcia, J.3
  • 97
    • 0029957245 scopus 로고    scopus 로고
    • XRCC1 polypeptide interacts with DNA polymerase β and possible poly(ADP-ribose) polymerase and DNA ligase III is a novel molecular "nick-sensor" in vitro
    • Caldecott K.W., Aoufouchi S., Johnson P., Shall S. XRCC1 polypeptide interacts with DNA polymerase β and possible poly(ADP-ribose) polymerase and DNA ligase III is a novel molecular "nick-sensor" in vitro // Nucl. Acids Res. 1996. V. 24. P. 4387-4394.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 4387-4394
    • Caldecott, K.W.1    Aoufouchi, S.2    Johnson, P.3    Shall, S.4
  • 98
    • 0041386129 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase in base excision repair: Always engaged, but not essential for DNA damage processing
    • Allison S.L., Dianova I.I., Dianov G.L. Poly(ADP-ribose) polymerase in base excision repair: Always engaged, but not essential for DNA damage processing // Acta Biochem. Polonica. 2003. V. 50. P. 169-179.
    • (2003) Acta Biochem. Polonica , vol.50 , pp. 169-179
    • Allison, S.L.1    Dianova, I.I.2    Dianov, G.L.3


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