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Volumn 32, Issue 18, 2004, Pages 5486-5498

Repair of U/G and U/A in DNA by UNG2-associated repair complexes takes place predominantly by short-patch repair both in proliferating and growth-arrested cells

Author keywords

[No Author keywords available]

Indexed keywords

CYCLINE; DNA; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA DIRECTED DNA POLYMERASE BETA; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; PROTEIN ANTIBODY; URACIL DNA GLYCOSYLTRANSFERASE; APEX1 PROTEIN, HUMAN; DNA BINDING PROTEIN; DNA GLYCOSYLTRANSFERASE; SMUG1 PROTEIN, HUMAN; UNG2 PROTEIN, HUMAN; URACIL; URACIL DNA GLYCOSIDASE; X RAY REPAIR CROSS COMPLEMENTING PROTEIN 1; X-RAY REPAIR CROSS COMPLEMENTING PROTEIN 1;

EID: 6044230603     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh872     Document Type: Article
Times cited : (96)

References (66)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl,T. (1993) Instability and decay of the primary structure of DNA. Nature, 362, 709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 2
    • 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., Skjelbred,C., Bharati,S. and Krokan,H.E. (2000) Repair of chromosomal abasic sites in vivo involves at least three different repair pathways. EMBO J., 19, 5542-5551.
    • (2000) EMBO J. , vol.19 , pp. 5542-5551
    • Otterlei, M.1    Kavli, B.2    Standal, R.3    Skjelbred, C.4    Bharati, S.5    Krokan, H.E.6
  • 3
    • 0345379628 scopus 로고    scopus 로고
    • Phenotypic change caused by transcriptional bypass of uracil in nondividing cells
    • Viswanathan,A., You,H.J. and Doetsch,P.W. (1999) Phenotypic change caused by transcriptional bypass of uracil in nondividing cells. Science, 284, 159-162.
    • (1999) Science , vol.284 , pp. 159-162
    • Viswanathan, A.1    You, H.J.2    Doetsch, P.W.3
  • 4
    • 0025156152 scopus 로고
    • The specific binding of nuclear protein(s) to the cAMP responsive element (CRE) sequence (TGACGTCA) is reduced by the misincorporation of U and increased by the deamination of C
    • Verri,A., Mazzarello,P., Biamonti,G., Spadari,S. and Focher,F. (1990) The specific binding of nuclear protein(s) to the cAMP responsive element (CRE) sequence (TGACGTCA) is reduced by the misincorporation of U and increased by the deamination of C. Nucleic Acids Res., 18, 5775-5780.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5775-5780
    • Verri, A.1    Mazzarello, P.2    Biamonti, G.3    Spadari, S.4    Focher, F.5
  • 5
    • 0041474807 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase: A dual role in class-switch recombination and somatic hypermutation
    • Durandy,A. (2003) Activation-induced cytidine deaminase: a dual role in class-switch recombination and somatic hypermutation. Eur. J. Immunol., 33, 2069-2073.
    • (2003) Eur. J. Immunol. , vol.33 , pp. 2069-2073
    • Durandy, A.1
  • 6
    • 0037115911 scopus 로고    scopus 로고
    • Uracil in DNA-occurrence, consequences and repair
    • Krokan,H.E., Drablos,F. and Slupphaug,G. (2002) Uracil in DNA-occurrence, consequences and repair. Oncogene, 21, 8935-8948.
    • (2002) Oncogene , vol.21 , pp. 8935-8948
    • Krokan, H.E.1    Drablos, F.2    Slupphaug, G.3
  • 7
    • 18644363009 scopus 로고    scopus 로고
    • hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup
    • Kavli,B., Sundheim,O., Akbari,M., Otterlei,M., Nilsen,H., Skorpen,F., Aas,P.A., Hagen,L., Krokan,H.E. and Slupphaug,G. (2002) hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup. J. Biol. Chem., 277, 39926-39936.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39926-39936
    • Kavli, B.1    Sundheim, O.2    Akbari, M.3    Otterlei, M.4    Nilsen, H.5    Skorpen, F.6    Aas, P.A.7    Hagen, L.8    Krokan, H.E.9    Slupphaug, G.10
  • 8
    • 0030841051 scopus 로고    scopus 로고
    • Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene
    • Nilsen,H., Otterlei,M., Haug,T., Solum,K., Nagelhus,T.A., Skorpen,F. and Krokan,H.E. (1997) Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene. Nucleic Acids Res., 25, 750-755.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 750-755
    • Nilsen, H.1    Otterlei, M.2    Haug, T.3    Solum, K.4    Nagelhus, T.A.5    Skorpen, F.6    Krokan, H.E.7
  • 9
    • 0032213289 scopus 로고    scopus 로고
    • Human mitochondrial uracil-DNA glycosylase preform (UNG1) is processed to two forms one of which is resistant to inhibition by AP sites
    • Bharati,S., Krokan,H.E., Kristiansen,L., Otterlei,M. and Slupphaug,G. (1998) Human mitochondrial uracil-DNA glycosylase preform (UNG1) is processed to two forms one of which is resistant to inhibition by AP sites. Nucleic Acids Res., 26, 4953-4959.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4953-4959
    • Bharati, S.1    Krokan, H.E.2    Kristiansen, L.3    Otterlei, M.4    Slupphaug, G.5
  • 10
    • 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., Wilson,S.H. and Bohr,V.A. (1999) Role of DNA polymerase β in the excision step of long patch mammalian base excision repair. J. Biol. Chem., 274, 13741-13743.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13741-13743
    • Dianov, G.L.1    Prasad, R.2    Wilson, S.H.3    Bohr, V.A.4
  • 11
    • 0034635403 scopus 로고    scopus 로고
    • FEN1 stimulation of DNA polymerase β mediates an excision step in mammalian long patch base excision repair
    • Prasad,R., Dianov,G.L., Bohr,V.A. and Wilson,S.H. (2000) FEN1 stimulation of DNA polymerase β mediates an excision step in mammalian long patch base excision repair. J. Biol. Chem., 275, 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
  • 12
    • 0242268065 scopus 로고    scopus 로고
    • Mammalian DNA base excision repair proteins: Their interactions and role in repair of oxidative DNA damage
    • Izumi,T., Wiederhold,L.R., Roy,G., Roy,R., Jaiswal,A., Bhakat,K.K., Mitra,S. and Hazra,T.K. (2003) Mammalian DNA base excision repair proteins: their interactions and role in repair of oxidative DNA damage. Toxicology, 193, 43-65.
    • (2003) Toxicology , vol.193 , pp. 43-65
    • Izumi, T.1    Wiederhold, L.R.2    Roy, G.3    Roy, R.4    Jaiswal, A.5    Bhakat, K.K.6    Mitra, S.7    Hazra, T.K.8
  • 14
    • 1642473885 scopus 로고    scopus 로고
    • RNA polymerase II transcription apparatus in Schizosaccharomyces pombe
    • Mitsuzawa,H. and Ishihama,A. (2004) RNA polymerase II transcription apparatus in Schizosaccharomyces pombe. Curr. Genet., 44, 287-294.
    • (2004) Curr. Genet. , vol.44 , pp. 287-294
    • Mitsuzawa, H.1    Ishihama, A.2
  • 15
    • 0034655991 scopus 로고    scopus 로고
    • BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures
    • Wang,Y., Cortez,D., Yazdi,P., Neff,N., Elledge,S.J. and Qin,J. (2000) BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures. Genes Dev. 14, 927-939.
    • (2000) Genes Dev. , vol.14 , pp. 927-939
    • Wang, Y.1    Cortez, D.2    Yazdi, P.3    Neff, N.4    Elledge, S.J.5    Qin, J.6
  • 17
    • 0030801529 scopus 로고    scopus 로고
    • Isolation of human complexes proficient in nucleotide excision repair
    • He,Z. and Ingles,C.J. (1997) Isolation of human complexes proficient in nucleotide excision repair. Nucleic Acids Res., 25, 1136-1141.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1136-1141
    • He, Z.1    Ingles, C.J.2
  • 18
    • 0035102950 scopus 로고    scopus 로고
    • Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome
    • Araujo,S.J., Nigg,E.A. and Wood,R.D. (2001) Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome. Mol. Cell. Biol., 21, 2281-2291.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2281-2291
    • Araujo, S.J.1    Nigg, E.A.2    Wood, R.D.3
  • 19
    • 0040241960 scopus 로고    scopus 로고
    • Protein complexes in nucleotide excision repair
    • Araujo,S.J. and Wood,R.D. (1999) Protein complexes in nucleotide excision repair. Mutat. Res., 435, 23-33.
    • (1999) Mutat. Res. , vol.435 , pp. 23-33
    • Araujo, S.J.1    Wood, R.D.2
  • 20
    • 0030018848 scopus 로고    scopus 로고
    • Specific interaction of DNA polymerase β and DNA ligase I in a multiprotein base exision repair complex from bovine testis
    • Prasad,R., Singhal,R.K., Srivastava,D.K., Molina,J.T., Tomkinson,A.E. and Wilson,S.H. (1996) Specific interaction of DNA polymerase β and DNA ligase I in a multiprotein base exision repair complex from bovine testis. J. Biol. Chem., 271, 16000-16007.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16000-16007
    • Prasad, R.1    Singhal, R.K.2    Srivastava, D.K.3    Molina, J.T.4    Tomkinson, A.E.5    Wilson, S.H.6
  • 21
    • 0030996226 scopus 로고    scopus 로고
    • A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A
    • Nagelhus,T.A., Haug,T., Singh,K.K., Keshav,K.F., Skorpen,F., Otterlei,M., Bharati,S., Lindmo,T., Benichou,S., Benarous,R. et al. (1997) A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A. J. Biol. Chem., 272, 6561-6566.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6561-6566
    • Nagelhus, T.A.1    Haug, T.2    Singh, K.K.3    Keshav, K.F.4    Skorpen, F.5    Otterlei, M.6    Bharati, S.7    Lindmo, T.8    Benichou, S.9    Benarous, R.10
  • 23
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): A dancer with many partners
    • Maga,G. and Hübscher,U. (2003) Proliferating cell nuclear antigen (PCNA): a dancer with many partners. J. Cell Sci., 116, 3051-3060.
    • (2003) J. Cell Sci. , vol.116 , pp. 3051-3060
    • Maga, G.1    Hübscher, U.2
  • 25
    • 0033777562 scopus 로고    scopus 로고
    • The puzzle of PCNA's many partners
    • Warbrick,E. (2000) The puzzle of PCNA's many partners. Bioessays, 22, 997-1006.
    • (2000) Bioessays , vol.22 , pp. 997-1006
    • Warbrick, E.1
  • 27
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase β and the XRCC1 protein
    • Kubota,Y., Nash,R.A., Klungland,A., Schar,P., Barnes,D.E. and Lindahl,T. (1996) Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase β and the XRCC1 protein. EMBO J., 15, 6662-6670.
    • (1996) EMBO J. , vol.15 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schar, P.4    Barnes, D.E.5    Lindahl, T.6
  • 28
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway
    • Bennett,R.A., Wilson,D.M., III, Wong,D. and Demple,B. (1997) Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway. Proc. Natl Acad. Sci. USA, 94, 7166-7169.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7166-7169
    • Bennett, R.A.1    Wilson III, D.M.2    Wong, D.3    Demple, B.4
  • 30
    • 0031844311 scopus 로고    scopus 로고
    • XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
    • Masson,M., Niedergang,C., Schreiber,V., Muller,S., Menissier-de Murcia,J. and de Murcia,G. (1998) XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol. Cell. Biol., 18, 3563-3571.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3563-3571
    • Masson, M.1    Niedergang, C.2    Schreiber, V.3    Muller, S.4    Menissier-de Murcia, J.5    de Murcia, G.6
  • 33
    • 0041378046 scopus 로고    scopus 로고
    • XRCC1 and DNA strand break repair
    • Caldecott,K.W. (2003) XRCC1 and DNA strand break repair. DNA Repair (Amst.), 2, 955-969.
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 955-969
    • Caldecott, K.W.1
  • 34
    • 0032604883 scopus 로고    scopus 로고
    • In vitro base excision repair assay using mammalian cell extracts
    • Frosina,G., Cappelli,E., Fortini,P. and Dogliotti,E. (1999) In vitro base excision repair assay using mammalian cell extracts. Methods Mol. Biol., 113, 301-315.
    • (1999) Methods Mol. Biol. , vol.113 , pp. 301-315
    • Frosina, G.1    Cappelli, E.2    Fortini, P.3    Dogliotti, E.4
  • 35
    • 0028933306 scopus 로고
    • Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase
    • Slupphaug,G., Eftedal,I., Kavli,B., Bharati,S., Helle,N.M., Haug,T., Levine,D.W. and Krokan,H.E. (1995) Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase. Biochemistry, 34, 128-138.
    • (1995) Biochemistry , vol.34 , pp. 128-138
    • Slupphaug, G.1    Eftedal, I.2    Kavli, B.3    Bharati, S.4    Helle, N.M.5    Haug, T.6    Levine, D.W.7    Krokan, H.E.8
  • 37
    • 0026559099 scopus 로고
    • Promoter-selective activation domains in Oct-1 and Oct-2 direct differential activation of an snRNA and mRNA promoter
    • Tanaka,M., Lai,J.S. and Herr,W. (1992) Promoter-selective activation domains in Oct-1 and Oct-2 direct differential activation of an snRNA and mRNA promoter. Cell, 68, 755-767.
    • (1992) Cell , vol.68 , pp. 755-767
    • Tanaka, M.1    Lai, J.S.2    Herr, W.3
  • 38
    • 0032502675 scopus 로고    scopus 로고
    • Involvement of flap endonuclease 1 in base excision DNA repair
    • Kim,K., Biade,S. and Matsumoto,Y. (1998) Involvement of flap endonuclease 1 in base excision DNA repair. J. Biol. Chem., 273, 8842-8848.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8842-8848
    • Kim, K.1    Biade, S.2    Matsumoto, Y.3
  • 39
    • 0033585072 scopus 로고    scopus 로고
    • Reconstitution of proliferating cell nuclear antigen-dependent repair of apurinic/apyrimidinic sites with purified human proteins
    • Matsumoto,Y., Kim,K., Hurwitz,J., Gary,R., Levin,D.S., Tomkinson,A.E. and Park,M.S. (1999) Reconstitution of proliferating cell nuclear antigen-dependent repair of apurinic/apyrimidinic sites with purified human proteins. J. Biol. Chem., 274, 33703-33708.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33703-33708
    • Matsumoto, Y.1    Kim, K.2    Hurwitz, J.3    Gary, R.4    Levin, D.S.5    Tomkinson, A.E.6    Park, M.S.7
  • 40
    • 0037162995 scopus 로고    scopus 로고
    • Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions
    • Hazra,T.K., Kow,Y.W., Hatahet,Z., Imhoff,B., Boldogh,I., Mokkapati,S.K., Mitra,S. and Izumi,T. (2002) Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions. J. Biol. Chem., 277, 30417-30420.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30417-30420
    • Hazra, T.K.1    Kow, Y.W.2    Hatahet, Z.3    Imhoff, B.4    Boldogh, I.5    Mokkapati, S.K.6    Mitra, S.7    Izumi, T.8
  • 41
    • 0032951710 scopus 로고    scopus 로고
    • Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1
    • Waters,T.R., Gallinari,P., Jiricny,J. and Swann,P.F. (1999) Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1. J. Biol. Chem., 274, 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
  • 42
    • 0034695632 scopus 로고    scopus 로고
    • Protection against methylation-induced cytotoxicity by DNA polymerase β-dependent long patch base excision repair
    • Horton,J.K., Prasad,R., Hou,E. and Wilson,S.H. (2000) Protection against methylation-induced cytotoxicity by DNA polymerase β-dependent long patch base excision repair. J. Biol. Chem., 275, 2211-2218.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2211-2218
    • Horton, J.K.1    Prasad, R.2    Hou, E.3    Wilson, S.H.4
  • 43
    • 0035980003 scopus 로고    scopus 로고
    • DNA polymerase β-mediated long patch base excision repair. Poly(ADP-ribose)polymerase-1 stimulates strand displacement DNA synthesis
    • Prasad,R., Lavrik,O.I., Kim,S.J., Kedar,P., Yang,X.P., Vande Berg,B.J. and Wilson,S.H. (2001) DNA polymerase β-mediated long patch base excision repair. Poly(ADP-ribose)polymerase-1 stimulates strand displacement DNA synthesis. J. Biol. Chem., 276, 32411-32414.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32411-32414
    • Prasad, R.1    Lavrik, O.I.2    Kim, S.J.3    Kedar, P.4    Yang, X.P.5    Vande Berg, B.J.6    Wilson, S.H.7
  • 46
    • 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. and Tainer,J.A. (2000) DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination. Nature, 403, 451-456.
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 47
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA: Evidence for an induced fit mechanism
    • Sawaya,M.R., Prasad,R., Wilson,S.H., Kraut,J. and Pelletier,H. (1997) Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA: evidence for an induced fit mechanism. Biochemistry, 36, 11205-11215.
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, R.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 50
    • 0035421186 scopus 로고    scopus 로고
    • Excision of deaminated cytosine from the vertebrate genome: Role of the SMUG1 uracil-DNA glycosylase
    • Nilsen,H., Haushalter,K.A., Robins,P., Barnes,D.E., Verdine,G.L. and Lindahl,T. (2001) Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase. EMBO J., 20, 4278-4286.
    • (2001) EMBO J. , vol.20 , pp. 4278-4286
    • Nilsen, H.1    Haushalter, K.A.2    Robins, P.3    Barnes, D.E.4    Verdine, G.L.5    Lindahl, T.6
  • 51
    • 0033602148 scopus 로고    scopus 로고
    • Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors
    • Haushalter,K.A., Todd Stukenberg,M.W., Kirschner,M.W. and Verdine,G.L. (1999) Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors. Curr. Biol., 9, 174-185.
    • (1999) Curr. Biol. , vol.9 , pp. 174-185
    • Haushalter, K.A.1    Todd Stukenberg, M.W.2    Kirschner, M.W.3    Verdine, G.L.4
  • 52
    • 0037509930 scopus 로고    scopus 로고
    • Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions
    • Masaoka,A., Matsubara,M., Hasegawa,R., Tanaka,T., Kurisu,S., Terato,H., Ohyama,Y., Karino,N., Matsuda,A. and Ide,H. (2003) Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions. Biochemistry, 42, 5003-5012.
    • (2003) Biochemistry , vol.42 , pp. 5003-5012
    • Masaoka, A.1    Matsubara, M.2    Hasegawa, R.3    Tanaka, T.4    Kurisu, S.5    Terato, H.6    Ohyama, Y.7    Karino, N.8    Matsuda, A.9    Ide, H.10
  • 53
    • 0037108463 scopus 로고    scopus 로고
    • Immunoglobulin isotype switching is inhibited and somatic hypermutation perturbed in UNG-deficient mice
    • Rada,C., Williams,G.T., Nilsen,H., Barnes,D.E., Lindahl,T. and Neuberger,M.S. (2002) Immunoglobulin isotype switching is inhibited and somatic hypermutation perturbed in UNG-deficient mice. Curr. Biol. 12, 1748-1755.
    • (2002) Curr. Biol. , vol.12 , pp. 1748-1755
    • Rada, C.1    Williams, G.T.2    Nilsen, H.3    Barnes, D.E.4    Lindahl, T.5    Neuberger, M.S.6
  • 55
    • 0033591336 scopus 로고    scopus 로고
    • The type of DNA glycosylase determines the base excision repair pathway in mammalian cells
    • Fortini,P., Parlanti,E., Sidorkina,O.M., Laval,J. and Dogliotti,E. (1999) The type of DNA glycosylase determines the base excision repair pathway in mammalian cells. J. Biol. Chem., 274, 15230-15236.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15230-15236
    • Fortini, P.1    Parlanti, E.2    Sidorkina, O.M.3    Laval, J.4    Dogliotti, E.5
  • 56
    • 0038102398 scopus 로고    scopus 로고
    • Long-patch DNA repair synthesis during base excision repair in mammalian cells
    • Sattler,U., Frit,P., Salles,B. and Calsou,P. (2003) Long-patch DNA repair synthesis during base excision repair in mammalian cells. EMBO Rep., 4, 363-367.
    • (2003) EMBO Rep. , vol.4 , pp. 363-367
    • Sattler, U.1    Frit, P.2    Salles, B.3    Calsou, P.4
  • 57
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair
    • Matsumoto,Y. and Kim,K. (1995) Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair. Science, 269, 699-702.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 58
    • 0035869014 scopus 로고    scopus 로고
    • Human DNA polymerase β initiates DNA synthesis during long-patch repair of reduced AP sites in DNA
    • Podlutsky,A.J., Dianova, II, Podust,V.N., Bohr,V.A. and Dianov,G.L. (2001) Human DNA polymerase β initiates DNA synthesis during long-patch repair of reduced AP sites in DNA. EMBO J., 20, 1477-1482.
    • (2001) EMBO J. , vol.20 , pp. 1477-1482
    • Podlutsky, A.J.1    Dianova, I.I.2    Podust, V.N.3    Bohr, V.A.4    Dianov, G.L.5
  • 60
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN1)
    • Klungland,A. and Lindahl,T. (1997) Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1). EMBO J., 16, 3341-3348.
    • (1997) EMBO J. , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 61
    • 0032516831 scopus 로고    scopus 로고
    • Mammalian abasic site base excision repair. Identification of the reaction sequence and rate-determining steps
    • Srivastava,D.K., Berg,B.J., Prasad,R., Molina,J.T., Beard,W.A., Tomkinson,A.E. and Wilson,S.H. (1998) Mammalian abasic site base excision repair. Identification of the reaction sequence and rate-determining steps. J. Biol. Chem., 273, 21203-21209.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21203-21209
    • Srivastava, D.K.1    Berg, B.J.2    Prasad, R.3    Molina, J.T.4    Beard, W.A.5    Tomkinson, A.E.6    Wilson, S.H.7
  • 62
    • 0033923815 scopus 로고    scopus 로고
    • Requirement for human AP endonuclease 1 for repair of 3′-blocking damage at DNA single-strand breaks induced by reactive oxygen species
    • Izumi,T., Hazra,T.K., Boldogh,I., Tomkinson,A.E., Park,M.S., Ikeda,S. and Mitra,S. (2000) Requirement for human AP endonuclease 1 for repair of 3′-blocking damage at DNA single-strand breaks induced by reactive oxygen species. Carcinogenesis, 21, 1329-1334.
    • (2000) Carcinogenesis , vol.21 , pp. 1329-1334
    • Izumi, T.1    Hazra, T.K.2    Boldogh, I.3    Tomkinson, A.E.4    Park, M.S.5    Ikeda, S.6    Mitra, S.7
  • 63
    • 0037472087 scopus 로고    scopus 로고
    • Escherichia coli uracil- and ethenocytosine-initiated base excision DNA repair: Rate-limiting stepand patch size distribution
    • Sung,J.S. and Mosbaugh,D.W. (2003) Escherichia coli uracil- and ethenocytosine-initiated base excision DNA repair: rate-limiting stepand patch size distribution. Biochemistry, 42, 4613-4625.
    • (2003) Biochemistry , vol.42 , pp. 4613-4625
    • Sung, J.S.1    Mosbaugh, D.W.2
  • 64
    • 0034725720 scopus 로고    scopus 로고
    • ATP for the DNA ligation step in base excision repair is generated from poly(ADP-ribose)
    • Oei,S.L. and Ziegler,M. (2000) ATP for the DNA ligation step in base excision repair is generated from poly(ADP-ribose). J. Biol. Chem., 275, 23234-23239.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23234-23239
    • Oei, S.L.1    Ziegler, M.2
  • 65
    • 0042342532 scopus 로고    scopus 로고
    • A mechanistic perspective on the chemistry of DNA repair glycosylases
    • Stivers,J.T. and Jiang,Y.L. (2003) A mechanistic perspective on the chemistry of DNA repair glycosylases. Chem. Rev., 103, 2729-2759.
    • (2003) Chem. Rev. , vol.103 , pp. 2729-2759
    • Stivers, J.T.1    Jiang, Y.L.2
  • 66
    • 0032573432 scopus 로고    scopus 로고
    • Heterogeneous repair of N-methylpurines at the nucleotide level in normal human cells
    • Ye,N., Holmquist,G.P. and O'Connor,T.R. (1998) Heterogeneous repair of N-methylpurines at the nucleotide level in normal human cells. J. Mol. Biol., 284, 269-285.
    • (1998) J. Mol. Biol. , vol.284 , pp. 269-285
    • Ye, N.1    Holmquist, G.P.2    O'Connor, T.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.