메뉴 건너뛰기




Volumn 327, Issue 1-2, 2012, Pages 73-89

Base excision repair and cancer

Author keywords

Base excision repair; Cancer variants

Indexed keywords

8 HYDROXYGUANINE; APURINIC ENDONUCLEASE 1; APURINIC ENDONUCLEASE 2; DNA DIRECTED DNA POLYMERASE BETA; DNA GLYCOSYLTRANSFERASE; ENDONUCLEASE; LIGASE III ALPHA; LITHOCHOLIC ACID; METHYL CPG BINDING DOMAIN PROTEIN 4; METHYLPURINE DNA GLYCOSYLASE; OXIDIZED PYRIMIDINE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; PROTEIN NEIL1; PROTEIN NEIL2; PROTEIN NEIL3; PROTEIN NTH1; PROTEIN OGG1; PROTEIN SMUG1; PYRIMIDINE DERIVATIVE; TEMOZOLOMIDE; THYMINE DNA GLYCOSYLASE; UNCLASSIFIED DRUG; URACIL DNA GLYCOSIDASE; XRCC1 PROTEIN;

EID: 84865093016     PISSN: 03043835     EISSN: 18727980     Source Type: Journal    
DOI: 10.1016/j.canlet.2011.12.038     Document Type: Review
Times cited : (249)

References (346)
  • 2
    • 0000476915 scopus 로고
    • An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues
    • Lindahl T. An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues. Proc. Natl. Acad. Sci. USA 1974, 71:3649-3653.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 3649-3653
    • Lindahl, T.1
  • 6
    • 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., Hazra T.K. Mammalian DNA base excision repair proteins: their interactions and role in repair of oxidative DNA damage. Toxicology 2003, 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
  • 8
    • 10944251591 scopus 로고    scopus 로고
    • Repair and genetic consequences of endogenous DNA base damage in mammalian cells
    • Barnes D.E., Lindahl T. Repair and genetic consequences of endogenous DNA base damage in mammalian cells. Annu. Rev. Genet. 2004, 38:445-476.
    • (2004) Annu. Rev. Genet. , vol.38 , pp. 445-476
    • Barnes, D.E.1    Lindahl, T.2
  • 9
    • 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. 1998, 150:S60-79.
    • (1998) Radiat. Res. , vol.150
    • Wallace, S.S.1
  • 10
    • 0037115912 scopus 로고    scopus 로고
    • Enzymology of the repair of free radicals-induced DNA damage
    • Gros L., Saparbaev M.K., Laval J. Enzymology of the repair of free radicals-induced DNA damage. Oncogene 2002, 21:8905-8925.
    • (2002) Oncogene , vol.21 , pp. 8905-8925
    • Gros, L.1    Saparbaev, M.K.2    Laval, J.3
  • 11
    • 44449112688 scopus 로고    scopus 로고
    • Base excision DNA repair
    • Zharkov D.O. Base excision DNA repair. Cell Mol. Life Sci. 2008, 65:1544-1565.
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 1544-1565
    • Zharkov, D.O.1
  • 12
    • 0025120572 scopus 로고
    • The enzymology of apurinic/apyrimidinic endonucleases
    • Doetsch P.W., Cunningham R.P. The enzymology of apurinic/apyrimidinic endonucleases. Mutat. Res. 1990, 236:173-201.
    • (1990) Mutat. Res. , vol.236 , pp. 173-201
    • Doetsch, P.W.1    Cunningham, R.P.2
  • 13
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair
    • Matsumoto Y., Kim K. Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair. Science 1995, 269:699-702.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 14
    • 0032510962 scopus 로고    scopus 로고
    • Human DNA polymerase beta deoxyribose phosphate lyase. Substrate specificity and catalytic mechanism
    • Prasad R., Beard W.A., Strauss P.R., Wilson S.H. Human DNA polymerase beta deoxyribose phosphate lyase. Substrate specificity and catalytic mechanism. J. Biol. Chem. 1998, 273:15263-15270.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15263-15270
    • Prasad, R.1    Beard, W.A.2    Strauss, P.R.3    Wilson, S.H.4
  • 15
    • 0023127167 scopus 로고
    • Escherichia coli endonuclease III is not an endonuclease but a beta-elimination catalyst
    • Bailly V., Verly W.G. Escherichia coli endonuclease III is not an endonuclease but a beta-elimination catalyst. Biochem. J. 1987, 242:565-572.
    • (1987) Biochem. J. , vol.242 , pp. 565-572
    • Bailly, V.1    Verly, W.G.2
  • 16
    • 0024410314 scopus 로고
    • Delta-elimination in the repair of AP (apurinic/apyrimidinic) sites in DNA
    • Bailly V., Derydt M., Verly W.G. Delta-elimination in the repair of AP (apurinic/apyrimidinic) sites in DNA. Biochem. J. 1989, 261:707-713.
    • (1989) Biochem. J. , vol.261 , pp. 707-713
    • Bailly, V.1    Derydt, M.2    Verly, W.G.3
  • 17
    • 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. Nucleic Acids Res. 1991, 19:5907-5914.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5907-5914
    • Chen, D.S.1    Herman, T.2    Demple, B.3
  • 20
    • 78650399787 scopus 로고    scopus 로고
    • Substrate channeling in mammalian base excision repair pathways: passing the baton
    • Prasad R., Shock D.D., Beard W.A., Wilson S.H. Substrate channeling in mammalian base excision repair pathways: passing the baton. J. Biol. Chem. 2010, 285:40479-40488.
    • (2010) J. Biol. Chem. , vol.285 , pp. 40479-40488
    • Prasad, R.1    Shock, D.D.2    Beard, W.A.3    Wilson, S.H.4
  • 21
    • 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. 1998, 407:1-9.
    • (1998) Mutat. Res. , vol.407 , pp. 1-9
    • Tomkinson, A.E.1    Mackey, Z.B.2
  • 22
    • 48249095920 scopus 로고    scopus 로고
    • Single-strand break repair and genetic disease
    • Caldecott K.W. Single-strand break repair and genetic disease. Nat. Rev. Genet. 2008, 9:619-631.
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 619-631
    • Caldecott, K.W.1
  • 24
    • 0029957245 scopus 로고    scopus 로고
    • XRCC1 polypeptide interacts with DNA polymerase beta and possibly 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 beta and possibly poly (ADP-ribose) polymerase, and DNA ligase III is a novel molecular 'nick-sensor' in vitro. Nucleic Acids Res. 1996, 24:4387-4394.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4387-4394
    • Caldecott, K.W.1    Aoufouchi, S.2    Johnson, P.3    Shall, S.4
  • 26
    • 0033553510 scopus 로고    scopus 로고
    • Role of DNA polymerase beta in the excision step of long patch mammalian base excision repair
    • Dianov G.L., Prasad R., Wilson S.H., Bohr V.A. Role of DNA polymerase beta in the excision step of long patch mammalian base excision repair. J. Biol. Chem. 1999, 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
  • 27
    • 34247599335 scopus 로고    scopus 로고
    • A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification
    • Almeida K.H., Sobol R.W. A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification. DNA Repair (Amst.) 2007, 6:695-711.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 695-711
    • Almeida, K.H.1    Sobol, R.W.2
  • 28
    • 28244438393 scopus 로고    scopus 로고
    • Long-patch base excision DNA repair of 2-deoxyribonolactone prevents the formation of DNA-protein cross-links with DNA polymerase beta
    • Sung J.S., DeMott M.S., Demple B. Long-patch base excision DNA repair of 2-deoxyribonolactone prevents the formation of DNA-protein cross-links with DNA polymerase beta. J. Biol. Chem. 2005, 280:39095-39103.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39095-39103
    • Sung, J.S.1    DeMott, M.S.2    Demple, B.3
  • 29
  • 30
    • 0036862512 scopus 로고    scopus 로고
    • Flap endonuclease 1 efficiently cleaves base excision repair and DNA replication intermediates assembled into nucleosomes
    • Huggins C.F., Chafin D.R., Aoyagi S., Henricksen L.A., Bambara R.A., Hayes J.J. Flap endonuclease 1 efficiently cleaves base excision repair and DNA replication intermediates assembled into nucleosomes. Mol. Cell 2002, 10:1201-1211.
    • (2002) Mol. Cell , vol.10 , pp. 1201-1211
    • Huggins, C.F.1    Chafin, D.R.2    Aoyagi, S.3    Henricksen, L.A.4    Bambara, R.A.5    Hayes, J.J.6
  • 31
    • 67649342599 scopus 로고    scopus 로고
    • Long patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complex
    • Balakrishnan L., Brandt P.D., Lindsey-Boltz L.A., Sancar A., Bambara R.A. Long patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complex. J. Biol. Chem. 2009, 284:15158-15172.
    • (2009) J. Biol. Chem. , vol.284 , pp. 15158-15172
    • Balakrishnan, L.1    Brandt, P.D.2    Lindsey-Boltz, L.A.3    Sancar, A.4    Bambara, R.A.5
  • 32
    • 0034635403 scopus 로고    scopus 로고
    • FEN1 stimulation of DNA polymerase beta mediates 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 beta mediates an excision step in mammalian long patch base excision repair. J. Biol. Chem. 2000, 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
  • 33
    • 33646092313 scopus 로고    scopus 로고
    • Roles of DNA ligase III and XRCC1 in regulating the switch between short patch and long patch BER
    • Petermann E., Keil C., Oei S.L. Roles of DNA ligase III and XRCC1 in regulating the switch between short patch and long patch BER. DNA Repair (Amst.) 2006, 5:544-555.
    • (2006) DNA Repair (Amst.) , vol.5 , pp. 544-555
    • Petermann, E.1    Keil, C.2    Oei, S.L.3
  • 34
    • 38049112778 scopus 로고    scopus 로고
    • Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
    • Hegde M.L., Hazra T.K., Mitra S. Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells. Cell Res. 2008, 18:27-47.
    • (2008) Cell Res. , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 35
    • 16644366519 scopus 로고    scopus 로고
    • Commentary: DNA base excision repair defects in human pathologies
    • Frosina G. Commentary: DNA base excision repair defects in human pathologies. Free Radic Res. 2004, 38:1037-1054.
    • (2004) Free Radic Res. , vol.38 , pp. 1037-1054
    • Frosina, G.1
  • 36
    • 27744531188 scopus 로고    scopus 로고
    • Genetic polymorphisms in the base excision repair pathway and cancer risk: a HuGE review
    • Hung R.J., Hall J., Brennan P., Boffetta P. Genetic polymorphisms in the base excision repair pathway and cancer risk: a HuGE review. Am. J. Epidemiol. 2005, 162:925-942.
    • (2005) Am. J. Epidemiol. , vol.162 , pp. 925-942
    • Hung, R.J.1    Hall, J.2    Brennan, P.3    Boffetta, P.4
  • 37
    • 27844492836 scopus 로고    scopus 로고
    • Modulation of oxidative mutagenesis and carcinogenesis by polymorphic forms of human DNA repair enzymes
    • Nohmi T., Kim S.R., Yamada M. Modulation of oxidative mutagenesis and carcinogenesis by polymorphic forms of human DNA repair enzymes. Mutat. Res. 2005, 591:60-73.
    • (2005) Mutat. Res. , vol.591 , pp. 60-73
    • Nohmi, T.1    Kim, S.R.2    Yamada, M.3
  • 38
    • 33745083977 scopus 로고    scopus 로고
    • Base excision repair fidelity in normal and cancer cells
    • Chan K.K., Zhang Q.M., Dianov G.L. Base excision repair fidelity in normal and cancer cells. Mutagenesis 2006, 21:173-178.
    • (2006) Mutagenesis , vol.21 , pp. 173-178
    • Chan, K.K.1    Zhang, Q.M.2    Dianov, G.L.3
  • 39
    • 32244435724 scopus 로고    scopus 로고
    • Is base excision repair a tumor suppressor mechanism?
    • Sweasy J.B., Lang T., DiMaio D. Is base excision repair a tumor suppressor mechanism?. Cell Cycle 2006, 5:250-259.
    • (2006) Cell Cycle , vol.5 , pp. 250-259
    • Sweasy, J.B.1    Lang, T.2    DiMaio, D.3
  • 40
    • 34548292501 scopus 로고    scopus 로고
    • Base excision repair modulation as a risk factor for human cancers
    • Tudek B. Base excision repair modulation as a risk factor for human cancers. Mol. Aspects Med. 2007, 28:258-275.
    • (2007) Mol. Aspects Med. , vol.28 , pp. 258-275
    • Tudek, B.1
  • 41
    • 47849100494 scopus 로고    scopus 로고
    • Mechanism of oxidative DNA damage repair and relevance to human pathology
    • D'Errico M., Parlanti E., Dogliotti E. Mechanism of oxidative DNA damage repair and relevance to human pathology. Mutat. Res. 2008, 659:4-14.
    • (2008) Mutat. Res. , vol.659 , pp. 4-14
    • D'Errico, M.1    Parlanti, E.2    Dogliotti, E.3
  • 42
    • 44449161947 scopus 로고    scopus 로고
    • DNA repair of oxidative DNA damage in human carcinogenesis: potential application for cancer risk assessment and prevention
    • Paz-Elizur T., Sevilya Z., Leitner-Dagan Y., Elinger D., Roisman L.C., Livneh Z. DNA repair of oxidative DNA damage in human carcinogenesis: potential application for cancer risk assessment and prevention. Cancer Lett. 2008, 266:60-72.
    • (2008) Cancer Lett. , vol.266 , pp. 60-72
    • Paz-Elizur, T.1    Sevilya, Z.2    Leitner-Dagan, Y.3    Elinger, D.4    Roisman, L.C.5    Livneh, Z.6
  • 43
    • 78649487460 scopus 로고    scopus 로고
    • Variant base excision repair proteins: contributors to genomic instability
    • Nemec A.A., Wallace S.S., Sweasy J.B. Variant base excision repair proteins: contributors to genomic instability. Semin. Cancer Biol. 2010, 20:320-328.
    • (2010) Semin. Cancer Biol. , vol.20 , pp. 320-328
    • Nemec, A.A.1    Wallace, S.S.2    Sweasy, J.B.3
  • 45
    • 0037115911 scopus 로고    scopus 로고
    • Uracil in DNA - occurrence, consequences and repair
    • Krokan H.E., Drablos F., Slupphaug G. Uracil in DNA - occurrence, consequences and repair. Oncogene 2002, 21:8935-8948.
    • (2002) Oncogene , vol.21 , pp. 8935-8948
    • Krokan, H.E.1    Drablos, F.2    Slupphaug, G.3
  • 50
    • 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., Slupphaug G. 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. 2002, 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
  • 51
    • 33847621554 scopus 로고    scopus 로고
    • Uracil in DNA - general mutagen, but normal intermediate in acquired immunity
    • Kavli B., Otterlei M., Slupphaug G., Krokan H.E. Uracil in DNA - general mutagen, but normal intermediate in acquired immunity. DNA Repair (Amst.) 2007, 6:505-516.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 505-516
    • Kavli, B.1    Otterlei, M.2    Slupphaug, G.3    Krokan, H.E.4
  • 53
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis
    • Mol C.D., Arvai A.S., Slupphaug G., Kavli B., Alseth I., Krokan H.E., Tainer J.A. Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. Cell 1995, 80:869-878.
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavli, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 54
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracil-DNA glycosylase
    • Savva R., McAuley-Hecht K., Brown T., Pearl L. The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature 1995, 373:487-493.
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R.1    McAuley-Hecht, K.2    Brown, T.3    Pearl, L.4
  • 55
    • 0034734383 scopus 로고    scopus 로고
    • Structure and function in the uracil-DNA glycosylase superfamily
    • Pearl L.H. Structure and function in the uracil-DNA glycosylase superfamily. Mutat. Res. 2000, 460:165-181.
    • (2000) Mutat. Res. , vol.460 , pp. 165-181
    • Pearl, L.H.1
  • 56
    • 0038771139 scopus 로고    scopus 로고
    • Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1
    • Wibley J.E., Waters T.R., Haushalter K., Verdine G.L., Pearl L.H. Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1. Mol. Cell 2003, 11:1647-1659.
    • (2003) Mol. Cell , vol.11 , pp. 1647-1659
    • Wibley, J.E.1    Waters, T.R.2    Haushalter, K.3    Verdine, G.L.4    Pearl, L.H.5
  • 57
    • 0033575886 scopus 로고    scopus 로고
    • The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites
    • Hendrich B., Hardeland U., Ng H.H., Jiricny J., Bird A. The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites. Nature 1999, 401:301-304.
    • (1999) Nature , vol.401 , pp. 301-304
    • Hendrich, B.1    Hardeland, U.2    Ng, H.H.3    Jiricny, J.4    Bird, A.5
  • 58
    • 0032498302 scopus 로고    scopus 로고
    • Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions
    • Barrett T.E., Savva R., Panayotou G., Barlow T., Brown T., Jiricny J., Pearl L.H. Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 1998, 92:117-129.
    • (1998) Cell , vol.92 , pp. 117-129
    • Barrett, T.E.1    Savva, R.2    Panayotou, G.3    Barlow, T.4    Brown, T.5    Jiricny, J.6    Pearl, L.H.7
  • 60
    • 48249147403 scopus 로고    scopus 로고
    • Crystal structure of human thymine DNA glycosylase bound to DNA elucidates sequence-specific mismatch recognition
    • Maiti A., Morgan M.T., Pozharski E., Drohat A.C. Crystal structure of human thymine DNA glycosylase bound to DNA elucidates sequence-specific mismatch recognition. Proc. Natl. Acad. Sci. USA 2008, 105:8890-8895.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8890-8895
    • Maiti, A.1    Morgan, M.T.2    Pozharski, E.3    Drohat, A.C.4
  • 62
    • 80052461558 scopus 로고    scopus 로고
    • Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
    • Ito S., Shen L., Dai Q., Wu S.C., Collins L.B., Swenberg J.A., He C., Zhang Y. Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine. Science 2011, 333:1300-1303.
    • (2011) Science , vol.333 , pp. 1300-1303
    • Ito, S.1    Shen, L.2    Dai, Q.3    Wu, S.C.4    Collins, L.B.5    Swenberg, J.A.6    He, C.7    Zhang, Y.8
  • 63
    • 0036305835 scopus 로고    scopus 로고
    • Structure and activity of a thermostable thymine-DNA glycosylase: evidence for base twisting to remove mismatched normal DNA bases
    • Mol C.D., Arvai A.S., Begley T.J., Cunningham R.P., Tainer J.A. Structure and activity of a thermostable thymine-DNA glycosylase: evidence for base twisting to remove mismatched normal DNA bases. J. Mol. Biol. 2002, 315:373-384.
    • (2002) J. Mol. Biol. , vol.315 , pp. 373-384
    • Mol, C.D.1    Arvai, A.S.2    Begley, T.J.3    Cunningham, R.P.4    Tainer, J.A.5
  • 65
    • 0035906936 scopus 로고    scopus 로고
    • Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA
    • Ohki I., Shimotake N., Fujita N., Jee J., Ikegami T., Nakao M., Shirakawa M. Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA. Cell 2001, 105:487-497.
    • (2001) Cell , vol.105 , pp. 487-497
    • Ohki, I.1    Shimotake, N.2    Fujita, N.3    Jee, J.4    Ikegami, T.5    Nakao, M.6    Shirakawa, M.7
  • 66
    • 73349104113 scopus 로고    scopus 로고
    • Active DNA demethylation mediated by DNA glycosylases
    • Zhu J.K. Active DNA demethylation mediated by DNA glycosylases. Annu. Rev. Genet. 2009, 43:143-166.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 143-166
    • Zhu, J.K.1
  • 67
    • 30344455023 scopus 로고    scopus 로고
    • Database of mouse strains carrying targeted mutations in genes affecting biological responses to DNA damage Version 7
    • Friedberg E.C., Meira L.B. Database of mouse strains carrying targeted mutations in genes affecting biological responses to DNA damage Version 7. DNA Repair (Amst.) 2006, 5:189-209.
    • (2006) DNA Repair (Amst.) , vol.5 , pp. 189-209
    • Friedberg, E.C.1    Meira, L.B.2
  • 68
    • 33845522879 scopus 로고    scopus 로고
    • Organ and cell specificity of base excision repair mutants in mice
    • Larsen E., Meza T.J., Kleppa L., Klungland A. Organ and cell specificity of base excision repair mutants in mice. Mutat. Res. 2007, 614:56-68.
    • (2007) Mutat. Res. , vol.614 , pp. 56-68
    • Larsen, E.1    Meza, T.J.2    Kleppa, L.3    Klungland, A.4
  • 72
    • 33750614308 scopus 로고    scopus 로고
    • Evaluation of NTHL1, NEIL1, NEIL2, MPG, TDG, UNG and SMUG1 genes in familial colorectal cancer predisposition
    • Broderick P., Bagratuni T., Vijayakrishnan J., Lubbe S., Chandler I., Houlston R.S. Evaluation of NTHL1, NEIL1, NEIL2, MPG, TDG, UNG and SMUG1 genes in familial colorectal cancer predisposition. BMC Cancer 2006, 6:243.
    • (2006) BMC Cancer , vol.6 , pp. 243
    • Broderick, P.1    Bagratuni, T.2    Vijayakrishnan, J.3    Lubbe, S.4    Chandler, I.5    Houlston, R.S.6
  • 75
    • 0030812371 scopus 로고    scopus 로고
    • Human thymine-DNA glycosylase maps at chromosome 12q22-q24.1: a region of high loss of heterozygosity in gastric cancer
    • Schmutte C., Baffa R., Veronese L.M., Murakumo Y., Fishel R. Human thymine-DNA glycosylase maps at chromosome 12q22-q24.1: a region of high loss of heterozygosity in gastric cancer. Cancer Res. 1997, 57:3010-3015.
    • (1997) Cancer Res. , vol.57 , pp. 3010-3015
    • Schmutte, C.1    Baffa, R.2    Veronese, L.M.3    Murakumo, Y.4    Fishel, R.5
  • 77
    • 66849141266 scopus 로고    scopus 로고
    • Polymorphisms in uracil-processing genes, but not one-carbon nutrients, are associated with altered DNA uracil concentrations in an urban Puerto Rican population
    • Chanson A., Parnell L.D., Ciappio E.D., Liu Z., Crott J.W., Tucker K.L., Mason J.B. Polymorphisms in uracil-processing genes, but not one-carbon nutrients, are associated with altered DNA uracil concentrations in an urban Puerto Rican population. Am. J. Clin. Nutr. 2009, 89:1927-1936.
    • (2009) Am. J. Clin. Nutr. , vol.89 , pp. 1927-1936
    • Chanson, A.1    Parnell, L.D.2    Ciappio, E.D.3    Liu, Z.4    Crott, J.W.5    Tucker, K.L.6    Mason, J.B.7
  • 78
    • 4444220781 scopus 로고    scopus 로고
    • Polymorphisms in TDG and MGMT genes - epidemiological and functional study in lung cancer patients from Poland
    • Krzesniak M., Butkiewicz D., Samojedny A., Chorazy M., Rusin M. Polymorphisms in TDG and MGMT genes - epidemiological and functional study in lung cancer patients from Poland. Ann. Hum. Genet. 2004, 68:300-312.
    • (2004) Ann. Hum. Genet. , vol.68 , pp. 300-312
    • Krzesniak, M.1    Butkiewicz, D.2    Samojedny, A.3    Chorazy, M.4    Rusin, M.5
  • 80
    • 3042614143 scopus 로고    scopus 로고
    • Identification of genetic variants in base excision repair pathway and their associations with risk of esophageal squamous cell carcinoma
    • Hao B., Wang H., Zhou K., Li Y., Chen X., Zhou G., Zhu Y., Miao X., Tan W., Wei Q., Lin D., He F. Identification of genetic variants in base excision repair pathway and their associations with risk of esophageal squamous cell carcinoma. Cancer Res. 2004, 64:4378-4384.
    • (2004) Cancer Res. , vol.64 , pp. 4378-4384
    • Hao, B.1    Wang, H.2    Zhou, K.3    Li, Y.4    Chen, X.5    Zhou, G.6    Zhu, Y.7    Miao, X.8    Tan, W.9    Wei, Q.10    Lin, D.11    He, F.12
  • 82
    • 68149134842 scopus 로고    scopus 로고
    • The Glu346Lys polymorphism and frameshift mutations of the Methyl-CpG Binding Domain 4 gene in gastrointestinal cancer
    • Song J.H., Maeng E.J., Cao Z., Kim S.Y., Nam S.W., Lee J.Y., Park W.S. The Glu346Lys polymorphism and frameshift mutations of the Methyl-CpG Binding Domain 4 gene in gastrointestinal cancer. Neoplasma 2009, 56:343-347.
    • (2009) Neoplasma , vol.56 , pp. 343-347
    • Song, J.H.1    Maeng, E.J.2    Cao, Z.3    Kim, S.Y.4    Nam, S.W.5    Lee, J.Y.6    Park, W.S.7
  • 85
    • 0016893372 scopus 로고
    • New class of enzymes acting on damaged DNA
    • Lindahl T. New class of enzymes acting on damaged DNA. Nature 1976, 259:64-66.
    • (1976) Nature , vol.259 , pp. 64-66
    • Lindahl, T.1
  • 86
    • 0025108951 scopus 로고
    • Isolation and structure of a cDNA expressing a mammalian 3-methyladenine-DNA glycosylase
    • O'Connor T.R., Laval F. Isolation and structure of a cDNA expressing a mammalian 3-methyladenine-DNA glycosylase. EMBO J. 1990, 9:3337-3342.
    • (1990) EMBO J. , vol.9 , pp. 3337-3342
    • O'Connor, T.R.1    Laval, F.2
  • 87
    • 0025949662 scopus 로고
    • Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase
    • Chakravarti D., Ibeanu G.C., Tano K., Mitra S. Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase. J. Biol. Chem. 1991, 266:15710-15715.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15710-15715
    • Chakravarti, D.1    Ibeanu, G.C.2    Tano, K.3    Mitra, S.4
  • 88
    • 0025784273 scopus 로고
    • Human cDNA expressing a functional DNA glycosylase excising 3-methyladenine and 7-methylguanine
    • O'Connor T.R., Laval J. Human cDNA expressing a functional DNA glycosylase excising 3-methyladenine and 7-methylguanine. Biochem. Biophys. Res. Commun. 1991, 176:1170-1177.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 1170-1177
    • O'Connor, T.R.1    Laval, J.2
  • 89
    • 0025990209 scopus 로고
    • Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16
    • Samson L., Derfler B., Boosalis M., Call K. Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16. Proc. Natl. Acad. Sci. USA 1991, 88:9127-9131.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9127-9131
    • Samson, L.1    Derfler, B.2    Boosalis, M.3    Call, K.4
  • 90
    • 0028087282 scopus 로고
    • All four known cyclic adducts formed in DNA by the vinyl chloride metabolite chloroacetaldehyde are released by a human DNA glycosylase
    • Dosanjh M.K., Chenna A., Kim E., Fraenkel-Conrat H., Samson L., Singer B. All four known cyclic adducts formed in DNA by the vinyl chloride metabolite chloroacetaldehyde are released by a human DNA glycosylase. Proc. Natl. Acad. Sci. USA 1994, 91:1024-1028.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1024-1028
    • Dosanjh, M.K.1    Chenna, A.2    Kim, E.3    Fraenkel-Conrat, H.4    Samson, L.5    Singer, B.6
  • 91
    • 0029133553 scopus 로고
    • Escherichia coli, Saccharomyces cerevisiae, rat and human 3-methyladenine DNA glycosylases repair 1,N6-ethenoadenine when present in DNA
    • Saparbaev M., Kleibl K., Laval J. Escherichia coli, Saccharomyces cerevisiae, rat and human 3-methyladenine DNA glycosylases repair 1,N6-ethenoadenine when present in DNA. Nucleic Acids Res. 1995, 23:3750-3755.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3750-3755
    • Saparbaev, M.1    Kleibl, K.2    Laval, J.3
  • 92
    • 0028239225 scopus 로고
    • Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases
    • Saparbaev M., Laval J. Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases. Proc. Natl. Acad. Sci. USA 1994, 91:5873-5877.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5873-5877
    • Saparbaev, M.1    Laval, J.2
  • 95
    • 0032538337 scopus 로고    scopus 로고
    • Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision
    • Lau A.Y., Scharer O.D., Samson L., Verdine G.L., Ellenberger T. Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision. Cell 1998, 95:249-258.
    • (1998) Cell , vol.95 , pp. 249-258
    • Lau, A.Y.1    Scharer, O.D.2    Samson, L.3    Verdine, G.L.4    Ellenberger, T.5
  • 98
    • 78649767885 scopus 로고    scopus 로고
    • Both base excision repair and O6-methylguanine-DNA methyltransferase protect against methylation-induced colon carcinogenesis
    • Wirtz S., Nagel G., Eshkind L., Neurath M.F., Samson L.D., Kaina B. Both base excision repair and O6-methylguanine-DNA methyltransferase protect against methylation-induced colon carcinogenesis. Carcinogenesis 2010, 31:2111-2117.
    • (2010) Carcinogenesis , vol.31 , pp. 2111-2117
    • Wirtz, S.1    Nagel, G.2    Eshkind, L.3    Neurath, M.F.4    Samson, L.D.5    Kaina, B.6
  • 100
    • 0030041960 scopus 로고    scopus 로고
    • Repair-deficient 3-methyladenine DNA glycosylase homozygous mutant mouse cells have increased sensitivity to alkylation-induced chromosome damage and cell killing
    • Engelward B.P., Dreslin A., Christensen J., Huszar D., Kurahara C., Samson L. Repair-deficient 3-methyladenine DNA glycosylase homozygous mutant mouse cells have increased sensitivity to alkylation-induced chromosome damage and cell killing. EMBO J. 1996, 15:945-952.
    • (1996) EMBO J. , vol.15 , pp. 945-952
    • Engelward, B.P.1    Dreslin, A.2    Christensen, J.3    Huszar, D.4    Kurahara, C.5    Samson, L.6
  • 101
    • 0036468545 scopus 로고    scopus 로고
    • 3-Methyladenine DNA glycosylase-deficient Aag null mice display unexpected bone marrow alkylation resistance
    • Roth R.B., Samson L.D. 3-Methyladenine DNA glycosylase-deficient Aag null mice display unexpected bone marrow alkylation resistance. Cancer Res. 2002, 62:656-660.
    • (2002) Cancer Res. , vol.62 , pp. 656-660
    • Roth, R.B.1    Samson, L.D.2
  • 102
    • 0028801762 scopus 로고
    • Overexpression of N-methylpurine-DNA glycosylase in Chinese hamster ovary cells renders them more sensitive to the production of chromosomal aberrations by methylating agents - a case of imbalanced DNA repair
    • Coquerelle T., Dosch J., Kaina B. Overexpression of N-methylpurine-DNA glycosylase in Chinese hamster ovary cells renders them more sensitive to the production of chromosomal aberrations by methylating agents - a case of imbalanced DNA repair. Mutat. Res. 1995, 336:9-17.
    • (1995) Mutat. Res. , vol.336 , pp. 9-17
    • Coquerelle, T.1    Dosch, J.2    Kaina, B.3
  • 104
    • 60549110715 scopus 로고    scopus 로고
    • Screening and association testing of common coding variation in steroid hormone receptor co-activator and co-repressor genes in relation to breast cancer risk: the Multiethnic Cohort
    • Haiman C.A., Garcia R.R., Hsu C., Xia L., Ha H., Sheng X., Le Marchand L., Kolonel L.N., Henderson B.E., Stallcup M.R., Greene G.L., Press M.F. Screening and association testing of common coding variation in steroid hormone receptor co-activator and co-repressor genes in relation to breast cancer risk: the Multiethnic Cohort. BMC Cancer 2009, 9:43.
    • (2009) BMC Cancer , vol.9 , pp. 43
    • Haiman, C.A.1    Garcia, R.R.2    Hsu, C.3    Xia, L.4    Ha, H.5    Sheng, X.6    Le Marchand, L.7    Kolonel, L.N.8    Henderson, B.E.9    Stallcup, M.R.10    Greene, G.L.11    Press, M.F.12
  • 105
    • 0033584567 scopus 로고    scopus 로고
    • Novel genetic polymorphisms in DNA repair genes: O(6)-methylguanine-DNA methyltransferase (MGMT) and N-methylpurine-DNA glycosylase (MPG) in lung cancer patients from Poland
    • Rusin M., Samojedny A., Harris C.C., Chorazy M. Novel genetic polymorphisms in DNA repair genes: O(6)-methylguanine-DNA methyltransferase (MGMT) and N-methylpurine-DNA glycosylase (MPG) in lung cancer patients from Poland. Hum. Mutat. 1999, 14:269-270.
    • (1999) Hum. Mutat. , vol.14 , pp. 269-270
    • Rusin, M.1    Samojedny, A.2    Harris, C.C.3    Chorazy, M.4
  • 107
    • 0031172802 scopus 로고    scopus 로고
    • A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer
    • Lu R., Nash H.M., Verdine G.L. A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer. Curr. Biol. 1997, 7:397-407.
    • (1997) Curr. Biol. , vol.7 , pp. 397-407
    • Lu, R.1    Nash, H.M.2    Verdine, G.L.3
  • 109
    • 0030912695 scopus 로고    scopus 로고
    • Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue
    • Aburatani H., Hippo Y., Ishida T., Takashima R., Matsuba C., Kodama T., Takao M., Yasui A., Yamamoto K., Asano M. Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue. Cancer Res. 1997, 57:2151-2156.
    • (1997) Cancer Res. , vol.57 , pp. 2151-2156
    • Aburatani, H.1    Hippo, Y.2    Ishida, T.3    Takashima, R.4    Matsuba, C.5    Kodama, T.6    Takao, M.7    Yasui, A.8    Yamamoto, K.9    Asano, M.10
  • 110
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae
    • Radicella J.P., Dherin C., Desmaze C., Fox M.S., Boiteux S. Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 1997, 94:8010-8015.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8010-8015
    • Radicella, J.P.1    Dherin, C.2    Desmaze, C.3    Fox, M.S.4    Boiteux, S.5
  • 112
    • 0030703177 scopus 로고    scopus 로고
    • Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites
    • Bjoras M., Luna L., Johnsen B., Hoff E., Haug T., Rognes T., Seeberg E. Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites. EMBO J. 1997, 16:6314-6322.
    • (1997) EMBO J. , vol.16 , pp. 6314-6322
    • Bjoras, M.1    Luna, L.2    Johnsen, B.3    Hoff, E.4    Haug, T.5    Rognes, T.6    Seeberg, E.7
  • 113
    • 0031926508 scopus 로고    scopus 로고
    • Opposite base-dependent excision of 7,8-dihydro-8-oxoadenine by the Ogg1 protein of Saccharomyces cerevisiae
    • Girard P.M., D'Ham C., Cadet J., Boiteux S. Opposite base-dependent excision of 7,8-dihydro-8-oxoadenine by the Ogg1 protein of Saccharomyces cerevisiae. Carcinogenesis 1998, 19:1299-1305.
    • (1998) Carcinogenesis , vol.19 , pp. 1299-1305
    • Girard, P.M.1    D'Ham, C.2    Cadet, J.3    Boiteux, S.4
  • 114
    • 0034666313 scopus 로고    scopus 로고
    • Substrate specificity and reaction mechanism of murine 8-oxoguanine-DNA glycosylase
    • Zharkov D.O., Rosenquist T.A., Gerchman S.E., Grollman A.P. Substrate specificity and reaction mechanism of murine 8-oxoguanine-DNA glycosylase. J. Biol. Chem. 2000, 275:28607-28617.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28607-28617
    • Zharkov, D.O.1    Rosenquist, T.A.2    Gerchman, S.E.3    Grollman, A.P.4
  • 115
    • 0034637604 scopus 로고    scopus 로고
    • Recognition of formamidopyrimidine by Escherichia coli and mammalian thymine glycol glycosylases. Distinctive paired base effects and biological and mechanistic implications
    • Asagoshi K., Yamada T., Okada Y., Terato H., Ohyama Y., Seki S., Ide H. Recognition of formamidopyrimidine by Escherichia coli and mammalian thymine glycol glycosylases. Distinctive paired base effects and biological and mechanistic implications. J. Biol. Chem. 2000, 275:24781-24786.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24781-24786
    • Asagoshi, K.1    Yamada, T.2    Okada, Y.3    Terato, H.4    Ohyama, Y.5    Seki, S.6    Ide, H.7
  • 116
    • 0034681444 scopus 로고    scopus 로고
    • Distinct repair activities of human 7,8-dihydro-8-oxoguanine DNA glycosylase and formamidopyrimidine DNA glycosylase for formamidopyrimidine and 7,8-dihydro-8-oxoguanine
    • Asagoshi K., Yamada T., Terato H., Ohyama Y., Monden Y., Arai T., Nishimura S., Aburatani H., Lindahl T., Ide H. Distinct repair activities of human 7,8-dihydro-8-oxoguanine DNA glycosylase and formamidopyrimidine DNA glycosylase for formamidopyrimidine and 7,8-dihydro-8-oxoguanine. J. Biol. Chem. 2000, 275:4956-4964.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4956-4964
    • Asagoshi, K.1    Yamada, T.2    Terato, H.3    Ohyama, Y.4    Monden, Y.5    Arai, T.6    Nishimura, S.7    Aburatani, H.8    Lindahl, T.9    Ide, H.10
  • 117
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • Bruner S.D., Norman D.P., Verdine G.L. Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature 2000, 403:859-866.
    • (2000) Nature , vol.403 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.2    Verdine, G.L.3
  • 118
    • 0036290411 scopus 로고    scopus 로고
    • Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase
    • Bjoras M., Seeberg E., Luna L., Pearl L.H., Barrett T.E. Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase. J. Mol. Biol. 2002, 317:171-177.
    • (2002) J. Mol. Biol. , vol.317 , pp. 171-177
    • Bjoras, M.1    Seeberg, E.2    Luna, L.3    Pearl, L.H.4    Barrett, T.E.5
  • 119
    • 4644259458 scopus 로고    scopus 로고
    • Structural basis for the dual coding potential of 8-oxoguanosine by a high-fidelity DNA polymerase
    • Brieba L.G., Eichman B.F., Kokoska R.J., Doublie S., Kunkel T.A., Ellenberger T. Structural basis for the dual coding potential of 8-oxoguanosine by a high-fidelity DNA polymerase. EMBO J. 2004, 23:3452-3461.
    • (2004) EMBO J. , vol.23 , pp. 3452-3461
    • Brieba, L.G.1    Eichman, B.F.2    Kokoska, R.J.3    Doublie, S.4    Kunkel, T.A.5    Ellenberger, T.6
  • 120
    • 4544273926 scopus 로고    scopus 로고
    • Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase
    • Hsu G.W., Ober M., Carell T., Beese L.S. Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase. Nature 2004, 431:217-221.
    • (2004) Nature , vol.431 , pp. 217-221
    • Hsu, G.W.1    Ober, M.2    Carell, T.3    Beese, L.S.4
  • 121
    • 0037966257 scopus 로고
    • Escherichia coli mutY gene product is required for specific A-G--C.G mismatch correction
    • Au K.G., Cabrera M., Miller J.H., Modrich P. Escherichia coli mutY gene product is required for specific A-G--C.G mismatch correction. Proc. Natl. Acad. Sci. USA 1988, 85:9163-9166.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9163-9166
    • Au, K.G.1    Cabrera, M.2    Miller, J.H.3    Modrich, P.4
  • 122
    • 0028831129 scopus 로고
    • Characterization of a mammalian homolog of the Escherichia coli MutY mismatch repair protein
    • McGoldrick J.P., Yeh Y.C., Solomon M., Essigmann J.M., Lu A.L. Characterization of a mammalian homolog of the Escherichia coli MutY mismatch repair protein. Mol. Cell Biol. 1995, 15:989-996.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 989-996
    • McGoldrick, J.P.1    Yeh, Y.C.2    Solomon, M.3    Essigmann, J.M.4    Lu, A.L.5
  • 123
    • 0028825742 scopus 로고
    • DNA determinants and substrate specificities of Escherichia coli MutY
    • Lu A.L., Tsai-Wu J.J., Cillo J. DNA determinants and substrate specificities of Escherichia coli MutY. J. Biol. Chem. 1995, 270:23582-23588.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23582-23588
    • Lu, A.L.1    Tsai-Wu, J.J.2    Cillo, J.3
  • 124
    • 0030004207 scopus 로고    scopus 로고
    • Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage
    • Slupska M.M., Baikalov C., Luther W.M., Chiang J.H., Wei Y.F., Miller J.H. Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage. J. Bacteriol. 1996, 178:3885-3892.
    • (1996) J. Bacteriol. , vol.178 , pp. 3885-3892
    • Slupska, M.M.1    Baikalov, C.2    Luther, W.M.3    Chiang, J.H.4    Wei, Y.F.5    Miller, J.H.6
  • 125
    • 0032840464 scopus 로고    scopus 로고
    • Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein
    • Slupska M.M., Luther W.M., Chiang J.H., Yang H., Miller J.H. Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein. J. Bacteriol. 1999, 181:6210-6213.
    • (1999) J. Bacteriol. , vol.181 , pp. 6210-6213
    • Slupska, M.M.1    Luther, W.M.2    Chiang, J.H.3    Yang, H.4    Miller, J.H.5
  • 126
    • 0042527365 scopus 로고    scopus 로고
    • Repair of DNA containing Fapy.dG and its beta-C-nucleoside analogue by formamidopyrimidine DNA glycosylase and MutY
    • Wiederholt C.J., Delaney M.O., Pope M.A., David S.S., Greenberg M.M. Repair of DNA containing Fapy.dG and its beta-C-nucleoside analogue by formamidopyrimidine DNA glycosylase and MutY. Biochemistry 2003, 42:9755-9760.
    • (2003) Biochemistry , vol.42 , pp. 9755-9760
    • Wiederholt, C.J.1    Delaney, M.O.2    Pope, M.A.3    David, S.S.4    Greenberg, M.M.5
  • 127
    • 7944228647 scopus 로고    scopus 로고
    • DNA damage recognition and repair by the murine MutY homologue
    • Pope M.A., David S.S. DNA damage recognition and repair by the murine MutY homologue. DNA Repair (Amst.) 2005, 4:91-102.
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 91-102
    • Pope, M.A.1    David, S.S.2
  • 129
    • 1342304229 scopus 로고    scopus 로고
    • Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase
    • Fromme J.C., Banerjee A., Huang S.J., Verdine G.L. Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase. Nature 2004, 427:652-656.
    • (2004) Nature , vol.427 , pp. 652-656
    • Fromme, J.C.1    Banerjee, A.2    Huang, S.J.3    Verdine, G.L.4
  • 130
    • 0025301064 scopus 로고
    • MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III
    • Michaels M.L., Pham L., Nghiem Y., Cruz C., Miller J.H. MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III. Nucleic Acids Res. 1990, 18:3841-3845.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3841-3845
    • Michaels, M.L.1    Pham, L.2    Nghiem, Y.3    Cruz, C.4    Miller, J.H.5
  • 131
    • 0030979263 scopus 로고    scopus 로고
    • DNA glycosylases
    • Cunningham R.P. DNA glycosylases. Mutat. Res. 1997, 383:189-196.
    • (1997) Mutat. Res. , vol.383 , pp. 189-196
    • Cunningham, R.P.1
  • 132
    • 0037040962 scopus 로고    scopus 로고
    • Activation of human MutS homologs by 8-oxo-guanine DNA damage
    • Mazurek A., Berardini M., Fishel R. Activation of human MutS homologs by 8-oxo-guanine DNA damage. J. Biol. Chem. 2002, 277:8260-8266.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8260-8266
    • Mazurek, A.1    Berardini, M.2    Fishel, R.3
  • 134
    • 24944557945 scopus 로고    scopus 로고
    • 8-Oxoguanine incorporation into DNA repeats in vitro and mismatch recognition by MutSalpha
    • Macpherson P., Barone F., Maga G., Mazzei F., Karran P., Bignami M. 8-Oxoguanine incorporation into DNA repeats in vitro and mismatch recognition by MutSalpha. Nucleic Acids Res. 2005, 33:5094-5105.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5094-5105
    • Macpherson, P.1    Barone, F.2    Maga, G.3    Mazzei, F.4    Karran, P.5    Bignami, M.6
  • 137
    • 0034812540 scopus 로고    scopus 로고
    • Age-related and tissue-specific accumulation of oxidative DNA base damage in 7,8-dihydro-8-oxoguanine-DNA glycosylase (Ogg1) deficient mice
    • Osterod M., Hollenbach S., Hengstler J.G., Barnes D.E., Lindahl T., Epe B. Age-related and tissue-specific accumulation of oxidative DNA base damage in 7,8-dihydro-8-oxoguanine-DNA glycosylase (Ogg1) deficient mice. Carcinogenesis 2001, 22:1459-1463.
    • (2001) Carcinogenesis , vol.22 , pp. 1459-1463
    • Osterod, M.1    Hollenbach, S.2    Hengstler, J.G.3    Barnes, D.E.4    Lindahl, T.5    Epe, B.6
  • 138
    • 0036955119 scopus 로고    scopus 로고
    • High accumulation of oxidative DNA damage, 8-hydroxyguanine, in Mmh/Ogg1 deficient mice by chronic oxidative stress
    • Arai T., Kelly V.P., Minowa O., Noda T., Nishimura S. High accumulation of oxidative DNA damage, 8-hydroxyguanine, in Mmh/Ogg1 deficient mice by chronic oxidative stress. Carcinogenesis 2002, 23:2005-2010.
    • (2002) Carcinogenesis , vol.23 , pp. 2005-2010
    • Arai, T.1    Kelly, V.P.2    Minowa, O.3    Noda, T.4    Nishimura, S.5
  • 139
  • 142
  • 143
    • 13944281044 scopus 로고    scopus 로고
    • Polymorphic variation in hOGG1 and risk of cancer: a review of the functional and epidemiologic literature
    • Weiss J.M., Goode E.L., Ladiges W.C., Ulrich C.M. Polymorphic variation in hOGG1 and risk of cancer: a review of the functional and epidemiologic literature. Mol. Carcinog. 2005, 42:127-141.
    • (2005) Mol. Carcinog. , vol.42 , pp. 127-141
    • Weiss, J.M.1    Goode, E.L.2    Ladiges, W.C.3    Ulrich, C.M.4
  • 144
    • 53549117748 scopus 로고    scopus 로고
    • The hOGG1 Ser326Cys polymorphism and lung cancer risk: a meta-analysis
    • Li H., Hao X., Zhang W., Wei Q., Chen K. The hOGG1 Ser326Cys polymorphism and lung cancer risk: a meta-analysis. Cancer Epidemiol. Biomarkers Prev. 2008, 17:1739-1745.
    • (2008) Cancer Epidemiol. Biomarkers Prev. , vol.17 , pp. 1739-1745
    • Li, H.1    Hao, X.2    Zhang, W.3    Wei, Q.4    Chen, K.5
  • 145
    • 69949183601 scopus 로고    scopus 로고
    • Interactive effect of cigarette smoking with human 8-oxoguanine DNA N-glycosylase 1 (hOGG1) polymorphisms on the risk of lung cancer: a case-control study in Taiwan
    • Chang C.H., Hsiao C.F., Chang G.C., Tsai Y.H., Chen Y.M., Huang M.S., Su W.C., Hsieh W.S., Yang P.C., Chen C.J., Hsiung C.A. Interactive effect of cigarette smoking with human 8-oxoguanine DNA N-glycosylase 1 (hOGG1) polymorphisms on the risk of lung cancer: a case-control study in Taiwan. Am. J. Epidemiol. 2009, 170:695-702.
    • (2009) Am. J. Epidemiol. , vol.170 , pp. 695-702
    • Chang, C.H.1    Hsiao, C.F.2    Chang, G.C.3    Tsai, Y.H.4    Chen, Y.M.5    Huang, M.S.6    Su, W.C.7    Hsieh, W.S.8    Yang, P.C.9    Chen, C.J.10    Hsiung, C.A.11
  • 147
    • 77955662755 scopus 로고    scopus 로고
    • Lack of association between the hOGG1 Ser326Cys polymorphism and breast cancer risk: evidence from 11 case-control studies
    • Gu D., Wang M., Zhang Z., Chen J. Lack of association between the hOGG1 Ser326Cys polymorphism and breast cancer risk: evidence from 11 case-control studies. Breast Cancer Res. Treat. 2010, 122:527-531.
    • (2010) Breast Cancer Res. Treat. , vol.122 , pp. 527-531
    • Gu, D.1    Wang, M.2    Zhang, Z.3    Chen, J.4
  • 151
    • 79955755852 scopus 로고    scopus 로고
    • HOGG1 Ser326Cys polymorphism and renal cell carcinoma risk in a Chinese population
    • Zhao H., Qin C., Yan F., Wu B., Cao Q., Wang M., Zhang Z., Yin C. hOGG1 Ser326Cys polymorphism and renal cell carcinoma risk in a Chinese population. DNA Cell Biol. 2011, 30:317-321.
    • (2011) DNA Cell Biol. , vol.30 , pp. 317-321
    • Zhao, H.1    Qin, C.2    Yan, F.3    Wu, B.4    Cao, Q.5    Wang, M.6    Zhang, Z.7    Yin, C.8
  • 152
    • 79958244828 scopus 로고    scopus 로고
    • Two functional variations in 5'-UTR of hoGG1 gene associated with the risk of breast cancer in Chinese
    • Chen X., Wang J., Guo W., Liu X., Sun C., Cai Z., Fan Y., Wang Y. Two functional variations in 5'-UTR of hoGG1 gene associated with the risk of breast cancer in Chinese. Breast Cancer Res. Treat. 2011, 127:795-803.
    • (2011) Breast Cancer Res. Treat. , vol.127 , pp. 795-803
    • Chen, X.1    Wang, J.2    Guo, W.3    Liu, X.4    Sun, C.5    Cai, Z.6    Fan, Y.7    Wang, Y.8
  • 153
    • 0034661689 scopus 로고    scopus 로고
    • Effect of single mutations in the OGG1 gene found in human tumors on the substrate specificity of the Ogg1 protein
    • Audebert M., Radicella J.P., Dizdaroglu M. Effect of single mutations in the OGG1 gene found in human tumors on the substrate specificity of the Ogg1 protein. Nucleic Acids Res. 2000, 28:2672-2678.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2672-2678
    • Audebert, M.1    Radicella, J.P.2    Dizdaroglu, M.3
  • 154
    • 0033569954 scopus 로고    scopus 로고
    • Excision of oxidatively damaged DNA bases by the human alpha-hOgg1 protein and the polymorphic alpha-hOgg1(Ser326Cys) protein which is frequently found in human populations
    • Dherin C., Radicella J.P., Dizdaroglu M., Boiteux S. Excision of oxidatively damaged DNA bases by the human alpha-hOgg1 protein and the polymorphic alpha-hOgg1(Ser326Cys) protein which is frequently found in human populations. Nucleic Acids Res. 1999, 27:4001-4007.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4001-4007
    • Dherin, C.1    Radicella, J.P.2    Dizdaroglu, M.3    Boiteux, S.4
  • 155
    • 69449104051 scopus 로고    scopus 로고
    • Substrate specificity and excision kinetics of natural polymorphic variants and phosphomimetic mutants of human 8-oxoguanine-DNA glycosylase
    • Sidorenko V.S., Grollman A.P., Jaruga P., Dizdaroglu M., Zharkov D.O. Substrate specificity and excision kinetics of natural polymorphic variants and phosphomimetic mutants of human 8-oxoguanine-DNA glycosylase. FEBS J. 2009, 276:5149-5162.
    • (2009) FEBS J. , vol.276 , pp. 5149-5162
    • Sidorenko, V.S.1    Grollman, A.P.2    Jaruga, P.3    Dizdaroglu, M.4    Zharkov, D.O.5
  • 156
    • 0035833661 scopus 로고    scopus 로고
    • DNA repair activity of 8-oxoguanine DNA glycosylase 1 (OGG1) in human lymphocytes is not dependent on genetic polymorphism Ser326/Cys326
    • Janssen K., Schlink K., Gotte W., Hippler B., Kaina B., Oesch F. DNA repair activity of 8-oxoguanine DNA glycosylase 1 (OGG1) in human lymphocytes is not dependent on genetic polymorphism Ser326/Cys326. Mutat. Res. 2001, 486:207-216.
    • (2001) Mutat. Res. , vol.486 , pp. 207-216
    • Janssen, K.1    Schlink, K.2    Gotte, W.3    Hippler, B.4    Kaina, B.5    Oesch, F.6
  • 157
    • 0032565998 scopus 로고    scopus 로고
    • Genetic polymorphisms and alternative splicing of the hOGG1 gene, that is involved in the repair of 8-hydroxyguanine in damaged DNA
    • Kohno T., Shinmura K., Tosaka M., Tani M., Kim S.R., Sugimura H., Nohmi T., Kasai H., Yokota J. Genetic polymorphisms and alternative splicing of the hOGG1 gene, that is involved in the repair of 8-hydroxyguanine in damaged DNA. Oncogene 1998, 16:3219-3225.
    • (1998) Oncogene , vol.16 , pp. 3219-3225
    • Kohno, T.1    Shinmura, K.2    Tosaka, M.3    Tani, M.4    Kim, S.R.5    Sugimura, H.6    Nohmi, T.7    Kasai, H.8    Yokota, J.9
  • 158
    • 4344611782 scopus 로고    scopus 로고
    • Differential ability of polymorphic OGG1 proteins to suppress mutagenesis induced by 8-hydroxyguanine in human cell in vivo
    • Yamane A., Kohno T., Ito K., Sunaga N., Aoki K., Yoshimura K., Murakami H., Nojima Y., Yokota J. Differential ability of polymorphic OGG1 proteins to suppress mutagenesis induced by 8-hydroxyguanine in human cell in vivo. Carcinogenesis 2004, 25:1689-1694.
    • (2004) Carcinogenesis , vol.25 , pp. 1689-1694
    • Yamane, A.1    Kohno, T.2    Ito, K.3    Sunaga, N.4    Aoki, K.5    Yoshimura, K.6    Murakami, H.7    Nojima, Y.8    Yokota, J.9
  • 159
    • 33645472299 scopus 로고    scopus 로고
    • Dimerization and opposite base-dependent catalytic impairment of polymorphic S326C OGG1 glycosylase
    • Hill J.W., Evans M.K. Dimerization and opposite base-dependent catalytic impairment of polymorphic S326C OGG1 glycosylase. Nucleic Acids Res. 2006, 34:1620-1632.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1620-1632
    • Hill, J.W.1    Evans, M.K.2
  • 160
    • 33750010979 scopus 로고    scopus 로고
    • Activity of OGG1 variants in the repair of pro-oxidant-induced 8-oxo-2'-deoxyguanosine
    • Smart D.J., Chipman J.K., Hodges N.J. Activity of OGG1 variants in the repair of pro-oxidant-induced 8-oxo-2'-deoxyguanosine. DNA Repair (Amst.) 2006, 5:1337-1345.
    • (2006) DNA Repair (Amst.) , vol.5 , pp. 1337-1345
    • Smart, D.J.1    Chipman, J.K.2    Hodges, N.J.3
  • 161
    • 65949112277 scopus 로고    scopus 로고
    • Oxidation status of human OGG1-S326C polymorphic variant determines cellular DNA repair capacity
    • Bravard A., Vacher M., Moritz E., Vaslin L., Hall J., Epe B., Radicella J.P. Oxidation status of human OGG1-S326C polymorphic variant determines cellular DNA repair capacity. Cancer Res. 2009, 69:3642-3649.
    • (2009) Cancer Res. , vol.69 , pp. 3642-3649
    • Bravard, A.1    Vacher, M.2    Moritz, E.3    Vaslin, L.4    Hall, J.5    Epe, B.6    Radicella, J.P.7
  • 162
    • 17844409595 scopus 로고    scopus 로고
    • Dynamic relocalization of hOGG1 during the cell cycle is disrupted in cells harbouring the hOGG1-Cys326 polymorphic variant
    • Luna L., Rolseth V., Hildrestrand G.A., Otterlei M., Dantzer F., Bjoras M., Seeberg E. Dynamic relocalization of hOGG1 during the cell cycle is disrupted in cells harbouring the hOGG1-Cys326 polymorphic variant. Nucleic Acids Res. 2005, 33:1813-1824.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 1813-1824
    • Luna, L.1    Rolseth, V.2    Hildrestrand, G.A.3    Otterlei, M.4    Dantzer, F.5    Bjoras, M.6    Seeberg, E.7
  • 164
    • 67650302611 scopus 로고    scopus 로고
    • Catalytically impaired hMYH and NEIL1 mutant proteins identified in patients with primary sclerosing cholangitis and cholangiocarcinoma
    • Forsbring M., Vik E.S., Dalhus B., Karlsen T.H., Bergquist A., Schrumpf E., Bjoras M., Boberg K.M., Alseth I. Catalytically impaired hMYH and NEIL1 mutant proteins identified in patients with primary sclerosing cholangitis and cholangiocarcinoma. Carcinogenesis 2009, 30:1147-1154.
    • (2009) Carcinogenesis , vol.30 , pp. 1147-1154
    • Forsbring, M.1    Vik, E.S.2    Dalhus, B.3    Karlsen, T.H.4    Bergquist, A.5    Schrumpf, E.6    Bjoras, M.7    Boberg, K.M.8    Alseth, I.9
  • 165
  • 168
    • 33847333956 scopus 로고    scopus 로고
    • MUTYH-associated polyposis - from defect in base excision repair to clinical genetic testing
    • Cheadle J.P., Sampson J.R. MUTYH-associated polyposis - from defect in base excision repair to clinical genetic testing. DNA Repair (Amst.) 2007, 6:274-279.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 274-279
    • Cheadle, J.P.1    Sampson, J.R.2
  • 169
    • 34250900982 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage
    • David S.S., O'Shea V.L., Kundu S. Base-excision repair of oxidative DNA damage. Nature 2007, 447:941-950.
    • (2007) Nature , vol.447 , pp. 941-950
    • David, S.S.1    O'Shea, V.L.2    Kundu, S.3
  • 171
    • 0141960200 scopus 로고    scopus 로고
    • Exposing the MYtH about base excision repair and human inherited disease
    • Cheadle J.P., Sampson J.R. Exposing the MYtH about base excision repair and human inherited disease. Hum. Mol. Genet. 12 Spec. No. 2003, 2:R159-R165.
    • (2003) Hum. Mol. Genet. 12 Spec. No. , vol.2
    • Cheadle, J.P.1    Sampson, J.R.2
  • 175
    • 33644511436 scopus 로고    scopus 로고
    • Structure of a DNA glycosylase searching for lesions
    • Banerjee A., Santos W.L., Verdine G.L. Structure of a DNA glycosylase searching for lesions. Science 2006, 311:1153-1157.
    • (2006) Science , vol.311 , pp. 1153-1157
    • Banerjee, A.1    Santos, W.L.2    Verdine, G.L.3
  • 176
    • 80053206516 scopus 로고    scopus 로고
    • Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA
    • Dunn A.R., Kad N.M., Nelson S.R., Warshaw D.M., Wallace S.S. Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA. Nucleic Acids Res. 2011, 39:7487-7498.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 7487-7498
    • Dunn, A.R.1    Kad, N.M.2    Nelson, S.R.3    Warshaw, D.M.4    Wallace, S.S.5
  • 177
    • 0037459233 scopus 로고    scopus 로고
    • Insight into the functional consequences of inherited variants of the hMYH adenine glycosylase associated with colorectal cancer: complementation assays with hMYH variants and pre-steady-state kinetics of the corresponding mutated E. coli enzymes
    • Chmiel N.H., Livingston A.L., David S.S. Insight into the functional consequences of inherited variants of the hMYH adenine glycosylase associated with colorectal cancer: complementation assays with hMYH variants and pre-steady-state kinetics of the corresponding mutated E. coli enzymes. J. Mol. Biol. 2003, 327:431-443.
    • (2003) J. Mol. Biol. , vol.327 , pp. 431-443
    • Chmiel, N.H.1    Livingston, A.L.2    David, S.S.3
  • 179
    • 13744261252 scopus 로고    scopus 로고
    • Functional characterization of two human MutY homolog (hMYH) missense mutations (R227W and V232F) that lie within the putative hMSH6 binding domain and are associated with hMYH polyposis
    • Bai H., Jones S., Guan X., Wilson T.M., Sampson J.R., Cheadle J.P., Lu A.L. Functional characterization of two human MutY homolog (hMYH) missense mutations (R227W and V232F) that lie within the putative hMSH6 binding domain and are associated with hMYH polyposis. Nucleic Acids Res. 2005, 33:597-604.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 597-604
    • Bai, H.1    Jones, S.2    Guan, X.3    Wilson, T.M.4    Sampson, J.R.5    Cheadle, J.P.6    Lu, A.L.7
  • 180
    • 33947580840 scopus 로고    scopus 로고
    • Functional characterization of human MutY homolog (hMYH) missense mutation (R231L) that is linked with hMYH-associated polyposis
    • Bai H., Grist S., Gardner J., Suthers G., Wilson T.M., Lu A.L. Functional characterization of human MutY homolog (hMYH) missense mutation (R231L) that is linked with hMYH-associated polyposis. Cancer Lett. 2007, 250:74-81.
    • (2007) Cancer Lett. , vol.250 , pp. 74-81
    • Bai, H.1    Grist, S.2    Gardner, J.3    Suthers, G.4    Wilson, T.M.5    Lu, A.L.6
  • 181
    • 48549095660 scopus 로고    scopus 로고
    • Characterization of mutant MUTYH proteins associated with familial colorectal cancer
    • Ali M., Kim H., Cleary S., Cupples C., Gallinger S., Bristow R. Characterization of mutant MUTYH proteins associated with familial colorectal cancer. Gastroenterology 2008, 135:499-507.
    • (2008) Gastroenterology , vol.135 , pp. 499-507
    • Ali, M.1    Kim, H.2    Cleary, S.3    Cupples, C.4    Gallinger, S.5    Bristow, R.6
  • 182
    • 70450224248 scopus 로고    scopus 로고
    • Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associated with colorectal cancer
    • Kundu S., Brinkmeyer M.K., Livingston A.L., David S.S. Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associated with colorectal cancer. DNA Repair (Amst.) 2009, 8:1400-1410.
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 1400-1410
    • Kundu, S.1    Brinkmeyer, M.K.2    Livingston, A.L.3    David, S.S.4
  • 184
    • 78049418933 scopus 로고    scopus 로고
    • Adenine DNA glycosylase activity of 14 human MutY homolog (MUTYH) variant proteins found in patients with colorectal polyposis and cancer
    • Goto M., Shinmura K., Nakabeppu Y., Tao H., Yamada H., Tsuneyoshi T., Sugimura H. Adenine DNA glycosylase activity of 14 human MutY homolog (MUTYH) variant proteins found in patients with colorectal polyposis and cancer. Hum. Mutat. 2010, 31:E1861-1874.
    • (2010) Hum. Mutat. , vol.31
    • Goto, M.1    Shinmura, K.2    Nakabeppu, Y.3    Tao, H.4    Yamada, H.5    Tsuneyoshi, T.6    Sugimura, H.7
  • 186
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
    • Maki H., Sekiguchi M. MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Nature 1992, 355:273-275.
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 187
    • 0027368923 scopus 로고
    • Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis
    • Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., Sekiguchi M. Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 1993, 268:23524-23530.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23524-23530
    • Sakumi, K.1    Furuichi, M.2    Tsuzuki, T.3    Kakuma, T.4    Kawabata, S.5    Maki, H.6    Sekiguchi, M.7
  • 188
    • 0028566359 scopus 로고
    • Genomic structure and chromosome location of the human mutT homologue gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to C:G transversion
    • Furuichi M., Yoshida M.C., Oda H., Tajiri T., Nakabeppu Y., Tsuzuki T., Sekiguchi M. Genomic structure and chromosome location of the human mutT homologue gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to C:G transversion. Genomics 1994, 24:485-490.
    • (1994) Genomics , vol.24 , pp. 485-490
    • Furuichi, M.1    Yoshida, M.C.2    Oda, H.3    Tajiri, T.4    Nakabeppu, Y.5    Tsuzuki, T.6    Sekiguchi, M.7
  • 189
    • 0033580647 scopus 로고    scopus 로고
    • The C-terminal domain of the adenine-DNA glycosylase MutY confers specificity for 8-oxoguanine.adenine mispairs and may have evolved from MutT, an 8-oxo-dGTPase
    • Noll D.M., Gogos A., Granek J.A., Clarke N.D. The C-terminal domain of the adenine-DNA glycosylase MutY confers specificity for 8-oxoguanine.adenine mispairs and may have evolved from MutT, an 8-oxo-dGTPase. Biochemistry 1999, 38:6374-6379.
    • (1999) Biochemistry , vol.38 , pp. 6374-6379
    • Noll, D.M.1    Gogos, A.2    Granek, J.A.3    Clarke, N.D.4
  • 190
    • 0035863770 scopus 로고    scopus 로고
    • Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain
    • Chmiel N.H., Golinelli M.P., Francis A.W., David S.S. Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain. Nucleic Acids Res. 2001, 29:553-564.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 553-564
    • Chmiel, N.H.1    Golinelli, M.P.2    Francis, A.W.3    David, S.S.4
  • 197
    • 0030890419 scopus 로고    scopus 로고
    • Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III
    • Hilbert T.P., Chaung W., Boorstein R.J., Cunningham R.P., Teebor G.W. Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III. J. Biol. Chem. 1997, 272:6733-6740.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6733-6740
    • Hilbert, T.P.1    Chaung, W.2    Boorstein, R.J.3    Cunningham, R.P.4    Teebor, G.W.5
  • 198
    • 0032555571 scopus 로고    scopus 로고
    • Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue
    • Ikeda S., Biswas T., Roy R., Izumi T., Boldogh I., Kurosky A., Sarker A.H., Seki S., Mitra S. Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue. J. Biol. Chem. 1998, 273:21585-21593.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21585-21593
    • Ikeda, S.1    Biswas, T.2    Roy, R.3    Izumi, T.4    Boldogh, I.5    Kurosky, A.6    Sarker, A.H.7    Seki, S.8    Mitra, S.9
  • 201
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer M.M., Ahern H., Xing D., Cunningham R.P., Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 1995, 14:4108-4120.
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 203
    • 41249094475 scopus 로고    scopus 로고
    • Interaction of the human DNA glycosylase NEIL1 with proliferating cell nuclear antigen. The potential for replication-associated repair of oxidized bases in mammalian genomes
    • Dou H., Theriot C.A., Das A., Hegde M.L., Matsumoto Y., Boldogh I., Hazra T.K., Bhakat K.K., Mitra S. Interaction of the human DNA glycosylase NEIL1 with proliferating cell nuclear antigen. The potential for replication-associated repair of oxidized bases in mammalian genomes. J. Biol. Chem. 2008, 283:3130-3140.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3130-3140
    • Dou, H.1    Theriot, C.A.2    Das, A.3    Hegde, M.L.4    Matsumoto, Y.5    Boldogh, I.6    Hazra, T.K.7    Bhakat, K.K.8    Mitra, S.9
  • 204
    • 55249083320 scopus 로고    scopus 로고
    • Physical and functional interaction between human oxidized base-specific DNA glycosylase NEIL1 and flap endonuclease 1
    • Hegde M.L., Theriot C.A., Das A., Hegde P.M., Guo Z., Gary R.K., Hazra T.K., Shen B., Mitra S. Physical and functional interaction between human oxidized base-specific DNA glycosylase NEIL1 and flap endonuclease 1. J. Biol. Chem. 2008, 283:27028-27037.
    • (2008) J. Biol. Chem. , vol.283 , pp. 27028-27037
    • Hegde, M.L.1    Theriot, C.A.2    Das, A.3    Hegde, P.M.4    Guo, Z.5    Gary, R.K.6    Hazra, T.K.7    Shen, B.8    Mitra, S.9
  • 205
    • 77952580830 scopus 로고    scopus 로고
    • RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures
    • Theriot C.A., Hegde M.L., Hazra T.K., Mitra S. RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures. DNA Repair (Amst.) 2010, 9:643-652.
    • (2010) DNA Repair (Amst.) , vol.9 , pp. 643-652
    • Theriot, C.A.1    Hegde, M.L.2    Hazra, T.K.3    Mitra, S.4
  • 206
    • 0037125133 scopus 로고    scopus 로고
    • A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII
    • Bandaru V., Sunkara S., Wallace S.S., Bond J.P. A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII. DNA Repair (Amst.) 2002, 1:517-529.
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 517-529
    • Bandaru, V.1    Sunkara, S.2    Wallace, S.S.3    Bond, J.P.4
  • 207
    • 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., Izumi T. Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions. J. Biol. Chem. 2002, 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
  • 208
    • 0037112668 scopus 로고    scopus 로고
    • Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA
    • Morland I., Rolseth V., Luna L., Rognes T., Bjoras M., Seeberg E. Human DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNA. Nucleic Acids Res. 2002, 30:4926-4936.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4926-4936
    • Morland, I.1    Rolseth, V.2    Luna, L.3    Rognes, T.4    Bjoras, M.5    Seeberg, E.6
  • 210
    • 10844284635 scopus 로고    scopus 로고
    • Mouse NEIL1 protein is specific for excision of 2,6-diamino-4-hydroxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidine from oxidatively damaged DNA
    • Jaruga P., Birincioglu M., Rosenquist T.A., Dizdaroglu M. Mouse NEIL1 protein is specific for excision of 2,6-diamino-4-hydroxy-5-formamidopyrimidine and 4,6-diamino-5-formamidopyrimidine from oxidatively damaged DNA. Biochemistry 2004, 43:15909-15914.
    • (2004) Biochemistry , vol.43 , pp. 15909-15914
    • Jaruga, P.1    Birincioglu, M.2    Rosenquist, T.A.3    Dizdaroglu, M.4
  • 211
    • 1842638748 scopus 로고    scopus 로고
    • Differential specificity of human and Escherichia coli endonuclease III and VIII homologues for oxidative base lesions
    • Katafuchi A., Nakano T., Masaoka A., Terato H., Iwai S., Hanaoka F., Ide H. Differential specificity of human and Escherichia coli endonuclease III and VIII homologues for oxidative base lesions. J. Biol. Chem. 2004, 279:14464-14471.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14464-14471
    • Katafuchi, A.1    Nakano, T.2    Masaoka, A.3    Terato, H.4    Iwai, S.5    Hanaoka, F.6    Ide, H.7
  • 214
    • 7944227532 scopus 로고    scopus 로고
    • DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells
    • Zhang Q.M., Yonekura S., Takao M., Yasui A., Sugiyama H., Yonei S. DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells. DNA Repair (Amst.) 2005, 4:71-79.
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 71-79
    • Zhang, Q.M.1    Yonekura, S.2    Takao, M.3    Yasui, A.4    Sugiyama, H.5    Yonei, S.6
  • 216
    • 77951285397 scopus 로고    scopus 로고
    • The role of mammalian NEIL1 protein in the repair of 8-oxo-7,8-dihydroadenine in DNA
    • Grin I.R., Dianov G.L., Zharkov D.O. The role of mammalian NEIL1 protein in the repair of 8-oxo-7,8-dihydroadenine in DNA. FEBS Lett. 2010, 584:1553-1557.
    • (2010) FEBS Lett. , vol.584 , pp. 1553-1557
    • Grin, I.R.1    Dianov, G.L.2    Zharkov, D.O.3
  • 217
    • 46849104669 scopus 로고    scopus 로고
    • Superior removal of hydantoin lesions relative to other oxidized bases by the human DNA glycosylase hNEIL1
    • Krishnamurthy N., Zhao X., Burrows C.J., David S.S. Superior removal of hydantoin lesions relative to other oxidized bases by the human DNA glycosylase hNEIL1. Biochemistry 2008, 47:7137-7146.
    • (2008) Biochemistry , vol.47 , pp. 7137-7146
    • Krishnamurthy, N.1    Zhao, X.2    Burrows, C.J.3    David, S.S.4
  • 218
    • 77749252749 scopus 로고    scopus 로고
    • Mutation versus repair: NEIL1 removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts
    • Zhao X., Krishnamurthy N., Burrows C.J., David S.S. Mutation versus repair: NEIL1 removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts. Biochemistry 2010, 49:1658-1666.
    • (2010) Biochemistry , vol.49 , pp. 1658-1666
    • Zhao, X.1    Krishnamurthy, N.2    Burrows, C.J.3    David, S.S.4
  • 219
    • 3142702720 scopus 로고    scopus 로고
    • The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity
    • Doublie S., Bandaru V., Bond J.P., Wallace S.S. The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity. Proc. Natl. Acad. Sci. USA 2004, 101:10284-10289.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10284-10289
    • Doublie, S.1    Bandaru, V.2    Bond, J.P.3    Wallace, S.S.4
  • 220
    • 0347379928 scopus 로고    scopus 로고
    • Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2
    • Dou H., Mitra S., Hazra T.K. Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2. J. Biol. Chem. 2003, 278:49679-49684.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49679-49684
    • Dou, H.1    Mitra, S.2    Hazra, T.K.3
  • 221
    • 7944222565 scopus 로고    scopus 로고
    • Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2
    • Hailer M.K., Slade P.G., Martin B.D., Rosenquist T.A., Sugden K.D. Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2. DNA Repair (Amst.) 2005, 4:41-50.
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 41-50
    • Hailer, M.K.1    Slade, P.G.2    Martin, B.D.3    Rosenquist, T.A.4    Sugden, K.D.5
  • 224
    • 32944471308 scopus 로고    scopus 로고
    • Hematopoietic tissue-specific expression of mouse Neil3 for endonuclease VIII-like protein
    • Torisu K., Tsuchimoto D., Ohnishi Y., Nakabeppu Y. Hematopoietic tissue-specific expression of mouse Neil3 for endonuclease VIII-like protein. J. Biochem. 2005, 138:763-772.
    • (2005) J. Biochem. , vol.138 , pp. 763-772
    • Torisu, K.1    Tsuchimoto, D.2    Ohnishi, Y.3    Nakabeppu, Y.4
  • 225
    • 60849115568 scopus 로고    scopus 로고
    • Human Nei-like protein NEIL3 has AP lyase activity specific for single-stranded DNA and confers oxidative stress resistance in Escherichia coli mutant
    • Takao M., Oohata Y., Kitadokoro K., Kobayashi K., Iwai S., Yasui A., Yonei S., Zhang Q.M. Human Nei-like protein NEIL3 has AP lyase activity specific for single-stranded DNA and confers oxidative stress resistance in Escherichia coli mutant. Genes. Cells 2009, 14:261-270.
    • (2009) Genes. Cells , vol.14 , pp. 261-270
    • Takao, M.1    Oohata, Y.2    Kitadokoro, K.3    Kobayashi, K.4    Iwai, S.5    Yasui, A.6    Yonei, S.7    Zhang, Q.M.8
  • 235
    • 27844501168 scopus 로고    scopus 로고
    • Molecular and biological roles of Ape1 protein in mammalian base excision repair
    • Demple B., Sung J.S. Molecular and biological roles of Ape1 protein in mammalian base excision repair. DNA Repair (Amst.) 2005, 4:1442-1449.
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 1442-1449
    • Demple, B.1    Sung, J.S.2
  • 236
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis S., Miao G., Wang F., Pan Y.C., Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 1992, 11:3323-3335.
    • (1992) EMBO J. , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.C.4    Curran, T.5
  • 238
    • 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 1991, 88:11450-11454.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 239
    • 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. Nucleic Acids Res. 1991, 19:5519-5523.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5519-5523
    • Robson, C.N.1    Hickson, I.D.2
  • 240
    • 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 1992, 1131:287-299.
    • (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
  • 241
    • 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., de La Fortelle E., Mol C.D., Tainer J.A., Hickson I.D., Freemont P.S. The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites. EMBO J. 1997, 16:6548-6558.
    • (1997) EMBO J. , vol.16 , pp. 6548-6558
    • Gorman, M.A.1    Morera, S.2    Rothwell, D.G.3    de La Fortelle, E.4    Mol, C.D.5    Tainer, J.A.6    Hickson, I.D.7    Freemont, P.S.8
  • 242
    • 0034531986 scopus 로고    scopus 로고
    • Second human protein with homology to the Escherichia coli abasic endonuclease exonuclease III
    • Hadi M.Z., Wilson D.M. Second human protein with homology to the Escherichia coli abasic endonuclease exonuclease III. Environ. Mol. Mutagen 2000, 36:312-324.
    • (2000) Environ. Mol. Mutagen , vol.36 , pp. 312-324
    • Hadi, M.Z.1    Wilson, D.M.2
  • 243
    • 33744502385 scopus 로고    scopus 로고
    • Human Ape2 protein has a 3'-5' exonuclease activity that acts preferentially on mismatched base pairs
    • Burkovics P., Szukacsov V., Unk I., Haracska L. Human Ape2 protein has a 3'-5' exonuclease activity that acts preferentially on mismatched base pairs. Nucleic Acids Res. 2006, 34:2508-2515.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 2508-2515
    • Burkovics, P.1    Szukacsov, V.2    Unk, I.3    Haracska, L.4
  • 244
    • 67949109632 scopus 로고    scopus 로고
    • Role of PCNA-dependent stimulation of 3'-phosphodiesterase and 3'-5' exonuclease activities of human Ape2 in repair of oxidative DNA damage
    • Burkovics P., Hajdu I., Szukacsov V., Unk I., Haracska L. Role of PCNA-dependent stimulation of 3'-phosphodiesterase and 3'-5' exonuclease activities of human Ape2 in repair of oxidative DNA damage. Nucleic Acids Res. 2009, 37:4247-4255.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 4247-4255
    • Burkovics, P.1    Hajdu, I.2    Szukacsov, V.3    Unk, I.4    Haracska, L.5
  • 245
    • 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. Determinants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III. J. Mol. Biol. 2002, 316:853-866.
    • (2002) J. Mol. Biol. , vol.316 , pp. 853-866
    • Hadi, M.Z.1    Ginalski, K.2    Nguyen, L.H.3    Wilson, D.M.4
  • 246
    • 79951837402 scopus 로고    scopus 로고
    • Apurinic/apyrimidinic endonuclease 2 is necessary for normal B cell development and recovery of lymphoid progenitors after chemotherapeutic challenge
    • Guikema J.E., Gerstein R.M., Linehan E.K., Cloherty E.K., Evan-Browning E., Tsuchimoto D., Nakabeppu Y., Schrader C.E. Apurinic/apyrimidinic endonuclease 2 is necessary for normal B cell development and recovery of lymphoid progenitors after chemotherapeutic challenge. J. Immunol. 2011, 186:1943-1950.
    • (2011) J. Immunol. , vol.186 , pp. 1943-1950
    • Guikema, J.E.1    Gerstein, R.M.2    Linehan, E.K.3    Cloherty, E.K.4    Evan-Browning, E.5    Tsuchimoto, D.6    Nakabeppu, Y.7    Schrader, C.E.8
  • 247
    • 0029759283 scopus 로고    scopus 로고
    • Redox regulation of AP-1: a link between transcription factor signaling and DNA repair
    • Xanthoudakis S., Curran T. Redox regulation of AP-1: a link between transcription factor signaling and DNA repair. Adv. Exp. Med. Biol. 1996, 387:69-75.
    • (1996) Adv. Exp. Med. Biol. , vol.387 , pp. 69-75
    • Xanthoudakis, S.1    Curran, T.2
  • 251
    • 13244299159 scopus 로고    scopus 로고
    • A vital role for Ape1/Ref1 protein in repairing spontaneous DNA damage in human cells
    • Fung H., Demple B. A vital role for Ape1/Ref1 protein in repairing spontaneous DNA damage in human cells. Mol. Cell 2005, 17:463-470.
    • (2005) Mol. Cell , vol.17 , pp. 463-470
    • Fung, H.1    Demple, B.2
  • 253
    • 2442572164 scopus 로고    scopus 로고
    • Apurinic/apyrimidinic endonuclease (APE/REF-1) haploinsufficient mice display tissue-specific differences in DNA polymerase beta-dependent base excision repair
    • Raffoul J.J., Cabelof D.C., Nakamura J., Meira L.B., Friedberg E.C., Heydari A.R. Apurinic/apyrimidinic endonuclease (APE/REF-1) haploinsufficient mice display tissue-specific differences in DNA polymerase beta-dependent base excision repair. J. Biol. Chem. 2004, 279:18425-18433.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18425-18433
    • Raffoul, J.J.1    Cabelof, D.C.2    Nakamura, J.3    Meira, L.B.4    Friedberg, E.C.5    Heydari, A.R.6
  • 254
    • 33846580207 scopus 로고    scopus 로고
    • High-order interactions among genetic variants in DNA base excision repair pathway genes and smoking in bladder cancer susceptibility
    • Huang M., Dinney C.P., Lin X., Lin J., Grossman H.B., Wu X. High-order interactions among genetic variants in DNA base excision repair pathway genes and smoking in bladder cancer susceptibility. Cancer Epidemiol. Biomarkers Prev. 2007, 16:84-91.
    • (2007) Cancer Epidemiol. Biomarkers Prev. , vol.16 , pp. 84-91
    • Huang, M.1    Dinney, C.P.2    Lin, X.3    Lin, J.4    Grossman, H.B.5    Wu, X.6
  • 255
    • 77953926931 scopus 로고    scopus 로고
    • Genetic variants of XRCC1, APE1, and ADPRT genes and risk of bladder cancer
    • Wang M., Qin C., Zhu J., Yuan L., Fu G., Zhang Z., Yin C. Genetic variants of XRCC1, APE1, and ADPRT genes and risk of bladder cancer. DNA Cell Biol. 2010, 29:303-311.
    • (2010) DNA Cell Biol. , vol.29 , pp. 303-311
    • Wang, M.1    Qin, C.2    Zhu, J.3    Yuan, L.4    Fu, G.5    Zhang, Z.6    Yin, C.7
  • 257
    • 33750311904 scopus 로고    scopus 로고
    • Association of genetic polymorphisms in the base excision repair pathway with lung cancer risk: a meta-analysis
    • Kiyohara C., Takayama K., Nakanishi Y. Association of genetic polymorphisms in the base excision repair pathway with lung cancer risk: a meta-analysis. Lung Cancer 2006, 54:267-283.
    • (2006) Lung Cancer , vol.54 , pp. 267-283
    • Kiyohara, C.1    Takayama, K.2    Nakanishi, Y.3
  • 260
    • 0036203729 scopus 로고    scopus 로고
    • Genetic regulation of ionizing radiation sensitivity and breast cancer risk
    • Hu J.J., Smith T.R., Miller M.S., Lohman K., Case L.D. Genetic regulation of ionizing radiation sensitivity and breast cancer risk. Environ. Mol. Mutagen 2002, 39:208-215.
    • (2002) Environ. Mol. Mutagen , vol.39 , pp. 208-215
    • Hu, J.J.1    Smith, T.R.2    Miller, M.S.3    Lohman, K.4    Case, L.D.5
  • 265
    • 70449688321 scopus 로고    scopus 로고
    • The DNA repair gene APE1 T1349G polymorphism and cancer risk: a meta-analysis of 27 case-control studies
    • Gu D., Wang M., Zhang Z., Chen J. The DNA repair gene APE1 T1349G polymorphism and cancer risk: a meta-analysis of 27 case-control studies. Mutagenesis 2009, 24:507-512.
    • (2009) Mutagenesis , vol.24 , pp. 507-512
    • Gu, D.1    Wang, M.2    Zhang, Z.3    Chen, J.4
  • 268
    • 0035130776 scopus 로고    scopus 로고
    • Common polymorphisms and somatic mutations in human base excision repair genes in ovarian and endometrial cancers
    • Pieretti M., Khattar N.H., Smith S.A. Common polymorphisms and somatic mutations in human base excision repair genes in ovarian and endometrial cancers. Mutat. Res. 2001, 432:53-59.
    • (2001) Mutat. Res. , vol.432 , pp. 53-59
    • Pieretti, M.1    Khattar, N.H.2    Smith, S.A.3
  • 269
    • 0021872030 scopus 로고
    • The mutational specificity of DNA polymerase-beta during in vitro DNA synthesis. Production of frameshift, base substitution, and deletion mutations
    • Kunkel T.A. The mutational specificity of DNA polymerase-beta during in vitro DNA synthesis. Production of frameshift, base substitution, and deletion mutations. J. Biol. Chem. 1985, 260:5787-5796.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5787-5796
    • Kunkel, T.A.1
  • 270
    • 0032080334 scopus 로고    scopus 로고
    • Functional analysis of the amino-terminal 8-kDa domain of DNA polymerase beta as revealed by site-directed mutagenesis. DNA binding and 5'-deoxyribose phosphate lyase activities
    • Prasad R., Beard W.A., Chyan J.Y., Maciejewski M.W., Mullen G.P., Wilson S.H. Functional analysis of the amino-terminal 8-kDa domain of DNA polymerase beta as revealed by site-directed mutagenesis. DNA binding and 5'-deoxyribose phosphate lyase activities. J. Biol. Chem. 1998, 273:11121-11126.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11121-11126
    • Prasad, R.1    Beard, W.A.2    Chyan, J.Y.3    Maciejewski, M.W.4    Mullen, G.P.5    Wilson, S.H.6
  • 271
    • 0034659935 scopus 로고    scopus 로고
    • The lyase activity of the DNA repair protein beta-polymerase protects from DNA-damage-induced cytotoxicity
    • Sobol R.W., Prasad R., Evenski A., Baker A., Yang X.P., Horton J.K., Wilson S.H. The lyase activity of the DNA repair protein beta-polymerase protects from DNA-damage-induced cytotoxicity. Nature 2000, 405:807-810.
    • (2000) Nature , vol.405 , pp. 807-810
    • Sobol, R.W.1    Prasad, R.2    Evenski, A.3    Baker, A.4    Yang, X.P.5    Horton, J.K.6    Wilson, S.H.7
  • 272
    • 0028049441 scopus 로고
    • Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP
    • Pelletier H., Sawaya M.R., Kumar A., Wilson S.H., Kraut J. Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP. Science 1994, 264:1891-1903.
    • (1994) Science , vol.264 , pp. 1891-1903
    • Pelletier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 273
    • 33745211646 scopus 로고    scopus 로고
    • Activities and mechanism of DNA polymerase beta
    • Beard W.A., Prasad R., Wilson S.H. Activities and mechanism of DNA polymerase beta. Methods Enzymol. 2006, 408:91-107.
    • (2006) Methods Enzymol. , vol.408 , pp. 91-107
    • Beard, W.A.1    Prasad, R.2    Wilson, S.H.3
  • 274
    • 77954384819 scopus 로고    scopus 로고
    • Mutagenic conformation of 8-oxo-7,8-dihydro-2'-dGTP in the confines of a DNA polymerase active site
    • Batra V.K., Beard W.A., Hou E.W., Pedersen L.C., Prasad R., Wilson S.H. Mutagenic conformation of 8-oxo-7,8-dihydro-2'-dGTP in the confines of a DNA polymerase active site. Nat. Struct. Mol. Biol. 2010, 17:889-890.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 889-890
    • Batra, V.K.1    Beard, W.A.2    Hou, E.W.3    Pedersen, L.C.4    Prasad, R.5    Wilson, S.H.6
  • 275
    • 77955297664 scopus 로고    scopus 로고
    • DNA polymerase beta ribonucleotide discrimination: insertion, misinsertion, extension, and coding
    • Cavanaugh N.A., Beard W.A., Wilson S.H. DNA polymerase beta ribonucleotide discrimination: insertion, misinsertion, extension, and coding. J. Biol. Chem. 2010, 285:24457-24465.
    • (2010) J. Biol. Chem. , vol.285 , pp. 24457-24465
    • Cavanaugh, N.A.1    Beard, W.A.2    Wilson, S.H.3
  • 277
    • 42949164023 scopus 로고    scopus 로고
    • Structures of DNA polymerase beta with active-site mismatches suggest a transient abasic site intermediate during misincorporation
    • Batra V.K., Beard W.A., Shock D.D., Pedersen L.C., Wilson S.H. Structures of DNA polymerase beta with active-site mismatches suggest a transient abasic site intermediate during misincorporation. Mol. Cell 2008, 30:315-324.
    • (2008) Mol. Cell , vol.30 , pp. 315-324
    • Batra, V.K.1    Beard, W.A.2    Shock, D.D.3    Pedersen, L.C.4    Wilson, S.H.5
  • 278
    • 70450257567 scopus 로고    scopus 로고
    • DNA polymerase beta substrate specificity: side chain modulation of the "A-rule"
    • Beard W.A., Shock D.D., Batra V.K., Pedersen L.C., Wilson S.H. DNA polymerase beta substrate specificity: side chain modulation of the "A-rule" J. Biol. Chem. 2009, 284:31680-31689.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31680-31689
    • Beard, W.A.1    Shock, D.D.2    Batra, V.K.3    Pedersen, L.C.4    Wilson, S.H.5
  • 280
    • 58149170452 scopus 로고    scopus 로고
    • Loop II of DNA polymerase beta is important for discrimination during substrate binding
    • Lin G.C., Jaeger J., Eckert K.A., Sweasy J.B. Loop II of DNA polymerase beta is important for discrimination during substrate binding. DNA Repair (Amst.) 2009, 8:182-189.
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 182-189
    • Lin, G.C.1    Jaeger, J.2    Eckert, K.A.3    Sweasy, J.B.4
  • 281
    • 63549093737 scopus 로고    scopus 로고
    • Population-specific variation in haplotype composition and heterozygosity at the POLB locus
    • Yamtich J., Speed W.C., Straka E., Kidd J.R., Sweasy J.B., Kidd K.K. Population-specific variation in haplotype composition and heterozygosity at the POLB locus. DNA Repair (Amst.) 2009, 8:579-584.
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 579-584
    • Yamtich, J.1    Speed, W.C.2    Straka, E.3    Kidd, J.R.4    Sweasy, J.B.5    Kidd, K.K.6
  • 282
    • 0028059099 scopus 로고
    • Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting
    • Gu H., Marth J.D., Orban P.C., Mossmann H., Rajewsky K. Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting. Science 1994, 265:103-106.
    • (1994) Science , vol.265 , pp. 103-106
    • Gu, H.1    Marth, J.D.2    Orban, P.C.3    Mossmann, H.4    Rajewsky, K.5
  • 283
    • 0034654379 scopus 로고    scopus 로고
    • Neonatal lethality with abnormal neurogenesis in mice deficient in DNA polymerase beta
    • Sugo N., Aratani Y., Nagashima Y., Kubota Y., Koyama H. Neonatal lethality with abnormal neurogenesis in mice deficient in DNA polymerase beta. EMBO J. 2000, 19:1397-1404.
    • (2000) EMBO J. , vol.19 , pp. 1397-1404
    • Sugo, N.1    Aratani, Y.2    Nagashima, Y.3    Kubota, Y.4    Koyama, H.5
  • 284
    • 0141731310 scopus 로고    scopus 로고
    • Base excision repair deficiency caused by polymerase beta haploinsufficiency: accelerated DNA damage and increased mutational response to carcinogens
    • Cabelof D.C., Guo Z., Raffoul J.J., Sobol R.W., Wilson S.H., Richardson A., Heydari A.R. Base excision repair deficiency caused by polymerase beta haploinsufficiency: accelerated DNA damage and increased mutational response to carcinogens. Cancer Res. 2003, 63:5799-5807.
    • (2003) Cancer Res. , vol.63 , pp. 5799-5807
    • Cabelof, D.C.1    Guo, Z.2    Raffoul, J.J.3    Sobol, R.W.4    Wilson, S.H.5    Richardson, A.6    Heydari, A.R.7
  • 285
    • 67249087934 scopus 로고    scopus 로고
    • Human DNA polymerase beta polymorphism, Arg137Gln, impairs its polymerase activity and interaction with PCNA and the cellular base excision repair capacity
    • Guo Z., Zheng L., Dai H., Zhou M., Xu H., Shen B. Human DNA polymerase beta polymorphism, Arg137Gln, impairs its polymerase activity and interaction with PCNA and the cellular base excision repair capacity. Nucleic Acids Res. 2009, 37:3431-3441.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3431-3441
    • Guo, Z.1    Zheng, L.2    Dai, H.3    Zhou, M.4    Xu, H.5    Shen, B.6
  • 287
    • 13944279514 scopus 로고    scopus 로고
    • Is there a link between DNA polymerase beta and cancer?
    • Starcevic D., Dalal S., Sweasy J.B. Is there a link between DNA polymerase beta and cancer?. Cell Cycle 2004, 3:998-1001.
    • (2004) Cell Cycle , vol.3 , pp. 998-1001
    • Starcevic, D.1    Dalal, S.2    Sweasy, J.B.3
  • 289
    • 28544444617 scopus 로고    scopus 로고
    • Prostate-cancer-associated I260M variant of DNA polymerase beta is a sequence-specific mutator
    • Dalal S., Hile S., Eckert K.A., Sun K.W., Starcevic D., Sweasy J.B. Prostate-cancer-associated I260M variant of DNA polymerase beta is a sequence-specific mutator. Biochemistry 2005, 44:15664-15673.
    • (2005) Biochemistry , vol.44 , pp. 15664-15673
    • Dalal, S.1    Hile, S.2    Eckert, K.A.3    Sun, K.W.4    Starcevic, D.5    Sweasy, J.B.6
  • 290
    • 34547195827 scopus 로고    scopus 로고
    • The E295K DNA polymerase beta gastric cancer-associated variant interferes with base excision repair and induces cellular transformation
    • Lang T., Dalal S., Chikova A., DiMaio D., Sweasy J.B. The E295K DNA polymerase beta gastric cancer-associated variant interferes with base excision repair and induces cellular transformation. Mol. Cell Biol. 2007, 27:5587-5596.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 5587-5596
    • Lang, T.1    Dalal, S.2    Chikova, A.3    DiMaio, D.4    Sweasy, J.B.5
  • 291
    • 39149130715 scopus 로고    scopus 로고
    • The Leu22Pro tumor-associated variant of DNA polymerase beta is dRP lyase deficient
    • Dalal S., Chikova A., Jaeger J., Sweasy J.B. The Leu22Pro tumor-associated variant of DNA polymerase beta is dRP lyase deficient. Nucleic Acids Res. 2008, 36:411-422.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 411-422
    • Dalal, S.1    Chikova, A.2    Jaeger, J.3    Sweasy, J.B.4
  • 292
    • 26444605433 scopus 로고    scopus 로고
    • Expression of DNA polymerase {beta} cancer-associated variants in mouse cells results in cellular transformation
    • Sweasy J.B., Lang T., Starcevic D., Sun K.W., Lai C.C., Dimaio D., Dalal S. Expression of DNA polymerase {beta} cancer-associated variants in mouse cells results in cellular transformation. Proc. Natl. Acad. Sci. USA 2005, 102:14350-14355.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14350-14355
    • Sweasy, J.B.1    Lang, T.2    Starcevic, D.3    Sun, K.W.4    Lai, C.C.5    Dimaio, D.6    Dalal, S.7
  • 293
    • 0032987099 scopus 로고    scopus 로고
    • DNA polymerase beta expression differences in selected human tumors and cell lines
    • Srivastava D.K., Husain I., Arteaga C.L., Wilson S.H. DNA polymerase beta expression differences in selected human tumors and cell lines. Carcinogenesis 1999, 20:1049-1054.
    • (1999) Carcinogenesis , vol.20 , pp. 1049-1054
    • Srivastava, D.K.1    Husain, I.2    Arteaga, C.L.3    Wilson, S.H.4
  • 295
    • 4844225948 scopus 로고    scopus 로고
    • DNA polymerase beta overexpression stimulates the Rad51-dependent homologous recombination in mammalian cells
    • Canitrot Y., Capp J.P., Puget N., Bieth A., Lopez B., Hoffmann J.S., Cazaux C. DNA polymerase beta overexpression stimulates the Rad51-dependent homologous recombination in mammalian cells. Nucleic Acids Res. 2004, 32:5104-5112.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5104-5112
    • Canitrot, Y.1    Capp, J.P.2    Puget, N.3    Bieth, A.4    Lopez, B.5    Hoffmann, J.S.6    Cazaux, C.7
  • 298
    • 33845614891 scopus 로고    scopus 로고
    • ATM mediates oxidative stress-induced dephosphorylation of DNA ligase IIIalpha
    • 5721-5279
    • Dong Z., Tomkinson A.E. ATM mediates oxidative stress-induced dephosphorylation of DNA ligase IIIalpha. Nucleic Acids Res. 2006, 34. 5721-5279.
    • (2006) Nucleic Acids Res. , vol.34
    • Dong, Z.1    Tomkinson, A.E.2
  • 300
    • 33646589977 scopus 로고    scopus 로고
    • Early embryonic lethality due to targeted inactivation of DNA ligase III
    • Puebla-Osorio N., Lacey D.B., Alt F.W., Zhu C. Early embryonic lethality due to targeted inactivation of DNA ligase III. Mol. Cell Biol. 2006, 26:3935-3941.
    • (2006) Mol. Cell Biol. , vol.26 , pp. 3935-3941
    • Puebla-Osorio, N.1    Lacey, D.B.2    Alt, F.W.3    Zhu, C.4
  • 302
    • 0041378046 scopus 로고    scopus 로고
    • XRCC1 and DNA strand break repair
    • Caldecott K.W. XRCC1 and DNA strand break repair. DNA Repair (Amst.) 2003, 2:955-969.
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 955-969
    • Caldecott, K.W.1
  • 304
    • 80053212145 scopus 로고    scopus 로고
    • Human Mre11/Human Rad50/Nbs1 and DNA ligase III{alpha}/XRCC1 protein complexes act together in an alternative nonhomologous end joining pathway
    • Della-Maria J., Zhou Y., Tsai M.S., Kuhnlein J., Carney J.P., Paull T.T., Tomkinson A.E. Human Mre11/Human Rad50/Nbs1 and DNA ligase III{alpha}/XRCC1 protein complexes act together in an alternative nonhomologous end joining pathway. J. Biol. Chem. 2011, 286:33845-33853.
    • (2011) J. Biol. Chem. , vol.286 , pp. 33845-33853
    • Della-Maria, J.1    Zhou, Y.2    Tsai, M.S.3    Kuhnlein, J.4    Carney, J.P.5    Paull, T.T.6    Tomkinson, A.E.7
  • 305
    • 68849105162 scopus 로고    scopus 로고
    • DNA 3'-phosphatase activity is critical for rapid global rates of single-strand break repair following oxidative stress
    • Breslin C., Caldecott K.W. DNA 3'-phosphatase activity is critical for rapid global rates of single-strand break repair following oxidative stress. Mol. Cell Biol. 2009, 29:4653-4662.
    • (2009) Mol. Cell Biol. , vol.29 , pp. 4653-4662
    • Breslin, C.1    Caldecott, K.W.2
  • 308
    • 0035890069 scopus 로고    scopus 로고
    • XRCC1 coordinates the initial and late stages of DNA abasic site repair through 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 through protein-protein interactions. EMBO J. 2001, 20:6530-6539.
    • (2001) EMBO J. , vol.20 , pp. 6530-6539
    • Vidal, A.E.1    Boiteux, S.2    Hickson, I.D.3    Radicella, J.P.4
  • 312
    • 0019956767 scopus 로고
    • A CHO-cell strain having hypersensitivity to mutagens, a defect in DNA strand-break repair, and an extraordinary baseline frequency of sister-chromatid exchange
    • Thompson L.H., Brookman K.W., Dillehay L.E., Carrano A.V., Mazrimas J.A., Mooney C.L., Minkler J.L. A CHO-cell strain having hypersensitivity to mutagens, a defect in DNA strand-break repair, and an extraordinary baseline frequency of sister-chromatid exchange. Mutat. Res. 1982, 95:427-440.
    • (1982) Mutat. Res. , vol.95 , pp. 427-440
    • Thompson, L.H.1    Brookman, K.W.2    Dillehay, L.E.3    Carrano, A.V.4    Mazrimas, J.A.5    Mooney, C.L.6    Minkler, J.L.7
  • 313
    • 0025202114 scopus 로고
    • Molecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange
    • Thompson L.H., Brookman K.W., Jones N.J., Allen S.A., Carrano A.V. Molecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange. Mol. Cell Biol. 1990, 10:6160-6171.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 6160-6171
    • Thompson, L.H.1    Brookman, K.W.2    Jones, N.J.3    Allen, S.A.4    Carrano, A.V.5
  • 315
    • 79955098984 scopus 로고    scopus 로고
    • Polymorphism in the DNA repair enzyme XRCC1: utility of current database and implications for human health risk assessment
    • Ginsberg G., Angle K., Guyton K., Sonawane B. Polymorphism in the DNA repair enzyme XRCC1: utility of current database and implications for human health risk assessment. Mutat. Res. 2011, 727:1-15.
    • (2011) Mutat. Res. , vol.727 , pp. 1-15
    • Ginsberg, G.1    Angle, K.2    Guyton, K.3    Sonawane, B.4
  • 316
    • 84555208304 scopus 로고    scopus 로고
    • Involvement of the XRCC1 Arg399Gln gene polymorphism in the development of cervical carcinoma
    • Roszak A., Lianeri M., Jagodzinski P.P. Involvement of the XRCC1 Arg399Gln gene polymorphism in the development of cervical carcinoma. Int. J. Biol. Markers 2011.
    • (2011) Int. J. Biol. Markers
    • Roszak, A.1    Lianeri, M.2    Jagodzinski, P.P.3
  • 318
    • 69249220333 scopus 로고    scopus 로고
    • XRCC1 genetic polymorphism Arg399Gln and prostate cancer risk: a meta-analysis
    • Geng J., Zhang Q., Zhu C., Wang J., Chen L. XRCC1 genetic polymorphism Arg399Gln and prostate cancer risk: a meta-analysis. Urology 2009, 74:648-653.
    • (2009) Urology , vol.74 , pp. 648-653
    • Geng, J.1    Zhang, Q.2    Zhu, C.3    Wang, J.4    Chen, L.5
  • 322
    • 53249127493 scopus 로고    scopus 로고
    • Association between polymorphisms in DNA base excision repair genes XRCC1, APE1, and ADPRT and differentiated thyroid carcinoma
    • Chiang F.Y., Wu C.W., Hsiao P.J., Kuo W.R., Lee K.W., Lin J.C., Liao Y.C., Juo S.H. Association between polymorphisms in DNA base excision repair genes XRCC1, APE1, and ADPRT and differentiated thyroid carcinoma. Clin. Cancer Res. 2008, 14:5919-5924.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 5919-5924
    • Chiang, F.Y.1    Wu, C.W.2    Hsiao, P.J.3    Kuo, W.R.4    Lee, K.W.5    Lin, J.C.6    Liao, Y.C.7    Juo, S.H.8
  • 323
    • 79551700974 scopus 로고    scopus 로고
    • X-ray repair cross-complementing group 1 (XRCC1) genetic polymorphisms and gastric cancer risk: a HuGE review and meta-analysis
    • Xue H., Ni P., Lin B., Xu H., Huang G. X-ray repair cross-complementing group 1 (XRCC1) genetic polymorphisms and gastric cancer risk: a HuGE review and meta-analysis. Am. J. Epidemiol. 2011, 173:363-375.
    • (2011) Am. J. Epidemiol. , vol.173 , pp. 363-375
    • Xue, H.1    Ni, P.2    Lin, B.3    Xu, H.4    Huang, G.5
  • 327
    • 84872821769 scopus 로고    scopus 로고
    • DNA repair gene polymorphism associated with sensitivity of lung cancer to therapy
    • Li D., Zhou Q., Liu Y., Yang Y., Li Q. DNA repair gene polymorphism associated with sensitivity of lung cancer to therapy. Med. Oncol. 2011.
    • (2011) Med. Oncol.
    • Li, D.1    Zhou, Q.2    Liu, Y.3    Yang, Y.4    Li, Q.5
  • 328
    • 50549086678 scopus 로고    scopus 로고
    • Uracil in DNA: consequences for carcinogenesis and chemotherapy
    • Berger S.H., Pittman D.L., Wyatt M.D. Uracil in DNA: consequences for carcinogenesis and chemotherapy. Biochem. Pharmacol. 2008, 76:697-706.
    • (2008) Biochem. Pharmacol. , vol.76 , pp. 697-706
    • Berger, S.H.1    Pittman, D.L.2    Wyatt, M.D.3
  • 330
    • 78149471618 scopus 로고    scopus 로고
    • Targeting DNA repair proteins for cancer treatment
    • Tell G., Wilson D.M. Targeting DNA repair proteins for cancer treatment. Cell Mol. Life Sci. 2010, 67:3569-3572.
    • (2010) Cell Mol. Life Sci. , vol.67 , pp. 3569-3572
    • Tell, G.1    Wilson, D.M.2
  • 331
    • 0030611436 scopus 로고    scopus 로고
    • Inhibition of O6-alkylguanine DNA-alkyltransferase or poly(ADP-ribose) polymerase increases susceptibility of leukemic cells to apoptosis induced by temozolomide
    • Tentori L., Orlando L., Lacal P.M., Benincasa E., Faraoni I., Bonmassar E., D'Atri S., Graziani G. Inhibition of O6-alkylguanine DNA-alkyltransferase or poly(ADP-ribose) polymerase increases susceptibility of leukemic cells to apoptosis induced by temozolomide. Mol. Pharmacol. 1997, 52:249-258.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 249-258
    • Tentori, L.1    Orlando, L.2    Lacal, P.M.3    Benincasa, E.4    Faraoni, I.5    Bonmassar, E.6    D'Atri, S.7    Graziani, G.8
  • 332
    • 47949120006 scopus 로고    scopus 로고
    • Human methyl purine DNA glycosylase and DNA polymerase beta expression collectively predict sensitivity to temozolomide
    • Trivedi R.N., Wang X.H., Jelezcova E., Goellner E.M., Tang J.B., Sobol R.W. Human methyl purine DNA glycosylase and DNA polymerase beta expression collectively predict sensitivity to temozolomide. Mol. Pharmacol. 2008, 74:505-516.
    • (2008) Mol. Pharmacol. , vol.74 , pp. 505-516
    • Trivedi, R.N.1    Wang, X.H.2    Jelezcova, E.3    Goellner, E.M.4    Tang, J.B.5    Sobol, R.W.6
  • 337
    • 78149471195 scopus 로고    scopus 로고
    • Understanding different functions of mammalian AP endonuclease (APE1) as a promising tool for cancer treatment
    • Tell G., Fantini D., Quadrifoglio F. Understanding different functions of mammalian AP endonuclease (APE1) as a promising tool for cancer treatment. Cell Mol. Life Sci. 2010, 67:3589-3608.
    • (2010) Cell Mol. Life Sci. , vol.67 , pp. 3589-3608
    • Tell, G.1    Fantini, D.2    Quadrifoglio, F.3
  • 338
    • 78149466586 scopus 로고    scopus 로고
    • Small molecule inhibitors of DNA repair nuclease activities of APE1
    • Wilson D.M., Simeonov A. Small molecule inhibitors of DNA repair nuclease activities of APE1. Cell Mol. Life Sci. 2010, 67:3621-3631.
    • (2010) Cell Mol. Life Sci. , vol.67 , pp. 3621-3631
    • Wilson, D.M.1    Simeonov, A.2
  • 339
    • 75149154678 scopus 로고    scopus 로고
    • Potentiation of temozolomide cytotoxicity by inhibition of DNA polymerase beta is accentuated by BRCA2 mutation
    • Stachelek G.C., Dalal S., Donigan K.A., Campisi Hegan D., Sweasy J.B., Glazer P.M. Potentiation of temozolomide cytotoxicity by inhibition of DNA polymerase beta is accentuated by BRCA2 mutation. Cancer Res. 2010, 70:409-417.
    • (2010) Cancer Res. , vol.70 , pp. 409-417
    • Stachelek, G.C.1    Dalal, S.2    Donigan, K.A.3    Campisi Hegan, D.4    Sweasy, J.B.5    Glazer, P.M.6
  • 340
    • 80052168685 scopus 로고    scopus 로고
    • The underlying mechanism for the PARP and BRCA synthetic lethality: clearing up the misunderstandings
    • Helleday T. The underlying mechanism for the PARP and BRCA synthetic lethality: clearing up the misunderstandings. Mol. Oncol. 2011, 5:387-393.
    • (2011) Mol. Oncol. , vol.5 , pp. 387-393
    • Helleday, T.1
  • 341
    • 33847669187 scopus 로고    scopus 로고
    • Hypersensitivity phenotypes associated with genetic and synthetic inhibitor-induced base excision repair deficiency
    • Horton J.K., Wilson S.H. Hypersensitivity phenotypes associated with genetic and synthetic inhibitor-induced base excision repair deficiency. DNA Repair (Amst.) 2007, 6:530-543.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 530-543
    • Horton, J.K.1    Wilson, S.H.2
  • 344
    • 77949551370 scopus 로고    scopus 로고
    • Modifications to the dNTP triphosphate moiety: from mechanistic probes for DNA polymerases to antiviral and anti-cancer drug design
    • McKenna C.E., Kashemirov B.A., Peterson L.W., Goodman M.F. Modifications to the dNTP triphosphate moiety: from mechanistic probes for DNA polymerases to antiviral and anti-cancer drug design. Biochim. Biophys. Acta 2010, 1804:1223-1230.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1223-1230
    • McKenna, C.E.1    Kashemirov, B.A.2    Peterson, L.W.3    Goodman, M.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.