메뉴 건너뛰기




Volumn 6, Issue 6, 2007, Pages 695-711

A unified view of base excision repair: Lesion-dependent protein complexes regulated by post-translational modification

Author keywords

Base excision repair; Endonuclease; Glycosylase; Ligase; PARP; Polymerase; Post translational modification; Protein complexes; XRCC1

Indexed keywords

BASE EXCISION REPAIR PROTEIN; DEOXYRIBONUCLEOPROTEIN; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA GLYCOSYLTRANSFERASE; DNA LIGASE 3; DNA TOPOISOMERASE; EXCISION REPAIR CROSS COMPLEMENTING PROTEIN 1; NEIL2 DNA GLYCOSYLASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 34247599335     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2007.01.009     Document Type: Review
Times cited : (359)

References (192)
  • 1
    • 33847673237 scopus 로고    scopus 로고
    • The intricate structural chemistry of base excision repair machinery: Implications for DNA damage recognition, removal, and repair
    • Hitomi K., Iwai S., and Tainer J.A. The intricate structural chemistry of base excision repair machinery: Implications for DNA damage recognition, removal, and repair. DNA Repair 6 (2007) 410-428
    • (2007) DNA Repair , vol.6 , pp. 410-428
    • Hitomi, K.1    Iwai, S.2    Tainer, J.A.3
  • 2
    • 0034093291 scopus 로고    scopus 로고
    • Passing the baton in base excision repair
    • Wilson S.H., and Kunkel T.A. Passing the baton in base excision repair. Nat. Struct. Biol. 7 (2000) 176-178
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 176-178
    • Wilson, S.H.1    Kunkel, T.A.2
  • 3
    • 0031984807 scopus 로고    scopus 로고
    • Highly sensitive apurinic/apyrimidinic site assay can detect spontaneous and chemically induced depurination under physiological conditions
    • Nakamura J., Walker V.E., Upton P.B., Chiang S.Y., Kow Y.W., and Swenberg J.A. Highly sensitive apurinic/apyrimidinic site assay can detect spontaneous and chemically induced depurination under physiological conditions. Cancer Res. 58 (1998) 222-225
    • (1998) Cancer Res. , vol.58 , pp. 222-225
    • Nakamura, J.1    Walker, V.E.2    Upton, P.B.3    Chiang, S.Y.4    Kow, Y.W.5    Swenberg, J.A.6
  • 4
    • 0033520969 scopus 로고    scopus 로고
    • Quality control by DNA repair
    • Lindahl T., and Wood R.D. Quality control by DNA repair. Science 286 (1999) 1897-1905
    • (1999) Science , vol.286 , pp. 1897-1905
    • Lindahl, T.1    Wood, R.D.2
  • 5
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T. Instability and decay of the primary structure of DNA. Nature 362 (1993) 709-715
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 7
    • 0031773901 scopus 로고    scopus 로고
    • Enzymatic processing of radiation-induced free radical damage in DNA
    • Wallace S.S. Enzymatic processing of radiation-induced free radical damage in DNA. Radiat. Res. 150 (1998) S60-S79
    • (1998) Radiat. Res. , vol.150
    • Wallace, S.S.1
  • 8
    • 0033548096 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen facilitates excision in long-patch base excision repair
    • Gary R., Kim K., Cornelius H.L., Park M.S., and Matsumoto Y. Proliferating cell nuclear antigen facilitates excision in long-patch base excision repair. J. Biol. Chem. 274 (1999) 4354-4363
    • (1999) J. Biol. Chem. , vol.274 , pp. 4354-4363
    • Gary, R.1    Kim, K.2    Cornelius, H.L.3    Park, M.S.4    Matsumoto, Y.5
  • 9
    • 0032539979 scopus 로고    scopus 로고
    • Different DNA polymerases are involved in the short- and long-patch base excision repair in mammalian cells
    • Fortini P., Pascucci B., Parlanti E., Sobol R.W., Wilson S.H., and Dogliotti E. Different DNA polymerases are involved in the short- and long-patch base excision repair in mammalian cells. Biochemistry 37 (1998) 3575-3580
    • (1998) Biochemistry , vol.37 , pp. 3575-3580
    • Fortini, P.1    Pascucci, B.2    Parlanti, E.3    Sobol, R.W.4    Wilson, S.H.5    Dogliotti, E.6
  • 11
    • 0034635403 scopus 로고    scopus 로고
    • FEN1 stimulation of DNA polymerase β mediates an excision step in mammalian long patch base excision repair
    • Prasad R., Dianov G.L., Bohr V.A., and Wilson S.H. FEN1 stimulation of DNA polymerase β mediates an excision step in mammalian long patch base excision repair. J. Biol. Chem. 275 (2000) 4460-4466
    • (2000) J. Biol. Chem. , vol.275 , pp. 4460-4466
    • Prasad, R.1    Dianov, G.L.2    Bohr, V.A.3    Wilson, S.H.4
  • 12
    • 0035980003 scopus 로고    scopus 로고
    • DNA polymerase β-mediated long patch base excision repair: Poly(ADP-ribose)polymerase-1 stimulates strand displacement DNA synthesis
    • Prasad R., Lavrik O.I., Kim S.J., Kedar P., Yang X.P., Vande Berg B.J., and Wilson S.H. DNA polymerase β-mediated long patch base excision repair: Poly(ADP-ribose)polymerase-1 stimulates strand displacement DNA synthesis. J. Biol. Chem. 276 (2001) 32411-32414
    • (2001) J. Biol. Chem. , vol.276 , pp. 32411-32414
    • Prasad, R.1    Lavrik, O.I.2    Kim, S.J.3    Kedar, P.4    Yang, X.P.5    Vande Berg, B.J.6    Wilson, S.H.7
  • 13
    • 15944381621 scopus 로고    scopus 로고
    • Protein-protein interactions and posttranslational modifications in mammalian base excision repair
    • Fan J., and Wilson III D.M. Protein-protein interactions and posttranslational modifications in mammalian base excision repair. Free Radic. Biol. Med. 38 (2005) 1121-1138
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1121-1138
    • Fan, J.1    Wilson III, D.M.2
  • 15
    • 0029957245 scopus 로고    scopus 로고
    • XRCC1 polypeptide interacts with DNA polymerase β 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., and Shall S. XRCC1 polypeptide interacts with DNA polymerase β and possibly poly (ADP-ribose) polymerase, and DNA ligase III is a novel molecular 'nick-sensor' in vitro. Nucl. Acids Res. 24 (1996) 4387-4394
    • (1996) Nucl. Acids Res. , vol.24 , pp. 4387-4394
    • Caldecott, K.W.1    Aoufouchi, S.2    Johnson, P.3    Shall, S.4
  • 16
    • 0031844311 scopus 로고    scopus 로고
    • XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
    • Masson M., Niedergang C., Schreiber V., Muller S., Menissier-de Murcia J., and de Murcia G. XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol. Cell. Biol. 18 (1998) 3563-3571
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3563-3571
    • Masson, M.1    Niedergang, C.2    Schreiber, V.3    Muller, S.4    Menissier-de Murcia, J.5    de Murcia, G.6
  • 18
    • 0042632806 scopus 로고    scopus 로고
    • Physical and functional interaction between DNA ligase IIIalpha and poly(ADP-Ribose) polymerase 1 in DNA single-strand break repair
    • Leppard J.B., Dong Z., Mackey Z.B., and Tomkinson A.E. Physical and functional interaction between DNA ligase IIIalpha and poly(ADP-Ribose) polymerase 1 in DNA single-strand break repair. Mol. Cell. Biol. 23 (2003) 5919-5927
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5919-5927
    • Leppard, J.B.1    Dong, Z.2    Mackey, Z.B.3    Tomkinson, A.E.4
  • 19
    • 0141960298 scopus 로고    scopus 로고
    • Human proliferating cell nuclear antigen, poly(ADP-ribose) polymerase-1, and p21waf1/cip1: a dynamic exchange of partners
    • Frouin I., Maga G., Denegri M., Riva F., Savio M., Spadari S., Prosperi E., and Scovassi A.I. Human proliferating cell nuclear antigen, poly(ADP-ribose) polymerase-1, and p21waf1/cip1: a dynamic exchange of partners. J. Biol. Chem. 278 (2003) 39265-39268
    • (2003) J. Biol. Chem. , vol.278 , pp. 39265-39268
    • Frouin, I.1    Maga, G.2    Denegri, M.3    Riva, F.4    Savio, M.5    Spadari, S.6    Prosperi, E.7    Scovassi, A.I.8
  • 21
    • 1242320312 scopus 로고    scopus 로고
    • The major human AP endonuclease (Ape1) is involved in the nucleotide incision repair pathway
    • Gros L., Ishchenko A.A., Ide H., Elder R.H., and Saparbaev M.K. The major human AP endonuclease (Ape1) is involved in the nucleotide incision repair pathway. Nucl. Acids Res. 32 (2004) 73-81
    • (2004) Nucl. Acids Res. , vol.32 , pp. 73-81
    • Gros, L.1    Ishchenko, A.A.2    Ide, H.3    Elder, R.H.4    Saparbaev, M.K.5
  • 22
  • 25
    • 33845763523 scopus 로고    scopus 로고
    • Increased specificity and efficiency of base excision repair through complex formation
    • Siede W., Doetsch P.W., and Kow Y.W. (Eds), Marcel Dekker Inc., New York
    • Almeida K.H., and Sobol R.W. Increased specificity and efficiency of base excision repair through complex formation. In: Siede W., Doetsch P.W., and Kow Y.W. (Eds). DNA Damage Recognition (2005), Marcel Dekker Inc., New York 33-64
    • (2005) DNA Damage Recognition , pp. 33-64
    • Almeida, K.H.1    Sobol, R.W.2
  • 26
    • 0036184090 scopus 로고    scopus 로고
    • Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription
    • Tini M., Benecke A., Um S.J., Torchia J., Evans R.M., and Chambon P. Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription. Mol. Cell 9 (2002) 265-277
    • (2002) Mol. Cell , vol.9 , pp. 265-277
    • Tini, M.1    Benecke, A.2    Um, S.J.3    Torchia, J.4    Evans, R.M.5    Chambon, P.6
  • 27
    • 0037413689 scopus 로고    scopus 로고
    • Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase
    • Shimizu Y., Iwai S., Hanaoka F., and Sugasawa K. Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase. EMBO J. 22 (2003) 164-173
    • (2003) EMBO J. , vol.22 , pp. 164-173
    • Shimizu, Y.1    Iwai, S.2    Hanaoka, F.3    Sugasawa, K.4
  • 28
    • 20644453965 scopus 로고    scopus 로고
    • XRCC1 interactions with multiple DNA glycosylases: a model for its recruitment to base excision repair
    • Campalans A., Marsin S., Nakabeppu Y., O'Connor R., Boiteux T.S., and Radicella J.P. XRCC1 interactions with multiple DNA glycosylases: a model for its recruitment to base excision repair. DNA Repair (Amst) 4 (2005) 826-835
    • (2005) DNA Repair (Amst) , vol.4 , pp. 826-835
    • Campalans, A.1    Marsin, S.2    Nakabeppu, Y.3    O'Connor, R.4    Boiteux, T.S.5    Radicella, J.P.6
  • 30
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: enzymology and biology
    • Demple B., and Harrison L. Repair of oxidative damage to DNA: enzymology and biology. Annu. Rev. Biochem. 63 (1994) 915-948
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 31
    • 0035869114 scopus 로고    scopus 로고
    • Mechanism of stimulation of the DNA glycosylase activity of hOGG1 by the major human AP endonuclease: bypass of the AP lyase activity step
    • Vidal A.E., Hickson I.D., Boiteux S., and Radicella J.P. Mechanism of stimulation of the DNA glycosylase activity of hOGG1 by the major human AP endonuclease: bypass of the AP lyase activity step. Nucl. Acids Res. 29 (2001) 1285-1292
    • (2001) Nucl. Acids Res. , vol.29 , pp. 1285-1292
    • Vidal, A.E.1    Hickson, I.D.2    Boiteux, S.3    Radicella, J.P.4
  • 32
    • 0035253515 scopus 로고    scopus 로고
    • Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Ape1) in mammalian base excision repair of an A/GO mismatch
    • Yang H., Clendenin W.M., Wong D., Demple B., Slupska M.M., Chiang J.H., and Miller J.H. Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Ape1) in mammalian base excision repair of an A/GO mismatch. Nucl. Acids Res. 29 (2001) 743-752
    • (2001) Nucl. Acids Res. , vol.29 , pp. 743-752
    • Yang, H.1    Clendenin, W.M.2    Wong, D.3    Demple, B.4    Slupska, M.M.5    Chiang, J.H.6    Miller, J.H.7
  • 33
    • 0035863739 scopus 로고    scopus 로고
    • Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: potential coordination of the initial steps in base excision repair
    • Hill J.W., Hazra T.K., Izumi T., and Mitra S. Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: potential coordination of the initial steps in base excision repair. Nucl. Acids Res. 29 (2001) 430-438
    • (2001) Nucl. Acids Res. , vol.29 , pp. 430-438
    • Hill, J.W.1    Hazra, T.K.2    Izumi, T.3    Mitra, S.4
  • 35
    • 0023015325 scopus 로고
    • Mutagenesis by apurinic/apyrimidinic sites
    • Loeb L.A., and Preston B.D. Mutagenesis by apurinic/apyrimidinic sites. Annu. Rev. Genet. 20 (1986) 201-230
    • (1986) Annu. Rev. Genet. , vol.20 , pp. 201-230
    • Loeb, L.A.1    Preston, B.D.2
  • 36
    • 0029829265 scopus 로고    scopus 로고
    • The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice
    • Xanthoudakis S., Smeyne R.J., Wallace J.D., and Curran T. The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice. Proc. Natl. Acad. Sci. 93 (1996) 8919-8923
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 8919-8923
    • Xanthoudakis, S.1    Smeyne, R.J.2    Wallace, J.D.3    Curran, T.4
  • 40
    • 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., and Radicella J.P. XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactions. EMBO J. 20 (2001) 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
  • 41
    • 0037049975 scopus 로고    scopus 로고
    • Alternative nucleotide incision repair pathway for oxidative DNA damage
    • Ischenko A.A., and Saparbaev M.K. Alternative nucleotide incision repair pathway for oxidative DNA damage. Nature 415 (2002) 183-187
    • (2002) Nature , vol.415 , pp. 183-187
    • Ischenko, A.A.1    Saparbaev, M.K.2
  • 42
    • 0035940441 scopus 로고    scopus 로고
    • Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair
    • Dianova I.I., Bohr V.A., and Dianov G.L. Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair. Biochemistry 40 (2001) 12639-12644
    • (2001) Biochemistry , vol.40 , pp. 12639-12644
    • Dianova, I.I.1    Bohr, V.A.2    Dianov, G.L.3
  • 43
    • 0036828697 scopus 로고    scopus 로고
    • AP endonuclease 1 coordinates flap endonuclease 1 and DNA ligase I activity in long patch base excision repair
    • Ranalli T.A., Tom S., and Bambara R.A. AP endonuclease 1 coordinates flap endonuclease 1 and DNA ligase I activity in long patch base excision repair. J. Biol. Chem. 277 (2002) 41715-41724
    • (2002) J. Biol. Chem. , vol.277 , pp. 41715-41724
    • Ranalli, T.A.1    Tom, S.2    Bambara, R.A.3
  • 44
    • 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., and Bond J.P. A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII. DNA Repair (Amst) 1 (2002) 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
  • 45
    • 0032533794 scopus 로고    scopus 로고
    • The presence of two distinct 8-oxoguanine repair enzymes in human cells: their potential complementary roles in preventing mutation
    • Hazra T.K., Izumi T., Maidt L., Floyd R.A., and Mitra S. The presence of two distinct 8-oxoguanine repair enzymes in human cells: their potential complementary roles in preventing mutation. Nucl. Acids Res. 26 (1998) 5116-5122
    • (1998) Nucl. Acids Res. , vol.26 , pp. 5116-5122
    • Hazra, T.K.1    Izumi, T.2    Maidt, L.3    Floyd, R.A.4    Mitra, S.5
  • 46
    • 0037133684 scopus 로고    scopus 로고
    • Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA
    • Hazra T.K., Izumi T., Boldogh I., Imhoff B., Kow Y.W., Jaruga P., Dizdaroglu M., and Mitra S. Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA. Proc. Natl. Acad. Sci. 99 (2002) 3523-3528
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 3523-3528
    • Hazra, T.K.1    Izumi, T.2    Boldogh, I.3    Imhoff, B.4    Kow, Y.W.5    Jaruga, P.6    Dizdaroglu, M.7    Mitra, S.8
  • 47
    • 0036710699 scopus 로고    scopus 로고
    • Polynucleotide kinase: a versatile molecule makes a clean break
    • Caldecott K.W. Polynucleotide kinase: a versatile molecule makes a clean break. Structure 10 (2002) 1151-1152
    • (2002) Structure , vol.10 , pp. 1151-1152
    • Caldecott, K.W.1
  • 49
    • 0037115912 scopus 로고    scopus 로고
    • Enzymology of the repair of free radicals-induced DNA damage
    • Gros L., Saparbaev M.K., and Laval J. Enzymology of the repair of free radicals-induced DNA damage. Oncogene 21 (2002) 8905-8925
    • (2002) Oncogene , vol.21 , pp. 8905-8925
    • Gros, L.1    Saparbaev, M.K.2    Laval, J.3
  • 50
    • 0021111515 scopus 로고
    • Gamma Ray induced deoxyribonucleic acid strand breaks. 3′ Glycolate termini
    • Henner W.D., Rodriguez L.O., Hecht S.M., and Haseltine W.A. Gamma Ray induced deoxyribonucleic acid strand breaks. 3′ Glycolate termini. J. Biol. Chem. 258 (1983) 711-713
    • (1983) J. Biol. Chem. , vol.258 , pp. 711-713
    • Henner, W.D.1    Rodriguez, L.O.2    Hecht, S.M.3    Haseltine, W.A.4
  • 51
    • 0020354447 scopus 로고
    • Sites and structure of gamma radiation-induced DNA strand breaks
    • Henner W.D., Grunberg S.M., and Haseltine W.A. Sites and structure of gamma radiation-induced DNA strand breaks. J. Biol. Chem. 257 (1982) 11750-11754
    • (1982) J. Biol. Chem. , vol.257 , pp. 11750-11754
    • Henner, W.D.1    Grunberg, S.M.2    Haseltine, W.A.3
  • 52
    • 0021045679 scopus 로고
    • Enzyme action at 3′ termini of ionizing radiation-induced DNA strand breaks
    • Henner W.D., Grunberg S.M., and Haseltine W.A. Enzyme action at 3′ termini of ionizing radiation-induced DNA strand breaks. J. Biol. Chem. 258 (1983) 15198-15205
    • (1983) J. Biol. Chem. , vol.258 , pp. 15198-15205
    • Henner, W.D.1    Grunberg, S.M.2    Haseltine, W.A.3
  • 56
    • 0035834150 scopus 로고    scopus 로고
    • The tyrosyl-DNA phosphodiesterase Tdp1 is a member of the phospholipase D superfamily
    • Interthal H., Pouliot J.J., and Champoux J.J. The tyrosyl-DNA phosphodiesterase Tdp1 is a member of the phospholipase D superfamily. Proc. Natl. Acad. Sci. 98 (2001) 12009-12014
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 12009-12014
    • Interthal, H.1    Pouliot, J.J.2    Champoux, J.J.3
  • 57
    • 0037069381 scopus 로고    scopus 로고
    • Repair of topoisomerase I covalent complexes in the absence of the tyrosyl-DNA phosphodiesterase Tdp1
    • Liu C., Pouliot J.J., and Nash H.A. Repair of topoisomerase I covalent complexes in the absence of the tyrosyl-DNA phosphodiesterase Tdp1. Proc. Natl. Acad. Sci. 99 (2002) 14970-14975
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 14970-14975
    • Liu, C.1    Pouliot, J.J.2    Nash, H.A.3
  • 58
    • 0033588161 scopus 로고    scopus 로고
    • Molecular cloning of the human gene, PNKP, encoding a polynucleotide kinase 3'-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage
    • Jilani A., Ramotar D., Slack C., Ong C., Yang X.M., Scherer S.W., and Lasko D.D. Molecular cloning of the human gene, PNKP, encoding a polynucleotide kinase 3'-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage. J. Biol. Chem. 274 (1999) 24176-24186
    • (1999) J. Biol. Chem. , vol.274 , pp. 24176-24186
    • Jilani, A.1    Ramotar, D.2    Slack, C.3    Ong, C.4    Yang, X.M.5    Scherer, S.W.6    Lasko, D.D.7
  • 59
    • 34247562614 scopus 로고    scopus 로고
    • R. Trivedi, R.W. Sobol, Unpublished, 2004.
  • 60
    • 0345061277 scopus 로고    scopus 로고
    • Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions
    • Plo I., Liao Z.Y., Barcelo J.M., Kohlhagen G., Caldecott K.W., Weinfeld M., and Pommier Y. Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions. DNA Repair 2 (2003) 1087-1100
    • (2003) DNA Repair , vol.2 , pp. 1087-1100
    • Plo, I.1    Liao, Z.Y.2    Barcelo, J.M.3    Kohlhagen, G.4    Caldecott, K.W.5    Weinfeld, M.6    Pommier, Y.7
  • 61
    • 0345061277 scopus 로고    scopus 로고
    • Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions
    • Plo I., Liao Z.Y., Barcelo J.M., Kohlhagen G., Caldecott K.W., Weinfeld M., and Pommier Y. Association of XRCC1 and tyrosyl DNA phosphodiesterase (Tdp1) for the repair of topoisomerase I-mediated DNA lesions. DNA Repair (Amst) 2 (2003) 1087-1100
    • (2003) DNA Repair (Amst) , vol.2 , pp. 1087-1100
    • Plo, I.1    Liao, Z.Y.2    Barcelo, J.M.3    Kohlhagen, G.4    Caldecott, K.W.5    Weinfeld, M.6    Pommier, Y.7
  • 62
    • 34247609650 scopus 로고    scopus 로고
    • R. Trivedi, R.W. Sobol, Unpublished, 2007.
  • 64
    • 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., and Carrano A.V. Molecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange. Mol. Cell. Biol. 10 (1990) 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
  • 66
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase β and the XRCC1 protein
    • Kubota Y., Nash R.A., Klungland A., Schar P., Barnes D.E., and Lindahl T. Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase β and the XRCC1 protein. EMBO J. 15 (1996) 6662-6670
    • (1996) EMBO J. , vol.15 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schar, P.4    Barnes, D.E.5    Lindahl, T.6
  • 68
    • 0032858478 scopus 로고    scopus 로고
    • Holding damaged DNA together
    • Rice P.A. Holding damaged DNA together. Nat. Struct. Biol. 6 (1999) 805-806
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 805-806
    • Rice, P.A.1
  • 70
    • 0034985121 scopus 로고    scopus 로고
    • A cellular survival switch: poly(ADP-ribosyl)ation stimulates DNA repair and silences transcription
    • Ziegler M., and Oei S.L. A cellular survival switch: poly(ADP-ribosyl)ation stimulates DNA repair and silences transcription. Bioessays 23 (2001) 543-548
    • (2001) Bioessays , vol.23 , pp. 543-548
    • Ziegler, M.1    Oei, S.L.2
  • 78
    • 0035860767 scopus 로고    scopus 로고
    • Identification of an intrinsic 5′-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair
    • Garcia-Diaz M., Bebenek K., Kunkel T.A., and Blanco L. Identification of an intrinsic 5′-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair. J. Biol. Chem. 276 (2001) 34659-34663
    • (2001) J. Biol. Chem. , vol.276 , pp. 34659-34663
    • Garcia-Diaz, M.1    Bebenek, K.2    Kunkel, T.A.3    Blanco, L.4
  • 79
    • 22244448679 scopus 로고    scopus 로고
    • The role of base excision repair in the sensitivity and resistance to temozolomide mediated cell death
    • Trivedi R.N., Almeida K.H., Fornsaglio J.L., Schamus S., and Sobol R.W. The role of base excision repair in the sensitivity and resistance to temozolomide mediated cell death. Cancer Res. 65 (2005) 6394-6400
    • (2005) Cancer Res. , vol.65 , pp. 6394-6400
    • Trivedi, R.N.1    Almeida, K.H.2    Fornsaglio, J.L.3    Schamus, S.4    Sobol, R.W.5
  • 81
    • 0038690166 scopus 로고    scopus 로고
    • Properties of and substrate determinants for the exonuclease activity of human apurinic endonuclease Ape1
    • Wilson III D.M. Properties of and substrate determinants for the exonuclease activity of human apurinic endonuclease Ape1. J. Mol. Biol. 330 (2003) 1027-1037
    • (2003) J. Mol. Biol. , vol.330 , pp. 1027-1037
    • Wilson III, D.M.1
  • 82
    • 0141815703 scopus 로고    scopus 로고
    • Modulation of the 3′ → 5′-exonuclease activity of human apurinic endonuclease (Ape1) by Its 5′-incised abasic DNA product
    • Wong D., DeMott M.S., and Demple B. Modulation of the 3′ → 5′-exonuclease activity of human apurinic endonuclease (Ape1) by Its 5′-incised abasic DNA product. J. Biol. Chem. 278 (2003) 36242-36249
    • (2003) J. Biol. Chem. , vol.278 , pp. 36242-36249
    • Wong, D.1    DeMott, M.S.2    Demple, B.3
  • 83
    • 33845763523 scopus 로고    scopus 로고
    • Increased specificity and efficiency of base excision repair through complex formation
    • Siede W., Doetsch P.W., and Kow Y.W. (Eds), Marcel Dekker Inc., New York
    • Almeida K.H., and Sobol R.W. Increased specificity and efficiency of base excision repair through complex formation. In: Siede W., Doetsch P.W., and Kow Y.W. (Eds). DNA Damage Recognition (2005), Marcel Dekker Inc., New York
    • (2005) DNA Damage Recognition
    • Almeida, K.H.1    Sobol, R.W.2
  • 86
    • 0142153424 scopus 로고    scopus 로고
    • Physical and functional interaction of the Werner syndrome protein with poly-ADP ribosyl transferase
    • Adelfalk C., Kontou M., Hirsch-Kauffmann M., and Schweiger M. Physical and functional interaction of the Werner syndrome protein with poly-ADP ribosyl transferase. FEBS Lett. 554 (2003) 55-58
    • (2003) FEBS Lett. , vol.554 , pp. 55-58
    • Adelfalk, C.1    Kontou, M.2    Hirsch-Kauffmann, M.3    Schweiger, M.4
  • 87
    • 0242721664 scopus 로고    scopus 로고
    • Central role for the Werner syndrome protein/poly(ADP-ribose) polymerase 1 complex in the poly(ADP-ribosyl)ation pathway after DNA damage
    • von Kobbe C., Harrigan J.A., May A., Opresko P.L., Dawut L., Cheng W.H., and Bohr V.A. Central role for the Werner syndrome protein/poly(ADP-ribose) polymerase 1 complex in the poly(ADP-ribosyl)ation pathway after DNA damage. Mol. Cell. Biol. 23 (2003) 8601-8613
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8601-8613
    • von Kobbe, C.1    Harrigan, J.A.2    May, A.3    Opresko, P.L.4    Dawut, L.5    Cheng, W.H.6    Bohr, V.A.7
  • 88
    • 0038681010 scopus 로고    scopus 로고
    • The Werner syndrome protein stimulates DNA polymerase β strand displacement synthesis via its helicase activity
    • Harrigan J.A., Opresko P.L., von Kobbe C., Kedar P.S., Prasad R., Wilson S.H., and Bohr V.A. The Werner syndrome protein stimulates DNA polymerase β strand displacement synthesis via its helicase activity. J. Biol. Chem. 278 (2003) 22686-22695
    • (2003) J. Biol. Chem. , vol.278 , pp. 22686-22695
    • Harrigan, J.A.1    Opresko, P.L.2    von Kobbe, C.3    Kedar, P.S.4    Prasad, R.5    Wilson, S.H.6    Bohr, V.A.7
  • 91
    • 33845732323 scopus 로고    scopus 로고
    • DNA polymerase β null mouse embryonic fibroblasts harbor a homozygous null mutation in DNA polymerase iota
    • Sobol R.W. DNA polymerase β null mouse embryonic fibroblasts harbor a homozygous null mutation in DNA polymerase iota. DNA Repair (Amst) 6 (2007) 3-7
    • (2007) DNA Repair (Amst) , vol.6 , pp. 3-7
    • Sobol, R.W.1
  • 93
    • 0034659935 scopus 로고    scopus 로고
    • The lyase activity of the DNA repair protein β-polymerase protects from DNA-damage-induced cytotoxicity
    • Sobol R.W., Prasad R., Evenski A., Baker A., Yang X.P., Horton J.K., and Wilson S.H. The lyase activity of the DNA repair protein β-polymerase protects from DNA-damage-induced cytotoxicity. Nature 405 (2000) 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
  • 94
    • 0141731310 scopus 로고    scopus 로고
    • Base excision repair deficiency caused by polymerase β 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., and Heydari A.R. Base excision repair deficiency caused by polymerase β haploinsufficiency: accelerated DNA damage and increased mutational response to carcinogens. Cancer Res. 63 (2003) 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
  • 95
    • 33750619876 scopus 로고    scopus 로고
    • Posttranslational protein modifications: current implications for cancer detection, prevention, and therapeutics
    • Krueger K.E., and Srivastava S. Posttranslational protein modifications: current implications for cancer detection, prevention, and therapeutics. Mol. Cell Proteomics 5 (2006) 1799-1810
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 1799-1810
    • Krueger, K.E.1    Srivastava, S.2
  • 96
    • 20444487725 scopus 로고    scopus 로고
    • Phosphorylation of human oxoguanine DNA glycosylase (alpha-OGG1) modulates its function
    • Hu J., Imam S.Z., Hashiguchi K., de Souza-Pinto N.C., and Bohr V.A. Phosphorylation of human oxoguanine DNA glycosylase (alpha-OGG1) modulates its function. Nucl. Acids Res. 33 (2005) 3271-3282
    • (2005) Nucl. Acids Res. , vol.33 , pp. 3271-3282
    • Hu, J.1    Imam, S.Z.2    Hashiguchi, K.3    de Souza-Pinto, N.C.4    Bohr, V.A.5
  • 97
    • 4344560876 scopus 로고    scopus 로고
    • The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair
    • Lu X., Bocangel D., Nannenga B., Yamaguchi H., Appella E., and Donehower L.A. The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair. Mol. Cell 15 (2004) 621-634
    • (2004) Mol. Cell , vol.15 , pp. 621-634
    • Lu, X.1    Bocangel, D.2    Nannenga, B.3    Yamaguchi, H.4    Appella, E.5    Donehower, L.A.6
  • 99
    • 33845733594 scopus 로고    scopus 로고
    • SUMO-1-dependent allosteric regulation of thymine DNA glycosylase alters subnuclear localization and CBP/p300 recruitment
    • Mohan R.D., Rao A., Gagliardi J., and Tini F.M. SUMO-1-dependent allosteric regulation of thymine DNA glycosylase alters subnuclear localization and CBP/p300 recruitment. Mol. Cell Biol. 27 (2007) 229-243
    • (2007) Mol. Cell Biol. , vol.27 , pp. 229-243
    • Mohan, R.D.1    Rao, A.2    Gagliardi, J.3    Tini, F.M.4
  • 100
    • 17144410054 scopus 로고    scopus 로고
    • Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation
    • Steinacher R., and Schar P. Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation. Curr. Biol. 15 (2005) 616-623
    • (2005) Curr. Biol. , vol.15 , pp. 616-623
    • Steinacher, R.1    Schar, P.2
  • 101
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • Hardeland U., Steinacher R., Jiricny J., and Schar P. Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J. 21 (2002) 1456-1464
    • (2002) EMBO J. , vol.21 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schar, P.4
  • 102
    • 3042674067 scopus 로고    scopus 로고
    • Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity
    • Bhakat K.K., Hazra T.K., and Mitra S. Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity. Nucl. Acids Res. 32 (2004) 3033-3039
    • (2004) Nucl. Acids Res. , vol.32 , pp. 3033-3039
    • Bhakat, K.K.1    Hazra, T.K.2    Mitra, S.3
  • 103
    • 0033611583 scopus 로고    scopus 로고
    • Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1
    • Fritz G., and Kaina B. Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1. Oncogene 18 (1999) 1033-1040
    • (1999) Oncogene , vol.18 , pp. 1033-1040
    • Fritz, G.1    Kaina, B.2
  • 104
    • 0035879047 scopus 로고    scopus 로고
    • Activation of APE/Ref-1 redox activity is mediated by reactive oxygen species and PKC phosphorylation
    • Hsieh M.M., Hegde V., Kelley M.R., and Deutsch W.A. Activation of APE/Ref-1 redox activity is mediated by reactive oxygen species and PKC phosphorylation. Nucl. Acids Res. 29 (2001) 3116-3122
    • (2001) Nucl. Acids Res. , vol.29 , pp. 3116-3122
    • Hsieh, M.M.1    Hegde, V.2    Kelley, M.R.3    Deutsch, W.A.4
  • 105
    • 0037325818 scopus 로고    scopus 로고
    • A quantitative method for measuring protein phosphorylation
    • McKenzie J.A., and Strauss P.R. A quantitative method for measuring protein phosphorylation. Anal. Biochem. 313 (2003) 9-16
    • (2003) Anal. Biochem. , vol.313 , pp. 9-16
    • McKenzie, J.A.1    Strauss, P.R.2
  • 107
    • 0031439356 scopus 로고    scopus 로고
    • The DNA repair activity of human redox/repair protein APE/Ref-1 is inactivated by phosphorylation
    • Yacoub A., Kelley M.R., and Deutsch W.A. The DNA repair activity of human redox/repair protein APE/Ref-1 is inactivated by phosphorylation. Cancer Res. 57 (1997) 5457-5459
    • (1997) Cancer Res. , vol.57 , pp. 5457-5459
    • Yacoub, A.1    Kelley, M.R.2    Deutsch, W.A.3
  • 108
    • 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., and Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 11 (1992) 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
  • 109
    • 0346275195 scopus 로고    scopus 로고
    • Acetylation of human AP-endonuclease 1, a critical enzyme in DNA repair and transcription regulation
    • Bhakat K.K., Yang S.H., and Mitra S. Acetylation of human AP-endonuclease 1, a critical enzyme in DNA repair and transcription regulation. Methods Enzymol. 371 (2003) 292-300
    • (2003) Methods Enzymol. , vol.371 , pp. 292-300
    • Bhakat, K.K.1    Yang, S.H.2    Mitra, S.3
  • 110
    • 0347504848 scopus 로고    scopus 로고
    • Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene
    • Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., and Mitra S. Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene. EMBO J. 22 (2003) 6299-6309
    • (2003) EMBO J. , vol.22 , pp. 6299-6309
    • Bhakat, K.K.1    Izumi, T.2    Yang, S.H.3    Hazra, T.K.4    Mitra, S.5
  • 111
    • 0037326709 scopus 로고    scopus 로고
    • Protein-protein interactions during mammalian DNA single-strand break repair
    • Caldecott K.W. Protein-protein interactions during mammalian DNA single-strand break repair. Biochem. Soc. Trans. 31 (2003) 247-251
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 247-251
    • Caldecott, K.W.1
  • 112
    • 24044460404 scopus 로고    scopus 로고
    • Specificity of protein interactions mediated by BRCT domains of the XRCC1 DNA repair protein
    • Beernink P.T., Hwang M., Ramirez M., Murphy M.B., Doyle S.A., and Thelen M.P. Specificity of protein interactions mediated by BRCT domains of the XRCC1 DNA repair protein. J. Biol. Chem. 280 (2005) 30206-30213
    • (2005) J. Biol. Chem. , vol.280 , pp. 30206-30213
    • Beernink, P.T.1    Hwang, M.2    Ramirez, M.3    Murphy, M.B.4    Doyle, S.A.5    Thelen, M.P.6
  • 113
    • 0037151051 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1
    • Schreiber V., Ame J.C., Dolle P., Schultz I., Rinaldi B., Fraulob V., Menissier-de Murcia J., and de Murcia G. Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. J. Biol. Chem. 277 (2002) 23028-23036
    • (2002) J. Biol. Chem. , vol.277 , pp. 23028-23036
    • Schreiber, V.1    Ame, J.C.2    Dolle, P.3    Schultz, I.4    Rinaldi, B.5    Fraulob, V.6    Menissier-de Murcia, J.7    de Murcia, G.8
  • 114
    • 0142009654 scopus 로고    scopus 로고
    • A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage
    • El-Khamisy S.F., Masutani M., Suzuki H., and Caldecott K.W. A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage. Nucl. Acids Res. 31 (2003) 5526-5533
    • (2003) Nucl. Acids Res. , vol.31 , pp. 5526-5533
    • El-Khamisy, S.F.1    Masutani, M.2    Suzuki, H.3    Caldecott, K.W.4
  • 117
    • 14244249406 scopus 로고    scopus 로고
    • Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates
    • Gocke C.B., Yu H., and Kang J. Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates. J. Biol. Chem. 280 (2005) 5004-5012
    • (2005) J. Biol. Chem. , vol.280 , pp. 5004-5012
    • Gocke, C.B.1    Yu, H.2    Kang, J.3
  • 118
    • 33749260519 scopus 로고    scopus 로고
    • Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?
    • Hassa P.O., Haenni S.S., Elser M., and Hottiger M.O. Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?. Microbiol. Mol. Biol. Rev. 70 (2006) 789-829
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 789-829
    • Hassa, P.O.1    Haenni, S.S.2    Elser, M.3    Hottiger, M.O.4
  • 120
    • 13544261768 scopus 로고    scopus 로고
    • DNA polymerase beta and flap endonuclease 1 enzymatic specificities sustain DNA synthesis for long patch base excision repair
    • Liu Y., Beard W.A., Shock D.D., Prasad R., Hou E.W., and Wilson S.H. DNA polymerase beta and flap endonuclease 1 enzymatic specificities sustain DNA synthesis for long patch base excision repair. J. Biol. Chem. 280 (2005) 3665-3674
    • (2005) J. Biol. Chem. , vol.280 , pp. 3665-3674
    • Liu, Y.1    Beard, W.A.2    Shock, D.D.3    Prasad, R.4    Hou, E.W.5    Wilson, S.H.6
  • 121
    • 0042804874 scopus 로고    scopus 로고
    • Phosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation
    • Henneke G., Koundrioukoff S., and Hubscher U. Phosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation. Oncogene 22 (2003) 4301-4313
    • (2003) Oncogene , vol.22 , pp. 4301-4313
    • Henneke, G.1    Koundrioukoff, S.2    Hubscher, U.3
  • 122
    • 0037453277 scopus 로고    scopus 로고
    • The acetylatable lysines of human Fen1 are important for endo- and exonuclease activities
    • Friedrich-Heineken E., Henneke G., Ferrari E., and Hubscher U. The acetylatable lysines of human Fen1 are important for endo- and exonuclease activities. J. Mol. Biol. 328 (2003) 73-84
    • (2003) J. Mol. Biol. , vol.328 , pp. 73-84
    • Friedrich-Heineken, E.1    Henneke, G.2    Ferrari, E.3    Hubscher, U.4
  • 123
    • 0034969453 scopus 로고    scopus 로고
    • Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300
    • Hasan S., Stucki M., Hassa P.O., Imhof R., Gehrig P., Hunziker P., Hubscher U., and Hottiger M.O. Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300. Mol. Cell 7 (2001) 1221-1231
    • (2001) Mol. Cell , vol.7 , pp. 1221-1231
    • Hasan, S.1    Stucki, M.2    Hassa, P.O.3    Imhof, R.4    Gehrig, P.5    Hunziker, P.6    Hubscher, U.7    Hottiger, M.O.8
  • 125
    • 0037185024 scopus 로고    scopus 로고
    • DNA damage-induced translocation of the Werner helicase is regulated by acetylation
    • Blander G., Zalle N., Daniely Y., Taplick J., Gray M.D., and Oren M. DNA damage-induced translocation of the Werner helicase is regulated by acetylation. J. Biol. Chem. 277 (2002) 50934-50940
    • (2002) J. Biol. Chem. , vol.277 , pp. 50934-50940
    • Blander, G.1    Zalle, N.2    Daniely, Y.3    Taplick, J.4    Gray, M.D.5    Oren, M.6
  • 126
    • 34247581131 scopus 로고    scopus 로고
    • Impaired DNA repair via the base-excision repair pathway after focal ischemic brain injury: a protein phosphorylation-dependent mechanism reversed by hypothermic neuroprotection
    • Luo Y., Ji X., Ling F., Li W., Zhang F., Cao G., and Chen J. Impaired DNA repair via the base-excision repair pathway after focal ischemic brain injury: a protein phosphorylation-dependent mechanism reversed by hypothermic neuroprotection. Front Biosci. 12 (2007) 1852-1862
    • (2007) Front Biosci. , vol.12 , pp. 1852-1862
    • Luo, Y.1    Ji, X.2    Ling, F.3    Li, W.4    Zhang, F.5    Cao, G.6    Chen, J.7
  • 127
    • 0037188826 scopus 로고    scopus 로고
    • Hormonal regulation of DNA polymerase beta activity and expression in rat adrenal glands and testes
    • Kotake M., Nakai A., Nagasaka A., Itoh M., Hidaka H., and Yoshida S. Hormonal regulation of DNA polymerase beta activity and expression in rat adrenal glands and testes. Mol. Cell Endocrinol. 192 (2002) 127-132
    • (2002) Mol. Cell Endocrinol. , vol.192 , pp. 127-132
    • Kotake, M.1    Nakai, A.2    Nagasaka, A.3    Itoh, M.4    Hidaka, H.5    Yoshida, S.6
  • 129
    • 33846025995 scopus 로고    scopus 로고
    • Methylation of DNA polymerase beta by protein arginine methyltransferase 1 regulates its binding to proliferating cell nuclear antigen
    • El-Andaloussi N., Valovka T., Toueille M., Hassa P.O., Gehrig P., Covic M., Hubscher U., and Hottiger M.O. Methylation of DNA polymerase beta by protein arginine methyltransferase 1 regulates its binding to proliferating cell nuclear antigen. FASEB J. 21 (2007) 26-34
    • (2007) FASEB J. , vol.21 , pp. 26-34
    • El-Andaloussi, N.1    Valovka, T.2    Toueille, M.3    Hassa, P.O.4    Gehrig, P.5    Covic, M.6    Hubscher, U.7    Hottiger, M.O.8
  • 130
    • 33646871568 scopus 로고    scopus 로고
    • DNA ligase I is an in vivo substrate of DNA-dependent protein kinase and is activated by phosphorylation in response to DNA double-strand breaks
    • Bhat K.R., Benton B.J., and Ray R. DNA ligase I is an in vivo substrate of DNA-dependent protein kinase and is activated by phosphorylation in response to DNA double-strand breaks. Biochemistry 45 (2006) 6522-6528
    • (2006) Biochemistry , vol.45 , pp. 6522-6528
    • Bhat, K.R.1    Benton, B.J.2    Ray, R.3
  • 131
    • 33845614891 scopus 로고    scopus 로고
    • ATM mediates oxidative stress-induced dephosphorylation of DNA ligase IIIalpha
    • Dong Z., and Tomkinson A.E. ATM mediates oxidative stress-induced dephosphorylation of DNA ligase IIIalpha. Nucl. Acids Res. 34 (2006) 5279-5721
    • (2006) Nucl. Acids Res. , vol.34 , pp. 5279-5721
    • Dong, Z.1    Tomkinson, A.E.2
  • 132
    • 32644454570 scopus 로고    scopus 로고
    • Sumoylation of PCNA: wrestling with recombination at stalled replication forks
    • Watts F.Z. Sumoylation of PCNA: wrestling with recombination at stalled replication forks. DNA Repair (Amst) 5 (2006) 399-403
    • (2006) DNA Repair (Amst) , vol.5 , pp. 399-403
    • Watts, F.Z.1
  • 133
    • 14544287434 scopus 로고    scopus 로고
    • Replication of damaged DNA by translesion synthesis in human cells
    • Lehmann A.R. Replication of damaged DNA by translesion synthesis in human cells. FEBS Lett. 579 (2005) 873-876
    • (2005) FEBS Lett. , vol.579 , pp. 873-876
    • Lehmann, A.R.1
  • 134
    • 33746775293 scopus 로고    scopus 로고
    • Translesion synthesis in mammalian cells
    • Lehmann A.R. Translesion synthesis in mammalian cells. Exp. Cell Res 312 (2006) 2673-2676
    • (2006) Exp. Cell Res , vol.312 , pp. 2673-2676
    • Lehmann, A.R.1
  • 135
    • 33644634986 scopus 로고    scopus 로고
    • Structure and mechanism of DNA polymerase beta
    • Beard W.A., and Wilson S.H. Structure and mechanism of DNA polymerase beta. Chem. Rev. 106 (2006) 361-382
    • (2006) Chem. Rev. , vol.106 , pp. 361-382
    • Beard, W.A.1    Wilson, S.H.2
  • 136
    • 0034659815 scopus 로고    scopus 로고
    • Proteomics to study genes and genomes
    • Pandey A., and Mann M. Proteomics to study genes and genomes. Nature 405 (2000) 837-846
    • (2000) Nature , vol.405 , pp. 837-846
    • Pandey, A.1    Mann, M.2
  • 139
    • 0030219915 scopus 로고    scopus 로고
    • Specific association of cyclin-like uracil-DNA glycosylase with the proliferating cell nuclear antigen
    • Muller-Weeks S.J., and Caradonna S. Specific association of cyclin-like uracil-DNA glycosylase with the proliferating cell nuclear antigen. Exp. Cell Res. 226 (1996) 346-355
    • (1996) Exp. Cell Res. , vol.226 , pp. 346-355
    • Muller-Weeks, S.J.1    Caradonna, S.2
  • 140
    • 23844471513 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases
    • Schrofelbauer B., Yu Q., Zeitlin S.G., and Landau N.R. Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases. J. Virol. 79 (2005) 10978-10987
    • (2005) J. Virol. , vol.79 , pp. 10978-10987
    • Schrofelbauer, B.1    Yu, Q.2    Zeitlin, S.G.3    Landau, N.R.4
  • 141
    • 0032951710 scopus 로고    scopus 로고
    • Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1
    • Waters T.R., Gallinari P., Jiricny J., and Swann P.F. Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1. J. Biol. Chem. 274 (1999) 67-74
    • (1999) J. Biol. Chem. , vol.274 , pp. 67-74
    • Waters, T.R.1    Gallinari, P.2    Jiricny, J.3    Swann, P.F.4
  • 143
    • 0242363151 scopus 로고    scopus 로고
    • Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin
    • Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I., Shirakawa M., Kawasuji M., and Nakao M. Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin. Proc. Natl. Acad. Sci. 100 (2003) 12859-12864
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 12859-12864
    • Watanabe, S.1    Ichimura, T.2    Fujita, N.3    Tsuruzoe, S.4    Ohki, I.5    Shirakawa, M.6    Kawasuji, M.7    Nakao, M.8
  • 144
    • 0036837549 scopus 로고    scopus 로고
    • Functional crosstalk between hOgg1 and the helicase domain of Cockayne syndrome group B protein
    • Tuo J., Chen C., Zeng X., Christiansen M., and Bohr V.A. Functional crosstalk between hOgg1 and the helicase domain of Cockayne syndrome group B protein. DNA Repair 1 (2002) 913-927
    • (2002) DNA Repair , vol.1 , pp. 913-927
    • Tuo, J.1    Chen, C.2    Zeng, X.3    Christiansen, M.4    Bohr, V.A.5
  • 145
    • 0035937102 scopus 로고    scopus 로고
    • Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair
    • Parker A., Gu Y., Mahoney W., Lee S.H., Singh K.K., and Lu A.L. Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair. J. Biol. Chem. 276 (2001) 5547-5555
    • (2001) J. Biol. Chem. , vol.276 , pp. 5547-5555
    • Parker, A.1    Gu, Y.2    Mahoney, W.3    Lee, S.H.4    Singh, K.K.5    Lu, A.L.6
  • 146
    • 0033557139 scopus 로고    scopus 로고
    • Nucleotide excision repair 3′ endonuclease XPG stimulates the activity of base excision repairenzyme thymine glycol DNA glycosylase
    • Bessho T. Nucleotide excision repair 3′ endonuclease XPG stimulates the activity of base excision repairenzyme thymine glycol DNA glycosylase. Nucl. Acids Res. 27 (1999) 979-983
    • (1999) Nucl. Acids Res. , vol.27 , pp. 979-983
    • Bessho, T.1
  • 148
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway
    • Bennett R.A.O., Wilson III D.M., Wong D., and Demple B. Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway. Proc. Natl. Acad. Sci. 94 (1997) 7166-7169
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 7166-7169
    • Bennett, R.A.O.1    Wilson III, D.M.2    Wong, D.3    Demple, B.4
  • 149
    • 0032515067 scopus 로고    scopus 로고
    • Rapid dissociation of human apurinic endonuclease (Ape1) from incised DNA induced by magnesium
    • Masuda Y., Bennett R.A., and Demple B. Rapid dissociation of human apurinic endonuclease (Ape1) from incised DNA induced by magnesium. J. Biol. Chem. 273 (1998) 30360-30365
    • (1998) J. Biol. Chem. , vol.273 , pp. 30360-30365
    • Masuda, Y.1    Bennett, R.A.2    Demple, B.3
  • 150
    • 0033570048 scopus 로고    scopus 로고
    • Ref-1 regulates the transactivation and pro-apoptotic functions of p53 in vivo
    • Gaiddon C., Moorthy N.C., and Prives C. Ref-1 regulates the transactivation and pro-apoptotic functions of p53 in vivo. EMBO J. 18 (1999) 5609-5621
    • (1999) EMBO J. , vol.18 , pp. 5609-5621
    • Gaiddon, C.1    Moorthy, N.C.2    Prives, C.3
  • 151
    • 0030018848 scopus 로고    scopus 로고
    • Specific interaction of DNA polymerase β and DNA ligase I in a multiprotein base excision repair complex from bovine testis
    • Prasad R., Singhal R.K., Srivastava D.K., Molina J.T., Tomkinson A.E., and Wilson S.H. Specific interaction of DNA polymerase β and DNA ligase I in a multiprotein base excision repair complex from bovine testis. J. Biol. Chem. 271 (1996) 16000-16007
    • (1996) J. Biol. Chem. , vol.271 , pp. 16000-16007
    • Prasad, R.1    Singhal, R.K.2    Srivastava, D.K.3    Molina, J.T.4    Tomkinson, A.E.5    Wilson, S.H.6
  • 152
    • 0035865399 scopus 로고    scopus 로고
    • A role for p53 in base excision repair
    • Zhou J., Ahn J., Wilson S.H., and Prives C. A role for p53 in base excision repair. EMBO J. 20 (2001) 914-923
    • (2001) EMBO J. , vol.20 , pp. 914-923
    • Zhou, J.1    Ahn, J.2    Wilson, S.H.3    Prives, C.4
  • 153
    • 31544482730 scopus 로고    scopus 로고
    • Telomere repeat binding factor 2 interacts with base excision repair proteins and stimulates DNA synthesis by DNA polymerase beta
    • Muftuoglu M., Wong H.K., Imam S.Z., Wilson III D.M., Bohr V.A., and Opresko P.L. Telomere repeat binding factor 2 interacts with base excision repair proteins and stimulates DNA synthesis by DNA polymerase beta. Cancer Res. 66 (2006) 113-124
    • (2006) Cancer Res. , vol.66 , pp. 113-124
    • Muftuoglu, M.1    Wong, H.K.2    Imam, S.Z.3    Wilson III, D.M.4    Bohr, V.A.5    Opresko, P.L.6
  • 154
    • 0037163025 scopus 로고    scopus 로고
    • Direct interaction between mammalian DNA polymerase β and proliferating cell nuclear antigen
    • Kedar P.S., Kim S.J., Robertson A., Hou E., Prasad R., Horton J.K., and Wilson S.H. Direct interaction between mammalian DNA polymerase β and proliferating cell nuclear antigen. J. Biol. Chem. 277 (2002) 31115-31123
    • (2002) J. Biol. Chem. , vol.277 , pp. 31115-31123
    • Kedar, P.S.1    Kim, S.J.2    Robertson, A.3    Hou, E.4    Prasad, R.5    Horton, J.K.6    Wilson, S.H.7
  • 155
    • 2442431498 scopus 로고    scopus 로고
    • The post-translational modifications of proliferating cell nuclear antigen: acetylation, not phosphorylation, plays an important role in the regulation of its function
    • Naryzhny S.N., and Lee H. The post-translational modifications of proliferating cell nuclear antigen: acetylation, not phosphorylation, plays an important role in the regulation of its function. J. Biol. Chem. 279 (2004) 20194-20199
    • (2004) J. Biol. Chem. , vol.279 , pp. 20194-20199
    • Naryzhny, S.N.1    Lee, H.2
  • 156
    • 0035816708 scopus 로고    scopus 로고
    • Photoaffinity labeling of mouse fibroblast enzymes by a base excision repair intermediate: Evidence for the role of poly(ADP-ribose) polymerase-1 in DNA repair
    • Lavrik O.I., Prasad R., Sobol R.W., Horton J.K., Ackerman E.J., and Wilson S.H. Photoaffinity labeling of mouse fibroblast enzymes by a base excision repair intermediate: Evidence for the role of poly(ADP-ribose) polymerase-1 in DNA repair. J. Biol. Chem. 276 (2001) 25541-25548
    • (2001) J. Biol. Chem. , vol.276 , pp. 25541-25548
    • Lavrik, O.I.1    Prasad, R.2    Sobol, R.W.3    Horton, J.K.4    Ackerman, E.J.5    Wilson, S.H.6
  • 157
    • 0342350255 scopus 로고    scopus 로고
    • Interaction between PCNA and DNA ligase I is critical for joining of Okazaki fragments and long-patch base-excision repair
    • Levin D.S., McKenna A.E., Motycka T.A., Matsumoto Y., and Tomkinson A.E. Interaction between PCNA and DNA ligase I is critical for joining of Okazaki fragments and long-patch base-excision repair. Curr. Biol. 10 (2000) 919-922
    • (2000) Curr. Biol. , vol.10 , pp. 919-922
    • Levin, D.S.1    McKenna, A.E.2    Motycka, T.A.3    Matsumoto, Y.4    Tomkinson, A.E.5
  • 158
    • 0035816586 scopus 로고    scopus 로고
    • DNA ligase I and proliferating cell nuclear antigen form a functional complex
    • Tom S., Henricksen L.A., Park M.S., and Bambara R.A. DNA ligase I and proliferating cell nuclear antigen form a functional complex. J. Biol. Chem. 276 (2001) 24817-24825
    • (2001) J. Biol. Chem. , vol.276 , pp. 24817-24825
    • Tom, S.1    Henricksen, L.A.2    Park, M.S.3    Bambara, R.A.4
  • 159
    • 0034616199 scopus 로고    scopus 로고
    • Mechanism whereby proliferating cell nuclear antigen stimulates flap endonuclease 1
    • Tom S., Henricksen L.A., and Bambara R.A. Mechanism whereby proliferating cell nuclear antigen stimulates flap endonuclease 1. J. Biol. Chem. 275 (2000) 10498-10505
    • (2000) J. Biol. Chem. , vol.275 , pp. 10498-10505
    • Tom, S.1    Henricksen, L.A.2    Bambara, R.A.3
  • 160
    • 0029885134 scopus 로고    scopus 로고
    • Processing of branched DNA intermediates by a complex of human FEN-1 and PCNA
    • Wu X., Li J., Li X., Hsieh C.L., Burgers P.M., and Lieber M.R. Processing of branched DNA intermediates by a complex of human FEN-1 and PCNA. Nucl. Acids Res. 24 (1996) 2036-2043
    • (1996) Nucl. Acids Res. , vol.24 , pp. 2036-2043
    • Wu, X.1    Li, J.2    Li, X.3    Hsieh, C.L.4    Burgers, P.M.5    Lieber, M.R.6
  • 163
    • 0742288051 scopus 로고    scopus 로고
    • WRN helicase and FEN-1 form a complex upon replication arrest and together process branchmigrating DNA structures associated with the replication fork
    • Sharma S., Otterlei M., Sommers J.A., Driscoll H.C., Dianov G.L., Kao H.I., Bambara R.A., and Brosh Jr. R.M. WRN helicase and FEN-1 form a complex upon replication arrest and together process branchmigrating DNA structures associated with the replication fork. Mol. Biol. Cell. 15 (2004) 734-750
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 734-750
    • Sharma, S.1    Otterlei, M.2    Sommers, J.A.3    Driscoll, H.C.4    Dianov, G.L.5    Kao, H.I.6    Bambara, R.A.7    Brosh Jr., R.M.8
  • 164
    • 0030767281 scopus 로고    scopus 로고
    • The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21
    • Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., and Park M.S. The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21. J. Biol. Chem. 272 (1997) 24522-24529
    • (1997) J. Biol. Chem. , vol.272 , pp. 24522-24529
    • Gary, R.1    Ludwig, D.L.2    Cornelius, H.L.3    MacInnes, M.A.4    Park, M.S.5
  • 165
    • 0035869074 scopus 로고    scopus 로고
    • Transcription coactivator p300 binds PCNA and may have a role in DNA repair synthesis
    • Hasan S., Hassa P.O., Imhof R., and Hottiger M.O. Transcription coactivator p300 binds PCNA and may have a role in DNA repair synthesis. Nature 410 (2001) 387-391
    • (2001) Nature , vol.410 , pp. 387-391
    • Hasan, S.1    Hassa, P.O.2    Imhof, R.3    Hottiger, M.O.4
  • 166
    • 0242582360 scopus 로고    scopus 로고
    • The human proliferating Cell nuclear antigen regulates transcriptional coactivator p300 activity and promotes transcriptional repression
    • Hong R., and Chakravarti D. The human proliferating Cell nuclear antigen regulates transcriptional coactivator p300 activity and promotes transcriptional repression. J. Biol. Chem. 278 (2003) 44505-44513
    • (2003) J. Biol. Chem. , vol.278 , pp. 44505-44513
    • Hong, R.1    Chakravarti, D.2
  • 167
    • 0033799985 scopus 로고    scopus 로고
    • Human DNA-demethylating activity: a glycosylase associated with RNA and PCNA
    • Vairapandi M., Liebermann D.A., Hoffman B., and Duker N.J. Human DNA-demethylating activity: a glycosylase associated with RNA and PCNA. J. Cell. Biochem. 79 (2000) 249-260
    • (2000) J. Cell. Biochem. , vol.79 , pp. 249-260
    • Vairapandi, M.1    Liebermann, D.A.2    Hoffman, B.3    Duker, N.J.4
  • 168
    • 0035393812 scopus 로고    scopus 로고
    • hMYH cell cycle-dependent expression, subcellular localization and association with replication foci: evidence suggesting replication-coupled repair of adenine:8-oxoguanine mispairs
    • Boldogh I., Milligan D., Lee M.S., Bassett H., Lloyd R.S., and McCullough A.K. hMYH cell cycle-dependent expression, subcellular localization and association with replication foci: evidence suggesting replication-coupled repair of adenine:8-oxoguanine mispairs. Nucl. Acids Res. 29 (2001) 2802-2809
    • (2001) Nucl. Acids Res. , vol.29 , pp. 2802-2809
    • Boldogh, I.1    Milligan, D.2    Lee, M.S.3    Bassett, H.4    Lloyd, R.S.5    McCullough, A.K.6
  • 169
    • 0034738420 scopus 로고    scopus 로고
    • p21(WAF1/Cip1): more than a break to the cell cycle?
    • Dotto G.P. p21(WAF1/Cip1): more than a break to the cell cycle?. Biochim. Biophys. Acta 1471 (2000) M43-M56
    • (2000) Biochim. Biophys. Acta , vol.1471
    • Dotto, G.P.1
  • 170
    • 0242496900 scopus 로고    scopus 로고
    • Transcriptional coactivation of nuclear factor-kappaB-dependent gene expression by p300 is regulated by poly(ADP)-ribose polymerase-1
    • Hassa P.O., Buerki C., Lombardi C., Imhof R., and Hottiger M.O. Transcriptional coactivation of nuclear factor-kappaB-dependent gene expression by p300 is regulated by poly(ADP)-ribose polymerase-1. J. Biol. Chem. 278 (2003) 45145-45153
    • (2003) J. Biol. Chem. , vol.278 , pp. 45145-45153
    • Hassa, P.O.1    Buerki, C.2    Lombardi, C.3    Imhof, R.4    Hottiger, M.O.5
  • 171
    • 0344443371 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation accelerates DNA repair in a pathway dependent on Cockayne syndrome B protein
    • Flohr C., Burkle A., Radicella J.P., and Epe B. Poly(ADP-ribosyl)ation accelerates DNA repair in a pathway dependent on Cockayne syndrome B protein. Nucl. Acids Res. 31 (2003) 5332-5337
    • (2003) Nucl. Acids Res. , vol.31 , pp. 5332-5337
    • Flohr, C.1    Burkle, A.2    Radicella, J.P.3    Epe, B.4
  • 172
    • 0033575278 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase and Ku autoantigen form a complex and synergistically bind to matrix attachment sequences
    • Galande S., and Kohwi-Shigematsu T. Poly(ADP-ribose) polymerase and Ku autoantigen form a complex and synergistically bind to matrix attachment sequences. J. Biol. Chem. 274 (1999) 20521-20528
    • (1999) J. Biol. Chem. , vol.274 , pp. 20521-20528
    • Galande, S.1    Kohwi-Shigematsu, T.2
  • 173
    • 34247559561 scopus 로고    scopus 로고
    • SUMO-1 dependent allosteric regulation of Thymine DNA Glycosylase alters subnuclear localization and CBP/p300 recruitment
    • Mohan R.D., Rao A., Gagliardi J., and Tini M. SUMO-1 dependent allosteric regulation of Thymine DNA Glycosylase alters subnuclear localization and CBP/p300 recruitment. Mol. Cell. Biol. (2006)
    • (2006) Mol. Cell. Biol.
    • Mohan, R.D.1    Rao, A.2    Gagliardi, J.3    Tini, M.4
  • 174
    • 1842735419 scopus 로고    scopus 로고
    • Proteolytic degradation of the nuclear isoform of uracil-DNA glycosylase occurs during the S phase of the cell cycle
    • Fischer J.A., Muller-Weeks S., and Caradonna S. Proteolytic degradation of the nuclear isoform of uracil-DNA glycosylase occurs during the S phase of the cell cycle. DNA Repair (Amst) 3 (2004) 505-513
    • (2004) DNA Repair (Amst) , vol.3 , pp. 505-513
    • Fischer, J.A.1    Muller-Weeks, S.2    Caradonna, S.3
  • 175
    • 0035215909 scopus 로고    scopus 로고
    • The nature of enzymes involved in uracil-DNA repair: isoform characteristics of proteins responsible for nuclear and mitochondrial genomic integrity
    • Caradonna S., and Muller-Weeks S. The nature of enzymes involved in uracil-DNA repair: isoform characteristics of proteins responsible for nuclear and mitochondrial genomic integrity. Curr. Protein Pept. Sci. 2 (2001) 335-347
    • (2001) Curr. Protein Pept. Sci. , vol.2 , pp. 335-347
    • Caradonna, S.1    Muller-Weeks, S.2
  • 176
    • 1942425955 scopus 로고    scopus 로고
    • Interaction of estrogen receptor alpha with 3-methyladenine DNA glycosylase modulates transcription and DNA repair
    • Likhite V.S., Cass E.I., Anderson S.D., Yates J.R., and Nardulli A.M. Interaction of estrogen receptor alpha with 3-methyladenine DNA glycosylase modulates transcription and DNA repair. J. Biol. Chem. 279 (2004) 16875-16882
    • (2004) J. Biol. Chem. , vol.279 , pp. 16875-16882
    • Likhite, V.S.1    Cass, E.I.2    Anderson, S.D.3    Yates, J.R.4    Nardulli, A.M.5
  • 177
    • 0036606464 scopus 로고    scopus 로고
    • Human OGG1 undergoes serine phosphorylation and associates with the nuclear matrix and mitotic chromatin in vivo
    • Dantzer F., Luna L., Bjoras M., and Seeberg E. Human OGG1 undergoes serine phosphorylation and associates with the nuclear matrix and mitotic chromatin in vivo. Nucl. Acids Res. 30 (2002) 2349-2357
    • (2002) Nucl. Acids Res. , vol.30 , pp. 2349-2357
    • Dantzer, F.1    Luna, L.2    Bjoras, M.3    Seeberg, E.4
  • 178
    • 33646481320 scopus 로고    scopus 로고
    • Direct phosphorylation and regulation of poly(ADP-ribose) polymerase-1 by extracellular signal-regulated kinases 1/2
    • Kauppinen T.M., Chan W.Y., Suh S.W., Wiggins A.K., Huang E.J., and Swanson R.A. Direct phosphorylation and regulation of poly(ADP-ribose) polymerase-1 by extracellular signal-regulated kinases 1/2. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 7136-7141
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 7136-7141
    • Kauppinen, T.M.1    Chan, W.Y.2    Suh, S.W.3    Wiggins, A.K.4    Huang, E.J.5    Swanson, R.A.6
  • 180
    • 0034713227 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein processing controls radiation-induced apoptosis through the N-end rule pathway
    • Masdehors P., Glaisner S., Maciorowski Z., Magdelenat H., and Delic J. Ubiquitin-dependent protein processing controls radiation-induced apoptosis through the N-end rule pathway. Exp. Cell. Res. 257 (2000) 48-57
    • (2000) Exp. Cell. Res. , vol.257 , pp. 48-57
    • Masdehors, P.1    Glaisner, S.2    Maciorowski, Z.3    Magdelenat, H.4    Delic, J.5
  • 181
    • 0041690966 scopus 로고    scopus 로고
    • Werner syndrome protein phosphorylation by abl tyrosine kinase regulates its activity and distribution
    • Cheng W.H., von Kobbe C., Opresko P.L., Fields K.M., Ren J., Kufe D., and Bohr V.A. Werner syndrome protein phosphorylation by abl tyrosine kinase regulates its activity and distribution. Mol. Cell. Biol. 23 (2003) 6385-6395
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6385-6395
    • Cheng, W.H.1    von Kobbe, C.2    Opresko, P.L.3    Fields, K.M.4    Ren, J.5    Kufe, D.6    Bohr, V.A.7
  • 182
    • 25144471062 scopus 로고    scopus 로고
    • Cellular dynamics and modulation of WRN protein is DNA damage specific
    • Karmakar P., and Bohr V.A. Cellular dynamics and modulation of WRN protein is DNA damage specific. Mech. Ageing Dev. 126 (2005) 1146-1158
    • (2005) Mech. Ageing Dev. , vol.126 , pp. 1146-1158
    • Karmakar, P.1    Bohr, V.A.2
  • 183
  • 184
    • 0037435026 scopus 로고    scopus 로고
    • Werner's syndrome protein is phosphorylated in an ATR/ATM-dependent manner following replication arrest and DNA damage induced during the S phase of the cell cycle
    • Pichierri P., Rosselli F., and Franchitto A. Werner's syndrome protein is phosphorylated in an ATR/ATM-dependent manner following replication arrest and DNA damage induced during the S phase of the cell cycle. Oncogene 22 (2003) 1491-1500
    • (2003) Oncogene , vol.22 , pp. 1491-1500
    • Pichierri, P.1    Rosselli, F.2    Franchitto, A.3
  • 185
    • 0035851181 scopus 로고    scopus 로고
    • Werner syndrome protein is regulated and phosphorylated by DNA-dependent protein kinase
    • Yannone S.M., Roy S., Chan D.W., Murphy M.B., Huang S., Campisi J., and Chen D.J. Werner syndrome protein is regulated and phosphorylated by DNA-dependent protein kinase. J. Biol. Chem. 276 (2001) 38242-38248
    • (2001) J. Biol. Chem. , vol.276 , pp. 38242-38248
    • Yannone, S.M.1    Roy, S.2    Chan, D.W.3    Murphy, M.B.4    Huang, S.5    Campisi, J.6    Chen, D.J.7
  • 186
    • 0034647556 scopus 로고    scopus 로고
    • Covalent modification of the Werner's syndrome gene product with the ubiquitin-related protein, SUMO-1
    • Kawabe Y., Seki M., Seki T., Wang W.S., Imamura O., Furuichi Y., Saitoh H., and Enomoto T. Covalent modification of the Werner's syndrome gene product with the ubiquitin-related protein, SUMO-1. J. Biol. Chem. 275 (2000) 20963-20966
    • (2000) J. Biol. Chem. , vol.275 , pp. 20963-20966
    • Kawabe, Y.1    Seki, M.2    Seki, T.3    Wang, W.S.4    Imamura, O.5    Furuichi, Y.6    Saitoh, H.7    Enomoto, T.8
  • 188
    • 0027946715 scopus 로고
    • Proliferating cell nuclear antigen bound to DNA synthesis sites: phosphorylation and association with cyclin D1 and cyclin A
    • Prosperi E., Scovassi A.I., Stivala L.A., and Bianchi L. Proliferating cell nuclear antigen bound to DNA synthesis sites: phosphorylation and association with cyclin D1 and cyclin A. Exp. Cell Res. 215 (1994) 257-262
    • (1994) Exp. Cell Res. , vol.215 , pp. 257-262
    • Prosperi, E.1    Scovassi, A.I.2    Stivala, L.A.3    Bianchi, L.4
  • 189
    • 2942529467 scopus 로고    scopus 로고
    • Opposing effects of ubiquitin conjugation and SUMO modification of PCNA on replicational bypass of DNA lesions in Saccharomyces cerevisiae
    • Haracska L., Torres-Ramos C.A., Johnson R.E., Prakash S., and Prakash L. Opposing effects of ubiquitin conjugation and SUMO modification of PCNA on replicational bypass of DNA lesions in Saccharomyces cerevisiae. Mol. Cell Biol. 24 (2004) 4267-4274
    • (2004) Mol. Cell Biol. , vol.24 , pp. 4267-4274
    • Haracska, L.1    Torres-Ramos, C.A.2    Johnson, R.E.3    Prakash, S.4    Prakash, L.5
  • 190
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., and Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419 (2002) 135-141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 191
    • 4143131124 scopus 로고    scopus 로고
    • Dynamic targeting of the replication machinery to sites of DNA damage
    • Solomon D.A., Cardoso M.C., and Knudsen E.S. Dynamic targeting of the replication machinery to sites of DNA damage. J. Cell Biol. 166 (2004) 455-463
    • (2004) J. Cell Biol. , vol.166 , pp. 455-463
    • Solomon, D.A.1    Cardoso, M.C.2    Knudsen, E.S.3
  • 192
    • 14644391577 scopus 로고    scopus 로고
    • The Fanconi anemia pathway is required for the DNA replication stress response and for the regulation of common fragile site stability
    • Howlett N.G., Taniguchi T., Durkin S.G., D'Andrea A.D., and Glover T.W. The Fanconi anemia pathway is required for the DNA replication stress response and for the regulation of common fragile site stability. Hum. Mol. Genet. 14 (2005) 693-701
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 693-701
    • Howlett, N.G.1    Taniguchi, T.2    Durkin, S.G.3    D'Andrea, A.D.4    Glover, T.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.