메뉴 건너뛰기




Volumn 531, Issue 1-2, 2003, Pages 157-163

Repair of abasic sites in DNA

Author keywords

Abasic sites; Alkylating agents; DNA

Indexed keywords

CELL NUCLEUS ANTIGEN; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA DIRECTED DNA POLYMERASE BETA; DNA DIRECTED DNA POLYMERASE DELTA; ENDONUCLEASE; ISOENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; SUGAR PHOSPHATE;

EID: 0345448125     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2003.09.003     Document Type: Conference Paper
Times cited : (175)

References (72)
  • 1
    • 0015504248 scopus 로고
    • Rate of depurination of native deoxyribonucleic acid
    • Lindahl T., Nyberg B. Rate of depurination of native deoxyribonucleic acid. Biochemistry. 11:1972;3610-3618.
    • (1972) Biochemistry , vol.11 , pp. 3610-3618
    • Lindahl, T.1    Nyberg, B.2
  • 2
    • 0015753524 scopus 로고
    • Heat-induced depyrimidination of DNA
    • Lindahl T., Karlström O. Heat-induced depyrimidination of DNA. Biochemistry. 12:1973;5151-5154.
    • (1973) Biochemistry , vol.12 , pp. 5151-5154
    • Lindahl, T.1    Karlström, O.2
  • 3
    • 0015504253 scopus 로고
    • Rate of chain breakage of apurinic sites in double-stranded DNA
    • Lindahl T., Andersson A. Rate of chain breakage of apurinic sites in double-stranded DNA. Biochemistry. 11:1972;3618-3623.
    • (1972) Biochemistry , vol.11 , pp. 3618-3623
    • Lindahl, T.1    Andersson, A.2
  • 4
    • 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
  • 5
    • 0037013854 scopus 로고    scopus 로고
    • Endogenous DNA abasic sites cause cell death in the absence of APN1, APN2 and Rad1/Rad10 in Saccharomyces cerevisiae
    • Guillet M., Boiteux S. Endogenous DNA abasic sites cause cell death in the absence of APN1, APN2 and Rad1/Rad10 in Saccharomyces cerevisiae. EMBO J. 21:2002;2833-2841.
    • (2002) EMBO J. , vol.21 , pp. 2833-2841
    • Guillet, M.1    Boiteux, S.2
  • 6
    • 0023015325 scopus 로고
    • Mutagenesis by apurinic/apyrimidinic sites
    • Loeb L.A., Preston B.D. Mutagenesis by apurinic/apyrimidinic sites. Ann. Rev. Genet. 20:1986;201-230.
    • (1986) Ann. Rev. Genet. , vol.20 , pp. 201-230
    • Loeb, L.A.1    Preston, B.D.2
  • 8
    • 0034691679 scopus 로고    scopus 로고
    • Mutation spectra induced by replication of two vicinal oxidative DNA lesions in mammalian cells
    • Gentil A., Le Page F., Cadet J., Sarasin A. Mutation spectra induced by replication of two vicinal oxidative DNA lesions in mammalian cells. Mutat. Res. Fundam. Mol. Mech. Mutagen. 452:2000;51-56.
    • (2000) Mutat. Res. Fundam. Mol. Mech. Mutagen. , vol.452 , pp. 51-56
    • Gentil, A.1    Le Page, F.2    Cadet, J.3    Sarasin, A.4
  • 10
    • 0026004662 scopus 로고
    • Two distinct human diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidised DNA
    • Chen D.S., Herman V.G., Demple B. Two distinct human diesterases that hydrolyze 3′-blocking deoxyribose fragments from oxidised DNA. Nucl. Acids Res. 19:1991;5907-5914.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 5907-5914
    • Chen, D.S.1    Herman, V.G.2    Demple, B.3
  • 13
    • 0026507413 scopus 로고
    • Role of poly(ADP-ribose) formation in DNA repair
    • Satoh M.S., Lindahl T. Role of poly(ADP-ribose) formation in DNA repair. Nature. 356:1992;356-358.
    • (1992) Nature , vol.356 , pp. 356-358
    • Satoh, M.S.1    Lindahl, T.2
  • 14
    • 0027412686 scopus 로고
    • NAD(+)-dependent repair of damaged DNA by human cell extracts
    • Satoh M.S., Poirier G.G., Lindahl T. NAD(+)-dependent repair of damaged DNA by human cell extracts. J. Biol. Chem. 268:1993;5480-5487.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5480-5487
    • Satoh, M.S.1    Poirier, G.G.2    Lindahl, T.3
  • 15
    • 0041386129 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase in base excision repair: Always engaged but not essential for DNA damage processing
    • S.L. Allinson, I.I. Dianova, G.L. Dianov, Poly(ADP-ribose) polymerase in base excision repair: always engaged but not essential for DNA damage processing, Acta Biochim. Polonica, 50 (2003) 169-179.
    • (2003) Acta Biochim. Polonica , vol.50 , pp. 169-179
    • Allinson, S.L.1    Dianova, I.I.2    Dianov, G.L.3
  • 16
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours D., Desnoyers S., D'Silva I., Poirier G.G. Poly(ADP-ribosyl) ation reactions in the regulation of nuclear functions. Biochem. J. 324:1999;249-268.
    • (1999) Biochem. J. , vol.324 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 17
    • 0033362084 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase in the cellular response to DNA damage, apoptosis, and disease
    • Oliver F.J., Menissier-de Murcia J., de Murcia G. Poly(ADP-ribose) polymerase in the cellular response to DNA damage, apoptosis, and disease. Am. J. Hum. Genet. 64:1999;1282-1288.
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 1282-1288
    • Oliver, F.J.1    Menissier-De Murcia, J.2    De Murcia, G.3
  • 19
    • 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. 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
  • 23
    • 0035869014 scopus 로고    scopus 로고
    • Human DNA polymerase beta initiates DNA synthesis during long-patch repair of reduced AP sites in DNA
    • Podlutsky A.J., Dianova I.I., Podust V.N., Bohr V.A., Dianov G.L. Human DNA polymerase beta initiates DNA synthesis during long-patch repair of reduced AP sites in DNA. EMBO J. 20:2001;1477-1482.
    • (2001) EMBO J. , vol.20 , pp. 1477-1482
    • Podlutsky, A.J.1    Dianova, I.I.2    Podust, V.N.3    Bohr, V.A.4    Dianov, G.L.5
  • 24
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair
    • Matsumoto Y., Kim K. Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair. Science. 269:1995;699-702.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 25
    • 0035936560 scopus 로고    scopus 로고
    • DNA synthesis and dRPase activities of polymerase beta are both essential for single-nucleotide patch base excision repair in mammalian cell extracts
    • Podlutsky A.J., Dianova I.I., Wilson S.H., Bohr V.A., Dianov G.L. DNA synthesis and dRPase activities of polymerase beta are both essential for single-nucleotide patch base excision repair in mammalian cell extracts. Biochemistry. 40:2001;809-813.
    • (2001) Biochemistry , vol.40 , pp. 809-813
    • Podlutsky, A.J.1    Dianova, I.I.2    Wilson, S.H.3    Bohr, V.A.4    Dianov, G.L.5
  • 26
    • 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., 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;4460-4465.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4460-4465
    • Prasad, R.1    Dianov, G.L.2    Bohr, V.A.3    Wilson, S.H.4
  • 27
    • 0032502675 scopus 로고    scopus 로고
    • Involvement of flap endonuclease 1 in base excision DNA repair
    • Kim K., Biade S., Matsumoto Y. Involvement of flap endonuclease 1 in base excision DNA repair. J. Biol. Chem. 273:1998;8842-8848.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8842-8848
    • Kim, K.1    Biade, S.2    Matsumoto, Y.3
  • 28
    • 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., 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
  • 29
    • 0026589375 scopus 로고
    • Generation of single-nucleotide repair patches following excision of uracil residues from DNA
    • Dianov G., Price A., Lindahl T. Generation of single-nucleotide repair patches following excision of uracil residues from DNA. Mol. Cell. Biol. 12:1992;1605-1612.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1605-1612
    • Dianov, G.1    Price, A.2    Lindahl, T.3
  • 30
    • 0028966181 scopus 로고
    • DNA polymerase beta conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract
    • Singhal R.K., Prasad R., Wilson S.H. DNA polymerase beta conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract. J. Biol. Chem. 270:1995;949-957.
    • (1995) J. Biol. Chem. , vol.270 , pp. 949-957
    • Singhal, R.K.1    Prasad, R.2    Wilson, S.H.3
  • 31
    • 0027965229 scopus 로고
    • Proliferating cell nuclear antigen-dependent abasic site repair in Xenopus laevis oocytes: An alternative pathway of base excision DNA repair
    • Matsumoto Y., Kim K., Bogenhagen D.F. Proliferating cell nuclear antigen-dependent abasic site repair in Xenopus laevis oocytes: an alternative pathway of base excision DNA repair. Mol. Cell. Biol. 14:1994;6187-6197.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6187-6197
    • Matsumoto, Y.1    Kim, K.2    Bogenhagen, D.F.3
  • 34
    • 0033591336 scopus 로고    scopus 로고
    • The type of DNA glycosylase determines the base excision repair pathway in mammalian cells
    • Fortini P., Parlanti E., Sidorkina O.M., Laval J., Dogliotti E. The type of DNA glycosylase determines the base excision repair pathway in mammalian cells. J. Biol. Chem. 274:1999;15230-15236.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15230-15236
    • Fortini, P.1    Parlanti, E.2    Sidorkina, O.M.3    Laval, J.4    Dogliotti, E.5
  • 35
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN1)
    • Klungland A., Lindahl T. Second pathway for completion of human DNA base excision-repair: reconstitution with purified proteins and requirement for DNase IV (FEN1). EMBO J. 16:1997;3341-3348.
    • (1997) EMBO J. , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 36
    • 0033553510 scopus 로고    scopus 로고
    • Role of DNA polymerase β in the excision step of long patch mammalian base excision repair
    • Dianov G.L., Prasad R., Wilson S.H., Bohr V.A. Role of DNA polymerase β in the excision step of long patch mammalian base excision repair. J. Biol. Chem. 274:1999;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
  • 37
    • 0033600570 scopus 로고    scopus 로고
    • Replication protein a stimulates proliferating cell nuclear antigen-dependent repair of abasic sites in DNA by human cell extracts
    • Dianov G.L., Jensen B.R., Kenny M.K., Bohr V.A. Replication protein A stimulates proliferating cell nuclear antigen-dependent repair of abasic sites in DNA by human cell extracts. Biochemistry. 38:1999;11021-11025.
    • (1999) Biochemistry , vol.38 , pp. 11021-11025
    • Dianov, G.L.1    Jensen, B.R.2    Kenny, M.K.3    Bohr, V.A.4
  • 38
    • 0000632757 scopus 로고    scopus 로고
    • Cellular DNA polymerases
    • M.L. DePamphilis (Ed.) Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • T.S.-F. Wang, Cellular DNA polymerases, in: M.L. DePamphilis (Ed.), DNA Replication in Eukaryotic Cells, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1996, pp. 461-463.
    • (1996) DNA Replication in Eukaryotic Cells , pp. 461-463
    • Wang, T.S.-F.1
  • 39
    • 0024461703 scopus 로고
    • Repair of a synthetic abasic site in DNA in a Xenopus laevis oocyte extract
    • Matsumoto Y., Bogenhagen D. Repair of a synthetic abasic site in DNA in a Xenopus laevis oocyte extract. Mol. Cell Biol. 9:1989;3750-3757.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 3750-3757
    • Matsumoto, Y.1    Bogenhagen, D.2
  • 40
    • 0033585072 scopus 로고    scopus 로고
    • Reconstitution of proliferating cell nuclear antigen-dependent repair of apurinic/apyrimidinic sites with purified human proteins
    • Matsumoto Y., Kim K., Hurwitz J., Gary R., Levin D.S., Tomkinson A.E., Park M.S. Reconstitution of proliferating cell nuclear antigen-dependent repair of apurinic/apyrimidinic sites with purified human proteins. J. Biol. Chem. 274:1999;33703-33708.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33703-33708
    • Matsumoto, Y.1    Kim, K.2    Hurwitz, J.3    Gary, R.4    Levin, D.S.5    Tomkinson, A.E.6    Park, M.S.7
  • 41
    • 0029092897 scopus 로고
    • Lagging strand DNA synthesis at the eukaryotic replication fork involves binding and stimulation of FEN-1 by proliferating cell nuclear antigen
    • Li X., Li J., Harrington J., Lieber M.R., Burgers P.M. Lagging strand DNA synthesis at the eukaryotic replication fork involves binding and stimulation of FEN-1 by proliferating cell nuclear antigen. J. Biol. Chem. 270:1995;22109-22112.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22109-22112
    • Li, X.1    Li, J.2    Harrington, J.3    Lieber, M.R.4    Burgers, P.M.5
  • 42
    • 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., 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
  • 43
    • 0034616199 scopus 로고    scopus 로고
    • Mechanism whereby proliferating cell nuclear antigen stimulates flap endonuclease1
    • Tom S., Henricksen L.A., Bambara R.A. Mechanism whereby proliferating cell nuclear antigen stimulates flap endonuclease1. 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
  • 44
    • 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., 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
  • 45
    • 0025781295 scopus 로고
    • Biochemical and functional comparison of DNA polymerases α, δ, ε from calf thymus
    • Weiser T., Gassmann M., Thommes P., Ferraru E., Spadari S., Hubsher U. Biochemical and functional comparison of DNA polymerases α, δ, ε from calf thymus. J. Biol. Chem. 266:1991;10420-10428.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10420-10428
    • Weiser, T.1    Gassmann, M.2    Thommes, P.3    Ferraru, E.4    Spadari, S.5    Hubsher, U.6
  • 47
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway
    • Bennett R.A.O., Wilson D.M. Jr., Wong D., Demple B. Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway. Proc. Natl. Acad. Sci. U.S.A. 94:1997;7166-7169.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7166-7169
    • Bennett, R.A.O.1    Wilson, D.M.Jr.2    Wong, D.3    Demple, B.4
  • 48
    • 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. 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
  • 49
    • 0035940441 scopus 로고    scopus 로고
    • Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair
    • Dianova I.I., Bohr V.A., Dianov G.L. Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair. Biochemistry. 40:2001;12639-12644.
    • (2001) Biochemistry , vol.40 , pp. 12639-12644
    • Dianova, I.I.1    Bohr, V.A.2    Dianov, G.L.3
  • 50
    • 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., 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
  • 53
    • 0030692134 scopus 로고    scopus 로고
    • An interaction between DNA ligase I and proliferating cell nuclear antigen: Implication for Okazaki fragment synthesis and joining
    • Levin D.S., Bai W., Yao N., O'Donnell M., Tomkinson A.E. An interaction between DNA ligase I and proliferating cell nuclear antigen: implication for Okazaki fragment synthesis and joining. Proc. Natl. Acad. Sci. U.S.A. 94:1997;12863-12868.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12863-12868
    • Levin, D.S.1    Bai, W.2    Yao, N.3    O'Donnell, M.4    Tomkinson, A.E.5
  • 54
    • 0032126647 scopus 로고    scopus 로고
    • DNA ligase I is recruited to sites of DNA replication by an interaction with prolifirating cell nuclear antigen: Identification of a common targeting mechanism for the assembly of replication factories
    • Montecucco A., Rossi R., Levin D.S., Gary R., Park M.S., Motycka T.A., Giarrocchi G., Villa A., Biamonti G., Tomkinson A. DNA ligase I is recruited to sites of DNA replication by an interaction with prolifirating cell nuclear antigen: identification of a common targeting mechanism for the assembly of replication factories. EMBO J. 17:1998;3786-3795.
    • (1998) EMBO J. , vol.17 , pp. 3786-3795
    • Montecucco, A.1    Rossi, R.2    Levin, D.S.3    Gary, R.4    Park, M.S.5    Motycka, T.A.6    Giarrocchi, G.7    Villa, A.8    Biamonti, G.9    Tomkinson, A.10
  • 55
    • 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., Matsumoto Y. Proliferating cell nuclear antigen facilitates excision in long-patch base excision repair. J. Biol. Chem. 7:1999;4354-4363.
    • (1999) J. Biol. Chem. , vol.7 , pp. 4354-4363
    • Gary, R.1    Kim, K.2    Cornelius, H.L.3    Park, M.S.4    Matsumoto, Y.5
  • 56
    • 0034610276 scopus 로고    scopus 로고
    • Mutation of a BRCT domain selectively disrupts DNA single-strand break repair in noncycling Chinese hamster ovary cells
    • Moore D.J., Taylor R.M., Clements P., Caldecott K.W. Mutation of a BRCT domain selectively disrupts DNA single-strand break repair in noncycling Chinese hamster ovary cells. Proc. Natl. Acad. Sci. U.S.A. 97:2000;13649-13654.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13649-13654
    • Moore, D.J.1    Taylor, R.M.2    Clements, P.3    Caldecott, K.W.4
  • 57
    • 0030696203 scopus 로고    scopus 로고
    • Who binds wins: Competiton for PCNA rings out cell-cycle changes
    • Cox L.S. Who binds wins: competiton for PCNA rings out cell-cycle changes. Trends Cell Biol. 7:1997;493-498.
    • (1997) Trends Cell Biol. , vol.7 , pp. 493-498
    • Cox, L.S.1
  • 58
    • 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., 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.5    Lindahl, T.6
  • 60
    • 0030018848 scopus 로고    scopus 로고
    • Specific interaction of DNA polymerase beta 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., Wilson S.H. Specific interaction of DNA polymerase beta 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
  • 62
    • 0034093291 scopus 로고    scopus 로고
    • Passing the baton in base excision repair
    • Wilson S.H., 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
  • 63
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination
    • Mol C.D., Izumi T., Mitra S., Tainer J.A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination. Nature. 403:2000;451-454.
    • (2000) Nature , vol.403 , pp. 451-454
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 64
    • 0035834632 scopus 로고    scopus 로고
    • Fidelity of uracil-initiated base excision DNA repair in DNA polymerase beta-proficient and -deficient mouse embryonic fibroblast cell extracts
    • Bennett S.E., Sung J.S., Mosbaugh D.W. Fidelity of uracil-initiated base excision DNA repair in DNA polymerase beta-proficient and -deficient mouse embryonic fibroblast cell extracts. J. Biol. Chem. 276:2001;42588-42600.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42588-42600
    • Bennett, S.E.1    Sung, J.S.2    Mosbaugh, D.W.3
  • 65
    • 0035228762 scopus 로고    scopus 로고
    • Uracil-initiated base excision DNA repair synthesis fidelity in human colon adenocarcinoma LoVo and Escherichia coli cell extracts
    • Sanderson R.J., Bennett S.E., Sung J.S., Mosbaugh D.W. Uracil-initiated base excision DNA repair synthesis fidelity in human colon adenocarcinoma LoVo and Escherichia coli cell extracts. Prog. Nucl. Acid Res. Mol. Biol. 68:2001;165-188.
    • (2001) Prog. Nucl. Acid Res. Mol. Biol. , vol.68 , pp. 165-188
    • Sanderson, R.J.1    Bennett, S.E.2    Sung, J.S.3    Mosbaugh, D.W.4
  • 66
    • 0032544558 scopus 로고    scopus 로고
    • Fidelity and mutational specificity of uracil-initiated base excision DNA repair synthesis in human glioblastoma cell extracts
    • Sanderson R.J., Mosbaugh D.W. Fidelity and mutational specificity of uracil-initiated base excision DNA repair synthesis in human glioblastoma cell extracts. J. Biol. Chem. 273:1998;24822-24831.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24822-24831
    • Sanderson, R.J.1    Mosbaugh, D.W.2
  • 67
    • 0034769358 scopus 로고    scopus 로고
    • HPRT mutations in humans: Biomarkers for mechanistic studies
    • Albertini R. HPRT mutations in humans: biomarkers for mechanistic studies. Mutat. Res. 489:2001;1-16.
    • (2001) Mutat. Res. , vol.489 , pp. 1-16
    • Albertini, R.1
  • 69
    • 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. 336:1995;9-17.
    • (1995) Mutat. Res. , vol.336 , pp. 9-17
    • Coquerelle, T.1    Dosch, J.2    Kaina, B.3
  • 70
    • 0035959869 scopus 로고    scopus 로고
    • Enhanced expression and activity of DNA polymerase beta in human ovarian tumor cells: Impact on sensitivity towards antitumor agents
    • Bergoglio V., Canitrot Y., Hogarth L., Minto L., Howell S.B., Cazaux C., Hoffmann J.S. Enhanced expression and activity of DNA polymerase beta in human ovarian tumor cells: impact on sensitivity towards antitumor agents. Oncogene. 20:2001;6181-6187.
    • (2001) Oncogene , vol.20 , pp. 6181-6187
    • Bergoglio, V.1    Canitrot, Y.2    Hogarth, L.3    Minto, L.4    Howell, S.B.5    Cazaux, C.6    Hoffmann, J.S.7
  • 71
    • 0032514636 scopus 로고    scopus 로고
    • Overexpression of DNA polymerase beta in cell results in a mutator phenotype and a decreased sensitivity to anticancer drugs
    • Canitrot Y., Cazaux C., Frechet M., Bouayadi K., Lesca C., Salles B., Hoffmann J.S. Overexpression of DNA polymerase beta in cell results in a mutator phenotype and a decreased sensitivity to anticancer drugs. Proc. Natl. Acad. Sci. U.S.A. 95:1998;12586-12590.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 12586-12590
    • Canitrot, Y.1    Cazaux, C.2    Frechet, M.3    Bouayadi, K.4    Lesca, C.5    Salles, B.6    Hoffmann, J.S.7
  • 72
    • 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. 20:1999;1049-1054.
    • (1999) Carcinogenesis , vol.20 , pp. 1049-1054
    • Srivastava, D.K.1    Husain, I.2    Arteaga, C.L.3    Wilson, S.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.