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Volumn 193, Issue 1-2, 2003, Pages 3-34

Mechanisms of human DNA repair: An update

Author keywords

DNA damage signaling; DNA repair gene; DNA repair protein

Indexed keywords

ATAXIA TELANGIECTASIA RELATED PROTEIN; ATM PROTEIN; CLASTOGEN; DNA; DNA GLYCOSYLTRANSFERASE; DNA POLYMERASE; METHYLATED DNA PROTEIN CYSTEINE METHYLTRANSFERASE; MUTAGENIC AGENT; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PHOSPHATIDYLINOSITOL 3 KINASE; UNCLASSIFIED DRUG;

EID: 0242331221     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-483X(03)00287-7     Document Type: Review
Times cited : (473)

References (388)
  • 5
    • 0036791008 scopus 로고    scopus 로고
    • P53 and DNA damage-inducible expression of the xeroderma pigmentosum group C gene
    • Adimoolam S., Ford J.M. p53 and DNA damage-inducible expression of the xeroderma pigmentosum group C gene. Proc. Natl. Acad. Sci. U.S.A. 99:2002;12985-12990.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12985-12990
    • Adimoolam, S.1    Ford, J.M.2
  • 6
    • 0030962031 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of Msh2p-Msh6p: Role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition
    • Alani E., Sokolsky T., Studamire B., Miret J., Lahue R. Genetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition. Mol. Cell. Biol. 17:1997;2436-2447.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2436-2447
    • Alani, E.1    Sokolsky, T.2    Studamire, B.3    Miret, J.4    Lahue, R.5
  • 9
    • 0036490207 scopus 로고    scopus 로고
    • A nucleotide excision repair master-switch: P53 regulated coordinate induction of global genomic repair genes
    • Amundson S.A., Patterson A., Do K.T., Fornace A.J. Jr. A nucleotide excision repair master-switch: p53 regulated coordinate induction of global genomic repair genes. Cancer Biol. Ther. 1:2002;145-149.
    • (2002) Cancer Biol. Ther. , vol.1 , pp. 145-149
    • Amundson, S.A.1    Patterson, A.2    Do, K.T.3    Fornace A.J., Jr.4
  • 10
    • 0242605710 scopus 로고    scopus 로고
    • Nucleotide excision repair of DNA with recombinant human proteins: Definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK
    • Araujo S.J., Tirode F., Coin F., Pospiech H., Syvaoja J.E., Stucki M., Hubscher U., Egly J.M., Wood R.D. Nucleotide excision repair of DNA with recombinant human proteins: definition of the minimal set of factors, active forms of TFIIH, and modulation by CAK. Genes Dev. 14:2000;349-359.
    • (2000) Genes Dev. , vol.14 , pp. 349-359
    • Araujo, S.J.1    Tirode, F.2    Coin, F.3    Pospiech, H.4    Syvaoja, J.E.5    Stucki, M.6    Hubscher, U.7    Egly, J.M.8    Wood, R.D.9
  • 12
    • 0037472924 scopus 로고    scopus 로고
    • DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation
    • Bakkenist C.J., Kastan M.B. DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation. Nature. 421:2003;499-506.
    • (2003) Nature , vol.421 , pp. 499-506
    • Bakkenist, C.J.1    Kastan, M.B.2
  • 13
    • 0034732890 scopus 로고    scopus 로고
    • Genomic heterogeneity of nucleotide excision repair
    • Balajee A.S., Bohr V.A. Genomic heterogeneity of nucleotide excision repair. Gene. 250:2000;15-30.
    • (2000) Gene , vol.250 , pp. 15-30
    • Balajee, A.S.1    Bohr, V.A.2
  • 14
    • 0030902253 scopus 로고    scopus 로고
    • Reduced RNA polymerase II transcription in intact and permeabilized Cockayne syndrome group B cells
    • Balajee A.S., May A., Dianov G.L., Friedberg E.C., Bohr V.A. Reduced RNA polymerase II transcription in intact and permeabilized Cockayne syndrome group B cells. Proc. Natl. Acad. Sci. U.S.A. 94:1997;4306-4311.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 4306-4311
    • Balajee, A.S.1    May, A.2    Dianov, G.L.3    Friedberg, E.C.4    Bohr, V.A.5
  • 17
    • 0030766963 scopus 로고    scopus 로고
    • The human Rad51 protein: Polarity of strand transfer and stimulation by hRP-A
    • Baumann P., West S.C. The human Rad51 protein: polarity of strand transfer and stimulation by hRP-A. EMBO J. 16:1997;5198-5206.
    • (1997) EMBO J. , vol.16 , pp. 5198-5206
    • Baumann, P.1    West, S.C.2
  • 19
    • 0029901710 scopus 로고    scopus 로고
    • 6-methylguanine-DNA methyltransferase (MGMT) in transgenic mice protects against tumor initiation in two-stage skin carcinogenesis
    • 6-methylguanine-DNA methyltransferase (MGMT) in transgenic mice protects against tumor initiation in two-stage skin carcinogenesis. Cancer Res. 56:1996;3244-3249.
    • (1996) Cancer Res. , vol.56 , pp. 3244-3249
    • Becker, K.1    Dosch, J.2    Gregel, C.M.3    Martin, B.A.4    Kaina, B.5
  • 20
    • 0037357457 scopus 로고    scopus 로고
    • Becker, K., Gregel, C., Fricke, C., Komitowski, D., Dosch, J., Kaina, B., 2003. DNA-repair protein MGMT protects against N-methyl-N-nitrosurea induced conversion of benign into malignant tumors. Carcinogenesis, 24, 541-546.
    • Becker, K., Gregel, C., Fricke, C., Komitowski, D., Dosch, J., Kaina, B., 2003. DNA-repair protein MGMT protects against N-methyl-N-nitrosurea induced conversion of benign into malignant tumors. Carcinogenesis, 24, 541-546.
  • 21
    • 0030749230 scopus 로고    scopus 로고
    • 6-methylguanine-DNA methyltransferase protects against skin tumor formation induced by antineoplastic chloroethylnitrosourea
    • 6-methylguanine-DNA methyltransferase protects against skin tumor formation induced by antineoplastic chloroethylnitrosourea. Cancer Res. 57:1997;3335-3338.
    • (1997) Cancer Res. , vol.57 , pp. 3335-3338
    • Becker, K.1    Gregel, C.M.2    Kaina, B.3
  • 22
    • 0033816288 scopus 로고    scopus 로고
    • DNA excision repair and DNA damage-induced apoptosis are linked to poly(adp-ribosyl)ation but have different requirements for p53
    • Beneke R., Geisen C., Zevnik B., Bauch T., Muller W.U., Kupper J.H., Moroy T. DNA excision repair and DNA damage-induced apoptosis are linked to poly(adp-ribosyl)ation but have different requirements for p53. Mol. Cell. Biol. 20:2000;6695-6703.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6695-6703
    • Beneke, R.1    Geisen, C.2    Zevnik, B.3    Bauch, T.4    Muller, W.U.5    Kupper, J.H.6    Moroy, T.7
  • 23
    • 0028072098 scopus 로고
    • Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA.
    • Benson F.E., Stasiak A., West S.C. Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA. EMBO J. 13:1994;5764-5771.
    • (1994) EMBO J. , vol.13 , pp. 5764-5771
    • Benson, F.E.1    Stasiak, A.2    West, S.C.3
  • 24
    • 0025288239 scopus 로고
    • Distribution of methyl and ethyl adducts following alkylation with monofunctional alkylating agents
    • Beranek D.T. Distribution of methyl and ethyl adducts following alkylation with monofunctional alkylating agents. Mutat. Res. 231:1990;11-30.
    • (1990) Mutat. Res. , vol.231 , pp. 11-30
    • Beranek, D.T.1
  • 25
    • 0034622670 scopus 로고    scopus 로고
    • 6-methylguanine DNA adducts on the adenosine nucleotide switch functions of hMSH2-hMSH6 and hMSH2-hMSH3
    • 6- methylguanine DNA adducts on the adenosine nucleotide switch functions of hMSH2-hMSH6 and hMSH2-hMSH3. J. Biol. Chem. 275:2000;27851-27857.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27851-27857
    • Berardini, M.1    Mazurek, A.2    Fishel, R.3
  • 26
    • 0032938449 scopus 로고    scopus 로고
    • PADPRT-2: A novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans
    • Berghammer H., Ebner M., Marksteiner R., Auer B. pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans. FEBS Lett. 449:1999;259-263.
    • (1999) FEBS Lett. , vol.449 , pp. 259-263
    • Berghammer, H.1    Ebner, M.2    Marksteiner, R.3    Auer, B.4
  • 28
    • 0030703177 scopus 로고    scopus 로고
    • Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites
    • Bjoras M., Luna L., Johnsen B., Hoff E., Haug T., Rognes T., Seeberg E. Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites. EMBO J. 16:1997;6314-6322.
    • (1997) EMBO J. , vol.16 , pp. 6314-6322
    • Bjoras, M.1    Luna, L.2    Johnsen, B.3    Hoff, E.4    Haug, T.5    Rognes, T.6    Seeberg, E.7
  • 29
    • 0035823513 scopus 로고    scopus 로고
    • Distinct MutS DNA-binding modes that are differentially modulated by ATP binding and hydrolysis
    • Blackwell L.J., Bjornson K.P., Allen D.J., Modrich P. Distinct MutS DNA-binding modes that are differentially modulated by ATP binding and hydrolysis. J. Biol. Chem. 276:2001;34339-34347.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34339-34347
    • Blackwell, L.J.1    Bjornson, K.P.2    Allen, D.J.3    Modrich, P.4
  • 30
    • 0033610852 scopus 로고    scopus 로고
    • DNA-dependent activation of the hMutSalpha ATPase
    • Blackwell L.J., Bjornson K.P., Modrich P. DNA-dependent activation of the hMutSalpha ATPase. J. Biol. Chem. 273:1998a;32049-32054.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32049-32054
    • Blackwell, L.J.1    Bjornson, K.P.2    Modrich, P.3
  • 31
    • 0033610878 scopus 로고    scopus 로고
    • Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism
    • Blackwell L.J., Martik D., Bjornson K.P., Bjornson E.S., Modrich P. Nucleotide-promoted release of hMutSalpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism. J. Biol. Chem. 273:1998b;32055-32062.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32055-32062
    • Blackwell, L.J.1    Martik, D.2    Bjornson, K.P.3    Bjornson, E.S.4    Modrich, P.5
  • 32
    • 0021905437 scopus 로고
    • DNA repair in an active gene: Removal of pyrimidine dimers from the DHFR gene of CHO cells is much more efficient than in the genome overall
    • Bohr V.A., Smith C.A., Okumoto D.S., Hanawalt P.C. DNA repair in an active gene: removal of pyrimidine dimers from the DHFR gene of CHO cells is much more efficient than in the genome overall. Cell. 40:1985;359-369.
    • (1985) Cell , vol.40 , pp. 359-369
    • Bohr, V.A.1    Smith, C.A.2    Okumoto, D.S.3    Hanawalt, P.C.4
  • 34
    • 0027174179 scopus 로고
    • DNA repair. Engagement with transcription
    • Bootsma D., Hoeijmakers J.H. DNA repair. Engagement with transcription. Nature. 363:1993;114-115.
    • (1993) Nature , vol.363 , pp. 114-115
    • Bootsma, D.1    Hoeijmakers, J.H.2
  • 39
    • 0035495529 scopus 로고    scopus 로고
    • PARP-1: A regulator of genomic stability linked with mammalian longevity
    • Bürkle A. PARP-1: a regulator of genomic stability linked with mammalian longevity. Chembiochem. 2:2001;725-728.
    • (2001) Chembiochem , vol.2 , pp. 725-728
    • Bürkle, A.1
  • 40
    • 0035834693 scopus 로고    scopus 로고
    • ATM phosphorylates histone H2AX in response to DNA double-strand breaks
    • Burma S., Chen B.P., Murphy M., Kurimasa A., Chen D.J. ATM phosphorylates histone H2AX in response to DNA double-strand breaks. J. Biol. Chem. 276:2001;42462-42467.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42462-42467
    • Burma, S.1    Chen, B.P.2    Murphy, M.3    Kurimasa, A.4    Chen, D.J.5
  • 41
    • 0029943633 scopus 로고    scopus 로고
    • An affinity of human replication protein A for ultraviolet-damaged DNA
    • Burns J.L., Guzder S.N., Sung P., Prakash S., Prakash L. An affinity of human replication protein A for ultraviolet-damaged DNA. J. Biol. Chem. 271:1996;11607-11610.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11607-11610
    • Burns, J.L.1    Guzder, S.N.2    Sung, P.3    Prakash, S.4    Prakash, L.5
  • 42
    • 0035854804 scopus 로고    scopus 로고
    • Reconstitution and molecular analysis of the hRad9-hHus1-hRad1 (9-1-1) DNA damage responsive checkpoint complex
    • Burtelow M.A., Roos-Mattjus P.M., Rauen M., Babendure J.R., Karnitz L.M. Reconstitution and molecular analysis of the hRad9-hHus1-hRad1 (9-1-1) DNA damage responsive checkpoint complex. J. Biol. Chem. 276:2001;25903-25909.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25903-25909
    • Burtelow, M.A.1    Roos-Mattjus, P.M.2    Rauen, M.3    Babendure, J.R.4    Karnitz, L.M.5
  • 43
    • 0036714327 scopus 로고    scopus 로고
    • Induction of DNA polymerase beta-dependent base excision repair in response to oxidative stress in vivo
    • Cabelof D.C., Raffoul J.J., Yanamadala S., Guo Z., Heydari A.R. Induction of DNA polymerase beta-dependent base excision repair in response to oxidative stress in vivo. Carcinogenesis. 23:2002;1419-1425.
    • (2002) Carcinogenesis , vol.23 , pp. 1419-1425
    • Cabelof, D.C.1    Raffoul, J.J.2    Yanamadala, S.3    Guo, Z.4    Heydari, A.R.5
  • 44
    • 0029957245 scopus 로고    scopus 로고
    • XRCC1 polypeptide interacts with DNA polymerase beta and possibly poly (ADP-ribose) polymerase, and DNA ligase III is a novel molecular 'nick-sensor' in vitro
    • Caldecott K.W., Aoufouchi S., Johnson P., Shall S. XRCC1 polypeptide interacts with DNA polymerase beta and possibly poly (ADP-ribose) polymerase, and DNA ligase III is a novel molecular 'nick-sensor' in vitro. Nucleic Acids Res. 24:1996;4387-4394.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4387-4394
    • Caldecott, K.W.1    Aoufouchi, S.2    Johnson, P.3    Shall, S.4
  • 46
    • 0025949662 scopus 로고
    • Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase
    • Chakravarti D., Ibeanu G.C., Tano K., Mitra S. Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase. J. Biol. Chem. 266:1991;15710-15715.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15710-15715
    • Chakravarti, D.1    Ibeanu, G.C.2    Tano, K.3    Mitra, S.4
  • 47
    • 0034142325 scopus 로고    scopus 로고
    • Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53
    • Chehab N.H., Malikzay A., Appel M., Halazonetis T.D. Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53. Genes Dev. 14:2000;278-288.
    • (2000) Genes Dev. , vol.14 , pp. 278-288
    • Chehab, N.H.1    Malikzay, A.2    Appel, M.3    Halazonetis, T.D.4
  • 49
    • 0027984433 scopus 로고
    • The Escherichia coli AlkB protein protects human cells against alkylation-induced toxicity
    • Chen B.J., Carroll P., Samson L. The Escherichia coli AlkB protein protects human cells against alkylation-induced toxicity. J. Bacteriol. 176:1994;6255-6261.
    • (1994) J. Bacteriol. , vol.176 , pp. 6255-6261
    • Chen, B.J.1    Carroll, P.2    Samson, L.3
  • 51
    • 0035844130 scopus 로고    scopus 로고
    • ATM-dependent phosphorylation of human Rad9 is required for ionizing radiation-induced checkpoint activation
    • Chen M.J., Lin Y.T., Lieberman H.B., Chen G., Lee E.Y. ATM-dependent phosphorylation of human Rad9 is required for ionizing radiation-induced checkpoint activation. J. Biol. Chem. 276:2001;16580-16586.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16580-16586
    • Chen, M.J.1    Lin, Y.T.2    Lieberman, H.B.3    Chen, G.4    Lee, E.Y.5
  • 53
    • 0034623934 scopus 로고    scopus 로고
    • Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles
    • Chi N.W., Lodish H.F. Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles. J. Biol. Chem. 275:2000;38437-38444.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38437-38444
    • Chi, N.W.1    Lodish, H.F.2
  • 54
    • 0034680776 scopus 로고    scopus 로고
    • Nuclear translocation of mismatch repair proteins MSH2 and MSH6 as a response of cells to alkylating agents
    • Christmann M., Kaina B. Nuclear translocation of mismatch repair proteins MSH2 and MSH6 as a response of cells to alkylating agents. J. Biol. Chem. 275:2000;36256-36262.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36256-36262
    • Christmann, M.1    Kaina, B.2
  • 55
    • 0035313980 scopus 로고    scopus 로고
    • Acquired resistance of melanoma cells to the antineoplastic agent fotemustine is caused by reactivation of the DNA repair gene MGMT
    • Christmann M., Pick M., Lage H., Schadendorf D., Kaina B. Acquired resistance of melanoma cells to the antineoplastic agent fotemustine is caused by reactivation of the DNA repair gene MGMT. Int. J. Cancer. 92:2001;123-129.
    • (2001) Int. J. Cancer , vol.92 , pp. 123-129
    • Christmann, M.1    Pick, M.2    Lage, H.3    Schadendorf, D.4    Kaina, B.5
  • 56
    • 0036567603 scopus 로고    scopus 로고
    • Phosphorylation of mismatch repair proteins MSH2 and MSH6 affecting MutSα mismatch-binding activity
    • Christmann M., Tomicic M.T., Kaina B. Phosphorylation of mismatch repair proteins MSH2 and MSH6 affecting MutSα mismatch-binding activity. Nucleic Acids Res. 30:2002;1959-1966.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1959-1966
    • Christmann, M.1    Tomicic, M.T.2    Kaina, B.3
  • 57
    • 0002362694 scopus 로고
    • Dwarfism with retinal atrophy and deafness
    • Cockayne E.A. Dwarfism with retinal atrophy and deafness. Arch. Dis. Child. 11:1936;1-8.
    • (1936) Arch. Dis. Child. , vol.11 , pp. 1-8
    • Cockayne, E.A.1
  • 59
    • 0035951396 scopus 로고    scopus 로고
    • Branch migration and Holliday junction resolution catalyzed by activities from mammalian cells
    • Constantinou A., Davies A.A., West S.C. Branch migration and Holliday junction resolution catalyzed by activities from mammalian cells. Cell. 104:2001;259-268.
    • (2001) Cell , vol.104 , pp. 259-268
    • Constantinou, A.1    Davies, A.A.2    West, S.C.3
  • 61
    • 0035695023 scopus 로고    scopus 로고
    • Recombination at double-strand breaks and DNA ends: Conserved mechanisms from phage to humans
    • Cromie G.A., Connelly J.C., Leach D.R. Recombination at double-strand breaks and DNA ends: conserved mechanisms from phage to humans. Mol. Cell. 8:2001;1163-1174.
    • (2001) Mol. Cell , vol.8 , pp. 1163-1174
    • Cromie, G.A.1    Connelly, J.C.2    Leach, D.R.3
  • 62
    • 0032974109 scopus 로고    scopus 로고
    • Cytoplasmic localization of human cdc25C during interphase requires an intact 14-3-3 binding site
    • Dalal S.N., Schweitzer C.M., Gan J., DeCaprio J.A. Cytoplasmic localization of human cdc25C during interphase requires an intact 14-3-3 binding site. Mol. Cell. Biol. 19:1999;4465-4479.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4465-4479
    • Dalal, S.N.1    Schweitzer, C.M.2    Gan, J.3    DeCaprio, J.A.4
  • 65
    • 0032509471 scopus 로고    scopus 로고
    • Repair pathways for processing of 8-oxoguanine in DNA by mammalian cell extracts
    • Dianov G., Bischoff C., Piotrowski J., Bohr V.A. Repair pathways for processing of 8-oxoguanine in DNA by mammalian cell extracts. J. Biol. Chem. 273:1998;33811-33816.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33811-33816
    • Dianov, G.1    Bischoff, C.2    Piotrowski, J.3    Bohr, V.A.4
  • 66
    • 0026589375 scopus 로고
    • Generation of single-nucleotide repair patches following excision of uracil residues from DNA
    • Dianov G., Price A., Lindahl T. Generation of single-nucleotide repair patches following excision of uracil residues from DNA. Mol. Cell. Biol. 12:1992;1605-1612.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1605-1612
    • Dianov, G.1    Price, A.2    Lindahl, T.3
  • 67
    • 0030862095 scopus 로고    scopus 로고
    • Reduced RNA polymerase II transcription in extracts of cockayne syndrome and xeroderma pigmentosum/Cockayne syndrome cells
    • Dianov G.L., Houle J.F., Iyer N., Bohr V.A., Friedberg E.C. Reduced RNA polymerase II transcription in extracts of cockayne syndrome and xeroderma pigmentosum/Cockayne syndrome cells. Nucleic Acids Res. 25:1997;3636-3642.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3636-3642
    • Dianov, G.L.1    Houle, J.F.2    Iyer, N.3    Bohr, V.A.4    Friedberg, E.C.5
  • 68
    • 0033553510 scopus 로고    scopus 로고
    • Role of DNA polymerase beta in the excision step of long patch mammalian base excision repair
    • Dianov G.L., Prasad R., Wilson S.H., Bohr V.A. Role of DNA polymerase beta in the excision step of long patch mammalian base excision repair. J. Biol. Chem. 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
  • 69
    • 0031900748 scopus 로고    scopus 로고
    • Correlation between cellular radiosensitivity and non-repaired double-strand breaks studied in nine mammalian cell lines
    • Dikomey E., Dahm Daphi J., Brammer I., Martensen R., Kaina B. Correlation between cellular radiosensitivity and non-repaired double-strand breaks studied in nine mammalian cell lines. Int. J. Radiat. Biol. 73:1998;269-278.
    • (1998) Int. J. Radiat. Biol. , vol.73 , pp. 269-278
    • Dikomey, E.1    Dahm Daphi, J.2    Brammer, I.3    Martensen, R.4    Kaina, B.5
  • 70
    • 0034664066 scopus 로고    scopus 로고
    • Defective processing of methylated single-stranded DNA by E. coli AlkB mutants
    • Dinglay S., Trewick S.C., Lindahl T., Sedgwick B. Defective processing of methylated single-stranded DNA by E. coli AlkB mutants. Genes Dev. 14:2000;2097-2105.
    • (2000) Genes Dev. , vol.14 , pp. 2097-2105
    • Dinglay, S.1    Trewick, S.C.2    Lindahl, T.3    Sedgwick, B.4
  • 75
    • 0037131257 scopus 로고    scopus 로고
    • The Rad51-dependent pairing of long DNA substrates is stabilized by replication protein A
    • Eggler A.L., Inman R.B., Cox M.M. The Rad51-dependent pairing of long DNA substrates is stabilized by replication protein A. J. Biol. Chem. 277:2002;39280-39288.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39280-39288
    • Eggler, A.L.1    Inman, R.B.2    Cox, M.M.3
  • 77
    • 0035929237 scopus 로고    scopus 로고
    • Opening of the clamp: An intimate view of an ATP-driven biological machine
    • Ellison V., Stillman B. Opening of the clamp: an intimate view of an ATP-driven biological machine. Cell. 106:2001;655-660.
    • (2001) Cell , vol.106 , pp. 655-660
    • Ellison, V.1    Stillman, B.2
  • 78
    • 0031013308 scopus 로고    scopus 로고
    • Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein
    • Evans E., Fellows J., Coffer A., Wood R.D. Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein. EMBO J. 16:1997a;625-638.
    • (1997) EMBO J. , vol.16 , pp. 625-638
    • Evans, E.1    Fellows, J.2    Coffer, A.3    Wood, R.D.4
  • 79
    • 0030732132 scopus 로고    scopus 로고
    • Mechanism of open complex and dual incision formation by human nucleotide excision repair factors
    • Evans E., Moggs J.G., Hwang J.R., Egly J.M., Wood R.D. Mechanism of open complex and dual incision formation by human nucleotide excision repair factors. EMBO J. 16:1997b;6559-6573.
    • (1997) EMBO J. , vol.16 , pp. 6559-6573
    • Evans, E.1    Moggs, J.G.2    Hwang, J.R.3    Egly, J.M.4    Wood, R.D.5
  • 80
    • 0028297860 scopus 로고
    • Gene-specific DNA repair of UV-induced cyclobutane pyrimidine dimers in some cancer-prone and premature-aging human syndromes
    • Evans M.K., Bohr V.A. Gene-specific DNA repair of UV-induced cyclobutane pyrimidine dimers in some cancer-prone and premature-aging human syndromes. Mutat. Res. 314:1994;221-231.
    • (1994) Mutat. Res. , vol.314 , pp. 221-231
    • Evans, M.K.1    Bohr, V.A.2
  • 81
    • 0037068433 scopus 로고    scopus 로고
    • AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
    • Falnes P.O., Johansen R.F., Seeberg E. AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli. Nature. 419:2002;178-182.
    • (2002) Nature , vol.419 , pp. 178-182
    • Falnes, P.O.1    Johansen, R.F.2    Seeberg, E.3
  • 82
    • 0027269844 scopus 로고
    • Human strand-specific mismatch repair occurs by a bidirectional mechanism similar to that of the bacterial reaction
    • Fang W.H., Modrich P. Human strand-specific mismatch repair occurs by a bidirectional mechanism similar to that of the bacterial reaction. J. Biol. Chem. 268:1993;11838-11844.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11838-11844
    • Fang, W.H.1    Modrich, P.2
  • 83
    • 0037020269 scopus 로고    scopus 로고
    • Human DNA polymerase kappa bypasses and extends beyond thymine glycols during translesion synthesis in vitro, preferentially incorporating correct nucleotides
    • Fischhaber P.L., Gerlach V.L., Feaver W.J., Hatahet Z., Wallace S.S., Friedberg E.C. Human DNA polymerase kappa bypasses and extends beyond thymine glycols during translesion synthesis in vitro, preferentially incorporating correct nucleotides. J. Biol. Chem. 277:2002;37604-37611.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37604-37611
    • Fischhaber, P.L.1    Gerlach, V.L.2    Feaver, W.J.3    Hatahet, Z.4    Wallace, S.S.5    Friedberg, E.C.6
  • 84
    • 0032527704 scopus 로고    scopus 로고
    • Mismatch repair, molecular switches, and signal transduction
    • Fishel R. Mismatch repair, molecular switches, and signal transduction. Genes Dev. 12:1998;2096-2101.
    • (1998) Genes Dev. , vol.12 , pp. 2096-2101
    • Fishel, R.1
  • 85
    • 0027742295 scopus 로고
    • The human mutator gene homolog MSH2 and its association with hereditary nonpolyposis colon cancer
    • Fishel R., Lescoe M.K., Rao M.R., Copeland N.G., Jenkins N.A., Garber J., Kane M., Kolodner R. The human mutator gene homolog MSH2 and its association with hereditary nonpolyposis colon cancer. Cell. 75:1993;1027-1038.
    • (1993) Cell , vol.75 , pp. 1027-1038
    • Fishel, R.1    Lescoe, M.K.2    Rao, M.R.3    Copeland, N.G.4    Jenkins, N.A.5    Garber, J.6    Kane, M.7    Kolodner, R.8
  • 86
    • 0029029741 scopus 로고
    • Li-Fraumeni syndrome fibroblasts homozygous for p53 mutations are deficient in global DNA repair but exhibit normal transcription-coupled repair and enhanced UV resistance
    • Ford J.M., Hanawalt P.C. Li-Fraumeni syndrome fibroblasts homozygous for p53 mutations are deficient in global DNA repair but exhibit normal transcription-coupled repair and enhanced UV resistance. Proc. Natl. Acad. Sci. U.S.A. 92:1995;8876-8880.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8876-8880
    • Ford, J.M.1    Hanawalt, P.C.2
  • 87
    • 0030853074 scopus 로고    scopus 로고
    • Expression of wild-type p53 is required for efficient global genomic nucleotide excision repair in UV-irradiated human fibroblasts
    • Ford J.M., Hanawalt P.C. Expression of wild-type p53 is required for efficient global genomic nucleotide excision repair in UV-irradiated human fibroblasts. J. Biol. Chem. 272:1997;28073-28080.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28073-28080
    • Ford, J.M.1    Hanawalt, P.C.2
  • 88
    • 0035355203 scopus 로고    scopus 로고
    • Altered nucleotide misinsertion fidelity associated with poliota-dependent replication at the end of a DNA template
    • Frank E.G., Tissier A., McDonald J.P., Rapic-Otrin V., Zeng X., Gearhart P.J., Woodgate R. Altered nucleotide misinsertion fidelity associated with poliota-dependent replication at the end of a DNA template. EMBO J. 20:2001;2914-2922.
    • (2001) EMBO J. , vol.20 , pp. 2914-2922
    • Frank, E.G.1    Tissier, A.2    McDonald, J.P.3    Rapic-Otrin, V.4    Zeng, X.5    Gearhart, P.J.6    Woodgate, R.7
  • 89
    • 0035495386 scopus 로고    scopus 로고
    • How nucleotide excision repair protects against cancer
    • Friedberg E.C. How nucleotide excision repair protects against cancer. Nat. Rev. Cancer. 1:2001;22-33.
    • (2001) Nat. Rev. Cancer , vol.1 , pp. 22-33
    • Friedberg, E.C.1
  • 90
    • 85015066476 scopus 로고    scopus 로고
    • DNA damage and repair
    • Friedberg E.C. DNA damage and repair. Nature. 421:2003;436-440.
    • (2003) Nature , vol.421 , pp. 436-440
    • Friedberg, E.C.1
  • 91
    • 0025767132 scopus 로고
    • 6-methylguanine- DNA methyltransferase in mammalian cells by DNA-damaging treatments
    • 6-methylguanine-DNA methyltransferase in mammalian cells by DNA-damaging treatments. Mol. Cell. Biol. 11:1991;4660-4668.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4660-4668
    • Fritz, G.1    Tano, K.2    Mitra, S.3    Kaina, B.4
  • 93
    • 0028566359 scopus 로고
    • Genomic structure and chromosome location of the human mutT homologue gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to C:G transversion
    • Furuichi M., Yoshida M.C., Oda H., Tajiri T., Nakabeppu Y., Tsuzuki T., Sekiguchi M. Genomic structure and chromosome location of the human mutT homologue gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to C:G transversion. Genomics. 24:1994;485-490.
    • (1994) Genomics , vol.24 , pp. 485-490
    • Furuichi, M.1    Yoshida, M.C.2    Oda, H.3    Tajiri, T.4    Nakabeppu, Y.5    Tsuzuki, T.6    Sekiguchi, M.7
  • 97
    • 0037066720 scopus 로고    scopus 로고
    • Human exonuclease I is required for 5′ and 3′ mismatch repair
    • Genschel J., Bazemore L.R., Modrich P. Human exonuclease I is required for 5′ and 3′ mismatch repair. J. Biol. Chem. 277:2002;13302-13311.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13302-13311
    • Genschel, J.1    Bazemore, L.R.2    Modrich, P.3
  • 98
    • 0032584384 scopus 로고    scopus 로고
    • Isolation of MutSbeta from human cells and comparison of the mismatch repair specificities of MutSbeta and MutSalpha
    • Genschel J., Littman S.J., Drummond J.T., Modrich P. Isolation of MutSbeta from human cells and comparison of the mismatch repair specificities of MutSbeta and MutSalpha. J. Biol. Chem. 273:1998;19895-19901.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19895-19901
    • Genschel, J.1    Littman, S.J.2    Drummond, J.T.3    Modrich, P.4
  • 100
    • 0035808417 scopus 로고    scopus 로고
    • Purification and characterization of pol kappa, a DNA polymerase encoded by the human DINB1 gene
    • Gerlach V.L., Feaver W.J., Fischhaber P.L., Friedberg E.C. Purification and characterization of pol kappa, a DNA polymerase encoded by the human DINB1 gene. J. Biol. Chem. 276:2001;92-98.
    • (2001) J. Biol. Chem. , vol.276 , pp. 92-98
    • Gerlach, V.L.1    Feaver, W.J.2    Fischhaber, P.L.3    Friedberg, E.C.4
  • 101
    • 0032499748 scopus 로고    scopus 로고
    • A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase zeta
    • Gibbs P.E., McGregor W.G., Maher V.M., Nisson P., Lawrence C.W. A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase zeta. Proc. Natl. Acad. Sci. U.S.A. 95:1998;6876-6880.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6876-6880
    • Gibbs, P.E.1    McGregor, W.G.2    Maher, V.M.3    Nisson, P.4    Lawrence, C.W.5
  • 102
    • 0032403121 scopus 로고    scopus 로고
    • Interaction of human rad51 recombination protein with single-stranded DNA binding protein, RPA
    • Golub E.I., Gupta R.C., Haaf T., Wold M.S., Radding C.M. Interaction of human rad51 recombination protein with single-stranded DNA binding protein, RPA. Nucleic Acids Res. 26:1998;5388-5393.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5388-5393
    • Golub, E.I.1    Gupta, R.C.2    Haaf, T.3    Wold, M.S.4    Radding, C.M.5
  • 103
    • 0027397867 scopus 로고
    • The DNA-dependent protein kinase: Requirement for DNA ends and association with Ku antigen
    • Gottlieb T.M., Jackson S.P. The DNA-dependent protein kinase: requirement for DNA ends and association with Ku antigen. Cell. 72:1993;131-142.
    • (1993) Cell , vol.72 , pp. 131-142
    • Gottlieb, T.M.1    Jackson, S.P.2
  • 104
    • 0031456973 scopus 로고    scopus 로고
    • The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch
    • Gradia S., Acharya S., Fishel R. The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch. Cell. 91:1997;995-1005.
    • (1997) Cell , vol.91 , pp. 995-1005
    • Gradia, S.1    Acharya, S.2    Fishel, R.3
  • 105
    • 0034635517 scopus 로고    scopus 로고
    • The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch
    • Gradia S., Acharya S., Fishel R. The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch. J. Biol. Chem. 275:2000;3922-3930.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3922-3930
    • Gradia, S.1    Acharya, S.2    Fishel, R.3
  • 108
    • 0029803785 scopus 로고    scopus 로고
    • Induction of the alkyltransferase (MGMT) gene by DNA damaging agents and the glucocorticoid dexamethasone and comparison with the response of base excision repair genes
    • Grombacher T., Mitra S., Kaina B. Induction of the alkyltransferase (MGMT) gene by DNA damaging agents and the glucocorticoid dexamethasone and comparison with the response of base excision repair genes. Carcinogenesis. 17:1996;2329-2336.
    • (1996) Carcinogenesis , vol.17 , pp. 2329-2336
    • Grombacher, T.1    Mitra, S.2    Kaina, B.3
  • 109
    • 0034312277 scopus 로고    scopus 로고
    • Requirement for Atr in phosphorylation of Chk1 and cell cycle regulation in response to DNA replication blocks and UV-damaged DNA in Xenopus egg extracts
    • Guo Z., Kumagai A., Wang S.X., Dunphy W.G. Requirement for Atr in phosphorylation of Chk1 and cell cycle regulation in response to DNA replication blocks and UV-damaged DNA in Xenopus egg extracts. Genes Dev. 14:2000;2745-2756.
    • (2000) Genes Dev. , vol.14 , pp. 2745-2756
    • Guo, Z.1    Kumagai, A.2    Wang, S.X.3    Dunphy, W.G.4
  • 110
    • 0032544088 scopus 로고    scopus 로고
    • Polarity of DNA strand exchange promoted by recombination proteins of the RecA family
    • Gupta R.C., Golub E.I., Wold M.S., Radding C.M. Polarity of DNA strand exchange promoted by recombination proteins of the RecA family. Proc. Natl. Acad. Sci. U.S.A. 95:1998;9843-9848.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 9843-9848
    • Gupta, R.C.1    Golub, E.I.2    Wold, M.S.3    Radding, C.M.4
  • 111
    • 0034195218 scopus 로고    scopus 로고
    • Partners and pathways repairing a double-strand break
    • Haber J.E. Partners and pathways repairing a double-strand break. Trends Genet. 16:2000;259-264.
    • (2000) Trends Genet. , vol.16 , pp. 259-264
    • Haber, J.E.1
  • 112
    • 0028075835 scopus 로고
    • A conserved 5′ to 3′ exonuclease activity in the yeast and human nucleotide excision repair proteins RAD2 and XPG
    • Habraken Y., Sung P., Prakash L., Prakash S. A conserved 5′ to 3′ exonuclease activity in the yeast and human nucleotide excision repair proteins RAD2 and XPG. J. Biol. Chem. 269:1994;31342-31345.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31342-31345
    • Habraken, Y.1    Sung, P.2    Prakash, L.3    Prakash, S.4
  • 113
    • 0034695658 scopus 로고    scopus 로고
    • Activation of DNA-dependent protein kinase by single-stranded DNA ends
    • Hammarsten O., DeFazio L.G., Chu G. Activation of DNA-dependent protein kinase by single-stranded DNA ends. J. Biol. Chem. 275:2000;1541-1550.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1541-1550
    • Hammarsten, O.1    DeFazio, L.G.2    Chu, G.3
  • 114
    • 0035946009 scopus 로고    scopus 로고
    • Controlling the efficiency of excision repair
    • Hanawalt P.C. Controlling the efficiency of excision repair. Mutat. Res. 485:2001;3-13.
    • (2001) Mutat. Res. , vol.485 , pp. 3-13
    • Hanawalt, P.C.1
  • 115
    • 0037115936 scopus 로고    scopus 로고
    • Subpathways of nucleotide excision repair and their regulation
    • Hanawalt P.C. Subpathways of nucleotide excision repair and their regulation. Oncogene. 21:2002;8949-8956.
    • (2002) Oncogene , vol.21 , pp. 8949-8956
    • Hanawalt, P.C.1
  • 116
    • 0033609947 scopus 로고    scopus 로고
    • Human transcription release factor 2 dissociates RNA polymerases I and II stalled at a cyclobutane thymine dimer
    • Hara R., Selby C.P., Liu M., Price D.H., Sancar A. Human transcription release factor 2 dissociates RNA polymerases I and II stalled at a cyclobutane thymine dimer. J. Biol. Chem. 274:1999;24779-24786.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24779-24786
    • Hara, R.1    Selby, C.P.2    Liu, M.3    Price, D.H.4    Sancar, A.5
  • 117
    • 0037058976 scopus 로고    scopus 로고
    • Role of human DNA polymerase kappa as an extender in translesion synthesis
    • Haracska L., Prakash L., Prakash S. Role of human DNA polymerase kappa as an extender in translesion synthesis. Proc. Natl. Acad. Sci. U.S.A. 99:2002;16000-16005.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16000-16005
    • Haracska, L.1    Prakash, L.2    Prakash, S.3
  • 118
    • 0034425754 scopus 로고    scopus 로고
    • Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase eta
    • Haracska L., Yu S.L., Johnson R.E., Prakash L., Prakash S. Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase eta. Nat. Genet. 25:2000;458-461.
    • (2000) Nat. Genet. , vol.25 , pp. 458-461
    • Haracska, L.1    Yu, S.L.2    Johnson, R.E.3    Prakash, L.4    Prakash, S.5
  • 120
    • 0036724986 scopus 로고    scopus 로고
    • BRCA1 induces DNA damage recognition factors and enhances nucleotide excision repair
    • Hartman A.R., Ford J.M. BRCA1 induces DNA damage recognition factors and enhances nucleotide excision repair. Nat. Genet. 32:2002;180-184.
    • (2002) Nat. Genet. , vol.32 , pp. 180-184
    • Hartman, A.R.1    Ford, J.M.2
  • 121
    • 0033602148 scopus 로고    scopus 로고
    • Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors
    • Haushalter K.A., Todd Stukenberg M.W., Kirschner M.W., Verdine G.L. Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors. Curr. Biol. 9:1999;174-185.
    • (1999) Curr. Biol. , vol.9 , pp. 174-185
    • Haushalter, K.A.1    Todd Stukenberg, M.W.2    Kirschner, M.W.3    Verdine, G.L.4
  • 123
    • 0037162995 scopus 로고    scopus 로고
    • Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions
    • Hazra T.K., Kow Y.W., Hatahet Z., Imhoff B., Boldogh I., Mokkapati S.K., Mitra S., Izumi T. Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions. J. Biol. Chem. 277:2002b;30417-30420.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30417-30420
    • Hazra, T.K.1    Kow, Y.W.2    Hatahet, Z.3    Imhoff, B.4    Boldogh, I.5    Mokkapati, S.K.6    Mitra, S.7    Izumi, T.8
  • 124
    • 0028929611 scopus 로고
    • RPA involvement in the damage-recognition and incision steps of nucleotide excision repair
    • He Z., Henricksen L.A., Wold M.S., Ingles C.J. RPA involvement in the damage-recognition and incision steps of nucleotide excision repair. Nature. 374:1995;566-569.
    • (1995) Nature , vol.374 , pp. 566-569
    • He, Z.1    Henricksen, L.A.2    Wold, M.S.3    Ingles, C.J.4
  • 125
    • 0031792779 scopus 로고    scopus 로고
    • Identification and characterization of a family of mammalian methyl-CpG binding proteins
    • Hendrich B., Bird A. Identification and characterization of a family of mammalian methyl-CpG binding proteins. Mol. Cell. Biol. 18:1998;6538-6547.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6538-6547
    • Hendrich, B.1    Bird, A.2
  • 126
    • 0033575886 scopus 로고    scopus 로고
    • The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites
    • Hendrich B., Hardeland U., Ng H.H., Jiricny J., Bird A. The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites. Nature. 401:1999;301-304.
    • (1999) Nature , vol.401 , pp. 301-304
    • Hendrich, B.1    Hardeland, U.2    Ng, H.H.3    Jiricny, J.4    Bird, A.5
  • 127
  • 128
    • 0037188408 scopus 로고    scopus 로고
    • The XPC-HR23B complex displays high affinity and specificity for damaged DNA in a true-equilibrium fluorescence assay
    • Hey T., Lipps G., Sugasawa K., Iwai S., Hanaoka F., Krauss G. The XPC-HR23B complex displays high affinity and specificity for damaged DNA in a true-equilibrium fluorescence assay. Biochemistry. 41:2002;6583-6587.
    • (2002) Biochemistry , vol.41 , pp. 6583-6587
    • Hey, T.1    Lipps, G.2    Sugasawa, K.3    Iwai, S.4    Hanaoka, F.5    Krauss, G.6
  • 129
    • 0030890419 scopus 로고    scopus 로고
    • Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III
    • Hilbert T.P., Chaung W., Boorstein R.J., Cunningham R.P., Teebor G.W. Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III. J. Biol. Chem. 272:1997;6733-6740.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6733-6740
    • Hilbert, T.P.1    Chaung, W.2    Boorstein, R.J.3    Cunningham, R.P.4    Teebor, G.W.5
  • 131
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • Hoeijmakers J.H. Genome maintenance mechanisms for preventing cancer. Nature. 411:2001;366-374.
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.1
  • 132
    • 84959678845 scopus 로고
    • A mechanism for gene conversion in fungi
    • Holliday R. A mechanism for gene conversion in fungi. Genet. Res. 5:1964;282-304.
    • (1964) Genet. Res. , vol.5 , pp. 282-304
    • Holliday, R.1
  • 134
    • 0000516293 scopus 로고    scopus 로고
    • Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair
    • Hwang B.J., Ford J.M., Hanawalt P.C., Chu G. Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair. Proc. Natl. Acad. Sci. U.S.A. 96:1999;424-428.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 424-428
    • Hwang, B.J.1    Ford, J.M.2    Hanawalt, P.C.3    Chu, G.4
  • 135
    • 0032079736 scopus 로고    scopus 로고
    • HMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha
    • Iaccarino I., Marra G., Palombo F., Jiricny J. hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha. EMBO J. 17:1998;2677-2686.
    • (1998) EMBO J. , vol.17 , pp. 2677-2686
    • Iaccarino, I.1    Marra, G.2    Palombo, F.3    Jiricny, J.4
  • 136
    • 0028988703 scopus 로고
    • Uvs syndrome, a new general category of photosensitive disorder with defective DNA repair, is distinct from xeroderma pigmentosum variant and rodent complementation group I
    • Itoh T., Fujiwara Y., Ono T., Yamaizumi M. Uvs syndrome, a new general category of photosensitive disorder with defective DNA repair, is distinct from xeroderma pigmentosum variant and rodent complementation group I. Am. J. Hum. Genet. 56:1995;1267-1276.
    • (1995) Am. J. Hum. Genet. , vol.56 , pp. 1267-1276
    • Itoh, T.1    Fujiwara, Y.2    Ono, T.3    Yamaizumi, M.4
  • 137
    • 0030025947 scopus 로고    scopus 로고
    • Interactions involving the human RNA polymerase II transcription/ nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein
    • Iyer N., Reagan M.S., Wu K.J., Canagarajah B., Friedberg E.C. Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein. Biochemistry. 35:1996;2157-2167.
    • (1996) Biochemistry , vol.35 , pp. 2157-2167
    • Iyer, N.1    Reagan, M.S.2    Wu, K.J.3    Canagarajah, B.4    Friedberg, E.C.5
  • 139
    • 0035379611 scopus 로고    scopus 로고
    • The emerging genetic and molecular basis of Fanconi anaemia
    • Joenje H., Patel K.J. The emerging genetic and molecular basis of Fanconi anaemia. Nat. Rev. Genet. 2:2001;446-457.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 446-457
    • Joenje, H.1    Patel, K.J.2
  • 140
    • 0033135769 scopus 로고    scopus 로고
    • A human poly(ADP-ribose) polymerase gene family (ADPRTL): CDNA cloning of two novel poly(ADP-ribose) polymerase homologues
    • Johansson M. A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues. Genomics. 57:1999;442-445.
    • (1999) Genomics , vol.57 , pp. 442-445
    • Johansson, M.1
  • 141
    • 0034600975 scopus 로고    scopus 로고
    • Sister chromatid gene conversion is a prominent double-strand break repair pathway in mammalian cells
    • Johnson R.D., Jasin M. Sister chromatid gene conversion is a prominent double-strand break repair pathway in mammalian cells. EMBO J. 19:2000;3398-3407.
    • (2000) EMBO J. , vol.19 , pp. 3398-3407
    • Johnson, R.D.1    Jasin, M.2
  • 142
    • 0035034974 scopus 로고    scopus 로고
    • Role of DNA polymerase zeta in the bypass of a (6-4) TT photoproduct
    • Johnson R.E., Haracska L., Prakash S., Prakash L. Role of DNA polymerase zeta in the bypass of a (6-4) TT photoproduct. Mol. Cell. Biol. 21:2001;3558-3563.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3558-3563
    • Johnson, R.E.1    Haracska, L.2    Prakash, S.3    Prakash, L.4
  • 143
    • 0033538470 scopus 로고    scopus 로고
    • HRAD30 mutations in the variant form of xeroderma pigmentosum
    • Johnson R.E., Kondratick C.M., Prakash S., Prakash L. hRAD30 mutations in the variant form of xeroderma pigmentosum. Science. 285:1999;263-265.
    • (1999) Science , vol.285 , pp. 263-265
    • Johnson, R.E.1    Kondratick, C.M.2    Prakash, S.3    Prakash, L.4
  • 146
    • 0027483739 scopus 로고
    • Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA
    • Jones C.J., Wood R.D. Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA. Biochemistry. 32:1993;12096-12104.
    • (1993) Biochemistry , vol.32 , pp. 12096-12104
    • Jones, C.J.1    Wood, R.D.2
  • 148
    • 0035041934 scopus 로고    scopus 로고
    • Fission yeast Rad17 associates with chromatin in response to aberrant genomic structures
    • Kai M., Tanaka H., Wang T.S. Fission yeast Rad17 associates with chromatin in response to aberrant genomic structures. Mol. Cell. Biol. 21:2001;3289-3301.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3289-3301
    • Kai, M.1    Tanaka, H.2    Wang, T.S.3
  • 149
    • 0037224965 scopus 로고    scopus 로고
    • Checkpoint activation regulates mutagenic translesion synthesis
    • Kai M., Wang T.S. Checkpoint activation regulates mutagenic translesion synthesis. Genes Dev. 17:2003;64-76.
    • (2003) Genes Dev. , vol.17 , pp. 64-76
    • Kai, M.1    Wang, T.S.2
  • 150
    • 0025941670 scopus 로고
    • 6-methylguanine-DNA methyltransferase (MGMT) cDNA in Chinese hamster cells: The role of MGMT in protection against the genotoxic effects of alkylating agents
    • 6-methylguanine-DNA methyltransferase (MGMT) cDNA in Chinese hamster cells: the role of MGMT in protection against the genotoxic effects of alkylating agents. Carcinogenesis. 12:1991;1857-1867.
    • (1991) Carcinogenesis , vol.12 , pp. 1857-1867
    • Kaina, B.1    Fritz, G.2    Mitra, S.3    Coquerelle, T.4
  • 151
    • 0021333746 scopus 로고
    • Poly (ADP-ribose) synthetase. Separation and identification of three proteolytic fragments as the substrate-binding domain, the DNA-binding domain, and the automodification domain
    • Kameshita I., Matsuda Z., Taniguchi T., Shizuta Y. Poly (ADP-ribose) synthetase. Separation and identification of three proteolytic fragments as the substrate-binding domain, the DNA-binding domain, and the automodification domain. J. Biol. Chem. 259:1984;4770-4776.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4770-4776
    • Kameshita, I.1    Matsuda, Z.2    Taniguchi, T.3    Shizuta, Y.4
  • 152
  • 153
    • 0032443366 scopus 로고    scopus 로고
    • Determination of cell fate by c-Abl activation in the response to DNA damage
    • Kharbanda S., Yuan Z.M., Weichselbaum R., Kufe D. Determination of cell fate by c-Abl activation in the response to DNA damage. Oncogene. 17:1998;3309-3318.
    • (1998) Oncogene , vol.17 , pp. 3309-3318
    • Kharbanda, S.1    Yuan, Z.M.2    Weichselbaum, R.3    Kufe, D.4
  • 155
    • 0033621392 scopus 로고    scopus 로고
    • Substrate specificities and identification of putative substrates of ATM kinase family members
    • Kim S.T., Lim D.S., Canman C.E., Kastan M.B. Substrate specificities and identification of putative substrates of ATM kinase family members. J. Biol. Chem. 274:1999;37538-37543.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37538-37543
    • Kim, S.T.1    Lim, D.S.2    Canman, C.E.3    Kastan, M.B.4
  • 157
    • 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
  • 159
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase beta and the XRCC1 protein
    • Kubota Y., Nash R.A., Klungland A., Schar P., Barnes D.E., Lindahl T. Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta 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
  • 160
    • 0037415391 scopus 로고    scopus 로고
    • Functions of human DNA polymerases eta, kappa and iota suggested by their properties, including fidelity with undamaged DNA templates
    • Kunkel T.A., Pavlov Y.I., Bebenek K. Functions of human DNA polymerases eta, kappa and iota suggested by their properties, including fidelity with undamaged DNA templates. DNA Repair (Amst.). 2:2003;135-149.
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 135-149
    • Kunkel, T.A.1    Pavlov, Y.I.2    Bebenek, K.3
  • 161
    • 0037076519 scopus 로고    scopus 로고
    • Translesion synthesis by human DNA polymerase eta across thymine glycol lesions
    • Kusumoto R., Masutani C., Iwai S., Hanaoka F. Translesion synthesis by human DNA polymerase eta across thymine glycol lesions. Biochemistry. 41:2002;6090-6099.
    • (2002) Biochemistry , vol.41 , pp. 6090-6099
    • Kusumoto, R.1    Masutani, C.2    Iwai, S.3    Hanaoka, F.4
  • 163
    • 0034694959 scopus 로고    scopus 로고
    • Primary mouse fibroblasts deficient for c-Fos, p53 or for both proteins are hypersensitive to UV light and alkylating agent-induced chromosomal breakage and apoptosis
    • Lackinger D., Kaina B. Primary mouse fibroblasts deficient for c-Fos, p53 or for both proteins are hypersensitive to UV light and alkylating agent-induced chromosomal breakage and apoptosis. Mutat. Res. 457:2000;113-123.
    • (2000) Mutat. Res. , vol.457 , pp. 113-123
    • Lackinger, D.1    Kaina, B.2
  • 165
    • 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., Wilson S.H. Photoaffinity labeling of mouse fibroblast enzymes by a base excision
    • (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
  • 166
    • 0034646516 scopus 로고    scopus 로고
    • Transcription-coupled repair of 8-oxoguanine: Requirement for XPG, TFIIH, CSB and implications for Cockayne syndrome
    • Le Page F., Kwoh E.E., Avrutskaya A., Gentil A., Leadon S.A., Sarasin A., Cooper P.K. Transcription-coupled repair of 8-oxoguanine: requirement for XPG, TFIIH, CSB and implications for Cockayne syndrome. Cell. 101:2000;159-171.
    • (2000) Cell , vol.101 , pp. 159-171
    • Le Page, F.1    Kwoh, E.E.2    Avrutskaya, A.3    Gentil, A.4    Leadon, S.A.5    Sarasin, A.6    Cooper, P.K.7
  • 168
    • 0031939411 scopus 로고    scopus 로고
    • The XRCC4 gene product is a target for and interacts with the DNA-dependent protein kinase
    • Leber R., Wise T.W., Mizuta R., Meek K. The XRCC4 gene product is a target for and interacts with the DNA-dependent protein kinase. J. Biol. Chem. 273:1998;1794-1801.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1794-1801
    • Leber, R.1    Wise, T.W.2    Mizuta, R.3    Meek, K.4
  • 169
    • 0037224429 scopus 로고    scopus 로고
    • Requirement for XRCC4 and DNA ligase IV in alignment-based gap filling for nonhomologous DNA end joining in vitro
    • Lee J.W., Yannone S.M., Chen D.J., Povirk L.F. Requirement for XRCC4 and DNA ligase IV in alignment-based gap filling for nonhomologous DNA end joining in vitro. Cancer Res. 63:2003;22-24.
    • (2003) Cancer Res. , vol.63 , pp. 22-24
    • Lee, J.W.1    Yannone, S.M.2    Chen, D.J.3    Povirk, L.F.4
  • 170
    • 0037202616 scopus 로고    scopus 로고
    • Replication of damaged DNA in mammalian cells: New solutions to an old problem
    • Lehmann A.R. Replication of damaged DNA in mammalian cells: new solutions to an old problem. Mutat. Res. 509:2002;23-34.
    • (2002) Mutat. Res. , vol.509 , pp. 23-34
    • Lehmann, A.R.1
  • 171
    • 0028941627 scopus 로고
    • Restoration of mismatch repair to nuclear extracts of H6 colorectal tumor cells by a heterodimer of human MutL homologs
    • Li G.M., Modrich P. Restoration of mismatch repair to nuclear extracts of H6 colorectal tumor cells by a heterodimer of human MutL homologs. Proc. Natl. Acad. Sci. U.S.A. 92:1995;1950-1954.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1950-1954
    • Li, G.M.1    Modrich, P.2
  • 172
    • 0029661432 scopus 로고    scopus 로고
    • Human MutSalpha specifically binds to DNA containing aminofluorene and acetylaminofluorene adducts
    • Li G.M., Wang H., Romano L.J. Human MutSalpha specifically binds to DNA containing aminofluorene and acetylaminofluorene adducts. J. Biol. Chem. 271:1996;24084-24088.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24084-24088
    • Li, G.M.1    Wang, H.2    Romano, L.J.3
  • 173
    • 0035937809 scopus 로고    scopus 로고
    • ATM is required for IkappaB kinase (IKKk) activation in response to DNA double strand breaks
    • Li N., Banin S., Ouyang H., Li G.C., Courtois G., Shiloh Y., Karin M., Rotman G. ATM is required for IkappaB kinase (IKKk) activation in response to DNA double strand breaks. J. Biol. Chem. 276:2001;8898-8903.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8898-8903
    • Li, N.1    Banin, S.2    Ouyang, H.3    Li, G.C.4    Courtois, G.5    Shiloh, Y.6    Karin, M.7    Rotman, G.8
  • 176
    • 0032994152 scopus 로고    scopus 로고
    • A full-length cDNA of hREV3 is predicted to encode DNA polymerase zeta for damage-induced mutagenesis in humans
    • Lin W., Wu X., Wang Z. A full-length cDNA of hREV3 is predicted to encode DNA polymerase zeta for damage-induced mutagenesis in humans. Mutat. Res. 433:1999;89-98.
    • (1999) Mutat. Res. , vol.433 , pp. 89-98
    • Lin, W.1    Wu, X.2    Wang, Z.3
  • 177
    • 0025342965 scopus 로고
    • Repair of intrinsic DNA lesions
    • Lindahl T. Repair of intrinsic DNA lesions. Mutat. Res. 238:1990;305-311.
    • (1990) Mutat. Res. , vol.238 , pp. 305-311
    • Lindahl, T.1
  • 178
    • 0035225455 scopus 로고    scopus 로고
    • Lindahl, T., 2001. Keynote: past, present, and future aspects of base excision repair. Prog. Nucleic. Acid. Res. Mol. Biol. 68, xvii-xxx.
    • Lindahl, T., 2001. Keynote: past, present, and future aspects of base excision repair. Prog. Nucleic. Acid. Res. Mol. Biol. 68, xvii-xxx.
  • 179
    • 0028865245 scopus 로고
    • Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks
    • Lindahl T., Satoh M.S., Poirier G.G., Klungland A. Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks. Trends Biochem. Sci. 20:1995;405-411.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 405-411
    • Lindahl, T.1    Satoh, M.S.2    Poirier, G.G.3    Klungland, A.4
  • 180
    • 0035074129 scopus 로고    scopus 로고
    • DNA double-strand breaks trigger apoptosis in p53-deficient fibroblasts
    • Lips J., Kaina B. DNA double-strand breaks trigger apoptosis in p53-deficient fibroblasts. Carcinogenesis. 22:2001;579-585.
    • (2001) Carcinogenesis , vol.22 , pp. 579-585
    • Lips, J.1    Kaina, B.2
  • 181
    • 0032476005 scopus 로고    scopus 로고
    • A human RNA polymerase II transcription termination factor is a SWI2/ SNF2 family member
    • Liu M., Xie Z., Price D.H. A human RNA polymerase II transcription termination factor is a SWI2/SNF2 family member. J. Biol. Chem. 273:1998;25541-25544.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25541-25544
    • Liu, M.1    Xie, Z.2    Price, D.H.3
  • 182
    • 0037082427 scopus 로고    scopus 로고
    • Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells
    • Liu N., Schild D., Thelen M.P., Thompson L.H. Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells. Nucleic Acids Res. 30:2002;1009-1015.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1009-1015
    • Liu, N.1    Schild, D.2    Thelen, M.P.3    Thompson, L.H.4
  • 184
    • 0029785723 scopus 로고    scopus 로고
    • Blockage of RNA polymerase as a possible trigger for u.v. light-induced apoptosis
    • Ljungman M., Zhang F. Blockage of RNA polymerase as a possible trigger for u.v. light-induced apoptosis. Oncogene. 13:1996;823-831.
    • (1996) Oncogene , vol.13 , pp. 823-831
    • Ljungman, M.1    Zhang, F.2
  • 185
    • 0022037404 scopus 로고
    • Apurinic sites as mutagenic intermediates
    • Loeb L.A. Apurinic sites as mutagenic intermediates. Cell. 40:1985;483-484.
    • (1985) Cell , vol.40 , pp. 483-484
    • Loeb, L.A.1
  • 186
    • 0030935386 scopus 로고    scopus 로고
    • DNA polymerase delta is required for human mismatch repair in vitro
    • Longley M.J., Pierce A.J., Modrich P. DNA polymerase delta is required for human mismatch repair in vitro. J. Biol. Chem. 272:1997;10917-10921.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10917-10921
    • Longley, M.J.1    Pierce, A.J.2    Modrich, P.3
  • 187
  • 189
    • 0035976732 scopus 로고    scopus 로고
    • TCDD-inducible poly(ADP-ribose) polymerase: A novel response to 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Ma Q., Baldwin K.T., Renzelli A.J., McDaniel A., Dong L. TCDD-inducible poly(ADP-ribose) polymerase: a novel response to 2,3,7,8-tetrachlorodibenzo-p- dioxin. Biochem. Biophys. Res. Commun. 289:2001;499-506.
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 499-506
    • Ma, Q.1    Baldwin, K.T.2    Renzelli, A.J.3    McDaniel, A.4    Dong, L.5
  • 192
    • 0037169516 scopus 로고    scopus 로고
    • DNA-dependent protein kinase catalytic subunit. Structural requirements for kinase activation by DNA ends
    • Martensson S., Hammarsten O. DNA-dependent protein kinase catalytic subunit. Structural requirements for kinase activation by DNA ends. J. Biol. Chem. 277:2002;3020-3029.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3020-3029
    • Martensson, S.1    Hammarsten, O.2
  • 193
    • 0030764691 scopus 로고    scopus 로고
    • HMre11 and hRad50 nuclear foci are induced during the normal cellular response to DNA double-strand breaks
    • Maser R.S., Monsen K.J., Nelms B.E., Petrini J.H. hMre11 and hRad50 nuclear foci are induced during the normal cellular response to DNA double-strand breaks. Mol. Cell. Biol. 17:1997;6087-6096.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6087-6096
    • Maser, R.S.1    Monsen, K.J.2    Nelms, B.E.3    Petrini, J.H.4
  • 195
    • 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
  • 196
    • 0034660259 scopus 로고    scopus 로고
    • Mechanisms of accurate translesion synthesis by human DNA polymerase eta
    • Masutani C., Kusumoto R., Iwai S., Hanaoka F. Mechanisms of accurate translesion synthesis by human DNA polymerase eta. EMBO J. 19:2000;3100-3109.
    • (2000) EMBO J. , vol.19 , pp. 3100-3109
    • Masutani, C.1    Kusumoto, R.2    Iwai, S.3    Hanaoka, F.4
  • 199
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair
    • Matsumoto Y., Kim K. Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair. Science. 269:1995;699-702.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 200
    • 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
  • 205
    • 0030198880 scopus 로고    scopus 로고
    • The mismatch-repair protein hMSH2 binds selectively to DNA adducts of the anticancer drug cisplatin
    • Mello J.A., Acharya S., Fishel R., Essigmann J.M. The mismatch-repair protein hMSH2 binds selectively to DNA adducts of the anticancer drug cisplatin. Chem. Biol. 3:1996;579-589.
    • (1996) Chem. Biol. , vol.3 , pp. 579-589
    • Mello, J.A.1    Acharya, S.2    Fishel, R.3    Essigmann, J.M.4
  • 206
    • 0023663101 scopus 로고
    • Selective removal of transcription-blocking DNA damage from the transcribed strand of the mammalian DHFR gene
    • Mellon I., Spivak G., Hanawalt P.C. Selective removal of transcription-blocking DNA damage from the transcribed strand of the mammalian DHFR gene. Cell. 51:1987;241-249.
    • (1987) Cell , vol.51 , pp. 241-249
    • Mellon, I.1    Spivak, G.2    Hanawalt, P.C.3
  • 207
    • 0024456894 scopus 로고
    • Zinc-binding domain of poly(ADP-ribose)polymerase participates in the recognition of single strand breaks on DNA
    • Menissier-de Murcia J., Molinete M., Gradwohl G., Simonin F., de Murcia G. Zinc-binding domain of poly(ADP-ribose)polymerase participates in the recognition of single strand breaks on DNA. J. Mol. Biol. 210:1989;229-233.
    • (1989) J. Mol. Biol. , vol.210 , pp. 229-233
    • Menissier-De Murcia, J.1    Molinete, M.2    Gradwohl, G.3    Simonin, F.4    De Murcia, G.5
  • 208
    • 0029943449 scopus 로고    scopus 로고
    • Mismatch repair in replication fidelity, genetic recombination, and cancer biology
    • Modrich P., Lahue R. Mismatch repair in replication fidelity, genetic recombination, and cancer biology. Annu. Rev. Biochem. 65:1996;101-133.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 101-133
    • Modrich, P.1    Lahue, R.2
  • 210
    • 0028896837 scopus 로고
    • Reconstitution of human DNA repair excision nuclease in a highly defined system
    • Mu D., Park C.H., Matsunaga T., Hsu D.S., Reardon J.T., Sancar A. Reconstitution of human DNA repair excision nuclease in a highly defined system. J. Biol. Chem. 270:1995;2415-2418.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2415-2418
    • Mu, D.1    Park, C.H.2    Matsunaga, T.3    Hsu, D.S.4    Reardon, J.T.5    Sancar, A.6
  • 211
    • 0035981166 scopus 로고    scopus 로고
    • Photoimmunology and nucleotide excision repair: Impact of transcription coupled and global genome excision repair
    • Mullenders L.H., Berneburg M. Photoimmunology and nucleotide excision repair: impact of transcription coupled and global genome excision repair. J. Photochem. Photobiol. B. 65:2001;97-100.
    • (2001) J. Photochem. Photobiol. B , vol.65 , pp. 97-100
    • Mullenders, L.H.1    Berneburg, M.2
  • 212
    • 0026093209 scopus 로고
    • Isolation and characterization of a human cDNA encoding uracil-DNA glycosylase
    • Muller S.J., Caradonna S. Isolation and characterization of a human cDNA encoding uracil-DNA glycosylase. Biochim. Biophys. Acta. 1088:1991;197-207.
    • (1991) Biochim. Biophys. Acta. , vol.1088 , pp. 197-207
    • Muller, S.J.1    Caradonna, S.2
  • 213
    • 0037196067 scopus 로고    scopus 로고
    • The property of DNA polymerase zeta: REV7 is a putative protein involved in translesion DNA synthesis and cell cycle control
    • Murakumo Y. The property of DNA polymerase zeta: REV7 is a putative protein involved in translesion DNA synthesis and cell cycle control. Mutat. Res. 510:2002;37-44.
    • (2002) Mutat. Res. , vol.510 , pp. 37-44
    • Murakumo, Y.1
  • 215
    • 0034635445 scopus 로고    scopus 로고
    • A human REV7 homolog that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD 2
    • Murakumo Y., Roth T., Ishii H., Rasio D., Numata S., Croce C.M., Fishel R. A human REV7 homolog that interacts with the polymerase zeta catalytic subunit hREV3 and the spindle assembly checkpoint protein hMAD 2. J. Biol. Chem. 275:2000;4391-4397.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4391-4397
    • Murakumo, Y.1    Roth, T.2    Ishii, H.3    Rasio, D.4    Numata, S.5    Croce, C.M.6    Fishel, R.7
  • 216
    • 0034008136 scopus 로고    scopus 로고
    • 5′-nicked apurinic/apyrimidinic sites are resistant to beta-elimination by beta-polymerase and are persistent in human cultured cells after oxidative stress
    • Nakamura J., La D.K., Swenberg J.A. 5′-nicked apurinic/ apyrimidinic sites are resistant to beta-elimination by beta-polymerase and are persistent in human cultured cells after oxidative stress. J. Biol. Chem. 275:2000;5323-5328.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5323-5328
    • Nakamura, J.1    La, D.K.2    Swenberg, J.A.3
  • 219
    • 0027383758 scopus 로고
    • The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells
    • Neddermann P., Jiricny J. The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells. J. Biol. Chem. 268:1993;21218-21224.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21218-21224
    • Neddermann, P.1    Jiricny, J.2
  • 220
    • 0028201737 scopus 로고
    • Efficient removal of uracil from G.U mispairs by the mismatch-specific thymine DNA glycosylase from HeLa cells
    • Neddermann P., Jiricny J. Efficient removal of uracil from G.U mispairs by the mismatch-specific thymine DNA glycosylase from HeLa cells. Proc. Natl. Acad. Sci. U.S.A. 91:1994;1642-1646.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1642-1646
    • Neddermann, P.1    Jiricny, J.2
  • 221
    • 0032562595 scopus 로고    scopus 로고
    • In situ visualization of DNA double-strand break repair in human fibroblasts
    • Nelms B.E., Maser R.S., MacKay J.F., Lagally M.G., Petrini J.H. In situ visualization of DNA double-strand break repair in human fibroblasts. Science. 280:1998;590-592.
    • (1998) Science , vol.280 , pp. 590-592
    • Nelms, B.E.1    Maser, R.S.2    MacKay, J.F.3    Lagally, M.G.4    Petrini, J.H.5
  • 222
    • 0032556870 scopus 로고    scopus 로고
    • Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A
    • New J.H., Sugiyama T., Zaitseva E., Kowalczykowski S.C. Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A. Nature. 391:1998;407-410.
    • (1998) Nature , vol.391 , pp. 407-410
    • New, J.H.1    Sugiyama, T.2    Zaitseva, E.3    Kowalczykowski, S.C.4
  • 224
    • 0035421186 scopus 로고    scopus 로고
    • Excision of deaminated cytosine from the vertebrate genome: Role of the SMUG1 uracil-DNA glycosylase
    • Nilsen H., Haushalter K.A., Robins P., Barnes D.E., Verdine G.L., Lindahl T. Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase. EMBO J. 20:2001;4278-4286.
    • (2001) EMBO J. , vol.20 , pp. 4278-4286
    • Nilsen, H.1    Haushalter, K.A.2    Robins, P.3    Barnes, D.E.4    Verdine, G.L.5    Lindahl, T.6
  • 225
    • 0025784273 scopus 로고
    • Human cDNA expressing a functional DNA glycosylase excising 3-methyladenine and 7-methylguanine
    • O'Connor T.R., Laval J. Human cDNA expressing a functional DNA glycosylase excising 3-methyladenine and 7-methylguanine. Biochem. Biophys. Res. Commun. 176:1991;1170-1177.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 1170-1177
    • O'Connor, T.R.1    Laval, J.2
  • 226
    • 0028085556 scopus 로고
    • XPG endonuclease makes the 3′ incision in human DNA nucleotide excision repair
    • O'Donovan A., Davies A.A., Moggs J.G., West S.C., Wood R.D. XPG endonuclease makes the 3′ incision in human DNA nucleotide excision repair. Nature. 371:1994;432-435.
    • (1994) Nature , vol.371 , pp. 432-435
    • O'Donovan, A.1    Davies, A.A.2    Moggs, J.G.3    West, S.C.4    Wood, R.D.5
  • 228
    • 0033387531 scopus 로고    scopus 로고
    • Mutation enhancement by DINB1, a mammalian homologue of the Escherichia coli mutagenesis protein dinB
    • Ogi T., Kato T. Jr., Kato T., Ohmori H. Mutation enhancement by DINB1, a mammalian homologue of the Escherichia coli mutagenesis protein dinB. Genes Cells. 4:1999;607-618.
    • (1999) Genes Cells , vol.4 , pp. 607-618
    • Ogi, T.1    Kato T., Jr.2    Kato, T.3    Ohmori, H.4
  • 231
    • 0024414264 scopus 로고
    • Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme
    • Olsen L.C., Aasland R., Wittwer C.U., Krokan H.E., Helland D.E. Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme. EMBO J. 8:1989;3121-3125.
    • (1989) EMBO J. , vol.8 , pp. 3121-3125
    • Olsen, L.C.1    Aasland, R.2    Wittwer, C.U.3    Krokan, H.E.4    Helland, D.E.5
  • 233
    • 0029659046 scopus 로고    scopus 로고
    • HMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
    • Palombo F., Iaccarino I., Nakajima E., Ikejima M., Shimada T., Jiricny J. hMutSbeta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA. Curr. Biol. 6:1996;1181-1184.
    • (1996) Curr. Biol. , vol.6 , pp. 1181-1184
    • Palombo, F.1    Iaccarino, I.2    Nakajima, E.3    Ikejima, M.4    Shimada, T.5    Jiricny, J.6
  • 235
    • 0029768921 scopus 로고    scopus 로고
    • Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells
    • Park M.S., Ludwig D.L., Stigger E., Lee S.H. Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells. J. Biol. Chem. 271:1996;18996-19000.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18996-19000
    • Park, M.S.1    Ludwig, D.L.2    Stigger, E.3    Lee, S.H.4
  • 237
    • 0032540927 scopus 로고    scopus 로고
    • Identification of a human homologue of the Schizosaccharomyces pombe rad17+ checkpoint gene
    • Parker A.E., Van de Weyer I., Laus M.C., Verhasselt P., Luyten W.H. Identification of a human homologue of the Schizosaccharomyces pombe rad17+ checkpoint gene. J. Biol. Chem. 273:1998b;18340-18346.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18340-18346
    • Parker, A.E.1    Van De Weyer, I.2    Laus, M.C.3    Verhasselt, P.4    Luyten, W.H.5
  • 238
    • 0033563229 scopus 로고    scopus 로고
    • Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex
    • Paull T.T., Gellert M. Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex. Genes Dev. 13:1999;1276-1288.
    • (1999) Genes Dev. , vol.13 , pp. 1276-1288
    • Paull, T.T.1    Gellert, M.2
  • 240
    • 0030611095 scopus 로고    scopus 로고
    • Mitotic and G2 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216
    • Peng C.Y., Graves P.R., Thoma R.S., Wu Z., Shaw A.S., Piwnica-Worms H. Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216. Science. 277:1997;1501-1505.
    • (1997) Science , vol.277 , pp. 1501-1505
    • Peng, C.Y.1    Graves, P.R.2    Thoma, R.S.3    Wu, Z.4    Shaw, A.S.5    Piwnica-Worms, H.6
  • 241
    • 0032492853 scopus 로고    scopus 로고
    • Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins
    • Petukhova G., Stratton S., Sung P. Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins. Nature. 393:1998;91-94.
    • (1998) Nature , vol.393 , pp. 91-94
    • Petukhova, G.1    Stratton, S.2    Sung, P.3
  • 242
    • 0032832810 scopus 로고    scopus 로고
    • Yeast Rad54 promotes Rad51-dependent homologous DNA pairing via ATP hydrolysis-driven change in DNA double helix conformation
    • Petukhova G., Van Komen S., Vergano S., Klein H., Sung P. Yeast Rad54 promotes Rad51-dependent homologous DNA pairing via ATP hydrolysis-driven change in DNA double helix conformation. J. Biol. Chem. 274:1999;29453-29462.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29453-29462
    • Petukhova, G.1    Van Komen, S.2    Vergano, S.3    Klein, H.4    Sung, P.5
  • 243
    • 0033855389 scopus 로고    scopus 로고
    • Mechanisms of DNA double-strand break repair and their potential to induce chromosomal aberration
    • Pfeiffer P., Goedecke W., Obe G. Mechanisms of DNA double-strand break repair and their potential to induce chromosomal aberration. Mutagenesis. 15:2000;289-302.
    • (2000) Mutagenesis , vol.15 , pp. 289-302
    • Pfeiffer, P.1    Goedecke, W.2    Obe, G.3
  • 244
    • 0034731455 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins
    • Pleschke J.M., Kleczkowska H.E., Strohm M., Althaus F.R. Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 275:2000;40974-40980.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 245
    • 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
  • 246
    • 0035818485 scopus 로고    scopus 로고
    • Phosphorylation of serines 635 and 645 of human Rad17 is cell cycle regulated and is required for G(1)/S checkpoint activation in response to DNA damage
    • Post S., Weng Y.C., Cimprich K., Chen L.B., Xu Y., Lee E.Y. Phosphorylation of serines 635 and 645 of human Rad17 is cell cycle regulated and is required for G(1)/S checkpoint activation in response to DNA damage. Proc. Natl. Acad. Sci. U.S.A. 98:2001;13102-13107.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 13102-13107
    • Post, S.1    Weng, Y.C.2    Cimprich, K.3    Chen, L.B.4    Xu, Y.5    Lee, E.Y.6
  • 247
    • 0032510962 scopus 로고    scopus 로고
    • Human DNA polymerase beta deoxyribose phosphate lyase. Substrate specificity and catalytic mechanism
    • Prasad R., Beard W.A., Strauss P.R., Wilson S.H. Human DNA polymerase beta deoxyribose phosphate lyase. Substrate specificity and catalytic mechanism. J. Biol. Chem. 273:1998;15263-15270.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15263-15270
    • Prasad, R.1    Beard, W.A.2    Strauss, P.R.3    Wilson, S.H.4
  • 248
    • 0035980003 scopus 로고    scopus 로고
    • DNA polymerase beta-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., Van de Berg B.J., Wilson S.H. DNA polymerase beta-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    Van De Berg, B.J.6    Wilson, S.H.7
  • 249
    • 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
  • 250
    • 0029068041 scopus 로고
    • 6- methylguanine-DNA methyltransferase promoter: Correlation with gene suppression
    • 6-methylguanine-DNA methyltransferase promoter: correlation with gene suppression. Carcinogenesis. 16:1995;1385-1390.
    • (1995) Carcinogenesis , vol.16 , pp. 1385-1390
    • Qian, X.1    Von Wronski, M.A.2    Brent, T.P.3
  • 251
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae
    • Radicella J.P., Dherin C., Desmaze C., Fox M.S., Boiteux S. Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 94:1997;8010-8015.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8010-8015
    • Radicella, J.P.1    Dherin, C.2    Desmaze, C.3    Fox, M.S.4    Boiteux, S.5
  • 252
    • 0034703051 scopus 로고    scopus 로고
    • The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9
    • Rauen M., Burtelow M.A., Dufault V.M., Karnitz L.M. The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9. J. Biol. Chem. 275:2000;29767-29771.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29767-29771
    • Rauen, M.1    Burtelow, M.A.2    Dufault, V.M.3    Karnitz, L.M.4
  • 253
    • 0030966978 scopus 로고    scopus 로고
    • Human Rad52 protein promotes single-strand DNA annealing followed by branch migration
    • Reddy G., Golub E.I., Radding C.M. Human Rad52 protein promotes single-strand DNA annealing followed by branch migration. Mutat. Res. 377:1997;53-59.
    • (1997) Mutat. Res. , vol.377 , pp. 53-59
    • Reddy, G.1    Golub, E.I.2    Radding, C.M.3
  • 254
    • 0024524581 scopus 로고
    • Molecular cloning of cDNA encoding the p70 (Ku) lupus autoantigen
    • Reeves W.H., Sthoeger Z.M. Molecular cloning of cDNA encoding the p70 (Ku) lupus autoantigen. J. Biol. Chem. 264:1989;5047-5052.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5047-5052
    • Reeves, W.H.1    Sthoeger, Z.M.2
  • 256
    • 0034641963 scopus 로고    scopus 로고
    • Defying death after DNA damage
    • Rich T., Allen R.L., Wyllie A.H. Defying death after DNA damage. Nature. 407:2000;777-783.
    • (2000) Nature , vol.407 , pp. 777-783
    • Rich, T.1    Allen, R.L.2    Wyllie, A.H.3
  • 261
    • 0027368923 scopus 로고
    • Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis
    • Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., Sekiguchi M. Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 268:1993;23524-23530.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23524-23530
    • Sakumi, K.1    Furuichi, M.2    Tsuzuki, T.3    Kakuma, T.4    Kawabata, S.5    Maki, H.6    Sekiguchi, M.7
  • 262
    • 0025990209 scopus 로고
    • Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16
    • Samson L., Derfler B., Boosalis M., Call K. Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16. Proc. Natl. Acad. Sci. U.S.A. 88:1991;9127-9131.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9127-9131
    • Samson, L.1    Derfler, B.2    Boosalis, M.3    Call, K.4
  • 263
    • 0030867582 scopus 로고    scopus 로고
    • Conservation of the Chk1 checkpoint pathway in mammals: Linkage of DNA damage to Cdk regulation through Cdc25
    • Sanchez Y., Wong C., Thoma R.S., Richman R., Wu Z., Piwnica-Worms H., Elledge S.J. Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25. Science. 277:1997;1497-1501.
    • (1997) Science , vol.277 , pp. 1497-1501
    • Sanchez, Y.1    Wong, C.2    Thoma, R.S.3    Richman, R.4    Wu, Z.5    Piwnica-Worms, H.6    Elledge, S.J.7
  • 264
    • 0037125135 scopus 로고    scopus 로고
    • Down-regulation of DNA repair synthesis at DNA single-strand interruptions in poly(ADP-ribose) polymerase-1 deficient murine cell extracts
    • Sanderson R.J., Lindahl T. Down-regulation of DNA repair synthesis at DNA single-strand interruptions in poly(ADP-ribose) polymerase-1 deficient murine cell extracts. DNA Repair (Amst.). 1:2002;547-558.
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 547-558
    • Sanderson, R.J.1    Lindahl, T.2
  • 268
    • 0035111895 scopus 로고    scopus 로고
    • Recent progress in the biology, chemistry and structural biology of DNA glycosylases
    • Scharer O.D., Jiricny J. Recent progress in the biology, chemistry and structural biology of DNA glycosylases. Bioessays. 23:2001;270-281.
    • (2001) Bioessays , vol.23 , pp. 270-281
    • Scharer, O.D.1    Jiricny, J.2
  • 270
    • 0034596020 scopus 로고    scopus 로고
    • Evidence for simultaneous protein interactions between human Rad51 paralogs
    • Schild D., Lio Y.C., Collins D.W., Tsomondo T., Chen D.J. Evidence for simultaneous protein interactions between human Rad51 paralogs. J. Biol. Chem. 275:2000;16443-16449.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16443-16449
    • Schild, D.1    Lio, Y.C.2    Collins, D.W.3    Tsomondo, T.4    Chen, D.J.5
  • 271
  • 272
    • 0037115934 scopus 로고    scopus 로고
    • Recent progress on the Ada response for inducible repair of DNA alkylation damage
    • Sedgwick B., Lindahl T. Recent progress on the Ada response for inducible repair of DNA alkylation damage. Oncogene. 21:2002;8886-8894.
    • (2002) Oncogene , vol.21 , pp. 8886-8894
    • Sedgwick, B.1    Lindahl, T.2
  • 273
    • 0030804783 scopus 로고    scopus 로고
    • RNA polymerase II stalled at a thymine dimer: Footprint and effect on excision repair
    • Selby C.P., Drapkin R., Reinberg D., Sancar A. RNA polymerase II stalled at a thymine dimer: footprint and effect on excision repair. Nucleic Acids Res. 25:1997;787-793.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 787-793
    • Selby, C.P.1    Drapkin, R.2    Reinberg, D.3    Sancar, A.4
  • 274
    • 85047698593 scopus 로고    scopus 로고
    • Implication of p53 in base excision DNA repair: In vivo evidence
    • Seo Y.R., Fishel M.L., Amundson S., Kelley M.R., Smith M.L. Implication of p53 in base excision DNA repair: in vivo evidence. Oncogene. 21:2002;731-737.
    • (2002) Oncogene , vol.21 , pp. 731-737
    • Seo, Y.R.1    Fishel, M.L.2    Amundson, S.3    Kelley, M.R.4    Smith, M.L.5
  • 276
    • 0033166143 scopus 로고    scopus 로고
    • Cloning and chromosomal mapping of the human DNA polymerase theta (POLQ), the eighth human DNA polymerase
    • Sharief F.S., Vojta P.J., Ropp P.A., Copeland W.C. Cloning and chromosomal mapping of the human DNA polymerase theta (POLQ), the eighth human DNA polymerase. Genomics. 59:1999;90-96.
    • (1999) Genomics , vol.59 , pp. 90-96
    • Sharief, F.S.1    Vojta, P.J.2    Ropp, P.A.3    Copeland, W.C.4
  • 277
    • 0030047343 scopus 로고    scopus 로고
    • Specific interactions between the human RAD51 and RAD52 proteins
    • Shen Z., Cloud K.G., Chen D.J., Park M.S. Specific interactions between the human RAD51 and RAD52 proteins. J. Biol. Chem. 271:1996;148-152.
    • (1996) J. Biol. Chem. , vol.271 , pp. 148-152
    • Shen, Z.1    Cloud, K.G.2    Chen, D.J.3    Park, M.S.4
  • 278
    • 0034142034 scopus 로고    scopus 로고
    • The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites
    • Shieh S.Y., Ahn J., Tamai K., Taya Y., Prives C. The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites. Genes Dev. 14:2000;289-300.
    • (2000) Genes Dev. , vol.14 , pp. 289-300
    • Shieh, S.Y.1    Ahn, J.2    Tamai, K.3    Taya, Y.4    Prives, C.5
  • 279
    • 0036668474 scopus 로고    scopus 로고
    • Clamp and clamp loader structures of the human checkpoint protein complexes, Rad9-1-1 and Rad17-RFC
    • Shiomi Y., Shinozaki A., Nakada D., Sugimoto K., Usukura J., Obuse C., Tsurimoto T. Clamp and clamp loader structures of the human checkpoint protein complexes, Rad9-1-1 and Rad17-RFC. Genes Cells. 7:2002;861-868.
    • (2002) Genes Cells , vol.7 , pp. 861-868
    • Shiomi, Y.1    Shinozaki, A.2    Nakada, D.3    Sugimoto, K.4    Usukura, J.5    Obuse, C.6    Tsurimoto, T.7
  • 280
    • 0035893241 scopus 로고    scopus 로고
    • Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange
    • Sigurdsson S., Van Komen S., Bussen W., Schild D., Albala J.S., Sung P. Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange. Genes Dev. 15:2001;3308-3318.
    • (2001) Genes Dev. , vol.15 , pp. 3308-3318
    • Sigurdsson, S.1    Van Komen, S.2    Bussen, W.3    Schild, D.4    Albala, J.S.5    Sung, P.6
  • 282
    • 0029111784 scopus 로고
    • Gene for the catalytic subunit of the human DNA-activated protein kinase maps to the site of the XRCC7 gene on chromosome 8
    • Sipley J.D., Menninger J.C., Hartley K.O., Ward D.C., Jackson S.P., Anderson C.W. Gene for the catalytic subunit of the human DNA-activated protein kinase maps to the site of the XRCC7 gene on chromosome 8. Proc. Natl. Acad. Sci. U.S.A. 92:1995;7515-7519.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7515-7519
    • Sipley, J.D.1    Menninger, J.C.2    Hartley, K.O.3    Ward, D.C.4    Jackson, S.P.5    Anderson, C.W.6
  • 283
    • 0030004207 scopus 로고    scopus 로고
    • Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage
    • Slupska M.M., Baikalov C., Luther W.M., Chiang J.H., Wei Y.F., Miller J.H. Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage. J. Bacteriol. 178:1996;3885-3892.
    • (1996) J. Bacteriol. , vol.178 , pp. 3885-3892
    • Slupska, M.M.1    Baikalov, C.2    Luther, W.M.3    Chiang, J.H.4    Wei, Y.F.5    Miller, J.H.6
  • 284
    • 0032840464 scopus 로고    scopus 로고
    • Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein
    • Slupska M.M., Luther W.M., Chiang J.H., Yang H., Miller J.H. Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein. J. Bacteriol. 181:1999;6210-6213.
    • (1999) J. Bacteriol. , vol.181 , pp. 6210-6213
    • Slupska, M.M.1    Luther, W.M.2    Chiang, J.H.3    Yang, H.4    Miller, J.H.5
  • 286
    • 0033560796 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase
    • Smith G.C., Jackson S.P. The DNA-dependent protein kinase. Genes Dev. 13:1999;916-934.
    • (1999) Genes Dev. , vol.13 , pp. 916-934
    • Smith, G.C.1    Jackson, S.P.2
  • 287
    • 0032553473 scopus 로고    scopus 로고
    • Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
    • Smith S., Giriat I., Schmitt A., de Lange T. Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. Science. 282:1998;1484-1487.
    • (1998) Science , vol.282 , pp. 1484-1487
    • Smith, S.1    Giriat, I.2    Schmitt, A.3    De Lange, T.4
  • 289
    • 0034659935 scopus 로고    scopus 로고
    • The lyase activity of the DNA repair protein beta-polymerase protects from DNA-damage-induced cytotoxicity
    • Sobol R.W., Prasad R., Evenski A., Baker A., Yang X.P., Horton J.K., Wilson S.H. The lyase activity of the DNA repair protein beta-polymerase protects from DNA-damage-induced cytotoxicity. Nature. 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
  • 290
    • 0036022402 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 cleavage during apoptosis: An update
    • Soldani C., Scovassi A.I. Poly(ADP-ribose) polymerase-1 cleavage during apoptosis: an update. Apoptosis. 7:2002;321-328.
    • (2002) Apoptosis , vol.7 , pp. 321-328
    • Soldani, C.1    Scovassi, A.I.2
  • 292
    • 0037031218 scopus 로고    scopus 로고
    • Ultraviolet-sensitive syndrome cells are defective in transcription-coupled repair of cyclobutane pyrimidine dimers
    • Spivak G., Itoh T., Matsunaga T., Nikaido O., Hanawalt P., Yamaizumi M. Ultraviolet-sensitive syndrome cells are defective in transcription-coupled repair of cyclobutane pyrimidine dimers. DNA Repair (Amst.). 1:2002;629-643.
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 629-643
    • Spivak, G.1    Itoh, T.2    Matsunaga, T.3    Nikaido, O.4    Hanawalt, P.5    Yamaizumi, M.6
  • 293
    • 0032516831 scopus 로고    scopus 로고
    • Mammalian abasic site base excision repair. Identification of the reaction sequence and rate-determining steps
    • Srivastava D.K., Berg B.J., Prasad R., Molina J.T., Beard W.A., Tomkinson A.E., Wilson S.H. Mammalian abasic site base excision repair. Identification of the reaction sequence and rate-determining steps. J. Biol. Chem. 273:1998;21203-21209.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21203-21209
    • Srivastava, D.K.1    Berg, B.J.2    Prasad, R.3    Molina, J.T.4    Beard, W.A.5    Tomkinson, A.E.6    Wilson, S.H.7
  • 294
    • 0033018634 scopus 로고    scopus 로고
    • The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1
    • St Onge R.P., Udell C.M., Casselman R., Davey S. The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1. Mol. Biol. Cell. 10:1999;1985-1995.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1985-1995
    • St Onge, R.P.1    Udell, C.M.2    Casselman, R.3    Davey, S.4
  • 296
    • 0033572367 scopus 로고    scopus 로고
    • Identification of a novel gene (ADPRTL1) encoding a potential poly(ADP-ribosyl)transferase protein
    • Still I.H., Vince P., Cowell J.K. Identification of a novel gene (ADPRTL1) encoding a potential poly(ADP-ribosyl)transferase protein. Genomics. 62:1999;533-536.
    • (1999) Genomics , vol.62 , pp. 533-536
    • Still, I.H.1    Vince, P.2    Cowell, J.K.3
  • 298
    • 0035282109 scopus 로고    scopus 로고
    • A multistep damage recognition mechanism for global genomic nucleotide excision repair
    • Sugasawa K., Okamoto T., Shimizu Y., Masutani C., Iwai S., Hanaoka F. A multistep damage recognition mechanism for global genomic nucleotide excision repair. Genes Dev. 15:2001;507-521.
    • (2001) Genes Dev. , vol.15 , pp. 507-521
    • Sugasawa, K.1    Okamoto, T.2    Shimizu, Y.3    Masutani, C.4    Iwai, S.5    Hanaoka, F.6
  • 299
    • 0033520432 scopus 로고    scopus 로고
    • Recruitment of ATM protein to double strand DNA irradiated with ionizing radiation
    • Suzuki K., Kodama S., Watanabe M. Recruitment of ATM protein to double strand DNA irradiated with ionizing radiation. J. Biol. Chem. 274:1999;25571-25575.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25571-25575
    • Suzuki, K.1    Kodama, S.2    Watanabe, M.3
  • 300
    • 0036363646 scopus 로고    scopus 로고
    • Mechanisms of transcription-coupled DNA repair
    • Svejstrup J.Q. Mechanisms of transcription-coupled DNA repair. Nat. Rev. Mol. Cell. Biol. 3:2002;21-29.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 21-29
    • Svejstrup, J.Q.1
  • 301
    • 0037326318 scopus 로고    scopus 로고
    • Rescue of arrested RNA polymerase II complexes
    • Svejstrup J.Q. Rescue of arrested RNA polymerase II complexes. J. Cell Sci. 116:2003;447-451.
    • (2003) J. Cell Sci. , vol.116 , pp. 447-451
    • Svejstrup, J.Q.1
  • 304
    • 0032530658 scopus 로고    scopus 로고
    • Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells
    • Takata M., Sasaki M.S., Sonoda E., Morrison C., Hashimoto M., Utsumi H., Yamaguchi-Iwai Y., Shinohara A., Takeda S. Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells. EMBO J. 17:1998;5497-5508.
    • (1998) EMBO J. , vol.17 , pp. 5497-5508
    • Takata, M.1    Sasaki, M.S.2    Sonoda, E.3    Morrison, C.4    Hashimoto, M.5    Utsumi, H.6    Yamaguchi-Iwai, Y.7    Shinohara, A.8    Takeda, S.9
  • 305
    • 0036490983 scopus 로고    scopus 로고
    • BRCA1 transcriptionally regulates damaged DNA binding protein (DDB2) in the DNA repair response following UV-irradiation
    • Takimoto R., MacLachlan T.K., Dicker D.T., Niitsu Y., Mori T., el-Deiry W.S. BRCA1 transcriptionally regulates damaged DNA binding protein (DDB2) in the DNA repair response following UV-irradiation. Cancer Biol. Ther. 1:2002;177-186.
    • (2002) Cancer Biol. Ther. , vol.1 , pp. 177-186
    • Takimoto, R.1    MacLachlan, T.K.2    Dicker, D.T.3    Niitsu, Y.4    Mori, T.5    El-Deiry, W.S.6
  • 306
    • 0036234458 scopus 로고    scopus 로고
    • P53 binds and activates the xeroderma pigmentosum DDB2 gene in humans but not mice
    • Tan T., Chu G. p53 binds and activates the xeroderma pigmentosum DDB2 gene in humans but not mice. Mol. Cell. Biol. 22:2002;3247-3254.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3247-3254
    • Tan, T.1    Chu, G.2
  • 307
    • 0037031210 scopus 로고    scopus 로고
    • Xeroderma pigmentosum complementation group E and UV-damaged DNA-binding protein
    • Tang J., Chu G. Xeroderma pigmentosum complementation group E and UV-damaged DNA-binding protein. DNA Repair (Amst.). 1:2002;601-616.
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 601-616
    • Tang, J.1    Chu, G.2
  • 309
    • 0030667078 scopus 로고    scopus 로고
    • Recruitment of the putative transcription-repair coupling factor CSB/ERCC6 to RNA polymerase II elongation complexes
    • Tantin D., Kansal A., Carey M. Recruitment of the putative transcription-repair coupling factor CSB/ERCC6 to RNA polymerase II elongation complexes. Mol. Cell. Biol. 17:1997;6803-6814.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6803-6814
    • Tantin, D.1    Kansal, A.2    Carey, M.3
  • 310
    • 0033582906 scopus 로고    scopus 로고
    • A sliding clamp model for the Rad1 family of cell cycle checkpoint proteins
    • Thelen M.P., Venclovas C., Fidelis K. A sliding clamp model for the Rad1 family of cell cycle checkpoint proteins. Cell. 96:1999;769-770.
    • (1999) Cell , vol.96 , pp. 769-770
    • Thelen, M.P.1    Venclovas, C.2    Fidelis, K.3
  • 311
    • 0025777777 scopus 로고
    • Heteroduplex repair in extracts of human HeLa cells
    • Thomas D.C., Roberts J.D., Kunkel T.A. Heteroduplex repair in extracts of human HeLa cells. J. Biol. Chem. 266:1991;3744-3751.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3744-3751
    • Thomas, D.C.1    Roberts, J.D.2    Kunkel, T.A.3
  • 313
    • 0037115913 scopus 로고    scopus 로고
    • Photolyase/cryptochrome blue-light photoreceptors use photon energy to repair DNA and reset the circadian clock
    • Thompson C.L., Sancar A. Photolyase/cryptochrome blue-light photoreceptors use photon energy to repair DNA and reset the circadian clock. Oncogene. 21:2002;9043-9056.
    • (2002) Oncogene , vol.21 , pp. 9043-9056
    • Thompson, C.L.1    Sancar, A.2
  • 314
    • 0037202608 scopus 로고    scopus 로고
    • Recombinational DNA repair and human disease
    • Thompson L.H., Schild D. Recombinational DNA repair and human disease. Mutat. Res. 509:2002;49-78.
    • (2002) Mutat. Res. , vol.509 , pp. 49-78
    • Thompson, L.H.1    Schild, D.2
  • 317
    • 0034596992 scopus 로고    scopus 로고
    • Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase iota
    • Tissier A., Frank E.G., McDonald J.P., Iwai S., Hanaoka F., Woodgate R. Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase iota. EMBO J. 19:2000a;5259-5266.
    • (2000) EMBO J. , vol.19 , pp. 5259-5266
    • Tissier, A.1    Frank, E.G.2    McDonald, J.P.3    Iwai, S.4    Hanaoka, F.5    Woodgate, R.6
  • 318
    • 0034214838 scopus 로고    scopus 로고
    • Poliota, a remarkably error-prone human DNA polymerase
    • Tissier A., McDonald J.P., Frank E.G., Woodgate R. Poliota, a remarkably error-prone human DNA polymerase. Genes Dev. 14:2000b;1642-1650.
    • (2000) Genes Dev. , vol.14 , pp. 1642-1650
    • Tissier, A.1    McDonald, J.P.2    Frank, E.G.3    Woodgate, R.4
  • 321
    • 85030970983 scopus 로고    scopus 로고
    • Tornaletti, S., Patrick, S.M., Turchi, J.J., Hanawalt, P.C. Behavior of T7RNA polymerase and mammalian RNA polymerase II at site-specific cisplatin adducts in the template DNA. J. Biol. Chem., in press.
    • Tornaletti, S., Patrick, S.M., Turchi, J.J., Hanawalt, P.C. Behavior of T7RNA polymerase and mammalian RNA polymerase II at site-specific cisplatin adducts in the template DNA. J. Biol. Chem., in press.
  • 322
    • 0033588105 scopus 로고    scopus 로고
    • Structural characterization of RNA polymerase II complexes arrested by a cyclobutane pyrimidine dimer in the transcribed strand of template DNA
    • Tornaletti S., Reiness D., Hanawalt P.C. Structural characterization of RNA polymerase II complexes arrested by a cyclobutane pyrimidine dimer in the transcribed strand of template DNA. Biol. Chem. 274:1999;24124-24130.
    • (1999) Biol. Chem. , vol.274 , pp. 24124-24130
    • Tornaletti, S.1    Reiness, D.2    Hanawalt, P.C.3
  • 323
    • 0037068446 scopus 로고    scopus 로고
    • Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
    • Trewick S.C., Henshaw T.F., Hausinger R.P., Lindahl T., Sedgwick B. Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage. Nature. 419:2002;174-178.
    • (2002) Nature , vol.419 , pp. 174-178
    • Trewick, S.C.1    Henshaw, T.F.2    Hausinger, R.P.3    Lindahl, T.4    Sedgwick, B.5
  • 324
    • 0026465665 scopus 로고
    • ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes
    • Troelstra C., van Gool A., de Wit J., Vermeulen W., Bootsma D., Hoeijmakers J.H. ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes. Cell. 71:1992;939-953.
    • (1992) Cell , vol.71 , pp. 939-953
    • Troelstra, C.1    Van Gool, A.2    De Wit, J.3    Vermeulen, W.4    Bootsma, D.5    Hoeijmakers, J.H.6
  • 326
    • 0032555480 scopus 로고    scopus 로고
    • Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, p95
    • Trujillo K.M., Yuan S.S., Lee E.Y., Sung P. Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, p95. J. Biol. Chem. 273:1998;21447-21450.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21447-21450
    • Trujillo, K.M.1    Yuan, S.S.2    Lee, E.Y.3    Sung, P.4
  • 327
    • 0032569982 scopus 로고    scopus 로고
    • PCNA, a multifunctional ring on DNA
    • Tsurimoto T. PCNA, a multifunctional ring on DNA. Biochim. Biophys. Acta. 1443:1998;23-39.
    • (1998) Biochim. Biophys. Acta , vol.1443 , pp. 23-39
    • Tsurimoto, T.1
  • 329
    • 0035478982 scopus 로고    scopus 로고
    • Proteasomal degradation of oxidatively damaged endogenous histones in K562 human leukemic cells
    • Ullrich O., Grune T. Proteasomal degradation of oxidatively damaged endogenous histones in K562 human leukemic cells. Free Radic. Biol. Med. 31:2001;887-893.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 887-893
    • Ullrich, O.1    Grune, T.2
  • 331
    • 0027988576 scopus 로고
    • DNA loop repair by human cell extracts
    • Umar A., Boyer J.C., Kunkel T.A. DNA loop repair by human cell extracts. Science. 266:1994;814-816.
    • (1994) Science , vol.266 , pp. 814-816
    • Umar, A.1    Boyer, J.C.2    Kunkel, T.A.3
  • 332
    • 0029903164 scopus 로고    scopus 로고
    • DNA-replication fidelity, mismatch repair and genome instability in cancer cells
    • Umar A., Kunkel T.A. DNA-replication fidelity, mismatch repair and genome instability in cancer cells. Eur. J. Biochem. 238:1996;297-307.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 297-307
    • Umar, A.1    Kunkel, T.A.2
  • 336
    • 0033594407 scopus 로고    scopus 로고
    • Binding of double-strand breaks in DNA by human Rad52 protein
    • Van Dyck E., Stasiak A.Z., Stasiak A., West S.C. Binding of double-strand breaks in DNA by human Rad52 protein. Nature. 398:1999;728-731.
    • (1999) Nature , vol.398 , pp. 728-731
    • Van Dyck, E.1    Stasiak, A.Z.2    Stasiak, A.3    West, S.C.4
  • 340
    • 0029941444 scopus 로고    scopus 로고
    • The sensitivity of Cockayne's syndrome cells to DNA-damaging agents is not due to defective transcription-coupled repair of active genes
    • van Oosterwijk M.F., Versteeg A., Filon R., van Zeeland A.A., Mullenders L.H. The sensitivity of Cockayne's syndrome cells to DNA-damaging agents is not due to defective transcription-coupled repair of active genes. Mol. Cell. Biol. 16:1996;4436-4444.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4436-4444
    • Van Oosterwijk, M.F.1    Versteeg, A.2    Filon, R.3    Van Zeeland, A.A.4    Mullenders, L.H.5
  • 342
    • 0037197844 scopus 로고    scopus 로고
    • Human XPA and RPA DNA repair proteins participate in specific recognition of triplex-induced helical distortions
    • Vasquez K.M., Christensen J., Li L., Finch R.A., Glazer P.M. Human XPA and RPA DNA repair proteins participate in specific recognition of triplex-induced helical distortions. Proc. Natl. Acad. Sci. U.S.A. 99:2002;5848-5853.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5848-5853
    • Vasquez, K.M.1    Christensen, J.2    Li, L.3    Finch, R.A.4    Glazer, P.M.5
  • 343
    • 0034235463 scopus 로고    scopus 로고
    • Structure-based predictions of Rad1, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes
    • Venclovas C., Thelen M.P. Structure-based predictions of Rad1, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes. Nucleic Acids Res. 28:2000;2481-2493.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2481-2493
    • Venclovas, C.1    Thelen, M.P.2
  • 344
    • 0025341294 scopus 로고
    • The genetic defect in Cockayne syndrome is associated with a defect in repair of UV-induced DNA damage in transcriptionally active DNA
    • Venema J., Mullenders L.H., Natarajan A.T., van Zeeland A.A., Mayne L.V. The genetic defect in Cockayne syndrome is associated with a defect in repair of UV-induced DNA damage in transcriptionally active DNA. Proc. Natl. Acad. Sci. U.S.A. 87:1990;4707-4711.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4707-4711
    • Venema, J.1    Mullenders, L.H.2    Natarajan, A.T.3    Van Zeeland, A.A.4    Mayne, L.V.5
  • 347
    • 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
  • 349
    • 0033534613 scopus 로고    scopus 로고
    • Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex
    • Volkmer E., Karnitz L.M. Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex. J. Biol. Chem. 274:1999;567-570.
    • (1999) J. Biol. Chem. , vol.274 , pp. 567-570
    • Volkmer, E.1    Karnitz, L.M.2
  • 350
    • 0031663505 scopus 로고    scopus 로고
    • The DNA replication fork in eukaryotic cells
    • Waga S., Stillman B. The DNA replication fork in eukaryotic cells. Annu. Rev. Biochem. 67:1998;721-751.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 721-751
    • Waga, S.1    Stillman, B.2
  • 351
    • 0037127293 scopus 로고    scopus 로고
    • DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair
    • Wakasugi M., Kawashima A., Morioka H., Linn S., Sancar A., Mori T., Nikaido O., Matsunaga T. DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair. J. Biol. Chem. 277:2002;1637-1640.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1637-1640
    • Wakasugi, M.1    Kawashima, A.2    Morioka, H.3    Linn, S.4    Sancar, A.5    Mori, T.6    Nikaido, O.7    Matsunaga, T.8
  • 352
    • 0033603338 scopus 로고    scopus 로고
    • Order of assembly of human DNA repair excision nuclease
    • Wakasugi M., Sancar A. Order of assembly of human DNA repair excision nuclease. J. Biol. Chem. 274:1999;18759-18768.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18759-18768
    • Wakasugi, M.1    Sancar, A.2
  • 353
    • 0035805554 scopus 로고    scopus 로고
    • Damaged DNA-binding protein DDB stimulates the excision of cyclobutane pyrimidine dimers in vitro in concert with XPA and replication protein A
    • Wakasugi M., Shimizu M., Morioka H., Linn S., Nikaido O., Matsunaga T. Damaged DNA-binding protein DDB stimulates the excision of cyclobutane pyrimidine dimers in vitro in concert with XPA and replication protein A. J. Biol. Chem. 276:2001;15434-15440.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15434-15440
    • Wakasugi, M.1    Shimizu, M.2    Morioka, H.3    Linn, S.4    Nikaido, O.5    Matsunaga, T.6
  • 354
    • 0033548444 scopus 로고    scopus 로고
    • The topoisomerase-related function gene TRF4 affects cellular sensitivity to the antitumor agent camptothecin
    • Walowsky C., Fitzhugh D.J., Castano I.B., Ju J.Y., Levin N.A., Christman M.F. The topoisomerase-related function gene TRF4 affects cellular sensitivity to the antitumor agent camptothecin. J. Biol. Chem. 274:1999;7302-7308.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7302-7308
    • Walowsky, C.1    Fitzhugh, D.J.2    Castano, I.B.3    Ju, J.Y.4    Levin, N.A.5    Christman, M.F.6
  • 356
    • 0033546282 scopus 로고    scopus 로고
    • Specific binding of human MSH2. MSH6 mismatch-repair protein heterodimers to DNA incorporating thymine- or uracil-containing UV light photoproducts opposite mismatched bases
    • Wang H., Lawrence C.W., Li G.M., Hays J.B. Specific binding of human MSH2. MSH6 mismatch-repair protein heterodimers to DNA incorporating thymine- or uracil-containing UV light photoproducts opposite mismatched bases. J. Biol. Chem. 274:1999;16894-16900.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16894-16900
    • Wang, H.1    Lawrence, C.W.2    Li, G.M.3    Hays, J.B.4
  • 357
    • 0034693878 scopus 로고    scopus 로고
    • Regulation of cell death by the Abl tyrosine kinase
    • Wang J.Y. Regulation of cell death by the Abl tyrosine kinase. Oncogene. 19:2000;5643-5650.
    • (2000) Oncogene , vol.19 , pp. 5643-5650
    • Wang, J.Y.1
  • 358
    • 0034655991 scopus 로고    scopus 로고
    • BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures
    • Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J. BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures. Genes Dev. 14:2000a;927-939.
    • (2000) Genes Dev. , vol.14 , pp. 927-939
    • Wang, Y.1    Cortez, D.2    Yazdi, P.3    Neff, N.4    Elledge, S.J.5    Qin, J.6
  • 360
    • 0034604445 scopus 로고    scopus 로고
    • Pol kappa: A DNA polymerase required for sister chromatid cohesion
    • Wang Z., Castano I.B., De Las Penas A., Adams C., Christman M.F. Pol kappa: a DNA polymerase required for sister chromatid cohesion. Science. 289:2000b;774-779.
    • (2000) Science , vol.289 , pp. 774-779
    • Wang, Z.1    Castano, I.B.2    De Las Penas, A.3    Adams, C.4    Christman, M.F.5
  • 361
    • 0035920118 scopus 로고    scopus 로고
    • Identification of a p53 response element in the promoter region of the hMSH2 gene required for expression in A2780 ovarian cancer cells
    • Warnick C.T., Dabbas B., Ford C.D., Strait K.A. Identification of a p53 response element in the promoter region of the hMSH2 gene required for expression in A2780 ovarian cancer cells. J. Biol. Chem. 276:2001;27363-27370.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27363-27370
    • Warnick, C.T.1    Dabbas, B.2    Ford, C.D.3    Strait, K.A.4
  • 363
    • 0038497542 scopus 로고
    • A structure for deoxyribose nucleic acid
    • Watson J., Crick F. A structure for deoxyribose nucleic acid. Nature. 171:1953;737-738.
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.1    Crick, F.2
  • 364
    • 0029983394 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of a human cDNA encoding an Escherichia coli AlkB homolog, a protein involved in DNA alkylation damage repair
    • Wei Y.F., Carter K.C., Wang R.P., Shell B.K. Molecular cloning and functional analysis of a human cDNA encoding an Escherichia coli AlkB homolog, a protein involved in DNA alkylation damage repair. Nucleic Acids Res. 24:1996;931-937.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 931-937
    • Wei, Y.F.1    Carter, K.C.2    Wang, R.P.3    Shell, B.K.4
  • 365
    • 0025314841 scopus 로고
    • Mismatch-specific thymine DNA glycosylase and DNA polymerase beta mediate the correction of G.T mispairs in nuclear extracts from human cells
    • Wiebauer K., Jiricny J. Mismatch-specific thymine DNA glycosylase and DNA polymerase beta mediate the correction of G.T mispairs in nuclear extracts from human cells. Proc. Natl. Acad. Sci. U.S.A. 87:1990;5842-5845.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 5842-5845
    • Wiebauer, K.1    Jiricny, J.2
  • 367
    • 0035837587 scopus 로고    scopus 로고
    • The major human abasic endonuclease: Formation, consequences and repair of abasic lesions in DNA
    • Wilson D.M. 3rd, Barsky D. The major human abasic endonuclease: formation, consequences and repair of abasic lesions in DNA. Mutat. Res. 485:2001;283-307.
    • (2001) Mutat. Res. , vol.485 , pp. 283-307
    • Wilson D.M. III1    Barsky, D.2
  • 370
    • 0033513097 scopus 로고    scopus 로고
    • Mismatch repair processing of carcinogen-DNA adducts triggers apoptosis
    • Wu J., Gu L., Wang H., Geacintov N.E., Li G.-M. Mismatch repair processing of carcinogen-DNA adducts triggers apoptosis. Mol. Cell. Biol. 19:1999a;8292-8301.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8292-8301
    • Wu, J.1    Gu, L.2    Wang, H.3    Geacintov, N.E.4    Li, G.-M.5
  • 371
    • 0033574004 scopus 로고    scopus 로고
    • A role for FEN-1 in nonhomologous DNA end joining: The order of strand annealing and nucleolytic processing events
    • Wu X., Wilson T.E., Lieber M.R. A role for FEN-1 in nonhomologous DNA end joining: the order of strand annealing and nucleolytic processing events. Proc. Natl. Acad. Sci. U.S.A. 96:1999b;1303-1308.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1303-1308
    • Wu, X.1    Wilson, T.E.2    Lieber, M.R.3
  • 372
    • 0031845115 scopus 로고    scopus 로고
    • Identification, chromosomal mapping and tissue-specific expression of hREV3 encoding a putative human DNA polymerase zeta
    • Xiao W., Lechler T., Chow B.L., Fontanie T., Agustus M., Carter K.C., Wei Y.F. Identification, chromosomal mapping and tissue-specific expression of hREV3 encoding a putative human DNA polymerase zeta. Carcinogenesis. 19:1998;945-949.
    • (1998) Carcinogenesis , vol.19 , pp. 945-949
    • Xiao, W.1    Lechler, T.2    Chow, B.L.3    Fontanie, T.4    Agustus, M.5    Carter, K.C.6    Wei, Y.F.7
  • 373
    • 0037102275 scopus 로고    scopus 로고
    • Phosphorylation of serine 1387 in Brca1 is specifically required for the ATM-mediated S-phase checkpoint after ionizing irradiation
    • Xu B., O'Donnell A.H., Kim S.T., Kastan M.B. Phosphorylation of serine 1387 in Brca1 is specifically required for the ATM-mediated S-phase checkpoint after ionizing irradiation. Cancer Res. 62:2002;4588-4591.
    • (2002) Cancer Res. , vol.62 , pp. 4588-4591
    • Xu, B.1    O'Donnell, A.H.2    Kim, S.T.3    Kastan, M.B.4
  • 374
    • 0034235906 scopus 로고    scopus 로고
    • Complementation of defective translesion synthesis and UV light sensitivity in xeroderma pigmentosum variant cells by human and mouse DNA polymerase eta
    • Yamada A., Masutani C., Iwai S., Hanaoka F. Complementation of defective translesion synthesis and UV light sensitivity in xeroderma pigmentosum variant cells by human and mouse DNA polymerase eta. Nucleic Acids Res. 28:2000;2473-2480.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2473-2480
    • Yamada, A.1    Masutani, C.2    Iwai, S.3    Hanaoka, F.4
  • 375
    • 0030811508 scopus 로고    scopus 로고
    • Selective recognition of a cisplatin-DNA adduct by human mismatch repair proteins
    • Yamada M., O'Regan E., Brown R., Karran P. Selective recognition of a cisplatin-DNA adduct by human mismatch repair proteins. Nucleic Acids Res. 25:1997;491-496.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 491-496
    • Yamada, M.1    O'Regan, E.2    Brown, R.3    Karran, P.4
  • 376
    • 0242311016 scopus 로고    scopus 로고
    • RNA polymerase II stalled on a DNA template during transcription elongation is ubiquitinated and the ubiquitination facilitates displacement of the elongation complex
    • Yang L.Y., Jiang H., Rangel K.M. RNA polymerase II stalled on a DNA template during transcription elongation is ubiquitinated and the ubiquitination facilitates displacement of the elongation complex. Int. J. Oncol. 22:2003;683-689.
    • (2003) Int. J. Oncol. , vol.22 , pp. 683-689
    • Yang, L.Y.1    Jiang, H.2    Rangel, K.M.3
  • 377
    • 0020644782 scopus 로고
    • 6-methylguanine in DNA by demethylation is lacking in Mer- human tumor cell strains
    • 6-methylguanine in DNA by demethylation is lacking in Mer- human tumor cell strains. Carcinogenesis. 4:1983;199-205.
    • (1983) Carcinogenesis , vol.4 , pp. 199-205
    • Yarosh, D.B.1    Foote, R.S.2    Mitra, S.3    Day R.S. III4
  • 378
    • 0034737426 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA
    • Yokoi M., Masutani C., Maekawa T., Sugasawa K., Ohkuma Y., Hanaoka F. The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA. J. Biol. Chem. 275:2000;9870-9875.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9870-9875
    • Yokoi, M.1    Masutani, C.2    Maekawa, T.3    Sugasawa, K.4    Ohkuma, Y.5    Hanaoka, F.6
  • 386
    • 0035865399 scopus 로고    scopus 로고
    • A role for p53 in base excision repair
    • Zhou J., Ahn J., Wilson S.H., Prives C. A role for p53 in base excision repair. EMBO J. 20:2001a;914-923.
    • (2001) EMBO J. , vol.20 , pp. 914-923
    • Zhou, J.1    Ahn, J.2    Wilson, S.H.3    Prives, C.4
  • 388
    • 0037080675 scopus 로고    scopus 로고
    • Regulation of ATR substrate selection by Rad17-dependent loading of Rad9 complexes onto chromatin
    • Zou L., Cortez D., Elledge S.J. Regulation of ATR substrate selection by Rad17-dependent loading of Rad9 complexes onto chromatin. Genes Dev. 16:2002;198-208.
    • (2002) Genes Dev. , vol.16 , pp. 198-208
    • Zou, L.1    Cortez, D.2    Elledge, S.J.3


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