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Volumn 50, Issue 11, 2011, Pages 1901-1909

Assembly of the base excision repair complex on abasic DNA and role of adenomatous polyposis coli on its functional activity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOMATOUS POLYPOSIS COLI; BASE EXCISION REPAIRS; DNA LIGASES; DNA REPAIR; ESSENTIAL COMPONENT; FUNCTIONAL ACTIVITIES; IN-VIVO; MULTIPLE COMPONENTS; REPAIR PROCESS; WILD TYPES;

EID: 79952805997     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi102000q     Document Type: Article
Times cited : (21)

References (58)
  • 1
    • 0033520969 scopus 로고    scopus 로고
    • Quality control by DNA repair
    • Lindahl, T. and Wood, R. D. (1999) Quality control by DNA repair Science 286, 1897-1905 (Pubitemid 129515891)
    • (1999) Science , vol.286 , Issue.5446 , pp. 1897-1905
    • Lindahl, T.1    Wood, R.D.2
  • 2
    • 85015066476 scopus 로고    scopus 로고
    • DNA damage and repair
    • DOI 10.1038/nature01408
    • Friedberg, E. C. (2003) DNA damage and repair Nature 421, 436-440 (Pubitemid 36157951)
    • (2003) Nature , vol.421 , Issue.6921 , pp. 436-440
    • Friedberg, E.C.1
  • 3
    • 3242881500 scopus 로고    scopus 로고
    • The cellular response to general and programmed DNA double strand breaks
    • DOI 10.1016/j.dnarep.2004.06.001, PII S1568786404001752
    • Bassing, C. H. and Alt, F. W. (2004) The cellular response to general and programmed DNA double strand breaks DNA Repair 3, 781-796 (Pubitemid 38997922)
    • (2004) DNA Repair , vol.3 , Issue.8-9 , pp. 781-796
    • Bassing, C.H.1    Alt, F.W.2
  • 4
    • 1942469956 scopus 로고    scopus 로고
    • MGMT: Its role in cancer aetiology and cancer therapeutics
    • Gerson, S. L. (2004) MGMT: Its role in cancer aetiology and cancer therapeutics Nat. Rev. Cancer 4, 296-307 (Pubitemid 38525285)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.4 , pp. 296-307
    • Gerson, S.L.1
  • 5
    • 3943107573 scopus 로고    scopus 로고
    • Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints
    • DOI 10.1146/annurev.biochem.73.011303.073723
    • Sancar, A., Lindsey-Boltz, L. A., Unsal-Kaçmaz, K., and Linn, S. (2004) Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints Annu. Rev. Biochem. 73, 39-85 (Pubitemid 39050363)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 39-85
    • Sancar, A.1    Lindsey-Boltz, L.A.2    Unsal-Kacmaz, K.3    Linn, S.4
  • 6
    • 0242442569 scopus 로고    scopus 로고
    • Dna Mismatch Repair: Molecular Mechanisms and Biological Function
    • DOI 10.1146/annurev.micro.57.030502.090847
    • Schofield, M. J. and Hsieh, P. (2003) DNA mismatch repair: Molecular mechanisms and biological function Annu. Rev. Microbiol. 57, 579-608 (Pubitemid 37406637)
    • (2003) Annual Review of Microbiology , vol.57 , pp. 579-608
    • Schofield, M.J.1    Hsieh, P.2
  • 7
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • DOI 10.1038/362709a0
    • Lindahl, T. (1993) Instability and decay of the primary structure of DNA Nature 362, 709-715 (Pubitemid 23125973)
    • (1993) Nature , vol.362 , Issue.6422 , pp. 709-715
    • Lindahl, T.1
  • 8
    • 0029892846 scopus 로고    scopus 로고
    • Evidence for an imino intermediate in the DNA polymerase β deoxyribose phosphate excision reaction
    • DOI 10.1074/jbc.271.30.17811
    • Piersen, C. E., Prasad, R., Wilson, S. H., and Lloyd, R. S. (1996) Evidence for an imino intermediate in the DNA polymerase β deoxyribose phosphate excision reaction J. Biol. Chem. 271, 17811-17815 (Pubitemid 26250757)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.30 , pp. 17811-17815
    • Piersen, C.E.1    Prasad, R.2    Wilson, S.H.3    Lloyd, R.S.4
  • 9
    • 0037215540 scopus 로고    scopus 로고
    • The stalling of transcription at abasic sites is highly mutagenic
    • DOI 10.1128/MCB.23.1.382-388.2003
    • Yu, S. L., Lee, S. K., Johnson, R. E., Prakash, L., and Prakash, S. (2003) The stalling of transcription at abasic sites is highly mutagenic Mol. Cell. Biol. 23, 382-388 (Pubitemid 36008528)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.1 , pp. 382-388
    • Yu, S.-L.1    Lee, S.-K.2    Johnson, R.E.3    Prakash, L.4    Prakash, S.5
  • 10
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair
    • Matsumoto, Y. and Kim, K. (1995) Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair Science 269, 699-702
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 11
    • 0032502675 scopus 로고    scopus 로고
    • Involvement of flap endonuclease 1 in base excision DNA repair
    • DOI 10.1074/jbc.273.15.8842
    • Kim, K., Biade, S., and Matsumoto, Y. (1998) Involvement of flap endonuclease 1 in base excision DNA repair J. Biol. Chem. 273, 8842-8848 (Pubitemid 28176165)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.15 , pp. 8842-8848
    • Kim, K.1    Biade, S.2    Matsumoto, Y.3
  • 12
    • 0035869014 scopus 로고    scopus 로고
    • Human DNA polymerase β initiates DNA synthesis during long-patch repair of reduced AP sites in DNA
    • DOI 10.1093/emboj/20.6.1477
    • Podlutsky, A. J., Dianova, I. I., Podust, V. N., Bohr, V. A., and Dianov, G. L. (2001) Human DNA polymerase β initiates DNA synthesis during long-patch repair of reduced AP sites in DNA EMBO J. 20, 1477-1482 (Pubitemid 32233987)
    • (2001) EMBO Journal , vol.20 , Issue.6 , pp. 1477-1482
    • Podlutsky, A.Ja.1    Dianova, I.I.2    Podust, V.N.3    Bohr, V.A.4    Dianov, G.L.5
  • 13
    • 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)
    • DOI 10.1093/emboj/16.11.3341
    • Klungland, A. and Lindahl, T. (1997) Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN1) EMBO J. 16, 3341-3348 (Pubitemid 27234971)
    • (1997) EMBO Journal , vol.16 , Issue.11 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 14
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase β and the XRCC1 protein
    • Kubota, Y., Nash, R. A., Klungland, A., Schär, P., Barnes, D. E., and Lindahl, T. (1996) Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase β and the XRCC1 protein EMBO J. 15, 6662-6670 (Pubitemid 26413798)
    • (1996) EMBO Journal , vol.15 , Issue.23 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schar, P.4    Barnes, D.E.5    Lindahl, T.6
  • 15
    • 0028675314 scopus 로고
    • Reconstitution of the DNA base excision-repair pathway
    • Dianov, G. and Lindahl, T. (1994) Reconstitution of the DNA base excision-repair pathway Curr. Biol. 4, 1069-1076 (Pubitemid 124001593)
    • (1994) Current Biology , vol.4 , Issue.12 , pp. 1069-1076
    • Dianov, G.1    Lindahl, T.2
  • 16
    • 0035940441 scopus 로고    scopus 로고
    • Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair
    • DOI 10.1021/bi011117i
    • Dianova, I. I., Bohr, V. A., and Dianov, G. L. (2001) Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair Biochemistry 40, 12639-12644 (Pubitemid 32979716)
    • (2001) Biochemistry , vol.40 , Issue.42 , pp. 12639-12644
    • Dianova, I.I.1    Bohr, V.A.2    Dianov, G.L.3
  • 17
    • 34247128593 scopus 로고    scopus 로고
    • Human base excision repair complex is physically associated to DNA replication and cell cycle regulatory proteins
    • DOI 10.1093/nar/gkl1159
    • Parlanti, E., Locatelli, G., Maga, G., and Dogliotti, E. (2007) Human base excision repair complex is physically associated to DNA replication and cell cycle regulatory proteins Nucleic Acids Res. 35, 1569-1577 (Pubitemid 46592877)
    • (2007) Nucleic Acids Research , vol.35 , Issue.5 , pp. 1569-1577
    • Parlanti, E.1    Locatelli, G.2    Maga, G.3    Dogliotti, E.4
  • 18
    • 0028966181 scopus 로고
    • DNA polymerase β conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract
    • Singhal, R. K., Prasad, R., and Wilson, S. H. (1995) DNA polymerase β conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract J. Biol. Chem. 270, 949-957
    • (1995) J. Biol. Chem. , vol.270 , pp. 949-957
    • Singhal, R.K.1    Prasad, R.2    Wilson, S.H.3
  • 19
    • 0032510962 scopus 로고    scopus 로고
    • Human DNA polymerase β deoxyribose phosphate lyase: Substrate specificity and catalytic mechanism
    • DOI 10.1074/jbc.273.24.15263
    • Prasad, R., Beard, W. A., Strauss, P. R., and Wilson, S. H. (1998) Human DNA polymerase β deoxyribose phosphate lyase. Substrate specificity and catalytic mechanism J. Biol. Chem. 273, 15263-15270 (Pubitemid 28272828)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.24 , pp. 15263-15270
    • Prasad, R.1    Beard, W.A.2    Strauss, P.R.3    Wilson, S.H.4
  • 20
    • 77955016886 scopus 로고    scopus 로고
    • Conformational transitions in human AP endonuclease 1 and its active site mutant during abasic site repair
    • Kanazhevskaya, L. Y., Koval, V. V., Zharkov, D. O., Strauss, P. R., and Fedorova, O. S. (2010) Conformational transitions in human AP endonuclease 1 and its active site mutant during abasic site repair Biochemistry 49, 6451-6461
    • (2010) Biochemistry , vol.49 , pp. 6451-6461
    • Kanazhevskaya, L.Y.1    Koval, V.V.2    Zharkov, D.O.3    Strauss, P.R.4    Fedorova, O.S.5
  • 21
    • 58549101715 scopus 로고    scopus 로고
    • Enzymatic mechanism of human apurinic/apyrimidinic endonuclease against a THF AP site model substrate
    • Mundle, S. T., Delaney, J. C., Essigmann, J. M., and Strauss, P. R. (2009) Enzymatic mechanism of human apurinic/apyrimidinic endonuclease against a THF AP site model substrate Biochemistry 48, 19-26
    • (2009) Biochemistry , vol.48 , pp. 19-26
    • Mundle, S.T.1    Delaney, J.C.2    Essigmann, J.M.3    Strauss, P.R.4
  • 22
    • 0030018848 scopus 로고    scopus 로고
    • Specific interaction of DNA polymerase β and DNA ligase I in a multiprotein base excision repair complex from bovine testis
    • DOI 10.1074/jbc.271.27.16000
    • Prasad, R., Singhal, R. K., Srivastava, D. K., Molina, J. T., Tomkinson, A. E., and Wilson, S. H. (1996) Specific interaction of DNA polymerase β and DNA ligase I in a multiprotein base excision repair complex from bovine testis J. Biol. Chem. 271, 16000-16007 (Pubitemid 26236212)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.27 , 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
  • 23
    • 0037163025 scopus 로고    scopus 로고
    • Direct interaction between mammalian DNA polymerase β and proliferating cell nuclear antigen
    • DOI 10.1074/jbc.M201497200
    • Kedar, P. S., Kim, S. J., Robertson, A., Hou, E., Prasad, R., Horton, J. K., and Wilson, S. H. (2002) Direct interaction between mammalian DNA polymerase β and proliferating cell nuclear antigen J. Biol. Chem. 277, 31115-31123 (Pubitemid 34970817)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.34 , pp. 31115-31123
    • Kedar, P.S.1    Kim, S.-J.2    Robertson, A.3    Hou, E.4    Prasad, R.5    Horton, J.K.6    Wilson, S.H.7
  • 24
    • 33845935041 scopus 로고    scopus 로고
    • Mechanism of adenomatous polyposis coli (APC)-mediated blockage of long-patch base excision repair
    • DOI 10.1021/bi0607958
    • Jaiswal, A. S., Balusu, R., Armas, M. L., Kundu, C. N., and Narayan, S. (2006) Mechanism of adenomatous polyposis coli (APC)-mediated blockage of long-patch base excision repair Biochemistry 45, 15903-15914 (Pubitemid 46032511)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15903-15914
    • Jaiswal, A.S.1    Balusu, R.2    Armas, M.L.3    Kundu, C.N.4    Narayan, S.5
  • 25
    • 14844310303 scopus 로고    scopus 로고
    • Tumor suppressor APC blocks DNA polymerase β-dependent strand displacement synthesis during long patch but not short patch base excision repair and increases sensitivity to methylmethane sulfonate
    • DOI 10.1074/jbc.M409200200
    • Narayan, S., Jaiswal, A. S., and Balusu, R. (2005) Tumor suppressor APC blocks DNA polymerase-β-dependent strand displacement synthesis during long patch but not short patch base excision repair and increases sensitivity to methylmethane sulfonate J. Biol. Chem. 280, 6942-6949 (Pubitemid 40341250)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 6942-6949
    • Narayan, S.1    Jaiswal, A.S.2    Balusu, R.3
  • 26
    • 37149051581 scopus 로고    scopus 로고
    • Structure/function analysis of the interaction of adenomatous polyposis coli with DNA polymerase β and its implications for base excision repair
    • DOI 10.1021/bi701632e
    • Balusu, R., Jaiswal, A. S., Armas, M. L., Bloom, L. B., and Narayan, S. (2007) Structure/function analysis of the interaction of adenomatous polyposis coli (APC) with DNA polymerase β and its implications for base excision repair Biochemistry 46, 13961-13974 (Pubitemid 350253072)
    • (2007) Biochemistry , vol.46 , Issue.49 , pp. 13961-13974
    • Balusu, R.1    Jaiswal, A.S.2    Armas, M.L.3    Kundu, C.N.4    Bloom, L.B.5    Narayan, S.6
  • 27
    • 77951895418 scopus 로고    scopus 로고
    • Probing conformational changes in Ape1 during the progression of base excision repair
    • Yu, E., Gaucher, S. P., and Hadi, M. Z. (2010) Probing conformational changes in Ape1 during the progression of base excision repair Biochemistry 49, 3786-3796
    • (2010) Biochemistry , vol.49 , pp. 3786-3796
    • Yu, E.1    Gaucher, S.P.2    Hadi, M.Z.3
  • 28
    • 13544261768 scopus 로고    scopus 로고
    • DNA polymerase β and flap endonuclease 1 enzymatic specificities sustain DNA synthesis for long patch base excision repair
    • DOI 10.1074/jbc.M412922200
    • Liu, Y., Beard, W. A., Shock, D. D., Prasad, R., Hou, E. W., and Wilson, S. H. (2005) DNA polymerase β and flap endonuclease 1 enzymatic specificities sustain DNA synthesis for long patch base excision repair J. Biol. Chem. 280, 3665-3674 (Pubitemid 40223834)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.5 , pp. 3665-3674
    • Lin, Y.1    Beard, W.A.2    Shock, D.D.3    Prasad, R.4    Hou, E.W.5    Wilson, S.H.6
  • 30
    • 1942512288 scopus 로고    scopus 로고
    • Role of APC and DNA mismatch repair genes in the development of colorectal cancers
    • Narayan, S. and Roy, D. (2003) Role of APC and DNA mismatch repair genes in the development of colorectal cancers Mol. Cancer 2, 41
    • (2003) Mol. Cancer , vol.2 , pp. 41
    • Narayan, S.1    Roy, D.2
  • 31
    • 25444448653 scopus 로고    scopus 로고
    • Involvement of adenomatous polyposis coli in colorectal tumorigenesis
    • Jaiswal, A. S., Balusu, R., and Narayan, S. (2005) Involvement of adenomatous polyposis coli in colorectal tumorigenesis Front. Biosci. 10, 1118-1134
    • (2005) Front. Biosci. , vol.10 , pp. 1118-1134
    • Jaiswal, A.S.1    Balusu, R.2    Narayan, S.3
  • 32
    • 0035496104 scopus 로고    scopus 로고
    • APC, signal transduction and genetic instability in colorectal cancer
    • Fodde, R., Smits, R., and Clevers, H. (2001) APC, signal transduction and genetic instability in colorectal cancer Nat. Rev. Cancer 1, 55-67 (Pubitemid 33741881)
    • (2001) Nature Reviews Cancer , vol.1 , Issue.1 , pp. 55-67
    • Fodde, R.1    Smits, R.2    Clevers, H.3
  • 33
    • 8744311619 scopus 로고    scopus 로고
    • APC at a glance
    • DOI 10.1242/jcs.01313
    • Näthke, I. (2004) APC at a glance J. Cell Sci. 117, 4873-4875 (Pubitemid 39517503)
    • (2004) Journal of Cell Science , vol.117 , Issue.21 , pp. 4873-4875
    • Nathke, I.1
  • 34
    • 53249091946 scopus 로고    scopus 로고
    • A novel function of adenomatous polyposis coli (APC) in regulating DNA repair
    • Jaiswal, A. S. and Narayan, S. (2008) A novel function of adenomatous polyposis coli (APC) in regulating DNA repair Cancer Lett. 271, 272-280
    • (2008) Cancer Lett. , vol.271 , pp. 272-280
    • Jaiswal, A.S.1    Narayan, S.2
  • 35
    • 0023835505 scopus 로고
    • A high-efficiency HeLa cell nuclear transcription extract
    • Shapiro, D. J., Sharp, P. A., Wahli, W. W., and Keller, M. J. (1988) A high-efficiency HeLa cell nuclear transcription extract DNA 7, 47-55 (Pubitemid 18044633)
    • (1988) DNA , vol.7 , Issue.1 , pp. 47-55
    • Shapiro, D.J.1    Sharp, P.A.2    Wahli, W.W.3    Keller, M.J.4
  • 36
    • 35148859739 scopus 로고    scopus 로고
    • Adenomatous polyposis coli-mediated hypersensitivity of mouse embryonic fibroblast cell lines to methylmethane sulfonate treatment: Implication of base excision repair pathways
    • DOI 10.1093/carcin/bgm125
    • Kundu, C. N., Balusu, R., Jaiswal, A. S., and Narayan, S. (2007) Adenomatous polyposis coli-mediated hypersensitivity of mouse embryonic fibroblast cell lines to methylmethane sulfonate treatment: Implication of base excision repair Carcinogenesis 28, 2089-2095 (Pubitemid 47543367)
    • (2007) Carcinogenesis , vol.28 , Issue.10 , pp. 2089-2095
    • Kundu, C.N.1    Balusu, R.2    Jaiswal, A.S.3    Narayan, S.4
  • 37
    • 70350236645 scopus 로고    scopus 로고
    • Amino acid Asp181 of 5′-flap endonuclease 1 is a useful target for chemotherapeutic development
    • Panda, H., Jaiswal, A. S., Corsino, P. E., Armas, M. L., Law, B. K., and Narayan, S. (2009) Amino acid Asp181 of 5′-flap endonuclease 1 is a useful target for chemotherapeutic development Biochemistry 48, 9952-9958
    • (2009) Biochemistry , vol.48 , pp. 9952-9958
    • Panda, H.1    Jaiswal, A.S.2    Corsino, P.E.3    Armas, M.L.4    Law, B.K.5    Narayan, S.6
  • 38
    • 0034616199 scopus 로고    scopus 로고
    • Mechanism whereby proliferating cell nuclear antigen stimulates flap endonuclease 1
    • DOI 10.1074/jbc.275.14.10498
    • Tom, S., Henricksen, L. A., and Bambara, R. A. (2000) Mechanism whereby proliferating cell nuclear antigen stimulates flap endonuclease 1 J. Biol. Chem. 275, 10498-10505 (Pubitemid 30202112)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 10498-10505
    • Tom, S.1    Henricksen, L.A.2    Bambara, R.A.3
  • 39
    • 0029885134 scopus 로고    scopus 로고
    • Processing of branched DNA intermediates by a complex of human FEN-1 and PCNA
    • DOI 10.1093/nar/24.11.2036
    • Wu, X., Li, J., Li, X., Hsieh, C. L., Burgers, P. M., and Lieber, M. R. (1996) Processing of branched DNA intermediates by a complex of human FEN-1 and PCNA Nucleic Acids Res. 24, 2036-2043 (Pubitemid 26174544)
    • (1996) Nucleic Acids Research , vol.24 , Issue.11 , pp. 2036-2043
    • Wu, X.1    Li, J.2    Li, X.3    Hsieh, C.-L.4    Burgers, P.M.J.5    Lieber, M.R.6
  • 40
    • 0032515143 scopus 로고    scopus 로고
    • Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product
    • DOI 10.1074/jbc.273.46.30352
    • Masuda, Y., Bennett, R. A., and Demple, B. (1998) Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product J. Biol. Chem. 273, 30352-30359 (Pubitemid 28545505)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.46 , pp. 30352-30359
    • Masuda, Y.1    Bennett, R.A.O.2    Demple, B.3
  • 41
    • 0034734377 scopus 로고    scopus 로고
    • Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: The 3' ends justify the means
    • DOI 10.1016/S0921-8777(00)00028-8, PII S0921877700000288
    • Mol, C. D., Hosfield, D. J., and Tainer, J. A. (2000) Abasic site recognition by two apurinic/apyrimidinic endonuclease families in DNA base excision repair: The 3′ ends justify the means Mutat. Res. 460, 211-229 (Pubitemid 30628592)
    • (2000) Mutation Research - DNA Repair , vol.460 , Issue.3-4 , pp. 211-229
    • Mol, C.D.1    Hosfield, D.J.2    Tainer, J.A.3
  • 43
    • 0038681010 scopus 로고    scopus 로고
    • The Werner syndrome protein stimulates DNA polymerase β strand displacement synthesis via its helicase activity
    • DOI 10.1074/jbc.M213103200
    • Harrigan, J. A., Opresko, P. L., von Kobbe, C., Kedar, P. S., Prasad, R., Wilson, S. H., and Bohr, V. A. (2003) The Werner syndrome protein stimulates DNA polymerase β strand displacement synthesis via its helicase activity J. Biol. Chem. 278, 22686-22695 (Pubitemid 36833256)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.25 , pp. 22686-22695
    • Harrigan, J.A.1    Opresko, P.L.2    Von Kobbe, C.3    Kedar, P.S.4    Prasad, R.5    Wilson, S.H.6    Bohr, V.A.7
  • 44
    • 32644449296 scopus 로고    scopus 로고
    • The Werner syndrome protein operates in base excision repair and cooperates with DNA polymerase β
    • DOI 10.1093/nar/gkj475
    • Harrigan, J. A., Wilson, D. M., Prasad, R., Opresko, P. L., Beck, G., May, A., Wilson, S. H., and Bohr, V. A. (2006) The Werner syndrome protein operates in base excision repair and cooperates with DNA polymerase β Nucleic Acids Res. 34, 745-754 (Pubitemid 43240260)
    • (2006) Nucleic Acids Research , vol.34 , Issue.2 , pp. 745-754
    • Harrigan, J.A.1    Wilson III, D.M.2    Prasad, R.3    Opresko, P.L.4    Beck, G.5    May, A.6    Wilson, S.H.7    Bohr, V.A.8
  • 45
    • 0034720734 scopus 로고    scopus 로고
    • Base excision repair is impaired in mammalian cells lacking poly(ADP- ribose) polymerase-1
    • DOI 10.1021/bi0003442
    • Dantzer, F., de La Rubia, G., Menissier-De Murcia, J., Hostomsky, Z., de Murcia, G., and Schreiber, V. (2000) Base excision repair is impaired in mammalian cells lacking poly(ADP-ribose) polymerase-1 Biochemistry 39, 7559-7569 (Pubitemid 30422075)
    • (2000) Biochemistry , vol.39 , Issue.25 , pp. 7559-7569
    • Dantzer, F.1    De La Rubia, G.2    Menissier-De Murcia, J.3    Hostomsky, Z.4    De Murcia, G.5    Schreiber, V.6
  • 46
    • 0035980003 scopus 로고    scopus 로고
    • DNA polymerase β-mediated long patch base excision repair. Poly(ADP-ribose)polymerase-1 stimulates strand displacement DNA synthesis
    • Prasad, R., Lavrik, O. I., Kim, S. J., Kedar, P., Yang, X. P., Vande Berg, B. J., and Wilson, S. H. (2001) DNA polymerase β-mediated long patch base excision repair. Poly(ADP-ribose)polymerase-1 stimulates strand displacement DNA synthesis J. Biol. Chem. 276, 32411-32414
    • (2001) J. Biol. Chem. , vol.276 , pp. 32411-32414
    • Prasad, R.1    Lavrik, O.I.2    Kim, S.J.3    Kedar, P.4    Yang, X.P.5    Vande Berg, B.J.6    Wilson, S.H.7
  • 47
    • 0032538561 scopus 로고    scopus 로고
    • Replication protein A stimulates long patch DNA base excision repair
    • DOI 10.1074/jbc.273.42.27492
    • DeMott, M. S., Zigman, S., and Bambara, R. A. (1998) Replication protein A stimulates long patch DNA base excision repair J. Biol. Chem. 273, 27492-27498 (Pubitemid 28500468)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.42 , pp. 27492-27498
    • DeMott, M.S.1    Zigman, S.2    Bambara, R.A.3
  • 48
    • 0033955346 scopus 로고    scopus 로고
    • XRCC1 keeps DNA from getting stranded
    • DOI 10.1016/S0921-8777(99)00058-0, PII S0921877799000580
    • Thompson, L. H. and West, M. G. (2000) XRCC1 keeps DNA from getting stranded Mutat. Res. 459, 1-18 (Pubitemid 30085463)
    • (2000) Mutation Research - DNA Repair , vol.459 , Issue.1 , pp. 1-18
    • Thompson, L.H.1    West, M.G.2
  • 54
    • 48949112430 scopus 로고    scopus 로고
    • Truncation mutations abolish chromatin-associated activities of adenomatous polyposis coli
    • Kouzmenko, A. P., Takeyama, K., Kawasaki, Y., Akiyama, T., and Kato, S. (2008) Truncation mutations abolish chromatin-associated activities of adenomatous polyposis coli Oncogene 27, 4888-4899
    • (2008) Oncogene , vol.27 , pp. 4888-4899
    • Kouzmenko, A.P.1    Takeyama, K.2    Kawasaki, Y.3    Akiyama, T.4    Kato, S.5
  • 55
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): A dancer with many partners
    • DOI 10.1242/jcs.00653
    • Maga, G. and Hubscher, U. (2003) Proliferating cell nuclear antigen (PCNA): A dancer with many partners J. Cell Sci. 116, 3051-3060 (Pubitemid 37038954)
    • (2003) Journal of Cell Science , vol.116 , Issue.15 , pp. 3051-3060
    • Maga, G.1    Hubscher, U.2
  • 56
    • 0032539979 scopus 로고    scopus 로고
    • Different DNA polymerases are involved in the short- and long-patch base excision repair in mammalian cells
    • DOI 10.1021/bi972999h
    • Fortini, P., Pascucci, B., Parlanti, E., Sobol, R. W., Wilson, S. H., and Dogliotti, E. (1998) Different DNA polymerases are involved in the short- and long-patch base excision repair in mammalian cells Biochemistry 37, 3575-3580 (Pubitemid 28162911)
    • (1998) Biochemistry , vol.37 , Issue.11 , pp. 3575-3580
    • Fortini, P.1    Pascucci, B.2    Parlanti, E.3    Sobol, R.W.4    Wilson, S.H.5    Dogliotti, E.6
  • 57
    • 0035225868 scopus 로고    scopus 로고
    • Molecular mechanism of PCNA-dependent base excision repair
    • PII S0079660301680954, Base Excesion Repair
    • Matsumoto, Y. (2001) Molecular mechanism of PCNA-dependent base excision repair Prog. Nucleic Acid Res. Mol. Biol. 68, 129-138 (Pubitemid 33804658)
    • (2001) Progress in Nucleic Acid Research and Molecular Biology , vol.68 , pp. 129-138
    • Matsumoto, Y.1
  • 58
    • 0342350255 scopus 로고    scopus 로고
    • Interaction between PCNA and DNA ligase I is critical for joining of Okazaki fragments and long-patch base-excision repair
    • DOI 10.1016/S0960-9822(00)00619-9
    • Levin, D. S., McKenna, A. E., Motycka, T. A., Matsumoto, Y., and Tomkinson, A. E. (2000) Interaction between PCNA and DNA ligase I is critical for joining of Okazaki fragments and long-patch base-excision repair Curr. Biol. 10, 919-922 (Pubitemid 30647620)
    • (2000) Current Biology , vol.10 , Issue.15 , pp. 919-922
    • Levin, D.S.1    McKenna, A.E.2    Motycka, T.A.3    Matsumoto, Y.4    Tomkinson, A.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.