메뉴 건너뛰기




Volumn 51, Issue 6, 2012, Pages 1306-1321

Conformational dynamics of abasic DNA upon interactions with AP endonuclease 1 revealed by stopped-flow fluorescence analysis

Author keywords

[No Author keywords available]

Indexed keywords

2-AMINOPURINE; ALKYLATING AGENTS; AMINO ACID RESIDUES; AP-SITES; CATALYTIC CYCLES; CONFORMATIONAL DYNAMICS; CONFORMATIONAL FLEXIBILITY; CONFORMATIONAL TRANSITIONS; DNA LESIONS; DNA SUBSTRATES; ENDONUCLEASES; FLUORESCENCE ANALYSIS; FLUORESCENCE INTENSITIES; HUMAN CELLS; KINETIC SCHEME; MOLECULAR DYNAMICS SIMULATIONS; OXYGEN RADICAL; PHOSPHODIESTERS; REACTION STEPS; REAL TIME; SPECIFIC BINDING; STOPPED FLOW; STOPPED-FLOW TECHNIQUES; STRUCTURAL DISTORTIONS; TRP-FLUORESCENCE;

EID: 84856939661     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201444m     Document Type: Article
Times cited : (27)

References (66)
  • 1
  • 2
    • 0025936119 scopus 로고
    • Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E.coli xth (exonuclease III) mutants
    • Robson, C. N. and Hickson, I. D. (1991) Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants Nucleic Acids Res. 19, 5519-5523 (Pubitemid 21912949)
    • (1991) Nucleic Acids Research , vol.19 , Issue.20 , pp. 5519-5523
    • Robson, C.N.1    Hickson, I.D.2
  • 3
    • 0035837587 scopus 로고    scopus 로고
    • The major human abasic endonuclease: Formation, consequences and repair of abasic lesions in DNA
    • DOI 10.1016/S0921-8777(01)00063-5, PII S0921877701000635
    • Wilson, D. M., III and Barsky, D. (2001) The major human abasic endonuclease: Formation, consequences and repair of abasic lesions in DNA Mutat. Res. 485, 283-307 (Pubitemid 32406284)
    • (2001) Mutation Research - DNA Repair , vol.485 , Issue.4 , pp. 283-307
    • Wilson III, D.M.1    Barsky, D.2
  • 4
    • 27844501168 scopus 로고    scopus 로고
    • Molecular and biological roles of Ape1 protein in mammalian base excision repair
    • DOI 10.1016/j.dnarep.2005.09.004, PII S1568786405002557
    • Demple, B. and Sung, J. S. (2005) Molecular and biological roles of Ape1 protein in mammalian base excision repair DNA Repair 4, 1442-1449 (Pubitemid 41653305)
    • (2005) DNA Repair , vol.4 , Issue.12 , pp. 1442-1449
    • Demple, B.1    Sung, J.-S.2
  • 5
    • 0033152195 scopus 로고    scopus 로고
    • Endogenous apurinic/apyrimidinic sites in genomic DNA of mammalian tissues
    • Nakamura, J. and Swenberg, J. A. (1999) Endogenous apurinic/apyrimidinic sites in genomic DNA of mammalian tissues Cancer Res. 59, 2522-2526 (Pubitemid 29269091)
    • (1999) Cancer Research , vol.59 , Issue.11 , pp. 2522-2526
    • Nakamura, J.1    Swenberg, J.A.2
  • 6
    • 0037049975 scopus 로고    scopus 로고
    • Alternative nucleotide incision repair pathway for oxidative DNA damage
    • DOI 10.1038/415183a
    • Ischenko, A. A. and Saparbaev, M. K. (2002) Alternative nucleotide incision repair pathway for oxidative DNA damage Nature 415, 183-187 (Pubitemid 34059521)
    • (2002) Nature , vol.415 , Issue.6868 , pp. 183-187
    • Ischenko, A.A.1    Saparbaev, M.K.2
  • 7
    • 0025077481 scopus 로고
    • Redox regulation of fos and jun DNA-binding activity in vitro
    • Abate, C., Patel, L., Rauscher, F. J., III, and Curran, T. (1990) Redox regulation of fos and jun DNA-binding activity in vitro Science 249, 1157-1161
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher III, F.J.3    Curran, T.4
  • 8
    • 0026583944 scopus 로고
    • Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity
    • Xanthoudakis, S. and Curran, T. (1992) Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity EMBO J. 11, 653-665
    • (1992) EMBO J. , vol.11 , pp. 653-665
    • Xanthoudakis, S.1    Curran, T.2
  • 9
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis, S., Miao, G., Wang, F., Pan, Y. C., and Curran, T. (1992) Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme EMBO J. 11, 3323-3335
    • (1992) EMBO J. , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.C.4    Curran, T.5
  • 11
    • 0033570048 scopus 로고    scopus 로고
    • Ref-1 regulates the transactivation and pro-apoptotic functions of p53 in vivo
    • DOI 10.1093/emboj/18.20.5609
    • Gaiddon, C., Moorthy, N. C., and Prives, C. (1999) Ref-1 regulates the transactivation and pro-apoptotic functions of p53 in vivo EMBO J. 18, 5609-5621 (Pubitemid 29486380)
    • (1999) EMBO Journal , vol.18 , Issue.20 , pp. 5609-5621
    • Gaiddon, C.1    Moorthy, N.C.2    Prives, C.3
  • 13
    • 0034866372 scopus 로고    scopus 로고
    • Redox regulation of the DNA repair function of the human AP endonuclease Ape1/ref-1
    • Kelley, M. R. and Parsons, S. H. (2001) Redox regulation of the DNA repair function of the human AP endonuclease Ape1/ref-1 Antioxid. Redox Signaling 3, 671-683 (Pubitemid 32785989)
    • (2001) Antioxidants and Redox Signaling , vol.3 , Issue.4 , pp. 671-683
    • Kelley, M.R.1    Parsons, S.H.2
  • 14
    • 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
  • 15
    • 0030728449 scopus 로고    scopus 로고
    • The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites
    • DOI 10.1093/emboj/16.21.6548
    • Gorman, M. A., Morera, S., Rothwell, D. G., de La Fortelle, E., Mol, C. D., Tainer, J. A., Hickson, I. D., and Freemont, P. S. (1997) The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites EMBO J. 16, 6548-6558 (Pubitemid 27483279)
    • (1997) EMBO Journal , vol.16 , Issue.21 , pp. 6548-6558
    • Gorman, M.A.1    Morera, S.2    Rothwell, D.G.3    De La Fortelle, E.4    Mol, C.D.5    Tainer, J.A.6    Hickson, I.D.7    Freemont, P.S.8
  • 16
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 DNA repair and coordination
    • DOI 10.1038/35000249
    • Mol, C. D., Izumi, T., Mitra, S., and Tainer, J. A. (2000) DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination Nature 403, 451-456 (Pubitemid 30073097)
    • (2000) Nature , vol.403 , Issue.6768 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Talner, J.A.4
  • 17
    • 0035815108 scopus 로고    scopus 로고
    • Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: Implications for the catalytic mechanism
    • DOI 10.1006/jmbi.2001.4529
    • Beernink, P. T., Segelke, B. W., Hadi, M. Z., Erzberger, J. P., Wilson, D. M., III, and Rupp, B. (2001) Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: Implications for the catalytic mechanism J. Mol. Biol. 307, 1023-1034 (Pubitemid 33029950)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.4 , pp. 1023-1034
    • Beernink, P.T.1    Segelke, B.W.2    Hadi, M.Z.3    Erzberger, J.P.4    Wilson III, D.M.5    Rupp, B.6
  • 18
    • 0034607548 scopus 로고    scopus 로고
    • Mapping the protein-DNA interface and the metal-binding site of the major human apurinic/apyrimidinic endonuclease
    • Nguyen, L. H., Barsky, D., Erzberger, J. P., and Wilson, D. M., III (2000) Mapping the protein-DNA interface and the metal-binding site of the major human apurinic/apyrimidinic endonuclease J. Mol. Biol. 298, 447-459
    • (2000) J. Mol. Biol. , vol.298 , pp. 447-459
    • Nguyen, L.H.1    Barsky, D.2    Erzberger, J.P.3    Wilson III, D.M.4
  • 19
    • 0028923440 scopus 로고
    • Structure and function of the multifunctional DNA-repair enzyme exonuclease III
    • Mol, C. D., Kuo, C. F., Thayer, M. M., Cunningham, R. P., and Tainer, J. A. (1995) Structure and function of the multifunctional DNA-repair enzyme exonuclease III Nature 374, 381-386
    • (1995) Nature , vol.374 , pp. 381-386
    • Mol, C.D.1    Kuo, C.F.2    Thayer, M.M.3    Cunningham, R.P.4    Tainer, J.A.5
  • 20
    • 0030787013 scopus 로고    scopus 로고
    • What structural features determine repair enzyme specificity and mechanism in chemically modified DNA?
    • DOI 10.1021/tx970011e
    • Singer, B. and Hang, B. (1997) What structural features determine repair enzyme specificity and mechanism in chemically modified DNA? Chem. Res. Toxicol. 10, 713-732 (Pubitemid 27315104)
    • (1997) Chemical Research in Toxicology , vol.10 , Issue.7 , pp. 713-732
    • Singer, B.1    Hang, B.2
  • 21
    • 84961981834 scopus 로고    scopus 로고
    • Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases
    • DOI 10.1093/nar/26.11.2771
    • Erzberger, J. P., Barsky, D., Scharer, O. D., Colvin, M. E., and Wilson, D. M., III (1998) Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases Nucleic Acids Res. 26, 2771-2778 (Pubitemid 28297395)
    • (1998) Nucleic Acids Research , vol.26 , Issue.11 , pp. 2771-2778
    • Erzberger, J.P.1    Barsky, D.2    Scharer, O.D.3    Colvin, M.E.4    Wilson III, D.M.5
  • 22
    • 33645533295 scopus 로고    scopus 로고
    • Role of the tryptophan residue in the vicinity of the catalytic center of exonuclease III family AP endonucleases: AP site recognition mechanism
    • Kaneda, K., Sekiguchi, J., and Shida, T. (2006) Role of the tryptophan residue in the vicinity of the catalytic center of exonuclease III family AP endonucleases: AP site recognition mechanism Nucleic Acids Res. 34, 1552-1563
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1552-1563
    • Kaneda, K.1    Sekiguchi, J.2    Shida, T.3
  • 24
    • 34548276529 scopus 로고    scopus 로고
    • The DNA base excision repair protein Ape1/Ref-1 as a therapeutic and chemopreventive target
    • DOI 10.1016/j.mam.2007.04.005, PII S0098299707000350
    • Fishel, M. L. and Kelley, M. R. (2007) The DNA base excision repair protein Ape1/Ref-1 as a therapeutic and chemopreventive target Mol. Aspects Med. 28, 375-395 (Pubitemid 47331610)
    • (2007) Molecular Aspects of Medicine , vol.28 , Issue.3-4 , pp. 375-395
    • Fishel, M.L.1    Kelley, M.R.2
  • 25
    • 77956234314 scopus 로고    scopus 로고
    • Novel small-molecule inhibitor of apurinic/apyrimidinic endonuclease 1 blocks proliferation and reduces viability of glioblastoma cells
    • Bapat, A., Glass, L. S., Luo, M., Fishel, M. L., Long, E. C., Georgiadis, M. M., and Kelley, M. R. (2010) Novel small-molecule inhibitor of apurinic/apyrimidinic endonuclease 1 blocks proliferation and reduces viability of glioblastoma cells J. Pharmacol. Exp. Ther. 334, 988-998
    • (2010) J. Pharmacol. Exp. Ther. , vol.334 , pp. 988-998
    • Bapat, A.1    Glass, L.S.2    Luo, M.3    Fishel, M.L.4    Long, E.C.5    Georgiadis, M.M.6    Kelley, M.R.7
  • 26
    • 0029001186 scopus 로고
    • Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA
    • Wilson, D. M., III, Takeshita, M., Grollman, A. P., and Demple, B. (1995) Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA J. Biol. Chem. 270, 16002-16007
    • (1995) J. Biol. Chem. , vol.270 , pp. 16002-16007
    • Wilson III, D.M.1    Takeshita, M.2    Grollman, A.P.3    Demple, B.4
  • 27
    • 0031021533 scopus 로고    scopus 로고
    • Substrate binding by human apurinic/apyrimidinic endonuclease indicates a Briggs-Haldane mechanism
    • DOI 10.1074/jbc.272.2.1302
    • Strauss, P. R., Beard, W. A., Patterson, T. A., and Wilson, S. H. (1997) Substrate binding by human apurinic/apyrimidinic endonuclease indicates a Briggs-Haldane mechanism J. Biol. Chem. 272, 1302-1307 (Pubitemid 27034632)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.2 , pp. 1302-1307
    • Strauss, P.R.1    Beardt, W.A.2    Patterson, T.A.3    Wilson, S.H.4
  • 28
    • 4544362837 scopus 로고    scopus 로고
    • Novel role of tyrosine in catalysis by human AP endonuclease 1
    • DOI 10.1016/j.dnarep.2004.06.009, PII S1568786404001855
    • Mundle, S. T., Fattal, M. H., Melo, L. F., Coriolan, J. D., O'Regan, N. E., and Strauss, P. R. (2004) Novel role of tyrosine in catalysis by human AP endonuclease 1 DNA Repair 3, 1447-1455 (Pubitemid 39221742)
    • (2004) DNA Repair , vol.3 , Issue.11 , pp. 1447-1455
    • Mundle, S.T.1    Fattal, M.H.2    Melo, L.F.3    Coriolan, J.D.4    O'Regan, N.E.5    Strauss, P.R.6
  • 29
    • 1842735418 scopus 로고    scopus 로고
    • Human AP endonuclease (APE1) demonstrates endonucleolytic activity against AP sites in single-stranded DNA
    • DOI 10.1016/j.dnarep.2004.01.010, PII S1568786404000291
    • Marenstein, D. R., Wilson, D. M., III, and Teebor, G. W. (2004) Human AP endonuclease (APE1) demonstrates endonucleolytic activity against AP sites in single-stranded DNA DNA Repair 3, 527-533 (Pubitemid 38482027)
    • (2004) DNA Repair , vol.3 , Issue.5 , pp. 527-533
    • Marenstein, D.R.1    Wilson III, D.M.2    Teebor, G.W.3
  • 30
    • 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
  • 31
    • 35648950472 scopus 로고    scopus 로고
    • Pre-steady-state kinetic characterization of the AP endonuclease activity of human AP endonuclease 1
    • DOI 10.1074/jbc.M704341200
    • Maher, R. L. and Bloom, L. B. (2007) Pre-steady-state kinetic characterization of the AP endonuclease activity of human AP endonuclease 1 J. Biol. Chem. 282, 30577-30585 (Pubitemid 350035165)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.42 , pp. 30577-30585
    • Maher, R.L.1    Bloom, L.B.2
  • 32
    • 0031933081 scopus 로고    scopus 로고
    • Advances in transient-state kinetics
    • DOI 10.1016/S0958-1669(98)80089-X
    • Johnson, K. A. (1998) Advances in transient-state kinetics Curr. Opin. Biotechnol. 9, 87-89 (Pubitemid 28098320)
    • (1998) Current Opinion in Biotechnology , vol.9 , Issue.1 , pp. 87-89
    • Johnson, K.A.1
  • 33
    • 0037022175 scopus 로고    scopus 로고
    • Stopped-flow kinetic studies of the interaction between Escherichia coli Fpg protein and DNA substrates
    • DOI 10.1021/bi011524u
    • Fedorova, O. S., Nevinsky, G. A., Koval, V. V., Ishchenko, A. A., Vasilenko, N. L., and Douglas, K. T. (2002) Stopped-flow kinetic studies of the interaction between Escherichia coli Fpg protein and DNA substrates Biochemistry 41, 1520-1528 (Pubitemid 34112741)
    • (2002) Biochemistry , vol.41 , Issue.5 , pp. 1520-1528
    • Fedorova, O.S.1    Nevinsky, G.A.2    Koval, V.V.3    Ishchenko, A.A.4    Vasilenko, N.L.5    Douglas, K.T.6
  • 34
    • 2342487278 scopus 로고    scopus 로고
    • Pre-steady-state kinetics shows differences in processing of various DNA lesions by Escherichia coli formamidopyrimidine-DNA glycosylase
    • DOI 10.1093/nar/gkh237
    • Koval, V. V., Kuznetsov, N. A., Zharkov, D. O., Ishchenko, A. A., Douglas, K. T., Nevinsky, G. A., and Fedorova, O. S. (2004) Pre-steady-state kinetics shows differences in processing of various DNA lesions by Escherichia coli formamidopyrimidine-DNA glycosylase Nucleic Acids Res. 32, 926-935 (Pubitemid 38854695)
    • (2004) Nucleic Acids Research , vol.32 , Issue.3 , pp. 926-935
    • Koval, V.V.1    Kuznetsov, N.A.2    Zharkov, D.O.3    Ishchenko, A.A.4    Douglas, K.T.5    Nevinsky, G.A.6    Fedorova, O.S.7
  • 35
    • 76249089573 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Msh2-Msh6 DNA binding kinetics reveal a mechanism of targeting sites for DNA mismatch repair
    • Zhai, J. and Hingorani, M. M. (2010) Saccharomyces cerevisiae Msh2-Msh6 DNA binding kinetics reveal a mechanism of targeting sites for DNA mismatch repair Proc. Natl. Acad. Sci. U.S.A. 107, 680-685
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 680-685
    • Zhai, J.1    Hingorani, M.M.2
  • 37
    • 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
  • 38
    • 0035881038 scopus 로고    scopus 로고
    • Solution structure of an oligonucleotide containing an abasic site: Evidence for an unusual deoxyribose conformation
    • Hoehn, S. T., Turner, C. J., and Stubbe, J. (2001) Solution structure of an oligonucleotide containing an abasic site: Evidence for an unusual deoxyribose conformation Nucleic Acids Res. 29, 3413-3423 (Pubitemid 32799114)
    • (2001) Nucleic Acids Research , vol.29 , Issue.16 , pp. 3413-3423
    • Hoehn, S.T.1    Turner, C.J.2    Stubbe, J.3
  • 40
    • 0032546530 scopus 로고    scopus 로고
    • Thermodynamic consequences of an abasic lesion in duplex DNA are strongly dependent on base sequence
    • DOI 10.1021/bi9803372
    • Gelfand, C. A., Plum, G. E., Grollman, A. P., Johnson, F., and Breslauer, K. J. (1998) Thermodynamic consequences of an abasic lesion in duplex DNA are strongly dependent on base sequence Biochemistry 37, 7321-7327 (Pubitemid 28235215)
    • (1998) Biochemistry , vol.37 , Issue.20 , pp. 7321-7327
    • Gelfand, C.A.1    Plum, G.E.2    Grollman, A.P.3    Johnson, F.4    Breslauer, K.J.5
  • 41
    • 0029859713 scopus 로고    scopus 로고
    • Improved thermodynamic parameters and helix initiation factor to predict stability of DNA duplexes
    • DOI 10.1093/nar/24.22.4501
    • Sugimoto, N., Nakano, S., Yoneyama, M., and Honda, K. (1996) Improved thermodynamic parameters and helix initiation factor to predict stability of DNA duplexes Nucleic Acids Res. 24, 4501-4505 (Pubitemid 26388637)
    • (1996) Nucleic Acids Research , vol.24 , Issue.22 , pp. 4501-4505
    • Sugimoto, N.1    Nakano, S.-I.2    Yoneyama, M.3    Honda, K.-I.4
  • 42
    • 0037125947 scopus 로고    scopus 로고
    • Use of 2-aminopurine and tryptophan fluorescence as probes in kinetic analyses of DNA polymerase β
    • DOI 10.1021/bi025837g
    • Dunlap, C. A. and Tsai, M.-D. (2002) Use of 2-Aminopurine and Tryptophan Fluorescence as Probes in Kinetic Analyses of DNA Polymerase β Biochemistry 41, 11226-11235 (Pubitemid 35034025)
    • (2002) Biochemistry , vol.41 , Issue.37 , pp. 11226-11235
    • Dunlap, C.A.1    Tsai, M.-D.2
  • 43
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • DOI 10.1006/abio.1996.0238
    • Kuzmic, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase Anal. Biochem. 237, 260-273 (Pubitemid 26177089)
    • (1996) Analytical Biochemistry , vol.237 , Issue.2 , pp. 260-273
    • Kuzmic, P.1
  • 44
    • 33846223901 scopus 로고    scopus 로고
    • Pre-steady-state kinetic study of substrate specificity of Escherichia coli formamidopyrimidine-DNA glycosylase
    • DOI 10.1021/bi060787r
    • Kuznetsov, N. A., Koval, V. V., Zharkov, D. O., Vorobjev, Y. N., Nevinsky, G. A., Douglas, K. T., and Fedorova, O. S. (2007) Pre-steady-state kinetic study of substrate specificity of Escherichia coli formamidopyrimidine- DNA glycosylase Biochemistry 46, 424-435 (Pubitemid 46105434)
    • (2007) Biochemistry , vol.46 , Issue.2 , pp. 424-435
    • Kuznetsov, N.A.1    Koval, V.V.2    Zharkov, D.O.3    Vorobjev, Y.N.4    Nevinsky, G.A.5    Douglas, K.T.6    Fedorova, O.S.7
  • 45
    • 78049421039 scopus 로고    scopus 로고
    • GUI-BioPASED program for molecular dynamics modelling of biopolymers with a graphical user interface
    • Popov, A. V. and Vorob'ev, Iu. N. (2010) GUI-BioPASED program for molecular dynamics modelling of biopolymers with a graphical user interface Mol. Biol. (Moscow) 44, 735-742
    • (2010) Mol. Biol. (Moscow) , vol.44 , pp. 735-742
    • Popov, A.V.1    Vorob'Ev, Iu.N.2
  • 47
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • DOI 10.1002/(SICI)1097-0134(19990501)35:2<133::AID-PROT1>3.0.CO;2-N
    • Lazaridis, T. and Karplus, M. (1999) Effective energy function for proteins in solution Proteins 35, 133-152 (Pubitemid 29165128)
    • (1999) Proteins: Structure, Function and Genetics , vol.35 , Issue.2 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2
  • 49
    • 0034234593 scopus 로고    scopus 로고
    • New insights into the structure of abasic DNA from molecular dynamics simulations
    • Barsky, D., Foloppe, N., Ahmadia, S., Wilson, D. M., and MacKerell, A. D. (2000) New insights into the structure of abasic DNA from molecular dynamics simulations Nucleic Acids Res. 28, 2613-2626 (Pubitemid 30420861)
    • (2000) Nucleic Acids Research , vol.28 , Issue.13 , pp. 2613-2626
    • Barsky, D.1    Foloppe, N.2    Ahmadia, S.3    Wilson III, D.M.4    MacKerell Jr., A.D.5
  • 50
    • 0029758746 scopus 로고    scopus 로고
    • Spectroscopic and calorimetric characterizations of DNA duplexes containing 2-aminopurine
    • DOI 10.1021/bi9614545
    • Law, S. M., Eritja, R., Goodman, M. F., and Breslauer, K. J. (1996) Spectroscopic and calorimetric characterizations of DNA duplexes containing 2-aminopurine Biochemistry 35, 12329-12337 (Pubitemid 26331255)
    • (1996) Biochemistry , vol.35 , Issue.38 , pp. 12329-12337
    • Law, S.M.1    Eritja, R.2    Goodman, M.F.3    Breslauer, K.J.4
  • 51
    • 0037027319 scopus 로고    scopus 로고
    • 2-Aminopurine electronic structure and fluorescence properties in DNA
    • DOI 10.1021/bi020308y
    • Jean, J. M. and Hall, K. B. (2002) 2-Aminopurine electronic structure and fluorescence properties in DNA Biochemistry 41, 13152-13161 (Pubitemid 35244704)
    • (2002) Biochemistry , vol.41 , Issue.44 , pp. 13152-13161
    • Jean, J.M.1    Hall, K.B.2
  • 52
    • 0032529485 scopus 로고    scopus 로고
    • 2-Aminopurine fluorescence studies of base stacking interactions at abasic sites in DNA: Metal-ion and base sequence effects
    • DOI 10.1093/nar/26.16.3837
    • Stivers, J. T. (1998) 2-Aminopurine fluorescence studies of base stacking interactions at abasic sites in DNA: Metal-ion and base sequence effects Nucleic Acids Res. 26, 3837-3844 (Pubitemid 28367993)
    • (1998) Nucleic Acids Research , vol.26 , Issue.16 , pp. 3837-3844
    • Stivers, J.T.1
  • 53
    • 0035969981 scopus 로고    scopus 로고
    • Conformation and dynamics of abasic sites in DNA investigated by time-resolved fluorescence of 2-aminopurine
    • DOI 10.1021/bi001665g
    • Rachofsky, E. L., Seibert, E., Stivers, J. T., Osman, R., and Ross, J. B. (2001) Conformation and dynamics of abasic sites in DNA investigated by time-resolved fluorescence of 2-aminopurine Biochemistry 40, 957-967 (Pubitemid 32108588)
    • (2001) Biochemistry , vol.40 , Issue.4 , pp. 957-967
    • Rachofsky, E.L.1    Seibert, E.2    Stivers, J.T.3    Osman, R.4    Ross, J.B.A.5
  • 54
    • 0000812659 scopus 로고
    • Base pairing and mutagenesis: Observation of a protonated base pair between 2-aminopurine and cytosine in an oligonucleotide by proton NMR
    • DOI 10.1073/pnas.83.15.5434
    • Sowers, L. C., Fazakerley, G. V., Eritja, R., Kaplan, B. E., and Goodman, M. F. (1986) Base pairing and mutagenesis: Observation of a protonated base pair between 2-aminopurine and cytosine in an oligonucleotide by proton NMR Proc. Natl. Acad. Sci. U.S.A. 83, 5434-5438 (Pubitemid 16001237)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.15 , pp. 5434-5438
    • Sowers, L.C.1    Fazakerley, G.V.2    Eritja, R.3
  • 56
    • 0023664684 scopus 로고
    • Oligodeoxynucleotides containing synthetic abasic sites. Model substrates for DNA polymerases and apurinic/apyrimidinic endonucleases
    • Takeshita, M., Chang, C. N., Johnson, F., Will, S., and Grollman, A. P. (1987) Oligodeoxynucleotides containing synthetic abasic sites. Model substrates for DNA polymerases and apurinic/apyrimidinic endonucleases J. Biol. Chem. 262, 10171-10179
    • (1987) J. Biol. Chem. , vol.262 , pp. 10171-10179
    • Takeshita, M.1    Chang, C.N.2    Johnson, F.3    Will, S.4    Grollman, A.P.5
  • 57
    • 43049167396 scopus 로고    scopus 로고
    • Characterization of abasic endonuclease activity of human Ape1 on alternative substrates, as well as effects of ATP and sequence context on AP site incision
    • Berquist, B. R., McNeill, D. R., and Wilson, D. M., III (2008) Characterization of abasic endonuclease activity of human Ape1 on alternative substrates, as well as effects of ATP and sequence context on AP site incision J. Mol. Biol. 379, 17-27
    • (2008) J. Mol. Biol. , vol.379 , pp. 17-27
    • Berquist, B.R.1    McNeill, D.R.2    Wilson III, D.M.3
  • 59
    • 0030964066 scopus 로고    scopus 로고
    • Solution conformation of an abasic DNA undecamer duplex d(CGCACXCACGC)·d(GCGTGTGTGCG): The unpaired trymine stacks inside the helix
    • DOI 10.1021/bi962677y
    • Coppel, Y., Berthet, N., Coulombeau, C., Garcia, J., and Lhomme, J. (1997) Solution conformation of an abasic DNA undecamer duplex d(CGCACXCACGC) × d(GCGTGTGTGCG): The unpaired thymine stacks inside the helix Biochemistry 36, 4817-4830 (Pubitemid 27180962)
    • (1997) Biochemistry , vol.36 , Issue.16 , pp. 4817-4830
    • Coppel, Y.1    Berthet, N.2    Coulombeau, C.3    Coulombeau, C.4    Garcia, J.5    Lhomme, J.6
  • 60
    • 0029886521 scopus 로고    scopus 로고
    • NMR study of the conformation of the 2-aminopurine:cytosine mismatch in DNA
    • DOI 10.1021/bi952657g
    • Fagan, P. A., Fabrega, C., Eritja, R., Goodman, M. F., and Wemmer, D. E. (1996) NMR study of the conformation of the 2-aminopurine:cytosine mismatch in DNA Biochemistry 35, 4026-4033 (Pubitemid 26113459)
    • (1996) Biochemistry , vol.35 , Issue.13 , pp. 4026-4033
    • Fagan, P.A.1    Fabrega, C.2    Eritja, R.3    Goodman, M.F.4    Wemmer, D.E.5
  • 61
    • 0000694262 scopus 로고
    • Characterization of the Equilibrating Forms of the Aldehydic Abasic Site in Duplex DNA by O-17 NMR
    • Wilde, J. A., Bolton, P. H., Mazumder, A., Manoharan, M., and Gerlt, J. A. (1989) Characterization of the Equilibrating Forms of the Aldehydic Abasic Site in Duplex DNA by O-17 NMR J. Am. Chem. Soc. 111, 1894-1896
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 1894-1896
    • Wilde, J.A.1    Bolton, P.H.2    Mazumder, A.3    Manoharan, M.4    Gerlt, J.A.5
  • 63
    • 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
  • 64
    • 1642494900 scopus 로고    scopus 로고
    • Effects of Backbone Contacts 3′ to the Abasic Site on the Cleavage and the Product Binding by Human Apurinic/Apyrimidinic Endonuclease (APE1)
    • DOI 10.1021/bi0346190
    • Izumi, T., Schein, C. H., Oezguen, N., Feng, Y., and Braun, W. (2004) Effects of backbone contacts 3′ to the abasic site on the cleavage and the product binding by human apurinic/apyrimidinic endonuclease (APE1) Biochemistry 43, 684-689 (Pubitemid 38114055)
    • (2004) Biochemistry , vol.43 , Issue.3 , pp. 684-689
    • Izumi, T.1    Schein, C.H.2    Oezguen, N.3    Feng, Y.4    Braun, W.5
  • 65
    • 0034661689 scopus 로고    scopus 로고
    • Effect of single mutations in the OGG1 gene found in human tumors on the substrate specificity of the Ogg1 protein
    • Audebert, M., Radicella, J. P., and Dizdaroglu, M. (2000) Effect of single mutations in the OGG1 gene found in human tumors on the substrate specificity of the Ogg1 protein Nucleic Acids Res. 28, 2672-2678 (Pubitemid 30488010)
    • (2000) Nucleic Acids Research , vol.28 , Issue.14 , pp. 2672-2678
    • Audebert, M.1    Radicella, J.P.2    Dizdaroglu, M.3
  • 66
    • 34249862252 scopus 로고    scopus 로고
    • Interactions of pro- and eukaryotic DNA repair enzymes with oligodeoxyribonucleotides containing clustered lesions
    • Starostin, K. V., Ishchenko, A. A., Zharkov, D. O., Buneva, V. N., and Nevinskii, G. A. (2007) Interactions of pro- and eukaryotic DNA repair enzymes with oligodeoxyribonucleotides containing clustered lesions Mol. Biol. (Moscow) 41, 112-120
    • (2007) Mol. Biol. (Moscow) , vol.41 , pp. 112-120
    • Starostin, K.V.1    Ishchenko, A.A.2    Zharkov, D.O.3    Buneva, V.N.4    Nevinskii, G.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.