메뉴 건너뛰기




Volumn 40, Issue 6, 2006, Pages 952-960

Interactions of human 8-oxoguanine DNA glycosylase with single- and double-stranded DNAs

Author keywords

DNA recognition mechanism; Human 8 oxoguanine DNA glycosylase; Method of stepwise increase in ligand complexity

Indexed keywords


EID: 33845640485     PISSN: 00268933     EISSN: 16083245     Source Type: Journal    
DOI: 10.1134/S002689330606015X     Document Type: Article
Times cited : (2)

References (37)
  • 1
    • 0028959869 scopus 로고
    • The essential role of weak interactions in enzyme recognition of long DNA and RNA molecules
    • Nevinsky G.A. 1995. The essential role of weak interactions in enzyme recognition of long DNA and RNA molecules. Mol. Biol. 29, 16-37.
    • (1995) Mol. Biol. , vol.29 , pp. 16-37
    • Nevinsky, G.A.1
  • 2
    • 0033072594 scopus 로고    scopus 로고
    • Potential of the method of stepwise increase in ligand complexity in studies of protein-nucleic acid interactions: Mechanisms of the functioning of some replication, repair, topoisomerization, and restriction enzymes
    • Bugreev D.V., Nevinsky G.A. 1999. Potential of the method of stepwise increase in ligand complexity in studies of protein-nucleic acid interactions: Mechanisms of the functioning of some replication, repair, topoisomerization, and restriction enzymes. Biokhimiya. 64, 291-305.
    • (1999) Biokhimiya , vol.64 , pp. 291-305
    • Bugreev, D.V.1    Nevinsky, G.A.2
  • 3
    • 5444241653 scopus 로고    scopus 로고
    • Structural, thermodynamic, and kinetic basis of DNA- and RNA-dependent enzymes functioning: Important role of weak nonspecific additive interactions between enzymes and long nucleic acids for their recognition and transformation
    • Ed. Uversky V.N. Kerala: Research Signpost
    • Nevinsky G.A. 2003. Structural, thermodynamic, and kinetic basis of DNA- and RNA-dependent enzymes functioning: Important role of weak nonspecific additive interactions between enzymes and long nucleic acids for their recognition and transformation. In: Protein Structures: Kaleidoscope of Structural Properties and Functions. Ed. Uversky V.N. Kerala: Research Signpost, pp. 133-222.
    • (2003) Protein Structures: Kaleidoscope of Structural Properties and Functions , pp. 133-222
    • Nevinsky, G.A.1
  • 4
    • 5444244823 scopus 로고    scopus 로고
    • The role of weak specific and nonspecific interactions in enzymatic recognition and conversion of long DNAs
    • Nevinsky G.A. 2004. The role of weak specific and nonspecific interactions in enzymatic recognition and conversion of long DNAs. Mol. Biol. 38, 756-785.
    • (2004) Mol. Biol. , vol.38 , pp. 756-785
    • Nevinsky, G.A.1
  • 5
    • 0023913473 scopus 로고
    • Protein-nucleic acid interaction in reactions catalyzed with DNA polymerases
    • Knorre D.G., Lavrik O.I., Nevinsky G.A. 1988. Protein-nucleic acid interaction in reactions catalyzed with DNA polymerases. Biochimie. 70, 655-661.
    • (1988) Biochimie. , vol.70 , pp. 655-661
    • Knorre, D.G.1    Lavrik, O.I.2    Nevinsky, G.A.3
  • 6
    • 0025162225 scopus 로고
    • Structure-function analysis of mononucleotides and short oligonucleotides in the priming of enzymatic DNA synthesis
    • Nevinsky G.A., Veniaminova A.G., Levina A.S., Podust V.N., Lavrik O.I., Holler E. 1990. Structure-function analysis of mononucleotides and short oligonucleotides in the priming of enzymatic DNA synthesis. Biochemistry. 29, 1200-1207.
    • (1990) Biochemistry. , vol.29 , pp. 1200-1207
    • Nevinsky, G.A.1    Veniaminova, A.G.2    Levina, A.S.3    Podust, V.N.4    Lavrik, O.I.5    Holler, E.6
  • 7
    • 0025835232 scopus 로고
    • The mechanism of recognition of templates by DNA polymerases from pro- and eukaryotes as revealed by affinity modification data
    • Kolocheva T.I., Nevinsky G.A., Levina A.S., Khomov V.V., Lavrik O.I. 1991. The mechanism of recognition of templates by DNA polymerases from pro- and eukaryotes as revealed by affinity modification data. J. Biomol. Struct. Dyn. 9, 169-186.
    • (1991) J. Biomol. Struct. Dyn. , vol.9 , pp. 169-186
    • Kolocheva, T.I.1    Nevinsky, G.A.2    Levina, A.S.3    Khomov, V.V.4    Lavrik, O.I.5
  • 8
    • 20444470105 scopus 로고    scopus 로고
    • Formation of nucleoprotein RecA filament on single-stranded DNA: Analysis by stepwise increase in ligand complexity
    • Bugreeva I.P., Bugreev D.V., Nevinsky G.A. 2005. Formation of nucleoprotein RecA filament on single-stranded DNA: Analysis by stepwise increase in ligand complexity. FEBS J. 272, 2734-2745.
    • (2005) FEBS J. , vol.272 , pp. 2734-2745
    • Bugreeva, I.P.1    Bugreev, D.V.2    Nevinsky, G.A.3
  • 9
    • 0032058649 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase: Interpretation of X-ray data in the light of kinetic and thermodynamic studies
    • Vinogradova N.L., Bulychev N.V., Maksakova G.A., Johnson F., Nevinsky G.A. 1998. Uracil-DNA glycosylase: interpretation of X-ray data in the light of kinetic and thermodynamic studies. Mol. Biol. 32, 489-499.
    • (1998) Mol. Biol. , vol.32 , pp. 489-499
    • Vinogradova, N.L.1    Bulychev, N.V.2    Maksakova, G.A.3    Johnson, F.4    Nevinsky, G.A.5
  • 10
    • 0037129958 scopus 로고    scopus 로고
    • Thermodynamic, kinetic, and structural basis for recognition and repair of 8-oxoguanine in DNA by Fpg protein from Escherichia coli
    • Ishchenko A.A., Vasilenko N.L., Sinitsina O.I., Yamkovoy V.I., Fedorova O.S., Douglas K.T., Nevinsky G.A. 2002. Thermodynamic, kinetic, and structural basis for recognition and repair of 8-oxoguanine in DNA by Fpg protein from Escherichia coli. Biochemistry. 41, 7540-7548.
    • (2002) Biochemistry , vol.41 , pp. 7540-7548
    • Ishchenko, A.A.1    Vasilenko, N.L.2    Sinitsina, O.I.3    Yamkovoy, V.I.4    Fedorova, O.S.5    Douglas, K.T.6    Nevinsky, G.A.7
  • 11
    • 0345448159 scopus 로고    scopus 로고
    • Recognition of damaged DNA by Escherichia coli Fpg protein: Insights from structural and kinetic data
    • Zharkov D.O., Ishchenko A.A., Douglas K.T., Nevinsky G.A. 2003. Recognition of damaged DNA by Escherichia coli Fpg protein: Insights from structural and kinetic data. Mutat. Res. 531, 141-156.
    • (2003) Mutat. Res. , vol.531 , pp. 141-156
    • Zharkov, D.O.1    Ishchenko, A.A.2    Douglas, K.T.3    Nevinsky, G.A.4
  • 13
    • 0034871331 scopus 로고    scopus 로고
    • Interaction of endonuclease EcoRI with short specific and nonspecific oligonucleotides
    • Kolocheva T.I., Maksakova G.A., Bugreev D.V., Nevinsky G.A. 2001. Interaction of endonuclease EcoRI with short specific and nonspecific oligonucleotides. IUBMB Life. 51, 189-195.
    • (2001) IUBMB Life , vol.51 , pp. 189-195
    • Kolocheva, T.I.1    Maksakova, G.A.2    Bugreev, D.V.3    Nevinsky, G.A.4
  • 14
    • 0038505229 scopus 로고    scopus 로고
    • Mechanism of recognition of supercoiled DNA by eukaryotic DNA topoisomerases I: 1. Interactions of enzymes with nonspecific oligonucleotides
    • Bugreev D.V., Buneva V.N., Sinitsina O.I., Nevinsky G.A. 2003. Mechanism of recognition of supercoiled DNA by eukaryotic DNA topoisomerases I: 1. Interactions of enzymes with nonspecific oligonucleotides. Bioorg. Khim. 29, 163-174.
    • (2003) Bioorg. Khim. , vol.29 , pp. 163-174
    • Bugreev, D.V.1    Buneva, V.N.2    Sinitsina, O.I.3    Nevinsky, G.A.4
  • 15
    • 5444260290 scopus 로고    scopus 로고
    • Mechanism of recognition of supercoiled DNA by eukaryotic DNA topoisomerases I: 2. Comparison of enzyme interactions with specific and nonspecific oligonucleotides
    • Bugreev D.V., Buneva V.N., Sinitsina O.I., Nevinsky G.A. 2003. Mechanism of recognition of supercoiled DNA by eukaryotic DNA topoisomerases I: 2. Comparison of enzyme interactions with specific and nonspecific oligonucleotides. Bioorg. Khim. 29, 275-288.
    • (2003) Bioorg. Khim. , vol.29 , pp. 275-288
    • Bugreev, D.V.1    Buneva, V.N.2    Sinitsina, O.I.3    Nevinsky, G.A.4
  • 16
    • 0037668597 scopus 로고    scopus 로고
    • Mechanism of supercoiled DNA cleavage by human DNA topoisomerase I: Effect of ligand structure on the catalytic stage of the reaction
    • Bugreev D.V., Buneva V.N., Nevinsky G.A. 2003. Mechanism of supercoiled DNA cleavage by human DNA topoisomerase I: Effect of ligand structure on the catalytic stage of the reaction. Mol. Biol. 37, 325-339.
    • (2003) Mol. Biol. , vol.37 , pp. 325-339
    • Bugreev, D.V.1    Buneva, V.N.2    Nevinsky, G.A.3
  • 18
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman K.B., Ames B.N. 1998. The free radical theory of aging matures. Physiol. Rev. 78, 547-581.
    • (1998) Physiol. Rev. , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 19
    • 0034666313 scopus 로고    scopus 로고
    • Substrate specificity and reaction mechanism of murine 8-oxoguanine-DNA glycosylase
    • Zharkov D.O., Rosenquist T.A., Gerchman S.E., Grollman A.P. 2000. Substrate specificity and reaction mechanism of murine 8-oxoguanine-DNA glycosylase. J. Biol. Chem. 275, 28,607-28,617.
    • (2000) J. Biol. Chem. , vol.275
    • Zharkov, D.O.1    Rosenquist, T.A.2    Gerchman, S.E.3    Grollman, A.P.4
  • 20
    • 0033569954 scopus 로고    scopus 로고
    • Excision of oxidatively damaged DNA bases by the human α-hOgg1 protein and the polymorphic α-hOgg1(Ser326Cys) protein which is frequently found in human populations
    • Dherin C., Radicella J.P., Dizdaroglu M., Boiteux S. 1999. Excision of oxidatively damaged DNA bases by the human α-hOgg1 protein and the polymorphic α-hOgg1(Ser326Cys) protein which is frequently found in human populations. Nucleic Acids Res. 27, 4001-4007.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4001-4007
    • Dherin, C.1    Radicella, J.P.2    Dizdaroglu, M.3    Boiteux, S.4
  • 21
    • 0030220956 scopus 로고    scopus 로고
    • Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily
    • Nash H.M., Bruner S.D., Scharer O.D., Kawate T., Addona T.A., Spooner E., Lane W.S., Verdine G.L. 1996. Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily. Curr. Biol. 6, 968-980.
    • (1996) Curr. Biol. , vol.6 , pp. 968-980
    • Nash, H.M.1    Bruner, S.D.2    Scharer, O.D.3    Kawate, T.4    Addona, T.A.5    Spooner, E.6    Lane, W.S.7    Verdine, G.L.8
  • 22
    • 0030738194 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase
    • Rosenquist T.A., Zharkov D.O., Grollman A.P. 1997. Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase. Proc. Natl. Acad. Sci. USA. 94, 7429-7434.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7429-7434
    • Rosenquist, T.A.1    Zharkov, D.O.2    Grollman, A.P.3
  • 23
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • Bruner S.D., Norman D.P.G., Verdine G.L. 2000. Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature. 403, 859-866.
    • (2000) Nature , vol.403 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.G.2    Verdine, G.L.3
  • 24
    • 0036290411 scopus 로고    scopus 로고
    • Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase
    • Bjoras M., Seeberg E., Luna L., Pearl L.H., Barrett T.E. 2002. Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase. J. Mol. Biol. 317, 171-177.
    • (2002) J. Mol. Biol. , vol.317 , pp. 171-177
    • Bjoras, M.1    Seeberg, E.2    Luna, L.3    Pearl, L.H.4    Barrett, T.E.5
  • 25
    • 15844379169 scopus 로고    scopus 로고
    • Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA
    • Banerjee A., Yang W., Karplus M., Verdine G.L. 2005. Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA. Nature. 434, 612-618.
    • (2005) Nature , vol.434 , pp. 612-618
    • Banerjee, A.1    Yang, W.2    Karplus, M.3    Verdine, G.L.4
  • 29
    • 0028903531 scopus 로고
    • Transient kinetic approaches to enzyme mechanisms
    • Fierke C.A., Hammes G.G. 1995. Transient kinetic approaches to enzyme mechanisms. Methods Enzymol. 249, 3-37.
    • (1995) Methods Enzymol. , vol.249 , pp. 3-37
    • Fierke, C.A.1    Hammes, G.G.2
  • 32
    • 0028783875 scopus 로고
    • Influence of the oxidatively damaged adduct 8-oxodeoxyguanosine on the conformation, energetics, and thermodynamic stability of a DNA duplex
    • Plum G.E., Grollman A.P., Johnson F., Breslauer K.J. 1995. Influence of the oxidatively damaged adduct 8-oxodeoxyguanosine on the conformation, energetics, and thermodynamic stability of a DNA duplex. Biochemistry. 34, 16,148-16,160.
    • (1995) Biochemistry , vol.34
    • Plum, G.E.1    Grollman, A.P.2    Johnson, F.3    Breslauer, K.J.4
  • 33
    • 0043231319 scopus 로고    scopus 로고
    • Electrostatic energy analysis of 8-oxoguanine DNA lesion: Molecular dynamics study
    • Pinak M. 2003. Electrostatic energy analysis of 8-oxoguanine DNA lesion: Molecular dynamics study. Comput. Biol. Chem. 27, 431-441.
    • (2003) Comput. Biol. Chem. , vol.27 , pp. 431-441
    • Pinak, M.1
  • 34
    • 0032489634 scopus 로고    scopus 로고
    • Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA
    • Redinbo M.R., Stewart L., Kuhn P., Champoux J.J., Hol W.G. 1998. Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. Science. 279, 1504-1513.
    • (1998) Science , vol.279 , pp. 1504-1513
    • Redinbo, M.R.1    Stewart, L.2    Kuhn, P.3    Champoux, J.J.4    Hol, W.G.5
  • 37
    • 0025871264 scopus 로고
    • MutM, a protein that prevents G·C → T·A transversions, is formamidopyrimidine-DNA glycosylase
    • Michaels M.L., Pham L., Cruz C., Miller J.H. 1991. MutM, a protein that prevents G·C → T·A transversions, is formamidopyrimidine-DNA glycosylase. Nucleic Acids Res. 19, 3629-3632.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3629-3632
    • Michaels, M.L.1    Pham, L.2    Cruz, C.3    Miller, J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.