메뉴 건너뛰기




Volumn 95, Issue 7, 2008, Pages 3259-3268

Theoretical study of DNA damage recognition via electron transfer from the [4Fe-4S] complex of MutY

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA GLYCOSYLASE MUTY; DNA GLYCOSYLTRANSFERASE; GUANINE; IRON SULFUR PROTEIN;

EID: 55949131240     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.108.132183     Document Type: Article
Times cited : (20)

References (58)
  • 1
    • 0038799736 scopus 로고    scopus 로고
    • Oxidative DNA damage: Mechanisms, mutation, and disease
    • Cooke, M. S., M. D. Evans, M. Dizdaroglu, and J. Lunec. 2003. Oxidative DNA damage: mechanisms, mutation, and disease. FASEB J. 17:1195-1214.
    • (2003) FASEB J , vol.17 , pp. 1195-1214
    • Cooke, M.S.1    Evans, M.D.2    Dizdaroglu, M.3    Lunec, J.4
  • 2
    • 0026701365 scopus 로고
    • The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)
    • Michaels, M. L., and J. H. Miller. 1992. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 174:6321-6325.
    • (1992) J. Bacteriol , vol.174 , pp. 6321-6325
    • Michaels, M.L.1    Miller, J.H.2
  • 3
    • 0027528412 scopus 로고
    • Repair of DNA containing the oxidatively-damaged base, 8-oxoguanine
    • Tchou, J., and A. P. Grollman. 1993. Repair of DNA containing the oxidatively-damaged base, 8-oxoguanine. Mutat. Res. 299:277-287.
    • (1993) Mutat. Res , vol.299 , pp. 277-287
    • Tchou, J.1    Grollman, A.P.2
  • 4
    • 10044223573 scopus 로고    scopus 로고
    • Kinetics of protein-DNA interaction: Facilitated target location in sequence-dependent potential
    • Slutsky, M., and L. A. Mirny. 2004. Kinetics of protein-DNA interaction: facilitated target location in sequence-dependent potential. Biophys. J. 87:4021-4035.
    • (2004) Biophys. J , vol.87 , pp. 4021-4035
    • Slutsky, M.1    Mirny, L.A.2
  • 5
    • 24044492241 scopus 로고    scopus 로고
    • The DNA trackwalkers: Principles of lesion search and recognition by DNA glycosylases
    • Zharkov, D. O., and A. P. Grollman. 2005. The DNA trackwalkers: principles of lesion search and recognition by DNA glycosylases. Mutat. Res. 577:24-54.
    • (2005) Mutat. Res , vol.577 , pp. 24-54
    • Zharkov, D.O.1    Grollman, A.P.2
  • 6
    • 0024531901 scopus 로고
    • Facilitated target location in biological systems
    • von Hippel, P. H., and O. G. Berg. 1989. Facilitated target location in biological systems. J. Biol. Chem. 264:675-678.
    • (1989) J. Biol. Chem , vol.264 , pp. 675-678
    • von Hippel, P.H.1    Berg, O.G.2
  • 7
    • 0019867850 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 3. The Escherichia coli lac repressor-operator interaction: Kinetic measurements and conclusions
    • Winter, R. B., O. G. Berg, and P. H. von Hippel. 1981. Diffusion-driven mechanisms of protein translocation on nucleic acids. 3. The Escherichia coli lac repressor-operator interaction: kinetic measurements and conclusions. Biochemistry. 20:6961-6977.
    • (1981) Biochemistry , vol.20 , pp. 6961-6977
    • Winter, R.B.1    Berg, O.G.2    von Hippel, P.H.3
  • 8
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R. S., and M. T. Record. 1994. Coupling of local folding to site-specific binding of proteins to DNA. Science. 263:777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, M.T.2
  • 11
    • 0037966257 scopus 로고
    • Escherichia coli MutY gene product is required for specific A-G to C-G mismatch correction
    • Au, K. G., M. Cabrera, J. H. Miller, and P. Modrich. 1988. Escherichia coli MutY gene product is required for specific A-G to C-G mismatch correction. Proc. Natl. Acad. Sci. USA. 85:9163-9166.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9163-9166
    • Au, K.G.1    Cabrera, M.2    Miller, J.H.3    Modrich, P.4
  • 12
    • 0024332124 scopus 로고
    • Escherichia coli MutY gene encodes an adenine glycosylase active on G-A mispairs
    • Au, K. G., S. Clark, J. H. Miller, and P. Modrich. 1989. Escherichia coli MutY gene encodes an adenine glycosylase active on G-A mispairs. Proc. Natl. Acad. Sci. USA. 86:8877-8881.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8877-8881
    • Au, K.G.1    Clark, S.2    Miller, J.H.3    Modrich, P.4
  • 13
    • 0026684849 scopus 로고
    • Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA
    • Michaels, M. L., C. Cruz, A. P. Grollman, and J. H. Miller. 1992. Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA. Proc. Natl. Acad. Sci. USA. 89:7022-7025.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7022-7025
    • Michaels, M.L.1    Cruz, C.2    Grollman, A.P.3    Miller, J.H.4
  • 14
  • 15
    • 0032553004 scopus 로고
    • Single-turnover and pre-steady-state kinetics of the reaction of the adenine glycosylase MutY with mismatch-containing DNA substrates
    • Porello, S. L., A. E. Leyes, and S. S. David. 1988. Single-turnover and pre-steady-state kinetics of the reaction of the adenine glycosylase MutY with mismatch-containing DNA substrates. Biochemistry. 37:14756-14764.
    • (1988) Biochemistry , vol.37 , pp. 14756-14764
    • Porello, S.L.1    Leyes, A.E.2    David, S.S.3
  • 18
    • 0034653650 scopus 로고    scopus 로고
    • The trap depth (in DNA) of 8-oxo-7,8-dihydro-2′ deoxyguanosine as derived from electron-transfer equilibria in aqueous solution
    • Steenken, S., S. V. Jovanovic, M. Bietti, and K. Bernhard. 2000. The trap depth (in DNA) of 8-oxo-7,8-dihydro-2′ deoxyguanosine as derived from electron-transfer equilibria in aqueous solution. J. Am. Chem. Soc. 122:2373-2374.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 2373-2374
    • Steenken, S.1    Jovanovic, S.V.2    Bietti, M.3    Bernhard, K.4
  • 19
    • 1342304229 scopus 로고    scopus 로고
    • Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase
    • Fromme, J. C., A. Banerjee, S. J. Huang, and G. L. Verdine. 2004. Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase. Nature. 427:652-656.
    • (2004) Nature , vol.427 , pp. 652-656
    • Fromme, J.C.1    Banerjee, A.2    Huang, S.J.3    Verdine, G.L.4
  • 20
    • 13744261252 scopus 로고    scopus 로고
    • Functional characterization of two human MutY homolog (hMYH) missense mutations (R227W and V232F) that lie within the putative hMSH6 binding domain and are associated with hMYH polyposis
    • Bai, H. B., S. Jones, X. Guan, T. M. Wilson, J. R. Sampson, J. P. Cheadle, and A. L. Lu. 2005. Functional characterization of two human MutY homolog (hMYH) missense mutations (R227W and V232F) that lie within the putative hMSH6 binding domain and are associated with hMYH polyposis. Nucleic Acids Res. 33:597-604.
    • (2005) Nucleic Acids Res , vol.33 , pp. 597-604
    • Bai, H.B.1    Jones, S.2    Guan, X.3    Wilson, T.M.4    Sampson, J.R.5    Cheadle, J.P.6    Lu, A.L.7
  • 21
    • 0022004980 scopus 로고
    • Electron transfer in chemistry and biology
    • Marcus, R. A., and N. Sutin. 1985. Electron transfer in chemistry and biology. Biochim. Biophys. Acta. 811:265-322.
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 22
    • 85031356038 scopus 로고    scopus 로고
    • Beratan, D. N., and J. N. Onuchic. 1996. The protein bridge between redox centers. In Protein Electron Transfer. D. S. Bendall, editor. BIOS Scientific Publishers, Oxford, UK. 23-42.
    • Beratan, D. N., and J. N. Onuchic. 1996. The protein bridge between redox centers. In Protein Electron Transfer. D. S. Bendall, editor. BIOS Scientific Publishers, Oxford, UK. 23-42.
  • 23
    • 0037421834 scopus 로고    scopus 로고
    • Theoretical understanding of the interprotein electron transfer between cytochrome c(2) and the photosynthetic reaction center
    • Miyashita, O., M. Y. Okamura, and J. N. Onuchic. 2003. Theoretical understanding of the interprotein electron transfer between cytochrome c(2) and the photosynthetic reaction center. J. Phys. Chem. B. 107:1230-1241.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 1230-1241
    • Miyashita, O.1    Okamura, M.Y.2    Onuchic, J.N.3
  • 24
    • 14844342806 scopus 로고    scopus 로고
    • Interprotein electron transfer from cytochrome c(2) to photosynthetic reaction center: Tunneling across an aqueous interface
    • Miyashita, O., M. Y. Okamura, and J. N. Onuchic. 2005. Interprotein electron transfer from cytochrome c(2) to photosynthetic reaction center: tunneling across an aqueous interface. Proc. Natl. Acad. Sci. USA. 102:3558-3563.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3558-3563
    • Miyashita, O.1    Okamura, M.Y.2    Onuchic, J.N.3
  • 25
    • 7044239742 scopus 로고
    • Free energy calculations: Applications to chemical and biochemical phenomena
    • Kollman, P. A. 1993. Free energy calculations: applications to chemical and biochemical phenomena. Chem. Rev. 93:2395-2417.
    • (1993) Chem. Rev , vol.93 , pp. 2395-2417
    • Kollman, P.A.1
  • 26
    • 0040960707 scopus 로고
    • Electron tunneling through covalent and noncovalent pathways in proteins
    • Beratan, D. N., J. N. Onuchic, and J. J. Hopfield. 1987. Electron tunneling through covalent and noncovalent pathways in proteins. J. Chem. Phys. 86:4488-4498.
    • (1987) J. Chem. Phys , vol.86 , pp. 4488-4498
    • Beratan, D.N.1    Onuchic, J.N.2    Hopfield, J.J.3
  • 27
    • 0000895446 scopus 로고
    • Tunneling pathway and redox-state-dependent electronic couplings at nearly fixed distance in electron transfer proteins
    • Beratan, D. N., J. N. Betts, and J. N. Onuchic. 1992. Tunneling pathway and redox-state-dependent electronic couplings at nearly fixed distance in electron transfer proteins. J. Phys. Chem. 96:2852-2855.
    • (1992) J. Phys. Chem , vol.96 , pp. 2852-2855
    • Beratan, D.N.1    Betts, J.N.2    Onuchic, J.N.3
  • 28
    • 0011575148 scopus 로고
    • Distance, stereoelectronic effects, and the Marcus inverted region in intramolecular electron transfer in organic radical anions
    • Closs, G. L., L. T. Calcaterra, N. J. Green, K. W. Penfield, and J. R. Miller. 1986. Distance, stereoelectronic effects, and the Marcus inverted region in intramolecular electron transfer in organic radical anions. J. Phys. Chem. 90:3673-3683.
    • (1986) J. Phys. Chem , vol.90 , pp. 3673-3683
    • Closs, G.L.1    Calcaterra, L.T.2    Green, N.J.3    Penfield, K.W.4    Miller, J.R.5
  • 29
    • 0000911922 scopus 로고
    • A predictive theoretical model for electron tunneling pathways in proteins
    • Onuchic, J. N., and D. N. Beratan. 1990. A predictive theoretical model for electron tunneling pathways in proteins. J. Chem. Phys. 92:722-733.
    • (1990) J. Chem. Phys , vol.92 , pp. 722-733
    • Onuchic, J.N.1    Beratan, D.N.2
  • 30
    • 0029092621 scopus 로고
    • Direct evaluation of electronic coupling mediated by hydrogen bonds: Implications for biological electron transfer
    • de Rege, P. J. F., S. A. Williams, and J. T. Michael. 1995. Direct evaluation of electronic coupling mediated by hydrogen bonds: implications for biological electron transfer. Science. 269:1409-1413.
    • (1995) Science , vol.269 , pp. 1409-1413
    • de Rege, P.J.F.1    Williams, S.A.2    Michael, J.T.3
  • 31
    • 0000318315 scopus 로고
    • Density functional/Poisson-Boltzmann calculations of redox potentials for iron-sulfur clusters
    • Mouesca, J., J. L. Chen, L. Noodleman, D. Bashford, and D. A. Case. 1994. Density functional/Poisson-Boltzmann calculations of redox potentials for iron-sulfur clusters. J. Am. Chem. Soc. 116:11898-11914.
    • (1994) J. Am. Chem. Soc , vol.116 , pp. 11898-11914
    • Mouesca, J.1    Chen, J.L.2    Noodleman, L.3    Bashford, D.4    Case, D.A.5
  • 32
    • 0037442880 scopus 로고    scopus 로고
    • Torres, R. A., T. Lovell, L. Noodleman, and D. A. Case. 2003. Density functional-and reduction potential calculations of Fe4S4 clusters. J. Am. Chem. Soc. 125:1923-1936.
    • Torres, R. A., T. Lovell, L. Noodleman, and D. A. Case. 2003. Density functional-and reduction potential calculations of Fe4S4 clusters. J. Am. Chem. Soc. 125:1923-1936.
  • 33
    • 0000162043 scopus 로고    scopus 로고
    • Theoretical determination of electron affinity and ionization potential of DNA and RNA bases
    • Russo, N., M. Toscano, and A. Grand. 2000. Theoretical determination of electron affinity and ionization potential of DNA and RNA bases. J. Comput. Chem. 21:1243-1250.
    • (2000) J. Comput. Chem , vol.21 , pp. 1243-1250
    • Russo, N.1    Toscano, M.2    Grand, A.3
  • 35
    • 0346394774 scopus 로고    scopus 로고
    • Ground- and excited-state properties of DNA base molecules from plane-wave calculations using ultrasoft pseudopotentials
    • Preuss, M., W. G. Schmidt, K. Seino, J. Furthmüller, and F. Bechstedt. 2004. Ground- and excited-state properties of DNA base molecules from plane-wave calculations using ultrasoft pseudopotentials. J. Comput. Chem. 25:112-122.
    • (2004) J. Comput. Chem , vol.25 , pp. 112-122
    • Preuss, M.1    Schmidt, W.G.2    Seino, K.3    Furthmüller, J.4    Bechstedt, F.5
  • 36
    • 84962433238 scopus 로고    scopus 로고
    • Ab initio ionization energy thresholds of DNA and RNA bases in gas phase and in aqueous solution
    • Crespo-Hernández, C. E., R. Arce, Y. Ishikawa, L. Gorb, J. Leszczynski, and D. M. Close. 2004. Ab initio ionization energy thresholds of DNA and RNA bases in gas phase and in aqueous solution. J. Phys. Chem. A. 108:6373-6377.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 6373-6377
    • Crespo-Hernández, C.E.1    Arce, R.2    Ishikawa, Y.3    Gorb, L.4    Leszczynski, J.5    Close, D.M.6
  • 38
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: The RESP model
    • Bayly, C. I., P. Cieplak, W. D. Cornell, and P. A. Kollman. 1993. A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model. J. Phys. Chem. 97:10269-10280.
    • (1993) J. Phys. Chem , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 39
    • 0142212202 scopus 로고    scopus 로고
    • Theoretical investigations of Ferredoxin I: The possible role of internal water molecules on the coupled electron proton transfer reaction
    • Meuwly, M., and M. Karplus. 2003. Theoretical investigations of Ferredoxin I: The possible role of internal water molecules on the coupled electron proton transfer reaction. Faraday Discuss. 124:297-313.
    • (2003) Faraday Discuss , vol.124 , pp. 297-313
    • Meuwly, M.1    Karplus, M.2
  • 40
    • 0242538339 scopus 로고    scopus 로고
    • Ab initio quantum mechanical study of metal substitution in analogues of rubredoxin: Implications for redox potential control
    • Beck, B. W., J. B. Koerner, and T. Ichiye. 1999. Ab initio quantum mechanical study of metal substitution in analogues of rubredoxin: implications for redox potential control. J. Phys. Chem. B. 103:8006-8015.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 8006-8015
    • Beck, B.W.1    Koerner, J.B.2    Ichiye, T.3
  • 41
    • 0038626733 scopus 로고    scopus 로고
    • 8-Oxoguanine enhances bending of DNA that favors binding to glycosylases
    • Miller, J. H., C. C. P. Fan-Chiang, T. P. Straatsma, and M. A. Kennedy. 2003. 8-Oxoguanine enhances bending of DNA that favors binding to glycosylases. J. Am. Chem. Soc. 125:6331-6336.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 6331-6336
    • Miller, J.H.1    Fan-Chiang, C.C.P.2    Straatsma, T.P.3    Kennedy, M.A.4
  • 42
    • 0029633186 scopus 로고
    • AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules
    • Pearlman, D. A., D. A. Case, J. W. Caldwell, W. S. Ross, T. E. Cheatham, S. DeBolt, D. Ferguson, G. Seibel, and P. Kollman. 1995. AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comput. Phys. Commun. 91:1-41.
    • (1995) Comput. Phys. Commun , vol.91 , pp. 1-41
    • Pearlman, D.A.1    Case, D.A.2    Caldwell, J.W.3    Ross, W.S.4    Cheatham, T.E.5    DeBolt, S.6    Ferguson, D.7    Seibel, G.8    Kollman, P.9
  • 43
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang, J., P. Cieplak, and P. A. Kollman. 2000. How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J. Comput. Chem. 21:1049-1074.
    • (2000) J. Comput. Chem , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 46
    • 0026596911 scopus 로고
    • Calculations of antibody-antigen interactions: Microscopic and semi-microscopic evaluation of the free energies of binding of phosphorylcholine analogs to McPC603
    • Lee, F. S., Z. T. Chu, M. B. Bolger, and A. Warshel. 1992. Calculations of antibody-antigen interactions: microscopic and semi-microscopic evaluation of the free energies of binding of phosphorylcholine analogs to McPC603. Protein Eng. 5:215-228.
    • (1992) Protein Eng , vol.5 , pp. 215-228
    • Lee, F.S.1    Chu, Z.T.2    Bolger, M.B.3    Warshel, A.4
  • 47
    • 0028155689 scopus 로고
    • New method for predicting binding-affinity in computer-aided drug design
    • Aqvist, J., C. Medina, and J. E. Samuelsson. 1994. New method for predicting binding-affinity in computer-aided drug design. Protein Eng. 7:385-391.
    • (1994) Protein Eng , vol.7 , pp. 385-391
    • Aqvist, J.1    Medina, C.2    Samuelsson, J.E.3
  • 48
    • 33645807371 scopus 로고    scopus 로고
    • A base-excision DNA-repair protein finds intrahelical lesion bases by fast sliding in contact with DNA
    • Blainey, P. C., A. M. van Oijent, A. Banerjee, G. L. Verdine, and X. S. Xie. 2006. A base-excision DNA-repair protein finds intrahelical lesion bases by fast sliding in contact with DNA. Proc. Natl. Acad. Sci. USA. 103:5752-5757.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5752-5757
    • Blainey, P.C.1    van Oijent, A.M.2    Banerjee, A.3    Verdine, G.L.4    Xie, X.S.5
  • 50
    • 33644857131 scopus 로고    scopus 로고
    • Electron trap for DNA-bound repair enzymes: A strategy for DNA-mediated signaling
    • Yavin, E., E. D. A. Stemp, V. L. O'Shea, S. S. David, and J. K. Barton. 2006. Electron trap for DNA-bound repair enzymes: a strategy for DNA-mediated signaling. Proc. Natl. Acad. Sci. USA. 103:3610-3614.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 3610-3614
    • Yavin, E.1    Stemp, E.D.A.2    O'Shea, V.L.3    David, S.S.4    Barton, J.K.5
  • 51
    • 25144485436 scopus 로고    scopus 로고
    • The sacrificial role of easily oxidizable sites in the protection of DNA from damage
    • Kanvah, S., and G. B. Schuster. 2005. The sacrificial role of easily oxidizable sites in the protection of DNA from damage. Nucleic Acids Res. 33:5133-5138.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5133-5138
    • Kanvah, S.1    Schuster, G.B.2
  • 53
    • 14844286411 scopus 로고    scopus 로고
    • Combination reactions of superoxide with 8-oxo-7,8-dihyroguanine radicals in DNA
    • Misiaszek, R., Y. Uvaydov, C. Crean, N. E. Geacintov, and V. Shafirovich. 2005. Combination reactions of superoxide with 8-oxo-7,8-dihyroguanine radicals in DNA. J. Biol. Chem. 280:6293-6300.
    • (2005) J. Biol. Chem , vol.280 , pp. 6293-6300
    • Misiaszek, R.1    Uvaydov, Y.2    Crean, C.3    Geacintov, N.E.4    Shafirovich, V.5
  • 54
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • Demple, B., and L. Harrison. 1994. Repair of oxidative damage to DNA: enzymology and biology. Annu. Rev. Biochem. 63:915-948.
    • (1994) Annu. Rev. Biochem , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 55
    • 0042510225 scopus 로고    scopus 로고
    • Long-range DNA charge transport
    • Delaney, S., and J. K. Barton. 2003. Long-range DNA charge transport. J. Org. Chem. 68:6475-6483.
    • (2003) J. Org. Chem , vol.68 , pp. 6475-6483
    • Delaney, S.1    Barton, J.K.2
  • 56
    • 35348895032 scopus 로고    scopus 로고
    • DNA repair glycosylases with a [4Fe-4S] cluster: A redox cofactor for DNA-mediated charge transport?
    • Boal, A. K., E. Yavin, and J. K. Barton. 2007. DNA repair glycosylases with a [4Fe-4S] cluster: a redox cofactor for DNA-mediated charge transport? J. Inorg. Biochem. 101:1913-1921.
    • (2007) J. Inorg. Biochem , vol.101 , pp. 1913-1921
    • Boal, A.K.1    Yavin, E.2    Barton, J.K.3
  • 57
    • 33750078971 scopus 로고    scopus 로고
    • NMR structural and kinetic characterization of a homeodomain diffusing and hopping on nonspecific DNA
    • Iwahara, J., M. Zweckstetter, and G. M. Clore. 2006. NMR structural and kinetic characterization of a homeodomain diffusing and hopping on nonspecific DNA. Proc. Natl. Acad. Sci. USA. 103:15062-15067.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15062-15067
    • Iwahara, J.1    Zweckstetter, M.2    Clore, G.M.3
  • 58
    • 0037192812 scopus 로고    scopus 로고
    • Human MutY homolog, a DNA glycosylase involved in base excision repair, physically and functionally interacts with mismatch repair proteins human MutS homolog 2/human MutS homolog 6
    • Gu, Y. S., A. Parker, T. M. Wilson, H. B. Bai, D. Y. Chang, and A. L. Lu. 2003. Human MutY homolog, a DNA glycosylase involved in base excision repair, physically and functionally interacts with mismatch repair proteins human MutS homolog 2/human MutS homolog 6. J. Biol. Chem. 277:11135-11142.
    • (2003) J. Biol. Chem , vol.277 , pp. 11135-11142
    • Gu, Y.S.1    Parker, A.2    Wilson, T.M.3    Bai, H.B.4    Chang, D.Y.5    Lu, A.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.