메뉴 건너뛰기




Volumn 7, Issue 8, 1999, Pages 919-930

Identification of the Archaeoglobus fulgidus endonuclease III DNA interaction surface using heteronuclear NMR methods

Author keywords

Endonuclease; NMR; Protein DNA interactions

Indexed keywords

ADENINE DERIVATIVE; BACTERIAL DNA; CARBON MONOXIDE; ENDONUCLEASE; HYDROGEN; IRON SULFUR PROTEIN; NITROGEN;

EID: 0033566656     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80119-1     Document Type: Article
Times cited : (17)

References (72)
  • 2
    • 0030979263 scopus 로고    scopus 로고
    • DNA glycosylases
    • Cunningham, R.P. (1997). DNA glycosylases. Mutat. Res. 383, 189-196.
    • (1997) Mutat. Res. , vol.383 , pp. 189-196
    • Cunningham, R.P.1
  • 3
    • 0031239958 scopus 로고    scopus 로고
    • DNA repair: Caretakers of the genome?
    • Cunningham, R.P. (1997). DNA repair: Caretakers of the genome? Curr. Biol. 7, R576-579.
    • (1997) Curr. Biol. , vol.7
    • Cunningham, R.P.1
  • 4
    • 0001882582 scopus 로고    scopus 로고
    • Structural phylogenetics of DNA base excision repair
    • Eckstein, F. & Lilley, D.M.J., eds, Springer-Verlag, Berlin
    • Mol, C.D., Parikh, S.S., Lo, T.P. & Tainer, J.A. (1998). Structural phylogenetics of DNA base excision repair. In DNA Repair. (Eckstein, F. & Lilley, D.M.J., eds), pp 29-69, Springer-Verlag, Berlin.
    • (1998) DNA Repair , pp. 29-69
    • Mol, C.D.1    Parikh, S.S.2    Lo, T.P.3    Tainer, J.A.4
  • 5
    • 0016692306 scopus 로고
    • Endonucleolytic incision of x-irradiated deoxyribonucleic acid by extract of Escherichia coli
    • Strniste, G.F. & Wallace, S.S. (1975). Endonucleolytic incision of x-irradiated deoxyribonucleic acid by extract of Escherichia coli. Proc. Natl Acad. Sci. USA 72, 1997-2001.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 1997-2001
    • Strniste, G.F.1    Wallace, S.S.2
  • 6
    • 0017236583 scopus 로고
    • An endonuclease from Escherichia coli that introduces single polynucleotide chain scissions in ultraviolet-irradiated DNA
    • Radman, M. (1976). An endonuclease from Escherichia coli that introduces single polynucleotide chain scissions in ultraviolet-irradiated DNA. J. Biol. Chem. 251, 1438-1445.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1438-1445
    • Radman, M.1
  • 7
    • 0024328839 scopus 로고
    • UV-induced pyrimidine hydrates in DNA are repaired by bacterial and mammalian DNA glycosylase activities
    • Boorstein, R.J., Hilbert, T.P., Cadet, J., Cunningham, R.P. & Teebor, G.W. (1989). UV-induced pyrimidine hydrates in DNA are repaired by bacterial and mammalian DNA glycosylase activities. Biochemistry 28, 6164-6170.
    • (1989) Biochemistry , vol.28 , pp. 6164-6170
    • Boorstein, R.J.1    Hilbert, T.P.2    Cadet, J.3    Cunningham, R.P.4    Teebor, G.W.5
  • 8
    • 0026101901 scopus 로고
    • Stereochemical studies of the beta-elimination reactions at aldehydic abasic sites in DNA: Endonuclease III from Escherichia coli, sodium hydroxide, and Lys-Trp-Lys
    • Mazumder, A., et al., & Bolton, P.H. (1991). Stereochemical studies of the beta-elimination reactions at aldehydic abasic sites in DNA: Endonuclease III from Escherichia coli, sodium hydroxide, and Lys-Trp-Lys. Biochemistry 30, 1119-1126.
    • (1991) Biochemistry , vol.30 , pp. 1119-1126
    • Mazumder, A.1    Bolton, P.H.2
  • 9
    • 0023127167 scopus 로고
    • Escherichia coli endonuclease III is not an endonuclease but a β-elimination catalyst
    • Bailly, V. & Verly, W.G. (1987). Escherichia coli endonuclease III is not an endonuclease but a β-elimination catalyst. Biochem. J. 242, 565-572.
    • (1987) Biochem. J. , vol.242 , pp. 565-572
    • Bailly, V.1    Verly, W.G.2
  • 10
    • 0024283985 scopus 로고
    • The mechanisms of action of E. coli endonuclease III and T4 UV endonuclease (endonuclease V) at AP sites
    • Kim, J. & Linn, S. (1988). The mechanisms of action of E. coli endonuclease III and T4 UV endonuclease (endonuclease V) at AP sites. Nucleic Acids Res. 16, 1135-1141.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 1135-1141
    • Kim, J.1    Linn, S.2
  • 11
    • 0025120572 scopus 로고
    • The enzymology of apurinic/apyrimidinic endonucleases
    • Doetsch, P.W. & Cunningham, R.P. (1990). The enzymology of apurinic/apyrimidinic endonucleases. Mutat. Res. 236, 173-201.
    • (1990) Mutat. Res. , vol.236 , pp. 173-201
    • Doetsch, P.W.1    Cunningham, R.P.2
  • 12
    • 0343879974 scopus 로고
    • Endonuclease III (nth) mutants of Escherichia coli
    • Cunningham, R.P. & Weiss, B. (1985). Endonuclease III (nth) mutants of Escherichia coli. Proc. Natl. Acad Sci. USA 82, 474-478.
    • (1985) Proc. Natl. Acad Sci. USA , vol.82 , pp. 474-478
    • Cunningham, R.P.1    Weiss, B.2
  • 13
    • 0024393445 scopus 로고
    • Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene
    • Asahara, H., Wistort, P.M., Bank, J.F., Bakerian, R.H. & Cunningham, R.P. (1989). Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene. Biochemistry 28, 4444-4449.
    • (1989) Biochemistry , vol.28 , pp. 4444-4449
    • Asahara, H.1    Wistort, P.M.2    Bank, J.F.3    Bakerian, R.H.4    Cunningham, R.P.5
  • 14
    • 0024400711 scopus 로고
    • Endonuclease III is an iron-sulfur protein
    • Cunningham, R.P., et al., & Emptage, M.H. (1989). Endonuclease III is an iron-sulfur protein. Biochemistry 28, 4450-4455.
    • (1989) Biochemistry , vol.28 , pp. 4450-4455
    • Cunningham, R.P.1    Emptage, M.H.2
  • 16
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer, M.M., Ahern, H., Xing, D., Cunningham, R.P. & Tainer, J.A. (1995). Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 14, 4108-4120.
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 17
    • 0026707674 scopus 로고
    • The role of the iron-sulfur cluster in Escherichia coli endonuclease III. A resonance Raman study
    • Fu, W., O'Handley, S., Cunningham, R.P. & Johnson, M.K. (1992). The role of the iron-sulfur cluster in Escherichia coli endonuclease III. A resonance Raman study. J. Biol. Chem. 267, 16135-16137.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16135-16137
    • Fu, W.1    O'Handley, S.2    Cunningham, R.P.3    Johnson, M.K.4
  • 18
    • 0024332124 scopus 로고
    • Escherichia coli mutY gene encodes an adenine glycosylase active on G-A mispairs
    • Au, K.G., Clark, S., Miller, J.H. & Modrich, P. (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
  • 19
    • 0025301064 scopus 로고
    • MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III
    • Michaels, M.L., Pham, L., Nghiem, Y., Cruz, C. & Miller, J.H. (1990). MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III. Nucleic Acids Res. 18, 3841-3845.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3841-3845
    • Michaels, M.L.1    Pham, L.2    Nghiem, Y.3    Cruz, C.4    Miller, J.H.5
  • 20
    • 0026703168 scopus 로고
    • Escherichia coli MutY protein has both N-glycosylase and apurinic/apyrimidinic endonuclease activities on A·C and A·G mispairs
    • Tsai-Wu, J.J., Liu, H.F. & Lu, A.L. (1992). Escherichia coli MutY protein has both N-glycosylase and apurinic/apyrimidinic endonuclease activities on A·C and A·G mispairs. Proc. Natl Acad. Sci. USA 89, 8779-8783.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8779-8783
    • Tsai-Wu, J.J.1    Liu, H.F.2    Lu, A.L.3
  • 21
    • 0030004207 scopus 로고    scopus 로고
    • Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage
    • Slupska, M.M., Baikalov, C., Luther, W.M., Chiang, J.H., Wei, Y.F. & Miller, J.H. (1996). Cloning and sequencing a human homolog (hMyh) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage. J. Bacteriol. 178, 3885-3892.
    • (1996) J. Bacteriol. , vol.178 , pp. 3885-3892
    • Slupska, M.M.1    Baikalov, C.2    Luther, W.M.3    Chiang, J.H.4    Wei, Y.F.5    Miller, J.H.6
  • 22
    • 0029800969 scopus 로고    scopus 로고
    • Substrate specificity of Escherichia coli MutY protein
    • Bulychev, N.V., et al., & Johnson, F. (1996). Substrate specificity of Escherichia coli MutY protein. Biochemistry 35, 13147-13156.
    • (1996) Biochemistry , vol.35 , pp. 13147-13156
    • Bulychev, N.V.1    Johnson, F.2
  • 23
    • 0032497404 scopus 로고    scopus 로고
    • MutY DNA glycosylase: Base release and intermediate complex formation
    • Zharkov, D.O. & Grollman, A.P. (1998). MutY DNA glycosylase: Base release and intermediate complex formation. Biochemistry 37, 12384-12394.
    • (1998) Biochemistry , vol.37 , pp. 12384-12394
    • Zharkov, D.O.1    Grollman, A.P.2
  • 24
    • 0029834498 scopus 로고    scopus 로고
    • Counteracting the mutagenic effect of hydrolytic deamination of DNA 5-methylcytosine residues at high temperature: DNA mismatch N-glycosylase Mig.Mth of the thermophilic archaeon Methanobacterium thermoautotrophicum THF
    • Horst, J.P. & Fritz, H.J. (1996). Counteracting the mutagenic effect of hydrolytic deamination of DNA 5-methylcytosine residues at high temperature: DNA mismatch N-glycosylase Mig.Mth of the thermophilic archaeon Methanobacterium thermoautotrophicum THF. EMBO J. 15, 5459-5469.
    • (1996) EMBO J. , vol.15 , pp. 5459-5469
    • Horst, J.P.1    Fritz, H.J.2
  • 25
    • 0032953961 scopus 로고    scopus 로고
    • Methanobacterium thermoformicicium thymine DNA mismatch glycosylase: Conversion of an N-glycosylase to an AP lyase
    • Begley, T. & Cunningham, R.P. (1999). Methanobacterium thermoformicicium thymine DNA mismatch glycosylase: Conversion of an N-glycosylase to an AP lyase. Prot. Eng. 12, 333-340
    • (1999) Prot. Eng. , vol.12 , pp. 333-340
    • Begley, T.1    Cunningham, R.P.2
  • 26
    • 0028800939 scopus 로고
    • Purification and cloning of Micrococcus luteus ultraviolet endonuclease, an N-glycosylase/abasic lyase that proceeds via an imino enzyme-DNA intermediate
    • Piersen, C.E., Prince, M.A., Augustine, M.L., Dodson, M.L. & Lloyd, R.S. (1995). Purification and cloning of Micrococcus luteus ultraviolet endonuclease, an N-glycosylase/abasic lyase that proceeds via an imino enzyme-DNA intermediate. J. Biol. Chem. 270, 23475-23484.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23475-23484
    • Piersen, C.E.1    Prince, M.A.2    Augustine, M.L.3    Dodson, M.L.4    Lloyd, R.S.5
  • 27
    • 0030890419 scopus 로고    scopus 로고
    • Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III
    • Hilbert, T.P., Chaung, W., Boorstein, R.J., Cunningham, R.P. & Teebor, G.W. (1997). Cloning and expression of the cDNA encoding the human homologue of the DNA repair enzyme, Escherichia coli endonuclease III. J. Biol. Chem. 272, 6733-6740.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6733-6740
    • Hilbert, T.P.1    Chaung, W.2    Boorstein, R.J.3    Cunningham, R.P.4    Teebor, G.W.5
  • 29
    • 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., et al., & 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    Verdine, G.L.2
  • 30
    • 0029896229 scopus 로고    scopus 로고
    • Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N- methylformamidopyrimidine
    • van der Kemp, P.A., Thomas, D., Barbey, R., de Oliveira, R. & Boiteux, S. (1996). Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N- methylformamidopyrimidine. Proc. Natl Acad. Sci. USA 93, 5197-5202.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5197-5202
    • Van Der Kemp, P.A.1    Thomas, D.2    Barbey, R.3    De Oliveira, R.4    Boiteux, S.5
  • 31
    • 0029929070 scopus 로고    scopus 로고
    • The helix-hairpin-helix DNA-binding motif: A structural basis for non-sequence-specific recognition of DNA
    • Doherty, A.J., Serpell, L.C. & Ponting, C.P. (1996). The helix-hairpin-helix DNA-binding motif: A structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res. 24, 2488-2497.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2488-2497
    • Doherty, A.J.1    Serpell, L.C.2    Ponting, C.P.3
  • 32
    • 0031763884 scopus 로고    scopus 로고
    • MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily
    • Guan, Y., et al., & Tainer, J.A. (1998). MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily. Nat. Struct. Biol. 5, 1058-1064.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1058-1064
    • Guan, Y.1    Tainer, J.A.2
  • 33
    • 0028924802 scopus 로고
    • Endonuclease III interactions with DNA substrates. I. Binding and footprinting studies with oligonucleotides containing a reduced apyrimidinic site
    • O'Handley, S., Scholes, C.P. & Cunningham, R.P. (1995). Endonuclease III interactions with DNA substrates. I. Binding and footprinting studies with oligonucleotides containing a reduced apyrimidinic site. Biochemistry 34, 2528-2536.
    • (1995) Biochemistry , vol.34 , pp. 2528-2536
    • O'Handley, S.1    Scholes, C.P.2    Cunningham, R.P.3
  • 34
    • 0028906380 scopus 로고
    • Endonuclease III interactions with DNA substrates. II. The DNA repair enzyme endonuclease III binds differently to intact DNA and to apyrimidinic/apurinic DNA substrates as shown by tryptophan fluorescence quenching
    • Xing, D., Dorr, R., Cunningham, R.P. & Scholes, C.P. (1995). Endonuclease III interactions with DNA substrates. II. The DNA repair enzyme endonuclease III binds differently to intact DNA and to apyrimidinic/apurinic DNA substrates as shown by tryptophan fluorescence quenching. Biochemistry 34, 2537-2544.
    • (1995) Biochemistry , vol.34 , pp. 2537-2544
    • Xing, D.1    Dorr, R.2    Cunningham, R.P.3    Scholes, C.P.4
  • 36
    • 44949291986 scopus 로고
    • Three-dimensional triple resonance NMR spectroscopy of isotropically enriched proteins
    • Kay, L.E., Ikura, M., Tschudin, R. & Bax, A. (1990). Three-dimensional triple resonance NMR spectroscopy of isotropically enriched proteins. J. Magn. Reson. 89, 496-514.
    • (1990) J. Magn. Reson. , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 37
    • 44049117010 scopus 로고
    • Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein
    • Grzesiek, S. & Bax, A. (1992). Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein. J. Magn. Reson. 96, 432-440.
    • (1992) J. Magn. Reson. , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 38
    • 0026836698 scopus 로고
    • A refocussed and optimized HNCA: Increased sensitivity and resolution in large macromolecules
    • Farmer II, B.T., Venters, L.D., Spicer, L.D., Wittekind, M.G. & Mueller, L. (1992). A refocussed and optimized HNCA: Increased sensitivity and resolution in large macromolecules. J. Biomol. NMR 2, 195-202.
    • (1992) J. Biomol. NMR , vol.2 , pp. 195-202
    • Farmer B.T. II1    Venters, L.D.2    Spicer, L.D.3    Wittekind, M.G.4    Mueller, L.5
  • 41
    • 43949167657 scopus 로고
    • HNCACB, a high sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with alpha and beta carbon resonances in proteins
    • Wittekind, M.G. & Mueller, L. (1993). HNCACB, a high sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with alpha and beta carbon resonances in proteins. J. Magn. Reson. B 101, 201-295.
    • (1993) J. Magn. Reson. B , vol.101 , pp. 201-295
    • Wittekind, M.G.1    Mueller, L.2
  • 42
    • 0024362326 scopus 로고
    • 15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser- multiple quantum coherence spectroscopy: Application to interleukin 1 beta
    • 15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser- multiple quantum coherence spectroscopy: Application to interleukin 1 beta. Biochemistry 28, 6150-6156.
    • (1989) Biochemistry , vol.28 , pp. 6150-6156
    • Marion, D.1    Clore, G.M.2
  • 43
    • 0024595889 scopus 로고
    • Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a
    • Zuiderweg, E.R. & Fesik, S.W. (1989). Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a. Biochemistry 28, 2387-2391.
    • (1989) Biochemistry , vol.28 , pp. 2387-2391
    • Zuiderweg, E.R.1    Fesik, S.W.2
  • 45
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR 5, 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 48
    • 0031576984 scopus 로고    scopus 로고
    • + binding to perdeuterated MurB: Backbone atom NMR assignments and chemical-shift changes
    • + binding to perdeuterated MurB: Backbone atom NMR assignments and chemical-shift changes. J. Mol. Biol. 267, 1223-1246.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1223-1246
    • Constantine, K.L.1    Farmer B.T. II2
  • 49
    • 0030666085 scopus 로고    scopus 로고
    • Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation
    • Williamson, R.A., Carr, M.D., Frenkiel, T.A., Feeney, J. & Freedman, R.B. (1997). Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation. Biochemistry 36, 13882-13889.
    • (1997) Biochemistry , vol.36 , pp. 13882-13889
    • Williamson, R.A.1    Carr, M.D.2    Frenkiel, T.A.3    Feeney, J.4    Freedman, R.B.5
  • 50
    • 0030671070 scopus 로고    scopus 로고
    • Chemical shift mapping of the RNA-binding interface of the multiple-RBD protein sex-lethal
    • Lee, A.L., et al., & Wemmer, D.E. (1997). Chemical shift mapping of the RNA-binding interface of the multiple-RBD protein sex-lethal. Biochemistry 36, 14306-14317.
    • (1997) Biochemistry , vol.36 , pp. 14306-14317
    • Lee, A.L.1    Wemmer, D.E.2
  • 51
    • 0030822248 scopus 로고    scopus 로고
    • NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1
    • Schmiedeskamp, M., Rajagopal, P. & Klevit, R.E. (1997). NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1. Protein Sci. 6, 1835-1848.
    • (1997) Protein Sci. , vol.6 , pp. 1835-1848
    • Schmiedeskamp, M.1    Rajagopal, P.2    Klevit, R.E.3
  • 52
    • 2642605367 scopus 로고    scopus 로고
    • Demonstration of protein-protein interaction specificity by NMR chemical shift mapping
    • Rajagopal, P., Waygood, E.B., Reizer, J., Saier, M.H., Jr. & Klevit, R.E. (1997). Demonstration of protein-protein interaction specificity by NMR chemical shift mapping. Protein Sci. 6, 2624-2627.
    • (1997) Protein Sci. , vol.6 , pp. 2624-2627
    • Rajagopal, P.1    Waygood, E.B.2    Reizer, J.3    Saier M.H., Jr.4    Klevit, R.E.5
  • 53
    • 0032113850 scopus 로고    scopus 로고
    • Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA
    • Foster, M.P., et al., & Wright, P.E. (1998). Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA. J. Biomol. NMR 12, 51-71.
    • (1998) J. Biomol. NMR , vol.12 , pp. 51-71
    • Foster, M.P.1    Wright, P.E.2
  • 54
    • 0031149139 scopus 로고    scopus 로고
    • How do DNA repair proteins locate damaged bases in the genome?
    • Verdine, G.L. & Bruner, S.D. (1997). How do DNA repair proteins locate damaged bases in the genome? Chem. Biol. 4, 329-334.
    • (1997) Chem. Biol. , vol.4 , pp. 329-334
    • Verdine, G.L.1    Bruner, S.D.2
  • 55
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
    • Slupphaug, G., Mol, C.D., Kavli, B., Arvai, A.S., Krokan, H.E. & Tainer, J.A. (1996). A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Nature 384, 87-92.
    • (1996) Nature , vol.384 , pp. 87-92
    • Slupphaug, G.1    Mol, C.D.2    Kavli, B.3    Arvai, A.S.4    Krokan, H.E.5    Tainer, J.A.6
  • 56
    • 0032167424 scopus 로고    scopus 로고
    • Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA
    • Parikh, S.S., Mol, C.D., Slupphaug, G., Bharati, S., Krokan, H.E. & Tainer, J.A. (1998). Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. EMBO J. 17, 5214-5226.
    • (1998) EMBO J. , vol.17 , pp. 5214-5226
    • Parikh, S.S.1    Mol, C.D.2    Slupphaug, G.3    Bharati, S.4    Krokan, H.E.5    Tainer, J.A.6
  • 57
    • 0030703177 scopus 로고    scopus 로고
    • Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites
    • Bjoras, M., et al., & Seeberg, E. (1997). Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites. EMBO J. 16, 6314-6322.
    • (1997) EMBO J. , vol.16 , pp. 6314-6322
    • Bjoras, M.1    Seeberg, E.2
  • 58
    • 0031926508 scopus 로고    scopus 로고
    • Opposite base-dependent excision of 7,8-dihydro-8-oxoadenine by the Ogg1 protein of Saccharomyces cerevisiae
    • Girard, P.M., D'Ham, C., Cadet, J. & Boiteux, S. (1998). Opposite base-dependent excision of 7,8-dihydro-8-oxoadenine by the Ogg1 protein of Saccharomyces cerevisiae. Carcinogenesis 19, 1299-1305.
    • (1998) Carcinogenesis , vol.19 , pp. 1299-1305
    • Girard, P.M.1    D'Ham, C.2    Cadet, J.3    Boiteux, S.4
  • 59
    • 0028010888 scopus 로고
    • Hhal methyltransferase flips its target base out of the DNA helix
    • Klimasauskas, S., Kumar, S., Roberts, R.J. & Cheng, X. (1994). Hhal methyltransferase flips its target base out of the DNA helix. Cell 76, 357-369.
    • (1994) Cell , vol.76 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 60
    • 0029068629 scopus 로고
    • The crystal structure of Haelll methyltransferase convalently complexed to DNA: An extrahelical cytosine and rearranged base pairing
    • Reinisch, K.M., Chen, L., Verdine, G.L. & Lipscomb, W.N. (1995). The crystal structure of Haelll methyltransferase convalently complexed to DNA: An extrahelical cytosine and rearranged base pairing. Cell 82, 143-153.
    • (1995) Cell , vol.82 , pp. 143-153
    • Reinisch, K.M.1    Chen, L.2    Verdine, G.L.3    Lipscomb, W.N.4
  • 61
    • 0031667109 scopus 로고    scopus 로고
    • Structures of Hhal methyltransferase complexed with substrates containing mismatches at the target base
    • O'Gara, M., Horton, J.R., Roberts, R.J. & Cheng, X. (1998). Structures of Hhal methyltransferase complexed with substrates containing mismatches at the target base. Nat. Struct. Biol. 5, 872-877.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 872-877
    • O'Gara, M.1    Horton, J.R.2    Roberts, R.J.3    Cheng, X.4
  • 62
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul, S.F., et al., & Lipman, D.J. (1997). Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res, 25, 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Lipman, D.J.2
  • 63
    • 0024836418 scopus 로고
    • Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance
    • Muchmore, D.C., McIntosh, L.P., Russell, C.B., Anderson, D.E. & Dahlquist, F.W. (1989). Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods Enzymol. 177, 44-73.
    • (1989) Methods Enzymol. , vol.177 , pp. 44-73
    • Muchmore, D.C.1    McIntosh, L.P.2    Russell, C.B.3    Anderson, D.E.4    Dahlquist, F.W.5
  • 64
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three dimensional NMR experiments with improved sensitivity
    • Munhandriham, D.R. & Kay, L.E. (1994). Gradient-enhanced triple-resonance three dimensional NMR experiments with improved sensitivity. J. Magn. Res. B 103, 203-216.
    • (1994) J. Magn. Res. B , vol.103 , pp. 203-216
    • Munhandriham, D.R.1    Kay, L.E.2
  • 66
    • 48749144559 scopus 로고
    • Evaluation of a new broadband decoupling sequence: WALTZ-16
    • Shaka, A.J., Keeler, J. & Freeman, R. (1983). Evaluation of a new broadband decoupling sequence: WALTZ-16. J. Magn. Res. 53, 313-340.
    • (1983) J. Magn. Res. , vol.53 , pp. 313-340
    • Shaka, A.J.1    Keeler, J.2    Freeman, R.3
  • 67
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-Model internet based tool for automated comparative protein modelling
    • Peitsch, M.C. (1996). ProMod and Swiss-Model internet based tool for automated comparative protein modelling. Biochem. Soc. Trans. 24, 274-279.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 68
    • 0031473847 scopus 로고    scopus 로고
    • Swiss-Model and the Swiss-Pdbviewer: An environment for comparative protein modelling
    • Guex, N. & Peitsch, M.C. (1997). Swiss-Model and the Swiss-Pdbviewer: An environment for comparative protein modelling. Electrophoresis 18, 2714.
    • (1997) Electrophoresis , vol.18 , pp. 2714
    • Guex, N.1    Peitsch, M.C.2
  • 69
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of a protein structure
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: A program to check the stereochemical quality of a protein structure. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 70
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V. & Sklenar, V. (1992). Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 71
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. (1993). SETOR: Hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics 11, 134-138.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 72
    • 0000732609 scopus 로고
    • GRASP: A graphical representation and analysis of surface properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP: A graphical representation and analysis of surface properties. Biophys. J. 64, A166.
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.