메뉴 건너뛰기




Volumn 3, Issue 2, 2004, Pages 277-287

Redox potential regulates binding of universal minicircle sequence binding protein at the kinetoplast DNA replication origin

Author keywords

[No Author keywords available]

Indexed keywords

1,10 PHENANTHROLINE; 1,10-PHENANTHROLINE; DNA BINDING PROTEIN; KINETOPLAST DNA; PHENANTHROLINE DERIVATIVE; PROTOZOAL PROTEIN; THIOREDOXIN; UNIVERSAL MINICIRCLE SEQUENCE BINDING PROTEIN, PROTOZOAN; ZINC; ZINC FINGER PROTEIN;

EID: 16544372631     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.3.2.277-287.2004     Document Type: Article
Times cited : (55)

References (75)
  • 1
    • 0029328649 scopus 로고
    • Reversible oxidative aggregation obstructs specific proteolytic cleavage of glutathione S-transferase fusion proteins
    • Abeliovich, H., and J. Shlomai. 1995. Reversible oxidative aggregation obstructs specific proteolytic cleavage of glutathione S-transferase fusion proteins. Anal. Biochem. 228:351-354.
    • (1995) Anal. Biochem. , vol.228 , pp. 351-354
    • Abeliovich, H.1    Shlomai, J.2
  • 2
    • 0027422980 scopus 로고
    • A trypanosomal CCHC-type zinc finger protein which binds the conserved universal sequence of kinetoplast DNA minicircles: Isolation and analysis of the complete cDNA from Crithidia fasciculata
    • Abeliovich, H., Y. Tzfati, and J. Shlomai. 1993. A trypanosomal CCHC-type zinc finger protein which binds the conserved universal sequence of kinetoplast DNA minicircles: isolation and analysis of the complete cDNA from Crithidia fasciculata. Mol. Cell. Biol. 13:7766-7773.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7766-7773
    • Abeliovich, H.1    Tzfati, Y.2    Shlomai, J.3
  • 3
    • 0033532083 scopus 로고    scopus 로고
    • Universal minicircle sequence-binding protein, a sequence-specific DNA-binding protein that recognizes the two replication origins of the kinetoplast DNA minicircle
    • Abu-Elneel, K., I. Kapeller, and J. Shlomai. 1999. Universal minicircle sequence-binding protein, a sequence-specific DNA-binding protein that recognizes the two replication origins of the kinetoplast DNA minicircle. J. Biol. Chem. 274:13419-13426.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13419-13426
    • Abu-Elneel, K.1    Kapeller, I.2    Shlomai, J.3
  • 4
    • 0035858881 scopus 로고    scopus 로고
    • Intramitochondrial localization of universal minicircle sequence-binding protein, a trypanosomatid protein that binds kinetoplast minicircle replication origins
    • Abu-Elneel, K., D. R. Robinson, M. E. Drew, P. T. Englund, and J. Shlomai. 2001. Intramitochondrial localization of universal minicircle sequence-binding protein, a trypanosomatid protein that binds kinetoplast minicircle replication origins. J. Cell Biol. 153:725-734.
    • (2001) J. Cell Biol. , vol.153 , pp. 725-734
    • Abu-Elneel, K.1    Robinson, D.R.2    Drew, M.E.3    Englund, P.T.4    Shlomai, J.5
  • 5
    • 0034716939 scopus 로고    scopus 로고
    • NMR structure of stem-loop SL2 of the HIV-1 psi RNA packaging signal reveals a novel A-U-A base-triple platform
    • Amarasinghe, G. K., R. N. De Guzman, R. B. Turner, and M. F. Summers. 2000. NMR structure of stem-loop SL2 of the HIV-1 psi RNA packaging signal reveals a novel A-U-A base-triple platform. J. Mol. Biol. 299:145-156.
    • (2000) J. Mol. Biol. , vol.299 , pp. 145-156
    • Amarasinghe, G.K.1    De Guzman, R.N.2    Turner, R.B.3    Summers, M.F.4
  • 6
    • 0028809552 scopus 로고
    • A single-stranded DNA binding protein binds the origin of replication of the duplex kinetoplast DNA
    • Avrahami, D., Y. Tzfati, and J. Shlomai. 1995. A single-stranded DNA binding protein binds the origin of replication of the duplex kinetoplast DNA. Proc. Natl. Acad. Sci. USA 92:10511-10515.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10511-10515
    • Avrahami, D.1    Tzfati, Y.2    Shlomai, J.3
  • 7
    • 0036282179 scopus 로고    scopus 로고
    • Redox control of zinc finger proteins
    • Baldwin, M. A., and C. C. Benz. 2002. Redox control of zinc finger proteins. Methods Enzymol. 353:54-69.
    • (2002) Methods Enzymol. , vol.353 , pp. 54-69
    • Baldwin, M.A.1    Benz, C.C.2
  • 8
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • Berg, J. M., and Y. Shi. 1996. The galvanization of biology: a growing appreciation for the roles of zinc. Science 271:1081-1085.
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 9
    • 0027366669 scopus 로고
    • Functional complementation of an Escherichia coli ribonuclease H mutation by a cloned genomic fragment from the trypanosomatid Crithidia fasciculata
    • Campbell, A. G., and D. S. Ray. 1993. Functional complementation of an Escherichia coli ribonuclease H mutation by a cloned genomic fragment from the trypanosomatid Crithidia fasciculata. Proc. Natl. Acad. Sci. USA 90: 9350-9354.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9350-9354
    • Campbell, A.G.1    Ray, D.S.2
  • 10
    • 0034163437 scopus 로고    scopus 로고
    • HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase
    • Davis, D. A., F. M. Newcomb, J. Moskovitz, P. T. Wingfield, S. J. Stahl, J. Kaufman, H. M. Fales, R. L. Levine, and R. Yarchoan. 2000. HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductase. Biochem. J. 346:305-311.
    • (2000) Biochem. J. , vol.346 , pp. 305-311
    • Davis, D.A.1    Newcomb, F.M.2    Moskovitz, J.3    Wingfield, P.T.4    Stahl, S.J.5    Kaufman, J.6    Fales, H.M.7    Levine, R.L.8    Yarchoan, R.9
  • 11
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element
    • De Guzman, R. N. Z. R. Wu, C. C. Stalling, L. Pappalardo, P. N. Borer, and M. F. Summers. 1998. Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element. Science 279:384-388.
    • (1998) Science , vol.279 , pp. 384-388
    • De Guzman, R.N.1    Wu, Z.R.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 12
    • 0035253755 scopus 로고    scopus 로고
    • The Crithidia fasciculata RNH1 gene encodes both nuclear and mitochondrial isoforms of RNase H
    • Engel, M. L., J. C. Hines, and D. S. Ray. 2001. The Crithidia fasciculata RNH1 gene encodes both nuclear and mitochondrial isoforms of RNase H. Nucleic Acids Res. 29:725-731.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 725-731
    • Engel, M.L.1    Hines, J.C.2    Ray, D.S.3
  • 13
    • 0033587740 scopus 로고    scopus 로고
    • The kinetoplast structure-specific endonuclease I is related to the 5′ exo/endonuclease domain of bacterial DNA polymerase I and colocalizes with the kinetoplast topoisomerase II and DNA polymerase beta during replication
    • Engel, M. L., and D. S. Ray. 1999. The kinetoplast structure-specific endonuclease I is related to the 5′ exo/endonuclease domain of bacterial DNA polymerase I and colocalizes with the kinetoplast topoisomerase II and DNA polymerase beta during replication. Proc. Natl. Acad. Sci. USA 96:8455-8460.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8455-8460
    • Engel, M.L.1    Ray, D.S.2
  • 14
    • 0032531865 scopus 로고    scopus 로고
    • A structure-specific DNA endonuclease is enriched in kinetoplasts purified from Crithidia fasciculata
    • Engel, M. L., and D. S. Ray. 1998. A structure-specific DNA endonuclease is enriched in kinetoplasts purified from Crithidia fasciculata. Nucleic Acids Res. 26:4733-4738.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4733-4738
    • Engel, M.L.1    Ray, D.S.2
  • 15
    • 0022002912 scopus 로고
    • Trypanothione: A novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids
    • Fairlamb, A. H., P. Blackburn, P. Ulrich, B. T. Chait, and A. Cerami. 1985. Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids. Science 227:1485-1487.
    • (1985) Science , vol.227 , pp. 1485-1487
    • Fairlamb, A.H.1    Blackburn, P.2    Ulrich, P.3    Chait, B.T.4    Cerami, A.5
  • 16
    • 0021933665 scopus 로고
    • Identification of a novel, thiol-containing co-factor essential for glutathione reductase enzyme activity in trypanosomatids
    • Fairlamb, A. H., and A. Ceraml. 1985. Identification of a novel, thiol-containing co-factor essential for glutathione reductase enzyme activity in trypanosomatids. Mol. Biochem. Parasitol. 14:187-198.
    • (1985) Mol. Biochem. Parasitol. , vol.14 , pp. 187-198
    • Fairlamb, A.H.1    Ceraml, A.2
  • 18
    • 0031733864 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of Mason-Pfizer monkey virus (MPMV) nucleocapsid protein
    • Gao, Y., K. Kaluarachchi, and D. P. Giedroc. 1998. Solution structure and backbone dynamics of Mason-Pfizer monkey virus (MPMV) nucleocapsid protein. Protein Sci. 7:2265-2280.
    • (1998) Protein Sci. , vol.7 , pp. 2265-2280
    • Gao, Y.1    Kaluarachchi, K.2    Giedroc, D.P.3
  • 19
    • 0034507456 scopus 로고    scopus 로고
    • Functions and mechanisms of RNA editing
    • Gott, J. M., and R. B. Emeson. 2000. Functions and mechanisms of RNA editing. Annu. Rev. Genet. 34:499-531.
    • (2000) Annu. Rev. Genet. , vol.34 , pp. 499-531
    • Gott, J.M.1    Emeson, R.B.2
  • 20
    • 0037053366 scopus 로고    scopus 로고
    • A trypanosome mitochondrial RNA polymerase is required for transcription and replication
    • Grams, J., J. C. Morris, M. E. Drew, Z. Wang, P. T. Englund, and S. L. Hajduk. 2002. A trypanosome mitochondrial RNA polymerase is required for transcription and replication. J. Biol. Chem. 277:16952-16959.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16952-16959
    • Grams, J.1    Morris, J.C.2    Drew, M.E.3    Wang, Z.4    Englund, P.T.5    Hajduk, S.L.6
  • 21
    • 0021962337 scopus 로고
    • Proof that the endogenous, heat-stable glucocorticoid receptor-activating factor is thioredoxin
    • Grippo, J. F., A. Holmgren, and W. B. Pratt. 1985. Proof that the endogenous, heat-stable glucocorticoid receptor-activating factor is thioredoxin. J. Biol. Chem. 260:93-97.
    • (1985) J. Biol. Chem. , vol.260 , pp. 93-97
    • Grippo, J.F.1    Holmgren, A.2    Pratt, W.B.3
  • 22
    • 0024779343 scopus 로고
    • What is the role of the cys-his motif in retroviral nucleocapsid (NC) proteins?
    • Katz, R. A., and J. E. Jentoft. 1989. What is the role of the cys-his motif in retroviral nucleocapsid (NC) proteins? Bioessays 11:176-181.
    • (1989) Bioessays , vol.11 , pp. 176-181
    • Katz, R.A.1    Jentoft, J.E.2
  • 23
    • 0036342502 scopus 로고    scopus 로고
    • Multiple mitochondrial DNA polymerases in Trypanosoma brucei
    • Klingbeil, M. M., S. A. Motyka, and P. T. Englund. 2002. Multiple mitochondrial DNA polymerases in Trypanosoma brucei. Mol. Cell 10:175-186.
    • (2002) Mol. Cell , vol.10 , pp. 175-186
    • Klingbeil, M.M.1    Motyka, S.A.2    Englund, P.T.3
  • 24
    • 0029032723 scopus 로고
    • Protein motifs. 5. Zinc fingers
    • Klug, A., and J. W. Schwabe. 1995. Protein motifs. 5. Zinc fingers. FASEB J. 9:597-604.
    • (1995) FASEB J. , vol.9 , pp. 597-604
    • Klug, A.1    Schwabe, J.W.2
  • 25
    • 0030792096 scopus 로고    scopus 로고
    • Role of TrfA and DnaA proteins in origin opening during initiation of DNA replication of the broad host range plasmid RK2
    • Konieczny, I., K. S. Doran, D. R. Helinski, and A. Blasina. 1997. Role of TrfA and DnaA proteins in origin opening during initiation of DNA replication of the broad host range plasmid RK2. J. Biol. Chem. 272:20173-20178.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20173-20178
    • Konieczny, I.1    Doran, K.S.2    Helinski, D.R.3    Blasina, A.4
  • 26
    • 0031443871 scopus 로고    scopus 로고
    • The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone
    • Konieczny, I., and D. R. Helinski. 1997. The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone. Proc. Natl. Acad. Sci. USA 94:14378-14382.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14378-14382
    • Konieczny, I.1    Helinski, D.R.2
  • 27
    • 0035294657 scopus 로고    scopus 로고
    • Redox modulation of the activity of DNA topoisomerase I from carrot (Daucus carota) mitochondria
    • Konstantinov, Y., V. I. Tarasenko, and I. B. Rogozin. 2001. Redox modulation of the activity of DNA topoisomerase I from carrot (Daucus carota) mitochondria. Dokl. Biochem. Biophys. 377:82-84.
    • (2001) Dokl. Biochem. Biophys. , vol.377 , pp. 82-84
    • Konstantinov, Y.1    Tarasenko, V.I.2    Rogozin, I.B.3
  • 28
    • 0033215010 scopus 로고    scopus 로고
    • Enzymes of parasite thiol metabolism as drug targets
    • Krauth-Siegel, R. L., and G. H. Coombs. 1999. Enzymes of parasite thiol metabolism as drug targets. Parasitol. Today 15:404-409.
    • (1999) Parasitol. Today , vol.15 , pp. 404-409
    • Krauth-Siegel, R.L.1    Coombs, G.H.2
  • 29
    • 0033752435 scopus 로고    scopus 로고
    • Redox modulation of chloroplast DNA replication in Chlamydomonas reinhardtii
    • Lau, K. W., J. Ren, and M. Wu. 2000. Redox modulation of chloroplast DNA replication in Chlamydomonas reinhardtii. Antioxid. Redox Signal. 2:529-535.
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 529-535
    • Lau, K.W.1    Ren, J.2    Wu, M.3
  • 30
    • 0030749260 scopus 로고    scopus 로고
    • A mitochondrial DNA primase from the trypanosomatid Crithidia fasciculata
    • Li, C., and P. T. Englund. 1997. A mitochondrial DNA primase from the trypanosomatid Crithidia fasciculata. J. Biol. Chem. 272:20787-20792.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20787-20792
    • Li, C.1    Englund, P.T.2
  • 31
    • 0024499435 scopus 로고
    • Novobiocin affinity purification of a mitochondrial type II topoisomerase from the trypanosomatid Crithidia fasciculata
    • Melendy, T., and D. S. Ray. 1989. Novobiocin affinity purification of a mitochondrial type II topoisomerase from the trypanosomatid Crithidia fasciculata. J. Biol. Chem. 264:1870-1876.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1870-1876
    • Melendy, T.1    Ray, D.S.2
  • 32
    • 0024272032 scopus 로고
    • Localization of a type II DNA topoisomerase to two sites at the periphery of the kinetoplast DNA of Crithidia fasciculata
    • Melendy, T., C. Sheline, and D. S. Ray. 1988. Localization of a type II DNA topoisomerase to two sites at the periphery of the kinetoplast DNA of Crithidia fasciculata. Cell 55:1083-1088.
    • (1988) Cell , vol.55 , pp. 1083-1088
    • Melendy, T.1    Sheline, C.2    Ray, D.S.3
  • 33
    • 0031719808 scopus 로고    scopus 로고
    • Sequence, heterologous expression and functional characterization of a novel tryparedoxin from Crithidia fasciculata
    • Montemartini, M., H. M. Kalisz, M. Kiess, E. Nogoceke, M. Singh, P. Steinert, and L. Flohe. 1998. Sequence, heterologous expression and functional characterization of a novel tryparedoxin from Crithidia fasciculata. Biol. Chem. 379:1137-1142.
    • (1998) Biol. Chem. , vol.379 , pp. 1137-1142
    • Montemartini, M.1    Kalisz, H.M.2    Kiess, M.3    Nogoceke, E.4    Singh, M.5    Steinert, P.6    Flohe, L.7
  • 34
    • 0032570772 scopus 로고    scopus 로고
    • Sequence analysis of the tryparedoxin peroxidase gene from Crithidia fasciculata and its functional expression in Escherichia coli
    • Montemartini, M., E. Nogoceke, M. Singh, P. Steinert, L. Flohe, and H. M. Kalisz. 1998. Sequence analysis of the tryparedoxin peroxidase gene from Crithidia fasciculata and its functional expression in Escherichia coli. J. Biol. Chem. 273:4864-4871.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4864-4871
    • Montemartini, M.1    Nogoceke, E.2    Singh, M.3    Steinert, P.4    Flohe, L.5    Kalisz, H.M.6
  • 38
    • 0030861413 scopus 로고    scopus 로고
    • A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata
    • Nogoceke, E., D. U. Gommel, M. Kiess, H. M. Kalisz, and L. Flohe. 1997. A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata. Biol. Chem. 378:827-836.
    • (1997) Biol. Chem. , vol.378 , pp. 827-836
    • Nogoceke, E.1    Gommel, D.U.2    Kiess, M.3    Kalisz, H.M.4    Flohe, L.5
  • 39
    • 0032870929 scopus 로고    scopus 로고
    • Zinc finger of replication protein A, a non-DNA binding element, regulates its DNA binding activity through redox
    • Park, J. S., M. Wang, S. J. Park, and S. H. Lee. 1999. Zinc finger of replication protein A, a non-DNA binding element, regulates its DNA binding activity through redox. J. Biol. Chem. 274:29075-29080.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29075-29080
    • Park, J.S.1    Wang, M.2    Park, S.J.3    Lee, S.H.4
  • 40
    • 0024324798 scopus 로고
    • Identification of a zinc finger protein that binds to the sterol regulatory element
    • Rajavashisth, T. B., A. K. Taylor, A. Andalibi, K. L. Svenson, and A. J. Lusis. 1989. Identification of a zinc finger protein that binds to the sterol regulatory element. Science 245:640-643.
    • (1989) Science , vol.245 , pp. 640-643
    • Rajavashisth, T.B.1    Taylor, A.K.2    Andalibi, A.3    Svenson, K.L.4    Lusis, A.J.5
  • 41
    • 0023339897 scopus 로고
    • Kinetoplast DNA minicircles: High-copy-number mitochondrial plasmids
    • Ray, D. S. 1987. Kinetoplast DNA minicircles: high-copy-number mitochondrial plasmids. Plasmid 17:177-190.
    • (1987) Plasmid , vol.17 , pp. 177-190
    • Ray, D.S.1
  • 42
    • 0029006416 scopus 로고
    • Disruption of the Crithidia fasciculata RNH1 gene results in the loss of two active forms of ribonuclease H
    • Ray, D. S., and J. C. Hines. 1995. Disruption of the Crithidia fasciculata RNH1 gene results in the loss of two active forms of ribonuclease H. Nucleic Acids Res. 23:2526-2530.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2526-2530
    • Ray, D.S.1    Hines, J.C.2
  • 44
    • 0031984162 scopus 로고    scopus 로고
    • Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability
    • Rigobello, M. P., M. T. Callegaro, E. Barzon, M. Benetti, and A. Bindoli. 1998. Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability. Free Radic. Biol. Med. 24:370-376.
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 370-376
    • Rigobello, M.P.1    Callegaro, M.T.2    Barzon, E.3    Benetti, M.4    Bindoli, A.5
  • 45
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and G. Von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 46
    • 0039774420 scopus 로고    scopus 로고
    • NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine leukemia virus and the single-stranded pentanucleotide d(ACGCC): Comparison with HIV-NCp7 complexes
    • Schuler, W., C. Dong, K. Wecker, and B. P. Roques. 1999. NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine leukemia virus and the single-stranded pentanucleotide d(ACGCC): comparison with HIV-NCp7 complexes. Biochemistry 38:12984-12994.
    • (1999) Biochemistry , vol.38 , pp. 12984-12994
    • Schuler, W.1    Dong, C.2    Wecker, K.3    Roques, B.P.4
  • 47
    • 0028844115 scopus 로고
    • The structure and replication of kinetoplast DNA
    • Shapiro, T. A., and P. T. Englund. 1995. The structure and replication of kinetoplast DNA. Annu. Rev. Microbiol. 49:117-143.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 117-143
    • Shapiro, T.A.1    Englund, P.T.2
  • 48
    • 0028144787 scopus 로고
    • The assembly of kinetoplast DNA
    • Shlomai, J. 1994. The assembly of kinetoplast DNA. Parasitol. Today 10: 341-346.
    • (1994) Parasitol. Today , vol.10 , pp. 341-346
    • Shlomai, J.1
  • 50
    • 0027393609 scopus 로고
    • Zinc- and sequence-dependent binding to nucleic acids by the N-terminal zinc finger of the HIV-1 nucleocapsid protein: NMR structure of the complex with the Psi-site analog, dACGCC
    • South, T. L., and M. F. Summers. 1993. Zinc-and sequence-dependent binding to nucleic acids by the N-terminal zinc finger of the HIV-1 nucleocapsid protein: NMR structure of the complex with the Psi-site analog, dACGCC. Protein Sci. 2:3-19.
    • (1993) Protein Sci. , vol.2 , pp. 3-19
    • South, T.L.1    Summers, M.F.2
  • 51
    • 4244218956 scopus 로고    scopus 로고
    • Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism
    • Stadtman, E. R., J. Moskovitz, B. S. Berlett, and R. L. Levine. 2002. Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism. Mol. Cell. Biochem. 234-235:3-9.
    • (2002) Mol. Cell. Biochem. , vol.234-235 , pp. 3-9
    • Stadtman, E.R.1    Moskovitz, J.2    Berlett, B.S.3    Levine, R.L.4
  • 52
    • 0036194123 scopus 로고    scopus 로고
    • Trypanosomal antioxidants and emerging aspects of redox regulation in the trypanosomatids
    • Steenkamp, D. J. 2002. Trypanosomal antioxidants and emerging aspects of redox regulation in the trypanosomatids. Antioxid. Redox Signal. 4:105-121.
    • (2002) Antioxid. Redox Signal. , vol.4 , pp. 105-121
    • Steenkamp, D.J.1
  • 54
  • 55
    • 0029760957 scopus 로고    scopus 로고
    • Redox regulation of transcriptional activators
    • Sun, Y., and L. W. Oberley. 1996. Redox regulation of transcriptional activators. Free Radic. Biol. Med. 21:335-348.
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 335-348
    • Sun, Y.1    Oberley, L.W.2
  • 56
    • 0034889645 scopus 로고    scopus 로고
    • Molecular characterisation of mitochondrial and cytosolic trypanothione-dependent tryparedoxin peroxidases in Trypanosoma brucei
    • Tetaud, E., C. Giroud, A. R. Prescott, D. W. Parkin, D. Baltz, N. Biteau, T. Baltz, and A. H. Fairlamb. 2001. Molecular characterisation of mitochondrial and cytosolic trypanothione-dependent tryparedoxin peroxidases in Trypanosoma brucei. Mol. Biochem. Parasitol. 116:171-183.
    • (2001) Mol. Biochem. Parasitol. , vol.116 , pp. 171-183
    • Tetaud, E.1    Giroud, C.2    Prescott, A.R.3    Parkin, D.W.4    Baltz, D.5    Biteau, N.6    Baltz, T.7    Fairlamb, A.H.8
  • 57
    • 0028954473 scopus 로고
    • A DNA polymerase beta in the mitochondrion of the trypanosomatid Crithidia fasciculata
    • Torri, A. F., and P. T. Englund. 1995. A DNA polymerase beta in the mitochondrion of the trypanosomatid Crithidia fasciculata. J. Biol. Chem. 270:3495-3497.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3495-3497
    • Torri, A.F.1    Englund, P.T.2
  • 58
    • 0026644333 scopus 로고
    • Purification of a mitochondrial DNA polymerase from Crithidia fasciculata
    • Torri, A. F., and P. T. Englund. 1992. Purification of a mitochondrial DNA polymerase from Crithidia fasciculata. J. Biol. Chem. 267:4786-4792.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4786-4792
    • Torri, A.F.1    Englund, P.T.2
  • 59
    • 0028176424 scopus 로고
    • A beta-like DNA polymerase from the mitochondrion of the trypanosomatid Crithidia fasciculata
    • Torri, A. F., T. A. Kunkel, and P. T. Englund. 1994. A beta-like DNA polymerase from the mitochondrion of the trypanosomatid Crithidia fasciculata. J. Biol. Chem. 269:8165-8171.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8165-8171
    • Torri, A.F.1    Kunkel, T.A.2    Englund, P.T.3
  • 60
    • 0032570053 scopus 로고    scopus 로고
    • Trfa dimers play a role in copy-number control of RK2 replication
    • Toukdarian, A. E., and D. R. Helinski. 1998. TrfA dimers play a role in copy-number control of RK2 replication. Gene 223:205-211.
    • (1998) Gene , vol.223 , pp. 205-211
    • Toukdarian, A.E.1    Helinski, D.R.2
  • 61
    • 0029103420 scopus 로고
    • Universal minicircle sequence binding protein, a CCHC-type zinc finger protein that binds the universal minicircle sequence of trypanosomatids. Purification and characterization
    • Tzfati, Y., H. Abeliovich, D. Avrahami, and J. Shlomai. 1995. Universal minicircle sequence binding protein, a CCHC-type zinc finger protein that binds the universal minicircle sequence of trypanosomatids. Purification and characterization. J. Biol. Chem. 270:21339-21345.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21339-21345
    • Tzfati, Y.1    Abeliovich, H.2    Avrahami, D.3    Shlomai, J.4
  • 62
    • 0026769581 scopus 로고
    • A single-stranded DNA-binding protein from Crithidia fasciculata recognizes the nucleotide sequence at the origin of replication of kinetoplast DNA minicircles
    • Tzfati, Y., H. Abeliovich, I. Kapeller, and J. Shlomai. 1992. A single-stranded DNA-binding protein from Crithidia fasciculata recognizes the nucleotide sequence at the origin of replication of kinetoplast DNA minicircles. Proc. Natl. Acad. Sci. USA 89:6891-6895.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6891-6895
    • Tzfati, Y.1    Abeliovich, H.2    Kapeller, I.3    Shlomai, J.4
  • 63
    • 0032128037 scopus 로고    scopus 로고
    • Genomic organization and expression of the gene encoding the universal minicircle sequence binding protein
    • Tzfati, Y., and J. Shlomai. 1998. Genomic organization and expression of the gene encoding the universal minicircle sequence binding protein. Mol. Biochem. Parasitol. 94:137-141.
    • (1998) Mol. Biochem. Parasitol. , vol.94 , pp. 137-141
    • Tzfati, Y.1    Shlomai, J.2
  • 64
    • 0033583086 scopus 로고    scopus 로고
    • Binding properties of the human immunodeficiency virus type 1 nucleocapsid protein p7 to a model RNA: Elucidation of the structural determinants for function
    • Urbaneja, M. A., B. P. Kane, D. G. Johnson, R. J. Gorelick, L. E. Henderson, and J. R. Casas-Finet. 1999. Binding properties of the human immunodeficiency virus type 1 nucleocapsid protein p7 to a model RNA: elucidation of the structural determinants for function. J. Mol. Biol. 287:59-75.
    • (1999) J. Mol. Biol. , vol.287 , pp. 59-75
    • Urbaneja, M.A.1    Kane, B.P.2    Johnson, D.G.3    Gorelick, R.J.4    Henderson, L.E.5    Casas-Finet, J.R.6
  • 65
    • 0034866442 scopus 로고    scopus 로고
    • Role of zinc-finger motif in redox regulation of human replication protein A
    • Wang, M., J. S. You, and S. H. Lee. 2001. Role of zinc-finger motif in redox regulation of human replication protein A. Antioxid. Redox Signal. 3:657-669.
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 657-669
    • Wang, M.1    You, J.S.2    Lee, S.H.3
  • 66
    • 0034859820 scopus 로고    scopus 로고
    • Oxidation of zinc finger transcription factors: Physiological consequences
    • Webster, K. A., H. Prentice, and N. H. Bishopric. 2001. Oxidation of zinc finger transcription factors: physiological consequences. Antioxid. Redox Signal. 3:535-548.
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 535-548
    • Webster, K.A.1    Prentice, H.2    Bishopric, N.H.3
  • 67
    • 0028577262 scopus 로고
    • Rapid PCR site-directed mutagenesis
    • Weiner, M. P., and G. L. Costa. 1994. Rapid PCR site-directed mutagenesis. PCR Methods Appl. 4:5131-5136.
    • (1994) PCR Methods Appl. , vol.4 , pp. 5131-5136
    • Weiner, M.P.1    Costa, G.L.2
  • 68
    • 0034678059 scopus 로고    scopus 로고
    • Distinct mitochondrial and cytosolic enzymes mediate trypanothione- dependent peroxide metabolism in Trypanosoma cruzi
    • Wilkinson, S. R., N. J. Temperton, A. Mondragon, and J. M. Kelly. 2000. Distinct mitochondrial and cytosolic enzymes mediate trypanothione-dependent peroxide metabolism in Trypanosoma cruzi. J. Biol. Chem. 275:8220-8225.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8220-8225
    • Wilkinson, S.R.1    Temperton, N.J.2    Mondragon, A.3    Kelly, J.M.4
  • 69
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • Wray, W., T. Boulikas, V. P. Wray, and R. Hancock. 1981. Silver staining of proteins in polyacrylamide gels. Anal. Biochem. 118:197-203.
    • (1981) Anal. Biochem. , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4
  • 70
    • 0030042987 scopus 로고    scopus 로고
    • Physical and functional sensitivity of zinc finger transcription factors to redox change
    • Wu, X., N. H. Bishopric, D. J. Discher, B. J. Murphy, and K. A. Webster. 1996. Physical and functional sensitivity of zinc finger transcription factors to redox change. Mol. Cell. Biol. 16:1035-1046.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1035-1046
    • Wu, X.1    Bishopric, N.H.2    Discher, D.J.3    Murphy, B.J.4    Webster, K.A.5
  • 71
    • 0026583944 scopus 로고
    • Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity
    • Xanthoudakis, S., and T. Curran. 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
  • 72
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis, S., G. Miao, F. Wang, Y. C. Pan, and T. Curran. 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
  • 73
    • 0027499503 scopus 로고
    • Isolation of proteins associated with kinetoplast DNA networks in vivo
    • Xu, C., and D. S. Ray. 1993. Isolation of proteins associated with kinetoplast DNA networks in vivo. Proc. Natl. Acad. Sci. USA 90:1786-1789.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1786-1789
    • Xu, C.1    Ray, D.S.2
  • 74
    • 0030052478 scopus 로고    scopus 로고
    • Nucleus-encoded histone H1-like proteins are associated with kinetoplast DNA in the trypanosomatid Crithidia fasciculate
    • Xu, C. W., J. C. Hines, M. L. Engel, D. G. Russell, and D. S. Ray. 1996. Nucleus-encoded histone H1-like proteins are associated with kinetoplast DNA in the trypanosomatid Crithidia fasciculate. Mol. Cell. Biol. 16:564-576.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 564-576
    • Xu, C.W.1    Hines, J.C.2    Engel, M.L.3    Russell, D.G.4    Ray, D.S.5
  • 75
    • 0034711045 scopus 로고    scopus 로고
    • Functional characterization of zinc-finger motif in redox regulation of RPA-ssDNA interaction
    • You, J. S., M. Wang, and S. H. Lee. 2000. Functional characterization of zinc-finger motif in redox regulation of RPA-ssDNA interaction. Biochemistry 39:12953-12958.
    • (2000) Biochemistry , vol.39 , pp. 12953-12958
    • You, J.S.1    Wang, M.2    Lee, S.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.