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Volumn 369, Issue 4, 2007, Pages 1001-1014

Thioaptamer Interactions with Prion Proteins: Sequence-specific and Non-specific Binding Sites

Author keywords

aptamer; phosphorothioate; prions; thioaptamer

Indexed keywords

APTAMER; OLIGONUCLEOTIDE; PHOSPHOROTHIOIC ACID DERIVATIVE; PRION PROTEIN; SINGLE STRANDED DNA; THIOAPTAMER; UNCLASSIFIED DRUG;

EID: 34248598028     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.02.004     Document Type: Article
Times cited : (49)

References (63)
  • 1
    • 0001168222 scopus 로고
    • Rida, a chronic encephalitis of sheep with general remarks on infections which develop slowly and some of their special characteristics
    • Sigurdsson B. Rida, a chronic encephalitis of sheep with general remarks on infections which develop slowly and some of their special characteristics. Br. Vet. J. 110 (1954) 341-354
    • (1954) Br. Vet. J. , vol.110 , pp. 341-354
    • Sigurdsson, B.1
  • 3
    • 84961034678 scopus 로고
    • Scrapie produced experimentally in goats with special reference to the clinical syndrome
    • Pattison I.H., and Millson G.C. Scrapie produced experimentally in goats with special reference to the clinical syndrome. J. Comp. Pathol. 71 (1961) 101-108
    • (1961) J. Comp. Pathol. , vol.71 , pp. 101-108
    • Pattison, I.H.1    Millson, G.C.2
  • 4
    • 0014500760 scopus 로고
    • A comparison of some biological characteristics of the mouse-passaged scrapie agents, 22A and ME7
    • Dickinson A.G., and Meikle V.M. A comparison of some biological characteristics of the mouse-passaged scrapie agents, 22A and ME7. Genet. Res. 13 (1969) 213-225
    • (1969) Genet. Res. , vol.13 , pp. 213-225
    • Dickinson, A.G.1    Meikle, V.M.2
  • 5
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper T., Cramp W.A., Haig D.A., and Clarke M.C. Does the agent of scrapie replicate without nucleic acid?. Nature 214 (1967) 764-766
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 6
    • 0018215610 scopus 로고
    • Unusual resistance to ionizing radiation of the viruses of kuru, Creutzfeldt-Jakob disease
    • Gibbs Jr. C.J., Gajdusek D.C., and Latarjet R. Unusual resistance to ionizing radiation of the viruses of kuru, Creutzfeldt-Jakob disease. Proc. Natl Acad. Sci. USA 75 (1978) 6268-6270
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 6268-6270
    • Gibbs Jr., C.J.1    Gajdusek, D.C.2    Latarjet, R.3
  • 7
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 216 (1982) 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 8
    • 0026008203 scopus 로고
    • Search for a putative scrapie genome in purified prion fractions reveals a paucity of nucleic acids
    • Meyer N., Rosenbaum V., Schmidt B., Gilles K., Mirenda C., Groth D., et al. Search for a putative scrapie genome in purified prion fractions reveals a paucity of nucleic acids. J. Gen. Virol. 72 (1991) 37-49
    • (1991) J. Gen. Virol. , vol.72 , pp. 37-49
    • Meyer, N.1    Rosenbaum, V.2    Schmidt, B.3    Gilles, K.4    Mirenda, C.5    Groth, D.6
  • 9
    • 0026604959 scopus 로고
    • Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocussing gel electrophoresis (RRGE)
    • Kellings K., Meyer N., Mirenda C., Prusiner S.B., and Riesner D. Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocussing gel electrophoresis (RRGE). J. Gen. Virol. 73 (1992) 1025-1029
    • (1992) J. Gen. Virol. , vol.73 , pp. 1025-1029
    • Kellings, K.1    Meyer, N.2    Mirenda, C.3    Prusiner, S.B.4    Riesner, D.5
  • 11
    • 0035966046 scopus 로고    scopus 로고
    • DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation
    • Cordeiro Y., Machado F., Juliano L., Juliano M.A., Brentani R.R., Foguel D., and Silva J.L. DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation. J. Biol. Chem. 276 (2001) 49400-49409
    • (2001) J. Biol. Chem. , vol.276 , pp. 49400-49409
    • Cordeiro, Y.1    Machado, F.2    Juliano, L.3    Juliano, M.A.4    Brentani, R.R.5    Foguel, D.6    Silva, J.L.7
  • 12
    • 0035380709 scopus 로고    scopus 로고
    • The prion protein has RNA binding and chaperoning properties characteristic of nucleocapsid protein NCP7 of HIV-1
    • Gabus C., Derrington E., Leblanc P., Chnaiderman J., Dormont D., Swietnicki W., et al. The prion protein has RNA binding and chaperoning properties characteristic of nucleocapsid protein NCP7 of HIV-1. J. Biol. Chem. 276 (2001) 19301-19309
    • (2001) J. Biol. Chem. , vol.276 , pp. 19301-19309
    • Gabus, C.1    Derrington, E.2    Leblanc, P.3    Chnaiderman, J.4    Dormont, D.5    Swietnicki, W.6
  • 13
    • 0035815107 scopus 로고    scopus 로고
    • The prion protein has DNA strand transfer properties similar to retroviral nucleocapsid protein
    • Gabus C., Auxilien S., Pechoux C., Dormont D., Swietnicki W., Morillas M., et al. The prion protein has DNA strand transfer properties similar to retroviral nucleocapsid protein. J. Mol. Biol. 307 (2001) 1011-1021
    • (2001) J. Mol. Biol. , vol.307 , pp. 1011-1021
    • Gabus, C.1    Auxilien, S.2    Pechoux, C.3    Dormont, D.4    Swietnicki, W.5    Morillas, M.6
  • 14
    • 0035088898 scopus 로고    scopus 로고
    • Murine recombinant prion protein induces ordered aggregation of linear nucleic acids to condensed globular structures
    • Nandi P.K., and Sizaret P.Y. Murine recombinant prion protein induces ordered aggregation of linear nucleic acids to condensed globular structures. Arch. Virol. 146 (2001) 327-345
    • (2001) Arch. Virol. , vol.146 , pp. 327-345
    • Nandi, P.K.1    Sizaret, P.Y.2
  • 15
    • 0036970469 scopus 로고    scopus 로고
    • DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid
    • Nandi P.K., Leclerc E., Nicole J.C., and Takahashi M. DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid. J. Mol. Biol. 322 (2002) 153-161
    • (2002) J. Mol. Biol. , vol.322 , pp. 153-161
    • Nandi, P.K.1    Leclerc, E.2    Nicole, J.C.3    Takahashi, M.4
  • 16
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault N.R., Lucassen R.W., and Supattapone S. RNA molecules stimulate prion protein conversion. Nature 425 (2003) 717-720
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 17
    • 22844438894 scopus 로고    scopus 로고
    • Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions
    • Deleault N.R., Geoghegan J.C., Nishina K., Kascsak R., Williamson R.A., and Supattapone S. Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. J. Biol. Chem. 280 (2005) 26873-26879
    • (2005) J. Biol. Chem. , vol.280 , pp. 26873-26879
    • Deleault, N.R.1    Geoghegan, J.C.2    Nishina, K.3    Kascsak, R.4    Williamson, R.A.5    Supattapone, S.6
  • 18
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • Bessen R.A., and Marsh R.F. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J. Virol. 68 (1994) 7859-7868
    • (1994) J. Virol. , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 19
    • 12644272790 scopus 로고    scopus 로고
    • Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity
    • Telling G.C., Parchi P., DeArmond S.J., Cortelli P., Montagna P., Gabizon R., et al. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 274 (1996) 2079-2082
    • (1996) Science , vol.274 , pp. 2079-2082
    • Telling, G.C.1    Parchi, P.2    DeArmond, S.J.3    Cortelli, P.4    Montagna, P.5    Gabizon, R.6
  • 20
    • 0037071874 scopus 로고    scopus 로고
    • A change in the conformation of prions accompanies the emergence of a new prion strain
    • Peretz D., Williamson R.A., Legname G., Matsunaga Y., Vergara J., Burton D., et al. A change in the conformation of prions accompanies the emergence of a new prion strain. Neuron 34 (2002) 921-932
    • (2002) Neuron , vol.34 , pp. 921-932
    • Peretz, D.1    Williamson, R.A.2    Legname, G.3    Matsunaga, Y.4    Vergara, J.5    Burton, D.6
  • 22
    • 33746698975 scopus 로고    scopus 로고
    • The physical basis of how prion conformations determine strain phenotypes
    • Tanaka M., Collins S.R., Toyama B.H., and Weissman J.S. The physical basis of how prion conformations determine strain phenotypes. Nature 442 (2006) 585-589
    • (2006) Nature , vol.442 , pp. 585-589
    • Tanaka, M.1    Collins, S.R.2    Toyama, B.H.3    Weissman, J.S.4
  • 23
    • 0030475417 scopus 로고    scopus 로고
    • Deep penetration of an alpha-helix into a widened RNA major groove in the HIV-1 rev peptide-RNA aptamer complex
    • Ye X., Gorin A., Ellington A.D., and Patel D.J. Deep penetration of an alpha-helix into a widened RNA major groove in the HIV-1 rev peptide-RNA aptamer complex. Nature Struct. Biol. 3 (1996) 1026-1033
    • (1996) Nature Struct. Biol. , vol.3 , pp. 1026-1033
    • Ye, X.1    Gorin, A.2    Ellington, A.D.3    Patel, D.J.4
  • 24
    • 4143103761 scopus 로고    scopus 로고
    • NMR structure of the thrombin-binding DNA aptamer stabilized by Sr2+
    • Mao X., Marky L.A., and Gmeiner W.H. NMR structure of the thrombin-binding DNA aptamer stabilized by Sr2+. J. Biomol. Struct. Dynam. 22 (2004) 25-33
    • (2004) J. Biomol. Struct. Dynam. , vol.22 , pp. 25-33
    • Mao, X.1    Marky, L.A.2    Gmeiner, W.H.3
  • 27
    • 32244440049 scopus 로고    scopus 로고
    • DNA aptamers that bind to PrP(C) and not PrP(Sc) show sequence and structure specificity
    • Takemura K., Wang P., Vorberg I., Surewicz W., Priola S.A., Kanthasamy A., et al. DNA aptamers that bind to PrP(C) and not PrP(Sc) show sequence and structure specificity. Exp. Biol. Med. 231 (2006) 204-214
    • (2006) Exp. Biol. Med. , vol.231 , pp. 204-214
    • Takemura, K.1    Wang, P.2    Vorberg, I.3    Surewicz, W.4    Priola, S.A.5    Kanthasamy, A.6
  • 28
    • 0141891211 scopus 로고    scopus 로고
    • Characterization of 2′-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion
    • Rhie A., Kirby L., Sayer N., Wellesley R., Disterer P., Sylvester I., et al. Characterization of 2′-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion. J. Biol. Chem. 278 (2003) 39697-39705
    • (2003) J. Biol. Chem. , vol.278 , pp. 39697-39705
    • Rhie, A.1    Kirby, L.2    Sayer, N.3    Wellesley, R.4    Disterer, P.5    Sylvester, I.6
  • 29
    • 1842424691 scopus 로고    scopus 로고
    • Structural determinants of conformationally selective, prion-binding aptamers
    • Sayer N.M., Cubin M., Rhie A., Bullock M., Tahiri-Alaoui A., and James W. Structural determinants of conformationally selective, prion-binding aptamers. J. Biol. Chem. 279 (2004) 13102-13109
    • (2004) J. Biol. Chem. , vol.279 , pp. 13102-13109
    • Sayer, N.M.1    Cubin, M.2    Rhie, A.3    Bullock, M.4    Tahiri-Alaoui, A.5    James, W.6
  • 30
    • 0034015113 scopus 로고    scopus 로고
    • Phosphorothioate oligodeoxynucleotides: what is their origin and what is unique about them?
    • Eckstein F. Phosphorothioate oligodeoxynucleotides: what is their origin and what is unique about them?. Antisense Nucl. Acid Drug Dev. 10 (2000) 117-121
    • (2000) Antisense Nucl. Acid Drug Dev. , vol.10 , pp. 117-121
    • Eckstein, F.1
  • 31
  • 32
    • 0025191423 scopus 로고
    • Metal ion dependence of phosphorothioate ATP analogues in the Bacillus stearothermophilus tyrosyl-tRNA synthetase reaction
    • Garcia G.A., Leatherbarrow R.J., Eckstein F., and Fersht A.R. Metal ion dependence of phosphorothioate ATP analogues in the Bacillus stearothermophilus tyrosyl-tRNA synthetase reaction. Biochemistry 29 (1990) 1643-1648
    • (1990) Biochemistry , vol.29 , pp. 1643-1648
    • Garcia, G.A.1    Leatherbarrow, R.J.2    Eckstein, F.3    Fersht, A.R.4
  • 33
    • 0037199444 scopus 로고    scopus 로고
    • Combinatorial selection and binding of phosphorothioate aptamers targeting human NF-kappa B RelA(p65) and p50
    • King D.J., Bassett S.E., Li X., Fennewald S.A., Herzog N.K., Luxon B.A., et al. Combinatorial selection and binding of phosphorothioate aptamers targeting human NF-kappa B RelA(p65) and p50. Biochemistry 41 (2002) 9696-9706
    • (2002) Biochemistry , vol.41 , pp. 9696-9706
    • King, D.J.1    Bassett, S.E.2    Li, X.3    Fennewald, S.A.4    Herzog, N.K.5    Luxon, B.A.6
  • 34
    • 0037143011 scopus 로고    scopus 로고
    • Postexposure prophylaxis against prion disease with a stimulator of innate immunity
    • Sethi S., Lipford G., Wagner H., and Kretzschmar H. Postexposure prophylaxis against prion disease with a stimulator of innate immunity. Lancet 360 (2002) 229-230
    • (2002) Lancet , vol.360 , pp. 229-230
    • Sethi, S.1    Lipford, G.2    Wagner, H.3    Kretzschmar, H.4
  • 36
    • 0031901903 scopus 로고    scopus 로고
    • Methods and statistics for combining motif match scores
    • Bailey T.L., and Gribskov M. Methods and statistics for combining motif match scores. J. Comput. Biol. 5 (1998) 211-221
    • (1998) J. Comput. Biol. , vol.5 , pp. 211-221
    • Bailey, T.L.1    Gribskov, M.2
  • 37
    • 0030965735 scopus 로고    scopus 로고
    • Score distributions for simultaneous matching to multiple motifs
    • Bailey T.L., and Gribskov M. Score distributions for simultaneous matching to multiple motifs. J. Comput. Biol. 4 (1997) 45-59
    • (1997) J. Comput. Biol. , vol.4 , pp. 45-59
    • Bailey, T.L.1    Gribskov, M.2
  • 39
    • 0027074458 scopus 로고
    • Purification and properties of the cellular prion protein from Syrian hamster brain
    • Pan K.-M., Stahl N., and Prusiner S.B. Purification and properties of the cellular prion protein from Syrian hamster brain. Protein Sci. 1 (1992) 1343-1352
    • (1992) Protein Sci. , vol.1 , pp. 1343-1352
    • Pan, K.-M.1    Stahl, N.2    Prusiner, S.B.3
  • 43
    • 0019072839 scopus 로고
    • On the thermodynamics and kinetics of the cooperative binding of bacteriophage T4-coded gene 32 (helix destabilizing) protein to nucleic acid lattices
    • Kowalczykowski S.C., Lonberg N., Newport J.W., Paul L.S., and von Hippel P.H. On the thermodynamics and kinetics of the cooperative binding of bacteriophage T4-coded gene 32 (helix destabilizing) protein to nucleic acid lattices. Biophys. J. 32 (1980) 403-418
    • (1980) Biophys. J. , vol.32 , pp. 403-418
    • Kowalczykowski, S.C.1    Lonberg, N.2    Newport, J.W.3    Paul, L.S.4    von Hippel, P.H.5
  • 44
    • 33750322434 scopus 로고    scopus 로고
    • Mercey, R. Lantier I., Maurel M.C., Grosclaude J., Lantier F. & Marc, D. (2006). Fast, reversible interaction of prion protein with RNA aptamers containing specific sequence patterns. Arch. Virol. 151, 2197-2214.
  • 45
    • 0031875169 scopus 로고    scopus 로고
    • Polymerization of human prion peptide HuPrP 106-126 to amyloid in nucleic acid solution
    • Nandi P.K. Polymerization of human prion peptide HuPrP 106-126 to amyloid in nucleic acid solution. Arch. Virol. 143 (1998) 1251-1263
    • (1998) Arch. Virol. , vol.143 , pp. 1251-1263
    • Nandi, P.K.1
  • 47
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed β-helices into trimers
    • Govaerts C., Wille H., Prusiner S.B., and Cohen F.E. Evidence for assembly of prions with left-handed β-helices into trimers. Proc. Natl Acad. Sci. USA 101 (2004) 8342-8347
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 48
    • 0027474318 scopus 로고
    • Phosphorodithioate DNA as a potential therapeutic drug
    • Marshall W.S., and Caruthers M.H. Phosphorodithioate DNA as a potential therapeutic drug. Science 259 (1993) 1564-1570
    • (1993) Science , vol.259 , pp. 1564-1570
    • Marshall, W.S.1    Caruthers, M.H.2
  • 49
    • 0030943935 scopus 로고    scopus 로고
    • Comparative pharmacokinetics, tissue distribution, and tumor accumulation of phosphorothioate, phosphorodithioate, and methylphosphonate oligonucleotides in nude mice
    • DeLong R.K., Nolting A., Fisher M., Chen Q., Wickstrom E., Kligshteyn M., et al. Comparative pharmacokinetics, tissue distribution, and tumor accumulation of phosphorothioate, phosphorodithioate, and methylphosphonate oligonucleotides in nude mice. Antisense Nucl. Acid Drug Dev. 7 (1997) 71-77
    • (1997) Antisense Nucl. Acid Drug Dev. , vol.7 , pp. 71-77
    • DeLong, R.K.1    Nolting, A.2    Fisher, M.3    Chen, Q.4    Wickstrom, E.5    Kligshteyn, M.6
  • 53
    • 0038783253 scopus 로고    scopus 로고
    • Specific inhibition of pathological prion protein accumulation by small interfering RNAs
    • Daude N., Marella M., and Chabry J. Specific inhibition of pathological prion protein accumulation by small interfering RNAs. J. Cell Sci. 116 (2003) 2775-2779
    • (2003) J. Cell Sci. , vol.116 , pp. 2775-2779
    • Daude, N.1    Marella, M.2    Chabry, J.3
  • 54
    • 0029832863 scopus 로고    scopus 로고
    • Chemical chaperones interfere with the formation of scrapie prion protein
    • Tatzelt J., Prusiner S.B., and Welch W.J. Chemical chaperones interfere with the formation of scrapie prion protein. EMBO J. 15 (1996) 6363-6373
    • (1996) EMBO J. , vol.15 , pp. 6363-6373
    • Tatzelt, J.1    Prusiner, S.B.2    Welch, W.J.3
  • 55
    • 15844419908 scopus 로고    scopus 로고
    • High-level expression and characterization of a purified 142-residue polypeptide of the prion protein
    • Mehlhorn I., Groth D., Stöckel J., Moffat B., Reilly D., Yansura D., et al. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry 35 (1996) 5528-5537
    • (1996) Biochemistry , vol.35 , pp. 5528-5537
    • Mehlhorn, I.1    Groth, D.2    Stöckel, J.3    Moffat, B.4    Reilly, D.5    Yansura, D.6
  • 56
    • 0035827614 scopus 로고    scopus 로고
    • Folding of prion protein to its native α-helical conformation is under kinetic control
    • Baskakov I.V., Legname G., Prusiner S.B., and Cohen F.E. Folding of prion protein to its native α-helical conformation is under kinetic control. J. Biol. Chem. 276 (2001) 19687-19690
    • (2001) J. Biol. Chem. , vol.276 , pp. 19687-19690
    • Baskakov, I.V.1    Legname, G.2    Prusiner, S.B.3    Cohen, F.E.4
  • 58
    • 0035899413 scopus 로고    scopus 로고
    • Antibodies inhibit prion propagation and clear cell cultures of prion infectivity
    • Peretz D., Williamson R.A., Kaneko K., Vergara J., Leclerc E., Schmitt-Ulms G., et al. Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 412 (2001) 739-743
    • (2001) Nature , vol.412 , pp. 739-743
    • Peretz, D.1    Williamson, R.A.2    Kaneko, K.3    Vergara, J.4    Leclerc, E.5    Schmitt-Ulms, G.6
  • 59
    • 0036843448 scopus 로고    scopus 로고
    • Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice
    • Safar J.G., Scott M., Monaghan J., Deering C., Didorenko S., Vergara J., et al. Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice. Nature Biotechnol. 20 (2002) 1147-1150
    • (2002) Nature Biotechnol. , vol.20 , pp. 1147-1150
    • Safar, J.G.1    Scott, M.2    Monaghan, J.3    Deering, C.4    Didorenko, S.5    Vergara, J.6
  • 60
    • 14844342992 scopus 로고    scopus 로고
    • Binding of six nucleotide cofactors to the hexameric helicase RepA protein of plasmid RSF1010. 2. Base specificity, nucleotide structure, magnesium, and salt effect on the cooperative binding of the cofactors
    • Jezewska M.J., Lucius A.L., and Bujalowski W. Binding of six nucleotide cofactors to the hexameric helicase RepA protein of plasmid RSF1010. 2. Base specificity, nucleotide structure, magnesium, and salt effect on the cooperative binding of the cofactors. Biochemistry 44 (2005) 3877-3890
    • (2005) Biochemistry , vol.44 , pp. 3877-3890
    • Jezewska, M.J.1    Lucius, A.L.2    Bujalowski, W.3
  • 61
    • 14844349014 scopus 로고    scopus 로고
    • Binding of six nucleotide cofactors to the hexameric helicase RepA protein of plasmid RSF1010. 1. Direct evidence of cooperative interactions between the nucleotide-binding sites of a hexameric helicase
    • Jezewska M.J., Lucius A.L., and Bujalowski W. Binding of six nucleotide cofactors to the hexameric helicase RepA protein of plasmid RSF1010. 1. Direct evidence of cooperative interactions between the nucleotide-binding sites of a hexameric helicase. Biochemistry 44 (2005) 3865-3876
    • (2005) Biochemistry , vol.44 , pp. 3865-3876
    • Jezewska, M.J.1    Lucius, A.L.2    Bujalowski, W.3
  • 62
    • 0032319019 scopus 로고    scopus 로고
    • Theoretical aspects of isothermal titration calorimetry
    • Indyk L., and Fisher H.F. Theoretical aspects of isothermal titration calorimetry. Methods Enzymol. 295 (1998) 350-364
    • (1998) Methods Enzymol. , vol.295 , pp. 350-364
    • Indyk, L.1    Fisher, H.F.2
  • 63
    • 0030956737 scopus 로고    scopus 로고
    • Fluorescence methods for studying equilibrium macromolecule-ligand interactions
    • Eftink M.R. Fluorescence methods for studying equilibrium macromolecule-ligand interactions. Methods Enzymol. 278 (1997) 221-257
    • (1997) Methods Enzymol. , vol.278 , pp. 221-257
    • Eftink, M.R.1


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