메뉴 건너뛰기




Volumn 43, Issue 18, 2004, Pages 5551-5561

Decavanadate Binding to a High Affinity Site near the Myosin Catalytic Centre Inhibits F-Actin-Stimulated Myosin ATPase Activity

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; CATALYSIS; ENERGY TRANSFER; ENZYMES; FLUORESCENCE; TITRATION;

EID: 2442444212     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049910+     Document Type: Article
Times cited : (52)

References (64)
  • 1
    • 0000501984 scopus 로고
    • The biochemistry of vanadium
    • Chasteen, N. D. (1983) The biochemistry of vanadium. Struct. Bonding 53, 105-138.
    • (1983) Struct. Bonding , vol.53 , pp. 105-138
    • Chasteen, N.D.1
  • 3
    • 0025025643 scopus 로고
    • 51V 2-D NMR for studies of kinetic exchange between vanadate oligomers
    • 51V 2-D NMR for studies of kinetic exchange between vanadate oligomers. J. Am. Chem Soc. 112, 2901-2908.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 2901-2908
    • Crans, D.C.1    Rithner, C.D.2    Theisen, L.A.3
  • 4
    • 0000625505 scopus 로고    scopus 로고
    • Wrapping oxometalates with macrocyclic ligands: The decavanadate-cryptand system
    • Farahbakhsh, M., Kögerler, P., Schmidt, H., and Rehder, D. (1998) Wrapping oxometalates with macrocyclic ligands: the decavanadate-cryptand system. Inorg. Chem. Commun. 1, 111-114.
    • (1998) Inorg. Chem. Commun. , vol.1 , pp. 111-114
    • Farahbakhsh, M.1    Kögerler, P.2    Schmidt, H.3    Rehder, D.4
  • 5
    • 0037036051 scopus 로고    scopus 로고
    • Oxidative stress in toadfish (Halobatrachus didactylus) cardiac muscle: Acute exposure to vanadate oligomers
    • Aureliano, M., Joaquim, N., Sousa, A., Martins, H., Coucelo, J. M. (2002) Oxidative stress in toadfish (Halobatrachus didactylus) cardiac muscle: Acute exposure to vanadate oligomers. J. Inorg. Biochem. 90, 159-165.
    • (2002) J. Inorg. Biochem. , vol.90 , pp. 159-165
    • Aureliano, M.1    Joaquim, N.2    Sousa, A.3    Martins, H.4    Coucelo, J.M.5
  • 6
    • 0344406884 scopus 로고    scopus 로고
    • Cadmium and vanadate oligomers effects on metahemoglobin reductase activity from Lusitanian toadfish: In vivo and in vitro studies
    • Soares, S. S., Aureliano, M., Joaquim, N., Coucelo, J. M. (2003) Cadmium and vanadate oligomers effects on metahemoglobin reductase activity from Lusitanian toadfish: in vivo and in vitro studies. J. Inorg. Biochem. 94, 285-290.
    • (2003) J. Inorg. Biochem. , vol.94 , pp. 285-290
    • Soares, S.S.1    Aureliano, M.2    Joaquim, N.3    Coucelo, J.M.4
  • 7
    • 0029437151 scopus 로고
    • Inhibition of phosphate-metabolizing enzymes by oxovanadium(V) complexes in Metal ions
    • (Sigel H., Sigel A., Ed.), Marcel Dekker, New York
    • Stankiewicz, P. J., Tracey, A. S., and Crans, D. C. (1995) Inhibition of phosphate-metabolizing enzymes by oxovanadium(V) complexes in Metal ions in Biological Systems: Vanadium and its Role in Life (Sigel H., Sigel A., Ed.), pp 287-324, Marcel Dekker, New York.
    • (1995) Biological Systems: Vanadium and its Role in Life , pp. 287-324
    • Stankiewicz, P.J.1    Tracey, A.S.2    Crans, D.C.3
  • 9
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn, R. W., and Taylor, E. W. (1971) Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10, 4617-4624.
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 10
    • 0001064670 scopus 로고
    • Inhibition of myosin ATPase by vanadate ion
    • Goodno, C. C. (1979) Inhibition of myosin ATPase by vanadate ion. Proc. Natl. Acad. Sci. U.S.A. 76, 2620-2624.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 2620-2624
    • Goodno, C.C.1
  • 11
    • 0020023988 scopus 로고
    • Myosin active-site trapping with vanadate ion
    • Goodno, C. C. (1982) Myosin active-site trapping with vanadate ion. Methods Enzymol. 85, 116-123.
    • (1982) Methods Enzymol. , vol.85 , pp. 116-123
    • Goodno, C.C.1
  • 13
    • 0025089290 scopus 로고
    • A comparison of the effect of vanadate on the binding of myosin-subfragment-1 · ADP to actin and on actomyosin subfragment 1 ATPase activity
    • Smith, S. J., and Eisenberg, E. (1990) A comparison of the effect of vanadate on the binding of myosin-subfragment-1 · ADP to actin and on actomyosin subfragment 1 ATPase activity. Eur. J. Biochem. 193, 69-73.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 69-73
    • Smith, S.J.1    Eisenberg, E.2
  • 14
    • 0025196786 scopus 로고
    • 51V NMR study of vanadate binding to myosin and its subfragment 1
    • 51V NMR study of vanadate binding to myosin and its subfragment 1. Biochemistry 29, 9091-9096.
    • (1990) Biochemistry , vol.29 , pp. 9091-9096
    • Ringel, I.1    Peyser, Y.M.2    Muhlrad, A.3
  • 15
    • 0025113252 scopus 로고
    • Photocleavage of myosin subfragment 1 by vanadate
    • Cremo, C. R., Long, G. T., and Grammer, J. C. (1990) Photocleavage of myosin subfragment 1 by vanadate. Biochemistry 29, 7982-7990.
    • (1990) Biochemistry , vol.29 , pp. 7982-7990
    • Cremo, C.R.1    Long, G.T.2    Grammer, J.C.3
  • 17
    • 0034732840 scopus 로고    scopus 로고
    • Vanadate oligomer interactions with myosin
    • Aureliano, M. (2000) Vanadate oligomer interactions with myosin. J. Inorg. Biochem. 80, 141-143.
    • (2000) J. Inorg. Biochem. , vol.80 , pp. 141-143
    • Aureliano, M.1
  • 18
    • 0012182159 scopus 로고    scopus 로고
    • Quenching of myosin intrinsic fluorescence unravels the existence of a high affinity binding site for decavanadate
    • Tiago, T., Aureliano, M., and Gutiérrez-Merino, C. (2002) Quenching of myosin intrinsic fluorescence unravels the existence of a high affinity binding site for decavanadate. J. Fluoresc. 12, 87-90.
    • (2002) J. Fluoresc. , vol.12 , pp. 87-90
    • Tiago, T.1    Aureliano, M.2    Gutiérrez-Merino, C.3
  • 19
    • 37049104341 scopus 로고
    • Protonation of the decavanadate (6-) ion: A vanadium-51 nuclear magnetic resonance study
    • Howarth, O. W., and Jarold, M. (1978) Protonation of the decavanadate (6-) ion: a vanadium-51 nuclear magnetic resonance study. J. Chem. Soc., Dalton 503-506.
    • (1978) J. Chem. Soc., Dalton , pp. 503-506
    • Howarth, O.W.1    Jarold, M.2
  • 20
    • 0020600633 scopus 로고
    • Fluorescence energy transfer studies on the proximity of the two essential thiols of myosin subfragment-1
    • Cheung, H. C., Gonsoulin, F., and Garland, F. (1983) Fluorescence energy transfer studies on the proximity of the two essential thiols of myosin subfragment-1. J. Biol. Chem. 258, 5775-5786.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5775-5786
    • Cheung, H.C.1    Gonsoulin, F.2    Garland, F.3
  • 21
    • 0022971116 scopus 로고
    • Interaction of fluorescently labeled myosin subfragment-1 with nucleotides and actin
    • Aguirre, R., Gonsoulin, F., and Cheung, H. C. (1986) Interaction of fluorescently labeled myosin subfragment-1 with nucleotides and actin. Biochemistry 25, 6827-6835.
    • (1986) Biochemistry , vol.25 , pp. 6827-6835
    • Aguirre, R.1    Gonsoulin, F.2    Cheung, H.C.3
  • 22
    • 0026660981 scopus 로고
    • Characterization of stable beryllium fluoride, aluminum fluoride, and vanadate containing myosin subfragment-1 nucleotide complexes
    • Werber, M. M., Peyser, M., and Muhlrad, A. (1992) Characterization of stable beryllium fluoride, aluminum fluoride, and vanadate containing myosin subfragment-1 nucleotide complexes. Biochemistry 31, 7190-7197.
    • (1992) Biochemistry , vol.31 , pp. 7190-7197
    • Werber, M.M.1    Peyser, M.2    Muhlrad, A.3
  • 23
    • 0031032881 scopus 로고    scopus 로고
    • Effect of complexes of ADP and phosphate analogues on the conformation of the Cys707-Cys697 region of myosin subfragment 1
    • Phan, B. C., Peyser, Y. M., Reisler, E., and Muhlrad, A. (1997) Effect of complexes of ADP and phosphate analogues on the conformation of the Cys707-Cys697 region of myosin subfragment 1. Eur. J. Biochem. 243, 636-642.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 636-642
    • Phan, B.C.1    Peyser, Y.M.2    Reisler, E.3    Muhlrad, A.4
  • 24
    • 0020023995 scopus 로고
    • Sulfhydryl modification and labeling of myosin
    • Reisler, E. (1982) Sulfhydryl modification and labeling of myosin. Methods Enzymol. 85, 84-93.
    • (1982) Methods Enzymol. , vol.85 , pp. 84-93
    • Reisler, E.1
  • 25
    • 0033782192 scopus 로고    scopus 로고
    • Solution Structure of myosin-ADP-MgFn ternary complex by fluorescent probes and small-angle synchroton X-ray scattering
    • Maruta, S., Aihara, T., Uyehara, Y., Homma, K., Sugimoto, Y., and Wakabayashi, K. (2000) Solution Structure of myosin-ADP-MgFn ternary complex by fluorescent probes and small-angle synchroton X-ray scattering. J. Biochem. 128, 687-694.
    • (2000) J. Biochem. , vol.128 , pp. 687-694
    • Maruta, S.1    Aihara, T.2    Uyehara, Y.3    Homma, K.4    Sugimoto, Y.5    Wakabayashi, K.6
  • 26
    • 0016258106 scopus 로고
    • Myosin light-chain kinase, a new enzyme from striated muscle
    • Pires, E. M. V., Perry, S. V., and Thomas, M. A. W. (1974) Myosin light-chain kinase, a new enzyme from striated muscle. FEBS Lett. 41, 292-296.
    • (1974) FEBS Lett. , vol.41 , pp. 292-296
    • Pires, E.M.V.1    Perry, S.V.2    Thomas, M.A.W.3
  • 27
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian, S. S., and Lowey, S. (1982) Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol. 85, 55-72.
    • (1982) Methods Enzymol. , vol.85 , pp. 55-72
    • Margossian, S.S.1    Lowey, S.2
  • 28
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee, J. D., and Spudich, J. A. (1982) Purification of muscle actin. Methods Enzymol. 85, 164-181.
    • (1982) Methods Enzymol. , vol.85 , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 31
    • 84963198200 scopus 로고
    • Aqueous chemistry of labile oxovanadates: Relevance to biological studies
    • Crans, D. C. (1994) Aqueous chemistry of labile oxovanadates: relevance to biological studies. Comments Inorg. Chem. 16, 1-33.
    • (1994) Comments Inorg. Chem. , vol.16 , pp. 1-33
    • Crans, D.C.1
  • 32
    • 84963133580 scopus 로고
    • Enzyme interactions with labile oxovanadates and other polyoxometalates
    • Crans, D. C. (1994) Enzyme interactions with labile oxovanadates and other polyoxometalates. Comments Inorg. Chem. 16, 35-76.
    • (1994) Comments Inorg. Chem. , vol.16 , pp. 35-76
    • Crans, D.C.1
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 35
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske, C. H., and Subbarow, Y. (1925) The colorimetric determination of phosphorus. J. Biol. Chem. 66, 375-400.
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 36
    • 0024599426 scopus 로고
    • SH-1 modification of rabbit myosin interferes with calcium regulation
    • Titus, M. A., Ashiba, G., and Szent-György, A. G. (1989) SH-1 modification of rabbit myosin interferes with calcium regulation. J. Muscle Res. Cell Motil. 10, 25-33.
    • (1989) J. Muscle Res. Cell Motil. , vol.10 , pp. 25-33
    • Titus, M.A.1    Ashiba, G.2    Szent-György, A.G.3
  • 38
    • 0002110553 scopus 로고
    • (Hercules, D. M, Ed.), John Wiley and Sons, New York
    • Weber, G. (1966) in Fluorescence and Phosphorescence Analysis (Hercules, D. M, Ed.), pp 217-240, John Wiley and Sons, New York.
    • (1966) Fluorescence and Phosphorescence Analysis , pp. 217-240
    • Weber, G.1
  • 39
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer, L. (1978) Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47, 819-846.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 41
    • 0003468776 scopus 로고
    • (Sinanoglu, O., Ed.), Academic Press, New York
    • Förster, T. (1965) in Modern Quantum Chemistry (Sinanoglu, O., Ed.), Academic Press, New York.
    • (1965) Modern Quantum Chemistry
    • Förster, T.1
  • 42
    • 0026757684 scopus 로고
    • Location of functional centers in the microsomal cytochrome P450 system
    • Centeno, F., and Gutiérrez-Merino, C. (1992) Location of functional centers in the microsomal cytochrome P450 system. Biochemistry 31, 8473-8481.
    • (1992) Biochemistry , vol.31 , pp. 8473-8481
    • Centeno, F.1    Gutiérrez-Merino, C.2
  • 43
    • 0031555481 scopus 로고    scopus 로고
    • X-ray Crystal Structure and Solution Fluorescence Characterization of Mg·2′(3′)-O-(N-Methylanthraniloyl) Nucleotides Bound to the Dictyostelium discoideum Myosin Motor Domain
    • Bauer, C. B., Kuhlman, P. A., Bagshaw, C. R., and Rayment, I. (1997) X-ray Crystal Structure and Solution Fluorescence Characterization of Mg·2′(3′)-O-(N-Methylanthraniloyl) Nucleotides Bound to the Dictyostelium discoideum Myosin Motor Domain. J. Mol. Biol. 274, 394-407.
    • (1997) J. Mol. Biol. , vol.274 , pp. 394-407
    • Bauer, C.B.1    Kuhlman, P.A.2    Bagshaw, C.R.3    Rayment, I.4
  • 44
    • 0020022510 scopus 로고
    • Methods to measure actin polymerisation
    • Cooper, J. A., and Pollard, T. D. (1982) Methods to measure actin polymerisation. Methods Enzymol. 85, 182-211.
    • (1982) Methods Enzymol. , vol.85 , pp. 182-211
    • Cooper, J.A.1    Pollard, T.D.2
  • 46
    • 0021992946 scopus 로고
    • Muscle contraction and free energy transduction in biological systems
    • Eisenberg, E., and Hill, T. L. (1985) Muscle contraction and free energy transduction in biological systems. Science 227, 999-1006.
    • (1985) Science , vol.227 , pp. 999-1006
    • Eisenberg, E.1    Hill, T.L.2
  • 47
    • 0025829188 scopus 로고
    • Two-state equilibria of myosin subfragment 1 and its complexes with ADP and actin
    • Lin, S. H., and Cheung, H. C. (1991) Two-state equilibria of myosin subfragment 1 and its complexes with ADP and actin. Biochemistry 30, 4317-4322.
    • (1991) Biochemistry , vol.30 , pp. 4317-4322
    • Lin, S.H.1    Cheung, H.C.2
  • 48
    • 0029004346 scopus 로고
    • Internal movement in myosin subfragment 1 detected by fluorescence resonance energy transfer
    • Xing, L, and Cheung, H. C. (1995) Internal movement in myosin subfragment 1 detected by fluorescence resonance energy transfer. Biochemistry 34, 6475-6487.
    • (1995) Biochemistry , vol.34 , pp. 6475-6487
    • Xing, L.1    Cheung, H.C.2
  • 49
    • 0030869408 scopus 로고    scopus 로고
    • Opening of the myosin nucleotide triphosphate binding domain during the ATPase cycle
    • Pate, E., Naber, N., Matuska, M., Franks-Skiba, K., and Cooke, R. (1997) Opening of the myosin nucleotide triphosphate binding domain during the ATPase cycle. Biochemistry 36, 12155-12166.
    • (1997) Biochemistry , vol.36 , pp. 12155-12166
    • Pate, E.1    Naber, N.2    Matuska, M.3    Franks-Skiba, K.4    Cooke, R.5
  • 51
    • 0020822505 scopus 로고
    • Fluorescence energy transfer between the myosin subfragment-1 isoenzymes and F-actin in the absence and presence of nucleotides
    • Trayer, H. R., and Trayer, I. P. (1983) Fluorescence energy transfer between the myosin subfragment-1 isoenzymes and F-actin in the absence and presence of nucleotides. Eur. J. Biochem. 135, 47-59.
    • (1983) Eur. J. Biochem. , vol.135 , pp. 47-59
    • Trayer, H.R.1    Trayer, I.P.2
  • 52
    • 0030735355 scopus 로고    scopus 로고
    • Effect of nucleotides and actin on the orientation of the light chain-binding domain in myosin subfragment 1
    • Smyczynski, C., and Kasprzak, A. A. (1997) Effect of nucleotides and actin on the orientation of the light chain-binding domain in myosin subfragment 1. Biochemistry 36, 13201-13207.
    • (1997) Biochemistry , vol.36 , pp. 13201-13207
    • Smyczynski, C.1    Kasprzak, A.A.2
  • 53
    • 0034282747 scopus 로고    scopus 로고
    • Decavanadate inhibits catalysis by ribonuclease A
    • Messmore, J. M., and Raines, R. T. (2000) Decavanadate inhibits catalysis by ribonuclease A. Arch. Biochem. Biophys. 381, 25-30.
    • (2000) Arch. Biochem. Biophys. , vol.381 , pp. 25-30
    • Messmore, J.M.1    Raines, R.T.2
  • 55
    • 0022977769 scopus 로고
    • Identification of polyphosphate recognition sites communicating with actin sites on the skeletal myosin subfragment 1 heavy chain
    • Chaussepied, P., Mornet, D., and Kassab, R. (1986) Identification of polyphosphate recognition sites communicating with actin sites on the skeletal myosin subfragment 1 heavy chain. Biochemistry 25, 6426-6432.
    • (1986) Biochemistry , vol.25 , pp. 6426-6432
    • Chaussepied, P.1    Mornet, D.2    Kassab, R.3
  • 56
    • 0025762214 scopus 로고
    • The isolated 21 kDa N-terminal fragment of myosin binds to actin in an ATP and ionic strength-dependent manner
    • Muhlrad, A. (1991) The isolated 21 kDa N-terminal fragment of myosin binds to actin in an ATP and ionic strength-dependent manner. Biochim. Biophys. Acta 1077, 308-315.
    • (1991) Biochim. Biophys. Acta , vol.1077 , pp. 308-315
    • Muhlrad, A.1
  • 58
    • 0019891873 scopus 로고
    • Fluorescence Quenching in Model membranes. 1. Characterization of Quenching Caused by a Spin-Labeled Phospholipid
    • London, E., and Feigenson, G. W. (1981) Fluorescence Quenching in Model membranes. 1. Characterization of Quenching Caused by a Spin-Labeled Phospholipid. Biochemistry 20, 1932-1938.
    • (1981) Biochemistry , vol.20 , pp. 1932-1938
    • London, E.1    Feigenson, G.W.2
  • 59
    • 0029946042 scopus 로고    scopus 로고
    • Effect of divalent cations on the formation and stability of myosin subfragment 1-ADP-phosphate analog complexes
    • Peyser, Y. M., Ben-Hur, M., Werber, M. M., and Muhlrad, A. (1996) Effect of divalent cations on the formation and stability of myosin subfragment 1-ADP-phosphate analog complexes. Biochemistry 35, 4409-4416.
    • (1996) Biochemistry , vol.35 , pp. 4409-4416
    • Peyser, Y.M.1    Ben-Hur, M.2    Werber, M.M.3    Muhlrad, A.4
  • 60
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesium(II)·ADP·vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution
    • Smith, R., and Rayment, I. (1996) X-ray structure of the magnesium(II)·ADP·vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution. Biochemistry 35, 5404-5417.
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, R.1    Rayment, I.2
  • 61
    • 0022421581 scopus 로고
    • An investigation of the SH1-SH2 and SH1-ATPase distances in myosin subfragment-1 by resonance energy transfer using nanosecond fluorimetry
    • Cheung, H. C., Garland, F., and Gonsoulin, F. (1985) An investigation of the SH1-SH2 and SH1-ATPase distances in myosin subfragment-1 by resonance energy transfer using nanosecond fluorimetry. Biochim. Biophys. Acta 832, 52-62.
    • (1985) Biochim. Biophys. Acta , vol.832 , pp. 52-62
    • Cheung, H.C.1    Garland, F.2    Gonsoulin, F.3
  • 62
    • 0025726760 scopus 로고
    • Conformational flexibility of the Cys 697-Cys 707 segment of myosin subfragment-1. Distance distributions by frequency-domain fluorometry
    • Cheung, H. C., Gryczynski, I., Malak, H., Wiczk, W., Johnson, M. L., and Lakowicz, J. R. (1991) Conformational flexibility of the Cys 697-Cys 707 segment of myosin subfragment-1. Distance distributions by frequency-domain fluorometry. Biophys. Chem. 40, 1-17.
    • (1991) Biophys. Chem. , vol.40 , pp. 1-17
    • Cheung, H.C.1    Gryczynski, I.2    Malak, H.3    Wiczk, W.4    Johnson, M.L.5    Lakowicz, J.R.6
  • 63
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J., and Gay, N. J. (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 64
    • 0036849354 scopus 로고    scopus 로고
    • Vanadate inhibits the ATPase activity and DNA binding capability of bacterial MutS. A structural model for the vanadate-MutS interaction at the Walker A motif
    • Pezza, R. J., Villarreal, M. A., Montich, G. G., and Argaraña, C. E. (2002) Vanadate inhibits the ATPase activity and DNA binding capability of bacterial MutS. A structural model for the vanadate-MutS interaction at the Walker A motif. Nucleic Acids Res. 30, 4700-4708.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4700-4708
    • Pezza, R.J.1    Villarreal, M.A.2    Montich, G.G.3    Argaraña, C.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.