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Volumn 74, Issue 3, 1998, Pages 1115-1134

Loss of conformational stability in calmodulin upon methionine oxidation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALMODULIN; HYDROGEN PEROXIDE; MALEIMIDE DERIVATIVE; METHIONINE;

EID: 0031885987     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77830-0     Document Type: Article
Times cited : (158)

References (90)
  • 2
    • 0027946813 scopus 로고
    • The role of calcium-binding proteins in selective motor neuron vulnerability in amyotrophic lateral sclerosis
    • Alexianu, M. E., B.-K. Ho, A. H. Mohamed, V. La Bella, R. G. Smith, and S. H. Appel. 1994. The role of calcium-binding proteins in selective motor neuron vulnerability in amyotrophic lateral sclerosis. Ann. Neurol. 36:846-858.
    • (1994) Ann. Neurol. , vol.36 , pp. 846-858
    • Alexianu, M.E.1    Ho, B.-K.2    Mohamed, A.H.3    La Bella, V.4    Smith, R.G.5    Appel, S.H.6
  • 3
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Å resolution
    • Babu, Y. S., C. E. Bugg, and W. J. Cook. 1988. Structure of calmodulin refined at 2.2 Å resolution. J. Mol. Biol. 204:191-204.
    • (1988) J. Mol. Biol. , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 4
    • 0026748968 scopus 로고
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry. 31:5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.3    Pastor, R.W.4    Bax, A.5
  • 5
    • 0026459928 scopus 로고
    • The α-helical content of calmodulin is increased in solution conditions favouring protein crystallization
    • Bayley, P. M., and S. R. Martin. 1992. The α-helical content of calmodulin is increased in solution conditions favouring protein crystallization. Biochim. Biophys. Acta. 1160:16-21.
    • (1992) Biochim. Biophys. Acta. , vol.1160 , pp. 16-21
    • Bayley, P.M.1    Martin, S.R.2
  • 6
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel, W. J., and J. A. Schellman. 1987. Protein stability curves. Biopolymers. 26:1859-1877.
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 7
    • 0000335117 scopus 로고
    • The global analysis of fluorescence intensity and anisotropy decay data: Second generation theory and programs
    • J. R. Lakowicz, editor. Plenum Press, New York
    • Beechem, J. M., E. Gratton, M. Ameloot, J. R. Knutson, and L. Brand. 1991. The global analysis of fluorescence intensity and anisotropy decay data: second generation theory and programs. In Topics in Fluorescence Spectroscopy, Vol. 2. J. R. Lakowicz, editor. Plenum Press, New York. 1-52.
    • (1991) Topics in Fluorescence Spectroscopy , vol.2 , pp. 1-52
    • Beechem, J.M.1    Gratton, E.2    Ameloot, M.3    Knutson, J.R.4    Brand, L.5
  • 9
    • 0029110258 scopus 로고
    • PCR-generated cDNA library of transition-stage maize embryos: Cloning and expression of calmodulin genes during early embryogenesis
    • Breton, C., A. Chaboud, E. Matthys-Rochon, E. E. M. Bates, J. M. Cock, H. Fromm, and C. Dumas. 1995. PCR-generated cDNA library of transition-stage maize embryos: cloning and expression of calmodulin genes during early embryogenesis. Plant Mol. Biol. 27:105-113.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 105-113
    • Breton, C.1    Chaboud, A.2    Matthys-Rochon, E.3    Bates, E.E.M.4    Cock, J.M.5    Fromm, H.6    Dumas, C.7
  • 10
    • 0023069451 scopus 로고
    • Intracellular calcium homeostasis
    • Carafoli, E. 1987. Intracellular calcium homeostasis. Annu. Rev. Biochem. 56:395-433.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 395-433
    • Carafoli, E.1
  • 12
    • 0031195030 scopus 로고    scopus 로고
    • Collision cross sections of myoglobin and cytochrome c ions with Ne, Ar, and Kr
    • Chen, Y.-L., B. A. Collings, and D. J. Douglas. 1997. Collision cross sections of myoglobin and cytochrome c ions with Ne, Ar, and Kr. J. Am. Soc. Mass Spectrom. 8:681-687.
    • (1997) J. Am. Soc. Mass Spectrom. , vol.8 , pp. 681-687
    • Chen, Y.-L.1    Collings, B.A.2    Douglas, D.J.3
  • 13
    • 0000056380 scopus 로고
    • Resonance energy transfer
    • J. R. Lakowicz, editor. Plenum Press, New York
    • Cheung, H. C. 1991. Resonance energy transfer. In Topics in Fluorescence Spectroscopy, Vol. 2. J. R. Lakowicz, editor. Plenum Press, New York. 128-176.
    • (1991) Topics in Fluorescence Spectroscopy , vol.2 , pp. 128-176
    • Cheung, H.C.1
  • 14
    • 0029803672 scopus 로고    scopus 로고
    • Methionine to glutamine substitutions in the C-terminal domain of calmodulin impair the activation of three protein kinases
    • Chin, D., and A. R. Means. 1996. Methionine to glutamine substitutions in the C-terminal domain of calmodulin impair the activation of three protein kinases. J. Biol. Chem. 29:30465-30471.
    • (1996) J. Biol. Chem. , vol.29 , pp. 30465-30471
    • Chin, D.1    Means, A.R.2
  • 15
    • 0029169544 scopus 로고
    • A cDNA clone encoding Brassica calmodulin
    • Chye, M. L., C. M. Liu, and C. T. Tan. 1995. A cDNA clone encoding Brassica calmodulin. Plant Mol. Biol. 27:419-423.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 419-423
    • Chye, M.L.1    Liu, C.M.2    Tan, C.T.3
  • 16
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders
    • Coyle, J. T., and P. Puttfarcken. 1993. Oxidative stress, glutamate, and neurodegenerative disorders. Science. 262:689-695.
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 17
    • 0023644673 scopus 로고
    • Site-specific mutagenesis of the alpha-helices of calmodulin. Effect of altering a charge cluster in the helix that links the two halves of calmodulin
    • Craig, T. A., D. M. Watterson, F. G. Prendergast, J. Haiech, and D. M. Roberts. 1987. Site-specific mutagenesis of the alpha-helices of calmodulin. Effect of altering a charge cluster in the helix that links the two halves of calmodulin. J. Biol. Chem. 262:3278-3284.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3278-3284
    • Craig, T.A.1    Watterson, D.M.2    Prendergast, F.G.3    Haiech, J.4    Roberts, D.M.5
  • 18
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici, A., and M. Ikura. 1995. Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Strucr. 24: 85-116.
    • (1995) Annu. Rev. Biophys. Biomol. Strucr. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 19
    • 0001605715 scopus 로고
    • Intramolecular energy transfer and molecular conformation
    • Dale, R. E., and J. Eisenger. 1976. Intramolecular energy transfer and molecular conformation. Proc. Natl. Acad. Sci. USA. 73:271-273.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 271-273
    • Dale, R.E.1    Eisenger, J.2
  • 20
    • 0018464261 scopus 로고
    • The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer
    • Dale, R. E., J. Eisenger, and W. E. Blumberg. 1979. The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer. Biophys. J. 26:161-193.
    • (1979) Biophys. J. , vol.26 , pp. 161-193
    • Dale, R.E.1    Eisenger, J.2    Blumberg, W.E.3
  • 21
    • 0030019645 scopus 로고    scopus 로고
    • Molecular recognition by calmodulin: Pressure-induced reorganization of a novel calmodulin-peptide complex
    • Ehrhardt, M. R., L. Erijman, G. Weber, and A. J. Wand. 1996. Molecular recognition by calmodulin: pressure-induced reorganization of a novel calmodulin-peptide complex. Biochemistry. 35:1599-1605.
    • (1996) Biochemistry , vol.35 , pp. 1599-1605
    • Ehrhardt, M.R.1    Erijman, L.2    Weber, G.3    Wand, A.J.4
  • 22
    • 0017917406 scopus 로고
    • The use of singlet-singlet energy transfer to study macromolecular assemblies
    • Fairclough, R. H., and C. R. Cantor. 1978. The use of singlet-singlet energy transfer to study macromolecular assemblies. Methods Enzymol. 48: 347-379.
    • (1978) Methods Enzymol. , vol.48 , pp. 347-379
    • Fairclough, R.H.1    Cantor, C.R.2
  • 24
    • 0344019216 scopus 로고
    • Oxidation of methionine in proteins of isolated rat heart myocytes and tissue slices by neutrophil-generated oxygen radicals
    • Fliss, H., and G. Docherty. 1987. Oxidation of methionine in proteins of isolated rat heart myocytes and tissue slices by neutrophil-generated oxygen radicals. Dev. Cardiovasc. Med. 67:85-98.
    • (1987) Dev. Cardiovasc. Med. , vol.67 , pp. 85-98
    • Fliss, H.1    Docherty, G.2
  • 25
    • 0027690192 scopus 로고
    • Isolation, sequencing and analysis of the expression of Bryonia calmodulin after mechanical perturbation
    • Galaud, J. P., J. J. Lareyre, and N. Boyer. 1993. Isolation, sequencing and analysis of the expression of Bryonia calmodulin after mechanical perturbation. Plant Mol. Biol. 23:839-846.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 839-846
    • Galaud, J.P.1    Lareyre, J.J.2    Boyer, N.3
  • 26
    • 0030062258 scopus 로고    scopus 로고
    • Disruption of coiled coil formation by methionine oxidation
    • Garcia-Echeverria, C. 1996. Disruption of coiled coil formation by methionine oxidation. Bioorg. Med. Chem. Lett. 6:229-232.
    • (1996) Bioorg. Med. Chem. Lett. , vol.6 , pp. 229-232
    • Garcia-Echeverria, C.1
  • 27
    • 0017844245 scopus 로고
    • Amino acid sequence of the troponin C-like protein (modulator protein) from bovine uterus
    • Grand, R. J. A., and S. V. Perry. 1978. Amino acid sequence of the troponin C-like protein (modulator protein) from bovine uterus. FEBS Lett. 92:137-142.
    • (1978) FEBS Lett. , vol.92 , pp. 137-142
    • Grand, R.J.A.1    Perry, S.V.2
  • 28
    • 0028406871 scopus 로고
    • Isolation and sequence comparison of a maize calmodulin cDNA
    • Griess, E. A., G. L. Igloi, and G. Feix. 1994. Isolation and sequence comparison of a maize calmodulin cDNA. Plant Physiol. 104: 1467-1468.
    • (1994) Plant Physiol. , vol.104 , pp. 1467-1468
    • Griess, E.A.1    Igloi, G.L.2    Feix, G.3
  • 29
    • 0018267881 scopus 로고
    • Effect of the orientation of donor and acceptor on the probability of energy transfer involving electronic transitions of mixed polarization
    • Haas, E., E. Katchalski-Katzir, and I. Steinberg. 1978. Effect of the orientation of donor and acceptor on the probability of energy transfer involving electronic transitions of mixed polarization. Biochemistry. 17:5064-5070.
    • (1978) Biochemistry , vol.17 , pp. 5064-5070
    • Haas, E.1    Katchalski-Katzir, E.2    Steinberg, I.3
  • 30
    • 0002491536 scopus 로고
    • The free-radical theory of aging
    • R. N. Butler, E. L. Schneider, R. L. Sprott, and H. R. Warner, editors. Raven Press, New York
    • Harman, D. 1987. The free-radical theory of aging. In Modern Biological Theories of Aging. R. N. Butler, E. L. Schneider, R. L. Sprott, and H. R. Warner, editors. Raven Press, New York. 81-87.
    • (1987) Modern Biological Theories of Aging , pp. 81-87
    • Harman, D.1
  • 31
    • 0023845141 scopus 로고
    • Comparison of the crystal and solution structures of calmodulin and troponin C
    • Heidorn, D. B., and J. Trewhella. 1988. Comparison of the crystal and solution structures of calmodulin and troponin C. Biochemistry. 27: 909-915.
    • (1988) Biochemistry , vol.27 , pp. 909-915
    • Heidorn, D.B.1    Trewhella, J.2
  • 33
    • 0028921581 scopus 로고
    • Calmodulin-binding domains: Just two faced or multi-faceted?
    • James, P., T. Vorherr, and E. Carafoli. 1995. Calmodulin-binding domains: just two faced or multi-faceted? Trends Biochem. Sci. 20:38-42.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 38-42
    • James, P.1    Vorherr, T.2    Carafoli, E.3
  • 34
    • 0024672412 scopus 로고
    • Molecular cloning and sequencing of a cDNA for plant calmodulin: Signal-induced changes in the expression of calmodulin
    • Jena, P. K., A. S. N. Reddy, and B. W. Poovaiah. 1989. Molecular cloning and sequencing of a cDNA for plant calmodulin: signal-induced changes in the expression of calmodulin. Proc. Natl. Acad. Sci. USA. 86: 3644-3648.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3644-3648
    • Jena, P.K.1    Reddy, A.S.N.2    Poovaiah, B.W.3
  • 35
    • 0020600345 scopus 로고
    • Allosteric interactions among drug binding sites on calmodulin
    • Johnson, J. D. 1983. Allosteric interactions among drug binding sites on calmodulin. Biochem. Biophys. Res. Commun. 112:787-793.
    • (1983) Biochem. Biophys. Res. Commun. , vol.112 , pp. 787-793
    • Johnson, J.D.1
  • 36
    • 0026718393 scopus 로고
    • Parameter estimation by least-squares methods
    • Johnson, M. L., and L. M. Faunt. 1992. Parameter estimation by least-squares methods. Methods Enzymol. 210:1-37.
    • (1992) Methods Enzymol. , vol.210 , pp. 1-37
    • Johnson, M.L.1    Faunt, L.M.2
  • 37
    • 0025778565 scopus 로고
    • Small angle x-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker region retains a predominantly alpha-helical conformation
    • Kataoka, M., J. F. Head, A. Persechini, R. H. Kretsinger, and D. M. Engelman. 1991. Small angle x-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker region retains a predominantly alpha-helical conformation. Biochemistry. 30:1188-1192.
    • (1991) Biochemistry , vol.30 , pp. 1188-1192
    • Kataoka, M.1    Head, J.F.2    Persechini, A.3    Kretsinger, R.H.4    Engelman, D.M.5
  • 38
    • 0028651951 scopus 로고
    • Calcium hypothesis of Alzheimer's disease and brain aging
    • Khachaturian, Z. S. 1994. Calcium hypothesis of Alzheimer's disease and brain aging. Ann. N.Y. Acad. Sci. 747:1-11.
    • (1994) Ann. N.Y. Acad. Sci. , vol.747 , pp. 1-11
    • Khachaturian, Z.S.1
  • 39
    • 0026662333 scopus 로고
    • Use of engineered proteins with internal tryptophan reporter groups and perturbation techniques to probe the mechanism of ligand-protein interactions: Investigation of the mechanism of calcium binding to calcium
    • Kilhouffer, M. C., M. Kubina, F. Travers, and J. Haiech. 1992. Use of engineered proteins with internal tryptophan reporter groups and perturbation techniques to probe the mechanism of ligand-protein interactions: investigation of the mechanism of calcium binding to calcium. Biochemistry. 31:8098-8106.
    • (1992) Biochemistry , vol.31 , pp. 8098-8106
    • Kilhouffer, M.C.1    Kubina, M.2    Travers, F.3    Haiech, J.4
  • 40
    • 0017355688 scopus 로고
    • 2+ to the protein activator of 3′,5′-cyclic adenosine monophosphate phosphodiesterase
    • 2+ to the protein activator of 3′,5′-cyclic adenosine monophosphate phosphodiesterase. Biochemistry. 16:1017-1024.
    • (1977) Biochemistry , vol.16 , pp. 1017-1024
    • Klee, C.B.1
  • 41
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of proteins structures
    • Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of proteins structures. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 43
    • 0022425328 scopus 로고
    • Time-resolved fluorescence anisotropies of diphenylhexatriene and perylene in solvents and lipid bilayers obtained from multifrequency phase-modulation fluorometry
    • Lakowicz, J. R., H. Cherek, B. P. Maliwal, and E. Gratton. 1985. Time-resolved fluorescence anisotropies of diphenylhexatriene and perylene in solvents and lipid bilayers obtained from multifrequency phase-modulation fluorometry. Biochemistry. 24:376-383.
    • (1985) Biochemistry , vol.24 , pp. 376-383
    • Lakowicz, J.R.1    Cherek, H.2    Maliwal, B.P.3    Gratton, E.4
  • 44
    • 0000772394 scopus 로고
    • Frequency-domain fluorescence spectroscopy
    • J. R. Lakowicz, editor. Plenum Press, New York
    • Lakowicz, J. R., and I. Gryczynski. 1991. Frequency-domain fluorescence spectroscopy. In Topics in Fluorescence Spectroscopy, Vol. I. J. R. Lakowicz, editor. Plenum Press, New York. 293-335.
    • (1991) Topics in Fluorescence Spectroscopy , vol.1 , pp. 293-335
    • Lakowicz, J.R.1    Gryczynski, I.2
  • 45
    • 0000714251 scopus 로고
    • Cloning of cDNA sequences encoding the calcium-binding protein, calmodulin, from barley (Hordeum vugare L.)
    • Ling, V., and R. E. Zielinski. 1989. Cloning of cDNA sequences encoding the calcium-binding protein, calmodulin, from barley (Hordeum vugare L.). Plant Physiol. 90:714-719.
    • (1989) Plant Physiol. , vol.90 , pp. 714-719
    • Ling, V.1    Zielinski, R.E.2
  • 46
    • 0019878589 scopus 로고
    • Proximity relationships within the Fc segment of rabbit immunoglobulin G analyzed by resonance energy transfer
    • Luedtke, R., C. S. Owen, J. M. Vanderkooi, and F. Karush. 1981. Proximity relationships within the Fc segment of rabbit immunoglobulin G analyzed by resonance energy transfer. Biochemistry. 20:2927-2936.
    • (1981) Biochemistry , vol.20 , pp. 2927-2936
    • Luedtke, R.1    Owen, C.S.2    Vanderkooi, J.M.3    Karush, F.4
  • 47
    • 0001079621 scopus 로고
    • Structural characterization of a higher plant calmodulin: Spinacia oleracea
    • Lukas, T. J., D. B. Iverson, M. Schleicher, and D. M. Watterson. 1984. Structural characterization of a higher plant calmodulin: Spinacia oleracea. Plant Physiol. 75:788-795.
    • (1984) Plant Physiol. , vol.75 , pp. 788-795
    • Lukas, T.J.1    Iverson, D.B.2    Schleicher, M.3    Watterson, D.M.4
  • 48
    • 0025789801 scopus 로고
    • Calcium-induced sensitization of the central helix of calmodulin to proteolysis
    • MacKall, J., and C. B. Klee. 1991. Calcium-induced sensitization of the central helix of calmodulin to proteolysis. Biochemistry. 30:7242-7247.
    • (1991) Biochemistry , vol.30 , pp. 7242-7247
    • MacKall, J.1    Klee, C.B.2
  • 50
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex
    • Meador, W. E., A. R. Means, and F. A. Quiocho. 1992. Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Science. 257:1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 51
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structure
    • Meador, W. E., A. R. Means, and F. A. Quiocho. 1993. Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structure. Science. 262:1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 53
    • 0029972702 scopus 로고    scopus 로고
    • Interlobe communication in multiple calcium-binding site mutants of Drosophila calmodulin
    • Mukherjea, P., J. F. Maune, and K. Beckingham. 1996. Interlobe communication in multiple calcium-binding site mutants of Drosophila calmodulin. Protein Sci. 5:468-477.
    • (1996) Protein Sci. , vol.5 , pp. 468-477
    • Mukherjea, P.1    Maune, J.F.2    Beckingham, K.3
  • 54
    • 0002874331 scopus 로고
    • Fast atom bombardment mass spectrometry of phospholipids
    • Murphy, R. C., and K. A. Harrison. 1994. Fast atom bombardment mass spectrometry of phospholipids. Mass Spectrom. Rev. 13:57-75.
    • (1994) Mass Spectrom. Rev. , vol.13 , pp. 57-75
    • Murphy, R.C.1    Harrison, K.A.2
  • 56
    • 0028927330 scopus 로고
    • 2+ binding to calmodulin: Proteolytic susceptibility of E31 and E87 indicates interdomain interactions
    • 2+ binding to calmodulin: proteolytic susceptibility of E31 and E87 indicates interdomain interactions. Biochemistry. 34:1179-1196.
    • (1995) Biochemistry , vol.34 , pp. 1179-1196
    • Pedigo, S.1    Shea, M.A.2
  • 57
    • 0029147004 scopus 로고
    • 1H-nuclear magnetic resonance spectroscopy
    • 1H-nuclear magnetic resonance spectroscopy. Biochemistry. 34:10676-10689.
    • (1995) Biochemistry , vol.34 , pp. 10676-10689
    • Pedigo, S.1    Shea, M.A.2
  • 60
    • 0027637310 scopus 로고
    • Understanding fluorescence decays in proteins
    • Royer, C. A. 1993. Understanding fluorescence decays in proteins. Biophys. J. 65:9-10.
    • (1993) Biophys. J. , vol.65 , pp. 9-10
    • Royer, C.A.1
  • 62
    • 0015057050 scopus 로고
    • A new basis for interpreting the circular dichroic spectra of proteins
    • Saxena, V. P., and D. B. Wetlaufer. 1971. A new basis for interpreting the circular dichroic spectra of proteins. Proc. Natl. Acad. Sci. USA. 66: 969-972.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.66 , pp. 969-972
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 63
    • 0029119568 scopus 로고
    • RASMOL: Biomolecular graphics for all
    • Sayle, R. A., and E. J. Milner. 1995. RASMOL: biomolecular graphics for all. Trends Biochem. Sci. 20:374-376.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 374-376
    • Sayle, R.A.1    Milner, E.J.2
  • 65
    • 0019319097 scopus 로고
    • Calcium- and magnesium-dependent conformational states of calmodulin as determined by nuclear magnetic resonance
    • Seamon, K. B. 1980. Calcium-and magnesium-dependent conformational states of calmodulin as determined by nuclear magnetic resonance. Biochemistry. 19:207-215.
    • (1980) Biochemistry , vol.19 , pp. 207-215
    • Seamon, K.B.1
  • 66
    • 0031038918 scopus 로고    scopus 로고
    • Alzheimer's disease: Genotypes, phenotypes, and treatments
    • Selkoe, D. J. 1997. Alzheimer's disease: genotypes, phenotypes, and treatments. Science. 275:630-631.
    • (1997) Science , vol.275 , pp. 630-631
    • Selkoe, D.J.1
  • 68
    • 0024284795 scopus 로고
    • Fluorescence anisotropy decay demonstrates calcium-dependent shape changes in photo-cross-linked calmodulin
    • Small, E. W., and S. R. Anderson. 1988. Fluorescence anisotropy decay demonstrates calcium-dependent shape changes in photo-cross-linked calmodulin. Biochemistry. 27:419-428.
    • (1988) Biochemistry , vol.27 , pp. 419-428
    • Small, E.W.1    Anderson, S.R.2
  • 70
    • 0039926756 scopus 로고
    • Principles and practice of electrospray ionization-mass spectrometry for large polypeptides and proteins
    • Smith, R. D., J. A. Loo, R. R. Ogorzalek, M. Bushman, and H. R. Udseth. 1991. Principles and practice of electrospray ionization-mass spectrometry for large polypeptides and proteins. Mass. Spectrom. Rev. 10: 359-451.
    • (1991) Mass. Spectrom. Rev. , vol.10 , pp. 359-451
    • Smith, R.D.1    Loo, J.A.2    Ogorzalek, R.R.3    Bushman, M.4    Udseth, H.R.5
  • 71
    • 0030038103 scopus 로고    scopus 로고
    • Oxidative stress, caloric restriction, and aging
    • Sohal, R. S., and R. Weindruch. 1996. Oxidative stress, caloric restriction, and aging. Science. 273:59-63.
    • (1996) Science , vol.273 , pp. 59-63
    • Sohal, R.S.1    Weindruch, R.2
  • 72
    • 0029753786 scopus 로고    scopus 로고
    • Calcium binding decreases the Stokes radius of calmodulin and mutants R74A, R90A, and R90G
    • Sorensen, B. R., and M. A. Shea. 1996. Calcium binding decreases the Stokes radius of calmodulin and mutants R74A, R90A, and R90G. Biophys. J. 71:3407-3420.
    • (1996) Biophys. J. , vol.71 , pp. 3407-3420
    • Sorensen, B.R.1    Shea, M.A.2
  • 73
    • 0027080159 scopus 로고
    • A series of point mutations reveal interactions between the calcium-binding sites of calmodulin
    • Starovasnik, M. A., D.-R. Su, K. Beckingham, and R. E. Klevit. 1992. A series of point mutations reveal interactions between the calcium-binding sites of calmodulin. Protein Sci. 1:245-253.
    • (1992) Protein Sci. , vol.1 , pp. 245-253
    • Starovasnik, M.A.1    Su, D.-R.2    Beckingham, K.3    Klevit, R.E.4
  • 74
    • 0001966229 scopus 로고
    • Fluorescence anisotropy: Theory and applications
    • J. R. Lakowicz, editor. Plenum Press, New York
    • Steiner, R. F. 1991. Fluorescence anisotropy: theory and applications. In Topics in Fluorescence Spectroscopy, Vol. 2. J. R. Lakowicz, editor. Plenum Press, New York. 1-52.
    • (1991) Topics in Fluorescence Spectroscopy , vol.2 , pp. 1-52
    • Steiner, R.F.1
  • 76
    • 0029240357 scopus 로고
    • Calmodulin gene family in potato: Developmental and touch-induced expression of the mRNA encoding a novel isoform
    • Takezawa, D., Z. H. Liu, G. An, and B. W. Poovaiah. 1995. Calmodulin gene family in potato: developmental and touch-induced expression of the mRNA encoding a novel isoform. Plant Mol. Biol. 27:693-703.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 693-703
    • Takezawa, D.1    Liu, Z.H.2    An, G.3    Poovaiah, B.W.4
  • 77
    • 0021354296 scopus 로고
    • Metal ion and drug binding to proteolytic fragments of calmodulm: Proteolytic, cadmium-113, and proton nuclear magnetic resonance studies
    • Thulin, E., A. Anderson, T. Drakenberg, S. Forsen, and H. J. Vogel. 1984. Metal ion and drug binding to proteolytic fragments of calmodulm: proteolytic, cadmium-113, and proton nuclear magnetic resonance studies. Biochemistry. 23:1862-1870.
    • (1984) Biochemistry , vol.23 , pp. 1862-1870
    • Thulin, E.1    Anderson, A.2    Drakenberg, T.3    Forsen, S.4    Vogel, H.J.5
  • 78
    • 0022126384 scopus 로고
    • Amino acid sequence of calmodulin from wheat germ
    • Toda, H., M. Yazawa, F. Sakiyama, and K. Yagi. 1985. Amino acid sequence of calmodulin from wheat germ. J. Biochem. (Tokyo). 98: 833-842.
    • (1985) J. Biochem. (Tokyo) , vol.98 , pp. 833-842
    • Toda, H.1    Yazawa, M.2    Sakiyama, F.3    Yagi, K.4
  • 79
    • 0028376070 scopus 로고
    • Correction to amino acid sequence of calmodulin from wheat germ
    • Toda, H., M. Yazawa, F. Sakiyama, and K. Yagi. 1994. Correction to amino acid sequence of calmodulin from wheat germ. J. Biochem. (Tokyo). 115:367.
    • (1994) J. Biochem. (Tokyo) , vol.115 , pp. 367
    • Toda, H.1    Yazawa, M.2    Sakiyama, F.3    Yagi, K.4
  • 80
    • 0026536393 scopus 로고
    • Effects of calcium binding on the internal dynamic properties of bovine brain calmodulin, studied by NMR and optical spectroscopy
    • Török, K., A. N. Lane, S. N. Martin, J.-M. Janot, and P. M. Bailey. 1992. Effects of calcium binding on the internal dynamic properties of bovine brain calmodulin, studied by NMR and optical spectroscopy. Biochemistry. 31:3452-3462.
    • (1992) Biochemistry , vol.31 , pp. 3452-3462
    • Török, K.1    Lane, A.N.2    Martin, S.N.3    Janot, J.-M.4    Bailey, P.M.5
  • 82
    • 0001142223 scopus 로고
    • Resolution of the fluorescence lifetimes in a heterogeneous system by phase and modulation measurements
    • Weber, G. 1981. Resolution of the fluorescence lifetimes in a heterogeneous system by phase and modulation measurements. J. Phys. Chem. 85:949-953.
    • (1981) J. Phys. Chem. , vol.85 , pp. 949-953
    • Weber, G.1
  • 83
    • 0029999946 scopus 로고    scopus 로고
    • Characterization of the calmodulin gene family in wheat: Structure, chromosomal location, and evolutionary aspects
    • Yang, T., G. Segal, S. Abbo, M. Feldman, and H. Fromm. 1996. Characterization of the calmodulin gene family in wheat: structure, chromosomal location, and evolutionary aspects. Mol. Gen. Genet. 252: 684-694.
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 684-694
    • Yang, T.1    Segal, G.2    Abbo, S.3    Feldman, M.4    Fromm, H.5
  • 84
    • 0028232698 scopus 로고
    • Resolution of structural changes associated with calcium activation of calmodulin using frequency-domain fluorescence spectroscopy
    • Yao, Y., Ch. Schöneich, and T. C. Squier. 1994. Resolution of structural changes associated with calcium activation of calmodulin using frequency-domain fluorescence spectroscopy. Biochemistry. 33: 7797-7810.
    • (1994) Biochemistry , vol.33 , pp. 7797-7810
    • Yao, Y.1    Schöneich, Ch.2    Squier, T.C.3
  • 85
    • 0029982749 scopus 로고    scopus 로고
    • Variable conformation and dynamics of calmodulin complexed with peptides derived from the autoinhibitory domains of target proteins
    • Yao, Y., and T. C. Squier. 1996. Variable conformation and dynamics of calmodulin complexed with peptides derived from the autoinhibitory domains of target proteins. Biochemistry. 35:6815-6827.
    • (1996) Biochemistry , vol.35 , pp. 6815-6827
    • Yao, Y.1    Squier, T.C.2
  • 86
    • 0029969392 scopus 로고    scopus 로고
    • Oxidative modification of a carboxyl-terminal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase
    • Yao, Y., D. Yin, G. Jas, K. Kuczera, T. D. Williams, Ch. Schöneich, and T. C. Squier. 1996. Oxidative modification of a carboxyl-terminal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase. Biochemistry 35:2767-2787.
    • (1996) Biochemistry , vol.35 , pp. 2767-2787
    • Yao, Y.1    Yin, D.2    Jas, G.3    Kuczera, K.4    Williams, T.D.5    Schöneich, Ch.6    Squier, T.C.7
  • 87
    • 0009741751 scopus 로고
    • Vicinal methionines define the oxidatively sensitive sites on calmodulin
    • Yin, D., A. Hühmer, Ch. Schöneich, and T. C. Squier. 1995. Vicinal methionines define the oxidatively sensitive sites on calmodulin. Biophys. J. 68:A165.
    • (1995) Biophys. J. , vol.68
    • Yin, D.1    Hühmer, A.2    Schöneich, Ch.3    Squier, T.C.4
  • 88
    • 0020988987 scopus 로고
    • Divalent cation binding to wheat germ calmodulin
    • Yoshida, M., O. Minowa, and K. Yagi. 1983. Divalent cation binding to wheat germ calmodulin. J. Biochem. (Tokyo). 94:1925-1933.
    • (1983) J. Biochem. (Tokyo) , vol.94 , pp. 1925-1933
    • Yoshida, M.1    Minowa, O.2    Yagi, K.3
  • 89
    • 0028176721 scopus 로고
    • The effect of Met → Leu mutations on calmodulin's ability to activate cyclic nucleotide phosphodiesterase
    • Zhang, M., M. Li, J. H. Wang, and H. J. Vogel. 1994. The effect of Met → Leu mutations on calmodulin's ability to activate cyclic nucleotide phosphodiesterase. J. Biol. Chem. 269:15546-15552.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15546-15552
    • Zhang, M.1    Li, M.2    Wang, J.H.3    Vogel, H.J.4
  • 90
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., T. Tanaka, and M. Ikura. 1995. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nature Struct. Biol. 2:758-767.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3


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