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Volumn 44, Issue 1, 2005, Pages 278-284

Direct detection of calmodulin tuning by ryanodine receptor channel targets using a Ca2+-sensitive acrylodan-labeled calmodulin

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENCE; MUSCLE; PHYSIOLOGY; POLYPEPTIDES; POSITIVE IONS;

EID: 11844277586     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048246u     Document Type: Article
Times cited : (18)

References (33)
  • 1
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich, K. P., and Ikura, M. (2002) Calmodulin in action: Diversity in target recognition and activation mechanisms, Cell 108, 739-742.
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 2
    • 0037318056 scopus 로고    scopus 로고
    • Novel aspects of calmodulin target recognition and activation
    • Vetter, S. W., and Leclerc, E. (2003) Novel aspects of calmodulin target recognition and activation, Eur. J. Biochem. 270, 404-414.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 404-414
    • Vetter, S.W.1    Leclerc, E.2
  • 3
    • 0022318905 scopus 로고
    • Calcium binding to complexes of calmodulin and calmodulin binding proteins
    • Olwin, B. B., and Storm, D. R. (1985) Calcium binding to complexes of calmodulin and calmodulin binding proteins, Biochemistry 24, 8081-8086.
    • (1985) Biochemistry , vol.24 , pp. 8081-8086
    • Olwin, B.B.1    Storm, D.R.2
  • 7
    • 0028047785 scopus 로고
    • Calmodulin interaction with the skeletal muscle sarcoplasmic reticulum calcium channel protein
    • Yang, H. C., Reedy, M. M., Burke, C. L., and Strasburg, G. M. (1994) Calmodulin interaction with the skeletal muscle sarcoplasmic reticulum calcium channel protein, Biochemistry 33, 518-525.
    • (1994) Biochemistry , vol.33 , pp. 518-525
    • Yang, H.C.1    Reedy, M.M.2    Burke, C.L.3    Strasburg, G.M.4
  • 9
    • 0036147144 scopus 로고    scopus 로고
    • Modulation of intracellular calcium-release channels by calmodulin
    • Balshaw, D. M., Yamaguchi, N., and Meissner, G. (2002) Modulation of intracellular calcium-release channels by calmodulin, J. Membr. Biol. 185, 1-8.
    • (2002) J. Membr. Biol. , vol.185 , pp. 1-8
    • Balshaw, D.M.1    Yamaguchi, N.2    Meissner, G.3
  • 11
    • 0037059329 scopus 로고    scopus 로고
    • 2+-calmodulin bind to neighboring locations on the ryanodine receptor
    • 2+-calmodulin bind to neighboring locations on the ryanodine receptor, J. Biol. Chem. 277, 1349-1353.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1349-1353
    • Samso, M.1    Wagenknecht, T.2
  • 13
    • 0035910462 scopus 로고    scopus 로고
    • Calcium binding to calmodulin leads to an N-terminal shift in its binding site on the ryanodine receptor
    • Rodney, G. G., Moore, C. P., Williams, B. Y., Zhang, J. Z., Krol, J., Pedersen, S. E., and Hamilton, S. L. (2001) Calcium binding to calmodulin leads to an N-terminal shift in its binding site on the ryanodine receptor, J. Biol. Chem. 276, 2069-2074.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2069-2074
    • Rodney, G.G.1    Moore, C.P.2    Williams, B.Y.3    Zhang, J.Z.4    Krol, J.5    Pedersen, S.E.6    Hamilton, S.L.7
  • 17
    • 0030777358 scopus 로고    scopus 로고
    • 2+ release by direct and specific action at skeletal muscle ryanodine receptors
    • 2+ release by direct and specific action at skeletal muscle ryanodine receptors, J. Biol. Chem. 272, 26965-26971.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26965-26971
    • Fruen, B.R.1    Mickelson, J.R.2    Louis, C.F.3
  • 19
    • 0020493109 scopus 로고
    • 2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatography
    • 2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatography, Biochem. Biophys. Res. Commun. 104, 830-836.
    • (1982) Biochem. Biophys. Res. Commun. , vol.104 , pp. 830-836
    • Gopalakrishna, R.1    Anderson, W.B.2
  • 21
    • 0026531719 scopus 로고
    • Bound and Determined: A computer program for making buffers of defined ion concentrations
    • Brooks, S. P., and Storey, K. B. (1992) Bound and Determined: A computer program for making buffers of defined ion concentrations, Anal. Biochem. 201, 119-126.
    • (1992) Anal. Biochem. , vol.201 , pp. 119-126
    • Brooks, S.P.1    Storey, K.B.2
  • 22
    • 0035827585 scopus 로고    scopus 로고
    • Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor)
    • Balshaw, D. M., Xu, L., Yamaguchi, N., Pasek, D. A., and Meissner, G. (2001) Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor), J. Biol. Chem. 276, 20144-20153.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20144-20153
    • Balshaw, D.M.1    Xu, L.2    Yamaguchi, N.3    Pasek, D.A.4    Meissner, G.5
  • 23
    • 0031851511 scopus 로고    scopus 로고
    • Interactions of a reversible ryanoid (21-amino-9α-hydroxyryanodine) with single sheep cardiac ryanodine receptor channels
    • Tanna, B., Welch, W., Ruest, L., Sutko, J. L., and Williams, A. J. (1998) Interactions of a reversible ryanoid (21-amino-9α-hydroxyryanodine) with single sheep cardiac ryanodine receptor channels, J. Gen. Physiol. 112, 55-69.
    • (1998) J. Gen. Physiol. , vol.112 , pp. 55-69
    • Tanna, B.1    Welch, W.2    Ruest, L.3    Sutko, J.L.4    Williams, A.J.5
  • 26
    • 0021112116 scopus 로고
    • Synthesis, spectral properties, and use of 6-acryloyl-2- dimethylaminonaphthalene (Acrylodan). A thiol-selective, polarity-sensitive fluorescent probe
    • Prendergast, F. G., Meyer, M., Carlson, G. L., Iida, S., and Potter, J. D. (1983) Synthesis, spectral properties, and use of 6-acryloyl-2- dimethylaminonaphthalene (Acrylodan). A thiol-selective, polarity-sensitive fluorescent probe, J. Biol. Chem. 258, 7541-7544.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7541-7544
    • Prendergast, F.G.1    Meyer, M.2    Carlson, G.L.3    Iida, S.4    Potter, J.D.5
  • 27
    • 0025079867 scopus 로고
    • Fluorescent adducts of wheat calmodulin implicate the amino-terminal region in the activation of skeletal muscle myosin light chain kinase
    • Zot, H. G., Aden, R., Samy, S., and Puett, D. (1990) Fluorescent adducts of wheat calmodulin implicate the amino-terminal region in the activation of skeletal muscle myosin light chain kinase, J. Biol. Chem. 265, 14796-14801.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14796-14801
    • Zot, H.G.1    Aden, R.2    Samy, S.3    Puett, D.4
  • 28
    • 0023880226 scopus 로고
    • Site-specific derivatives of wheat germ calmodulin. Interactions with troponin and sarcoplasmic reticulum
    • Strasburg, G. M., Hogan, M., Birmachu, W., Thomas, D. D., and Louis, C. F. (1988) Site-specific derivatives of wheat germ calmodulin. Interactions with troponin and sarcoplasmic reticulum, J. Biol. Chem. 263, 542-548.
    • (1988) J. Biol. Chem. , vol.263 , pp. 542-548
    • Strasburg, G.M.1    Hogan, M.2    Birmachu, W.3    Thomas, D.D.4    Louis, C.F.5
  • 29
    • 0035066857 scopus 로고    scopus 로고
    • Oxidatively modified calmodulin binds to the plasma membrane Ca-ATPase in a nonproductive and conformationally disordered complex
    • Gao, J., Yao, Y., and Squier, T. C. (2001) Oxidatively modified calmodulin binds to the plasma membrane Ca-ATPase in a nonproductive and conformationally disordered complex. Biophys. J. 80, 1791-1801.
    • (2001) Biophys. J. , vol.80 , pp. 1791-1801
    • Gao, J.1    Yao, Y.2    Squier, T.C.3
  • 30
    • 0024282315 scopus 로고
    • Biologically active fluorescent derivatives of spinach calmodulin that report calmodulin target protein binding
    • Mills, J. S., Walsh, M. P., Nemcek, K., and Johnson, J. D. (1988) Biologically active fluorescent derivatives of spinach calmodulin that report calmodulin target protein binding. Biochemistry 27, 991-996.
    • (1988) Biochemistry , vol.27 , pp. 991-996
    • Mills, J.S.1    Walsh, M.P.2    Nemcek, K.3    Johnson, J.D.4
  • 31
    • 0028232698 scopus 로고
    • Resolution of structural changes associated with calcium activation of calmodulin using frequency domain fluorescence spectroscopy
    • Yao, Y., Schoneich, C., and Squier, T. C. (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    Schoneich, C.2    Squier, T.C.3
  • 32
    • 0032204474 scopus 로고    scopus 로고
    • Effects of Fluorescent Reporter Group Structure on the Dynamics Surrounding Cysteine-26 in Spinach Calmodulin: A Model Biorecognition Element
    • Watkins, A. N., and Bright, F. V. (1998) Effects of Fluorescent Reporter Group Structure on the Dynamics Surrounding Cysteine-26 in Spinach Calmodulin: A Model Biorecognition Element, Appl. Spectrosc. 52, 1447-1456.
    • (1998) Appl. Spectrosc. , vol.52 , pp. 1447-1456
    • Watkins, A.N.1    Bright, F.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.