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Volumn 15, Issue 6, 2000, Pages 281-284

Calmodulin and excitation-contraction coupling

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EID: 0034556442     PISSN: 08861714     EISSN: None     Source Type: Journal    
DOI: 10.1152/physiologyonline.2000.15.6.281     Document Type: Article
Times cited : (28)

References (15)
  • 1
    • 0030789142 scopus 로고    scopus 로고
    • Ryanodine receptors of striated muscles: A complex channel capable of multiple interactions
    • Franzini-Armstrong C and Protasi F. Ryanodine receptors of striated muscles: a complex channel capable of multiple interactions. Physiol Rev 77: 699-729, 1997.
    • (1997) Physiol Rev , vol.77 , pp. 699-729
    • Franzini-Armstrong, C.1    Protasi, F.2
  • 2
    • 0010323182 scopus 로고    scopus 로고
    • Calmodulin activation of skeletal muscle (but not cardiac) ryanodine receptors: Modulation by effectors of calcium-induced calcium release
    • Fruen BR, Bardy JM, and Louis CF. Calmodulin activation of skeletal muscle (but not cardiac) ryanodine receptors: modulation by effectors of calcium-induced calcium release (Abstract). Biophys J 74: A61, 1998.
    • (1998) Biophys J , vol.74
    • Fruen, B.R.1    Bardy, J.M.2    Louis, C.F.3
  • 3
    • 0030589509 scopus 로고    scopus 로고
    • 2+-free calmodulin binding to unconventional myosins reveals how calmodulin acts as a regulatory switch
    • 2+-free calmodulin binding to unconventional myosins reveals how calmodulin acts as a regulatory switch. Structure 4: 1475-1490, 1996.
    • (1996) Structure , vol.4 , pp. 1475-1490
    • Houdusse, A.1    Silver, M.2    Cohen, C.3
  • 4
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, and Bax A. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256: 632-638, 1992.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 7
    • 0033601348 scopus 로고    scopus 로고
    • A role for cysteine 3635 of RYR1 in redox modulation and calmodulin binding
    • Moore CP, Zhang JZ, and Hamilton SL. A role for cysteine 3635 of RYR1 in redox modulation and calmodulin binding. J Biol Chem 274: 36831-36834, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 36831-36834
    • Moore, C.P.1    Zhang, J.Z.2    Hamilton, S.L.3
  • 9
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • Rhoads AR and Friedberg F. Sequence motifs for calmodulin recognition. FASEB J 1:331-340, 1997.
    • (1997) FASEB J , vol.1 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 12
    • 0028135535 scopus 로고
    • Localization of calmodulin binding sites on the ryanodine receptor from skeletal muscle by electron microscopy
    • Wagenknecht T, Berkowitz J, Grassucci R, Timerman A, and Fleischer S. Localization of calmodulin binding sites on the ryanodine receptor from skeletal muscle by electron microscopy. Biophys J 67: 2286-2295, 1994.
    • (1994) Biophys J , vol.67 , pp. 2286-2295
    • Wagenknecht, T.1    Berkowitz, J.2    Grassucci, R.3    Timerman, A.4    Fleischer, S.5
  • 13
    • 0031736790 scopus 로고    scopus 로고
    • Potential for pharmacology of ryanodine receptor/calcium release channels
    • Xu L, Tripathy A, Pasek DA, and Meissner G. Potential for pharmacology of ryanodine receptor/calcium release channels. Ann NY Acad Sci 853: 130-148, 1998.
    • (1998) Ann NY Acad Sci , vol.853 , pp. 130-148
    • Xu, L.1    Tripathy, A.2    Pasek, D.A.3    Meissner, G.4
  • 15
    • 0345465665 scopus 로고    scopus 로고
    • Calmodulin supports both inactivation and facilitation of L-type calcium channels
    • Zuhlke RD, Pitt GS, Deisseroth K, Tsien RW, and Reuter H. Calmodulin supports both inactivation and facilitation of L-type calcium channels. Nature 399: 59-62, 1999.
    • (1999) Nature , vol.399 , pp. 59-62
    • Zuhlke, R.D.1    Pitt, G.S.2    Deisseroth, K.3    Tsien, R.W.4    Reuter, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.