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Volumn 33, Issue 9, 2006, Pages 763-772

Excitation-contraction coupling from the 1950s into the new millennium

Author keywords

Calcium signalling; Cardiac muscle; Excitation contraction coupling; Signal transduction; Skeletal muscle

Indexed keywords

1,4 DIHYDROPYRIDINE RECEPTOR; CALCIUM; CALCIUM BINDING PROTEIN; CALCIUM CHANNEL L TYPE; CALSEQUESTRIN; FK 506 BINDING PROTEIN; GLUTATHIONE TRANSFERASE; INOSITOL 1,4,5 TRISPHOSPHATE; RYANODINE RECEPTOR;

EID: 33747045217     PISSN: 03051870     EISSN: 14401681     Source Type: Journal    
DOI: 10.1111/j.1440-1681.2006.04441.x     Document Type: Short Survey
Times cited : (124)

References (81)
  • 1
    • 33646167958 scopus 로고
    • Local activation of interfibrillar structures in striated muscle
    • Huxley AF, Straub RW. Local activation of interfibrillar structures in striated muscle. J. Physiol. 1958; 143: P40-1.
    • (1958) J. Physiol. , vol.143
    • Huxley, A.F.1    Straub, R.W.2
  • 2
    • 70449247729 scopus 로고
    • Local activation of striated muscle fibres
    • Huxley AF, Taylor RE. Local activation of striated muscle fibres. J. Physiol. 1958; 144: 426-41.
    • (1958) J. Physiol. , vol.144 , pp. 426-441
    • Huxley, A.F.1    Taylor, R.E.2
  • 3
    • 0001659046 scopus 로고
    • Studies on the endoplasmic reticulum. III. Its form and distribution in striated muscle cells
    • Porter KR, Palade GE. Studies on the endoplasmic reticulum. III. Its form and distribution in striated muscle cells. J. Biophys. Biochem. Cytol. 1957; 3: 269-300.
    • (1957) J. Biophys. Biochem. Cytol. , vol.3 , pp. 269-300
    • Porter, K.R.1    Palade, G.E.2
  • 4
    • 33747067808 scopus 로고
    • Fine structure of sarcoplasmic reticulum and tranverse tubular system in muscle fibers
    • Franzini-Armstrong C. Fine structure of sarcoplasmic reticulum and tranverse tubular system in muscle fibers. Fed. Proc. 1964; 23: 887-95.
    • (1964) Fed. Proc. , vol.23 , pp. 887-895
    • Franzini-Armstrong, C.1
  • 5
    • 0014570765 scopus 로고
    • Radial spread of contraction in frog muscle fibres
    • Adrian RH, Costantin LL, Peachey LD. Radial spread of contraction in frog muscle fibres. J. Physiol. 1969; 204: 231-57.
    • (1969) J. Physiol. , vol.204 , pp. 231-257
    • Adrian, R.H.1    Costantin, L.L.2    Peachey, L.D.3
  • 6
    • 0014483887 scopus 로고
    • Ionic conductances of the surface and transverse tubular membranes of frog sartorius fibers
    • Eisenberg RS, Gage PW. Ionic conductances of the surface and transverse tubular membranes of frog sartorius fibers. J. Gen. Physiol. 1969; 53: 279-97.
    • (1969) J. Gen. Physiol. , vol.53 , pp. 279-297
    • Eisenberg, R.S.1    Gage, P.W.2
  • 7
    • 0015622679 scopus 로고
    • Electrical properties of toad skeletal muscle fibres in summer and winter
    • Dulhunty AF, Gage PW. Electrical properties of toad skeletal muscle fibres in summer and winter. J. Physiol. 1973; 230: 619-41.
    • (1973) J. Physiol. , vol.230 , pp. 619-641
    • Dulhunty, A.F.1    Gage, P.W.2
  • 8
    • 85006142608 scopus 로고
    • Studies of the triad. I. Structure of the junction in frog twitch fibers
    • Franzini-Armstrong C. Studies of the triad. I. Structure of the junction in frog twitch fibers. J. Cell Biol. 1970; 47: 488-98.
    • (1970) J. Cell Biol. , vol.47 , pp. 488-498
    • Franzini-Armstrong, C.1
  • 9
    • 0014478733 scopus 로고
    • Action potentials, afterpotentials, and excitation-contraction coupling in frog sartorius fibers without transverse tubules
    • Gage PW, Eisenberg RS. Action potentials, afterpotentials, and excitation-contraction coupling in frog sartorius fibers without transverse tubules. J. Gen. Physiol. 1969; 53: 298-310.
    • (1969) J. Gen. Physiol. , vol.53 , pp. 298-310
    • Gage, P.W.1    Eisenberg, R.S.2
  • 10
    • 0015549376 scopus 로고
    • Studies of the triad. IV. Structure of the junction in frog slow fibers
    • Franzini-Armstrong C. Studies of the triad. IV. Structure of the junction in frog slow fibers. J. Cell Biol. 1973; 56: 120-8.
    • (1973) J. Cell Biol. , vol.56 , pp. 120-128
    • Franzini-Armstrong, C.1
  • 11
    • 0015963187 scopus 로고
    • Stereological analysis of mammalian skeletal muscle
    • Eisenberg BR, Kuda AM, Peter JB. Stereological analysis of mammalian skeletal muscle. J. Cell Biol. 1974; 60: 732-54.
    • (1974) J. Cell Biol. , vol.60 , pp. 732-754
    • Eisenberg, B.R.1    Kuda, A.M.2    Peter, J.B.3
  • 12
    • 0017356222 scopus 로고
    • The passive electrical properties of frog skeletal muscle fibres at different sarcomere lengths
    • Dulhunty AF, Franzini-Armstrong C. The passive electrical properties of frog skeletal muscle fibres at different sarcomere lengths. J. Physiol. 1977; 266: 687-711.
    • (1977) J. Physiol. , vol.266 , pp. 687-711
    • Dulhunty, A.F.1    Franzini-Armstrong, C.2
  • 13
    • 0016754249 scopus 로고
    • The relative contributions of the folds and caveolae to the surface membrane of frog skeletal muscle fibres at different sarcomere lengths
    • Dulhunty AF, Franzini-Armstrong C. The relative contributions of the folds and caveolae to the surface membrane of frog skeletal muscle fibres at different sarcomere lengths. J. Physiol. 1975; 250: 513-39.
    • (1975) J. Physiol. , vol.250 , pp. 513-539
    • Dulhunty, A.F.1    Franzini-Armstrong, C.2
  • 14
    • 0017904273 scopus 로고
    • The dependence of membrane potential on extracellular chloride concentration in mammalian skeletal muscle fibres
    • Dulhunty AF. The dependence of membrane potential on extracellular chloride concentration in mammalian skeletal muscle fibres. J. Physiol. 1978; 276: 67-82.
    • (1978) J. Physiol. , vol.276 , pp. 67-82
    • Dulhunty, A.F.1
  • 15
    • 0018687595 scopus 로고
    • Distribution of potassium and chloride permeability over the surface and T-tubule membranes of mammalian skeletal muscle
    • Dulhunty AF. Distribution of potassium and chloride permeability over the surface and T-tubule membranes of mammalian skeletal muscle. J. Membr. Biol. 1979; 45: 293-310.
    • (1979) J. Membr. Biol. , vol.45 , pp. 293-310
    • Dulhunty, A.F.1
  • 16
    • 0015868742 scopus 로고
    • Currents related to movement of the gating particles of the sodium channels
    • Armstrong CM, Bezanilla F. Currents related to movement of the gating particles of the sodium channels. Nature 1973; 242: 459-61.
    • (1973) Nature , vol.242 , pp. 459-461
    • Armstrong, C.M.1    Bezanilla, F.2
  • 17
    • 0016354136 scopus 로고
    • Charge movement associated with the opening and closing of the activation gates of the Na channels
    • Armstrong CM, Bezanilla F. Charge movement associated with the opening and closing of the activation gates of the Na channels. J. Gen. Physiol. 1974; 63: 533-52.
    • (1974) J. Gen. Physiol. , vol.63 , pp. 533-552
    • Armstrong, C.M.1    Bezanilla, F.2
  • 18
    • 35649001607 scopus 로고
    • A quantitative description of membrane current and its application to conduction and excitation in nerve
    • Hodgkin AL, Huxley AF. A quantitative description of membrane current and its application to conduction and excitation in nerve. J. Physiol. 1952; 117: 500-44.
    • (1952) J. Physiol. , vol.117 , pp. 500-544
    • Hodgkin, A.L.1    Huxley, A.F.2
  • 19
    • 0015856482 scopus 로고
    • Voltage dependent charge movement of skeletal muscle: A possible step in excitation-contraction coupling
    • Schneider MF, Chandler WK. Voltage dependent charge movement of skeletal muscle: A possible step in excitation-contraction coupling. Nature 1973; 242: 244-6.
    • (1973) Nature , vol.242 , pp. 244-246
    • Schneider, M.F.1    Chandler, W.K.2
  • 20
    • 0016882456 scopus 로고
    • Effects of glycerol treatment and maintained depolarization on charge movement in skeletal muscle
    • Chandler WK, Rakowski RF, Schneider MF. Effects of glycerol treatment and maintained depolarization on charge movement in skeletal muscle. J. Physiol. 1976; 254: 285-316.
    • (1976) J. Physiol. , vol.254 , pp. 285-316
    • Chandler, W.K.1    Rakowski, R.F.2    Schneider, M.F.3
  • 21
    • 0020642965 scopus 로고
    • Asymmetrical charge movement in slow- and fast-twitch mammalian muscle fibres in normal and paraplegic rats
    • Dulhunty AF, Gage PW. Asymmetrical charge movement in slow- and fast-twitch mammalian muscle fibres in normal and paraplegic rats. J. Physiol. 1983; 341: 213-31.
    • (1983) J. Physiol. , vol.341 , pp. 213-231
    • Dulhunty, A.F.1    Gage, P.W.2
  • 22
    • 0020642938 scopus 로고
    • Paralysis of frog skeletal muscle fibres by the calcium antagonist D-600
    • Eisenberg RS, McCarthy RT, Milton RL. Paralysis of frog skeletal muscle fibres by the calcium antagonist D-600. J. Physiol. 1983; 341: 495-505.
    • (1983) J. Physiol. , vol.341 , pp. 495-505
    • Eisenberg, R.S.1    McCarthy, R.T.2    Milton, R.L.3
  • 23
    • 0023933609 scopus 로고
    • Effects of extracellular calcium concentration and dihydropyridines on contraction in mammalian skeletal muscle
    • Dulhunty AF, Gage PW. Effects of extracellular calcium concentration and dihydropyridines on contraction in mammalian skeletal muscle. J. Physiol. 1988; 399: 63-80.
    • (1988) J. Physiol. , vol.399 , pp. 63-80
    • Dulhunty, A.F.1    Gage, P.W.2
  • 24
    • 0023162179 scopus 로고
    • Asymmetric charge movement in polarized and depolarized muscle fibres of the rabbit
    • Lamb GD. Asymmetric charge movement in polarized and depolarized muscle fibres of the rabbit. J. Physiol. 1987; 383: 349-67.
    • (1987) J. Physiol. , vol.383 , pp. 349-367
    • Lamb, G.D.1
  • 25
    • 0023113884 scopus 로고
    • Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle
    • Rios E, Brum G. Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle. Nature 1987; 325: 717-20.
    • (1987) Nature , vol.325 , pp. 717-720
    • Rios, E.1    Brum, G.2
  • 26
    • 0017345293 scopus 로고
    • Calcium release from the sarcoplasmic reticulum
    • Fabiato A, Fabiato F. Calcium release from the sarcoplasmic reticulum. Circ. Res. 1977; 40: 119-29.
    • (1977) Circ. Res. , vol.40 , pp. 119-129
    • Fabiato, A.1    Fabiato, F.2
  • 27
    • 0347641882 scopus 로고
    • Inositol 1,4,5-trisphosphate: A possible chemical link in excitation-contraction coupling in muscle
    • Vergara J, Tsien RY, Delay M. Inositol 1,4,5-trisphosphate: A possible chemical link in excitation-contraction coupling in muscle. Proc. Natl Acad. Sci. USA 1985; 82: 6352-6.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6352-6356
    • Vergara, J.1    Tsien, R.Y.2    Delay, M.3
  • 28
    • 0024346624 scopus 로고
    • Inositol trisphosphate and excitation-contraction coupling in skeletal muscle
    • Hidalgo C, Jaimovich E. Inositol trisphosphate and excitation-contraction coupling in skeletal muscle. J. Bioenerg. Biomembr. 1989; 21: 267-81.
    • (1989) J. Bioenerg. Biomembr. , vol.21 , pp. 267-281
    • Hidalgo, C.1    Jaimovich, E.2
  • 29
    • 0036025369 scopus 로고    scopus 로고
    • 2+ signals in muscle cells are involved in regulation of gene expression
    • 2+ signals in muscle cells are involved in regulation of gene expression. Biol. Res. 2002; 35: 195-202.
    • (2002) Biol. Res. , vol.35 , pp. 195-202
    • Jaimovich, E.1    Carrasco, M.A.2
  • 30
    • 0023008143 scopus 로고
    • 2+ release channel of sarcoplasmic reticulum
    • 2+ release channel of sarcoplasmic reticulum. J. Biol. Chem. 1986; 261: 6300-6.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6300-6306
    • Meissner, G.1
  • 31
    • 0022413366 scopus 로고
    • Sarcoplasmic reticulum contains adenine nucleotide-activated calcium channels
    • Smith JS, Coronado R, Meissner G. Sarcoplasmic reticulum contains adenine nucleotide-activated calcium channels. Nature 1985; 316: 446-9.
    • (1985) Nature , vol.316 , pp. 446-449
    • Smith, J.S.1    Coronado, R.2    Meissner, G.3
  • 32
    • 0022151294 scopus 로고
    • 2+ release channels with ryanodine in junctional terminal cisternae of sarcoplasmic reticulum of fast skeletal muscle
    • 2+ release channels with ryanodine in junctional terminal cisternae of sarcoplasmic reticulum of fast skeletal muscle. Proc. Natl Acad. Sci. USA 1985; 82: 7256-9.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7256-7259
    • Fleischer, S.1    Ogunbunmi, E.M.2    Dixon, M.C.3    Fleer, E.A.4
  • 33
    • 0023644484 scopus 로고
    • Purification of the ryanodine receptor and identity with feet structures of junctional terminal cisternae of sarcoplasmic reticulum from fast skeletal muscle
    • Inui M, Saito A, Fleischer S. Purification of the ryanodine receptor and identity with feet structures of junctional terminal cisternae of sarcoplasmic reticulum from fast skeletal muscle. J. Biol. Chem. 1987; 262: 1740-7.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1740-1747
    • Inui, M.1    Saito, A.2    Fleischer, S.3
  • 34
    • 0024245148 scopus 로고
    • Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle
    • Block BA, Imagawa T, Campbell KP, Franzini-Armstrong C. Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle. J. Cell Biol. 1988; 107: 2587-600.
    • (1988) J. Cell Biol. , vol.107 , pp. 2587-2600
    • Block, B.A.1    Imagawa, T.2    Campbell, K.P.3    Franzini-Armstrong, C.4
  • 35
    • 0027231287 scopus 로고
    • Ratio of ryanodine to dihydropyridine receptors in cardiac and skeletal muscle and implications for E-C coupling
    • Bers DM, Stiffel VM. Ratio of ryanodine to dihydropyridine receptors in cardiac and skeletal muscle and implications for E-C coupling. Am. J. Physiol. 1993; 264: C1587-93.
    • (1993) Am. J. Physiol. , vol.264
    • Bers, D.M.1    Stiffel, V.M.2
  • 36
    • 0000559465 scopus 로고
    • Reconstitution of cell membrane structure in vitro and its transformation into an excitable system
    • Mueller P, Rudin DO, Tien HT, Wescott WC. Reconstitution of cell membrane structure in vitro and its transformation into an excitable system. Nature 1962; 194: 979-80.
    • (1962) Nature , vol.194 , pp. 979-980
    • Mueller, P.1    Rudin, D.O.2    Tien, H.T.3    Wescott, W.C.4
  • 37
    • 0028180422 scopus 로고
    • ++ release channels and their regulation by endogenous effectors
    • ++ release channels and their regulation by endogenous effectors. Annu. Rev. Physiol. 1994; 56: 485-508.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 485-508
    • Meissner, G.1
  • 38
    • 0025364896 scopus 로고
    • Subunit structure and localization of dihydropyridine-sensitive calcium channels in mammalian brain, spinal cord, and retina
    • Ahlijanian MK, Westenbroek RE, Catterall WA. Subunit structure and localization of dihydropyridine-sensitive calcium channels in mammalian brain, spinal cord, and retina. Neuron 1990; 4: 819-32.
    • (1990) Neuron , vol.4 , pp. 819-832
    • Ahlijanian, M.K.1    Westenbroek, R.E.2    Catterall, W.A.3
  • 39
    • 0022640513 scopus 로고
    • A lethal mutation in mice eliminates the slow calcium current in skeletal muscle cells
    • Beam KG, Knudson CM, Powell JA. A lethal mutation in mice eliminates the slow calcium current in skeletal muscle cells. Nature 1986; 320: 168-70.
    • (1986) Nature , vol.320 , pp. 168-170
    • Beam, K.G.1    Knudson, C.M.2    Powell, J.A.3
  • 40
    • 0025288735 scopus 로고
    • Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling
    • Tanabe T, Beam KG, Adams BA, Niidome T, Numa S. Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling. Nature 1990; 346: 567-8.
    • (1990) Nature , vol.346 , pp. 567-568
    • Tanabe, T.1    Beam, K.G.2    Adams, B.A.3    Niidome, T.4    Numa, S.5
  • 41
    • 0032566748 scopus 로고    scopus 로고
    • Localization in the II-III loop of the dihydropyridine receptor of a sequence critical for excitation-contraction coupling
    • Nakai J, Tanabe T, Konno T, Adams B, Beam KG. Localization in the II-III loop of the dihydropyridine receptor of a sequence critical for excitation-contraction coupling. J. Biol. Chem. 1998; 273: 24 983-6.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24983-24986
    • Nakai, J.1    Tanabe, T.2    Konno, T.3    Adams, B.4    Beam, K.G.5
  • 42
    • 1042289749 scopus 로고    scopus 로고
    • Structural requirements of the dihydropyridine receptor alpha1S II-III loop for skeletal-type excitation-contraction coupling
    • Kugler G, Weiss RG, Flucher BE, Grabner M. Structural requirements of the dihydropyridine receptor alpha1S II-III loop for skeletal-type excitation-contraction coupling. J. Biol. Chem. 2004; 279: 4721-8.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4721-4728
    • Kugler, G.1    Weiss, R.G.2    Flucher, B.E.3    Grabner, M.4
  • 43
    • 0029083935 scopus 로고
    • Identification of calcium release-triggering and blocking regions of the II-III loop of the skeletal muscle dihydropyridine receptor
    • el-Hayek R, Antoniu B, Wang J, Hamilton SL, Ikemoto N. Identification of calcium release-triggering and blocking regions of the II-III loop of the skeletal muscle dihydropyridine receptor. J. Biol. Chem. 1995; 270: 22 116-18.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22116-22118
    • El-Hayek, R.1    Antoniu, B.2    Wang, J.3    Hamilton, S.L.4    Ikemoto, N.5
  • 44
    • 0032975217 scopus 로고    scopus 로고
    • Activation and inhibition of skeletal RyR channels by a part of the skeletal DHPR II-III loop. Effects of DHPR Ser687 and FKBP12
    • Dulhunty AF, Laver DR, Gallant EM, Casarotto MG, Pace SM, Curtis S. Activation and inhibition of skeletal RyR channels by a part of the skeletal DHPR II-III loop. Effects of DHPR Ser687 and FKBP12. Biophys. J. 1999; 77: 189-203.
    • (1999) Biophys. J. , vol.77 , pp. 189-203
    • Dulhunty, A.F.1    Laver, D.R.2    Gallant, E.M.3    Casarotto, M.G.4    Pace, S.M.5    Curtis, S.6
  • 45
    • 0037662824 scopus 로고    scopus 로고
    • The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors
    • Haarmann CS, Green D, Casarotto MG, Laver DR, Dulhunty AF. The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors. Biochem. J. 2003; 372: 305-16.
    • (2003) Biochem. J. , vol.372 , pp. 305-316
    • Haarmann, C.S.1    Green, D.2    Casarotto, M.G.3    Laver, D.R.4    Dulhunty, A.F.5
  • 46
    • 0032566748 scopus 로고    scopus 로고
    • Localization in the II-III loop of the dihydropyridine receptor of a sequence critical for excitation-contraction coupling
    • Nakai J, Tanabe T, Konno T, Adams B, Beam KG. Localization in the II-III loop of the dihydropyridine receptor of a sequence critical for excitation-contraction coupling. J. Biol. Chem. 1998; 273: 24 983-6.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24983-24986
    • Nakai, J.1    Tanabe, T.2    Konno, T.3    Adams, B.4    Beam, K.G.5
  • 48
    • 0029983398 scopus 로고    scopus 로고
    • Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor
    • Nakai J, Dirksen RT, Nguyen HT, Pessah IN, Beam KG, Allen PD. Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor. Nature 1996; 380: 72-5.
    • (1996) Nature , vol.380 , pp. 72-75
    • Nakai, J.1    Dirksen, R.T.2    Nguyen, H.T.3    Pessah, I.N.4    Beam, K.G.5    Allen, P.D.6
  • 51
    • 0036930754 scopus 로고    scopus 로고
    • Multiple regions of RyR1 mediate functional and structural interactions with alpha (1S)-dihydropyridine receptors in skeletal muscle
    • Protasi F, Paolini C, Nakai J, Beam KG, Franzini-Armstrong C, Allen PD. Multiple regions of RyR1 mediate functional and structural interactions with alpha (1S)-dihydropyridine receptors in skeletal muscle. Biophys. J. 2002; 83: 3230-44.
    • (2002) Biophys. J. , vol.83 , pp. 3230-3244
    • Protasi, F.1    Paolini, C.2    Nakai, J.3    Beam, K.G.4    Franzini-Armstrong, C.5    Allen, P.D.6
  • 52
    • 30044435649 scopus 로고    scopus 로고
    • 2+ channel {beta}-subunit and ryanodine receptor type 1 strengthens excitation-contraction coupling
    • 2+ channel {beta}-subunit and ryanodine receptor type 1 strengthens excitation-contraction coupling. Proc. Natl Acad. Sci. USA 2005; 102: 19 225-30.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 19225-19230
    • Cheng, W.1    Altafaj, X.2    Ronjat, M.3    Coronado, R.4
  • 53
    • 6344282907 scopus 로고    scopus 로고
    • Mapping sites of potential proximity between the dihydropyridine receptor and RyR1 in muscle using a cyan fluorescent protein-yellow fluorescent protein tandem as a fluorescence resonance energy transfer probe
    • Papadopoulos S, Leuranguer V, Bannister RA, Beam KG. Mapping sites of potential proximity between the dihydropyridine receptor and RyR1 in muscle using a cyan fluorescent protein-yellow fluorescent protein tandem as a fluorescence resonance energy transfer probe. J. Biol. Chem. 2004; 279: 44 046-56.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44046-44056
    • Papadopoulos, S.1    Leuranguer, V.2    Bannister, R.A.3    Beam, K.G.4
  • 54
    • 6344226668 scopus 로고    scopus 로고
    • Metabolic biotinylation as a probe of supramolecular structure of the triad junction in skeletal muscle
    • Lorenzon NM, Haarmann CS, Norris EE, Papadopoulos S, Beam KG. Metabolic biotinylation as a probe of supramolecular structure of the triad junction in skeletal muscle. J. Biol. Chem. 2004; 279: 44 057-64.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44057-44064
    • Lorenzon, N.M.1    Haarmann, C.S.2    Norris, E.E.3    Papadopoulos, S.4    Beam, K.G.5
  • 55
    • 1842431755 scopus 로고    scopus 로고
    • Calsequestrin and the calcium release channel of skeletal and cardiac muscle
    • Beard NA, Laver DR, Dulhunty AF. Calsequestrin and the calcium release channel of skeletal and cardiac muscle. Prog. Biophys. Mol. Biol. 2004; 85: 33-69.
    • (2004) Prog. Biophys. Mol. Biol. , vol.85 , pp. 33-69
    • Beard, N.A.1    Laver, D.R.2    Dulhunty, A.F.3
  • 56
    • 0031020935 scopus 로고    scopus 로고
    • Subconductance states in single channel activity of skeletal muscle ryanodine receptors after removal of FKBP12
    • Ahern GP, Junankar PR, Dulhunty AF. Subconductance states in single channel activity of skeletal muscle ryanodine receptors after removal of FKBP12. Biophys. J. 1996; 72: 146-62.
    • (1996) Biophys. J. , vol.72 , pp. 146-162
    • Ahern, G.P.1    Junankar, P.R.2    Dulhunty, A.F.3
  • 59
    • 33745357718 scopus 로고    scopus 로고
    • Effects of an alpha-helical ryanodine receptor C-terminal tail peptide on ryanodine receptor activity: Modulation by Homer
    • Epub ahead of print
    • Pouliquin P, Pace SM, Curtis SM et al. Effects of an alpha-helical ryanodine receptor C-terminal tail peptide on ryanodine receptor activity: Modulation by Homer. Int. J. Biochem. Cell. Biol. 2006 [Epub ahead of print].
    • (2006) Int. J. Biochem. Cell. Biol.
    • Pouliquin, P.1    Pace, S.M.2    Curtis, S.M.3
  • 60
    • 0035200868 scopus 로고    scopus 로고
    • Characteristics of irreversible ATP activation suggest that native skeletal ryanodine receptors can be phosphorylated via an endogenous CaMKII
    • Dulhunty AF, Laver D, Curtis SM, Pace S, Haarmann C, Gallant EM. Characteristics of irreversible ATP activation suggest that native skeletal ryanodine receptors can be phosphorylated via an endogenous CaMKII. Biophys. J. 2001; 81: 3240-52.
    • (2001) Biophys. J. , vol.81 , pp. 3240-3252
    • Dulhunty, A.F.1    Laver, D.2    Curtis, S.M.3    Pace, S.4    Haarmann, C.5    Gallant, E.M.6
  • 61
    • 0037414827 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation of the cardiac calcium release channel (ryanodine receptor) in normal and failing hearts. Role of phosphatases and response to isoproterenol
    • Reiken S, Gaburjakova M, Guatimosim S et al. Protein kinase A phosphorylation of the cardiac calcium release channel (ryanodine receptor) in normal and failing hearts. Role of phosphatases and response to isoproterenol. J. Biol. Chem. 2003; 278: 444-53.
    • (2003) J. Biol. Chem. , vol.278 , pp. 444-453
    • Reiken, S.1    Gaburjakova, M.2    Guatimosim, S.3
  • 62
    • 27744546285 scopus 로고    scopus 로고
    • Ryanodine receptor type 1 (RyR1) mutations C4958S and C4961S reveal excitation-coupled calcium entry (ECCE) is independent of sarcoplasmic reticulum store depletion
    • Hurne AM, O'Brien JJ, Wingrove D et al. Ryanodine receptor type 1 (RyR1) mutations C4958S and C4961S reveal excitation-coupled calcium entry (ECCE) is independent of sarcoplasmic reticulum store depletion. J. Biol. Chem. 2005; 280: 36 994-7004.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36994-37004
    • Hurne, A.M.1    O'Brien, J.J.2    Wingrove, D.3
  • 63
    • 0038412004 scopus 로고    scopus 로고
    • Junctional membrane structure and store operated calcium entry in muscle cells
    • Ma J, Pan Z. Junctional membrane structure and store operated calcium entry in muscle cells. Front. Biosci. 2003; 8: D242-55.
    • (2003) Front. Biosci. , vol.8
    • Ma, J.1    Pan, Z.2
  • 64
    • 0026589932 scopus 로고
    • Cryo-EM of the native structure of the calcium release channel/ryanodine receptor from sarcoplasmic reticulum
    • Radermacher M, Wagenknecht T, Grassucci R et al. Cryo-EM of the native structure of the calcium release channel/ryanodine receptor from sarcoplasmic reticulum. Biophys. J. 1992; 61: 936-40.
    • (1992) Biophys. J. , vol.61 , pp. 936-940
    • Radermacher, M.1    Wagenknecht, T.2    Grassucci, R.3
  • 65
    • 0028937373 scopus 로고
    • Electron cryomicroscopy and angular reconstitution used to visualize the skeletal muscle calcium release channel
    • Serysheva II, Orlova EV, Chiu W, Sherman MB, Hamilton SL, van Heel M. Electron cryomicroscopy and angular reconstitution used to visualize the skeletal muscle calcium release channel. Nat. Struct. Biol. 1995; 2: 18-24.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 18-24
    • Serysheva, I.I.1    Orlova, E.V.2    Chiu, W.3    Sherman, M.B.4    Hamilton, S.L.5    Van Heel, M.6
  • 66
    • 22444444618 scopus 로고    scopus 로고
    • Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM
    • Samso M, Wagenknecht T, Allen PD. Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM. Nat. Struct. Mol. Biol. 2005; 12: 539-44.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 539-544
    • Samso, M.1    Wagenknecht, T.2    Allen, P.D.3
  • 69
    • 19444364685 scopus 로고    scopus 로고
    • Physical coupling between ryanodine receptor-calcium release channels
    • Yin CC, Blayney LM, Lai FA. Physical coupling between ryanodine receptor-calcium release channels. J. Mol. Biol. 2005; 349: 538-46.
    • (2005) J. Mol. Biol. , vol.349 , pp. 538-546
    • Yin, C.C.1    Blayney, L.M.2    Lai, F.A.3
  • 70
    • 0036617107 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of ryanodine receptors
    • Wagenknecht T, Samso M. Three-dimensional reconstruction of ryanodine receptors. Front. Biosci. 2002; 7: D1464-74.
    • (2002) Front. Biosci. , vol.7
    • Wagenknecht, T.1    Samso, M.2
  • 71
    • 1842786905 scopus 로고    scopus 로고
    • Location of divergent region 2 on the three-dimensional structure of cardiac muscle ryanodine receptor/calcium release channel
    • Liu Z, Zhang J, Wang R, Chen SR, Wagenknecht T. Location of divergent region 2 on the three-dimensional structure of cardiac muscle ryanodine receptor/calcium release channel. J. Mol. Biol. 2004; 338: 533-45.
    • (2004) J. Mol. Biol. , vol.338 , pp. 533-545
    • Liu, Z.1    Zhang, J.2    Wang, R.3    Chen, S.R.4    Wagenknecht, T.5
  • 72
    • 0034697313 scopus 로고    scopus 로고
    • A structural requirement for activation of skeletal ryanodine receptors by peptides of the dihydropyridine receptor II-III loop
    • Casarotto MG, Gibson F, Pace SM, Curtis SM, Mulcair M, Dulhunty AF. A structural requirement for activation of skeletal ryanodine receptors by peptides of the dihydropyridine receptor II-III loop. J. Biol. Chem. 2000; 275: 11 631-7.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11631-11637
    • Casarotto, M.G.1    Gibson, F.2    Pace, S.M.3    Curtis, S.M.4    Mulcair, M.5    Dulhunty, A.F.6
  • 73
    • 17644425846 scopus 로고    scopus 로고
    • Activating the ryanodine receptor with dihydropyridine receptor II-III loop segments: Size and charge do matter
    • Casarotto MG, Green D, Pace S, Young J, Dulhunty AF. Activating the ryanodine receptor with dihydropyridine receptor II-III loop segments: Size and charge do matter. Front. Biosci. 2004; 9: 2860-72.
    • (2004) Front. Biosci. , vol.9 , pp. 2860-2872
    • Casarotto, M.G.1    Green, D.2    Pace, S.3    Young, J.4    Dulhunty, A.F.5
  • 75
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 2005; 579: 3346-54.
    • (2005) FEBS Lett. , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 77
    • 0037708928 scopus 로고    scopus 로고
    • FKBP12.6 deficiency and defective calcium release channel (ryanodine receptor) function linked to exercise-induced sudden cardiac death
    • Wehrens XH, Lehnart SE, Huang F et al. FKBP12.6 deficiency and defective calcium release channel (ryanodine receptor) function linked to exercise-induced sudden cardiac death. Cell 2003; 113: 829-40.
    • (2003) Cell , vol.113 , pp. 829-840
    • Wehrens, X.H.1    Lehnart, S.E.2    Huang, F.3
  • 78
    • 0036514152 scopus 로고    scopus 로고
    • Regulation of calcium release by interdomain interaction within ryanodine receptors
    • Ikemoto N, Yamamoto T. Regulation of calcium release by interdomain interaction within ryanodine receptors. Front. Biosci. 2002; 7: D671-83.
    • (2002) Front. Biosci. , vol.7
    • Ikemoto, N.1    Yamamoto, T.2
  • 80
    • 20244362522 scopus 로고    scopus 로고
    • Functional implications of modifying RyR-activating peptides for membrane permeability
    • Dulhunty AF, Cengia L, Young J et al. Functional implications of modifying RyR-activating peptides for membrane permeability. Br. J. Pharmacol. 2005; 144: 743-54.
    • (2005) Br. J. Pharmacol. , vol.144 , pp. 743-754
    • Dulhunty, A.F.1    Cengia, L.2    Young, J.3


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