메뉴 건너뛰기




Volumn 49, Issue 1, 1997, Pages 53-98

The pharmacology of ryanodine and related compounds

Author keywords

[No Author keywords available]

Indexed keywords

10 O ACYLRYANODOL; 3 DEOXYRYANODOL; 3 O ACYL 3 EPIRYANODOL; CALCIUM CHANNEL; CALMODULIN; DRUG BINDING PROTEIN; HELOTHERMINE; IMPERATOXIN; LOCAL ANESTHETIC AGENT; MYOTOXIN; POLYAMINE; POLYCHLORINATED BIPHENYL; RYANODINE; RYANODINE RECEPTOR; RYANOTOXIN; SORCIN; SURAMIN; TACROLIMUS; TOXIN; TRIADIN; UNCLASSIFIED DRUG;

EID: 0030893595     PISSN: 00316997     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (252)

References (205)
  • 2
    • 0025126998 scopus 로고
    • Identification and localization of two triad junctional foot protein isoforms in mature avian fast twitch skeletal muscle
    • AIREY, J. A., BECK, C. F., TANKSLEY, S. J., MURAKAMI, K., DEERINCK, T. J., ELLISMAN, M. H., AND SUTKO, J. L.: Identification and localization of two triad junctional foot protein isoforms in mature avian fast twitch skeletal muscle. J. Biol. Chem. 265: 14187-14194, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14187-14194
    • Airey, J.A.1    Beck, C.F.2    Tanksley, S.J.3    Murakami, K.4    Deerinck, T.J.5    Ellisman, M.H.6    Sutko, J.L.7
  • 3
    • 0027427454 scopus 로고
    • Crooked Neck Dwarf (cn) chicken skeletal muscle cells in low density cultures fail to express normal a ryanodine receptor and exhibit a partial mutant phenotype
    • AIREY, J. A., DEERINCK, T. J., ELLISMAN, M. H., HOUENOU, L., IVANENKO, A., KENYON, J. L., MCKEMY, D. D., AND SUTKO, J. L.: Crooked Neck Dwarf (cn) chicken skeletal muscle cells in low density cultures fail to express normal a ryanodine receptor and exhibit a partial mutant phenotype. Dev. Dynam. 197: 189-202, 1993b.
    • (1993) Dev. Dynam. , vol.197 , pp. 189-202
    • Airey, J.A.1    Deerinck, T.J.2    Ellisman, M.H.3    Houenou, L.4    Ivanenko, A.5    Kenyon, J.L.6    McKemy, D.D.7    Sutko, J.L.8
  • 4
    • 0027193347 scopus 로고
    • Three ryanodine receptor isoforms exist in avian striated muscles
    • AIREY, J. A., GRINSELL, M. M., JONES, L. R., SUTKO, J. L., AND WITCHER, D. R.: Three ryanodine receptor isoforms exist in avian striated muscles. Biochemistry 32: 5739-5745, 1993c.
    • (1993) Biochemistry , vol.32 , pp. 5739-5745
    • Airey, J.A.1    Grinsell, M.M.2    Jones, L.R.3    Sutko, J.L.4    Witcher, D.R.5
  • 6
    • 15644383881 scopus 로고    scopus 로고
    • Peptide probe of ryanodine receptor function: Imperatoxin A is a selective activator of skeletal-type ryanodine receptor isoforms
    • Abstract
    • AREVALO, C., LOKUTA, A. J., AND VALDIVIA, H. H.: Peptide probe of ryanodine receptor function: imperatoxin A is a selective activator of skeletal-type ryanodine receptor isoforms. Biophys. J. 70: 123 (Abstract), 1996.
    • (1996) Biophys. J. , vol.70 , pp. 123
    • Arevalo, C.1    Lokuta, A.J.2    Valdivia, H.H.3
  • 9
    • 0028886224 scopus 로고
    • Activation and deactivation of sarcoplasmic reticulum calcium release channels: Molecular dissection of mechanisms via novel semi-synthetic ryanoids
    • BIDASEE, R. K., BESCH, H. R., JR., GERZON, K., AND HUMERICKHOUSE, R. A.: Activation and deactivation of sarcoplasmic reticulum calcium release channels: molecular dissection of mechanisms via novel semi-synthetic ryanoids. Mol. Cell. Biochem. 149/150: 145-159, 1995.
    • (1995) Mol. Cell. Biochem. , vol.149-150 , pp. 145-159
    • Bidasee, R.K.1    Besch Jr., H.R.2    Gerzon, K.3    Humerickhouse, R.A.4
  • 10
    • 0024245148 scopus 로고
    • Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle
    • BLOCK, B. A., IMAGAWA, T., CAMPBELL, K. P., AND 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. 107: 2587-2600, 1988.
    • (1988) J. Cell Biol. , vol.107 , pp. 2587-2600
    • Block, B.A.1    Imagawa, T.2    Campbell, K.P.3    Franzini-Armstrong, C.4
  • 12
    • 0025139194 scopus 로고
    • Molecular interactions of the junctional foot protein and dihydropyridine receptor in skeletal muscle triads
    • BRANDT, N. R., CASWELL, A. H., WEN, S.-R., AND TALVENHEIMO, J. A.: Molecular interactions of the junctional foot protein and dihydropyridine receptor in skeletal muscle triads. J. Membr. Biol. 113: 237-251, 1990.
    • (1990) J. Membr. Biol. , vol.113 , pp. 237-251
    • Brandt, N.R.1    Caswell, A.H.2    Wen, S.-R.3    Talvenheimo, J.A.4
  • 14
    • 0027081874 scopus 로고
    • Ryanodine stabilizes multiple conformational states of the skeletal muscle calcium release channel
    • BUCK, E., ZIMANY, I., ABRAMSON, J. J., AND PESSAH, I. N.: Ryanodine stabilizes multiple conformational states of the skeletal muscle calcium release channel. J. Biol. Chem. 267: 23560-23567, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23560-23567
    • Buck, E.1    Zimany, I.2    Abramson, J.J.3    Pessah, I.N.4
  • 15
    • 0027482905 scopus 로고
    • Sarcoplasmic reticulum release channels from frog skeletal muscle display two types of calcium dependence
    • BULL, R., AND MARENGO, J. J.: Sarcoplasmic reticulum release channels from frog skeletal muscle display two types of calcium dependence. FEBS Lett. 331: 223-227, 1993.
    • (1993) FEBS Lett. , vol.331 , pp. 223-227
    • Bull, R.1    Marengo, J.J.2
  • 18
    • 0028951459 scopus 로고
    • Immunolocalization of sarcolemmal dihydropyridine receptor and sarcoplasmic reticular triadin and ryanodine receptor in rabbit ventricle and atrium
    • CARL, S. L., FELIX, K., CASWELL, A. H., BRANDT, N. R., BALL, W. J., JR., VAGHY, P. L., MEISSNER, G., AND FERGUSON, D. G.: Immunolocalization of sarcolemmal dihydropyridine receptor and sarcoplasmic reticular triadin and ryanodine receptor in rabbit ventricle and atrium. J. Cell Biol. 129: 673-682, 1995.
    • (1995) J. Cell Biol. , vol.129 , pp. 673-682
    • Carl, S.L.1    Felix, K.2    Caswell, A.H.3    Brandt, N.R.4    Ball Jr., W.J.5    Vaghy, P.L.6    Meissner, G.7    Ferguson, D.G.8
  • 20
    • 0004257141 scopus 로고
    • Houghton Mifflin Co., Boston
    • CARSON, R.: Silent Spring, Houghton Mifflin Co., Boston, 1962.
    • (1962) Silent Spring
    • Carson, R.1
  • 21
    • 0025718478 scopus 로고
    • Localization and partial characterization of the oligomeric disulfide-linked molecular weight 95000 protein (triadin) which binds the ryanodine and dihydropyridine receptors in skeletal muscle triadic vesicles
    • CASWELL, A. H., BRANDT, N., BRUNSCHWIG, J.-P., AND PURKERSON, S.: Localization and partial characterization of the oligomeric disulfide-linked molecular weight 95000 protein (triadin) which binds the ryanodine and dihydropyridine receptors in skeletal muscle triadic vesicles. Biochemistry 30: 7507-7513, 1991.
    • (1991) Biochemistry , vol.30 , pp. 7507-7513
    • Caswell, A.H.1    Brandt, N.2    Brunschwig, J.-P.3    Purkerson, S.4
  • 23
    • 12644298942 scopus 로고
    • Calcium sparks: Elementary events underlying excitation-contraction coupling in heart muscle
    • Wash. DC
    • CHENG, H., LEDERER, W. J., AND CANNELL, M. B.: Calcium sparks: elementary events underlying excitation-contraction coupling in heart muscle. Science (Wash. DC) 268: 1045-1049, 1993.
    • (1993) Science , vol.268 , pp. 1045-1049
    • Cheng, H.1    Lederer, W.J.2    Cannell, M.B.3
  • 24
    • 0023219685 scopus 로고
    • Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate
    • CLAPPER, D. L., WALSETH, T. F., DARGIE, P. J., AND LEE H. C.: Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate. J. Biol. Chem. 262: 9561-9568, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9561-9568
    • Clapper, D.L.1    Walseth, T.F.2    Dargie, P.J.3    Lee, H.C.4
  • 25
    • 0029971070 scopus 로고    scopus 로고
    • Differential distribution of ryanodine receptor type 3 (RyR3) gene product in mammalian skeletal muscles
    • CONTI, A., GORZA, L., AND SORRENTINO, V.: Differential distribution of ryanodine receptor type 3 (RyR3) gene product in mammalian skeletal muscles. Biochem. J. 316: 19-23, 1996.
    • (1996) Biochem. J. , vol.316 , pp. 19-23
    • Conti, A.1    Gorza, L.2    Sorrentino, V.3
  • 27
    • 0023751431 scopus 로고
    • Comparative molecular field analysis (CoMFA): 1 - Effect of shape on binding of steroids to carrier proteins
    • CRAMER, R. D., III, PATTERSON, D. E., AND BUNCE, J. D.: Comparative molecular field analysis (CoMFA): 1 - effect of shape on binding of steroids to carrier proteins. J. Am. Chem. Soc. 110: 5959-5967, 1988.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 5959-5967
    • Cramer III, R.D.1    Patterson, D.E.2    Bunce, J.D.3
  • 28
    • 0011232376 scopus 로고
    • Minor insecticides of plant origin
    • ed. by M. Jacobson and D. G. Crosby, Marcel Dekker, Inc., New York
    • CROSBY, D. G.: Minor insecticides of plant origin. In Naturally occurring insecticides, ed. by M. Jacobson and D. G. Crosby, pp. 177-239, Marcel Dekker, Inc., New York, 1971.
    • (1971) Naturally Occurring Insecticides , pp. 177-239
    • Crosby, D.G.1
  • 29
    • 0025384609 scopus 로고
    • 2+ mobilizing activities of cyclic ADP-ribose and inositol trisphosphate
    • 2+ mobilizing activities of cyclic ADP-ribose and inositol trisphosphate. Cell Regul. 1: 279-290, 1990.
    • (1990) Cell Regul. , vol.1 , pp. 279-290
    • Dargie, P.J.1    Agre, M.C.2    Lee, H.C.3
  • 30
    • 0027989511 scopus 로고
    • Fluorescence photooxidation with eosin: A method for high resolution immunolocalization and in situ hybridization detection for light and electron microscopy
    • DEERINCK, T. J., MARTONE, M. E., LEV-RAM. V., GREEN, D. P. L., TSIEN, R. Y., SPECTOR, D. L., HUANG, S., AND ELLISMAN, M. H.: Fluorescence photooxidation with eosin: a method for high resolution immunolocalization and in situ hybridization detection for light and electron microscopy. J. Cell Biol. 126: 901-910, 1994.
    • (1994) J. Cell Biol. , vol.126 , pp. 901-910
    • Deerinck, T.J.1    Martone, M.E.2    Lev-Ram, V.3    Green, D.P.L.4    Tsien, R.Y.5    Spector, D.L.6    Huang, S.7    Ellisman, M.H.8
  • 33
    • 0029961557 scopus 로고    scopus 로고
    • 2+ release channel of sarcoplasmic reticulum
    • 2+ release channel of sarcoplasmic reticulum. Cell Struct. Funct. 21: 7-15, 1996.
    • (1996) Cell Struct. Funct. , vol.21 , pp. 7-15
    • Ding, J.1    Kasai, M.2
  • 34
    • 0026543195 scopus 로고
    • Extra-junctional ryanodine receptors in the terminal cisternae of mammalian skeletal muscle fibers
    • DULHUNTY, A. F., JUNKAR, P. R., AND STANHOPE, C.: Extra-junctional ryanodine receptors in the terminal cisternae of mammalian skeletal muscle fibers. Proc. R. Soc. Lond. B 247: 69-75, 1992.
    • (1992) Proc. R. Soc. Lond. B , vol.247 , pp. 69-75
    • Dulhunty, A.F.1    Junkar, P.R.2    Stanhope, C.3
  • 35
    • 0027475724 scopus 로고
    • The junctional foot protein during development of avian embryonic cardiac muscle
    • DUTRO, S., AIREY, J. A., BECK, C., SUTKO, J. L., AND TRUMBLE, W. R.: The junctional foot protein during development of avian embryonic cardiac muscle. Dev. Biol. 155: 431-441, 1993.
    • (1993) Dev. Biol. , vol.155 , pp. 431-441
    • Dutro, S.1    Airey, J.A.2    Beck, C.3    Sutko, J.L.4    Trumble, W.R.5
  • 36
    • 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, S. L., AND IKEMOTO, N.: Identification of calcium release-triggering and blocking regions of the II-III loop of the skeletal muscle dihydropyridine receptor. J. Biol. Chem. 270: 22116-22118, 1995a.
    • (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
  • 37
    • 0028845859 scopus 로고
    • Peptide probes of ryanodine receptor function. Imperatoxin A, a peptide from the venom of the scorpion, Pandinus imperator, selectively activates skeletal-type ryanodine receptor isoforms
    • EL-HAYEK, R., LOKUTA, A. J., AREVALO, C., AND VALDIVIA, H. H.: Peptide probes of ryanodine receptor function. Imperatoxin A, a peptide from the venom of the scorpion, Pandinus imperator, selectively activates skeletal-type ryanodine receptor isoforms. J. Biol. Chem. 270: 28696-28704, 1995b.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28696-28704
    • El-Hayek, R.1    Lokuta, A.J.2    Arevalo, C.3    Valdivia, H.H.4
  • 38
    • 0028284752 scopus 로고
    • Dual effect of suramin on calcium fluxes across sarcoplasmic reticulum vesicle membranes
    • EMMICK, J. T., KWON, S., BIDASEE, K. R., BESCH, K. T., AND BESCH, H. R., JR.: Dual effect of suramin on calcium fluxes across sarcoplasmic reticulum vesicle membranes. J. Pharmacol. Exp. Ther. 269: 717-724, 1994.
    • (1994) J. Pharmacol. Exp. Ther. , vol.269 , pp. 717-724
    • Emmick, J.T.1    Kwon, S.2    Bidasee, K.R.3    Besch, K.T.4    Besch Jr., H.R.5
  • 41
    • 0022330268 scopus 로고
    • Effects of ryanodine in skinned cardiac cells
    • FABIATO, A.: Effects of ryanodine in skinned cardiac cells. Fed. Proc. 44: 2970-2976, 1985.
    • (1985) Fed. Proc. , vol.44 , pp. 2970-2976
    • Fabiato, A.1
  • 42
    • 84986706442 scopus 로고
    • The preparation of tritium labelled ryanodine
    • FAIRHURST, A. S.: The preparation of tritium labelled ryanodine. J. Labelled Compd. 7: 133-136, 1971.
    • (1971) J. Labelled Compd. , vol.7 , pp. 133-136
    • Fairhurst, A.S.1
  • 43
    • 0016287809 scopus 로고
    • A ryanodine-caffeine-sensitive membrane fraction of skeletal muscle
    • FAIRHURST, A. S.: A ryanodine-caffeine-sensitive membrane fraction of skeletal muscle. Am. J. Physiol. 227: 1124-1131, 1974.
    • (1974) Am. J. Physiol. , vol.227 , pp. 1124-1131
    • Fairhurst, A.S.1
  • 44
    • 0014770764 scopus 로고
    • Calcium efflux from a heavy sarcotubular fraction: Effects of ryanodine, caffeine and magnesium
    • FAIRHURST, A. S., AND HASSELBACH, A. S.: Calcium efflux from a heavy sarcotubular fraction: effects of ryanodine, caffeine and magnesium. Eur. J. Bio-chem. 13: 504-509, 1970.
    • (1970) Eur. J. Bio-chem. , vol.13 , pp. 504-509
    • Fairhurst, A.S.1    Hasselbach, A.S.2
  • 45
    • 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 82: 7256-7259, 1985.
    • (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.M.4
  • 46
    • 85006142608 scopus 로고
    • Studies of the triad: I - Structure of the junction in frog twitch fibers
    • FBANZINI-ARMSTRONG, C.: Studies of the triad: I - structure of the junction in frog twitch fibers. J. Cell Biol. 47: 488-499, 1970.
    • (1970) J. Cell Biol. , vol.47 , pp. 488-499
    • Fbanzini-Armstrong, C.1
  • 47
    • 0015447824 scopus 로고
    • Studies of the triad: III - Structure of the junction in fast twitch fibers
    • FRANZINI-ARMSTRONG, C.: Studies of the triad: III - structure of the junction in fast twitch fibers. Tissue Cell 4: 469-478, 1972.
    • (1972) Tissue Cell , vol.4 , pp. 469-478
    • Franzini-Armstrong, C.1
  • 48
    • 0016652070 scopus 로고
    • Membrane particles and transmission at the triad
    • FRANZINI-ARMSTRONG, C.: Membrane particles and transmission at the triad. Fed. Proc. 34: 1382-1388, 1975.
    • (1975) Fed. Proc. , vol.34 , pp. 1382-1388
    • Franzini-Armstrong, C.1
  • 49
    • 0028349030 scopus 로고
    • Structure and development of E-C coupling units in skeletal muscle
    • FRANZINI-ARMSTRONG, C., AND JORGENSEN, A. O.: Structure and development of E-C coupling units in skeletal muscle. Ann. Rev. Physiol. 56: 509-534, 1994.
    • (1994) Ann. Rev. Physiol. , vol.56 , pp. 509-534
    • Franzini-Armstrong, C.1    Jorgensen, A.O.2
  • 50
    • 0028018016 scopus 로고
    • Cyclic ADP-ribose does not affect cardiac or skeletal muscle ryanodine receptors
    • FRUEN, B. R., MICKELSON, J. R., SHOMER, N. H., VELEZ, P., AND LOUIS, C. F.: Cyclic ADP-ribose does not affect cardiac or skeletal muscle ryanodine receptors. FEBS Lett. 352: 123-126, 1994.
    • (1994) FEBS Lett. , vol.352 , pp. 123-126
    • Fruen, B.R.1    Mickelson, J.R.2    Shomer, N.H.3    Velez, P.4    Louis, C.F.5
  • 52
    • 0028813820 scopus 로고
    • Tissue-specific and developmentally regulated alternative splicing in mouse skeletal ryanodine receptor mRNA
    • FUTATSUGI, A., KUWAJIMA, G., AND MIKOSHIBA, K.: Tissue-specific and developmentally regulated alternative splicing in mouse skeletal ryanodine receptor mRNA. Biochem. J. 305: 373-378, 1995.
    • (1995) Biochem. J. , vol.305 , pp. 373-378
    • Futatsugi, A.1    Kuwajima, G.2    Mikoshiba, K.3
  • 56
    • 0028925223 scopus 로고
    • The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues
    • GIANNINI, G., CONTI, A., MAMMARELLA, S., SCROBOGNA, M., AND SORRENTINO, V.: The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues. J. Cell Biol. 128: 893-904, 1995.
    • (1995) J. Cell Biol. , vol.128 , pp. 893-904
    • Giannini, G.1    Conti, A.2    Mammarella, S.3    Scrobogna, M.4    Sorrentino, V.5
  • 58
    • 0028906807 scopus 로고
    • Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum
    • GUO, W., AND CAMPBELL, K. P.: Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum. J. Biol. Chem. 270: 9027-9030, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9027-9030
    • Guo, W.1    Campbell, K.P.2
  • 59
    • 0028051807 scopus 로고
    • Characterization and ultrastructural localization of a novel 90-kDa protein unique to skeletal muscle junctional sarcoplasmic reticulum
    • GUO, W., JORGENSEN, A. O., AND CAMPBELL, K. P.: Characterization and ultrastructural localization of a novel 90-kDa protein unique to skeletal muscle junctional sarcoplasmic reticulum. J. Biol. Chem. 269: 28359-28365, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28359-28365
    • Guo, W.1    Jorgensen, A.O.2    Campbell, K.P.3
  • 61
    • 0026471048 scopus 로고
    • Primary structure and distribution of a novel ryanodine receptor/calcium release channel from rabbit brain
    • HAKAMATA, Y., NAKAI, J., TAKESHIMA, H., AND IMOTO, K.: Primary structure and distribution of a novel ryanodine receptor/calcium release channel from rabbit brain. FEBS Lett. 312: 229-235, 1992.
    • (1992) FEBS Lett. , vol.312 , pp. 229-235
    • Hakamata, Y.1    Nakai, J.2    Takeshima, H.3    Imoto, K.4
  • 62
    • 0027097029 scopus 로고
    • 2+-release channels: Identification and expression patterns of the inositol 1,4,5-trisphosphate and the ryanodine receptor genes
    • 2+-release channels: identification and expression patterns of the inositol 1,4,5-trisphosphate and the ryanodine receptor genes. Development 116: 967-975, 1992.
    • (1992) Development , vol.116 , pp. 967-975
    • Hasan, G.1    Rosbach, M.2
  • 64
    • 0022527248 scopus 로고
    • Extracellular calcium transients and action potential configuration changes related to post-stimulatory potentiation in rabbit atrium
    • HILGEMANN, D. W.: Extracellular calcium transients and action potential configuration changes related to post-stimulatory potentiation in rabbit atrium. J. Gen. Physiol. 87: 675-706, 1986.
    • (1986) J. Gen. Physiol. , vol.87 , pp. 675-706
    • Hilgemann, D.W.1
  • 65
    • 0021085353 scopus 로고
    • Activation-related cumulative depletions of free extracellular calcium in guinea pig atrium measured with Antipyrylazo III and tetramethylmurexide
    • HILGEMANN, D. W., DELAY, M., AND LANGER, G. A.: Activation-related cumulative depletions of free extracellular calcium in guinea pig atrium measured with Antipyrylazo III and tetramethylmurexide. Circ. Res. 53: 779-793, 1983.
    • (1983) Circ. Res. , vol.53 , pp. 779-793
    • Hilgemann, D.W.1    Delay, M.2    Langer, G.A.3
  • 66
    • 0027234769 scopus 로고
    • Differential activating and deactivating effects among natural ryanodine congeners on calcium release channels of sarcoplasmic reticulum: Evidence for separation of effects at functionally distinct sites
    • HUMERICKHOUSE, R. A., BESCH, H. R., JR., GERZON, K., RUEST, L., SUTKO, J. L., AND EMMICK, J. T.: Differential activating and deactivating effects among natural ryanodine congeners on calcium release channels of sarcoplasmic reticulum: evidence for separation of effects at functionally distinct sites. Mol. Pharmacol. 44: 412-421, 1993.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 412-421
    • Humerickhouse, R.A.1    Besch Jr., H.R.2    Gerzon, K.3    Ruest, L.4    Sutko, J.L.5    Emmick, J.T.6
  • 68
    • 0002254610 scopus 로고
    • Atypical pharmacology of commercial ryanodine: Characterization of novel Ryania constituents
    • Abstract
    • HUMERICKHOUSE, R. A., PASCHAL, J., ELVEY, T., BERRY, D., AND BESCH, H. R., JR.: Atypical pharmacology of commercial ryanodine: characterization of novel Ryania constituents. Pharmacologist 31: 185 (Abstract), 1989.
    • (1989) Pharmacologist , vol.31 , pp. 185
    • Humerickhouse, R.A.1    Paschal, J.2    Elvey, T.3    Berry, D.4    Besch Jr., H.R.5
  • 69
    • 0029085592 scopus 로고
    • 2+ release in the sarcoplasmic reticulum of rabbit skeletal muscle fibres
    • Lond.
    • 2+ release in the sarcoplasmic reticulum of rabbit skeletal muscle fibres. J. Physiol. (Lond.) 487: 3:573-582, 1995.
    • (1995) J. Physiol. , vol.487 , Issue.3 , pp. 573-582
    • Ikemoto, T.1    Iino, M.2    Endo, M.3
  • 71
    • 0023644484 scopus 로고
    • Purification of the RyR and identity with feet structures of junctional terminal cisternae of SR from fast skeletal muscle
    • INUI, M., SAITO, A., AND FLEISCHER, S.: Purification of the RyR and identity with feet structures of junctional terminal cisternae of SR from fast skeletal muscle. J. Biol. Chem. 262: 1740-1747, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1740-1747
    • Inui, M.1    Saito, A.2    Fleischer, S.3
  • 72
    • 85044012922 scopus 로고
    • Isolation of the ryanodine receptor from cardiac sarcoplasmic reticulum and identity with the feet structures
    • INUI, M., SAITO, A., AND FLEISCHER, S.: Isolation of the ryanodine receptor from cardiac sarcoplasmic reticulum and identity with the feet structures. J. Biol. Chem. 262: 15637-15642, 1988.
    • (1988) J. Biol. Chem. , vol.262 , pp. 15637-15642
    • Inui, M.1    Saito, A.2    Fleischer, S.3
  • 73
    • 0028926924 scopus 로고
    • Embryonic chicken skeletal muscle cells fail to develop normal excitation-contraction coupling in the absence of the β ryanodine receptor: Implications for a two-ryanodine receptor system
    • IVANENKO, A., MCKEMY, D. D., KENYON, J. L., AIREY, J. A., AND SUTKO, J. L.: Embryonic chicken skeletal muscle cells fail to develop normal excitation-contraction coupling in the absence of the β ryanodine receptor: implications for a two-ryanodine receptor system. J. Biol. Chem. 270: 4220-4223, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4220-4223
    • Ivanenko, A.1    Mckemy, D.D.2    Kenyon, J.L.3    Airey, J.A.4    Sutko, J.L.5
  • 75
    • 0029898988 scopus 로고    scopus 로고
    • Ryanodine action at calcium release channels 1. Importance of hydroxyl substituents
    • JEFFERIES, P. R., BLUMENKOPF, T. A., GENGO, P. J., COLE, L. C., AND CASIDA, J. E.: Ryanodine action at calcium release channels 1. Importance of hydroxyl substituents. J. Med. Chem. 39: 2331-2338, 1996a.
    • (1996) J. Med. Chem. , vol.39 , pp. 2331-2338
    • Jefferies, P.R.1    Blumenkopf, T.A.2    Gengo, P.J.3    Cole, L.C.4    Casida, J.E.5
  • 76
    • 2742611216 scopus 로고
    • Ryanoid chemistry and action
    • ed. by P. A. Hedin, J. J. Menn, and R. M. Hollingworth, Am. Chem. Soc. Symp. Ser. No. 551, Am. Chem. Soc., Wash. DC
    • JEFFERIES, P. R., AND CASIDA, J. E.: Ryanoid chemistry and action. In Natural and Engineered Pest Management Agents, ed. by P. A. Hedin, J. J. Menn, and R. M. Hollingworth, pp. 130-144, Am. Chem. Soc. Symp. Ser. No. 551, Am. Chem. Soc., Wash. DC, 1994.
    • (1994) Natural and Engineered Pest Management Agents , pp. 130-144
    • Jefferies, P.R.1    Casida, J.E.2
  • 77
    • 0029995522 scopus 로고    scopus 로고
    • Ryanodine action at calcium release channels 2. Relations to substituents of the cylohexane ring
    • JEFFERIES, P. R., GENGO, P. J., WATSON, M. J., AND CASIDA, J. E.: Ryanodine action at calcium release channels 2. Relations to substituents of the cylohexane ring. J. Med. Chem. 39: 2339-2346, 1996b.
    • (1996) J. Med. Chem. , vol.39 , pp. 2339-2346
    • Jefferies, P.R.1    Gengo, P.J.2    Watson, M.J.3    Casida, J.E.4
  • 79
    • 0027299017 scopus 로고
    • Ryanoids from nucleophilic additions to 4,12-seco-4,12-dioxoryanodine
    • JEFFERIES, P. R., LERMBERG, E., LAM, W.-W., AND CASIDA, J. E.: Ryanoids from nucleophilic additions to 4,12-seco-4,12-dioxoryanodine. J. Med. Chem. 36: 1128-1135, 1993.
    • (1993) J. Med. Chem. , vol.36 , pp. 1128-1135
    • Jefferies, P.R.1    Lermberg, E.2    Lam, W.-W.3    Casida, J.E.4
  • 81
    • 0025812873 scopus 로고
    • Ryanodyl 3-(pyridine-3-carboxylate): A novel ryanoid from Ryania insecticide
    • Lloydia
    • JEFFERIES, P. R., TOIA, R. F., AND CASIDA, J. E.: Ryanodyl 3-(pyridine-3-carboxylate): a novel ryanoid from Ryania insecticide. J. Nat. Prod. (Lloydia) 54: 1147-1149, 1991.
    • (1991) J. Nat. Prod. , vol.54 , pp. 1147-1149
    • Jefferies, P.R.1    Toia, R.F.2    Casida, J.E.3
  • 83
    • 10244247967 scopus 로고
    • Evidence for the presence of a novel skeletal-like ryanodine receptor (RyR) isoform in striated muscles of fish
    • Abstract
    • JENS, F. P. C., KEEN, J. E., LONDRAVILLE, R. L., BEAMSLEY, M. B., AND BLOCK, B. A.: Evidence for the presence of a novel skeletal-like ryanodine receptor (RyR) isoform in striated muscles of fish. Biophys. J. 68: 50 (Abstract), 1995.
    • (1995) Biophys. J. , vol.68 , pp. 50
    • Jens, F.P.C.1    Keen, J.E.2    Londraville, R.L.3    Beamsley, M.B.4    Block, B.A.5
  • 84
    • 0015576211 scopus 로고
    • Chicken cardiac muscle: Its elusive extended junctional sarcoplasmic reticulum and sarcoplasmic reticulum fenestrations
    • JEWETT, P. H., LEONARD, S. D., AND SOMMER, J. R.: Chicken cardiac muscle: its elusive extended junctional sarcoplasmic reticulum and sarcoplasmic reticulum fenestrations. J. Cell Biol. 56: 595-600, 1973.
    • (1973) J. Cell Biol. , vol.56 , pp. 595-600
    • Jewett, P.H.1    Leonard, S.D.2    Sommer, J.R.3
  • 86
    • 0027339572 scopus 로고
    • 2+-release channel/ryanodine receptor is localized in junctional and corbular sarcoplasmic reticulum in cardiac muscle
    • 2+-release channel/ryanodine receptor is localized in junctional and corbular sarcoplasmic reticulum in cardiac muscle. J. Cell Biol. 120: 969-980, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 969-980
    • Jorgensen, A.O.1    Shen, A.C.2    Arnold, W.3    Mcpherson, P.S.4    Campbell, K.P.5
  • 88
    • 37049100604 scopus 로고
    • An infrared study of the conformations and association of pyrrole-2-carbaldehydes and pyrrole-2-carboxylates
    • KAYE, P. T., MACRAE, R., MEAKINS, G. D., AND PATTERSON, C. H.: An infrared study of the conformations and association of pyrrole-2-carbaldehydes and pyrrole-2-carboxylates. J. Chem. Soc., Perkin Trans. II: 1631-1635, 1980.
    • (1980) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 1631-1635
    • Kaye, P.T.1    Macrae, R.2    Meakins, G.D.3    Patterson, C.H.4
  • 90
    • 0026292147 scopus 로고
    • HINT: A new method of empirical hydrophobic field calculation of CoMFA
    • KELLOGG, G. E., SEMUS, S. F., AND ABRAHAM, D. J.: HINT: a new method of empirical hydrophobic field calculation of CoMFA. J. Comput. Aided MoI. Design 5: 545-552, 1991.
    • (1991) J. Comput. Aided MoI. Design , vol.5 , pp. 545-552
    • Kellogg, G.E.1    Semus, S.F.2    Abraham, D.J.3
  • 91
    • 0024992021 scopus 로고
    • Isolation of terminal cisterna protein which may link the dihydropyridine receptor to the junctional foot protein in skeletal muscle
    • KIM, K. C., CASWELL, A. H., TALVENHEIMO, J. A., AND BRANDT, N. R.: Isolation of terminal cisterna protein which may link the dihydropyridine receptor to the junctional foot protein in skeletal muscle. Biochemistry 29: 9281-9289, 1990.
    • (1990) Biochemistry , vol.29 , pp. 9281-9289
    • Kim, K.C.1    Caswell, A.H.2    Talvenheimo, J.A.3    Brandt, N.R.4
  • 92
    • 0025816211 scopus 로고
    • Direct prediction of dissociation constants (pKa's) of clonidine-like imidazolines, 2-substituted imidazoles, and 1-methyl-2-substituted-imidazoles from 3D structures using a comparative molecular field analysis (CoMFA) approach
    • KIM, K. H., AND MARTIN, Y. C.: Direct prediction of dissociation constants (pKa's) of clonidine-like imidazolines, 2-substituted imidazoles, and 1-methyl-2-substituted-imidazoles from 3D structures using a comparative molecular field analysis (CoMFA) approach. J. Med. Chem. 34: 2056-2060, 1991.
    • (1991) J. Med. Chem. , vol.34 , pp. 2056-2060
    • Kim, K.H.1    Martin, Y.C.2
  • 93
    • 7344247143 scopus 로고
    • Ryanodine sensitivity and multiple conductance states of the Ca release channel from native SR membrane
    • Abstract
    • KWOK, W. M., AND BEST, P. M.: Ryanodine sensitivity and multiple conductance states of the Ca release channel from native SR membrane. Biophys. J. 67: 168(Abstract), 1990.
    • (1990) Biophys. J. , vol.67 , pp. 168
    • Kwok, W.M.1    Best, P.M.2
  • 96
    • 0024474146 scopus 로고
    • 2+ release channel complex of skeletal muscle sarcoplasmic reticulum: Evidence for a cooperatively coupled, negatively charged homotetramer
    • 2+ release channel complex of skeletal muscle sarcoplasmic reticulum: evidence for a cooperatively coupled, negatively charged homotetramer. J. Biol. Chem. 264: 16776-16785, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16776-16785
    • Lai, F.A.1    Misra, M.2    Xu, L.3    Smith, H.A.4    Meissner, G.5
  • 97
    • 0023196593 scopus 로고
    • The effects of ryanodine on passive calcium fluxes across sarcoplasmic reticulum membranes
    • LATTANZIO, F. A., JR., SCHLATTERER, R. G., NICAR, M., CAMPBELL, K. P., AND SUTKO, J. L.: The effects of ryanodine on passive calcium fluxes across sarcoplasmic reticulum membranes. J. Biol. Chem. 262: 2711-2718, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2711-2718
    • Lattanzio Jr., F.A.1    Schlatterer, R.G.2    Nicar, M.3    Campbell, K.P.4    Sutko, J.L.5
  • 98
    • 0027999930 scopus 로고
    • Tissue distribution of ryanodine receptor isoforms and alleles determined by reverse transcription polymerase chain reaction
    • LEDBETTER, M. W., PREINER, J. K., LOUIS, C. F., AND MICKELSON, J. R.: Tissue distribution of ryanodine receptor isoforms and alleles determined by reverse transcription polymerase chain reaction. J. Biol. Chem. 269: 31544-31551, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31544-31551
    • Ledbetter, M.W.1    Preiner, J.K.2    Louis, C.F.3    Mickelson, J.R.4
  • 99
    • 0029706922 scopus 로고    scopus 로고
    • Modulator and messenger functions of cycle ADP-ribose in calcium signaling
    • LEE, H. C.: Modulator and messenger functions of cycle ADP-ribose in calcium signaling. Recent Prog. Horm. Res. 51: 355-388, 1996.
    • (1996) Recent Prog. Horm. Res. , vol.51 , pp. 355-388
    • Lee, H.C.1
  • 100
    • 0028798088 scopus 로고
    • Ryanodine-induced calcium release from hepatic microsomes and permeabilized hepatocytes
    • LILLY, L. B., AND GOLLAN, J. L.: Ryanodine-induced calcium release from hepatic microsomes and permeabilized hepatocytes. Am. J. Physiol. 268: G1017-G1024, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Lilly, L.B.1    Gollan, J.L.2
  • 101
    • 0024519673 scopus 로고
    • Multiple conductance states of the purified calcium release channel complex from skeletal sarcoplasmic reticulum
    • LIU, Q.-Y., LAI, F. A., ROUSSEAU, E., JONES, R. V., AND MEISSNER, G.: Multiple conductance states of the purified calcium release channel complex from skeletal sarcoplasmic reticulum. Biophys. J. 55: 415-424, 1989.
    • (1989) Biophys. J. , vol.55 , pp. 415-424
    • Liu, Q.-Y.1    Lai, F.A.2    Rousseau, E.3    Jones, R.V.4    Meissner, G.5
  • 102
    • 0028063866 scopus 로고
    • Potentiation by metal ions of ryanodine contracture of the mouse diaphragm
    • LIU, S. H., AND LIN-SHIAU, S. Y.: Potentiation by metal ions of ryanodine contracture of the mouse diaphragm. Eur. J. Pharmacol. 251: 61-68, 1994.
    • (1994) Eur. J. Pharmacol. , vol.251 , pp. 61-68
    • Liu, S.H.1    Lin-Shiau, S.Y.2
  • 103
    • 0028031728 scopus 로고
    • Direct evidence for the existence and functional role of hyperreactive sulfhydryls on the ryanodine receptor-triadin complex selectively labeled by the coumarin maleimide 7-diethylamino-3-(4′-maleimidylphenyl)-4-methylcoumarin
    • LIU, G., ABRAMSON, J. J., ZABLE, A. C., AND PESSAH, I. N.: Direct evidence for the existence and functional role of hyperreactive sulfhydryls on the ryanodine receptor-triadin complex selectively labeled by the coumarin maleimide 7-diethylamino-3-(4′-maleimidylphenyl)-4-methylcoumarin. Mol. Pharmacol. 45: 189-200, 1994.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 189-200
    • Liu, G.1    Abramson, J.J.2    Zable, A.C.3    Pessah, I.N.4
  • 104
    • 0028567151 scopus 로고
    • Molecular interaction between ryanodine receptor and glycoprotein triadin involves redox cycling of functionally important hyperreactive sulfhydryls
    • LIU, G., AND PESSAH, I. N.: Molecular interaction between ryanodine receptor and glycoprotein triadin involves redox cycling of functionally important hyperreactive sulfhydryls. J. Biol. Chem. 269: 33028-33034, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 33028-33034
    • Liu, G.1    Pessah, I.N.2
  • 105
    • 0028352089 scopus 로고
    • Activation of the skeletal muscle calcium release channel by a cytoplasmic loop of the dihydropyridine receptor
    • LU, X., XU, L., AND MEISSNER, G.: Activation of the skeletal muscle calcium release channel by a cytoplasmic loop of the dihydropyridine receptor. J. Biol. Chem. 269: 6511-6515, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6511-6515
    • Lu, X.1    Xu, L.2    Meissner, G.3
  • 106
    • 0029150193 scopus 로고
    • Phosphorylation of dihydropyridine receptor II-III loop peptide regulates skeletal muscle calcium release channel function: Evidence for an essential role of the β-OH group of Ser687
    • LU, X., XU, L., AND MEISSNER, G.: Phosphorylation of dihydropyridine receptor II-III loop peptide regulates skeletal muscle calcium release channel function: evidence for an essential role of the β-OH group of Ser687. J. Biol. Chem. 270: 18459-18464, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18459-18464
    • Lu, X.1    Xu, L.2    Meissner, G.3
  • 107
    • 0024580990 scopus 로고
    • Positive cooperativity of ryanodine binding to the calcium release channel of sarcoplasmic reticulum from heart and skeletal muscle
    • MCGREW, S. G., WOLLEBEN, C., SIEGEL, P., INUI, M., AND FLEISCHER, S.: Positive cooperativity of ryanodine binding to the calcium release channel of sarcoplasmic reticulum from heart and skeletal muscle. Biochemistry 28: 1686-1691, 1989.
    • (1989) Biochemistry , vol.28 , pp. 1686-1691
    • Mcgrew, S.G.1    Wolleben, C.2    Siegel, P.3    Inui, M.4    Fleischer, S.5
  • 109
    • 0028788944 scopus 로고
    • Rectification of skeletal muscle ryanodine receptor mediated by FK506 binding protein
    • MA, J., BHAT, M. B., AND ZHAO, J.: Rectification of skeletal muscle ryanodine receptor mediated by FK506 binding protein. Biophys. J. 69: 2398-2404, 1995.
    • (1995) Biophys. J. , vol.69 , pp. 2398-2404
    • Ma, J.1    Bhat, M.B.2    Zhao, J.3
  • 110
    • 0028100737 scopus 로고
    • Novel modulators of skeletal muscle FKBP12/calcium channel complex from Ianthella basta. Role of FKBP12 in channel gating
    • MACK, M. M., MOLINSKI, T. F., BUCK, E. D., AND PESSAH, I. N.: Novel modulators of skeletal muscle FKBP12/calcium channel complex from Ianthella basta. Role of FKBP12 in channel gating. J. Biol. Chem. 269: 23236-23249, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23236-23249
    • Mack, M.M.1    Molinski, T.F.2    Buck, E.D.3    Pessah, I.N.4
  • 112
    • 0024372718 scopus 로고
    • Molecular cloning and characterization of the ryanodine receptor/junctional channel complex cDNA from skeletal muscle sarcoplasmic reticulum
    • MARKS, A. R., TEMPST, P., HWANG, K. S., TAUBMAN, M. B., INUI, M., CHADWICK, C., FLEISCHER, S., AND NADAL-GINARD, B.: Molecular cloning and characterization of the ryanodine receptor/junctional channel complex cDNA from skeletal muscle sarcoplasmic reticulum. Proc. Natl. Acad. Sci USA 86: 8683-8687, 1989.
    • (1989) Proc. Natl. Acad. Sci USA , vol.86 , pp. 8683-8687
    • Marks, A.R.1    Tempst, P.2    Hwang, K.S.3    Taubman, M.B.4    Inui, M.5    Chadwick, C.6    Fleischer, S.7    Nadal-Ginard, B.8
  • 113
    • 0023008143 scopus 로고
    • 2+ release channel of sarcoplasmic reticulum
    • 2+ release channel of sarcoplasmic reticulum. J. Biol. Chem. 261: 6300-6306, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6300-6306
    • Meissner, G.1
  • 114
    • 0028180422 scopus 로고
    • 2+ release channels and their regulation by endogenous effectors
    • 2+ release channels and their regulation by endogenous effectors. Annu. Rev. Physiol. 56: 484-508, 1994.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 484-508
    • Meissner, G.1
  • 118
    • 0024449839 scopus 로고
    • Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor
    • MIGNERY, G. A., SÜDHOF, T. C., TAKEI, K., AND DECAMILLI, P.: Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor. Nature (Lond.) 342: 192-195, 1989.
    • (1989) Nature (Lond.) , vol.342 , pp. 192-195
    • Mignery, G.A.1    Südhof, T.C.2    Takei, K.3    Decamilli, P.4
  • 119
    • 15644380763 scopus 로고    scopus 로고
    • The structural determinants for ryanodine binding are different than the molecular features which correlate to channel activation
    • Abstract
    • MITCHELL, K. E., VELASCO, J., RUEST, L., SUTKO, J. L., AND WELCH, W. H.: The structural determinants for ryanodine binding are different than the molecular features which correlate to channel activation. Biophys. J. 70: 388 (Abstract), 1996.
    • (1996) Biophys. J. , vol.70 , pp. 388
    • Mitchell, K.E.1    Velasco, J.2    Ruest, L.3    Sutko, J.L.4    Welch, W.H.5
  • 120
    • 0029738508 scopus 로고    scopus 로고
    • Purification and characterization of ryanotoxin, a peptide with actions similar to those of ryanodine
    • MORRISSETTE, J., BEURG, M., SUKHAREVA, M., AND CORONADO, R.: Purification and characterization of ryanotoxin, a peptide with actions similar to those of ryanodine. Biophys. J. 71: 707-721, 1996.
    • (1996) Biophys. J. , vol.71 , pp. 707-721
    • Morrissette, J.1    Beurg, M.2    Sukhareva, M.3    Coronado, R.4
  • 122
    • 0026437813 scopus 로고
    • Purification and characterization of two ryanodine-binding protein isoforms from sarcoplasmic reticulum of bullfrog skeletal muscle
    • MURAYAMA, T., AND OGAWA, Y.: Purification and characterization of two ryanodine-binding protein isoforms from sarcoplasmic reticulum of bullfrog skeletal muscle. J. Biochem. 112: 514-522, 1992.
    • (1992) J. Biochem. , vol.112 , pp. 514-522
    • Murayama, T.1    Ogawa, Y.2
  • 123
    • 0025835204 scopus 로고
    • The subtypes of the mouse inositol 1,4,5-trisphosphate receptor are expressed in a tissue-specific and developmentally specific manner
    • NAKAGAWA, T., OKANO, H., FURUICHI, T., AND ARUGA, J.: The subtypes of the mouse inositol 1,4,5-trisphosphate receptor are expressed in a tissue-specific and developmentally specific manner. Proc. Natl. Acad. Sci. USA 88: 6244-6248, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6244-6248
    • Nakagawa, T.1    Okano, H.2    Furuichi, T.3    Aruga, J.4
  • 124
    • 0029983398 scopus 로고    scopus 로고
    • Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor
    • NAKAI, J., DIRKSEN, R. T., NGUYEN, H. T., PESSAH, I. N., BEAM, K. G., AND ALLEN, P. D.: Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor. Nature (Lond.) 380: 72-75, 1996.
    • (1996) Nature (Lond.) , 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
  • 125
    • 0025123804 scopus 로고
    • Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel
    • NAKAI, J., IMAGAWA, T., HAKAMATA, Y., SHIGEKAWA, M., TAKESHIMA, H., AND NUMA, S.: Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel. FEBS Lett. 271: 169-177, 1990.
    • (1990) FEBS Lett. , vol.271 , pp. 169-177
    • Nakai, J.1    Imagawa, T.2    Hakamata, Y.3    Shigekawa, M.4    Takeshima, H.5    Numa, S.6
  • 126
    • 84985520823 scopus 로고
    • Simple method for the esterification of carboxylic acids
    • NEISES, B., AND STEGLICH, W.: Simple method for the esterification of carboxylic acids. Angew. Chem., Int., Ed. Engl. 117: 522, 1978.
    • (1978) Angew. Chem., Int., Ed. Engl. , vol.117 , pp. 522
    • Neises, B.1    Steglich, W.2
  • 128
    • 0027136257 scopus 로고
    • The fastest contracting muscles of nonmammalian vertebrates express only one isoform of the ryanodine receptor
    • O'BRIAN, J., MEISSNER, G., AND BLOCK, B. A.: The fastest contracting muscles of nonmammalian vertebrates express only one isoform of the ryanodine receptor. Biophys. J. 65: 2418-2427, 1993.
    • (1993) Biophys. J. , vol.65 , pp. 2418-2427
    • O'Brian, J.1    Meissner, G.2    Block, B.A.3
  • 129
    • 0028814907 scopus 로고
    • Physiological differences between the α and β ryanodine receptors of fish skeletal muscle
    • O'BRIAN, J., VALDIVIA, H. H., AND BLOCK, B. A.: Physiological differences between the α and β ryanodine receptors of fish skeletal muscle. Biophys. J. 68: 471-482, 1995.
    • (1995) Biophys. J. , vol.68 , pp. 471-482
    • O'Brian, J.1    Valdivia, H.H.2    Block, B.A.3
  • 130
  • 131
    • 0027676470 scopus 로고
    • Properties of the ryanodine receptor present in the sarcoplasmic reticulum from lobster skeletal muscle
    • OLIVARES, E., ARISPE, N., AND ROJAS, E.: Properties of the ryanodine receptor present in the sarcoplasmic reticulum from lobster skeletal muscle. Memb. Biochem. 10: 221-235, 1993.
    • (1993) Memb. Biochem. , vol.10 , pp. 221-235
    • Olivares, E.1    Arispe, N.2    Rojas, E.3
  • 135
    • 0029923335 scopus 로고    scopus 로고
    • α and β isoforms of ryanodine receptor from chicken muscle are homologues of mammalian RyR1 and RyR3
    • OTTINI, L., MARZIALI, G., CONTI, A., CHARLESWORTH, A., AND SORRENTINO, V.: α and β isoforms of ryanodine receptor from chicken muscle are homologues of mammalian RyR1 and RyR3. Biochem. J. 315: 207-216, 1996.
    • (1996) Biochem. J. , vol.315 , pp. 207-216
    • Ottini, L.1    Marziali, G.2    Conti, A.3    Charlesworth, A.4    Sorrentino, V.5
  • 136
    • 0028332825 scopus 로고
    • Primary structure and distribution of ryanodine-binding protein isoforms of the bullfrog skeletal muscle
    • OYAMADA, H., MURAYAMA, T., TAKAGI, T., IINO, M., IWABE, N., MIYATA, T., OGAWA, Y., AND ENDO, M.: Primary structure and distribution of ryanodine-binding protein isoforms of the bullfrog skeletal muscle. J. Biol. Chem. 269: 17206-17214, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17206-17214
    • Oyamada, H.1    Murayama, T.2    Takagi, T.3    Iino, M.4    Iwabe, N.5    Miyata, T.6    Ogawa, Y.7    Endo, M.8
  • 138
    • 84873487936 scopus 로고
    • Chemical effectors of the ryanodine receptor: A novel strategy for insect control
    • ed. L. Crombie, Royal Soc. of Chem., London
    • PESSAH, I. N.: Chemical effectors of the ryanodine receptor: A novel strategy for insect control. In Recent advances in the chemistry of insect control, II, ed. L. Crombie, pp. 278-296, Royal Soc. of Chem., London, 1990.
    • (1990) Recent Advances in the Chemistry of Insect Control , vol.2 , pp. 278-296
    • Pessah, I.N.1
  • 139
    • 0022395442 scopus 로고
    • The calcium-ryanodine receptor complex of skeletal and cardiac muscle
    • PESSAH, I. N., WATERHOUSE, A. L., AND CASIDA, J. E.: The calcium-ryanodine receptor complex of skeletal and cardiac muscle. Biochem. Biophys. Res. Comm. 128: 449-456, 1985.
    • (1985) Biochem. Biophys. Res. Comm. , vol.128 , pp. 449-456
    • Pessah, I.N.1    Waterhouse, A.L.2    Casida, J.E.3
  • 140
    • 0025922079 scopus 로고
    • 2+ release channel of sarcoplasmic reticulum from skeletal and cardiac muscle: Evidence for a sequential mechanism in ryanodine action
    • 2+ release channel of sarcoplasmic reticulum from skeletal and cardiac muscle: Evidence for a sequential mechanism in ryanodine action. Mol. Pharmacol. 39: 679-689, 1991.
    • (1991) Mol. Pharmacol. , vol.39 , pp. 679-689
    • Pessah, I.N.1    Zimanyi, I.2
  • 141
    • 84960958070 scopus 로고
    • The action of ryanodine on mammalian skeletal muscle in situ
    • PROCITA, L.: The action of ryanodine on mammalian skeletal muscle in situ. J. Pharmacol. Exp. Ther. 117: 363-373, 1956.
    • (1956) J. Pharmacol. Exp. Ther. , vol.117 , pp. 363-373
    • Procita, L.1
  • 142
    • 0028004249 scopus 로고
    • Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle
    • RADERMACHER, M., RAO, V., GRASSUCCI, R., FRANK, J. TIMERMAN, A. P., FLEISCHER, S., AND WAGENKNECHT, T.: Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle. J. Cell Biol. 127: 411-423, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 411-423
    • Radermacher, M.1    Rao, V.2    Grassucci, R.3    Frank, J.4    Timerman, A.P.5    Fleischer, S.6    Wagenknecht, T.7
  • 143
    • 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., FRANK, J., INUI, M., CHADWICK, C., AND FLEISCHER, S.: Cryo-EM of the native structure of the calcium release channel/ryanodine receptor from sarcoplasmic reticulum. Biophys. J. 61: 936-940, 1992.
    • (1992) Biophys. J. , vol.61 , pp. 936-940
    • Radermacher, M.1    Wagenknecht, T.2    Grassucci, R.3    Frank, J.4    Inui, M.5    Chadwick, C.6    Fleischer, S.7
  • 144
    • 33947440814 scopus 로고
    • Plant insecticides. I. Ryanodine: A new alkaloid from Ryania speciosa Vahl
    • ROGERS, E. F., KONIUSZY, F. R., SHAVEL, J., JR., AND FOLKERS, K.: Plant insecticides. I. Ryanodine: A new alkaloid from Ryania speciosa Vahl. J. Am. Chem. Soc. 70: 3086-3088, 1948.
    • (1948) J. Am. Chem. Soc. , vol.70 , pp. 3086-3088
    • Rogers, E.F.1    Koniuszy, F.R.2    Shavel Jr., J.3    Folkers, K.4
  • 146
    • 0027234855 scopus 로고
    • Ryanoids and related compounds. A total synthesis of 3-epiryanodine
    • RUEST, L., AND DESLONGCHAMPS, P.: Ryanoids and related compounds. A total synthesis of 3-epiryanodine. Can. J. Chem. 71:634-638, 1993.
    • (1993) Can. J. Chem. , vol.71 , pp. 634-638
    • Ruest, L.1    Deslongchamps, P.2
  • 147
    • 0030425066 scopus 로고    scopus 로고
    • Ryanoids and related compounds. Identification of five new ryanoids from the plant Ryania speciosa Vahl. A formal total synthesis of 3-deoxyryanodol (cinnzeylanol), 10-O-acetyl-3-deoxyryanodol (cinnzeylanine), 2-deoxyryanodol, 2-deoxy-2-epiryanodol, 2,3-dideoxy-2,3-dihydroryanodol, 2-deoxy-3-epiryanodol and 2-deoxy-3-epiryanodine
    • RUEST, L., AND DODIER, M.: Ryanoids and related compounds. Identification of five new ryanoids from the plant Ryania speciosa Vahl. A formal total synthesis of 3-deoxyryanodol (cinnzeylanol), 10-O-acetyl-3-deoxyryanodol (cinnzeylanine), 2-deoxyryanodol, 2-deoxy-2-epiryanodol, 2,3-dideoxy-2,3-dihydroryanodol, 2-deoxy-3-epiryanodol and 2-deoxy-3-epiryanodine. Can. J. Chem. 74: 2424-2433, 1996.
    • (1996) Can. J. Chem. , vol.74 , pp. 2424-2433
    • Ruest, L.1    Dodier, M.2
  • 148
    • 0001655317 scopus 로고
    • Investigation of the constituents of Ryania speciosa
    • RUEST, L., TAYLOR, D. R., AND DESLONGCHAMPS, P.: Investigation of the constituents of Ryania speciosa. Can. J. Chem. 63: 2840-2843, 1985.
    • (1985) Can. J. Chem. , vol.63 , pp. 2840-2843
    • Ruest, L.1    Taylor, D.R.2    Deslongchamps, P.3
  • 149
    • 0023690937 scopus 로고
    • Ultra-structure of the calcium release channel of sarcoplasmic reticulum
    • SAITO, A., INUI, M., RADERMACHER, M., FRANK, J., AND FLEISHCER, S.: Ultra-structure of the calcium release channel of sarcoplasmic reticulum. J. Cell Biol. 107: 211-219, 1988.
    • (1988) J. Cell Biol. , vol.107 , pp. 211-219
    • Saito, A.1    Inui, M.2    Radermacher, M.3    Frank, J.4    Fleishcer, S.5
  • 150
    • 0026683335 scopus 로고
    • 2+ release channel (ryanodine receptor) has functional properties distinct from the mammalian channel proteins
    • 2+ release channel (ryanodine receptor) has functional properties distinct from the mammalian channel proteins. J. Biol. Chem. 267: 15893-15901, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15893-15901
    • Seok, J.-H.1    Xu, L.2    Kramarcy, N.R.3    Sealock, R.4    Meissner, G.5
  • 151
    • 0028937373 scopus 로고
    • Electron cryomicroscopy and angular reconstitution used to visualize the skeletal muscle calcium release channel
    • SERYSHEVA, I. I., ORLOVA, E. V., CHIU, W., SHERMAN, M. B., HAMILTON, S. L., AND VAN HEEL, M.: Electron cryomicroscopy and angular reconstitution used to visualize the skeletal muscle calcium release channel. Nature Struct. Biol. 2: 18-24, 1995.
    • (1995) Nature 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
  • 154
    • 0025278671 scopus 로고
    • High affinity ryanodine binding sites in rat liver endoplasmic reticulum
    • SHOSHAN-BARMATZ, V.: High affinity ryanodine binding sites in rat liver endoplasmic reticulum. FEBS Lett. 263: 317-320, 1990.
    • (1990) FEBS Lett. , vol.263 , pp. 317-320
    • Shoshan-Barmatz, V.1
  • 156
    • 0025764306 scopus 로고
    • Characterization of high-affinity ryanodine-binding sites of rat liver endoplasmic reticulum. Differences between liver and skeletal muscle
    • SHOSHAN-BARMATZ, V., PRESSLEY, T. A., HIGHAM, S., AND KRAUS-FRIEDMANN, N.: Characterization of high-affinity ryanodine-binding sites of rat liver endoplasmic reticulum. Differences between liver and skeletal muscle. Biochem. J. 276: 41-46, 1991.
    • (1991) Biochem. J. , vol.276 , pp. 41-46
    • Shoshan-Barmatz, V.1    Pressley, T.A.2    Higham, S.3    Kraus-Friedmann, N.4
  • 160
    • 0029818042 scopus 로고    scopus 로고
    • Modification of the conductance and gating properties of ryanodine receptors by suramin
    • SITSAPESAN, R., AND WILLIAMS, A. J.: Modification of the conductance and gating properties of ryanodine receptors by suramin. J. Mol. Biol. 153: 93-103,1996.
    • (1996) J. Mol. Biol. , vol.153 , pp. 93-103
    • Sitsapesan, R.1    Williams, A.J.2
  • 162
    • 1542593711 scopus 로고
    • The molecular structure of ryanodol-p-bromobenzyl ether
    • SRIVASTAVA, S. N., AND PRZYBYLSKA, M.: The molecular structure of ryanodol-p-bromobenzyl ether. Can. J. Chem. 46: 795-797, 1968.
    • (1968) Can. J. Chem. , vol.46 , pp. 795-797
    • Srivastava, S.N.1    Przybylska, M.2
  • 164
    • 0029662341 scopus 로고    scopus 로고
    • 2+ release channels: Does diversity in form equal diversity in function
    • 2+ release channels: Does diversity in form equal diversity in function. Physiol. Rev. 76: 1027-1071, 1996.
    • (1996) Physiol. Rev. , vol.76 , pp. 1027-1071
    • Sutko, J.L.1    Airey, J.A.2
  • 166
    • 0022298118 scopus 로고
    • Ryanodine: A modifier of sarcoplasmic reticuluro calcium release in striated muscle
    • SUTKO, J. L., ITO, K., AND KENYON, J. L.: Ryanodine: A modifier of sarcoplasmic reticuluro calcium release in striated muscle. Fed. Proc. 44: 2984-2988, 1985.
    • (1985) Fed. Proc. , vol.44 , pp. 2984-2988
    • Sutko, J.L.1    Ito, K.2    Kenyon, J.L.3
  • 167
    • 1542489073 scopus 로고
    • Pharmacology of the Ryania alkaloids: The ester A, a ryanodine analog that only increases sarcoplasmic reticulum calcium permeability
    • ed. by C. Hidalgo, J. Bacigalupo, E. Jaimovich, and J. Vergara., Plenum Publishing Corp., New York
    • SUTKO, J. L., ROBINSON, E., LATTANZIO, F. A., JR., SCHLATTERER, R. G., DESLONGCHAMPS, P., AND RUEST, L.: Pharmacology of the Ryania alkaloids: The ester A, a ryanodine analog that only increases sarcoplasmic reticulum calcium permeability. In Transduction in Biological Systems, ed. by C. Hidalgo, J. Bacigalupo, E. Jaimovich, and J. Vergara., pp. 465-473, Plenum Publishing Corp., New York, 1990.
    • (1990) Transduction in Biological Systems , pp. 465-473
    • Sutko, J.L.1    Robinson, E.2    Lattanzio Jr., F.A.3    Schlatterer, R.G.4    Deslongchamps, P.5    Ruest, L.6
  • 169
    • 0018361364 scopus 로고
    • Ryanodine: Its alterations of cat papillary muscle contractile state and responsiveness to inotropic interventions. A suggested mechanism of action
    • SUTKO, J. L., WILLERSON, J. T., TEMPLETON, G. H., JONES, L. R., AND BESCH, H. R., JR.: Ryanodine: Its alterations of cat papillary muscle contractile state and responsiveness to inotropic interventions. A suggested mechanism of action. J. Pharmacol. Exp. Ther. 209: 37-47, 1979.
    • (1979) J. Pharmacol. Exp. Ther. , vol.209 , pp. 37-47
    • Sutko, J.L.1    Willerson, J.T.2    Templeton, G.H.3    Jones, L.R.4    Besch Jr., H.R.5
  • 170
    • 0028332473 scopus 로고
    • Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene
    • TAKESHIMA, H., IINO, M., TAKEKURA, H., NISHI, M., KUNO, J., MINOWA, O., TAKANO, H., AND NODA, T.: Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene. Nature (Lond.) 369: 556-559, 1994a.
    • (1994) Nature (Lond.) , vol.369 , pp. 556-559
    • Takeshima, H.1    Iino, M.2    Takekura, H.3    Nishi, M.4    Kuno, J.5    Minowa, O.6    Takano, H.7    Noda, T.8
  • 171
    • 0027977115 scopus 로고
    • Isolation and characterization of a gene for a ryanodine receptor/ calcium release channel in Drosophila melanogaster
    • TAKESHIMA, H., NISHI, M., IWABE, N., MIYATA, T., HOSOYA. T., MASAI, I., AND HOTTA, Y.: Isolation and characterization of a gene for a ryanodine receptor/ calcium release channel in Drosophila melanogaster. FEBS Lett. 337: 81-87, 1994b.
    • (1994) FEBS Lett. , vol.337 , pp. 81-87
    • Takeshima, H.1    Nishi, M.2    Iwabe, N.3    Miyata, T.4    Hosoya, T.5    Masai, I.6    Hotta, Y.7
  • 173
    • 0027191428 scopus 로고
    • A brain-specific transcript from the 3′-terminal region of the skeletal muscle ryanodine receptor gene
    • TAKESHIMA, H., NISHIMURA, S., NISHI, M., IKEDA, M., AND SUGIMOTO, T.: A brain-specific transcript from the 3′-terminal region of the skeletal muscle ryanodine receptor gene. FEBS Lett. 322: 105-110, 1993.
    • (1993) FEBS Lett. , vol.322 , pp. 105-110
    • Takeshima, H.1    Nishimura, S.2    Nishi, M.3    Ikeda, M.4    Sugimoto, T.5
  • 175
    • 0025288735 scopus 로고
    • Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling
    • TANABE, T., BEAM, K. G., ADAMS, B. A., NIIDOME, T., AND NUMA, S.: Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling. Nature (Lond.) 346: 567-569, 1990.
    • (1990) Nature (Lond.) , vol.346 , pp. 567-569
    • Tanabe, T.1    Beam, K.G.2    Adams, B.A.3    Niidome, T.4    Numa, S.5
  • 176
    • 0027500789 scopus 로고
    • The calcium release channel of sarcoplasmic reticulum is modulated by FK-506-binding protein
    • TIMERMAN, A. P., OGUNBUNMI, E., FREUND, E., WIEDERRECHT, G., MARKS, A. R., AND FLEISCHER, S.: The calcium release channel of sarcoplasmic reticulum is modulated by FK-506-binding protein. J. Biol. Chem. 268: 22992-22999, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22992-22999
    • Timerman, A.P.1    Ogunbunmi, E.2    Freund, E.3    Wiederrecht, G.4    Marks, A.R.5    Fleischer, S.6
  • 177
    • 0028836746 scopus 로고
    • Characterization of an exchange reaction between soluble FKBP-12 and the FKBP-ryanodine receptor complex: Modulation by FKBP mutants deficient in peptidyl-prolyl isomerase activity
    • TIMERMAN, A. P., WIEDERRECHT, G., MARCY, A., AND FLEISCHER, S.: Characterization of an exchange reaction between soluble FKBP-12 and the FKBP-ryanodine receptor complex: modulation by FKBP mutants deficient in peptidyl-prolyl isomerase activity. J. Biol. Chem. 270: 2451-2459, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2451-2459
    • Timerman, A.P.1    Wiederrecht, G.2    Marcy, A.3    Fleischer, S.4
  • 178
    • 0028206051 scopus 로고
    • The ryanodine receptor from canine heart sarcoplasmic reticulum is associated with a novel FK-506 binding protein
    • TIMERMAN, A., JAYARAMAN, T., WIEDERRECHT, G., ONOUE, H., MARKS, A., AND FLEISCHER, S.: The ryanodine receptor from canine heart sarcoplasmic reticulum is associated with a novel FK-506 binding protein. Biochem. Biophys. Res. Commun. 198: 701-706, 1994.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 701-706
    • Timerman, A.1    Jayaraman, T.2    Wiederrecht, G.3    Onoue, H.4    Marks, A.5    Fleischer, S.6
  • 181
    • 0030040481 scopus 로고    scopus 로고
    • Characteristics of cocaine block of purified cardiac sarcoplasmic reticulum calcium release channels
    • TSUSHIMA, R. G., KELLY, J. E., AND WASSERSTROM, J. A.: Characteristics of cocaine block of purified cardiac sarcoplasmic reticulum calcium release channels. Biophys. J. 70: 1263-1274, 1996.
    • (1996) Biophys. J. , vol.70 , pp. 1263-1274
    • Tsushima, R.G.1    Kelly, J.E.2    Wasserstrom, J.A.3
  • 182
    • 0029758928 scopus 로고    scopus 로고
    • Rectification of rabbit cardiac ryanodine receptor current by endogenous polyamines
    • UEHARA, A., FILL, M., VELEZ, P., YASUKOCHI, M., AND IMANAUA, I.: Rectification of rabbit cardiac ryanodine receptor current by endogenous polyamines. Biophys. J. 71: 769-777, 1996.
    • (1996) Biophys. J. , vol.71 , pp. 769-777
    • Uehara, A.1    Fill, M.2    Velez, P.3    Yasukochi, M.4    Imanaua, I.5
  • 184
    • 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. P., 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.P.4    Fleischer, S.5
  • 185
    • 0029917136 scopus 로고    scopus 로고
    • Cryoelectron microscopy resolves FK506-binding protein sites on the skeletal muscle ryanodine receptor
    • WAGENKNECHT, T., GRASSUCCI, R., BERKOWITZ, J., WIEDERRECHT, G. J., XIN, H.-B., AND FLEISCHER, S.: Cryoelectron microscopy resolves FK506-binding protein sites on the skeletal muscle ryanodine receptor. Biophys. J. 70: 1709-1715, 1996.
    • (1996) Biophys. J. , vol.70 , pp. 1709-1715
    • Wagenknecht, T.1    Grassucci, R.2    Berkowitz, J.3    Wiederrecht, G.J.4    Xin, H.-B.5    Fleischer, S.6
  • 186
    • 0029153507 scopus 로고
    • Three-dimensional architecture of the skeletal muscle ryanodine receptor
    • WAGENKNECHT, T., AND RADERMACHER, M.: Three-dimensional architecture of the skeletal muscle ryanodine receptor. FEBS Lett. 369: 43-46, 1995.
    • (1995) FEBS Lett. , vol.369 , pp. 43-46
    • Wagenknecht, T.1    Radermacher, M.2
  • 189
    • 37049100825 scopus 로고
    • 9,21-didehydroryanodine: A new principal toxic constituent of the botanical insecticide Ryania
    • WATERHOUSE, A. L., HOLDEN, I., AND CASIDA, J. E.: 9,21-didehydroryanodine: a new principal toxic constituent of the botanical insecticide Ryania. J. Chem. Soc. Chem. Commun. issue 19: 1265-1266, 1984.
    • (1984) J. Chem. Soc. Chem. Commun. , Issue.19 , pp. 1265-1266
    • Waterhouse, A.L.1    Holden, I.2    Casida, J.E.3
  • 190
    • 37049095386 scopus 로고
    • Ryanoid insecticides: Structural examination by fully coupled two-dimensional 1H-13C shift correlation nuclear magnetic resonance spectroscopy
    • WATERHOUSE, A. L., HOLDEN, I., AND CASIDA, J. E.: Ryanoid insecticides: structural examination by fully coupled two-dimensional 1H-13C shift correlation nuclear magnetic resonance spectroscopy. J. Chem. Soc. Perkin Trans. II: 1011-1016, 1985.
    • (1985) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 1011-1016
    • Waterhouse, A.L.1    Holden, I.2    Casida, J.E.3
  • 192
    • 0028227183 scopus 로고
    • Structural determinants of high affinity binding to the vertebrate skeletal muscle ryanodine receptor: A comparative molecular field analysis
    • WELCH, W., AHMAD, S., AIREY, J. A., GERZON, K., HUMERICKHOUSE, R. A., BESCH, H. R., JR., RUEST, L., DESLONGCHAMPS, P., AND SUTKO, J. L.: Structural determinants of high affinity binding to the vertebrate skeletal muscle ryanodine receptor: a comparative molecular field analysis. Biochemistry 33: 6074-6085, 1994.
    • (1994) Biochemistry , vol.33 , pp. 6074-6085
    • Welch, W.1    Ahmad, S.2    Airey, J.A.3    Gerzon, K.4    Humerickhouse, R.A.5    Besch Jr., H.R.6    Ruest, L.7    Deslongchamps, P.8    Sutko, J.L.9
  • 193
    • 0029898709 scopus 로고    scopus 로고
    • The pyrrole locus is the major orienting factor in ryanodine binding
    • WELCH, W., SUTKO, J. L., MITCHELL, K. E., AIREY, J., AND RUEST, L.: The pyrrole locus is the major orienting factor in ryanodine binding. Biochemistry 35: 7165-7173, 1996a.
    • (1996) Biochemistry , vol.35 , pp. 7165-7173
    • Welch, W.1    Sutko, J.L.2    Mitchell, K.E.3    Airey, J.4    Ruest, L.5
  • 195
    • 0000396523 scopus 로고
    • The structure of ryanodine
    • WIESNER, K.: The structure of ryanodine. Adv. Org. Chem. 8: 295-316, 1972.
    • (1972) Adv. Org. Chem. , vol.8 , pp. 295-316
    • Wiesner, K.1
  • 198
    • 0029931969 scopus 로고    scopus 로고
    • Ortho-substituted polychorinated biphenyls alter calcium regulation by a ryanodine receptor-mediated mechanism: Structural specificity toward skeletal- and cardiac-type microsomal calcium release channels
    • WONG, P. W., AND PESSAH, I. N.: Ortho-substituted polychorinated biphenyls alter calcium regulation by a ryanodine receptor-mediated mechanism: structural specificity toward skeletal- and cardiac-type microsomal calcium release channels. Mol. Pharmacol. 49: 740-751, 1996.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 740-751
    • Wong, P.W.1    Pessah, I.N.2
  • 199
    • 0001576379 scopus 로고
    • A new synthesis of thiol esters
    • YAMADA, S., YOKOYAMA, Y., AND SHIOIRI, T.: A new synthesis of thiol esters. J Org. Chem. 39: 3302-3303, 1974.
    • (1974) J Org. Chem. , vol.39 , pp. 3302-3303
    • Yamada, S.1    Yokoyama, Y.2    Shioiri, T.3
  • 200
    • 0028326771 scopus 로고
    • Myotoxin a reduces the threshold for calcium-induced calcium release in skeletal muscle
    • YUDKOWSKY, M. L., BEECH, J., AND FLETCHER, J. E.: Myotoxin a reduces the threshold for calcium-induced calcium release in skeletal muscle. Toxicon 32: 273-278, 1994.
    • (1994) Toxicon , vol.32 , pp. 273-278
    • Yudkowsky, M.L.1    Beech, J.2    Fletcher, J.E.3
  • 203
    • 0029877465 scopus 로고    scopus 로고
    • Ryanodine receptor/calcium release channel conformations as reflected in the different effects of propranolol on its ryanodine binding and channel activity
    • ZCHUT, S., FENG, W., AND SHOSHAN-BARMATZ, V.: Ryanodine receptor/calcium release channel conformations as reflected in the different effects of propranolol on its ryanodine binding and channel activity. Biochem. J. 315: 377-383, 1996.
    • (1996) Biochem. J. , vol.315 , pp. 377-383
    • Zchut, S.1    Feng, W.2    Shoshan-Barmatz, V.3
  • 205
    • 0028114269 scopus 로고
    • Identification of two ryanodine receptor transcripts in neonatal, slow-, and fast-twitch rabbit skeletal muscles
    • ZORZATO, F., SACCHETO, R., AND MARGRETH, A.: Identification of two ryanodine receptor transcripts in neonatal, slow-, and fast-twitch rabbit skeletal muscles. Biochem. Biophys. Res. Commun. 203: 1725-1730, 1994.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1725-1730
    • Zorzato, F.1    Saccheto, R.2    Margreth, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.