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Volumn 280, Issue 21, 2013, Pages 5456-5470

Ryanodine receptor calcium release channels: Lessons from structure-function studies

Author keywords

cryo electron microscopy; excitation contraction coupling; inositol 1,4,5 trisphosphate receptor; malignant hyperthermia; nuclear magnetic resonance spectroscopy; ryanodine receptor; X ray crystallography

Indexed keywords

1,4 DIHYDROPYRIDINE RECEPTOR; CALMODULIN; DANTROLENE; INHALATION ANESTHETIC AGENT; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; MUSCLE RELAXANT AGENT; RYANODINE RECEPTOR; RYANODINE RECEPTOR 1; RYANODINE RECEPTOR 2; RYANODINE RECEPTOR 3;

EID: 84886099424     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12194     Document Type: Conference Paper
Times cited : (56)

References (145)
  • 1
    • 0033768323 scopus 로고    scopus 로고
    • Excitation-contraction coupling in cardiac muscle revisited
    • Lewartowski B, (2000) Excitation-contraction coupling in cardiac muscle revisited. J Physiol Pharmacol 51, 371-386.
    • (2000) J Physiol Pharmacol , vol.51 , pp. 371-386
    • Lewartowski, B.1
  • 2
    • 0034093987 scopus 로고    scopus 로고
    • Excitation-contraction coupling in skeletal muscle: Comparisons with cardiac muscle
    • Lamb GD, (2000) Excitation-contraction coupling in skeletal muscle: comparisons with cardiac muscle. Clin Exp Pharmacol Physiol 27, 216-224.
    • (2000) Clin Exp Pharmacol Physiol , vol.27 , pp. 216-224
    • Lamb, G.D.1
  • 3
    • 77954346809 scopus 로고    scopus 로고
    • Looking for answers to EC coupling's persistent questions
    • Beam KG, &, Bannister RA, (2010) Looking for answers to EC coupling's persistent questions. J Gen Physiol 136, 7-12.
    • (2010) J Gen Physiol , vol.136 , pp. 7-12
    • Beam, K.G.1    Bannister, R.A.2
  • 4
    • 85006142608 scopus 로고
    • Studies of the Triad: I. Structure of the junction in Frog Twitch fibers
    • Franzini-Armstrong C, (1970) Studies of the Triad: I. Structure of the junction in Frog Twitch fibers. J Cell Biol 47, 488-499.
    • (1970) J Cell Biol , vol.47 , pp. 488-499
    • Franzini-Armstrong, C.1
  • 5
    • 0023654965 scopus 로고
    • Identification and characterization of the high affinity [3H]ryanodine receptor of the junctional sarcoplasmic reticulum Ca2 + release channel
    • Campbell KP, Knudson CM, Imagawa T, Leung AT, Sutko JL, Kahl SD, Raab CR, &, Madson L, (1987) Identification and characterization of the high affinity [3H]ryanodine receptor of the junctional sarcoplasmic reticulum Ca2 + release channel. J Biol Chem 262, 6460-6463.
    • (1987) J Biol Chem , vol.262 , pp. 6460-6463
    • Campbell, K.P.1    Knudson, C.M.2    Imagawa, T.3    Leung, A.T.4    Sutko, J.L.5    Kahl, S.D.6    Raab, C.R.7    Madson, L.8
  • 6
    • 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, (1987) Purification of the ryanodine receptor and identity with feet structures of junctional terminal cisternae of sarcoplasmic reticulum from fast skeletal muscle. J Biol Chem 262, 1740-1747.
    • (1987) J Biol Chem , vol.262 , pp. 1740-1747
    • Inui, M.1    Saito, A.2    Fleischer, S.3
  • 7
    • 0023903046 scopus 로고
    • Purification and reconstitution of the calcium release channel from skeletal muscle
    • Lai FA, Erickson HP, Rousseau E, Liu QY, &, Meissner G, (1988) Purification and reconstitution of the calcium release channel from skeletal muscle. Nature 331, 315-319.
    • (1988) Nature , vol.331 , pp. 315-319
    • Lai, F.A.1    Erickson, H.P.2    Rousseau, E.3    Liu, Q.Y.4    Meissner, G.5
  • 8
    • 33947440814 scopus 로고
    • Plant insecticides; Ryanodine, a new alkaloid from Ryania speciosa Vahl
    • Rogers EF, Koniuszy FR, Shavel J Jr,. &, Folkers K, (1948) Plant insecticides; ryanodine, a new alkaloid from Ryania speciosa Vahl. J Am Chem Soc 70, 3086-3088.
    • (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
  • 9
    • 0024449839 scopus 로고
    • Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor
    • Mignery GA, Sudhof TC, Takei K, &, De Camilli P, (1989) Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor. Nature 342, 192-195.
    • (1989) Nature , vol.342 , pp. 192-195
    • Mignery, G.A.1    Sudhof, T.C.2    Takei, K.3    De Camilli, P.4
  • 10
    • 0024397525 scopus 로고
    • Nucleotide sequence of cDNA encoding P400 protein in the mouse cerebellum
    • Furuichi T, Yoshikawa S, &, Mikoshiba K, (1989) Nucleotide sequence of cDNA encoding P400 protein in the mouse cerebellum. Nucleic Acids Res 17, 5385-5386.
    • (1989) Nucleic Acids Res , vol.17 , pp. 5385-5386
    • Furuichi, T.1    Yoshikawa, S.2    Mikoshiba, K.3
  • 11
    • 21244472239 scopus 로고    scopus 로고
    • Modulation of mammalian inositol 1,4,5-trisphosphate receptor isoforms by calcium: A role of calcium sensor region
    • Tu H, Wang Z, &, Bezprozvanny I, (2005) Modulation of mammalian inositol 1,4,5-trisphosphate receptor isoforms by calcium: a role of calcium sensor region. Biophys J 88, 1056-1069.
    • (2005) Biophys J , vol.88 , pp. 1056-1069
    • Tu, H.1    Wang, Z.2    Bezprozvanny, I.3
  • 13
    • 80054097452 scopus 로고    scopus 로고
    • Identification of intracellular and plasma membrane calcium channel homologues in pathogenic parasites
    • Prole DL, &, Taylor CW, (2011) Identification of intracellular and plasma membrane calcium channel homologues in pathogenic parasites. PLoS One 6, e26218.
    • (2011) PLoS One , vol.6
    • Prole, D.L.1    Taylor, C.W.2
  • 14
    • 0033976150 scopus 로고    scopus 로고
    • Novel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases
    • Ponting CP, (2000) Novel repeats in ryanodine and IP3 receptors and protein O-mannosyltransferases. Trends Biochem Sci 25, 48-50.
    • (2000) Trends Biochem Sci , vol.25 , pp. 48-50
    • Ponting, C.P.1
  • 16
    • 0025071723 scopus 로고
    • Molecular cloning of cDNA encoding human and rabbit forms of the Ca2 + release channel (ryanodine receptor) of skeletal muscle sarcoplasmic reticulum
    • Zorzato F, Fujii J, Otsu K, Phillips M, Green NM, Lai FA, Meissner G, &, MacLennan DH, (1990) Molecular cloning of cDNA encoding human and rabbit forms of the Ca2 + release channel (ryanodine receptor) of skeletal muscle sarcoplasmic reticulum. J Biol Chem 265, 2244-2256.
    • (1990) J Biol Chem , vol.265 , pp. 2244-2256
    • Zorzato, F.1    Fujii, J.2    Otsu, K.3    Phillips, M.4    Green, N.M.5    Lai, F.A.6    Meissner, G.7    Maclennan, D.H.8
  • 17
    • 0025171580 scopus 로고
    • Molecular cloning of cDNA encoding the Ca2 + release channel (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic reticulum
    • Otsu K, Willard HF, Khanna VK, Zorzato F, Green NM, &, MacLennan DH, (1990) Molecular cloning of cDNA encoding the Ca2 + release channel (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic reticulum. J Biol Chem 265, 13472-13483.
    • (1990) J Biol Chem , vol.265 , pp. 13472-13483
    • Otsu, K.1    Willard, H.F.2    Khanna, V.K.3    Zorzato, F.4    Green, N.M.5    Maclennan, D.H.6
  • 18
    • 0025123804 scopus 로고
    • Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel
    • Nakai J, Imagawa T, Hakamat Y, Shigekawa M, Takeshima H, &, Numa S, (1990) Primary structure and functional expression from cDNA of the cardiac ryanodine receptor/calcium release channel. FEBS Lett 271, 169-177.
    • (1990) FEBS Lett , vol.271 , pp. 169-177
    • Nakai, J.1    Imagawa, T.2    Hakamat, Y.3    Shigekawa, M.4    Takeshima, H.5    Numa, S.6
  • 19
    • 0034737812 scopus 로고    scopus 로고
    • Requirement of ryanodine receptor subtypes 1 and 2 for Ca(2 +)-induced Ca(2 +) release in vascular myocytes
    • Coussin F, Macrez N, Morel JL, &, Mironneau J, (2000) Requirement of ryanodine receptor subtypes 1 and 2 for Ca(2 +)-induced Ca(2 +) release in vascular myocytes. J Biol Chem 275, 9596-9603.
    • (2000) J Biol Chem , vol.275 , pp. 9596-9603
    • Coussin, F.1    Macrez, N.2    Morel, J.L.3    Mironneau, J.4
  • 20
    • 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, &, Sorrentino V, (1995) The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues. J Cell Biol 128, 893-904.
    • (1995) J Cell Biol , vol.128 , pp. 893-904
    • Giannini, G.1    Conti, A.2    Mammarella, S.3    Scrobogna, M.4    Sorrentino, V.5
  • 21
    • 0029923335 scopus 로고    scopus 로고
    • Alpha and beta isoforms of ryanodine receptor from chicken skeletal muscle are the homologues of mammalian RyR1 and RyR3
    • Ottini L, Marziali G, Conti A, Charlesworth A, &, Sorrentino V, (1996) Alpha and beta isoforms of ryanodine receptor from chicken skeletal muscle are the homologues of mammalian RyR1 and RyR3. Biochem J 315, 207-216.
    • (1996) Biochem J , vol.315 , pp. 207-216
    • Ottini, L.1    Marziali, G.2    Conti, A.3    Charlesworth, A.4    Sorrentino, V.5
  • 22
    • 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, &, Endo M, (1994) Primary structure and distribution of ryanodine-binding protein isoforms of the bullfrog skeletal muscle. J Biol Chem 269, 17206-17214.
    • (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
  • 23
    • 0029796183 scopus 로고    scopus 로고
    • Unc-68 encodes a ryanodine receptor involved in regulating C elegans body-wall muscle contraction
    • Maryon EB, Coronado R, &, Anderson P, (1996) unc-68 encodes a ryanodine receptor involved in regulating C. elegans body-wall muscle contraction. J Cell Biol 134, 885-893.
    • (1996) J Cell Biol , vol.134 , pp. 885-893
    • Maryon, E.B.1    Coronado, R.2    Anderson, P.3
  • 24
    • 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, &, Hotta Y, (1994) Isolation and characterization of a gene for a ryanodine receptor/calcium release channel in Drosophila melanogaster. FEBS Lett 337, 81-87.
    • (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
  • 25
  • 26
    • 0028263379 scopus 로고
    • Cloning and expression of human brain type i inositol 1,4,5-trisphosphate 5-phosphatase. High levels of mRNA in cerebellar Purkinje cells
    • De Smedt F, Verjans B, Mailleux P, &, Erneux C, (1994) Cloning and expression of human brain type I inositol 1,4,5-trisphosphate 5-phosphatase. High levels of mRNA in cerebellar Purkinje cells. FEBS Lett 347, 69-72.
    • (1994) FEBS Lett , vol.347 , pp. 69-72
    • De Smedt, F.1    Verjans, B.2    Mailleux, P.3    Erneux, C.4
  • 27
    • 0027318996 scopus 로고
    • Sequence and functional characterization of a third inositol trisphosphate receptor subtype, IP3R-3, expressed in pancreatic islets, kidney, gastrointestinal tract, and other tissues
    • Blondel O, Takeda J, Janssen H, Seino S, &, Bell GI, (1993) Sequence and functional characterization of a third inositol trisphosphate receptor subtype, IP3R-3, expressed in pancreatic islets, kidney, gastrointestinal tract, and other tissues. J Biol Chem 268, 11356-11363.
    • (1993) J Biol Chem , vol.268 , pp. 11356-11363
    • Blondel, O.1    Takeda, J.2    Janssen, H.3    Seino, S.4    Bell, G.I.5
  • 28
    • 0028108283 scopus 로고
    • Epithelial inositol 1,4,5-trisphosphate receptors. Multiplicity of localization, solubility, and isoforms
    • Bush KT, Stuart RO, Li SH, Moura LA, Sharp AH, Ross CA, &, Nigam SK, (1994) Epithelial inositol 1,4,5-trisphosphate receptors. Multiplicity of localization, solubility, and isoforms. J Biol Chem 269, 23694-23699.
    • (1994) J Biol Chem , vol.269 , pp. 23694-23699
    • Bush, K.T.1    Stuart, R.O.2    Li, S.H.3    Moura, L.A.4    Sharp, A.H.5    Ross, C.A.6    Nigam, S.K.7
  • 30
    • 0028172180 scopus 로고
    • Co-expression in vertebrate tissues and cell lines of multiple inositol 1,4,5-trisphosphate (InsP3) receptors with distinct affinities for InsP3
    • Newton CL, Mignery GA, &, Sudhof TC, (1994) Co-expression in vertebrate tissues and cell lines of multiple inositol 1,4,5-trisphosphate (InsP3) receptors with distinct affinities for InsP3. J Biol Chem 269, 28613-28619.
    • (1994) J Biol Chem , vol.269 , pp. 28613-28619
    • Newton, C.L.1    Mignery, G.A.2    Sudhof, T.C.3
  • 31
    • 0141483040 scopus 로고    scopus 로고
    • Loss of inositol 1,4,5-trisphosphate receptors from bile duct epithelia is a common event in cholestasis
    • Shibao K, Hirata K, Robert ME, &, Nathanson MH, (2003) Loss of inositol 1,4,5-trisphosphate receptors from bile duct epithelia is a common event in cholestasis. Gastroenterology 125, 1175-1187.
    • (2003) Gastroenterology , vol.125 , pp. 1175-1187
    • Shibao, K.1    Hirata, K.2    Robert, M.E.3    Nathanson, M.H.4
  • 32
    • 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, &, Noda T, (1994) Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene. Nature 369, 556-559.
    • (1994) Nature , 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
  • 33
    • 0032526717 scopus 로고    scopus 로고
    • Embryonic lethality and abnormal cardiac myocytes in mice lacking ryanodine receptor type 2
    • Takeshima H, Komazaki S, Hirose K, Nishi M, Noda T, &, Iino M, (1998) Embryonic lethality and abnormal cardiac myocytes in mice lacking ryanodine receptor type 2. EMBO J 17, 3309-3316.
    • (1998) EMBO J , vol.17 , pp. 3309-3316
    • Takeshima, H.1    Komazaki, S.2    Hirose, K.3    Nishi, M.4    Noda, T.5    Iino, M.6
  • 37
    • 72449180513 scopus 로고    scopus 로고
    • Comprehensive behavioral phenotyping of ryanodine receptor type 3 (RyR3) knockout mice: Decreased social contact duration in two social interaction tests
    • Matsuo N, Tanda K, Nakanishi K, Yamasaki N, Toyama K, Takao K, Takeshima H, &, Miyakawa T, (2009) Comprehensive behavioral phenotyping of ryanodine receptor type 3 (RyR3) knockout mice: decreased social contact duration in two social interaction tests. Front Behav Neurosci 3, 3.
    • (2009) Front Behav Neurosci , vol.3 , pp. 3
    • Matsuo, N.1    Tanda, K.2    Nakanishi, K.3    Yamasaki, N.4    Toyama, K.5    Takao, K.6    Takeshima, H.7    Miyakawa, T.8
  • 38
    • 0034629264 scopus 로고    scopus 로고
    • Mutant mice lacking ryanodine receptor type 3 exhibit deficits of contextual fear conditioning and activation of calcium/calmodulin-dependent protein kinase II in the hippocampus
    • Kouzu Y, Moriya T, Takeshima H, Yoshioka T, &, Shibata S, (2000) Mutant mice lacking ryanodine receptor type 3 exhibit deficits of contextual fear conditioning and activation of calcium/calmodulin-dependent protein kinase II in the hippocampus. Brain Res Mol Brain Res 76, 142-150.
    • (2000) Brain Res Mol Brain Res , vol.76 , pp. 142-150
    • Kouzu, Y.1    Moriya, T.2    Takeshima, H.3    Yoshioka, T.4    Shibata, S.5
  • 42
    • 44649151130 scopus 로고    scopus 로고
    • Decreased olfactory mucus secretion and nasal abnormality in mice lacking type 2 and type 3 IP3 receptors
    • Fukuda N, Shirasu M, Sato K, Ebisui E, Touhara K, &, Mikoshiba K, (2008) Decreased olfactory mucus secretion and nasal abnormality in mice lacking type 2 and type 3 IP3 receptors. Eur J Neurosci 27, 2665-2675.
    • (2008) Eur J Neurosci , vol.27 , pp. 2665-2675
    • Fukuda, N.1    Shirasu, M.2    Sato, K.3    Ebisui, E.4    Touhara, K.5    Mikoshiba, K.6
  • 43
    • 79960288856 scopus 로고    scopus 로고
    • Functional characterization of the P1059L mutation in the inositol 1,4,5-trisphosphate receptor type 1 identified in a Japanese SCA15 family
    • Yamazaki H, Nozaki H, Onodera O, Michikawa T, Nishizawa M, &, Mikoshiba K, (2011) Functional characterization of the P1059L mutation in the inositol 1,4,5-trisphosphate receptor type 1 identified in a Japanese SCA15 family. Biochem Biophys Res Commun 410, 754-758.
    • (2011) Biochem Biophys Res Commun , vol.410 , pp. 754-758
    • Yamazaki, H.1    Nozaki, H.2    Onodera, O.3    Michikawa, T.4    Nishizawa, M.5    Mikoshiba, K.6
  • 45
    • 24644471966 scopus 로고    scopus 로고
    • The inositol 1,4,5-trisphosphate receptors
    • Bezprozvanny I, (2005) The inositol 1,4,5-trisphosphate receptors. Cell Calcium 38, 261-272.
    • (2005) Cell Calcium , vol.38 , pp. 261-272
    • Bezprozvanny, I.1
  • 46
    • 45849109876 scopus 로고    scopus 로고
    • Unicellular Ca2 + signaling 'toolkit' at the origin of metazoa
    • Cai X, (2008) Unicellular Ca2 + signaling 'toolkit' at the origin of metazoa. Mol Biol Evol 25, 1357-1361.
    • (2008) Mol Biol Evol , vol.25 , pp. 1357-1361
    • Cai, X.1
  • 47
    • 84857686131 scopus 로고    scopus 로고
    • Ancestral Ca2 + signaling machinery in early animal and fungal evolution
    • Cai X, &, Clapham DE, (2012) Ancestral Ca2 + signaling machinery in early animal and fungal evolution. Mol Biol Evol 29, 91-100.
    • (2012) Mol Biol Evol , vol.29 , pp. 91-100
    • Cai, X.1    Clapham, D.E.2
  • 48
    • 84859917357 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels: An evolutionary perspective
    • Mackrill JJ, (2012) Ryanodine receptor calcium release channels: an evolutionary perspective. Adv Exp Med Biol 740, 159-182.
    • (2012) Adv Exp Med Biol , vol.740 , pp. 159-182
    • Mackrill, J.J.1
  • 49
    • 78649469923 scopus 로고    scopus 로고
    • The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule
    • Tung C-C, Lobo PA, Kimlicka L, &, Van Petegem F, (2010) The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule. Nature 468, 585-588.
    • (2010) Nature , vol.468 , pp. 585-588
    • Tung, C.-C.1    Lobo, P.A.2    Kimlicka, L.3    Van Petegem, F.4
  • 51
    • 80455164574 scopus 로고    scopus 로고
    • Apo and InsP(3)-bound crystal structures of the ligand-binding domain of an InsP(3) receptor
    • Lin CC, Baek K, &, Lu Z, (2011) Apo and InsP(3)-bound crystal structures of the ligand-binding domain of an InsP(3) receptor. Nat Struct Mol Biol 18, 1172-1174.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 1172-1174
    • Lin, C.C.1    Baek, K.2    Lu, Z.3
  • 53
    • 79959907270 scopus 로고    scopus 로고
    • Calcium signalling and Alzheimer's disease
    • Berridge MJ, (2011) Calcium signalling and Alzheimer's disease. Neurochem Res 36, 1149-1156.
    • (2011) Neurochem Res , vol.36 , pp. 1149-1156
    • Berridge, M.J.1
  • 54
    • 79955481474 scopus 로고    scopus 로고
    • Complications associated with the administration of dantrolene 1987 to 2006: A report from the North American Malignant Hyperthermia Registry of the Malignant Hyperthermia Association of the United States
    • Brandom BW, Larach MG, Chen MS, &, Young MC, (2011) Complications associated with the administration of dantrolene 1987 to 2006: a report from the North American Malignant Hyperthermia Registry of the Malignant Hyperthermia Association of the United States. Anesth Analg 112, 1115-1123.
    • (2011) Anesth Analg , vol.112 , pp. 1115-1123
    • Brandom, B.W.1    Larach, M.G.2    Chen, M.S.3    Young, M.C.4
  • 56
    • 84868194081 scopus 로고    scopus 로고
    • Mapping domains and mutations on the skeletal muscle ryanodine receptor channel
    • Hwang JH, Zorzato F, Clarke NF, &, Treves S, (2012) Mapping domains and mutations on the skeletal muscle ryanodine receptor channel. Trends Mol Med 18, 644-657.
    • (2012) Trends Mol Med , vol.18 , pp. 644-657
    • Hwang, J.H.1    Zorzato, F.2    Clarke, N.F.3    Treves, S.4
  • 57
  • 58
    • 0034849005 scopus 로고    scopus 로고
    • Functional effects of central core disease mutations in the cytoplasmic region of the skeletal muscle ryanodine receptor
    • Avila G, &, Dirksen RT, (2001) Functional effects of central core disease mutations in the cytoplasmic region of the skeletal muscle ryanodine receptor. J Gen Physiol 118, 277-290.
    • (2001) J Gen Physiol , vol.118 , pp. 277-290
    • Avila, G.1    Dirksen, R.T.2
  • 60
    • 0036323498 scopus 로고    scopus 로고
    • RYR1 mutations causing central core disease are associated with more severe malignant hyperthermia in vitro contracture test phenotypes
    • Robinson RL, Brooks C, Brown SL, Ellis FR, Halsall PJ, Quinnell RJ, Shaw MA, &, Hopkins PM, (2002) RYR1 mutations causing central core disease are associated with more severe malignant hyperthermia in vitro contracture test phenotypes. Hum Mutat 20, 88-97.
    • (2002) Hum Mutat , vol.20 , pp. 88-97
    • Robinson, R.L.1    Brooks, C.2    Brown, S.L.3    Ellis, F.R.4    Halsall, P.J.5    Quinnell, R.J.6    Shaw, M.A.7    Hopkins, P.M.8
  • 61
  • 62
    • 70349568135 scopus 로고    scopus 로고
    • The relationship between exertional heat illness, exertional rhabdomyolysis, and malignant hyperthermia
    • Capacchione JF, &, Muldoon SM, (2009) The relationship between exertional heat illness, exertional rhabdomyolysis, and malignant hyperthermia. Anesth Analg 109, 1065-1069.
    • (2009) Anesth Analg , vol.109 , pp. 1065-1069
    • Capacchione, J.F.1    Muldoon, S.M.2
  • 63
    • 0020118814 scopus 로고
    • Dantrolene in human malignant hyperthermia
    • Kolb ME, Horne ML, &, Martz R, (1982) Dantrolene in human malignant hyperthermia. Anesthesiology 56, 254-262.
    • (1982) Anesthesiology , vol.56 , pp. 254-262
    • Kolb, M.E.1    Horne, M.L.2    Martz, R.3
  • 64
    • 58749105519 scopus 로고    scopus 로고
    • Trends and outcomes of malignant hyperthermia in the United States, 2000 to 2005
    • Rosero EB, Adesanya AO, Timaran CH, &, Joshi GP, (2009) Trends and outcomes of malignant hyperthermia in the United States, 2000 to 2005. Anesthesiology 110, 89-94.
    • (2009) Anesthesiology , vol.110 , pp. 89-94
    • Rosero, E.B.1    Adesanya, A.O.2    Timaran, C.H.3    Joshi, G.P.4
  • 66
    • 0035958043 scopus 로고    scopus 로고
    • Dantrolene inhibition of ryanodine receptor Ca2 + release channels. Molecular mechanism and isoform selectivity
    • Zhao F, Li P, Chen SR, Louis CF, &, Fruen BR, (2001) Dantrolene inhibition of ryanodine receptor Ca2 + release channels. Molecular mechanism and isoform selectivity. J Biol Chem 276, 13810-13816.
    • (2001) J Biol Chem , vol.276 , pp. 13810-13816
    • Zhao, F.1    Li, P.2    Chen, S.R.3    Louis, C.F.4    Fruen, B.R.5
  • 67
    • 0026556355 scopus 로고
    • Malignant hyperthermia
    • MacLennan DH, &, Phillips MS, (1992) Malignant hyperthermia. Science 256, 789-794.
    • (1992) Science , vol.256 , pp. 789-794
    • Maclennan, D.H.1    Phillips, M.S.2
  • 71
    • 40149101317 scopus 로고    scopus 로고
    • Arrhythmogenic right ventricular dysplasia/cardiomyopathy
    • El Masry HZ, &, Yadav AV, (2008) Arrhythmogenic right ventricular dysplasia/cardiomyopathy. Expert Rev Cardiovasc Ther 6, 249-260.
    • (2008) Expert Rev Cardiovasc Ther , vol.6 , pp. 249-260
    • El Masry, H.Z.1    Yadav, A.V.2
  • 72
    • 84866395344 scopus 로고    scopus 로고
    • Ryanodine receptors: Structure and function
    • Van Petegem F, (2012) Ryanodine receptors: structure and function. J Biol Chem 287, 31624-31632.
    • (2012) J Biol Chem , vol.287 , pp. 31624-31632
    • Van Petegem, F.1
  • 73
    • 0030666554 scopus 로고    scopus 로고
    • Caffeine and halothane sensitivity of intracellular Ca2 + release is altered by 15 calcium release channel (ryanodine receptor) mutations associated with malignant hyperthermia and/or central core disease
    • Tong J, Oyamada H, Demaurex N, Grinstein S, McCarthy TV, &, MacLennan DH, (1997) Caffeine and halothane sensitivity of intracellular Ca2 + release is altered by 15 calcium release channel (ryanodine receptor) mutations associated with malignant hyperthermia and/or central core disease. J Biol Chem 272, 26332-26339.
    • (1997) J Biol Chem , vol.272 , pp. 26332-26339
    • Tong, J.1    Oyamada, H.2    Demaurex, N.3    Grinstein, S.4    McCarthy, T.V.5    Maclennan, D.H.6
  • 74
    • 4444357245 scopus 로고    scopus 로고
    • RyR2 mutations linked to ventricular tachycardia and sudden death reduce the threshold for store-overload-induced Ca2 + release (SOICR)
    • Jiang D, Xiao B, Yang D, Wang R, Choi P, Zhang L, Cheng H, &, Chen SR, (2004) RyR2 mutations linked to ventricular tachycardia and sudden death reduce the threshold for store-overload-induced Ca2 + release (SOICR). Proc Natl Acad Sci USA 101, 13062-13067.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13062-13067
    • Jiang, D.1    Xiao, B.2    Yang, D.3    Wang, R.4    Choi, P.5    Zhang, L.6    Cheng, H.7    Chen, S.R.8
  • 75
    • 59449088323 scopus 로고    scopus 로고
    • Defective domain-domain interactions within the ryanodine receptor as a critical cause of diastolic Ca2 + leak in failing hearts
    • Tateishi H, Yano M, Mochizuki M, Suetomi T, Ono M, Xu X, Uchinoumi H, Okuda S, Oda T, Kobayashi S, et al,. (2009) Defective domain-domain interactions within the ryanodine receptor as a critical cause of diastolic Ca2 + leak in failing hearts. Cardiovasc Res 81, 536-545.
    • (2009) Cardiovasc Res , vol.81 , pp. 536-545
    • Tateishi, H.1    Yano, M.2    Mochizuki, M.3    Suetomi, T.4    Ono, M.5    Xu, X.6    Uchinoumi, H.7    Okuda, S.8    Oda, T.9    Kobayashi, S.10
  • 76
    • 80051798088 scopus 로고    scopus 로고
    • Mutation-linked defective interdomain interactions within ryanodine receptor cause aberrant Ca2 + release leading to catecholaminergic polymorphic ventricular tachycardia/clinical perspective
    • Suetomi T, Yano M, Uchinoumi H, Fukuda M, Hino A, Ono M, Xu X, Tateishi H, Okuda S, Doi M, et al,. (2011) Mutation-linked defective interdomain interactions within ryanodine receptor cause aberrant Ca2 + release leading to catecholaminergic polymorphic ventricular tachycardia/clinical perspective. Circulation 124, 682-694.
    • (2011) Circulation , vol.124 , pp. 682-694
    • Suetomi, T.1    Yano, M.2    Uchinoumi, H.3    Fukuda, M.4    Hino, A.5    Ono, M.6    Xu, X.7    Tateishi, H.8    Okuda, S.9    Doi, M.10
  • 77
    • 0034444119 scopus 로고    scopus 로고
    • Postulated role of inter-domain interaction within the ryanodine receptor in Ca(2 +) channel regulation
    • Ikemoto N, &, Yamamoto T, (2000) Postulated role of inter-domain interaction within the ryanodine receptor in Ca(2 +) channel regulation. Trends Cardiovasc Med 10, 310-316.
    • (2000) Trends Cardiovasc Med , vol.10 , pp. 310-316
    • Ikemoto, N.1    Yamamoto, T.2
  • 78
    • 0034640113 scopus 로고    scopus 로고
    • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): Defective regulation in failing hearts
    • Marx SO, Reiken S, Hisamatsu Y, Jayaraman T, Burkhoff D, Rosemblit N, &, Marks AR, (2000) PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell 101, 365-376.
    • (2000) Cell , vol.101 , pp. 365-376
    • Marx, S.O.1    Reiken, S.2    Hisamatsu, Y.3    Jayaraman, T.4    Burkhoff, D.5    Rosemblit, N.6    Marks, A.R.7
  • 79
  • 81
    • 0141571322 scopus 로고    scopus 로고
    • Ryanodine receptor mutations associated with stress-induced ventricular tachycardia mediate increased calcium release in stimulated cardiomyocytes
    • George CH, Higgs GV, &, Lai FA, (2003) Ryanodine receptor mutations associated with stress-induced ventricular tachycardia mediate increased calcium release in stimulated cardiomyocytes. Circ Res 93, 531-540.
    • (2003) Circ Res , vol.93 , pp. 531-540
    • George, C.H.1    Higgs, G.V.2    Lai, F.A.3
  • 82
    • 77953812124 scopus 로고    scopus 로고
    • Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized cardiac myocytes and effects on Ca sparks
    • Guo T, Cornea RL, Huke S, Camors E, Yang Y, Picht E, Fruen BR, &, Bers DM, (2010) Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized cardiac myocytes and effects on Ca sparks. Circ Res 106, 1743-1752.
    • (2010) Circ Res , vol.106 , pp. 1743-1752
    • Guo, T.1    Cornea, R.L.2    Huke, S.3    Camors, E.4    Yang, Y.5    Picht, E.6    Fruen, B.R.7    Bers, D.M.8
  • 83
    • 33644673205 scopus 로고    scopus 로고
    • Enhanced store overload-induced Ca2 + release and channel sensitivity to luminal Ca2 + activation are common defects of RyR2 mutations linked to ventricular tachycardia and sudden death
    • Jiang D, Wang R, Xiao B, Kong H, Hunt DJ, Choi P, Zhang L, &, Chen SR, (2005) Enhanced store overload-induced Ca2 + release and channel sensitivity to luminal Ca2 + activation are common defects of RyR2 mutations linked to ventricular tachycardia and sudden death. Circ Res 97, 1173-1181.
    • (2005) Circ Res , vol.97 , pp. 1173-1181
    • Jiang, D.1    Wang, R.2    Xiao, B.3    Kong, H.4    Hunt, D.J.5    Choi, P.6    Zhang, L.7    Chen, S.R.8
  • 85
    • 36849017856 scopus 로고    scopus 로고
    • Removal of FKBP12.6 does not alter the conductance and activation of the cardiac ryanodine receptor or the susceptibility to stress-induced ventricular arrhythmias
    • Xiao J, Tian X, Jones PP, Bolstad J, Kong H, Wang R, Zhang L, Duff HJ, Gillis AM, Fleischer S, et al,. (2007) Removal of FKBP12.6 does not alter the conductance and activation of the cardiac ryanodine receptor or the susceptibility to stress-induced ventricular arrhythmias. J Biol Chem 282, 34828-34838.
    • (2007) J Biol Chem , vol.282 , pp. 34828-34838
    • Xiao, J.1    Tian, X.2    Jones, P.P.3    Bolstad, J.4    Kong, H.5    Wang, R.6    Zhang, L.7    Duff, H.J.8    Gillis, A.M.9    Fleischer, S.10
  • 86
    • 70450252291 scopus 로고    scopus 로고
    • The voltage-gated calcium-channel beta subunit: More than just an accessory
    • Karunasekara Y, Dulhunty AF, &, Casarotto MG, (2009) The voltage-gated calcium-channel beta subunit: more than just an accessory. Eur Biophys J 39, 75-81.
    • (2009) Eur Biophys J , vol.39 , pp. 75-81
    • Karunasekara, Y.1    Dulhunty, A.F.2    Casarotto, M.G.3
  • 87
    • 0035826780 scopus 로고    scopus 로고
    • Excitation-contraction coupling is unaffected by drastic alteration of the sequence surrounding residues L720-L764 of the alpha 1S II-III loop
    • Wilkens CM, Kasielke N, Flucher BE, Beam KG, &, Grabner M, (2001) Excitation-contraction coupling is unaffected by drastic alteration of the sequence surrounding residues L720-L764 of the alpha 1S II-III loop. Proc Natl Acad Sci USA 98, 5892-5897.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5892-5897
    • Wilkens, C.M.1    Kasielke, N.2    Flucher, B.E.3    Beam, K.G.4    Grabner, M.5
  • 88
    • 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, (1990) Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling. Nature 346, 567-569.
    • (1990) Nature , vol.346 , pp. 567-569
    • Tanabe, T.1    Beam, K.G.2    Adams, B.A.3    Niidome, T.4    Numa, S.5
  • 89
    • 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, (2004) Structural requirements of the dihydropyridine receptor alpha1S II-III loop for skeletal-type excitation-contraction coupling. J Biol Chem 279, 4721-4728.
    • (2004) J Biol Chem , vol.279 , pp. 4721-4728
    • Kugler, G.1    Weiss, R.G.2    Flucher, B.E.3    Grabner, M.4
  • 90
    • 2642513903 scopus 로고    scopus 로고
    • The monoclonal antibody mAB 1A binds to the excitation-contraction coupling domain in the II-III loop of the skeletal muscle calcium channel alpha(1S) subunit
    • Kugler G, Grabner M, Platzer J, Striessnig J, &, Flucher BE, (2004) The monoclonal antibody mAB 1A binds to the excitation-contraction coupling domain in the II-III loop of the skeletal muscle calcium channel alpha(1S) subunit. Arch Biochem Biophys 427, 91-100.
    • (2004) Arch Biochem Biophys , vol.427 , pp. 91-100
    • Kugler, G.1    Grabner, M.2    Platzer, J.3    Striessnig, J.4    Flucher, B.E.5
  • 91
    • 23244460576 scopus 로고    scopus 로고
    • Multiple loops of the dihydropyridine receptor pore subunit are required for full-scale excitation-contraction coupling in skeletal muscle
    • Carbonneau L, Bhattacharya D, Sheridan DC, &, Coronado R, (2005) Multiple loops of the dihydropyridine receptor pore subunit are required for full-scale excitation-contraction coupling in skeletal muscle. Biophys J 89, 243-255.
    • (2005) Biophys J , vol.89 , pp. 243-255
    • Carbonneau, L.1    Bhattacharya, D.2    Sheridan, D.C.3    Coronado, R.4
  • 93
    • 84870385652 scopus 로고    scopus 로고
    • An alpha-helical C-terminal tail segment of the skeletal L-type Ca2 + channel beta1a subunit activates ryanodine receptor type 1 via a hydrophobic surface
    • Karunasekara Y, Rebbeck RT, Weaver LM, Board PG, Dulhunty AF, &, Casarotto MG, (2012) An alpha-helical C-terminal tail segment of the skeletal L-type Ca2 + channel beta1a subunit activates ryanodine receptor type 1 via a hydrophobic surface. FASEB J. 26, 5049-5059.
    • (2012) FASEB J , vol.26 , pp. 5049-5059
    • Karunasekara, Y.1    Rebbeck, R.T.2    Weaver, L.M.3    Board, P.G.4    Dulhunty, A.F.5    Casarotto, M.G.6
  • 94
    • 17944398302 scopus 로고
    • Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum
    • Fabiato A, (1983) Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum. Am J Physiol 245, C1-14.
    • (1983) Am J Physiol , vol.245
    • Fabiato, A.1
  • 95
    • 0014931506 scopus 로고
    • Calcium induced release of calcium from the sarcoplasmic reticulum of skinned skeletal muscle fibres
    • Endo M, Tanaka M, &, Ogawa Y, (1970) Calcium induced release of calcium from the sarcoplasmic reticulum of skinned skeletal muscle fibres. Nature 228, 34-36.
    • (1970) Nature , vol.228 , pp. 34-36
    • Endo, M.1    Tanaka, M.2    Ogawa, Y.3
  • 96
    • 0023113884 scopus 로고
    • Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle
    • Rios E, &, Brum G, (1987) Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle. Nature 325, 717-720.
    • (1987) Nature , vol.325 , pp. 717-720
    • Rios, E.1    Brum, G.2
  • 97
    • 0034053101 scopus 로고    scopus 로고
    • Pharmacological clues to calmodulin-mediated activation of skeletal ryanodine receptor using [3H]-ryanodine binding
    • Damiani E, &, Margreth A, (2000) Pharmacological clues to calmodulin-mediated activation of skeletal ryanodine receptor using [3H]-ryanodine binding. J Muscle Res Cell Motil 21, 1-8.
    • (2000) J Muscle Res Cell Motil , vol.21 , pp. 1-8
    • Damiani, E.1    Margreth, A.2
  • 99
    • 84865741854 scopus 로고    scopus 로고
    • Calmodulin-binding locations on the skeletal and cardiac ryanodine receptors
    • Huang X, Fruen B, Farrington DT, Wagenknecht T, &, Liu Z, (2012) Calmodulin-binding locations on the skeletal and cardiac ryanodine receptors. J Biol Chem 287, 30328-30335.
    • (2012) J Biol Chem , vol.287 , pp. 30328-30335
    • Huang, X.1    Fruen, B.2    Farrington, D.T.3    Wagenknecht, T.4    Liu, Z.5
  • 100
    • 0035933869 scopus 로고    scopus 로고
    • Identification of apocalmodulin and Ca2 + -calmodulin regulatory domain in skeletal muscle Ca2 + release channel, ryanodine receptor
    • Yamaguchi N, Xin C, &, Meissner G, (2001) Identification of apocalmodulin and Ca2 + -calmodulin regulatory domain in skeletal muscle Ca2 + release channel, ryanodine receptor. J Biol Chem 276, 22579-22585.
    • (2001) J Biol Chem , vol.276 , pp. 22579-22585
    • Yamaguchi, N.1    Xin, C.2    Meissner, G.3
  • 101
    • 0029161843 scopus 로고
    • Calcium dependent activation of skeletal muscle Ca2 + release channel (ryanodine receptor) by calmodulin
    • Buratti R, Prestipino G, Menegazzi P, Treves S, &, Zorzato F, (1995) Calcium dependent activation of skeletal muscle Ca2 + release channel (ryanodine receptor) by calmodulin. Biochem Biophys Res Commun 213, 1082-1090.
    • (1995) Biochem Biophys Res Commun , vol.213 , pp. 1082-1090
    • Buratti, R.1    Prestipino, G.2    Menegazzi, P.3    Treves, S.4    Zorzato, F.5
  • 102
    • 0029006108 scopus 로고
    • Calmodulin activation and inhibition of skeletal muscle Ca2 + release channel (ryanodine receptor)
    • Tripathy A, Xu L, Mann G, &, Meissner G, (1995) Calmodulin activation and inhibition of skeletal muscle Ca2 + release channel (ryanodine receptor). Biophys J 69, 106-119.
    • (1995) Biophys J , vol.69 , pp. 106-119
    • Tripathy, A.1    Xu, L.2    Mann, G.3    Meissner, G.4
  • 103
    • 0035827585 scopus 로고    scopus 로고
    • Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor)
    • Balshaw DM, Xu L, Yamaguchi N, Pasek DA, &, Meissner G, (2001) Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor). J Biol Chem 276, 20144-20153.
    • (2001) J Biol Chem , vol.276 , pp. 20144-20153
    • Balshaw, D.M.1    Xu, L.2    Yamaguchi, N.3    Pasek, D.A.4    Meissner, G.5
  • 104
    • 0038607565 scopus 로고    scopus 로고
    • Molecular basis of calmodulin binding to cardiac muscle Ca(2 +) release channel (ryanodine receptor)
    • Yamaguchi N, Xu L, Pasek DA, Evans KE, &, Meissner G, (2003) Molecular basis of calmodulin binding to cardiac muscle Ca(2 +) release channel (ryanodine receptor). J Biol Chem 278, 23480-23486.
    • (2003) J Biol Chem , vol.278 , pp. 23480-23486
    • Yamaguchi, N.1    Xu, L.2    Pasek, D.A.3    Evans, K.E.4    Meissner, G.5
  • 105
    • 0141668955 scopus 로고    scopus 로고
    • Transgenic overexpression of the Ca2 + -binding protein S100A1 in the heart leads to increased in vivo myocardial contractile performance
    • Most P, Remppis A, Pleger ST, Loffler E, Ehlermann P, Bernotat J, Kleuss C, Heierhorst J, Ruiz P, Witt H, et al,. (2003) Transgenic overexpression of the Ca2 + -binding protein S100A1 in the heart leads to increased in vivo myocardial contractile performance. J Biol Chem 278, 33809-33817.
    • (2003) J Biol Chem , vol.278 , pp. 33809-33817
    • Most, P.1    Remppis, A.2    Pleger, S.T.3    Loffler, E.4    Ehlermann, P.5    Bernotat, J.6    Kleuss, C.7    Heierhorst, J.8    Ruiz, P.9    Witt, H.10
  • 107
    • 33749246223 scopus 로고    scopus 로고
    • Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode
    • Maximciuc AA, Putkey JA, Shamoo Y, &, Mackenzie KR, (2006) Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode. Structure 14, 1547-1556.
    • (2006) Structure , vol.14 , pp. 1547-1556
    • Maximciuc, A.A.1    Putkey, J.A.2    Shamoo, Y.3    Mackenzie, K.R.4
  • 109
    • 80053308273 scopus 로고    scopus 로고
    • S100A1 and calmodulin regulation of ryanodine receptor in striated muscle
    • Prosser BL, Hernandez-Ochoa EO, &, Schneider MF, (2011) S100A1 and calmodulin regulation of ryanodine receptor in striated muscle. Cell Calcium 50, 323-331.
    • (2011) Cell Calcium , vol.50 , pp. 323-331
    • Prosser, B.L.1    Hernandez-Ochoa, E.O.2    Schneider, M.F.3
  • 110
    • 67650469595 scopus 로고    scopus 로고
    • Crystal structure of type i ryanodine receptor amino-terminal β-trefoil domain reveals a disease-associated mutation 'hot spot' loop
    • Amador FJ, Liu S, Ishiyama N, Plevin MJ, Wilson A, MacLennan DH, &, Ikura M, (2009) Crystal structure of type I ryanodine receptor amino-terminal β-trefoil domain reveals a disease-associated mutation 'hot spot' loop. Proc Natl Acad Sci USA 106, 11040-11044.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11040-11044
    • Amador, F.J.1    Liu, S.2    Ishiyama, N.3    Plevin, M.J.4    Wilson, A.5    Maclennan, D.H.6    Ikura, M.7
  • 111
    • 70350709897 scopus 로고    scopus 로고
    • Crystal structures of the N-terminal domains of cardiac and skeletal muscle ryanodine receptors: Insights into disease mutations
    • Lobo PA, &, Van Petegem F, (2009) Crystal structures of the N-terminal domains of cardiac and skeletal muscle ryanodine receptors: insights into disease mutations. Structure 17, 1505-1514.
    • (2009) Structure , vol.17 , pp. 1505-1514
    • Lobo, P.A.1    Van Petegem, F.2
  • 112
    • 79958173577 scopus 로고    scopus 로고
    • The deletion of exon 3 in the cardiac ryanodine receptor is rescued by beta strand switching
    • Lobo PA, Kimlicka L, Tung CC, &, Van Petegem F, (2011) The deletion of exon 3 in the cardiac ryanodine receptor is rescued by beta strand switching. Structure 19, 790-798.
    • (2011) Structure , vol.19 , pp. 790-798
    • Lobo, P.A.1    Kimlicka, L.2    Tung, C.C.3    Van Petegem, F.4
  • 114
    • 84863513714 scopus 로고    scopus 로고
    • Disease mutations in the ryanodine receptor central region: Crystal structures of a phosphorylation hot spot domain
    • Yuchi Z, Lau K, &, Van Petegem F, (2012) Disease mutations in the ryanodine receptor central region: crystal structures of a phosphorylation hot spot domain. Structure 20, 1201-1211.
    • (2012) Structure , vol.20 , pp. 1201-1211
    • Yuchi, Z.1    Lau, K.2    Van Petegem, F.3
  • 115
    • 0032488899 scopus 로고    scopus 로고
    • Definition of optimal substrate recognition motifs of Ca2 + -calmodulin-dependent protein kinases IV and II reveals shared and distinctive features
    • White RR, Kwon YG, Taing M, Lawrence DS, &, Edelman AM, (1998) Definition of optimal substrate recognition motifs of Ca2 + -calmodulin- dependent protein kinases IV and II reveals shared and distinctive features. J Biol Chem 273, 3166-3172.
    • (1998) J Biol Chem , vol.273 , pp. 3166-3172
    • White, R.R.1    Kwon, Y.G.2    Taing, M.3    Lawrence, D.S.4    Edelman, A.M.5
  • 116
    • 0030974256 scopus 로고    scopus 로고
    • SPRY domains in ryanodine receptors (Ca(2 +)-release channels)
    • Ponting C, Schultz J, &, Bork P, (1997) SPRY domains in ryanodine receptors (Ca(2 +)-release channels). Trends Biochem Sci 22, 193-194.
    • (1997) Trends Biochem Sci , vol.22 , pp. 193-194
    • Ponting, C.1    Schultz, J.2    Bork, P.3
  • 117
    • 70450247255 scopus 로고    scopus 로고
    • Ubiquitous SPRY domains and their role in the skeletal type ryanodine receptor
    • Tae H, Casarotto MG, &, Dulhunty AF, (2009) Ubiquitous SPRY domains and their role in the skeletal type ryanodine receptor. Eur Biophys J 39, 51-59.
    • (2009) Eur Biophys J , vol.39 , pp. 51-59
    • Tae, H.1    Casarotto, M.G.2    Dulhunty, A.F.3
  • 118
    • 33750087518 scopus 로고    scopus 로고
    • Structural and functional characterization of interactions between the dihydropyridine receptor II-III loop and the ryanodine receptor
    • Casarotto MG, Cui Y, Karunasekara Y, Harvey PJ, Norris N, Board PG, &, Dulhunty AF, (2006) Structural and functional characterization of interactions between the dihydropyridine receptor II-III loop and the ryanodine receptor. Clin Exp Pharmacol Physiol 33, 1114-1117.
    • (2006) Clin Exp Pharmacol Physiol , vol.33 , pp. 1114-1117
    • Casarotto, M.G.1    Cui, Y.2    Karunasekara, Y.3    Harvey, P.J.4    Norris, N.5    Board, P.G.6    Dulhunty, A.F.7
  • 119
    • 33846323688 scopus 로고    scopus 로고
    • A variably spliced region in the type 1 ryanodine receptor may participate in an inter-domain interaction
    • Kimura T, Pace SM, Wei L, Beard NA, Dirksen RT, &, Dulhunty AF, (2007) A variably spliced region in the type 1 ryanodine receptor may participate in an inter-domain interaction. Biochem J 401, 317-324.
    • (2007) Biochem J , vol.401 , pp. 317-324
    • Kimura, T.1    Pace, S.M.2    Wei, L.3    Beard, N.A.4    Dirksen, R.T.5    Dulhunty, A.F.6
  • 120
    • 58149284005 scopus 로고    scopus 로고
    • A dihydropyridine receptor alpha1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor
    • Cui Y, Tae HS, Norris NC, Karunasekara Y, Pouliquin P, Board PG, Dulhunty AF, &, Casarotto MG, (2009) A dihydropyridine receptor alpha1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor. Int J Biochem Cell Biol 41, 677-686.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 677-686
    • Cui, Y.1    Tae, H.S.2    Norris, N.C.3    Karunasekara, Y.4    Pouliquin, P.5    Board, P.G.6    Dulhunty, A.F.7    Casarotto, M.G.8
  • 121
    • 79959352257 scopus 로고    scopus 로고
    • Cyclization of the intrinsically disordered alpha1S dihydropyridine receptor II-III loop enhances secondary structure and in vitro function
    • Tae HS, Cui Y, Karunasekara Y, Board PG, Dulhunty AF, &, Casarotto MG, (2011) Cyclization of the intrinsically disordered alpha1S dihydropyridine receptor II-III loop enhances secondary structure and in vitro function. J Biol Chem 286, 22589-22599.
    • (2011) J Biol Chem , vol.286 , pp. 22589-22599
    • Tae, H.S.1    Cui, Y.2    Karunasekara, Y.3    Board, P.G.4    Dulhunty, A.F.5    Casarotto, M.G.6
  • 122
    • 13444278746 scopus 로고    scopus 로고
    • The recombinant dihydropyridine receptor II-III loop and partly structured 'C' region peptides modify cardiac ryanodine receptor activity
    • Dulhunty AF, Karunasekara Y, Curtis SM, Harvey PJ, Board PG, &, Casarotto MG, (2005) The recombinant dihydropyridine receptor II-III loop and partly structured 'C' region peptides modify cardiac ryanodine receptor activity. Biochem J 385, 803-813.
    • (2005) Biochem J , vol.385 , pp. 803-813
    • Dulhunty, A.F.1    Karunasekara, Y.2    Curtis, S.M.3    Harvey, P.J.4    Board, P.G.5    Casarotto, M.G.6
  • 123
    • 0028352089 scopus 로고
    • Activation of the skeletal muscle calcium release channel by a cytoplasmic loop of the dihydropyridine receptor
    • Lu X, Xu L, &, Meissner G, (1994) Activation of the skeletal muscle calcium release channel by a cytoplasmic loop of the dihydropyridine receptor. J Biol Chem 269, 6511-6516.
    • (1994) J Biol Chem , vol.269 , pp. 6511-6516
    • Lu, X.1    Xu, L.2    Meissner, G.3
  • 124
    • 0034859251 scopus 로고    scopus 로고
    • Two domains in dihydropyridine receptor activate the skeletal muscle Ca(2 +) release channel
    • Stange M, Tripathy A, &, Meissner G, (2001) Two domains in dihydropyridine receptor activate the skeletal muscle Ca(2 +) release channel. Biophys J 81, 1419-1429.
    • (2001) Biophys J , vol.81 , pp. 1419-1429
    • Stange, M.1    Tripathy, A.2    Meissner, G.3
  • 125
    • 79951820580 scopus 로고    scopus 로고
    • The beta(1a) subunit of the skeletal DHPR binds to skeletal RyR1 and activates the channel via its 35-residue C-terminal tail
    • Rebbeck RT, Karunasekara Y, Gallant EM, Board PG, Beard NA, Casarotto MG, &, Dulhunty AF, (2011) The beta(1a) subunit of the skeletal DHPR binds to skeletal RyR1 and activates the channel via its 35-residue C-terminal tail. Biophys J 100, 922-930.
    • (2011) Biophys J , vol.100 , pp. 922-930
    • Rebbeck, R.T.1    Karunasekara, Y.2    Gallant, E.M.3    Board, P.G.4    Beard, N.A.5    Casarotto, M.G.6    Dulhunty, A.F.7
  • 126
    • 4143124295 scopus 로고    scopus 로고
    • Involvement of a heptad repeat in the carboxyl terminus of the dihydropyridine receptor beta1a subunit in the mechanism of excitation- contraction coupling in skeletal muscle
    • Sheridan DC, Cheng W, Carbonneau L, Ahern CA, &, Coronado R, (2004) Involvement of a heptad repeat in the carboxyl terminus of the dihydropyridine receptor beta1a subunit in the mechanism of excitation-contraction coupling in skeletal muscle. Biophys J 87, 929-942.
    • (2004) Biophys J , vol.87 , pp. 929-942
    • Sheridan, D.C.1    Cheng, W.2    Carbonneau, L.3    Ahern, C.A.4    Coronado, R.5
  • 127
    • 0032574727 scopus 로고    scopus 로고
    • Association of calcium channel alpha1S and beta1a subunits is required for the targeting of beta1a but not of alpha1S into skeletal muscle triads
    • Neuhuber B, Gerster U, Doring F, Glossmann H, Tanabe T, &, Flucher BE, (1998) Association of calcium channel alpha1S and beta1a subunits is required for the targeting of beta1a but not of alpha1S into skeletal muscle triads. Proc Natl Acad Sci USA 95, 5015-5020.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5015-5020
    • Neuhuber, B.1    Gerster, U.2    Doring, F.3    Glossmann, H.4    Tanabe, T.5    Flucher, B.E.6
  • 128
    • 33645647478 scopus 로고    scopus 로고
    • Organization of calcium channel beta1a subunits in triad junctions in skeletal muscle
    • Leuranguer V, Papadopoulos S, &, Beam KG, (2006) Organization of calcium channel beta1a subunits in triad junctions in skeletal muscle. J Biol Chem 281, 3521-3527.
    • (2006) J Biol Chem , vol.281 , pp. 3521-3527
    • Leuranguer, V.1    Papadopoulos, S.2    Beam, K.G.3
  • 129
    • 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 AP, Fleischer S, &, Wagenknecht T, (1994) Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle. J Cell Biol 127, 411-423.
    • (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
  • 130
    • 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, (1995) Electron cryomicroscopy and angular reconstitution used to visualize the skeletal muscle calcium release channel. Nat Struct Biol 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
  • 132
    • 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, (2005) Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM. Nat Struct Mol Biol 12, 539-544.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 539-544
    • Samso, M.1    Wagenknecht, T.2    Allen, P.D.3
  • 134
    • 67649637588 scopus 로고    scopus 로고
    • Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating
    • Samso M, Feng W, Pessah IN, &, Allen PD, (2009) Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating. PLoS Biol 7, e85.
    • (2009) PLoS Biol , vol.7
    • Samso, M.1    Feng, W.2    Pessah, I.N.3    Allen, P.D.4
  • 135
    • 79960625443 scopus 로고    scopus 로고
    • The structural biology of ryanodine receptors
    • Kimlicka L, &, Van Petegem F, (2011) The structural biology of ryanodine receptors. Sci China Life Sci 54, 712-724.
    • (2011) Sci China Life Sci , vol.54 , pp. 712-724
    • Kimlicka, L.1    Van Petegem, F.2
  • 136
    • 84862231309 scopus 로고    scopus 로고
    • FRET-based localization of fluorescent protein insertions within the ryanodine receptor type 1
    • Raina SA, Tsai J, Samso M, &, Fessenden JD, (2012) FRET-based localization of fluorescent protein insertions within the ryanodine receptor type 1. PLoS One 7, e38594.
    • (2012) PLoS One , vol.7
    • Raina, S.A.1    Tsai, J.2    Samso, M.3    Fessenden, J.D.4
  • 138
    • 41149098918 scopus 로고    scopus 로고
    • Ryanodine receptor arrays: Not just a pretty pattern?
    • Yin CC, D'Cruz LG, &, Lai FA, (2008) Ryanodine receptor arrays: not just a pretty pattern? Trends Cell Biol 18, 149-156.
    • (2008) Trends Cell Biol , vol.18 , pp. 149-156
    • Yin, C.C.1    D'Cruz, L.G.2    Lai, F.A.3
  • 139
    • 0034281991 scopus 로고    scopus 로고
    • Intrinsic lattice formation by the ryanodine receptor calcium-release channel
    • Yin CC, &, Lai FA, (2000) Intrinsic lattice formation by the ryanodine receptor calcium-release channel. Nat Cell Biol 2, 669-671.
    • (2000) Nat Cell Biol , vol.2 , pp. 669-671
    • Yin, C.C.1    Lai, F.A.2
  • 141
    • 79952546947 scopus 로고    scopus 로고
    • Common allosteric mechanisms between ryanodine and inositol-1,4,5- trisphosphate receptors
    • Yuchi Z, &, Van Petegem F, (2011) Common allosteric mechanisms between ryanodine and inositol-1,4,5-trisphosphate receptors. Channels (Austin) 5, 120-123.
    • (2011) Channels (Austin) , vol.5 , pp. 120-123
    • Yuchi, Z.1    Van Petegem, F.2
  • 142
    • 84857501714 scopus 로고    scopus 로고
    • The IP3 receptor/Ca2+ channel and its cellular function
    • Mikoshiba K, (2007) The IP3 receptor/Ca2+ channel and its cellular function. Biochem Soc Symp 74, 9-22.
    • (2007) Biochem Soc Symp , vol.74 , pp. 9-22
    • Mikoshiba, K.1
  • 143
    • 0034675855 scopus 로고    scopus 로고
    • Direct association of ligand-binding and pore domains in homo- and heterotetrameric inositol 1,4,5-trisphosphate receptors
    • Boehning D, &, Joseph SK, (2000) Direct association of ligand-binding and pore domains in homo- and heterotetrameric inositol 1,4,5-trisphosphate receptors. EMBO J 19, 5450-5459.
    • (2000) EMBO J , vol.19 , pp. 5450-5459
    • Boehning, D.1    Joseph, S.K.2
  • 144
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC, (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32, 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 145
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, &, Kumar S, (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28, 2731-2739.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6


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