메뉴 건너뛰기




Volumn 27, Issue 6, 2012, Pages 331-342

Themes and variations in ER/SR calcium release channels: Structure and function

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM CHANNEL; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; RYANODINE RECEPTOR;

EID: 84870791465     PISSN: 15489213     EISSN: 15489221     Source Type: Journal    
DOI: 10.1152/physiol.00013.2012     Document Type: Review
Times cited : (26)

References (141)
  • 1
    • 67650469595 scopus 로고    scopus 로고
    • Crystal structure of type I ryanodine receptor amino-terminal beta-trefoil domain reveals a disease-associated mutation "hot spot" loop
    • Amador FJ, Liu S, Ishiyama N, Plevin MJ, Wilson A, MacLennan DH, Ikura M. Crystal structure of type I ryanodine receptor amino-terminal beta-trefoil domain reveals a disease-associated mutation "hot spot" loop. Proc Natl Acad Sci USA 106: 11040-11044, 2009.
    • (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
  • 2
    • 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. Functional effects of central core disease mutations in the cytoplasmic region of the skeletal muscle ryanodine receptor. J Gen Physiol 118: 277-290, 2001.
    • (2001) J Gen Physiol , vol.118 , pp. 277-290
    • Avila, G.1    Dirksen, R.T.2
  • 3
    • 0033607777 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptors are strongly expressed in the nervous system, pharynx, intestine, gonad and excretory cell of Caenorhabditis elegans and are encoded by a single gene (itr-1)
    • Baylis H. Inositol 1,4,5-trisphosphate receptors are strongly expressed in the nervous system, pharynx, intestine, gonad and excretory cell of Caenorhabditis elegans and are encoded by a single gene (itr-1). J Mol Biol 294: 467-476, 1999.
    • (1999) J Mol Biol , vol.294 , pp. 467-476
    • Baylis, H.1
  • 7
    • 0026432666 scopus 로고
    • Bell-shaped calciumresponse curves of Ins(1,4,5)P3-and calcium-gated channels from endoplasmic reticulum of cerebellum
    • Bezprozvanny I, Watras J, Ehrlich BE. Bell-shaped calciumresponse curves of Ins(1,4,5)P3-and calcium-gated channels from endoplasmic reticulum of cerebellum. Nature 351: 751-754, 1991.
    • (1991) Nature , vol.351 , pp. 751-754
    • Bezprozvanny, I.1    Watras, J.2    Ehrlich, B.E.3
  • 9
    • 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. 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.
    • (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
  • 11
    • 12344249857 scopus 로고    scopus 로고
    • Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor
    • Bosanac I, Yamazaki H, Matsu-Ura T, Michikawa T, Mikoshiba K, Ikura M. Crystal structure of the ligand binding suppressor domain of type 1 inositol 1,4,5-trisphosphate receptor. Mol Cell 17: 193-203, 2005.
    • (2005) Mol Cell , vol.17 , pp. 193-203
    • Bosanac, I.1    Yamazaki, H.2    Matsu-Ura, T.3    Michikawa, T.4    Mikoshiba, K.5    Ikura, M.6
  • 13
    • 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. 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.
    • (2011) Anesth Analg , vol.112 , pp. 1115-1123
    • Brandom, B.W.1    Larach, M.G.2    Chen, M.S.3    Young, M.C.4
  • 14
    • 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. Epithelial inositol 1,4,5-trisphosphate receptors. Multiplicity of localization, solubility, and isoforms. J Biol Chem 269: 23694-23699, 1994.
    • (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
  • 15
    • 45849109876 scopus 로고    scopus 로고
    • 2+ signaling "toolkit" at the origin of metazoa
    • 2+ signaling "toolkit" at the origin of metazoa. Mol Biol Evol 25: 1357-1361, 2008.
    • (2008) Mol Biol Evol , vol.25 , pp. 1357-1361
    • Cai, X.1
  • 16
    • 84857686131 scopus 로고    scopus 로고
    • 2+ signaling machinery in early animal and fungal evolution
    • 2+ signaling machinery in early animal and fungal evolution. Mol Biol Evol 29: 91-100, 2011.
    • (2011) Mol Biol Evol , vol.29 , pp. 91-100
    • Cai, X.1    Clapham, D.E.2
  • 17
    • 0028960454 scopus 로고
    • 2+ mobilization pathways at the vacuolar membrane of Candida albicans
    • 2+ mobilization pathways at the vacuolar membrane of Candida albicans. J Biol Chem 270: 7272-7280, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 7272-7280
    • Calvert, C.M.1    Sanders, D.2
  • 18
    • 70349568135 scopus 로고    scopus 로고
    • The relationship between exertional heat illness, exertional rhabdomyolysis, and malignant hyperthermia
    • Capacchione JF, Muldoon SM. The relationship between exertional heat illness, exertional rhabdomyolysis, and malignant hyperthermia. Anesth Analg 109: 1065-1069, 2009.
    • (2009) Anesth Analg , vol.109 , pp. 1065-1069
    • Capacchione, J.F.1    Muldoon, S.M.2
  • 19
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • Castresana J. Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis. Mol Biol Evol 17: 540-552, 2000.
    • (2000) Mol Biol Evol , vol.17 , pp. 540-552
    • Castresana, J.1
  • 21
  • 22
    • 0024338088 scopus 로고
    • Inositol trisphosphate induces calcium release from Neurospora crassa vacuoles
    • Cornelius G, Gebauer G, Techel D. Inositol trisphosphate induces calcium release from Neurospora crassa vacuoles. Biochem Biophys Res Commun 162: 852-856, 1989.
    • (1989) Biochem Biophys Res Commun , vol.162 , pp. 852-856
    • Cornelius, G.1    Gebauer, G.2    Techel, D.3
  • 23
    • 0034064916 scopus 로고    scopus 로고
    • Arrhythmogenic right ventricular cardiomyopathy: Diagnosis, prognosis, and treatment
    • Corrado D, Basso C, Thiene G. Arrhythmogenic right ventricular cardiomyopathy: diagnosis, prognosis, and treatment. Heart 83: 588-595, 2000.
    • (2000) Heart , vol.83 , pp. 588-595
    • Corrado, D.1    Basso, C.2    Thiene, G.3
  • 24
    • 0037386525 scopus 로고    scopus 로고
    • Domain organization of the type 1 inositol 1,4,5-trisphosphate receptor as revealed by single-particle analysis
    • da Fonseca PC, Morris SA, Nerou EP, Taylor CW, Morris EP. Domain organization of the type 1 inositol 1,4,5-trisphosphate receptor as revealed by single-particle analysis. Proc Natl Acad Sci USA 100: 3936-3941, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3936-3941
    • da Fonseca, P.C.1    Morris, S.A.2    Nerou, E.P.3    Taylor, C.W.4    Morris, E.P.5
  • 25
    • 1642358986 scopus 로고    scopus 로고
    • Catecholaminergic polymorphic ventricular tachycardia: Successful emergency treatment with intravenous propranolol
    • De Rosa G, Delogu AB, Piastra M, Chiaretti A, Bloise R, Priori SG. Catecholaminergic polymorphic ventricular tachycardia: successful emergency treatment with intravenous propranolol. Pediatr Emerg Care 20: 175-177, 2004.
    • (2004) Pediatr Emerg Care , vol.20 , pp. 175-177
    • de Rosa, G.1    Delogu, A.B.2    Piastra, M.3    Chiaretti, A.4    Bloise, R.5    Priori, S.G.6
  • 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. 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.
    • (1994) FEBS Lett , vol.347 , pp. 69-72
    • de Smedt, F.1    Verjans, B.2    Mailleux, P.3    Erneux, C.4
  • 27
    • 0028129099 scopus 로고
    • Determination of relative amounts of inositol trisphosphate receptor mRNA isoforms by ratio polymerase chain reaction
    • De Smedt H, Missiaen L, Parys JB, Bootman MD, Mertens L, Van Den Bosch L, Casteels R. Determination of relative amounts of inositol trisphosphate receptor mRNA isoforms by ratio polymerase chain reaction. J Biol Chem 269: 21691-21698, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 21691-21698
    • de Smedt, H.1    Missiaen, L.2    Parys, J.B.3    Bootman, M.D.4    Mertens, L.5    van den Bosch, L.6    Casteels, R.7
  • 32
    • 0037964192 scopus 로고    scopus 로고
    • A missense mutation in the CASQ2 gene is associated with autosomal- recessive catecholamine-induced polymorphic ventricular tachycardia
    • Eldar M, Pras E, Lahat H. A missense mutation in the CASQ2 gene is associated with autosomal- recessive catecholamine-induced polymorphic ventricular tachycardia. Trends Cardiovasc Med 13: 148-151, 2003.
    • (2003) Trends Cardiovasc Med , vol.13 , pp. 148-151
    • Eldar, M.1    Pras, E.2    Lahat, H.3
  • 33
    • 0014931506 scopus 로고
    • Calcium induced release of calcium from the sarcoplasmic reticulum of skinned skeletal muscle fibres
    • Endo M, Tanaka M, Ogawa Y. Calcium induced release of calcium from the sarcoplasmic reticulum of skinned skeletal muscle fibres. Nature 228: 34-36, 1970.
    • (1970) Nature , vol.228 , pp. 34-36
    • Endo, M.1    Tanaka, M.2    Ogawa, Y.3
  • 34
    • 17944398302 scopus 로고
    • Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum
    • Fabiato A. Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum. Am J Physiol Cell Physiol 245: C1-C14, 1983.
    • (1983) Am J Physiol Cell Physiol , vol.245
    • Fabiato, A.1
  • 35
    • 0025890114 scopus 로고
    • Calcium as a coagonist of inositol 1,4,5-trisphosphate-induced calcium release
    • Finch E, Turner T, Goldin S. Calcium as a coagonist of inositol 1,4,5-trisphosphate-induced calcium release. Science 252: 443-446, 1991.
    • (1991) Science , vol.252 , pp. 443-446
    • Finch, E.1    Turner, T.2    Goldin, S.3
  • 38
    • 0024432232 scopus 로고
    • Primary structure and functional expression of the inositol 1,4,5-trisphosphate-binding protein P400
    • Furuichi T, Yoshikawa S, Miyawaki A, Wada K, Maeda N, Mikoshiba K. Primary structure and functional expression of the inositol 1,4,5-trisphosphate-binding protein P400. Nature 342: 32-38, 1989.
    • (1989) Nature , vol.342 , pp. 32-38
    • Furuichi, T.1    Yoshikawa, S.2    Miyawaki, A.3    Wada, K.4    Maeda, N.5    Mikoshiba, K.6
  • 40
    • 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. 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
  • 41
    • 1942423621 scopus 로고    scopus 로고
    • The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium
    • Gyorke I, Hester N, Jones LR, Gyorke S. The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium. Biophys J 86: 2121-2128, 2004.
    • (2004) Biophys J , vol.86 , pp. 2121-2128
    • Gyorke, I.1    Hester, N.2    Jones, L.R.3    Gyorke, S.4
  • 42
    • 0026471048 scopus 로고
    • Primary structure and distribution of a novel ryanodine receptor/calcium release channel from rabbit brain
    • Hakamata Y, Nakai J, Takeshima H, 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
  • 43
    • 0037077304 scopus 로고    scopus 로고
    • Two-state conformational changes in inositol 1,4,5-trisphosphate receptor regulated by calcium
    • Hamada K, Miyata T, Mayanagi K, Hirota J, Mikoshiba K. Two-state conformational changes in inositol 1,4,5-trisphosphate receptor regulated by calcium. J Biol Chem 277: 21115-21118, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 21115-21118
    • Hamada, K.1    Miyata, T.2    Mayanagi, K.3    Hirota, J.4    Mikoshiba, K.5
  • 44
    • 0346732272 scopus 로고    scopus 로고
    • Three-dimensional rearrangements within inositol 1,4,5- trisphosphate receptor by calcium
    • Hamada K, Terauchi A, Mikoshiba K. Three-dimensional rearrangements within inositol 1,4,5- trisphosphate receptor by calcium. J Biol Chem 278: 52881-52889, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 52881-52889
    • Hamada, K.1    Terauchi, A.2    Mikoshiba, K.3
  • 45
    • 77749323194 scopus 로고    scopus 로고
    • High prevalence of exercise-induced arrhythmias in catecholaminergic polymorphic ventricular tachycardia mutation- positive family members diagnosed by cascade genetic screening
    • Haugaa KH, Leren IS, Berge KE, Bathen J, Loennechen JP, Anfinsen OG, Fruh A, Edvardsen T, Kongsgard E, Leren TP, Amlie JP. High prevalence of exercise-induced arrhythmias in catecholaminergic polymorphic ventricular tachycardia mutation- positive family members diagnosed by cascade genetic screening. Europace 12: 417-423, 2010.
    • (2010) Europace , vol.12 , pp. 417-423
    • Haugaa, K.H.1    Leren, I.S.2    Berge, K.E.3    Bathen, J.4    Loennechen, J.P.5    Anfinsen, O.G.6    Fruh, A.7    Edvardsen, T.8    Kongsgard, E.9    Leren, T.P.10    Amlie, J.P.11
  • 47
    • 0025887569 scopus 로고
    • Evidence for related myopathies in exertional heat stroke and malignant hyperthermia
    • Hopkins PM, Ellis FR, Halsall PJ. Evidence for related myopathies in exertional heat stroke and malignant hyperthermia. Lancet 338: 1491-1492, 1991.
    • (1991) Lancet , vol.338 , pp. 1491-1492
    • Hopkins, P.M.1    Ellis, F.R.2    Halsall, P.J.3
  • 51
    • 34250362355 scopus 로고    scopus 로고
    • Molecular basis of the isoform-specific ligand-binding affinity of inositol 1,4,5-trisphosphate receptors
    • Iwai M, Michikawa T, Bosanac I, Ikura M, Mikoshiba K. Molecular basis of the isoform-specific ligand-binding affinity of inositol 1,4,5-trisphosphate receptors. J Biol Chem 282: 12755-12764, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 12755-12764
    • Iwai, M.1    Michikawa, T.2    Bosanac, I.3    Ikura, M.4    Mikoshiba, K.5
  • 53
    • 0037099206 scopus 로고    scopus 로고
    • Three-dimensional structure of the type 1 inositol 1,4,5-trisphosphate receptor at 24 A resolution
    • Jiang QX, Thrower EC, Chester DW, Ehrlich BE, Sigworth FJ. Three-dimensional structure of the type 1 inositol 1,4,5-trisphosphate receptor at 24 A resolution. EMBO J 21: 3575-3581, 2002.
    • (2002) EMBO J , vol.21 , pp. 3575-3581
    • Jiang, Q.X.1    Thrower, E.C.2    Chester, D.W.3    Ehrlich, B.E.4    Sigworth, F.J.5
  • 58
    • 77955019084 scopus 로고    scopus 로고
    • Parallelization of the MAFFT multiple sequence alignment program
    • Katoh K, Toh H. Parallelization of the MAFFT multiple sequence alignment program. Bioinformatics 26: 1899-1900, 2010.
    • (2010) Bioinformatics , vol.26 , pp. 1899-1900
    • Katoh, K.1    Toh, H.2
  • 60
    • 1842844355 scopus 로고    scopus 로고
    • Dantrolene: A review of its pharmacology, therapeutic use and new developments
    • Krause T, Gerbershagen MU, Fiege M, Weisshorn R, Wappler F. Dantrolene: a review of its pharmacology, therapeutic use and new developments. Anaesthesia 59: 364-373, 2004.
    • (2004) Anaesthesia , vol.59 , pp. 364-373
    • Krause, T.1    Gerbershagen, M.U.2    Fiege, M.3    Weisshorn, R.4    Wappler, F.5
  • 61
    • 33749403485 scopus 로고    scopus 로고
    • An Ins(1,4,5)P3 receptor in Paramecium is associated with the osmoregulatory system
    • Ladenburger EM, Korn I, Kasielke N, Wassmer T, Plattner H. An Ins(1,4,5)P3 receptor in Paramecium is associated with the osmoregulatory system. J Cell Sci 119: 3705-3717, 2006.
    • (2006) J Cell Sci , vol.119 , pp. 3705-3717
    • Ladenburger, E.M.1    Korn, I.2    Kasielke, N.3    Wassmer, T.4    Plattner, H.5
  • 63
    • 0242609817 scopus 로고    scopus 로고
    • Molecular genetics of exercise-induced polymorphic ventricular tachycardia: Identification of three novel cardiac ryanodine receptor mutations and two common calsequestrin 2 amino-acid polymorphisms
    • Laitinen PJ, Swan H, Kontula K. Molecular genetics of exercise-induced polymorphic ventricular tachycardia: identification of three novel cardiac ryanodine receptor mutations and two common calsequestrin 2 amino-acid polymorphisms. Eur J Hum Genet 11: 888-891, 2003.
    • (2003) Eur J Hum Genet , vol.11 , pp. 888-891
    • Laitinen, P.J.1    Swan, H.2    Kontula, K.3
  • 64
    • 84859907793 scopus 로고    scopus 로고
    • Ryanodine receptor physiology and its role in disease
    • Lanner JT. Ryanodine receptor physiology and its role in disease. Adv Exp Med Biol 740: 217-234, 2012.
    • (2012) Adv Exp Med Biol , vol.740 , pp. 217-234
    • Lanner, J.T.1
  • 66
    • 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. 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.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 1172-1174
    • Lin, C.C.1    Baek, K.2    Lu, Z.3
  • 67
    • 78650819612 scopus 로고    scopus 로고
    • Calmodulin kinase II inhibition prevents arrhythmias in RyR2(R4496C /) mice with catecholaminergic polymorphic ventricular tachycardia
    • Liu N, Ruan Y, Denegri M, Bachetti T, Li Y, Colombi B, Napolitano C, Coetzee WA, Priori SG. Calmodulin kinase II inhibition prevents arrhythmias in RyR2(R4496C /) mice with catecholaminergic polymorphic ventricular tachycardia. J Mol Cell Cardiol 50: 214-222, 2011.
    • (2011) J Mol Cell Cardiol , vol.50 , pp. 214-222
    • Liu, N.1    Ruan, Y.2    Denegri, M.3    Bachetti, T.4    Li, Y.5    Colombi, B.6    Napolitano, C.7    Coetzee, W.A.8    Priori, S.G.9
  • 68
    • 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. The deletion of exon 3 in the cardiac ryanodine receptor is rescued by beta strand switching. Structure 19: 790-798, 2011.
    • (2011) Structure , vol.19 , pp. 790-798
    • Lobo, P.A.1    Kimlicka, L.2    Tung, C.C.3    van Petegem, F.4
  • 69
    • 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. Crystal structures of the N-terminal domains of cardiac and skeletal muscle ryanodine receptors: insights into disease mutations. Structure 17: 1505-1514, 2009.
    • (2009) Structure , vol.17 , pp. 1505-1514
    • Lobo, P.A.1    van Petegem, F.2
  • 72
    • 84859917357 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels: An evolutionary perspective
    • Mackrill JJ. Ryanodine receptor calcium release channels: an evolutionary perspective. Adv Exp Med Biol 740: 159-182, 2012.
    • (2012) Adv Exp Med Biol , vol.740 , pp. 159-182
    • Mackrill, J.J.1
  • 73
    • 0028096222 scopus 로고
    • Primary structure, ligand binding, and localization of the human type 3 inositol 1,4,5-trisphosphate receptor expressed in intestinal epithelium
    • Maranto AR. Primary structure, ligand binding, and localization of the human type 3 inositol 1,4,5-trisphosphate receptor expressed in intestinal epithelium. J Biol Chem 269: 1222-1230, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 1222-1230
    • Maranto, A.R.1
  • 74
    • 0036132550 scopus 로고    scopus 로고
    • Involvement of the cardiac ryanodine receptor/calcium release channel in catecholaminergic polymorphic ventricular tachycardia
    • Marks AR, Priori S, Memmi M, Kontula K, Laitinen PJ. Involvement of the cardiac ryanodine receptor/calcium release channel in catecholaminergic polymorphic ventricular tachycardia. J Cell Physiol 190: 1-6, 2002.
    • (2002) J Cell Physiol , vol.190 , pp. 1-6
    • Marks, A.R.1    Priori, S.2    Memmi, M.3    Kontula, K.4    Laitinen, P.J.5
  • 75
    • 0024372718 scopus 로고
    • Molecular cloning and characterization of the ryanodine receptor/junctional channel complex cDNA from skeletal muscle sarcoplasmic reticulum
    • Marks AR, Tempst P, Hwang KS, Taubman MB, Inui M, Chadwick C, Fleischer S, 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
  • 76
    • 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. Unc-68 encodes a ryanodine receptor involved in regulating C. elegans body-wall muscle contraction. J Cell Biol 134: 885-893, 1996.
    • (1996) J Cell Biol , vol.134 , pp. 885-893
    • Maryon, E.B.1    Coronado, R.2    Anderson, P.3
  • 78
    • 33747380269 scopus 로고    scopus 로고
    • Cytosolic inositol 1,4,5- trisphosphate dynamics during intracellular calcium oscillations in living cells
    • Matsu-ura T, Michikawa T, Inoue T, Miyawaki A, Yoshida M, Mikoshiba K. Cytosolic inositol 1,4,5- trisphosphate dynamics during intracellular calcium oscillations in living cells. J Cell Biol 173: 755-765, 2006.
    • (2006) J Cell Biol , vol.173 , pp. 755-765
    • Matsu-Ura, T.1    Michikawa, T.2    Inoue, T.3    Miyawaki, A.4    Yoshida, M.5    Mikoshiba, K.6
  • 79
    • 71849090068 scopus 로고    scopus 로고
    • The RYR2-encoded ryanodine receptor/calcium release channel in patients diagnosed previously with either catecholaminergic polymorphic ventricular tachycardia or genotype negative, exercise-induced long QT syndrome: A comprehensive open reading frame mutational analysis
    • Medeiros-Domingo A, Bhuiyan ZA, Tester DJ, Hofman N, Bikker H, van Tintelen JP, Mannens MM, Wilde AA, Ackerman MJ. The RYR2-encoded ryanodine receptor/calcium release channel in patients diagnosed previously with either catecholaminergic polymorphic ventricular tachycardia or genotype negative, exercise-induced long QT syndrome: a comprehensive open reading frame mutational analysis. J Am Coll Cardiol 54: 2065-2074, 2009.
    • (2009) J Am Coll Cardiol , vol.54 , pp. 2065-2074
    • Medeiros-Domingo, A.1    Bhuiyan, Z.A.2    Tester, D.J.3    Hofman, N.4    Bikker, H.5    van Tintelen, J.P.6    Mannens, M.M.7    Wilde, A.A.8    Ackerman, M.J.9
  • 80
    • 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
  • 81
    • 0024449839 scopus 로고
    • Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor
    • Mignery GA, Südhof TC, Takei K, De Camilli P. Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor. Nature 342: 192-195, 1989.
    • (1989) Nature , vol.342 , pp. 192-195
    • Mignery, G.A.1    Südhof, T.C.2    Takei, K.3    de Camilli, P.4
  • 83
    • 46849084325 scopus 로고    scopus 로고
    • Arrhythmogenic right ventricular dysplasia
    • Muthappan P, Calkins H. Arrhythmogenic right ventricular dysplasia. Prog Cardiovasc Dis 51: 31-43, 2008.
    • (2008) Prog Cardiovasc Dis , vol.51 , pp. 31-43
    • Muthappan, P.1    Calkins, H.2
  • 84
    • 0025989363 scopus 로고
    • Differential localization of alternative spliced transcripts encoding inositol 1,4,5-trisphosphate receptors in mouse cerebellum and hippocampus: In situ hybridization study
    • Nakagawa T, Shiota C, Okano H, Mikoshiba K. Differential localization of alternative spliced transcripts encoding inositol 1,4,5-trisphosphate receptors in mouse cerebellum and hippocampus: in situ hybridization study. J Neurochem 57: 1807-1810, 1991.
    • (1991) J Neurochem , vol.57 , pp. 1807-1810
    • Nakagawa, T.1    Shiota, C.2    Okano, H.3    Mikoshiba, K.4
  • 85
    • 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. 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    Hakamat, Y.3    Shigekawa, M.4    Takeshima, H.5    Numa, S.6
  • 86
    • 0026478697 scopus 로고
    • Immunohistochemical localization of ryanodine receptors in mouse central nervous system
    • Nakanishi S, Kuwajima G, Mikoshiba K. Immunohistochemical localization of ryanodine receptors in mouse central nervous system. Neurosci Res 15: 130-142, 1992.
    • (1992) Neurosci Res , vol.15 , pp. 130-142
    • Nakanishi, S.1    Kuwajima, G.2    Mikoshiba, K.3
  • 87
    • 34247485039 scopus 로고    scopus 로고
    • Diagnosis and treatment of catecholaminergic polymorphic ventricular tachycardia
    • Napolitano C, Priori SG. Diagnosis and treatment of catecholaminergic polymorphic ventricular tachycardia. Heart Rhythm 4: 675-678, 2007.
    • (2007) Heart Rhythm , vol.4 , pp. 675-678
    • Napolitano, C.1    Priori, S.G.2
  • 88
    • 0036625926 scopus 로고    scopus 로고
    • 2+ regulating proteins
    • 2+ regulating proteins. Curr Mol Med 2: 347-369, 2002.
    • (2002) Curr Mol Med , vol.2 , pp. 347-369
    • Nelson, T.E.1
  • 89
    • 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, Südhof TC. 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.
    • (1994) J Biol Chem , vol.269 , pp. 28613-28619
    • Newton, C.L.1    Mignery, G.A.2    Südhof, T.C.3
  • 92
    • 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. 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.
    • (1996) Biochem J , vol.315 , pp. 207-216
    • Ottini, L.1    Marziali, G.2    Conti, A.3    Charlesworth, A.4    Sorrentino, V.5
  • 94
    • 0023890314 scopus 로고
    • Sudden death due to malignant hyperthermia
    • Pamukcoglu T. Sudden death due to malignant hyperthermia. Am J Forensic Med Pathol 9: 161-162, 1988.
    • (1988) Am J Forensic Med Pathol , vol.9 , pp. 161-162
    • Pamukcoglu, T.1
  • 95
    • 0029102837 scopus 로고
    • Identification of dantrolene binding sites in porcine skeletal muscle sarcoplasmic reticulum
    • Parness J, Palnitkar SS. Identification of dantrolene binding sites in porcine skeletal muscle sarcoplasmic reticulum. J Biol Chem 270: 18465-18472, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 18465-18472
    • Parness, J.1    Palnitkar, S.S.2
  • 96
    • 0035895322 scopus 로고    scopus 로고
    • Mutations in the cardiac ryanodine receptor gene (hRyR2) underlie catecholaminergic polymorphic ventricular tachycardia
    • Priori SG, Napolitano C, Tiso N, Memmi M, Vignati G, Bloise R, Sorrentino V, Danieli GA. Mutations in the cardiac ryanodine receptor gene (hRyR2) underlie catecholaminergic polymorphic ventricular tachycardia. Circulation 103: 196-200, 2001.
    • (2001) Circulation , vol.103 , pp. 196-200
    • Priori, S.G.1    Napolitano, C.2    Tiso, N.3    Memmi, M.4    Vignati, G.5    Bloise, R.6    Sorrentino, V.7    Danieli, G.A.8
  • 97
    • 80054097452 scopus 로고    scopus 로고
    • Identification of intracellular and plasma membrane calcium channel homologues in pathogenic parasites
    • Prole DL, Taylor CW. Identification of intracellular and plasma membrane calcium channel homologues in pathogenic parasites. PLos One 6: e26218, 2011.
    • (2011) PLos One , vol.6
    • Prole, D.L.1    Taylor, C.W.2
  • 99
    • 0028004249 scopus 로고
    • Cryoelectron 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. Cryoelectron 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
  • 100
    • 33748997392 scopus 로고    scopus 로고
    • Mutations in RYR1 in malignant hyperthermia and central core disease
    • Robinson R, Carpenter D, Shaw MA, Halsall J, Hopkins P. Mutations in RYR1 in malignant hyperthermia and central core disease. Hum Mutat 27: 977-989, 2006.
    • (2006) Hum Mutat , vol.27 , pp. 977-989
    • Robinson, R.1    Carpenter, D.2    Shaw, M.A.3    Halsall, J.4    Hopkins, P.5
  • 101
    • 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. RYR1 mutations causing central core disease are associated with more severe malignant hyperthermia in vitro contracture test phenotypes. Hum Mutat 20: 88-97, 2002.
    • (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
  • 104
    • 0026508615 scopus 로고
    • Three additional inositol 1,4,5-trisphosphate receptors: Molecular cloning and differential localization in brain and peripheral tissues
    • Ross CA, Danoff SK, Schell MJ, Snyder SH, Ullrich A. Three additional inositol 1,4,5-trisphosphate receptors: molecular cloning and differential localization in brain and peripheral tissues. Proc Natl Acad Sci USA 89: 4265-4269, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4265-4269
    • Ross, C.A.1    Danoff, S.K.2    Schell, M.J.3    Snyder, S.H.4    Ullrich, A.5
  • 106
    • 0031080890 scopus 로고    scopus 로고
    • Sudden unexplained death in a patient with a family history of malignant hyperthermia
    • Ryan JF, Tedeschi LG. Sudden unexplained death in a patient with a family history of malignant hyperthermia. J Clin Anesth 9: 66-68, 1997.
    • (1997) J Clin Anesth , vol.9 , pp. 66-68
    • Ryan, J.F.1    Tedeschi, L.G.2
  • 107
    • 0027853916 scopus 로고
    • Cloning and mapping of a ryanodine receptor homolog gene of Caenorhabditis elegans
    • Sakube Y, Ando H, Kagawa H. Cloning and mapping of a ryanodine receptor homolog gene of Caenorhabditis elegans. Ann NY Acad Sci 707: 540-545, 1993.
    • (1993) Ann NY Acad Sci , vol.707 , pp. 540-545
    • Sakube, Y.1    Ando, H.2    Kagawa, H.3
  • 108
    • 67649637588 scopus 로고    scopus 로고
    • Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating
    • Samso M, Feng W, Pessah IN, Allen PD. Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating. PLoS Biol 7: e85, 2009.
    • (2009) PLoS Biol , vol.7
    • Samso, M.1    Feng, W.2    Pessah, I.N.3    Allen, P.D.4
  • 109
    • 22444444618 scopus 로고    scopus 로고
    • Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM
    • Samso M, Wagenknecht T, Allen PD. Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM. Nat Struct Mol Biol 12: 539-544, 2005.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 539-544
    • Samso, M.1    Wagenknecht, T.2    Allen, P.D.3
  • 112
    • 0037677206 scopus 로고    scopus 로고
    • Structure of the type 1 inositol 1,4,5-trisphosphate receptor revealed by electron cryomicroscopy
    • Serysheva II, Bare DJ, Ludtke SJ, Kettlun CS, Chiu W, Mignery GA. Structure of the type 1 inositol 1,4,5-trisphosphate receptor revealed by electron cryomicroscopy. J Biol Chem 278: 21319-21322, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 21319-21322
    • Serysheva, I.I.1    Bare, D.J.2    Ludtke, S.J.3    Kettlun, C.S.4    Chiu, W.5    Mignery, G.A.6
  • 113
    • 0028937373 scopus 로고
    • Electron cryomicroscopy and angular reconstitution used to visualize the skeletal muscle calcium release channel
    • Serysheva II, Orlova EV, Chiu W, Sherman MB, Hamilton SL, van Heel M. Electron cryomicroscopy and angular reconstitution used to visualize the skeletal muscle calcium release channel. Nat Struct Biol 2: 18-24, 1995.
    • (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
  • 116
    • 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. Loss of Inositol 1,4,5-trisphosphate receptors from bile duct epithelia is a common event in cholestasis. Gastroenterology 125: 1175-1187, 2003.
    • (2003) Gastroenterology , vol.125 , pp. 1175-1187
    • Shibao, K.1    Hirata, K.2    Robert, M.E.3    Nathanson, M.H.4
  • 120
    • 0031007450 scopus 로고    scopus 로고
    • Genetic evidence for involvement of type 1, type 2 and type 3 inositol 1,4,5-trisphosphate receptors in signal transduction through the B-cell antigen receptor
    • Sugawara H, Kurosaki M, Takata M, Kurosaki T. Genetic evidence for involvement of type 1, type 2 and type 3 inositol 1,4,5-trisphosphate receptors in signal transduction through the B-cell antigen receptor. EMBO J 16: 3078-3088, 1997.
    • (1997) EMBO J , vol.16 , pp. 3078-3088
    • Sugawara, H.1    Kurosaki, M.2    Takata, M.3    Kurosaki, T.4
  • 121
    • 70450247255 scopus 로고    scopus 로고
    • Ubiquitous SPRY domains and their role in the skeletal type ryanodine receptor
    • Tae H, Casarotto MG, Dulhunty AF. Ubiquitous SPRY domains and their role in the skeletal type ryanodine receptor. Eur Biophys J 39: 51-59, 2009.
    • (2009) Eur Biophys J , vol.39 , pp. 51-59
    • Tae, H.1    Casarotto, M.G.2    Dulhunty, A.F.3
  • 122
    • 0024318429 scopus 로고
    • Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor
    • Takeshima H, Nishimura S, Matsumoto T, Ishida H. Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor. Nature 339: 439-445, 1989.
    • (1989) Nature , vol.339 , pp. 439-445
    • Takeshima, H.1    Nishimura, S.2    Matsumoto, T.3    Ishida, H.4
  • 123
    • 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. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28: 2731-2739, 2011.
    • (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
  • 126
  • 129
    • 78649469923 scopus 로고    scopus 로고
    • The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule
    • Tung CC, Lobo PA, Kimlicka L, Van Petegem F. The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule. Nature 468: 585-588, 2010.
    • (2010) Nature , vol.468 , pp. 585-588
    • Tung, C.C.1    Lobo, P.A.2    Kimlicka, L.3    van Petegem, F.4
  • 132
    • 1242298679 scopus 로고    scopus 로고
    • Subcellular distribution of the inositol 1,4,5-trisphosphate receptors: Functional relevance and molecular determinants
    • Vermassen E, Parys JB, Mauger JP. Subcellular distribution of the inositol 1,4,5-trisphosphate receptors: functional relevance and molecular determinants. Biol Cell 96: 3-17, 2004.
    • (2004) Biol Cell , vol.96 , pp. 3-17
    • Vermassen, E.1    Parys, J.B.2    Mauger, J.P.3
  • 134
    • 0022529046 scopus 로고
    • A review of its pharmacodynamic and pharmacokinetic properties and therapeutic use in malignant hyperthermia, the neuroleptic malignant syndrome and an update of its use in muscle spasticity
    • Ward A, Chaffman MO, Sorkin Dantrolene EM. A review of its pharmacodynamic and pharmacokinetic properties and therapeutic use in malignant hyperthermia, the neuroleptic malignant syndrome and an update of its use in muscle spasticity. Drugs 32: 130-168, 1986.
    • (1986) Drugs , vol.32 , pp. 130-168
    • Ward, A.1    Chaffman, M.O.2    Sorkin, D.E.M.3
  • 136
    • 0345490780 scopus 로고    scopus 로고
    • Altered function and regulation of cardiac ryanodine receptors in cardiac disease
    • Wehrens XH, Marks AR. Altered function and regulation of cardiac ryanodine receptors in cardiac disease. Trends Biochem Sci 28: 671-678, 2003.
    • (2003) Trends Biochem Sci , vol.28 , pp. 671-678
    • Wehrens, X.H.1    Marks, A.R.2
  • 137
    • 3543134142 scopus 로고    scopus 로고
    • Novel therapeutic approaches for heart failure by normalizing calcium cycling
    • Wehrens XH, Marks AR. Novel therapeutic approaches for heart failure by normalizing calcium cycling. Nat Rev Drug Discov 3: 565-573, 2004.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 565-573
    • Wehrens, X.H.1    Marks, A.R.2
  • 138
    • 78149237173 scopus 로고    scopus 로고
    • Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor mediates functional coupling between ligand binding and channel opening
    • Yamazaki H, Chan J, Ikura M, Michikawa T, Mikoshiba K. Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor mediates functional coupling between ligand binding and channel opening. J Biol Chem 285: 36081-36091, 2010.
    • (2010) J Biol Chem , vol.285 , pp. 36081-36091
    • Yamazaki, H.1    Chan, J.2    Ikura, M.3    Michikawa, T.4    Mikoshiba, K.5
  • 139
    • 0029898559 scopus 로고    scopus 로고
    • Mutational analysis of the ligand binding site of the inositol 1,4,5-trisphosphate receptor
    • Yoshikawa F, Morita M, Monkawa T, Michikawa T, Furuichi T, Mikoshiba K. Mutational analysis of the ligand binding site of the inositol 1,4,5-trisphosphate receptor. J Biol Chem 271: 18277-18284, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 18277-18284
    • Yoshikawa, F.1    Morita, M.2    Monkawa, T.3    Michikawa, T.4    Furuichi, T.5    Mikoshiba, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.