메뉴 건너뛰기




Volumn 44, Issue 2, 2016, Pages 452-459

ER-luminal thiol/selenol-mediated regulation of Ca 2+ signalling

Author keywords

Calcium; Endoplasmic reticulum (ER); Inositol 1,4,5 trisphosphate receptor (IP3R); Mitochondria associated membrane (MAM); Redox dependent regulation; Sarco endoplasmic reticulum Ca 2+ transport ATPase (SERCA); Signal transduction

Indexed keywords

CHAPERONE; CYSTEINE; DISULFIDE; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; ORGANOSELENIUM DERIVATIVE; OXIDOREDUCTASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE 2; SELENOL; SELENOPROTEIN; THIOL; UNCLASSIFIED DRUG; SELENIUM DERIVATIVE; THIOL DERIVATIVE;

EID: 85009912613     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20150233     Document Type: Review
Times cited : (36)

References (95)
  • 1
    • 72949126637 scopus 로고
    • The calcium pump of the "relaxing granules" of muscle and its dependence on ATP-splitting
    • Hasselbach, W. and Makinose, M. (1961) [The calcium pump of the "relaxing granules" of muscle and its dependence on ATP-splitting]. Biochem Z. 333, 518-528
    • (1961) Biochem Z , vol.333 , pp. 518-528
    • Hasselbach, W.1    Makinose, M.2
  • 3
    • 0023819315 scopus 로고    scopus 로고
    • A novel Ca2+ pump expressed in brain, kidney, and stomach is encoded by an alternative transcript of the slow-twitch muscle sarcoplasmic reticulum Ca-ATPase gene. Identification of cDNAs encoding Ca2+ and other cation-transporting ATPases using an oligonucleotide probe derived from the ATP-binding site
    • Gunteski-Hamblin, A.M., Greeb, J. and Shull, G.E. (1998) A novel Ca2+ pump expressed in brain, kidney, and stomach is encoded by an alternative transcript of the slow-twitch muscle sarcoplasmic reticulum Ca-ATPase gene. Identification of cDNAs encoding Ca2+ and other cation-transporting ATPases using an oligonucleotide probe derived from the ATP-binding site. J. Biol. Chem. 263, 15032-15040
    • (1998) J. Biol. Chem. , vol.263 , pp. 15032-15040
    • Gunteski-Hamblin, A.M.1    Greeb, J.2    Shull, G.E.3
  • 4
    • 0023737219 scopus 로고
    • Molecular cloning of cDNAs from human kidney coding for two alternatively spliced products of the cardiac Ca2+ -ATPase gene
    • Lytton, J. and MacLennan, D.H. (1988) Molecular cloning of cDNAs from human kidney coding for two alternatively spliced products of the cardiac Ca2+ -ATPase gene. J. Biol. Chem. 263, 15024-15031
    • (1988) J. Biol. Chem. , vol.263 , pp. 15024-15031
    • Lytton, J.1    MacLennan, D.H.2
  • 5
    • 0020643801 scopus 로고
    • Release of Ca2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate
    • Streb, H., Irvine, R.F., Berridge, M.J. and Schulz, I. (1983) Release of Ca2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate. Nature 306, 67-69
    • (1983) Nature , vol.306 , pp. 67-69
    • Streb, H.1    Irvine, R.F.2    Berridge, M.J.3    Schulz, I.4
  • 6
    • 0021645893 scopus 로고
    • Ca2+ homeostasis in permeabilized human neutrophils. Characterization of Ca2+ -sequestering pools and the action of inositol 1, 4,5-triphosphate
    • Prentki, M., Wollheim, C.B. and Lew, P.D. (1984) Ca2+ homeostasis in permeabilized human neutrophils. Characterization of Ca2+ -sequestering pools and the action of inositol 1, 4,5-triphosphate. J. Biol. Chem. 259, 13777-13782
    • (1984) J. Biol. Chem. , vol.259 , pp. 13777-13782
    • Prentki, M.1    Wollheim, C.B.2    Lew, P.D.3
  • 7
    • 0014770764 scopus 로고
    • Calcium efflux from a heavy sarcotubular fraction. Effects of ryanodine, caffeine and magnesium
    • Fairhurst, A.S. and Hasselbach, W. (1970) Calcium efflux from a heavy sarcotubular fraction. Effects of ryanodine, caffeine and magnesium. Eur. J. Biochem. 13, 504-509
    • (1970) Eur. J. Biochem. , vol.13 , pp. 504-509
    • Fairhurst, A.S.1    Hasselbach, W.2
  • 8
    • 84898792542 scopus 로고    scopus 로고
    • Redox dependence of endoplasmic reticulum (ER) Ca(2)( + ) signaling
    • Raturi, A., Ortiz-Sandoval, C. and Simmen, T. (2014) Redox dependence of endoplasmic reticulum (ER) Ca(2)( + ) signaling. Histol. Histopathol. 29, 543-552
    • (2014) Histol. Histopathol , vol.29 , pp. 543-552
    • Raturi, A.1    Ortiz-Sandoval, C.2    Simmen, T.3
  • 10
    • 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
  • 11
    • 0017364364 scopus 로고
    • Calcium release from the sarcoplasmic reticulum
    • Endo, M. (1977) Calcium release from the sarcoplasmic reticulum. Physiol. Rev. 57, 71-108
    • (1977) Physiol. Rev. , vol.57 , pp. 71-108
    • Endo, M.1
  • 12
    • 0023113884 scopus 로고
    • Involvement of dihydropyridine receptors in excitation-contraction coupling in skeletal muscle
    • Rios, E. and 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
  • 13
    • 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. 9-22
    • (2007) Biochem. Soc. Symp , pp. 9-22
    • Mikoshiba, K.1
  • 14
    • 34547897405 scopus 로고    scopus 로고
    • IP3 receptor/Ca2+ channel: From discovery to new signaling concepts
    • Mikoshiba, K. (2007) IP3 receptor/Ca2+ channel: from discovery to new signaling concepts. J. Neurochem. 102, 1426-1446
    • (2007) J. Neurochem. , vol.102 , pp. 1426-1446
    • Mikoshiba, K.1
  • 15
    • 0036878788 scopus 로고    scopus 로고
    • Calcium leak from intracellular stores - The enigma of calcium signalling
    • Camello, C., Lomax, R., Petersen, O.H. and Tepikin, A.V. (2002) Calcium leak from intracellular stores - the enigma of calcium signalling. Cell Calcium 32, 355-361
    • (2002) Cell Calcium , vol.32 , pp. 355-361
    • Camello, C.1    Lomax, R.2    Petersen, O.H.3    Tepikin, A.V.4
  • 22
    • 84880167897 scopus 로고    scopus 로고
    • Regulators of calcium homeostasis identified by inference of kinetic model parameters from live single cells perturbed by siRNA
    • Bandara, S., Malmersjo, S. and Meyer, T. (2013) Regulators of calcium homeostasis identified by inference of kinetic model parameters from live single cells perturbed by siRNA. Sci. Signal. 6, ra56
    • (2013) Sci. Signal , vol.6 , pp. ra56
    • Bandara, S.1    Malmersjo, S.2    Meyer, T.3
  • 23
    • 84859483029 scopus 로고    scopus 로고
    • Lack of evidence for presenilins as endoplasmic reticulum Ca2+ leak channels
    • Shilling, D., Mak, D.O., Kang, D.E. and Foskett, J.K. (2012) Lack of evidence for presenilins as endoplasmic reticulum Ca2+ leak channels. J. Biol. Chem. 287, 10933-10944
    • (2012) J. Biol. Chem. , vol.287 , pp. 10933-10944
    • Shilling, D.1    Mak, D.O.2    Kang, D.E.3    Foskett, J.K.4
  • 24
    • 11844284861 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum
    • Oakes, S.A., Scorrano, L., Opferman, J.T., Bassik, M.C., Nishino, M., Pozzan, T. and Korsmeyer, S.J. (2005) Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum. Proc. Natl. Acad. Sci. U.S.A. 102, 105-110
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 105-110
    • Oakes, S.A.1    Scorrano, L.2    Opferman, J.T.3    Bassik, M.C.4    Nishino, M.5    Pozzan, T.6    Korsmeyer, S.J.7
  • 25
    • 78650436415 scopus 로고    scopus 로고
    • Enhanced ROS generation mediated by Alzheimer's disease presenilin regulation of InsP3R Ca2+ signaling
    • Muller, M., Cheung, K.H. and Foskett, J.K. (2011) Enhanced ROS generation mediated by Alzheimer's disease presenilin regulation of InsP3R Ca2+ signaling. Antioxid. Redox Signal. 14, 1225-1235
    • (2011) Antioxid. Redox Signal , vol.14 , pp. 1225-1235
    • Muller, M.1    Cheung, K.H.2    Foskett, J.K.3
  • 26
    • 29244462514 scopus 로고    scopus 로고
    • Polycystin 2 interacts with type I inositol 1, 4,5-trisphosphate receptor to modulate intracellular Ca2+ signaling
    • Li, Y., Wright, J.M., Qian, F., Germino, G.G. and Guggino, W.B. (2005) Polycystin 2 interacts with type I inositol 1, 4,5-trisphosphate receptor to modulate intracellular Ca2+ signaling. J. Biol. Chem. 280, 41298-41306
    • (2005) J. Biol. Chem. , vol.280 , pp. 41298-41306
    • Li, Y.1    Wright, J.M.2    Qian, F.3    Germino, G.G.4    Guggino, W.B.5
  • 27
    • 0022575011 scopus 로고
    • A model for receptor-regulated calcium entry
    • Putney, Jr, J.W. (1986) A model for receptor-regulated calcium entry. Cell Calcium 7, 1-12
    • (1986) Cell Calcium , vol.7 , pp. 1-12
    • Putney, J.W.1
  • 28
    • 33847136350 scopus 로고    scopus 로고
    • Intracellular Ca(2+ ) release via the ER translocon activates store-operated calcium entry
    • Ong, H.L., Liu, X., Sharma, A., Hegde, R.S. and Ambudkar, I.S. (2007) Intracellular Ca(2+ ) release via the ER translocon activates store-operated calcium entry. Pflugers. Arch. 453, 797-808
    • (2007) Pflugers. Arch. , vol.453 , pp. 797-808
    • Ong, H.L.1    Liu, X.2    Sharma, A.3    Hegde, R.S.4    Ambudkar, I.S.5
  • 29
    • 84940119926 scopus 로고    scopus 로고
    • Store-operated calcium channels
    • Prakriya, M. and Lewis, R.S. (2015) Store-operated calcium channels. Physiol. Rev. 95, 1383-1436
    • (2015) Physiol. Rev. , vol.95 , pp. 1383-1436
    • Prakriya, M.1    Lewis, R.S.2
  • 30
    • 84892164786 scopus 로고    scopus 로고
    • The STIM1/Orai signaling machinery
    • Austin
    • Fahrner, M., Derler, I., Jardin, I. and Romanin, C. (2013) The STIM1/Orai signaling machinery. Channels (Austin) 7, 330-343
    • (2013) Channels , vol.7 , pp. 330-343
    • Fahrner, M.1    Derler, I.2    Jardin, I.3    Romanin, C.4
  • 31
    • 84940896352 scopus 로고    scopus 로고
    • The STIM1-ORAI1 microdomain
    • Hogan, P.G. (2015) The STIM1-ORAI1 microdomain. Cell Calcium 58, 357-367
    • (2015) Cell Calcium , vol.58 , pp. 357-367
    • Hogan, P.G.1
  • 33
    • 79959513944 scopus 로고    scopus 로고
    • Calcium signaling and disease: Preface
    • Brini, M. and Carafoli, E. (2011) Calcium signaling and disease: preface. Biofactors 37, 131
    • (2011) Biofactors , vol.37 , pp. 131
    • Brini, M.1    Carafoli, E.2
  • 34
    • 77149136381 scopus 로고    scopus 로고
    • Calcium binding chaperones of the endoplasmic reticulum
    • Coe, H. and Michalak, M. (2009) Calcium binding chaperones of the endoplasmic reticulum. Gen. Physiol. Biophys. 28 Spec No Focus, F96-F103
    • (2009) Gen. Physiol. Biophys. , vol.28 , Issue.SPEC NO FOCUS , pp. F96-F103
    • Coe, H.1    Michalak, M.2
  • 35
    • 84931565973 scopus 로고    scopus 로고
    • N-linked sugar-regulated protein folding and quality control in the ER
    • Tannous, A., Pisoni, G.B., Hebert, D.N. and Molinari, M. (2015) N-linked sugar-regulated protein folding and quality control in the ER. Semin. Cell Dev. Biol. 41, 79-89
    • (2015) Semin. Cell Dev. Biol. , vol.41 , pp. 79-89
    • Tannous, A.1    Pisoni, G.B.2    Hebert, D.N.3    Molinari, M.4
  • 36
    • 84875251847 scopus 로고    scopus 로고
    • Luminal Ca2+ depletion during the unfolded protein response in Xenopus oocytes: Cause and consequence
    • Paredes, R.M., Bollo, M., Holstein, D. and Lechleiter, J.D. (2013) Luminal Ca2+ depletion during the unfolded protein response in Xenopus oocytes: cause and consequence. Cell Calcium 53, 286-296
    • (2013) Cell Calcium , vol.53 , pp. 286-296
    • Paredes, R.M.1    Bollo, M.2    Holstein, D.3    Lechleiter, J.D.4
  • 37
    • 77953725586 scopus 로고    scopus 로고
    • Oxidative protein folding in the endoplasmic reticulum: Tight links to the mitochondria-associated membrane (MAM)
    • Simmen, T., Lynes, E.M., Gesson, K. and Thomas, G. (2010) Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM). Biochim. Biophys. Acta 1798, 1465-1473
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1465-1473
    • Simmen, T.1    Lynes, E.M.2    Gesson, K.3    Thomas, G.4
  • 38
    • 84875608277 scopus 로고    scopus 로고
    • Modulation of ER stress and apoptosis by endoplasmic reticulum calcium leak via translocon during unfolded protein response: Involvement of GRP78
    • Hammadi, M., Oulidi, A., Gackiere, F., Katsogiannou, M., Slomianny, C., Roudbaraki, M., Dewailly, E., Delcourt, P., Lepage, G. and Lotteau, S. (2013) Modulation of ER stress and apoptosis by endoplasmic reticulum calcium leak via translocon during unfolded protein response: involvement of GRP78. FASEB J. 27, 1600-1609
    • (2013) FASEB J , vol.27 , pp. 1600-1609
    • Hammadi, M.1    Oulidi, A.2    Gackiere, F.3    Katsogiannou, M.4    Slomianny, C.5    Roudbaraki, M.6    Dewailly, E.7    Delcourt, P.8    Lepage, G.9    Lotteau, S.10
  • 40
    • 80255123366 scopus 로고    scopus 로고
    • Modulation of STIM1 and capacitative Ca2+ entry by the endoplasmic reticulum luminal oxidoreductase ERp57
    • Prins, D., Groenendyk, J., Touret, N. and Michalak, M. (2011) Modulation of STIM1 and capacitative Ca2+ entry by the endoplasmic reticulum luminal oxidoreductase ERp57. EMBO Rep. 12, 1182-1188
    • (2011) EMBO Rep. , vol.12 , pp. 1182-1188
    • Prins, D.1    Groenendyk, J.2    Touret, N.3    Michalak, M.4
  • 45
    • 77953703354 scopus 로고    scopus 로고
    • Redox state of the endoplasmic reticulum is controlled by Ero1L-alpha and intraluminal calcium
    • Enyedi, B., Varnai, P. and Geiszt, M. (2010) Redox state of the endoplasmic reticulum is controlled by Ero1L-alpha and intraluminal calcium. Antioxid. Redox Signal. 13, 721-729
    • (2010) Antioxid. Redox Signal , vol.13 , pp. 721-729
    • Enyedi, B.1    Varnai, P.2    Geiszt, M.3
  • 46
    • 0014673435 scopus 로고
    • Calcium uptake by isolated sarcoplasmic reticulum treated with dithiothreitol
    • Van der Kloot, W. (1969) Calcium uptake by isolated sarcoplasmic reticulum treated with dithiothreitol. Science 164, 1294-1295
    • (1969) Science , vol.164 , pp. 1294-1295
    • Van Der Kloot, W.1
  • 47
    • 0015218980 scopus 로고
    • The role of calcium and magnesium in the adenosine triphosphatase reaction of sarcoplasmic reticulum
    • Panet, R., Pick, U. and Selinger, Z. (1971) The role of calcium and magnesium in the adenosine triphosphatase reaction of sarcoplasmic reticulum. J. Biol. Chem. 246, 7349-7356
    • (1971) J. Biol. Chem. , vol.246 , pp. 7349-7356
    • Panet, R.1    Pick, U.2    Selinger, Z.3
  • 48
    • 9144266981 scopus 로고    scopus 로고
    • S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
    • Adachi, T., Weisbrod, R.M., Pimentel, D.R., Ying, J., Sharov, V.S., Schoneich, C. and Cohen, R.A. (2004) S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide. Nat. Med. 10, 1200-1207
    • (2004) Nat. Med. , vol.10 , pp. 1200-1207
    • Adachi, T.1    Weisbrod, R.M.2    Pimentel, D.R.3    Ying, J.4    Sharov, V.S.5    Schoneich, C.6    Cohen, R.A.7
  • 50
    • 0023017221 scopus 로고
    • Calcium efflux from sarcoplasmic reticulum microsomes due to oxidation and sulfhydryl-binding agents
    • Scherer, N.M. and Deamer, D.W. (1986) Calcium efflux from sarcoplasmic reticulum microsomes due to oxidation and sulfhydryl-binding agents. J. Free Radic. Biol. Med. 2, 249-254
    • (1986) J. Free Radic. Biol. Med. , vol.2 , pp. 249-254
    • Scherer, N.M.1    Deamer, D.W.2
  • 51
    • 2942590128 scopus 로고    scopus 로고
    • Thimerosal stimulates Ca2+ flux through inositol 1, 4,5-trisphosphate receptor type 1, but not type 3, via modulation of an isoform-specific Ca2+ -dependent intramolecular interaction
    • Bultynck, G., Szlufcik, K., Kasri, N.N., Assefa, Z., Callewaert, G., Missiaen, L., Parys, J.B. and De Smedt, H. (2004) Thimerosal stimulates Ca2+ flux through inositol 1, 4,5-trisphosphate receptor type 1, but not type 3, via modulation of an isoform-specific Ca2+ -dependent intramolecular interaction. Biochem. J. 381, 87-96
    • (2004) Biochem. J , vol.381 , pp. 87-96
    • Bultynck, G.1    Szlufcik, K.2    Kasri, N.N.3    Assefa, Z.4    Callewaert, G.5    Missiaen, L.6    Parys, J.B.7    De Smedt, H.8
  • 52
    • 84875632863 scopus 로고    scopus 로고
    • Subtype-selective regulation of IP(3) receptors by thimerosal via cysteine residues within the IP(3)-binding core and suppressor domain
    • Khan, S.A., Rossi, A.M., Riley, A.M., Potter, B.V. and Taylor, C.W. (2013) Subtype-selective regulation of IP(3) receptors by thimerosal via cysteine residues within the IP(3)-binding core and suppressor domain. Biochem. J. 451, 177-184
    • (2013) Biochem. J , vol.451 , pp. 177-184
    • Khan, S.A.1    Rossi, A.M.2    Riley, A.M.3    Potter, B.V.4    Taylor, C.W.5
  • 58
    • 41549159471 scopus 로고    scopus 로고
    • The human PDI family: Versatility packed into a single fold
    • Appenzeller-Herzog, C. and Ellgaard, L. (2008) The human PDI family: versatility packed into a single fold. Biochim. Biophys. Acta 1783, 535-548
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 535-548
    • Appenzeller-Herzog, C.1    Ellgaard, L.2
  • 59
    • 0347753252 scopus 로고    scopus 로고
    • Ca2+ -dependent redox modulation of SERCA 2b by ERp57
    • Li, Y. and Camacho, P. (2004) Ca2+ -dependent redox modulation of SERCA 2b by ERp57. J. Cell Biol. 164, 35-46
    • (2004) J. Cell Biol. , vol.164 , pp. 35-46
    • Li, Y.1    Camacho, P.2
  • 60
    • 0027231872 scopus 로고
    • Increased frequency of calcium waves in Xenopus laevis oocytes that express a calcium-ATPase
    • Camacho, P. and Lechleiter, J.D. (1993) Increased frequency of calcium waves in Xenopus laevis oocytes that express a calcium-ATPase. Science 260, 226-229
    • (1993) Science , vol.260 , pp. 226-229
    • Camacho, P.1    Lechleiter, J.D.2
  • 61
    • 0842302342 scopus 로고    scopus 로고
    • Inhibitors of SERCA and mitochondrial Ca-uniporter decrease velocity of calcium waves in rat cardiomyocytes
    • Landgraf, G., Gellerich, F.N. and Wussling, M.H. (2004) Inhibitors of SERCA and mitochondrial Ca-uniporter decrease velocity of calcium waves in rat cardiomyocytes. Mol. Cell Biochem. 256-257, 379-386
    • (2004) Mol. Cell Biochem. , vol.256-257 , pp. 379-386
    • Landgraf, G.1    Gellerich, F.N.2    Wussling, M.H.3
  • 62
    • 0035980058 scopus 로고    scopus 로고
    • Mutations of either or both Cys876 and Cys888 residues of sarcoplasmic reticulum Ca2+ -ATPase result in a complete loss of Ca2+ transport activity without a loss of Ca2+ -dependent ATPase activity. Role of the CYS876-CYS888 disulfide bond
    • Daiho, T., Yamasaki, K., Saino, T., Kamidochi, M., Satoh, K., Iizuka, H. and Suzuki, H. (2001) Mutations of either or both Cys876 and Cys888 residues of sarcoplasmic reticulum Ca2+ -ATPase result in a complete loss of Ca2+ transport activity without a loss of Ca2+ -dependent ATPase activity. Role of the CYS876-CYS888 disulfide bond. J. Biol. Chem. 276, 32771-32778
    • (2001) J. Biol. Chem. , vol.276 , pp. 32771-32778
    • Daiho, T.1    Yamasaki, K.2    Saino, T.3    Kamidochi, M.4    Satoh, K.5    Iizuka, H.6    Suzuki, H.7
  • 64
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima, C., Nakasako, M., Nomura, H. and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405, 647-655
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 65
    • 0032877634 scopus 로고    scopus 로고
    • ATP2A2 mutations in Darier's disease: Variant cutaneous phenotypes are associated with missense mutations, but neuropsychiatric features are independent of mutation class
    • Ruiz-Perez, V.L., Carter, S.A., Healy, E., Todd, C., Rees, J.L., Steijlen, P.M., Carmichael, A.J., Lewis, H.M., Hohl, D. and Itin, P. (1999) ATP2A2 mutations in Darier's disease: variant cutaneous phenotypes are associated with missense mutations, but neuropsychiatric features are independent of mutation class. Hum. Mol. Genet. 8, 1621-1630
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1621-1630
    • Ruiz-Perez, V.L.1    Carter, S.A.2    Healy, E.3    Todd, C.4    Rees, J.L.5    Steijlen, P.M.6    Carmichael, A.J.7    Lewis, H.M.8    Hohl, D.9    Itin, P.10
  • 67
    • 84901724029 scopus 로고    scopus 로고
    • Mid-range Ca2+ signalling mediated by functional coupling between store-operated Ca2+ entry and IP3-dependent Ca2+ release
    • Courjaret, R. and Machaca, K. (2014) Mid-range Ca2+ signalling mediated by functional coupling between store-operated Ca2+ entry and IP3-dependent Ca2+ release. Nat. Commun. 5, 3916
    • (2014) Nat. Commun. , vol.5 , pp. 3916
    • Courjaret, R.1    Machaca, K.2
  • 68
    • 0029745744 scopus 로고    scopus 로고
    • Activation of different Cl currents in Xenopus oocytes by Ca liberated from stores and by capacitative Ca influx
    • Hartzell, H.C. (1996) Activation of different Cl currents in Xenopus oocytes by Ca liberated from stores and by capacitative Ca influx. J. Gen. Physiol. 108, 157-175
    • (1996) J. Gen. Physiol. , vol.108 , pp. 157-175
    • Hartzell, H.C.1
  • 69
    • 84892427728 scopus 로고    scopus 로고
    • Modulation of intracellular calcium waves and triggered activities by mitochondrial ca flux in mouse cardiomyocytes
    • Zhao, Z., Gordan, R., Wen, H., Fefelova, N., Zang, W.J. and Xie, L.H. (2013) Modulation of intracellular calcium waves and triggered activities by mitochondrial ca flux in mouse cardiomyocytes. PLoS One 8, e80574
    • (2013) PLoS One , vol.8
    • Zhao, Z.1    Gordan, R.2    Wen, H.3    Fefelova, N.4    Zang, W.J.5    Xie, L.H.6
  • 70
    • 0034640960 scopus 로고    scopus 로고
    • Cytosolic phosphorylation of calnexin controls intracellular Ca(2+ ) oscillations via an interaction with SERCA2b
    • Roderick, H.L., Lechleiter, J.D. and Camacho, P. (2000) Cytosolic phosphorylation of calnexin controls intracellular Ca(2+ ) oscillations via an interaction with SERCA2b. J. Cell Biol. 149, 1235-1248
    • (2000) J. Cell Biol. , vol.149 , pp. 1235-1248
    • Roderick, H.L.1    Lechleiter, J.D.2    Camacho, P.3
  • 72
    • 84926475413 scopus 로고    scopus 로고
    • SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 pump activity
    • Marino, M., Stoilova, T., Giorgi, C., Bachi, A., Cattaneo, A., Auricchio, A., Pinton, P. and Zito, E. (2015) SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 pump activity. Hum. Mol. Genet. 24, 1843-1855
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 1843-1855
    • Marino, M.1    Stoilova, T.2    Giorgi, C.3    Bachi, A.4    Cattaneo, A.5    Auricchio, A.6    Pinton, P.7    Zito, E.8
  • 73
    • 84903600136 scopus 로고    scopus 로고
    • Selenoproteins: Molecular pathways and physiological roles
    • Labunskyy, V.M., Hatfield, D.L. and Gladyshev, V.N. (2014) Selenoproteins: molecular pathways and physiological roles. Physiol. Rev. 94, 739-777
    • (2014) Physiol. Rev. , vol.94 , pp. 739-777
    • Labunskyy, V.M.1    Hatfield, D.L.2    Gladyshev, V.N.3
  • 74
    • 67650066807 scopus 로고    scopus 로고
    • Oxidative stress in SEPN1-related myopathy: From pathophysiology to treatment
    • Arbogast, S., Beuvin, M., Fraysse, B., Zhou, H., Muntoni, F. and Ferreiro, A. (2009) Oxidative stress in SEPN1-related myopathy: from pathophysiology to treatment. Ann. Neurol. 65, 677-686
    • (2009) Ann. Neurol. , vol.65 , pp. 677-686
    • Arbogast, S.1    Beuvin, M.2    Fraysse, B.3    Zhou, H.4    Muntoni, F.5    Ferreiro, A.6
  • 77
    • 84929300310 scopus 로고    scopus 로고
    • The antioxidant machinery of the endoplasmic reticulum: Protection and signaling
    • Delaunay-Moisan, A. and Appenzeller-Herzog, C. (2015) The antioxidant machinery of the endoplasmic reticulum: Protection and signaling. Free Radic. Biol. Med. 83, 341-351
    • (2015) Free Radic. Biol. Med. , vol.83 , pp. 341-351
    • Delaunay-Moisan, A.1    Appenzeller-Herzog, C.2
  • 79
    • 84886099424 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels: Lessons from structure-function studies
    • Amador, F.J., Stathopulos, P.B., Enomoto, M. and Ikura, M. (2013) Ryanodine receptor calcium release channels: lessons from structure-function studies. FEBS J. 280, 5456-5470
    • (2013) FEBS J , vol.280 , pp. 5456-5470
    • Amador, F.J.1    Stathopulos, P.B.2    Enomoto, M.3    Ikura, M.4
  • 80
    • 84952628203 scopus 로고    scopus 로고
    • Structural insights into endoplasmic reticulum stored calcium regulation by inositol 1,4,5-trisphosphate and ryanodine receptors
    • Seo, M.D., Enomoto, M., Ishiyama, N., Stathopulos, P.B. and Ikura, M. (2015) Structural insights into endoplasmic reticulum stored calcium regulation by inositol 1,4,5-trisphosphate and ryanodine receptors. Biochim. Biophys. Acta 1853, 1980-1991
    • (2015) Biochim. Biophys. Acta , vol.1853 , pp. 1980-1991
    • Seo, M.D.1    Enomoto, M.2    Ishiyama, N.3    Stathopulos, P.B.4    Ikura, M.5
  • 81
    • 84926182977 scopus 로고    scopus 로고
    • Toward a high-resolution structure of IP(3)R channel
    • Serysheva, I.I. (2014) Toward a high-resolution structure of IP(3)R channel. Cell Calcium 56, 125-132
    • (2014) Cell Calcium , vol.56 , pp. 125-132
    • Serysheva, I.I.1
  • 83
    • 11844269232 scopus 로고    scopus 로고
    • Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44
    • Higo, T., Hattori, M., Nakamura, T., Natsume, T., Michikawa, T. and Mikoshiba, K. (2005) Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell 120, 85-98
    • (2005) Cell , vol.120 , pp. 85-98
    • Higo, T.1    Hattori, M.2    Nakamura, T.3    Natsume, T.4    Michikawa, T.5    Mikoshiba, K.6
  • 84
    • 0037083869 scopus 로고    scopus 로고
    • ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family
    • Anelli, T., Alessio, M., Mezghrani, A., Simmen, T., Talamo, F., Bachi, A. and Sitia, R. (2002) ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J. 21, 835-844
    • (2002) EMBO J , vol.21 , pp. 835-844
    • Anelli, T.1    Alessio, M.2    Mezghrani, A.3    Simmen, T.4    Talamo, F.5    Bachi, A.6    Sitia, R.7
  • 86
    • 54449100767 scopus 로고    scopus 로고
    • Effects of redox potential and Ca2+ on the inositol 1, 4,5-trisphosphate receptor L3-1 loop region: Implications for receptor regulation
    • Kang, S., Kang, J., Kwon, H., Frueh, D., Yoo, S.H., Wagner, G. and Park, S. (2008) Effects of redox potential and Ca2+ on the inositol 1, 4,5-trisphosphate receptor L3-1 loop region: implications for receptor regulation. J. Biol. Chem. 283, 25567-25575
    • (2008) J. Biol. Chem. , vol.283 , pp. 25567-25575
    • Kang, S.1    Kang, J.2    Kwon, H.3    Frueh, D.4    Yoo, S.H.5    Wagner, G.6    Park, S.7
  • 87
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-alpha-mediated stimulation of inositol 1, 4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li, G., Mongillo, M., Chin, K.T., Harding, H., Ron, D., Marks, A.R. and Tabas, I. (2009) Role of ERO1-alpha-mediated stimulation of inositol 1, 4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J. Cell Biol. 186, 783-792
    • (2009) J. Cell Biol. , vol.186 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6    Tabas, I.7
  • 88
    • 77955708533 scopus 로고    scopus 로고
    • Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM)
    • Gilady, S.Y., Bui, M., Lynes, E.M., Benson, M.D., Watts, R., Vance, J.E. and Simmen, T. (2010) Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM). Cell Stress Chaperones 15, 619-629
    • (2010) Cell Stress Chaperones , vol.15 , pp. 619-629
    • Gilady, S.Y.1    Bui, M.2    Lynes, E.M.3    Benson, M.D.4    Watts, R.5    Vance, J.E.6    Simmen, T.7
  • 90
    • 0033945128 scopus 로고    scopus 로고
    • Type 3 inositol 1, 4,5-trisphosphate receptor modulates cell death
    • Blackshaw, S., Sawa, A., Sharp, A.H., Ross, C.A., Snyder, S.H. and Khan, A.A. (2000) Type 3 inositol 1, 4,5-trisphosphate receptor modulates cell death. FASEB J. 14, 1375-1379
    • (2000) FASEB J , vol.14 , pp. 1375-1379
    • Blackshaw, S.1    Sawa, A.2    Sharp, A.H.3    Ross, C.A.4    Snyder, S.H.5    Khan, A.A.6
  • 91
    • 35549006797 scopus 로고    scopus 로고
    • Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival
    • Hayashi, T. and Su, T.P. (2007) Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival. Cell 131, 596-610
    • (2007) Cell , vol.131 , pp. 596-610
    • Hayashi, T.1    Su, T.P.2
  • 92
  • 94
    • 0032487674 scopus 로고    scopus 로고
    • Type III InsP3 receptor channel stays open in the presence of increased calcium
    • Hagar, R.E., Burgstahler, A.D., Nathanson, M.H. and Ehrlich, B.E. (1998) Type III InsP3 receptor channel stays open in the presence of increased calcium. Nature 396, 81-84
    • (1998) Nature , vol.396 , pp. 81-84
    • Hagar, R.E.1    Burgstahler, A.D.2    Nathanson, M.H.3    Ehrlich, B.E.4
  • 95
    • 0032563599 scopus 로고    scopus 로고
    • Differential modulation of SERCA2 isoforms by calreticulin
    • John, L.M., Lechleiter, J.D. and Camacho, P. (1998) Differential modulation of SERCA2 isoforms by calreticulin. J. Cell Biol. 142, 963-973
    • (1998) J. Cell Biol. , vol.142 , pp. 963-973
    • John, L.M.1    Lechleiter, J.D.2    Camacho, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.