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Volumn 34, Issue 1, 2013, Pages 49-59

Loss of endoplasmic reticulum Ca2+ homeostasis: Contribution to neuronal cell death during cerebral ischemia

Author keywords

Ca2+homeostasis; ER stress; IP3R; ischemia; neuronal cell death; RyR; SERCA; unfolded protein response(UPR)

Indexed keywords

CALCIUM ION; INOSITOL TRIPHOSPHATE RECEPTOR; RECEPTOR; RYANODINE RECEPTOR 1; RYANODINE RECEPTOR 2; RYANODINE RECEPTOR 3; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

EID: 84872079384     PISSN: 16714083     EISSN: 17457254     Source Type: Journal    
DOI: 10.1038/aps.2012.139     Document Type: Review
Times cited : (50)

References (132)
  • 1
    • 0032127595 scopus 로고    scopus 로고
    • Neuronal calcium signaling
    • DOI 10.1016/S0896-6273(00)80510-3
    • Berridge MJ. Neuronal calcium signaling. Neuron 1998;21:13-26. (Pubitemid 28355688)
    • (1998) Neuron , vol.21 , Issue.1 , pp. 13-26
    • Berridge, M.J.1
  • 2
    • 0037025272 scopus 로고    scopus 로고
    • The endoplasmic reticulum as an integrating signalling organelle: From neuronal signalling to neuronal death
    • DOI 10.1016/S0014-2999(02)01838-1, PII S0014299902018381
    • Verkhratsky A, Petersen OH. The endoplasmic reticulum as an integrating signalling organelle: from neuronal signalling to neuronal death. Eur J Pharmacol 2002;447:141-54. (Pubitemid 34874448)
    • (2002) European Journal of Pharmacology , vol.447 , Issue.2-3 , pp. 141-154
    • Verkhratsky, A.1    Petersen, O.H.2
  • 3
    • 12944314765 scopus 로고    scopus 로고
    • Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurons
    • DOI 10.1152/physrev.00004.2004
    • Verkhratsky A. Physiology and pathophysiology of the calcium store in the endoplasmic reticulum of neurons. Physiol Rev 2005;85:201-79. (Pubitemid 40173995)
    • (2005) Physiological Reviews , vol.85 , Issue.1 , pp. 201-279
    • Verkhratsky, A.1
  • 4
    • 0031048249 scopus 로고    scopus 로고
    • Neuroprotective nitric oxide synthase inhibitor reduces intracellular calcium accumulation following transient global ischemia in the gerbil
    • DOI 10.1016/S0304-3940(97)13459-0, PII S0304394097134590
    • Kohno K, Higuchi T, Ohta S, Kohno K, Kumon Y, Sakaki S. Neuroprotective nitric oxide synthase inhibitor reduces intracellular calcium accumulation following transient global ischemia in the gerbil. Neurosci Lett 1997;224:17-20. (Pubitemid 27112859)
    • (1997) Neuroscience Letters , vol.224 , Issue.1 , pp. 17-20
    • Kohno, K.1    Higuchi, T.2    Ohta, S.3    Kohno, K.4    Kumon, Y.5    Sakaki, S.6
  • 5
    • 0020051129 scopus 로고
    • Delayed neuronal death in the gerbil hippocampus following ischemia
    • DOI 10.1016/0006-8993(82)90833-2
    • Kirino T. Delayed neuronal death in the gerbil hippocampus following ischemia. Brain Res 1982;239:57-69. (Pubitemid 12101768)
    • (1982) Brain Research , vol.239 , Issue.1 , pp. 57-69
    • Kirino, T.1
  • 6
    • 12244266803 scopus 로고    scopus 로고
    • 2+ show depletion prior to the final steps in delayed CA1 neuronal death
    • DOI 10.1152/jn.00015.2004
    • Xing H, Zimi-Zonooz A, Shuttleworth CW, Connor JA. Caffeine releasable stores of Ca2+ show depletion prior to the final steps in delayed CA1 neuronal death. J Neurophysiol 2004;92:2960-7. (Pubitemid 40340505)
    • (2004) Journal of Neurophysiology , vol.92 , Issue.5 , pp. 2960-2967
    • Xing, H.1    Azimi-Zonooz, A.2    Shuttleworth, C.W.3    Connor, J.A.4
  • 7
    • 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 2012;740:217-34.
    • (2012) Adv Exp Med Biol , vol.740 , pp. 217-234
    • Lanner, J.T.1
  • 8
    • 0032930964 scopus 로고    scopus 로고
    • Single synaptic events evoke NMDA receptor-mediated release of calcium from internal stores in hippocampal dendritic spines
    • DOI 10.1016/S0896-6273(00)80683-2
    • Emptage N, Bliss TV, Fine A. Single synaptic events evoke NMDA receptor-mediated release of calcium from internal stores in hippocampal dendritic spines. Neuron 1999;22:115-24. (Pubitemid 29070098)
    • (1999) Neuron , vol.22 , Issue.1 , pp. 115-124
    • Emptage, N.1    Bliss, T.V.P.2    Fine, A.3
  • 9
  • 11
    • 0036715034 scopus 로고    scopus 로고
    • Ryanodine receptors contribute to cGMP-induced late-phase LTP and CREB phosphorylation in the hippocampus
    • Lu YF, Hawkins RD. Ryanodine receptors contribute to cGMP-induced late-phase LTP and CREB phosphorylation in the hippocampus. J Neurophysiol 2002;88:1270-8. (Pubitemid 35025381)
    • (2002) Journal of Neurophysiology , vol.88 , Issue.3 , pp. 1270-1278
    • Lu, Y.-F.1    Hawkins, R.D.2
  • 12
    • 79551557613 scopus 로고    scopus 로고
    • Generation of dendritic Ca2+ oscillations as a consequence of altered ryanodine receptor function in AD neurons
    • Goussakov I, Chakroborty S, Stutzmann GE. Generation of dendritic Ca2+ oscillations as a consequence of altered ryanodine receptor function in AD neurons. Channels (Austin) 2011;5:9-13.
    • (2011) Channels (Austin) , vol.5 , pp. 9-13
    • Goussakov, I.1    Chakroborty, S.2    Stutzmann, G.E.3
  • 13
    • 31844450573 scopus 로고    scopus 로고
    • 2+ store in the plasticity of central neurons
    • DOI 10.1016/j.tips.2005.12.008, PII S016561470500338X
    • Bardo S, Cavazzini MG, Emptage N. The role of the endoplasmic reticulum Ca2+ store in the plasticity of central neurons. Trends Pharmacol Sci 2006;27:78-84. (Pubitemid 43184028)
    • (2006) Trends in Pharmacological Sciences , vol.27 , Issue.2 , pp. 78-84
    • Bardo, S.1    Cavazzini, M.G.2    Emptage, N.3
  • 16
    • 33646584876 scopus 로고    scopus 로고
    • Ischemia opens neuronal gap junction hemichannels
    • DOI 10.1126/science.1126241
    • Thompson RJ, Zhou N, MacVicar BA. Ischemia opens neuronal gap junction hemichannels. Science 2006;312:924-7. (Pubitemid 43727327)
    • (2006) Science , vol.312 , Issue.5775 , pp. 924-927
    • Thompson, R.J.1    Zhou, N.2    MacVicar, B.A.3
  • 17
    • 32044455816 scopus 로고    scopus 로고
    • 2+ signaling, cell death and stroke
    • DOI 10.1016/j.tins.2005.12.001, PII S0166223605003061
    • MacDonald JF, Xiong ZG, Jackson MF. Paradox of Ca (2+) signaling, cell death and stroke. Trends Neurosci 2006;29:75-81. (Pubitemid 43202596)
    • (2006) Trends in Neurosciences , vol.29 , Issue.2 , pp. 75-81
    • MacDonald, J.F.1    Xiong, Z.-G.2    Jackson, M.F.3
  • 18
    • 0032498185 scopus 로고    scopus 로고
    • Activation of the cardiac calcium release channel (Ryanodoine receptor) by poly-S-nitrosylation
    • DOI 10.1126/science.279.5348.234
    • Xu L, Eu JP, Meissner G, Stamler JS. Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation. Science 1998;279:234-7. (Pubitemid 28103882)
    • (1998) Science , vol.279 , Issue.5348 , pp. 234-237
    • Xu, L.1    Eu, J.P.2    Meissner, G.3    Stamler, J.S.4
  • 19
    • 58149347130 scopus 로고    scopus 로고
    • Ischemia enhances activation by Ca2+ and redox modification of ryanodine receptor channels from rat brain cortex
    • Bull R, Finkelstein JP, Galvez J, Sanchez G, Donoso P, Behrens MI, et al. Ischemia enhances activation by Ca2+ and redox modification of ryanodine receptor channels from rat brain cortex. J Neurosci 2008;28:9463-72.
    • (2008) J Neurosci , vol.28 , pp. 9463-9472
    • Bull, R.1    Finkelstein, J.P.2    Galvez, J.3    Sanchez, G.4    Donoso, P.5    Behrens, M.I.6
  • 22
    • 84857193479 scopus 로고    scopus 로고
    • Nitric oxide-induced calcium release via ryanodine receptors regulates neuronal function
    • Kakizawa S, Yamazawa T, Chen Y, Ito A, Murayama T, Oyamada H, et al. Nitric oxide-induced calcium release via ryanodine receptors regulates neuronal function. EMBO J 2012;31:417-28.
    • (2012) EMBO J , vol.31 , pp. 417-428
    • Kakizawa, S.1    Yamazawa, T.2    Chen, Y.3    Ito, A.4    Murayama, T.5    Oyamada, H.6
  • 23
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • DOI 10.1152/physrev.00029.2006
    • Pacher P, Beckman JS, Liaudet L. Nitric oxide and peroxynitrite in health and disease. Physiol Rev 2007;87:315-424. (Pubitemid 46217686)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 24
    • 78651515878 scopus 로고    scopus 로고
    • Effects of dantrolene on ischemia-reperfusion injury in animal models: A review of outcomes in heart, brain, liver, and kidney
    • Boys JA, Toledo AH, Naya-Prado R, Lopez-Neblina F, Toledo-Pereyra LH. Effects of dantrolene on ischemia-reperfusion injury in animal models: a review of outcomes in heart, brain, liver, and kidney. J Investig Med 2010;58:875-82.
    • (2010) J Investig Med , vol.58 , pp. 875-882
    • Boys, J.A.1    Toledo, A.H.2    Naya-Prado, R.3    Lopez-Neblina, F.4    Toledo-Pereyra, L.H.5
  • 25
    • 78650308809 scopus 로고    scopus 로고
    • The cytoprotective effects of dantrolene: A ryanodine receptor antagonist
    • Inan S, Wei H. The cytoprotective effects of dantrolene: a ryanodine receptor antagonist. Anesth Analg 2010;111:1400-10.
    • (2010) Anesth Analg , vol.111 , pp. 1400-1410
    • Inan, S.1    Wei, H.2
  • 26
    • 63249121147 scopus 로고    scopus 로고
    • Dantrolene: Mechanisms of neuroprotection and possible clinical applications in the neurointensive care unit
    • Muehlschlegel S, Sims JR. Dantrolene: mechanisms of neuroprotection and possible clinical applications in the neurointensive care unit. Neurocrit Care 2009;10:103-15.
    • (2009) Neurocrit Care , vol.10 , pp. 103-115
    • Muehlschlegel, S.1    Sims, J.R.2
  • 28
    • 48749131140 scopus 로고    scopus 로고
    • Endoplasmic reticulum Ca2+ dysregulation and endoplasmic reticulum stress following in vitro neuronal ischemia: Role of Na+-K+-Cl-cotransporter
    • Chen X, Kintner DB, Luo J, Baba A, Matsuda T, Sun D. Endoplasmic reticulum Ca2+ dysregulation and endoplasmic reticulum stress following in vitro neuronal ischemia: role of Na+-K+-Cl-cotransporter. J Neurochem 2008;106:1563-76.
    • (2008) J Neurochem , vol.106 , pp. 1563-1576
    • Chen, X.1    Kintner, D.B.2    Luo, J.3    Baba, A.4    Matsuda, T.5    Sun, D.6
  • 29
    • 70349829186 scopus 로고    scopus 로고
    • Endoplasmic reticulum Ca (2+) release through ryanodine and IP (3) receptors contributes to neuronal excitotoxicity
    • Ruiz A, Matute C, Alberdi E. Endoplasmic reticulum Ca (2+) release through ryanodine and IP (3) receptors contributes to neuronal excitotoxicity. Cell Calcium 2009;46:273-81.
    • (2009) Cell Calcium , vol.46 , pp. 273-281
    • Ruiz, A.1    Matute, C.2    Alberdi, E.3
  • 31
    • 0032487674 scopus 로고    scopus 로고
    • 3 receptor channel stays open in the presence of increased calcium
    • DOI 10.1038/23954
    • Hagar RE, Burgstahler AD, Nathanson MH, Ehrlich BE. Type III InsP3 receptor channel stays open in the presence of increased calcium. Nature 1998;396:81-4. (Pubitemid 28520453)
    • (1998) Nature , vol.396 , Issue.6706 , pp. 81-84
    • Hagar, R.E.1    Burgstahler, A.D.2    Nathanson, M.H.3    Ehrlich, B.E.4
  • 34
    • 84864296756 scopus 로고    scopus 로고
    • Protein S-glutathionylation enhances Ca2+-induced Ca2+ release via the IP3 receptor in cultured aortic endothelial cells
    • Lock JT, Sinkins WG, Schilling WP. Protein S-glutathionylation enhances Ca2+-induced Ca2+ release via the IP3 receptor in cultured aortic endothelial cells. J Physiol 2012;590:3431-47.
    • (2012) J Physiol , vol.590 , pp. 3431-3447
    • Lock, J.T.1    Sinkins, W.G.2    Schilling, W.P.3
  • 39
    • 0033542745 scopus 로고    scopus 로고
    • 2+ ATPase
    • DOI 10.1016/S0006-8993(99)01504-8, PII S0006899399015048
    • Parsons JT, Churn SB, De Lorenzo RJ. Global ischemia-induced inhibition of the coupling ratio of calcium uptake and ATP hydrolysis by rat whole brain microsomal Mg (2+)/Ca (2+) ATPase. Brain Res 1999;834:32-41. (Pubitemid 29332007)
    • (1999) Brain Research , vol.834 , Issue.1-2 , pp. 32-41
    • Parsons, J.T.1    Churn, S.B.2    Delorenzo, R.J.3
  • 40
    • 0029915016 scopus 로고    scopus 로고
    • The oxidative inactivation of sarcoplasmic reticulum Ca (2+)-ATPase by peroxynitrite
    • Viner RI, Huhmer AF, Bigelow DJ, Schoneich C. The oxidative inactivation of sarcoplasmic reticulum Ca (2+)-ATPase by peroxynitrite. Free Radic Res 1996;24:243-59.
    • (1996) Free Radic Res , vol.24 , pp. 243-259
    • Viner, R.I.1    Huhmer, A.F.2    Bigelow, D.J.3    Schoneich, C.4
  • 41
    • 77956589569 scopus 로고    scopus 로고
    • Cardiac contractile dysfunction during acute hyperglycemia due to impairment of SERCA by polyol pathway-mediated oxidative stress
    • Tang WH, Cheng WT, Kravtsov GM, Tong XY, Hou XY, Chung SK, et al. Cardiac contractile dysfunction during acute hyperglycemia due to impairment of SERCA by polyol pathway-mediated oxidative stress. Am J Physiol Cell Physiol 2010;299:C643-53.
    • (2010) Am J Physiol Cell Physiol , vol.299
    • Tang, W.H.1    Cheng, W.T.2    Kravtsov, G.M.3    Tong, X.Y.4    Hou, X.Y.5    Chung, S.K.6
  • 44
    • 0031015476 scopus 로고    scopus 로고
    • 2+-ATPase function by direct attack on the ATP binding site
    • Xu KY, Zweier JL, Becker LC. Hydroxyl radical inhibits sarcoplasmic reticulum Ca (2+)-ATPase function by direct attack on the ATP binding site. Circ Res 1997;80:76-81. (Pubitemid 27030371)
    • (1997) Circulation Research , vol.80 , Issue.1 , pp. 76-81
    • Xu, K.Y.1    Zweier, J.L.2    Becker, L.C.3
  • 45
    • 0033564289 scopus 로고    scopus 로고
    • 2+-ATPase in skeletal muscle
    • DOI 10.1042/0264-6021:3400657
    • Viner RI, Ferrington DA, Williams TD, Bigelow DJ, Schoneich C. Protein modification during biological aging: selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca2+- ATPase in skeletal muscle. Biochem J 1999;340:657-69. (Pubitemid 29312862)
    • (1999) Biochemical Journal , vol.340 , Issue.3 , pp. 657-669
    • Viner, R.I.1    Ferrington, D.A.2    Williams, T.D.3    Bigelow, D.J.4    Schoneich, C.5
  • 46
    • 25444450030 scopus 로고    scopus 로고
    • 3-Nitrotyrosine modification of SERCA2a in the aging heart: A distinct signature of the cellular redox environment
    • DOI 10.1021/bi051226n
    • Knyushko TV, Sharov VS, Williams TD, Schoneich C, Bigelow DJ. 3-Nitrotyrosine modification of SERCA2a in the aging heart: a distinct signature of the cellular redox environment. Biochemistry 2005;44:13071-81. (Pubitemid 41377287)
    • (2005) Biochemistry , vol.44 , Issue.39 , pp. 13071-13081
    • Knyushko, T.V.1    Sharov, V.S.2    Williams, T.D.3    Schoneich, C.4    Bigelow, D.J.5
  • 47
    • 24644438715 scopus 로고    scopus 로고
    • Intraluminal calcium as a primary regulator of endoplasmic reticulum function
    • DOI 10.1016/j.ceca.2005.06.010, PII S0143416005000953
    • Burdakov D, Petersen OH, Verkhratsky A. Intraluminal calcium as a primary regulator of endoplasmic reticulum function. Cell Calcium 2005;38:303-10. (Pubitemid 41283268)
    • (2005) Cell Calcium , vol.38 , pp. 303-310
    • Burdakov, D.1    Petersen, O.H.2    Verkhratsky, A.3
  • 48
    • 0036877146 scopus 로고    scopus 로고
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum
    • DOI 10.1016/S0143416002001884
    • Michalak M, Robert Parker JM, Opas M. Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 2002;32:269-78. (Pubitemid 36175750)
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 269-278
    • Michalak, M.1    Parker, J.M.R.2    Opas, M.3
  • 49
    • 1842405433 scopus 로고    scopus 로고
    • 2+
    • DOI 10.1074/jbc.272.49.30873
    • Lievremont JP, Rizzuto R, Hendershot L, Meldolesi J. BiP, a major chaperone protein of the endoplasmic reticulum lumen, plays a direct and important role in the storage of the rapidly exchanging pool of Ca2+. J Biol Chem 1997;272:30873-9. (Pubitemid 27527530)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.49 , pp. 30873-30879
    • Lievremont, J.-P.1    Rizzuto, R.2    Hendershot, L.3    Meldolesi, J.4
  • 50
    • 51849162371 scopus 로고    scopus 로고
    • Redox-based endoplasmic reticulum dysfunction in neurological diseases
    • Banhegyi G, Mandl J, Csala M. Redox-based endoplasmic reticulum dysfunction in neurological diseases. J Neurochem 2008;107:20-34.
    • (2008) J Neurochem , vol.107 , pp. 20-34
    • Banhegyi, G.1    Mandl, J.2    Csala, M.3
  • 52
    • 36448993027 scopus 로고    scopus 로고
    • Protein aggregation and proteasome dysfunction after brain ischemia
    • DOI 10.1161/STROKEAHA.107.487108, PII 0000767020071200000021
    • Ge P, Luo Y, Liu CL, Hu B. Protein aggregation and proteasome dysfunction after brain ischemia. Stroke 2007;38:3230-6. (Pubitemid 350175742)
    • (2007) Stroke , vol.38 , Issue.12 , pp. 3230-3236
    • Ge, P.1    Luo, Y.2    Liu, C.L.3    Hu, B.4
  • 53
    • 34247252415 scopus 로고    scopus 로고
    • Convergence of stress granules and protein aggregates in hippocampal cornu ammonis 1 at later reperfusion following global brain ischemia
    • DOI 10.1016/j.neuroscience.2007.01.050, PII S0306452207001029
    • De Gracia DJ, Rudolph J, Roberts GG, Rafols JA, Wang J. Convergence of stress granules and protein aggregates in hippocampal cornu ammonis 1 at later reperfusion following global brain ischemia. Neuroscience 2007;146:562-72. (Pubitemid 46621138)
    • (2007) Neuroscience , vol.146 , Issue.2 , pp. 562-572
    • DeGracia, D.J.1    Rudolph, J.2    Roberts, G.G.3    Rafols, J.A.4    Wang, J.5
  • 54
    • 21744453627 scopus 로고    scopus 로고
    • Ischemic preconditioning prevents protein aggregation after transient cerebral ischemia
    • DOI 10.1016/j.neuroscience.2005.03.036, PII S0306452205003350
    • Liu C, Chen S, Kamme F, Hu BR. Ischemic preconditioning prevents protein aggregation after transient cerebral ischemia. Neuroscience 2005;134:69-80. (Pubitemid 40943635)
    • (2005) Neuroscience , vol.134 , Issue.1 , pp. 69-80
    • Liu, C.1    Chen, S.2    Kamme, F.3    Hu, B.R.4
  • 55
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter P, Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011;334:1081-6.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 56
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • Hetz C. The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat Rev Mol Cell Biol 2012;13:89-102.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 89-102
    • Hetz, C.1
  • 57
    • 80053369081 scopus 로고    scopus 로고
    • Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response
    • Gardner BM, Walter P. Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response. Science 2011;333:1891-4.
    • (2011) Science , vol.333 , pp. 1891-1894
    • Gardner, B.M.1    Walter, P.2
  • 58
    • 80054026314 scopus 로고    scopus 로고
    • A review of the mammalian unfolded protein response
    • Chakrabarti A, Chen AW, Varner JD. A review of the mammalian unfolded protein response. Biotechnol Bioeng 2011;108:2777-93.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 2777-2793
    • Chakrabarti, A.1    Chen, A.W.2    Varner, J.D.3
  • 59
    • 57049117856 scopus 로고    scopus 로고
    • Cell death and endoplasmic reticulum stress: Disease relevance and therapeutic opportunities
    • Kim I, Xu W, Reed JC. Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities. Nat Rev Drug Discov 2008;7:1013-30.
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 60
    • 30444432257 scopus 로고    scopus 로고
    • CHOP plays a pivotal role in the astrocyte death induced by oxygen and glucose deprivation
    • DOI 10.1002/glia.20242
    • Benavides A, Pastor D, Santos P, Tranque P, Calvo S. CHOP plays a pivotal role in the astrocyte death induced by oxygen and glucose deprivation. Glia 2005;52:261-75. (Pubitemid 43076219)
    • (2005) GLIA , vol.52 , Issue.4 , pp. 261-275
    • Benavides, A.1    Pastor, D.2    Santos, P.3    Tranque, P.4    Calvo, S.5
  • 63
    • 37849026711 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum stress in the neuronal death induced by transient forebrain ischemia in gerbil
    • Oida Y, Shimazawa M, Imaizumi K, Hara H. Involvement of endoplasmic reticulum stress in the neuronal death induced by transient forebrain ischemia in gerbil. Neuroscience 2008;151:111-9.
    • (2008) Neuroscience , vol.151 , pp. 111-119
    • Oida, Y.1    Shimazawa, M.2    Imaizumi, K.3    Hara, H.4
  • 64
    • 43049126481 scopus 로고    scopus 로고
    • Induction of BiP, an ER-resident protein, prevents the neuronal death induced by transient forebrain ischemia in gerbil
    • Oida Y, Izuta H, Oyagi A, Shimazawa M, Kudo T, Imaizumi K, et al. Induction of BiP, an ER-resident protein, prevents the neuronal death induced by transient forebrain ischemia in gerbil. Brain Res 2008;1208:217-24.
    • (2008) Brain Res , vol.1208 , pp. 217-224
    • Oida, Y.1    Izuta, H.2    Oyagi, A.3    Shimazawa, M.4    Kudo, T.5    Imaizumi, K.6
  • 66
    • 0037426614 scopus 로고    scopus 로고
    • Activation of caspase-12 by endoplasmic reticulum stress induced by transient middle cerebral artery occlusion in mice
    • DOI 10.1016/S0306-4522(02)00910-7
    • Shibata M, Hattori H, Sasaki T, Gotoh J, Hamada J, Fukuuchi Y. Activation of caspase-12 by endoplasmic reticulum stress induced by transient middle cerebral artery occlusion in mice. Neuroscience 2003;118:491-9. (Pubitemid 36423263)
    • (2003) Neuroscience , vol.118 , Issue.2 , pp. 491-499
    • Shibata, M.1    Hattori, H.2    Sasaki, T.3    Gotoh, J.4    Hamada, J.5    Fukuuchi, Y.6
  • 67
    • 79959595004 scopus 로고    scopus 로고
    • Appearance of nuclear-sorted caspase-12 fragments in cerebral cortical and hippocampal neurons in rats damaged by autologous blood clot embolic brain infarctions
    • Shimoke K, Matsuki Y, Fukunaga K, Matsumura Y, Fujita E, Sugihara K, et al. Appearance of nuclear-sorted caspase-12 fragments in cerebral cortical and hippocampal neurons in rats damaged by autologous blood clot embolic brain infarctions. Cell Mol Neurobiol 2011;31:795-802.
    • (2011) Cell Mol Neurobiol , vol.31 , pp. 795-802
    • Shimoke, K.1    Matsuki, Y.2    Fukunaga, K.3    Matsumura, Y.4    Fujita, E.5    Sugihara, K.6
  • 70
    • 0027517597 scopus 로고
    • Induction of glucose regulated protein (grp78) and inducible heat shock protein (hsp70) mRNAs in rat brain after kainic acid seizures and focal ischemia
    • Wang S, Longo FM, Chen J, Butman M, Graham SH, Haglid KG, et al. Induction of glucose regulated protein (grp78) and inducible heat shock protein (hsp70) mRNAs in rat brain after kainic acid seizures and focal ischemia. Neurochem Int 1993;23:575-82.
    • (1993) Neurochem Int , vol.23 , pp. 575-582
    • Wang, S.1    Longo, F.M.2    Chen, J.3    Butman, M.4    Graham, S.H.5    Haglid, K.G.6
  • 71
    • 0033015485 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: Suppression of oxidative stress and stabilization of calcium homeostasis
    • DOI 10.1006/exnr.1998.7002
    • Yu Z, Luo H, Fu W, Mattson MP. The endoplasmic reticulum stressresponsive protein GRP78 protects neurons against excitotoxicity and apoptosis: suppression of oxidative stress and stabilization of calcium homeostasis. Exp Neurol 1999;155:302-14. (Pubitemid 29124724)
    • (1999) Experimental Neurology , vol.155 , Issue.2 , pp. 302-314
    • Yu, Z.1    Luo, H.2    Fu, W.3    Mattson, M.P.4
  • 73
    • 1542300773 scopus 로고    scopus 로고
    • Oxidative injury to the endoplasmic reticulum in mouse brains after transient focal ischemia
    • DOI 10.1016/j.nbd.2003.10.005, PII S0969996103002079
    • Hayashi T, Saito A, Okuno S, Ferrand-Drake M, Dodd RL, Chan PH. Oxidative injury to the endoplasmic reticulum in mouse brains after transient focal ischemia. Neurobiol Dis 2004;15:229-39. (Pubitemid 38296754)
    • (2004) Neurobiology of Disease , vol.15 , Issue.2 , pp. 229-239
    • Hayashi, T.1    Saito, A.2    Okuno, S.3    Ferrand-Drake, M.4    Dodd, R.L.5    Chan, P.H.6
  • 76
    • 24144440965 scopus 로고    scopus 로고
    • PERK is responsible for the increased phosphorylation of eIF2α and the severe inhibition of protein synthesis after transient global brain ischemia
    • DOI 10.1111/j.1471-4159.2005.03276.x
    • Owen CR, Kumar R, Zhang P, McGrath BC, Cavener DR, Krause GS. PERK is responsible for the increased phosphorylation of eIF2alpha and the severe inhibition of protein synthesis after transient global brain ischemia. J Neurochem 2005;94:1235-42. (Pubitemid 41232579)
    • (2005) Journal of Neurochemistry , vol.94 , Issue.5 , pp. 1235-1242
    • Owen, C.R.1    Kumar, R.2    Zhang, P.3    McGrath, B.C.4    Cavener, D.R.5    Krause, G.S.6
  • 77
    • 79959979647 scopus 로고    scopus 로고
    • Induction of ER stress in response to oxygen-glucose deprivation of cortical cultures involves the activation of the PERK and IRE-1 pathways and of caspase-12
    • Badiola N, Penas C, Minano-Molina A, Barneda-Zahonero B, Fado R, Sanchez-Opazo G, et al. Induction of ER stress in response to oxygen-glucose deprivation of cortical cultures involves the activation of the PERK and IRE-1 pathways and of caspase-12. Cell Death Dis 2011;2:e149.
    • (2011) Cell Death Dis , vol.2
    • Badiola, N.1    Penas, C.2    Minano-Molina, A.3    Barneda-Zahonero, B.4    Fado, R.5    Sanchez-Opazo, G.6
  • 78
    • 34247524717 scopus 로고    scopus 로고
    • Irreversible translation arrest in the reperfused brain
    • DOI 10.1038/sj.jcbfm.9600388, PII 9600388
    • De Gracia DJ, Hu BR. Irreversible translation arrest in the reperfused brain. J Cereb Blood Flow Metab 2007;27:875-93. (Pubitemid 46661555)
    • (2007) Journal of Cerebral Blood Flow and Metabolism , vol.27 , Issue.5 , pp. 875-893
    • DeGracia, D.J.1    Hu, B.R.2
  • 79
    • 0037385160 scopus 로고    scopus 로고
    • Transient cerebral ischemia activates processing of xbp1 messenger RNA indicative of endoplasmic reticulum stress
    • Paschen W, Aufenberg C, Hotop S, Mengesdorf T. Transient cerebral ischemia activates processing of xbp1 messenger RNA indicative of endoplasmic reticulum stress. J Cereb Blood Flow Metab 2003;23:449-61. (Pubitemid 36403027)
    • (2003) Journal of Cerebral Blood Flow and Metabolism , vol.23 , Issue.4 , pp. 449-461
    • Paschen, W.1    Aufenberg, C.2    Hotop, S.3    Mengesdorf, T.4
  • 80
    • 0033168080 scopus 로고    scopus 로고
    • 2-Deoxy-D-glucose protects hippocampal neurons against excitotoxic and oxidative injury: Evidence for the involvement of stress proteins
    • DOI 10.1002/(SICI)1097-4547(19990701)57:1<48::AID-JNR6>3.0.CO;2-L
    • Lee J, Bruce-Keller AJ, Kruman Y, Chan SL, Mattson MP. 2-Deoxy-D-glucose protects hippocampal neurons against excitotoxic and oxidative injury: evidence for the involvement of stress proteins. J Neurosci Res 1999;57:48-61. (Pubitemid 29293579)
    • (1999) Journal of Neuroscience Research , vol.57 , Issue.1 , pp. 48-61
    • Lee, J.1    Bruce-Keller, A.J.2    Kruman, Y.3    Chan, S.L.4    Mattson, M.P.5
  • 81
    • 80052515471 scopus 로고    scopus 로고
    • Post-treatment of a BiP inducer prevents cell death after middle cerebral artery occlusion in mice
    • Oida Y, Hamanaka J, Hyakkoku K, Shimazawa M, Kudo T, Imaizumi K, et al. Post-treatment of a BiP inducer prevents cell death after middle cerebral artery occlusion in mice. Neurosci Lett 2010;484:43-6.
    • (2010) Neurosci Lett , vol.484 , pp. 43-46
    • Oida, Y.1    Hamanaka, J.2    Hyakkoku, K.3    Shimazawa, M.4    Kudo, T.5    Imaizumi, K.6
  • 83
    • 77956288847 scopus 로고    scopus 로고
    • Activation of PERK signaling attenuates Abeta-mediated ER stress
    • Lee DY, Lee KS, Lee HJ, Kim DH, Noh YH, Yu K, et al. Activation of PERK signaling attenuates Abeta-mediated ER stress. PLoS One 2010;5:e10489.
    • (2010) PLoS One , vol.5
    • Lee, D.Y.1    Lee, K.S.2    Lee, H.J.3    Kim, D.H.4    Noh, Y.H.5    Yu, K.6
  • 84
    • 78650412221 scopus 로고    scopus 로고
    • Neuronal apoptosis induced by endoplasmic reticulum stress is regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only member PUMA
    • Galehdar Z, Swan P, Fuerth B, Callaghan SM, Park DS, Cregan SP. Neuronal apoptosis induced by endoplasmic reticulum stress is regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only member PUMA. J Neurosci 2010;30:16938-48.
    • (2010) J Neurosci , vol.30 , pp. 16938-16948
    • Galehdar, Z.1    Swan, P.2    Fuerth, B.3    Callaghan, S.M.4    Park, D.S.5    Cregan, S.P.6
  • 87
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • DOI 10.1172/JCI26373
    • Xu C, Bailly-Maitre B, Reed JC. Endoplasmic reticulum stress: cell life and death decisions. J Clin Invest 2005;115:2656-64. (Pubitemid 41434389)
    • (2005) Journal of Clinical Investigation , vol.115 , Issue.10 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 89
    • 77449095179 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress plays critical role in brain damage after cerebral ischemia/reperfusion in rats
    • Nakka VP, Gusain A, Raghubir R. Endoplasmic reticulum stress plays critical role in brain damage after cerebral ischemia/reperfusion in rats. Neurotox Res 2010;17:189-202.
    • (2010) Neurotox Res , vol.17 , pp. 189-202
    • Nakka, V.P.1    Gusain, A.2    Raghubir, R.3
  • 90
    • 63149183734 scopus 로고    scopus 로고
    • Apolipoprotein E-deficient mice are more vulnerable to ER stress after transient forebrain ischemia
    • Osada N, Kosuge Y, Kihara T, Ishige K, Ito Y. Apolipoprotein E-deficient mice are more vulnerable to ER stress after transient forebrain ischemia. Neurochem Int 2009;54:403-9.
    • (2009) Neurochem Int , vol.54 , pp. 403-409
    • Osada, N.1    Kosuge, Y.2    Kihara, T.3    Ishige, K.4    Ito, Y.5
  • 91
    • 77953539363 scopus 로고    scopus 로고
    • Characterization of neuronal and astroglial responses to ER stress in the hippocampal CA1 area in mice following transient forebrain ischemia
    • Osada N, Kosuge Y, Ishige K, Ito Y. Characterization of neuronal and astroglial responses to ER stress in the hippocampal CA1 area in mice following transient forebrain ischemia. Neurochem Int 2010;57:1-7.
    • (2010) Neurochem Int , vol.57 , pp. 1-7
    • Osada, N.1    Kosuge, Y.2    Ishige, K.3    Ito, Y.4
  • 92
    • 0032544514 scopus 로고    scopus 로고
    • Activation of gadd153 expression through transient cerebral ischemia: Evidence that ischemia causes endoplasmic reticulum dysfunction
    • DOI 10.1016/S0169-328X(98)00180-6, PII S0169328X98001806
    • Paschen W, Gissel C, Linden T, Althausen S, Doutheil J. Activation of gadd153 expression through transient cerebral ischemia: evidence that ischemia causes endoplasmic reticulum dysfunction. Brain Res Mol Brain Res 1998;60:115-22. (Pubitemid 28433201)
    • (1998) Molecular Brain Research , vol.60 , Issue.1 , pp. 115-122
    • Paschen, W.1    Gissel, C.2    Linden, T.3    Althausen, S.4    Doutheil, J.5
  • 93
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bc12 and perturbing the cellular redox state
    • DOI 10.1128/MCB.21.4.1249-1259.2001
    • McCullough KD, Martindale JL, Klotz LO, Aw TY, Holbrook NJ. Gadd153 sensitizes cells to endoplasmic reticulum stress by downregulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 2001;21:1249-59. (Pubitemid 32114973)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.4 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.-O.3    Aw, T.-Y.4    Holbrook, N.J.5
  • 96
    • 84856433369 scopus 로고    scopus 로고
    • CHOP silencing reduces acute brain injury in the rat model of subarachnoid hemorrhage
    • He Z, Ostrowski RP, Sun X, Ma Q, Huang B, Zhan Y, et al. CHOP silencing reduces acute brain injury in the rat model of subarachnoid hemorrhage. Stroke 2012;43:484-90.
    • (2012) Stroke , vol.43 , pp. 484-490
    • He, Z.1    Ostrowski, R.P.2    Sun, X.3    Ma, Q.4    Huang, B.5    Zhan, Y.6
  • 99
    • 0037072937 scopus 로고    scopus 로고
    • An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12
    • Morishima N, Nakanishi K, Takenouchi H, Shibata T, Yasuhiko Y. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J Biol Chem 2002;277:34287-94.
    • (2002) J Biol Chem , vol.277 , pp. 34287-34294
    • Morishima, N.1    Nakanishi, K.2    Takenouchi, H.3    Shibata, T.4    Yasuhiko, Y.5
  • 100
    • 23844481790 scopus 로고    scopus 로고
    • Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis
    • DOI 10.1074/jbc.M502685200
    • Obeng EA, Boise LH. Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis. J Biol Chem 2005;280:29578-87. (Pubitemid 41177033)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.33 , pp. 29578-29587
    • Obeng, E.A.1    Boise, L.H.2
  • 101
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • DOI 10.1038/47513
    • Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000;403:98-103. (Pubitemid 30038529)
    • (2000) Nature , vol.403 , Issue.6765 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 102
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • DOI 10.1093/emboj/cdg537
    • Hetz C, Russelakis-Carneiro M, Maundrell K, Castilla J, Soto C. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J 2003;22:5435-45. (Pubitemid 37279953)
    • (2003) EMBO Journal , vol.22 , Issue.20 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 103
    • 0037428823 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplasmic reticulum resident caspase, after permanent focal ischemia in rat
    • DOI 10.1097/00001756-200302100-00004
    • Mouw G, Zechel JL, Gamboa J, Lust WD, Selman WR, Ratcheson RA. Activation of caspase-12, an endoplasmic reticulum resident caspase, after permanent focal ischemia in rat. Neuroreport 2003;14:183-6. (Pubitemid 36308406)
    • (2003) NeuroReport , vol.14 , Issue.2 , pp. 183-186
    • Mouw, G.1    Zechel, J.L.2    Gamboa, J.3    Lust, W.D.4    Selman, W.R.5    Ratcheson, R.A.6
  • 104
    • 0035823579 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation
    • Rao RV, Hermel E, Castro-Obregon S, Del RG, Ellerby LM, Ellerby HM, et al. Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation. J Biol Chem 2001;276:33869-74.
    • (2001) J Biol Chem , vol.276 , pp. 33869-33874
    • Rao, R.V.1    Hermel, E.2    Castro-Obregon, S.3    Del, R.G.4    Ellerby, L.M.5    Ellerby, H.M.6
  • 105
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families: Activation of caspase-12 by calpain in apoptosis
    • DOI 10.1083/jcb.150.4.887
    • Nakagawa T, Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 2000;150:887-94. (Pubitemid 30663424)
    • (2000) Journal of Cell Biology , vol.150 , Issue.4 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 106
    • 0036791560 scopus 로고    scopus 로고
    • Caspase-12 processing and fragment translocation into nuclei of tunicamycin-treated cells
    • Fujita E, Kouroku Y, Jimbo A, Isoai A, Maruyama K, Momoi T. Caspase-12 processing and fragment translocation into nuclei of tunicamycin-treated cells. Cell Death Differ 2002;9:1108-14.
    • (2002) Cell Death Differ , vol.9 , pp. 1108-1114
    • Fujita, E.1    Kouroku, Y.2    Jimbo, A.3    Isoai, A.4    Maruyama, K.5    Momoi, T.6
  • 108
    • 79960672046 scopus 로고    scopus 로고
    • Endoplasmic reticulum Ca (2+) handling in excitable cells in health and disease
    • Stutzmann GE, Mattson MP. Endoplasmic reticulum Ca (2+) handling in excitable cells in health and disease. Pharmacol Rev 2011;63:700-27.
    • (2011) Pharmacol Rev , vol.63 , pp. 700-727
    • Stutzmann, G.E.1    Mattson, M.P.2
  • 109
    • 0022575011 scopus 로고
    • A model for receptor-regulated calcium entry
    • DOI 10.1016/0143-4160(86)90026-6
    • Putney JW Jr. A model for receptor-regulated calcium entry. Cell Calcium 1986;7:1-12. (Pubitemid 16130733)
    • (1986) Cell Calcium , vol.7 , Issue.1 , pp. 1-12
    • Putney Jr., J.W.1
  • 112
    • 0030882681 scopus 로고    scopus 로고
    • GOK: A gene at 11p15 involved in rhabdomyosarcoma and rhabdoid tumor development
    • Sabbioni S, Barbanti-Brodano G, Croce CM, Negrini M. GOK: a gene at 11p15 involved in rhabdomyosarcoma and rhabdoid tumor development. Cancer Res 1997;57:4493-7. (Pubitemid 27441051)
    • (1997) Cancer Research , vol.57 , Issue.20 , pp. 4493-4497
    • Sabbioni, S.1    Barbanti-Brodano, G.2    Croce, C.M.3    Negrini, M.4
  • 113
    • 33846021649 scopus 로고    scopus 로고
    • 2+ entry
    • DOI 10.1074/jbc.M608247200
    • Stathopulos PB, Li GY, Plevin MJ, Ames JB, Ikura M. Stored Ca2+ depletion-induced oligomerization of stromal interaction molecule 1 (STIM1) via the EF-SAM region: An initiation mechanism for capacitive Ca2+ entry. J Biol Chem 2006;281:35855-62. (Pubitemid 46041317)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.47 , pp. 35855-35862
    • Stathopulos, P.B.1    Li, G.-Y.2    Plevin, M.J.3    Ames, J.B.4    Ikura, M.5
  • 114
    • 53149128421 scopus 로고    scopus 로고
    • Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry
    • Stathopulos PB, Zheng L, Li GY, Plevin MJ, Ikura M. Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry. Cell 2008;135:110-22.
    • (2008) Cell , vol.135 , pp. 110-122
    • Stathopulos, P.B.1    Zheng, L.2    Li, G.Y.3    Plevin, M.J.4    Ikura, M.5
  • 115
    • 33748655172 scopus 로고    scopus 로고
    • Molecular identification of the CRAC channel by altered ion selectivity in a mutant of Orai
    • DOI 10.1038/nature05108, PII NATURE05108
    • Yeromin AV, Zhang SL, Jiang W, Yu Y, Safrina O, Cahalan MD. Molecular identification of the CRAC channel by altered ion selectivity in a mutant of Orai. Nature 2006;443:226-9. (Pubitemid 44387612)
    • (2006) Nature , vol.443 , Issue.7108 , pp. 226-229
    • Yeromin, A.V.1    Zhang, S.L.2    Jiang, W.3    Yu, Y.4    Safrina, O.5    Cahalan, M.D.6
  • 116
    • 77957332175 scopus 로고    scopus 로고
    • The CRAC channel activator STIM1 binds and inhibits L-type voltage-gated calcium channels
    • Park CY, Shcheglovitov A, Dolmetsch R. The CRAC channel activator STIM1 binds and inhibits L-type voltage-gated calcium channels. Science 2010;330:101-5.
    • (2010) Science , vol.330 , pp. 101-105
    • Park, C.Y.1    Shcheglovitov, A.2    Dolmetsch, R.3
  • 117
    • 77957349183 scopus 로고    scopus 로고
    • The calcium store sensor, STIM1, reciprocally controls Orai and CaV1.2 channels
    • Wang Y, Deng X, Mancarella S, Hendron E, Eguchi S, Soboloff J, et al. The calcium store sensor, STIM1, reciprocally controls Orai and CaV1.2 channels. Science 2010;330:105-9.
    • (2010) Science , vol.330 , pp. 105-109
    • Wang, Y.1    Deng, X.2    Mancarella, S.3    Hendron, E.4    Eguchi, S.5    Soboloff, J.6
  • 119
    • 84859717205 scopus 로고    scopus 로고
    • Neurotoxin-induced ER stress in mouse dopaminergic neurons involves downregulation of TRPC1 and inhibition of AKT/mTOR signaling
    • Selvaraj S, Sun Y, Watt JA, Wang S, Lei S, Birnbaumer L, et al. Neurotoxin-induced ER stress in mouse dopaminergic neurons involves downregulation of TRPC1 and inhibition of AKT/mTOR signaling. J Clin Invest 2012;122:1354-67.
    • (2012) J Clin Invest , vol.122 , pp. 1354-1367
    • Selvaraj, S.1    Sun, Y.2    Watt, J.A.3    Wang, S.4    Lei, S.5    Birnbaumer, L.6
  • 121
    • 79960532138 scopus 로고    scopus 로고
    • Sensing cellular stress through STIM proteins
    • Soboloff J, Madesh M, Gill DL. Sensing cellular stress through STIM proteins. Nat Chem Biol 2011;7:488-92.
    • (2011) Nat Chem Biol , vol.7 , pp. 488-492
    • Soboloff, J.1    Madesh, M.2    Gill, D.L.3
  • 122
    • 85027919657 scopus 로고    scopus 로고
    • Temperature-dependent STIM1 activation induces Ca (2) + influx and modulates gene expression
    • Xiao B, Coste B, Mathur J, Patapoutian A. Temperature-dependent STIM1 activation induces Ca (2) + influx and modulates gene expression. Nat Chem Biol 2011;7:351-8.
    • (2011) Nat Chem Biol , vol.7 , pp. 351-358
    • Xiao, B.1    Coste, B.2    Mathur, J.3    Patapoutian, A.4
  • 123
    • 67749114700 scopus 로고    scopus 로고
    • The short N-terminal domains of STIM1 and STIM2 control the activation kinetics of Orai1 channels
    • Zhou Y, Mancarella S, Wang Y, Yue C, Ritchie M, Gill DL, et al. The short N-terminal domains of STIM1 and STIM2 control the activation kinetics of Orai1 channels. J Biol Chem 2009;284:19164-8.
    • (2009) J Biol Chem , vol.284 , pp. 19164-19168
    • Zhou, Y.1    Mancarella, S.2    Wang, Y.3    Yue, C.4    Ritchie, M.5    Gill, D.L.6
  • 125
    • 37349129852 scopus 로고    scopus 로고
    • 2+ Levels
    • DOI 10.1016/j.cell.2007.11.039, PII S0092867407015437
    • Brandman O, Liou J, Park WS, Meyer T. STIM2 is a feedback regulator that stabilizes basal cytosolic and endoplasmic reticulum Ca2+ levels. Cell 2007;131:1327-39. (Pubitemid 350297421)
    • (2007) Cell , vol.131 , Issue.7 , pp. 1327-1339
    • Brandman, O.1    Liou, J.2    Park, W.S.3    Meyer, T.4
  • 126
    • 74549161843 scopus 로고    scopus 로고
    • STIM2 regulates capacitive Ca2+ entry in neurons and plays a key role in hypoxic neuronal cell death
    • Berna-Erro A, Braun A, Kraft R, Kleinschnitz C, Schuhmann MK, Stegner D, et al. STIM2 regulates capacitive Ca2+ entry in neurons and plays a key role in hypoxic neuronal cell death. Sci Signal 2009;2:ra67.
    • (2009) Sci Signal , vol.2
    • Berna-Erro, A.1    Braun, A.2    Kraft, R.3    Kleinschnitz, C.4    Schuhmann, M.K.5    Stegner, D.6
  • 130
    • 33646166316 scopus 로고    scopus 로고
    • The role of the endoplasmic reticulum in the accumulation of beta-amyloid peptide in Alzheimer's disease
    • Ghribi O. The role of the endoplasmic reticulum in the accumulation of beta-amyloid peptide in Alzheimer's disease. Curr Mol Med 2006;6:119-33.
    • (2006) Curr Mol Med , vol.6 , pp. 119-133
    • Ghribi, O.1
  • 131
    • 77953634580 scopus 로고    scopus 로고
    • ER calcium and Alzheimer's disease: In a state of flux
    • Mattson MP. ER calcium and Alzheimer's disease: in a state of flux. Sci Signal 2010;3:e10.
    • (2010) Sci Signal , vol.3
    • Mattson, M.P.1
  • 132
    • 74549169836 scopus 로고    scopus 로고
    • ER stress in Alzheimer's disease: A novel neuronal trigger for inflammation and Alzheimer's pathology
    • Salminen A, Kauppinen A, Suuronen T, Kaarniranta K, Ojala J. ER stress in Alzheimer's disease: a novel neuronal trigger for inflammation and Alzheimer's pathology. J Neuroinflammation 2009;6:41.
    • (2009) J Neuroinflammation , vol.6 , pp. 41
    • Salminen, A.1    Kauppinen, A.2    Suuronen, T.3    Kaarniranta, K.4    Ojala, J.5


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