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Volumn 30, Issue 9, 2013, Pages 2279-2289

Role of intracellular calcium in proteasome inhibitor-induced endoplasmic reticulum stress, Autophagy, and cell death

Author keywords

autophagy; cell death; ER stress; intracellular calcium; proteasome inhibitor

Indexed keywords

CALCIUM; PROTEASOME;

EID: 84883282553     PISSN: 07248741     EISSN: 1573904X     Source Type: Journal    
DOI: 10.1007/s11095-013-1139-8     Document Type: Article
Times cited : (53)

References (42)
  • 1
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • 9759494 10.1146/annurev.biochem.67.1.425 1:CAS:528:DyaK1cXlsFOmsLc%3D
    • Hershko A, Ciechanover A. The ubiquitin system. Annu Rev Biochem. 1998;67:425-79.
    • (1998) Annu Rev Biochem , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 2
    • 0038649638 scopus 로고    scopus 로고
    • The proteasome - An emerging therapeutic target in cancer
    • 12826633 10.1056/NEJMp030092
    • Mitchell BS. The proteasome - an emerging therapeutic target in cancer. N Engl J Med. 2003;348(26):2597-8.
    • (2003) N Engl J Med , vol.348 , Issue.26 , pp. 2597-2598
    • Mitchell, B.S.1
  • 3
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • 15144949 10.1016/S1535-6108(04)00120-5 1:CAS:528:DC%2BD2cXksFCmt7s%3D
    • Adams J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell. 2004;5(5):417-21.
    • (2004) Cancer Cell , vol.5 , Issue.5 , pp. 417-421
    • Adams, J.1
  • 4
    • 13844320703 scopus 로고    scopus 로고
    • Proteasome inhibition in multiple myeloma: Therapeutic implication
    • 15822185 10.1146/annurev.pharmtox.45.120403.100037 1:CAS:528: DC%2BD2MXisVWjtL0%3D
    • Chauhan D, Hideshima T, Anderson KC. Proteasome inhibition in multiple myeloma: therapeutic implication. Annu Rev Pharmacol Toxicol. 2005;45:465-76.
    • (2005) Annu Rev Pharmacol Toxicol , vol.45 , pp. 465-476
    • Chauhan, D.1    Hideshima, T.2    Anderson, K.C.3
  • 5
    • 35948986297 scopus 로고    scopus 로고
    • Absence of Bax switched MG132-induced apoptosis to non-apoptotic cell death that could be suppressed by transcriptional or translational inhibition
    • 10.1007/s10495-007-0142-0 1:CAS:528:DC%2BD2sXht1OksrzE
    • Ding WX, Ni HM, Yin XM. Absence of Bax switched MG132-induced apoptosis to non-apoptotic cell death that could be suppressed by transcriptional or translational inhibition. Apoptosis: Int J Programmed Cell Death. 2007;12(12):2233-44.
    • (2007) Apoptosis: Int J Programmed Cell Death , vol.12 , Issue.12 , pp. 2233-2244
    • Ding, W.X.1    Ni, H.M.2    Yin, X.M.3
  • 6
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • 15068787 10.1016/S1534-5807(04)00099-1 1:CAS:528:DC%2BD2cXjsFeqsbs%3D
    • Levine B, Klionsky DJ. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev Cell. 2004;6(4):463-77.
    • (2004) Dev Cell , vol.6 , Issue.4 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 7
    • 20344406240 scopus 로고    scopus 로고
    • Autophagy in metazoans: Cell survival in the land of plenty
    • 15928708 10.1038/nrm1660 1:CAS:528:DC%2BD2MXks1Gmtb0%3D
    • Lum JJ, DeBerardinis RJ, Thompson CB. Autophagy in metazoans: cell survival in the land of plenty. Nat Rev Mol Cell Biol. 2005;6(6):439-48.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.6 , pp. 439-448
    • Lum, J.J.1    Deberardinis, R.J.2    Thompson, C.B.3
  • 8
    • 0042322394 scopus 로고    scopus 로고
    • Autophagy in yeast: A TOR-mediated response to nutrient starvation
    • 14560952 10.1007/978-3-642-18930-2-5 1:CAS:528:DC%2BD3sXpt1SktbY%3D
    • Kamada Y, Sekito T, Ohsumi Y. Autophagy in yeast: a TOR-mediated response to nutrient starvation. Curr Top Microbiol Immunol. 2004;279:73-84.
    • (2004) Curr Top Microbiol Immunol , vol.279 , pp. 73-84
    • Kamada, Y.1    Sekito, T.2    Ohsumi, Y.3
  • 9
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • 17620365 10.2353/ajpath.2007.070188 1:CAS:528:DC%2BD2sXpsFaiu7w%3D
    • Ding WX, Ni HM, Gao W, Yoshimori T, Stolz DB, Ron D, et al. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol. 2007;171(2):513-24.
    • (2007) Am J Pathol , vol.171 , Issue.2 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6
  • 10
    • 75149175502 scopus 로고    scopus 로고
    • Proteasome inhibitors activate autophagy as a cytoprotective response in human prostate cancer cells
    • 19881538 10.1038/onc.2009.343 1:CAS:528:DC%2BD1MXhtlers7bK
    • Zhu K, Dunner Jr K, McConkey DJ. Proteasome inhibitors activate autophagy as a cytoprotective response in human prostate cancer cells. Oncogene. 2010;29(3):451-62.
    • (2010) Oncogene , vol.29 , Issue.3 , pp. 451-462
    • Zhu, K.1    Dunner, Jr.K.2    McConkey, D.J.3
  • 11
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • 16625205 10.1038/nature04723 1:CAS:528:DC%2BD28XlvVGlsbY%3D
    • Komatsu M, Waguri S, Chiba T, Murata S, Iwata J, Tanida I, et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature. 2006;441(7095):880-4.
    • (2006) Nature , vol.441 , Issue.7095 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 12
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • Korolchuk VI, Mansilla A, Menzies FM, Rubinsztein DC. Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol Cell. 2009;33(4):517-27.
    • (2009) Mol Cell. , vol.33 , Issue.4 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 13
    • 67651155954 scopus 로고    scopus 로고
    • Oncogenic transformation confers a selective susceptibility to the combined suppression of the proteasome and autophagy
    • 19584239 10.1158/1535-7163.MCT-08-1169 1:CAS:528:DC%2BD1MXosVymt7o%3D
    • Ding WX, Ni HM, Gao W, Chen X, Kang JH, Stolz DB, et al. Oncogenic transformation confers a selective susceptibility to the combined suppression of the proteasome and autophagy. Mol Cancer Ther. 2009;8(7):2036-45.
    • (2009) Mol Cancer Ther , vol.8 , Issue.7 , pp. 2036-2045
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Chen, X.4    Kang, J.H.5    Stolz, D.B.6
  • 14
    • 80052342419 scopus 로고    scopus 로고
    • PERK integrates autophagy and oxidative stress responses to promote survival during extracellular matrix detachment
    • 21709020 10.1128/MCB.05164-11 1:CAS:528:DC%2BC3MXhtV2gtbzJ
    • Avivar-Valderas A, Salas E, Bobrovnikova-Marjon E, Diehl JA, Nagi C, Debnath J, et al. PERK integrates autophagy and oxidative stress responses to promote survival during extracellular matrix detachment. Mol Cell Biol. 2011;31(17):3616-29.
    • (2011) Mol Cell Biol , vol.31 , Issue.17 , pp. 3616-3629
    • Avivar-Valderas, A.1    Salas, E.2    Bobrovnikova-Marjon, E.3    Diehl, J.A.4    Nagi, C.5    Debnath, J.6
  • 15
    • 79951847989 scopus 로고    scopus 로고
    • Principles and current strategies for targeting autophagy for cancer treatment
    • 21325294 10.1158/1078-0432.CCR-10-2634 1:CAS:528:DC%2BC3MXitVSqtLc%3D
    • Amaravadi RK, Lippincott-Schwartz J, Yin XM, Weiss WA, Takebe N, Timmer W, et al. Principles and current strategies for targeting autophagy for cancer treatment. Clin Cancer Res. 2011;17(4):654-66.
    • (2011) Clin Cancer Res , vol.17 , Issue.4 , pp. 654-666
    • Amaravadi, R.K.1    Lippincott-Schwartz, J.2    Yin, X.M.3    Weiss, W.A.4    Takebe, N.5    Timmer, W.6
  • 16
    • 0025332577 scopus 로고
    • Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase
    • 2138778 10.1073/pnas.87.7.2466 1:CAS:528:DyaK3cXhvFemurk%3D
    • Thastrup O, Cullen PJ, Drobak BK, Hanley MR, Dawson AP. Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase. Proc Natl Acad Sci U S A. 1990;87(7):2466-70.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , Issue.7 , pp. 2466-2470
    • Thastrup, O.1    Cullen, P.J.2    Drobak, B.K.3    Hanley, M.R.4    Dawson, A.P.5
  • 17
    • 33846189759 scopus 로고    scopus 로고
    • Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-beta, and Bcl-2
    • 17244528 10.1016/j.molcel.2006.12.009
    • Hoyer-Hansen M, Bastholm L, Szyniarowski P, Campanella M, Szabadkai G, Farkas T, et al. Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-beta, and Bcl-2. Mol Cell. 2007;25(2):193-205.
    • (2007) Mol Cell , vol.25 , Issue.2 , pp. 193-205
    • Hoyer-Hansen, M.1    Bastholm, L.2    Szyniarowski, P.3    Campanella, M.4    Szabadkai, G.5    Farkas, T.6
  • 18
    • 50249137038 scopus 로고    scopus 로고
    • Induction of macroautophagy by exogenously introduced calcium
    • 18560273 1:CAS:528:DC%2BD1cXhtVynt7jK
    • Gao W, Ding WX, Stolz DB, Yin XM. Induction of macroautophagy by exogenously introduced calcium. Autophagy. 2008;4(6):754-61.
    • (2008) Autophagy , vol.4 , Issue.6 , pp. 754-761
    • Gao, W.1    Ding, W.X.2    Stolz, D.B.3    Yin, X.M.4
  • 19
    • 65249089754 scopus 로고    scopus 로고
    • Methodological considerations for assessing autophagy modulators: A study with calcium phosphate precipitates
    • 19182529 10.4161/auto.5.3.7664 1:CAS:528:DC%2BD1MXnvVyku7g%3D
    • Sarkar S, Korolchuk V, Renna M, Winslow A, Rubinsztein DC. Methodological considerations for assessing autophagy modulators: a study with calcium phosphate precipitates. Autophagy. 2009;5(3):307-13.
    • (2009) Autophagy , vol.5 , Issue.3 , pp. 307-313
    • Sarkar, S.1    Korolchuk, V.2    Renna, M.3    Winslow, A.4    Rubinsztein, D.C.5
  • 20
    • 42249106042 scopus 로고    scopus 로고
    • Novel targets for Huntington's disease in an mTOR-independent autophagy pathway
    • 18391949 10.1038/nchembio.79 1:CAS:528:DC%2BD1cXkvVSmt7c%3D
    • Williams A, Sarkar S, Cuddon P, Ttofi EK, Saiki S, Siddiqi FH, et al. Novel targets for Huntington's disease in an mTOR-independent autophagy pathway. Nat Chem Biol. 2008;4(5):295-305.
    • (2008) Nat Chem Biol , vol.4 , Issue.5 , pp. 295-305
    • Williams, A.1    Sarkar, S.2    Cuddon, P.3    Ttofi, E.K.4    Saiki, S.5    Siddiqi, F.H.6
  • 21
    • 84870880174 scopus 로고    scopus 로고
    • The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes
    • 23217709 10.1016/j.cell.2012.11.001 1:CAS:528:DC%2BC38XhvVaisrvK
    • Itakura E, Kishi-Itakura C, Mizushima N. The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes. Cell. 2012;151(6):1256-69.
    • (2012) Cell , vol.151 , Issue.6 , pp. 1256-1269
    • Itakura, E.1    Kishi-Itakura, C.2    Mizushima, N.3
  • 22
    • 7244255989 scopus 로고    scopus 로고
    • Role for Rab7 in maturation of late autophagic vacuoles
    • 15340014 10.1242/jcs.01370
    • Jager S, Bucci C, Tanida I, Ueno T, Kominami E, Saftig P, et al. Role for Rab7 in maturation of late autophagic vacuoles. J Cell Sci. 2004;117(Pt 20):4837-48.
    • (2004) J Cell Sci , vol.117 , Issue.PART 20 , pp. 4837-4848
    • Jager, S.1    Bucci, C.2    Tanida, I.3    Ueno, T.4    Kominami, E.5    Saftig, P.6
  • 23
    • 69449089915 scopus 로고    scopus 로고
    • How do ESCRT proteins control autophagy?
    • 19535733 10.1242/jcs.050021 1:CAS:528:DC%2BD1MXps1ehsb0%3D
    • Rusten TE, Stenmark H. How do ESCRT proteins control autophagy? J Cell Sci. 2009;122(Pt 13):2179-83.
    • (2009) J Cell Sci , vol.122 , Issue.PART 13 , pp. 2179-2183
    • Rusten, T.E.1    Stenmark, H.2
  • 25
    • 0034729167 scopus 로고    scopus 로고
    • The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles
    • 10831609 10.1083/jcb.149.5.1053 1:CAS:528:DC%2BD3cXjvFejs7Y%3D
    • Pryor PR, Mullock BM, Bright NA, Gray SR, Luzio JP. The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. J Cell Biol. 2000;149(5):1053-62.
    • (2000) J Cell Biol , vol.149 , Issue.5 , pp. 1053-1062
    • Pryor, P.R.1    Mullock, B.M.2    Bright, N.A.3    Gray, S.R.4    Luzio, J.P.5
  • 26
    • 79959346132 scopus 로고    scopus 로고
    • Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest
    • 21700220 10.1016/j.molcel.2011.04.024 1:CAS:528:DC%2BC3MXotVChtrY%3D
    • Ganley IG, Wong PM, Gammoh N, Jiang X. Distinct autophagosomal-lysosomal fusion mechanism revealed by thapsigargin-induced autophagy arrest. Mol Cell. 2011;42(6):731-43.
    • (2011) Mol Cell , vol.42 , Issue.6 , pp. 731-743
    • Ganley, I.G.1    Wong, P.M.2    Gammoh, N.3    Jiang, X.4
  • 27
    • 34250787966 scopus 로고    scopus 로고
    • Proteasome inhibitor lactacystin disturbs the intracellular calcium homeostasis of dopamine neurons in ventral mesencephalic cultures
    • 17561309 10.1016/j.neuint.2007.04.014 1:CAS:528:DC%2BD2sXmvVKmsLg%3D
    • Li X, Yang D, Li L, Peng C, Chen S, Le W. Proteasome inhibitor lactacystin disturbs the intracellular calcium homeostasis of dopamine neurons in ventral mesencephalic cultures. Neurochem Int. 2007;50(7-8):959-65.
    • (2007) Neurochem Int , vol.50 , Issue.7-8 , pp. 959-965
    • Li, X.1    Yang, D.2    Li, L.3    Peng, C.4    Chen, S.5    Le, W.6
  • 28
    • 0034602188 scopus 로고    scopus 로고
    • Role of BAX in the apoptotic response to anticancer agents
    • 11062132 10.1126/science.290.5493.989 1:CAS:528:DC%2BD3cXnvVWku7w%3D
    • Zhang L, Yu J, Park BH, Kinzler KW, Vogelstein B. Role of BAX in the apoptotic response to anticancer agents. Science. 2000;290(5493):989-92.
    • (2000) Science , vol.290 , Issue.5493 , pp. 989-992
    • Zhang, L.1    Yu, J.2    Park, B.H.3    Kinzler, K.W.4    Vogelstein, B.5
  • 29
    • 84871279726 scopus 로고    scopus 로고
    • Parkin and mitofusins reciprocally regulate mitophagy and mitochondrial spheroid formation
    • 23095748 10.1074/jbc.M112.413682 1:CAS:528:DC%2BC38Xhslyks7rJ
    • Ding WX, Guo F, Ni HM, Bockus A, Manley S, Stolz DB, et al. Parkin and mitofusins reciprocally regulate mitophagy and mitochondrial spheroid formation. J Biol Chem. 2012;287(50):42379-88.
    • (2012) J Biol Chem , vol.287 , Issue.50 , pp. 42379-42388
    • Ding, W.X.1    Guo, F.2    Ni, H.M.3    Bockus, A.4    Manley, S.5    Stolz, D.B.6
  • 30
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • 9639028 10.1247/csf.23.33 1:CAS:528:DyaK1cXivFWmu7Y%3D
    • Yamamoto A, Tagawa Y, Yoshimori T, Moriyama Y, Masaki R, Tashiro Y. Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct Funct. 1998;23(1):33-42.
    • (1998) Cell Struct Funct , vol.23 , Issue.1 , pp. 33-42
    • Yamamoto, A.1    Tagawa, Y.2    Yoshimori, T.3    Moriyama, Y.4    Masaki, R.5    Tashiro, Y.6
  • 31
    • 34547897405 scopus 로고    scopus 로고
    • IP3 receptor/Ca2+ channel: From discovery to new signaling concepts
    • 17697045 10.1111/j.1471-4159.2007.04825.x 1:CAS:528:DC%2BD2sXhtVWnt73E
    • Mikoshiba K. IP3 receptor/Ca2+ channel: from discovery to new signaling concepts. J Neurochem. 2007;102(5):1426-46.
    • (2007) J Neurochem , vol.102 , Issue.5 , pp. 1426-1446
    • Mikoshiba, K.1
  • 32
    • 0038420824 scopus 로고    scopus 로고
    • 2-Aminoethoxydiphenyl borate (2-APB) antagonises inositol 1,4,5-trisphosphate-induced calcium release, inhibits calcium pumps and has a use-dependent and slowly reversible action on store-operated calcium entry channels
    • 12767897 10.1016/S0143-4160(03)00026-5 1:CAS:528:DC%2BD3sXktFGitr4%3D
    • Peppiatt CM, Collins TJ, Mackenzie L, Conway SJ, Holmes AB, Bootman MD, et al. 2-Aminoethoxydiphenyl borate (2-APB) antagonises inositol 1,4,5-trisphosphate-induced calcium release, inhibits calcium pumps and has a use-dependent and slowly reversible action on store-operated calcium entry channels. Cell Calcium. 2003;34(1):97-108.
    • (2003) Cell Calcium , vol.34 , Issue.1 , pp. 97-108
    • Peppiatt, C.M.1    Collins, T.J.2    Mackenzie, L.3    Conway, S.J.4    Holmes, A.B.5    Bootman, M.D.6
  • 33
    • 79551553480 scopus 로고    scopus 로고
    • Dissecting the dynamic turnover of GFP-LC3 in the autolysosome
    • 21107021 10.4161/auto.7.2.14181 1:CAS:528:DC%2BC3MXivVSmu7k%3D
    • Ni HM, Bockus A, Wozniak AL, Jones K, Weinman S, Yin XM, et al. Dissecting the dynamic turnover of GFP-LC3 in the autolysosome. Autophagy. 2011;7(2):188-204.
    • (2011) Autophagy , vol.7 , Issue.2 , pp. 188-204
    • Ni, H.M.1    Bockus, A.2    Wozniak, A.L.3    Jones, K.4    Weinman, S.5    Yin, X.M.6
  • 34
    • 84862295360 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy
    • 22966490 10.4161/auto.19496 1:CAS:528:DC%2BC38Xht1art7zK
    • Klionsky DJ, Abdalla FC, Abeliovich H, Abraham RT, Acevedo-Arozena A, Adeli K, et al. Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy. 2012;8(4):445-544.
    • (2012) Autophagy , vol.8 , Issue.4 , pp. 445-544
    • Klionsky, D.J.1    Abdalla, F.C.2    Abeliovich, H.3    Abraham, R.T.4    Acevedo-Arozena, A.5    Adeli, K.6
  • 35
    • 84869498677 scopus 로고    scopus 로고
    • Targeting autophagy for the treatment of liver diseases
    • 22871337 10.1016/j.phrs.2012.07.003 1:CAS:528:DC%2BC38XhslSmt7nP
    • Ni HM, Williams JA, Yang H, Shi YH, Fan J, Ding WX. Targeting autophagy for the treatment of liver diseases. Pharmacol Res. 2012;66(6):463-74.
    • (2012) Pharmacol Res , vol.66 , Issue.6 , pp. 463-474
    • Ni, H.M.1    Williams, J.A.2    Yang, H.3    Shi, Y.H.4    Fan, J.5    Ding, W.X.6
  • 36
    • 46349090290 scopus 로고    scopus 로고
    • The sarcoplasmic reticulum: An organized patchwork of specialized domains
    • 18266914 10.1111/j.1600-0854.2008.00717.x 1:CAS:528:DC%2BD1cXotlKksr8%3D
    • Rossi D, Barone V, Giacomello E, Cusimano V, Sorrentino V. The sarcoplasmic reticulum: an organized patchwork of specialized domains. Traffic. 2008;9(7):1044-9.
    • (2008) Traffic , vol.9 , Issue.7 , pp. 1044-1049
    • Rossi, D.1    Barone, V.2    Giacomello, E.3    Cusimano, V.4    Sorrentino, V.5
  • 37
    • 24644438715 scopus 로고    scopus 로고
    • Intraluminal calcium as a primary regulator of endoplasmic reticulum function
    • 16076486 10.1016/j.ceca.2005.06.010 1:CAS:528:DC%2BD2MXpvV2ls70%3D
    • Burdakov D, Petersen OH, Verkhratsky A. Intraluminal calcium as a primary regulator of endoplasmic reticulum function. Cell Calcium. 2005;38(3-4):303-10.
    • (2005) Cell Calcium , vol.38 , Issue.3-4 , pp. 303-310
    • Burdakov, D.1    Petersen, O.H.2    Verkhratsky, A.3
  • 38
    • 0036877146 scopus 로고    scopus 로고
    • Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum
    • 12543089 10.1016/S0143416002001884 1:CAS:528:DC%2BD3sXhtFKntbw%3D
    • Michalak M, Robert Parker JM, Opas M. Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium. 2002;32(5-6):269-78.
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 269-278
    • Michalak, M.1    Robert Parker, J.M.2    Opas, M.3
  • 39
    • 33947497050 scopus 로고    scopus 로고
    • Differential effects of endoplasmic reticulum stress-induced autophagy on cell survival
    • 17135238 10.1074/jbc.M609267200 1:CAS:528:DC%2BD2sXhsFKgsLs%3D
    • Ding WX, Ni HM, Gao W, Hou YF, Melan MA, Chen X, et al. Differential effects of endoplasmic reticulum stress-induced autophagy on cell survival. J Biol Chem. 2007;282(7):4702-10.
    • (2007) J Biol Chem , vol.282 , Issue.7 , pp. 4702-4710
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Hou, Y.F.4    Melan, M.A.5    Chen, X.6
  • 40
    • 77956322223 scopus 로고    scopus 로고
    • The molecular identity of the mitochondrial Ca2+ sequestration system
    • 20659159 10.1111/j.1742-4658.2010.07756.x 1:CAS:528:DC%2BC3cXhtFygsrrM
    • Starkov AA. The molecular identity of the mitochondrial Ca2+ sequestration system. FEBS J. 2010;277(18):3652-63.
    • (2010) FEBS J , vol.277 , Issue.18 , pp. 3652-3663
    • Starkov, A.A.1
  • 41
    • 0027495705 scopus 로고
    • Dependence of hepatocytic autophagy on intracellularly sequestered calcium
    • 8253727 1:CAS:528:DyaK3sXmsVKlsr8%3D
    • Gordon PB, Holen I, Fosse M, Rotnes JS, Seglen PO. Dependence of hepatocytic autophagy on intracellularly sequestered calcium. J Biol Chem. 1993;268(35):26107-12.
    • (1993) J Biol Chem , vol.268 , Issue.35 , pp. 26107-26112
    • Gordon, P.B.1    Holen, I.2    Fosse, M.3    Rotnes, J.S.4    Seglen, P.O.5
  • 42
    • 80051470524 scopus 로고    scopus 로고
    • Lysosomal Ca(2+) homeostasis: Role in pathogenesis of lysosomal storage diseases
    • 21724254 10.1016/j.ceca.2011.03.010 1:CAS:528:DC%2BC3MXhtVaisLjO
    • Lloyd-Evans E, Platt FM. Lysosomal Ca(2+) homeostasis: role in pathogenesis of lysosomal storage diseases. Cell Calcium. 2011;50(2):200-5.
    • (2011) Cell Calcium , vol.50 , Issue.2 , pp. 200-205
    • Lloyd-Evans, E.1    Platt, F.M.2


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