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Volumn 5, Issue APR, 2015, Pages

Stress responses from the endoplasmic reticulum in cancer

Author keywords

Cancer; Endoplasmic reticulum; ER stress; Mitochondria associated ER membrane; Unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; CRYOPYRIN; GLYCEROPHOSPHOLIPID; INOSITOL REQUIRING ENZYME 1 ALPHA; MITOFUSIN 1; MITOFUSIN 2; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN IRE1; RIBONUCLEASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SPHINGOLIPID; UNCLASSIFIED DRUG; X BOX BINDING PROTEIN 1;

EID: 84934755624     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2015.00093     Document Type: Review
Times cited : (76)

References (194)
  • 1
    • 33947286240 scopus 로고    scopus 로고
    • Fatty acid synthesis and elongation in yeast
    • Tehlivets O, Scheuringer K, Kohlwein SD. Fatty acid synthesis and elongation in yeast. Biochim Biophys Acta (2007) 1771:255-70. doi: 10.1016/j.bbalip.2006.07.004
    • (2007) Biochim Biophys Acta , vol.1771 , pp. 255-270
    • Tehlivets, O.1    Scheuringer, K.2    Kohlwein, S.D.3
  • 2
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen B, Braakman I. Protein folding and quality control in the endoplasmic reticulum. Curr Opin Cell Biol (2004) 16:343-9. doi:10.1016/j.ceb.2004.08.003
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 3
    • 2342572271 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in mammalian cells
    • Vance JE, Vance DE. Phospholipid biosynthesis in mammalian cells. Biochem Cell Biol (2004) 82:113-28. doi:10.1139/o03-073
    • (2004) Biochem Cell Biol , vol.82 , pp. 113-128
    • Vance, J.E.1    Vance, D.E.2
  • 4
    • 0041534405 scopus 로고    scopus 로고
    • Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability
    • Brostrom MA, Brostrom CO. Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability. Cell Calcium (2003) 34:345-63. doi:10.1016/S0143-4160(03)00127-1
    • (2003) Cell Calcium , vol.34 , pp. 345-363
    • Brostrom, M.A.1    Brostrom, C.O.2
  • 5
    • 0036877142 scopus 로고    scopus 로고
    • The endoplasmic reticulum: a multifunctional signaling organelle
    • Berridge MJ. The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium (2002) 32:235-49. doi:10.1016/S0143416002001823
    • (2002) Cell Calcium , vol.32 , pp. 235-249
    • Berridge, M.J.1
  • 6
    • 0037067649 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages
    • Gagnon E, Duclos S, Rondeau C, Chevet E, Cameron PH, Steele-Mortimer O, et al. Endoplasmic reticulum-mediated phagocytosis is a mechanism of entry into macrophages. Cell (2002) 110:119-31. doi:10.1016/S0092-8674(02)00797-3
    • (2002) Cell , vol.110 , pp. 119-131
    • Gagnon, E.1    Duclos, S.2    Rondeau, C.3    Chevet, E.4    Cameron, P.H.5    Steele-Mortimer, O.6
  • 7
    • 84863740827 scopus 로고    scopus 로고
    • The impact of the unfolded protein response on human disease
    • Wang S, Kaufman RJ. The impact of the unfolded protein response on human disease. J Cell Biol (2012) 197:857-67. doi:10.1083/jcb.201110131
    • (2012) J Cell Biol , vol.197 , pp. 857-867
    • Wang, S.1    Kaufman, R.J.2
  • 8
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol (2007) 8:519-29. doi:10.1038/nrm2199
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 9
    • 84875242776 scopus 로고    scopus 로고
    • Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains
    • Volmer R, Van Der Ploeg K, Ron D. Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains. Proc Natl Acad Sci U S A (2013) 110:4628-33. doi:10.1073/pnas.1217611110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 4628-4633
    • Volmer, R.1    Van Der Ploeg, K.2    Ron, D.3
  • 10
    • 84883163223 scopus 로고    scopus 로고
    • Membrane lipid saturation activates IRE1alpha without inducing clustering
    • Kitai Y, Ariyama H, Kono N, Oikawa D, Iwawaki T, Arai H. Membrane lipid saturation activates IRE1alpha without inducing clustering. Genes Cells (2013) 18:798-809. doi:10.1111/gtc.12074
    • (2013) Genes Cells , vol.18 , pp. 798-809
    • Kitai, Y.1    Ariyama, H.2    Kono, N.3    Oikawa, D.4    Iwawaki, T.5    Arai, H.6
  • 12
    • 77954579285 scopus 로고    scopus 로고
    • Decrease in membrane phospholipid unsaturation induces unfolded protein response
    • Ariyama H, Kono N, Matsuda S, Inoue T, Arai H. Decrease in membrane phospholipid unsaturation induces unfolded protein response. J Biol Chem (2010) 285:22027-35. doi:10.1074/jbc.M110.126870
    • (2010) J Biol Chem , vol.285 , pp. 22027-22035
    • Ariyama, H.1    Kono, N.2    Matsuda, S.3    Inoue, T.4    Arai, H.5
  • 13
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • Hotamisligil GS. Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell (2010) 140:900-17. doi:10.1016/j.cell.2010.02.034
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 14
    • 0025332577 scopus 로고
    • Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase
    • 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) 87:2466-70. doi:10.1073/pnas.87.7.2466
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 2466-2470
    • Thastrup, O.1    Cullen, P.J.2    Drobak, B.K.3    Hanley, M.R.4    Dawson, A.P.5
  • 15
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: coping with stress
    • Rutkowski DT, Kaufman RJ. A trip to the ER: coping with stress. Trends Cell Biol (2004) 14:20-8. doi:10.1016/j.tcb.2003.11.001
    • (2004) Trends Cell Biol , vol.14 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 16
    • 34248571826 scopus 로고    scopus 로고
    • GRP78 induction in cancer: therapeutic and prognostic implications
    • Lee AS. GRP78 induction in cancer: therapeutic and prognostic implications. Cancer Res (2007) 67:3496-9. doi:10.1158/0008-5472.CAN-07-0325
    • (2007) Cancer Res , vol.67 , pp. 3496-3499
    • Lee, A.S.1
  • 17
    • 36348943088 scopus 로고    scopus 로고
    • Integrated endoplasmic reticulum stress responses in cancer
    • Moenner M, Pluquet O, Bouchecareilh M, Chevet E. Integrated endoplasmic reticulum stress responses in cancer. Cancer Res (2007) 67:10631-4. doi:10.1158/0008-5472.CAN-07-1705
    • (2007) Cancer Res , vol.67 , pp. 10631-10634
    • Moenner, M.1    Pluquet, O.2    Bouchecareilh, M.3    Chevet, E.4
  • 18
    • 4344660747 scopus 로고    scopus 로고
    • XBP1 is essential for survival under hypoxic conditions and is required for tumor growth
    • Romero-Ramirez L, Cao H, Nelson D, Hammond E, Lee AH, Yoshida H, et al. XBP1 is essential for survival under hypoxic conditions and is required for tumor growth. Cancer Res (2004) 64:5943-7. doi:10.1158/0008-5472.CAN-04-1606
    • (2004) Cancer Res , vol.64 , pp. 5943-5947
    • Romero-Ramirez, L.1    Cao, H.2    Nelson, D.3    Hammond, E.4    Lee, A.H.5    Yoshida, H.6
  • 19
    • 33749022800 scopus 로고    scopus 로고
    • Structural and functional features and significance of the physical linkage between ER and mitochondria
    • Csordas G, Renken C, Varnai P, Walter L, Weaver D, Buttle KF, et al. Structural and functional features and significance of the physical linkage between ER and mitochondria. J Cell Biol (2006) 174:915-21. doi:10.1083/jcb.200604016
    • (2006) J Cell Biol , vol.174 , pp. 915-921
    • Csordas, G.1    Renken, C.2    Varnai, P.3    Walter, L.4    Weaver, D.5    Buttle, K.F.6
  • 20
    • 0032511112 scopus 로고    scopus 로고
    • Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses
    • Rizzuto R, Pinton P, Carrington W, Fay FS, Fogarty KE, Lifshitz LM, et al. Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses. Science (1998) 280:1763-6. doi:10.1126/science.280.5370.1763
    • (1998) Science , vol.280 , pp. 1763-1766
    • Rizzuto, R.1    Pinton, P.2    Carrington, W.3    Fay, F.S.4    Fogarty, K.E.5    Lifshitz, L.M.6
  • 21
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • De Brito OM, Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature (2008) 456:605-10. doi:10.1038/nature07534
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 22
    • 33845692166 scopus 로고    scopus 로고
    • Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
    • Szabadkai G, Bianchi K, Varnai P, De Stefani D, Wieckowski MR, Cavagna D, et al. Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels. J Cell Biol (2006) 175:901-11. doi:10.1083/jcb.200608073
    • (2006) J Cell Biol , vol.175 , pp. 901-911
    • Szabadkai, G.1    Bianchi, K.2    Varnai, P.3    De Stefani, D.4    Wieckowski, M.R.5    Cavagna, D.6
  • 23
    • 79551600416 scopus 로고    scopus 로고
    • Fis1 and Bap31 bridge the mitochondria-ER interface to establish a platform for apoptosis induction
    • Iwasawa R, Mahul-Mellier AL, Datler C, Pazarentzos E, Grimm S. Fis1 and Bap31 bridge the mitochondria-ER interface to establish a platform for apoptosis induction. EMBO J (2011) 30:556-68. doi:10.1038/emboj.2010.346
    • (2011) EMBO J , vol.30 , pp. 556-568
    • Iwasawa, R.1    Mahul-Mellier, A.L.2    Datler, C.3    Pazarentzos, E.4    Grimm, S.5
  • 24
    • 84863393591 scopus 로고    scopus 로고
    • VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis
    • De Vos KJ, Morotz GM, Stoica R, Tudor EL, Lau KF, Ackerley S, et al. VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis. Hum Mol Genet (2012) 21:1299-311. doi:10.1093/hmg/ddr559
    • (2012) Hum Mol Genet , vol.21 , pp. 1299-1311
    • De Vos, K.J.1    Morotz, G.M.2    Stoica, R.3    Tudor, E.L.4    Lau, K.F.5    Ackerley, S.6
  • 25
    • 0027973135 scopus 로고
    • A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins
    • Rusinol AE, Cui Z, Chen MH, Vance JE. A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins. J Biol Chem (1994) 269:27494-502.
    • (1994) J Biol Chem , vol.269 , pp. 27494-27502
    • Rusinol, A.E.1    Cui, Z.2    Chen, M.H.3    Vance, J.E.4
  • 26
    • 0026088027 scopus 로고
    • Newly made phosphatidylserine and phosphatidylethanolamine are preferentially translocated between rat liver mitochondria and endoplasmic reticulum
    • Vance JE. Newly made phosphatidylserine and phosphatidylethanolamine are preferentially translocated between rat liver mitochondria and endoplasmic reticulum. J Biol Chem (1991) 266:89-97.
    • (1991) J Biol Chem , vol.266 , pp. 89-97
    • Vance, J.E.1
  • 27
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance JE. Phospholipid synthesis in a membrane fraction associated with mitochondria. J Biol Chem (1990) 265:7248-56.
    • (1990) J Biol Chem , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 28
    • 0141754206 scopus 로고    scopus 로고
    • Stable interactions between mitochondria and endoplasmic reticulum allow rapid accumulation of calcium in a subpopulation of mitochondria
    • Filippin L, Magalhaes PJ, Di Benedetto G, Colella M, Pozzan T. Stable interactions between mitochondria and endoplasmic reticulum allow rapid accumulation of calcium in a subpopulation of mitochondria. J Biol Chem (2003) 278:39224-34. doi:10.1074/jbc.M302301200
    • (2003) J Biol Chem , vol.278 , pp. 39224-39234
    • Filippin, L.1    Magalhaes, P.J.2    Di Benedetto, G.3    Colella, M.4    Pozzan, T.5
  • 29
    • 0027340729 scopus 로고
    • Microdomains with high Ca2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria
    • Rizzuto R, Brini M, Murgia M, Pozzan T. Microdomains with high Ca2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria. Science (1993) 262:744-7. doi:10.1126/science.8235595
    • (1993) Science , vol.262 , pp. 744-747
    • Rizzuto, R.1    Brini, M.2    Murgia, M.3    Pozzan, T.4
  • 30
    • 77955041880 scopus 로고    scopus 로고
    • Essential regulation of cell bioenergetics by constitutive InsP3 receptor Ca2+ transfer to mitochondria
    • Cardenas C, Miller RA, Smith I, Bui T, Molgo J, Muller M, et al. Essential regulation of cell bioenergetics by constitutive InsP3 receptor Ca2+ transfer to mitochondria. Cell (2010) 142:270-83. doi:10.1016/j.cell.2010.06.007
    • (2010) Cell , vol.142 , pp. 270-283
    • Cardenas, C.1    Miller, R.A.2    Smith, I.3    Bui, T.4    Molgo, J.5    Muller, M.6
  • 31
    • 70449088871 scopus 로고    scopus 로고
    • GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca(2+)-dependent mitochondrial apoptosis
    • Sano R, Annunziata I, Patterson A, Moshiach S, Gomero E, Opferman J, et al. GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca(2+)-dependent mitochondrial apoptosis. Mol Cell (2009) 36:500-11. doi:10.1016/j.molcel.2009.10.021
    • (2009) Mol Cell , vol.36 , pp. 500-511
    • Sano, R.1    Annunziata, I.2    Patterson, A.3    Moshiach, S.4    Gomero, E.5    Opferman, J.6
  • 32
    • 33748325741 scopus 로고    scopus 로고
    • Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER
    • Browman DT, Resek ME, Zajchowski LD, Robbins SM. Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER. J Cell Sci (2006) 119:3149-60. doi:10.1242/jcs.03060
    • (2006) J Cell Sci , vol.119 , pp. 3149-3160
    • Browman, D.T.1    Resek, M.E.2    Zajchowski, L.D.3    Robbins, S.M.4
  • 33
    • 0037924355 scopus 로고    scopus 로고
    • Sigma-1 receptors (sigma(1) binding sites) form raft-like microdomains and target lipid droplets on the endoplasmic reticulum: roles in endoplasmic reticulum lipid compartmentalization and export
    • Hayashi T, Su TP. Sigma-1 receptors (sigma(1) binding sites) form raft-like microdomains and target lipid droplets on the endoplasmic reticulum: roles in endoplasmic reticulum lipid compartmentalization and export. J Pharmacol Exp Ther (2003) 306:718-25. doi:10.1124/jpet.103.051284
    • (2003) J Pharmacol Exp Ther , vol.306 , pp. 718-725
    • Hayashi, T.1    Su, T.P.2
  • 34
    • 0035816532 scopus 로고    scopus 로고
    • Acyl-CoA synthetase isoforms 1, 4, and 5 are present in different subcellular membranes in rat liver and can be inhibited independently
    • Lewin TM, Kim JH, Granger DA, Vance JE, Coleman RA. Acyl-CoA synthetase isoforms 1, 4, and 5 are present in different subcellular membranes in rat liver and can be inhibited independently. J Biol Chem (2001) 276:24674-9. doi:10.1074/jbc.M102036200
    • (2001) J Biol Chem , vol.276 , pp. 24674-24679
    • Lewin, T.M.1    Kim, J.H.2    Granger, D.A.3    Vance, J.E.4    Coleman, R.A.5
  • 35
    • 0034602158 scopus 로고    scopus 로고
    • Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes
    • Stone SJ, Vance JE. Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes. J Biol Chem (2000) 275:34534-40. doi:10.1074/jbc.M002865200
    • (2000) J Biol Chem , vol.275 , pp. 34534-34540
    • Stone, S.J.1    Vance, J.E.2
  • 36
    • 84863837081 scopus 로고    scopus 로고
    • Lipid metabolism in cancer
    • Santos CR, Schulze A. Lipid metabolism in cancer. FEBS J (2012) 279:2610-23. doi:10.1111/j.1742-4658.2012.08644.x
    • (2012) FEBS J , vol.279 , pp. 2610-2623
    • Santos, C.R.1    Schulze, A.2
  • 38
    • 3543114272 scopus 로고    scopus 로고
    • Biologically active sphingolipids in cancer pathogenesis and treatment
    • Ogretmen B, Hannun YA. Biologically active sphingolipids in cancer pathogenesis and treatment. Nat Rev Cancer (2004) 4:604-16. doi:10.1038/nrc1411
    • (2004) Nat Rev Cancer , vol.4 , pp. 604-616
    • Ogretmen, B.1    Hannun, Y.A.2
  • 39
    • 84904967279 scopus 로고    scopus 로고
    • New functions of mitochondria associated membranes in cellular signaling
    • Van Vliet AR, Verfaillie T, Agostinis P. New functions of mitochondria associated membranes in cellular signaling. Biochim Biophys Acta (2014) 1843:2253-62. doi:10.1016/j.bbamcr.2014.03.009
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 2253-2262
    • Van Vliet, A.R.1    Verfaillie, T.2    Agostinis, P.3
  • 40
    • 84871726622 scopus 로고    scopus 로고
    • Where the endoplasmic reticulum and the mitochondrion tie the knot: the mitochondria-associated membrane (MAM)
    • Raturi A, Simmen T. Where the endoplasmic reticulum and the mitochondrion tie the knot: the mitochondria-associated membrane (MAM). Biochim Biophys Acta (2013) 1833:213-24. doi:10.1016/j.bbamcr.2012.04.013
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 213-224
    • Raturi, A.1    Simmen, T.2
  • 41
    • 77953725586 scopus 로고    scopus 로고
    • Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM)
    • Simmen T, Lynes EM, Gesson K, Thomas G. Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM). Biochim Biophys Acta (2010) 1798:1465-73. doi:10.1016/j.bbamem.2010.04.009
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1465-1473
    • Simmen, T.1    Lynes, E.M.2    Gesson, K.3    Thomas, G.4
  • 42
    • 84905019401 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress associated responses in cancer
    • Wang WA, Groenendyk J, Michalak M. Endoplasmic reticulum stress associated responses in cancer. Biochim Biophys Acta (2014) 1843:2143-9. doi:10.1016/j.bbamcr.2014.01.012
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 2143-2149
    • Wang, W.A.1    Groenendyk, J.2    Michalak, M.3
  • 44
    • 4444302042 scopus 로고    scopus 로고
    • Effect on tumor cells of blocking survival response to glucose deprivation
    • Park HR, Tomida A, Sato S, Tsukumo Y, Yun J, Yamori T, et al. Effect on tumor cells of blocking survival response to glucose deprivation. J Natl Cancer Inst (2004) 96:1300-10. doi:10.1093/jnci/djh243
    • (2004) J Natl Cancer Inst , vol.96 , pp. 1300-1310
    • Park, H.R.1    Tomida, A.2    Sato, S.3    Tsukumo, Y.4    Yun, J.5    Yamori, T.6
  • 45
    • 0032053823 scopus 로고    scopus 로고
    • The unique physiology of solid tumors: opportunities (and problems) for cancer therapy
    • Brown JM, Giaccia AJ. The unique physiology of solid tumors: opportunities (and problems) for cancer therapy. Cancer Res (1998) 58:1408-16.
    • (1998) Cancer Res , vol.58 , pp. 1408-1416
    • Brown, J.M.1    Giaccia, A.J.2
  • 46
    • 85016352015 scopus 로고    scopus 로고
    • Endoplasmic reticulum calcium pumps and cancer cell differentiation
    • Papp B, Brouland JP, Arbabian A, Gelebart P, Kovacs T, Bobe R, et al. Endoplasmic reticulum calcium pumps and cancer cell differentiation. Biomolecules (2012) 2:165-86. doi:10.3390/biom2010165
    • (2012) Biomolecules , vol.2 , pp. 165-186
    • Papp, B.1    Brouland, J.P.2    Arbabian, A.3    Gelebart, P.4    Kovacs, T.5    Bobe, R.6
  • 47
    • 79960759956 scopus 로고    scopus 로고
    • Calcium in tumour metastasis: new roles for known actors
    • Prevarskaya N, Skryma R, Shuba Y. Calcium in tumour metastasis: new roles for known actors. Nat Rev Cancer (2011) 11:609-18. doi:10.1038/nrc3105
    • (2011) Nat Rev Cancer , vol.11 , pp. 609-618
    • Prevarskaya, N.1    Skryma, R.2    Shuba, Y.3
  • 48
    • 42549164808 scopus 로고    scopus 로고
    • Ca2+ signalling checkpoints in cancer: remodelling Ca2+ for cancer cell proliferation and survival
    • Roderick HL, Cook SJ. Ca2+ signalling checkpoints in cancer: remodelling Ca2+ for cancer cell proliferation and survival. Nat Rev Cancer (2008) 8:361-75. doi:10.1038/nrc2374
    • (2008) Nat Rev Cancer , vol.8 , pp. 361-375
    • Roderick, H.L.1    Cook, S.J.2
  • 49
    • 84872375449 scopus 로고    scopus 로고
    • Endoplasmic reticulum and the unfolded protein response: dynamics and metabolic integration
    • Bravo R, Parra V, Gatica D, Rodriguez AE, Torrealba N, Paredes F, et al. Endoplasmic reticulum and the unfolded protein response: dynamics and metabolic integration. Int Rev Cell Mol Biol (2013) 301:215-90. doi:10.1016/B978-0-12-407704-1.00005-1
    • (2013) Int Rev Cell Mol Biol , vol.301 , pp. 215-290
    • Bravo, R.1    Parra, V.2    Gatica, D.3    Rodriguez, A.E.4    Torrealba, N.5    Paredes, F.6
  • 50
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding HP, Novoa I, Zhang Y, Zeng H, Wek R, Schapira M, et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell (2000) 6:1099-108. doi:10.1016/S1097-2765(00)00108-8
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6
  • 51
    • 84884164633 scopus 로고    scopus 로고
    • Translational control by eIF2alpha kinases in long-lasting synaptic plasticity and long-term memory
    • Trinh MA, Klann E. Translational control by eIF2alpha kinases in long-lasting synaptic plasticity and long-term memory. Neurobiol Learn Mem (2013) 105:93-9. doi:10.1016/j.nlm.2013.04.013
    • (2013) Neurobiol Learn Mem , vol.105 , pp. 93-99
    • Trinh, M.A.1    Klann, E.2
  • 52
    • 35848935017 scopus 로고    scopus 로고
    • Translational control and the unfolded protein response
    • Wek RC, Cavener DR. Translational control and the unfolded protein response. Antioxid Redox Signal (2007) 9:2357-71. doi:10.1089/ars.2007.1764
    • (2007) Antioxid Redox Signal , vol.9 , pp. 2357-2371
    • Wek, R.C.1    Cavener, D.R.2
  • 53
    • 32544446451 scopus 로고    scopus 로고
    • Coping with stress: eIF2 kinases and translational control
    • Wek RC, Jiang HY, Anthony TG. Coping with stress: eIF2 kinases and translational control. Biochem Soc Trans (2006) 34:7-11. doi:10.1042/BST0340007
    • (2006) Biochem Soc Trans , vol.34 , pp. 7-11
    • Wek, R.C.1    Jiang, H.Y.2    Anthony, T.G.3
  • 54
    • 84885944468 scopus 로고    scopus 로고
    • The emerging role of the Nrf2-Keap1 signaling pathway in cancer
    • Jaramillo MC, Zhang DD. The emerging role of the Nrf2-Keap1 signaling pathway in cancer. Genes Dev (2013) 27:2179-91. doi:10.1101/gad.225680.113
    • (2013) Genes Dev , vol.27 , pp. 2179-2191
    • Jaramillo, M.C.1    Zhang, D.D.2
  • 55
    • 2442542312 scopus 로고    scopus 로고
    • PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress
    • Cullinan SB, Diehl JA. PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress. J Biol Chem (2004) 279:20108-17. doi:10.1074/jbc.M314219200
    • (2004) J Biol Chem , vol.279 , pp. 20108-20117
    • Cullinan, S.B.1    Diehl, J.A.2
  • 56
    • 0141752795 scopus 로고    scopus 로고
    • Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival
    • Cullinan SB, Zhang D, Hannink M, Arvisais E, Kaufman RJ, Diehl JA. Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival. Mol Cell Biol (2003) 23:7198-209. doi:10.1128/MCB.23.20.7198-7209.2003
    • (2003) Mol Cell Biol , vol.23 , pp. 7198-7209
    • Cullinan, S.B.1    Zhang, D.2    Hannink, M.3    Arvisais, E.4    Kaufman, R.J.5    Diehl, J.A.6
  • 57
    • 0842285401 scopus 로고    scopus 로고
    • Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2
    • Lu PD, Jousse C, Marciniak SJ, Zhang Y, Novoa I, Scheuner D, et al. Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2. EMBO J (2004) 23:169-79. doi:10.1038/sj.emboj.7600030
    • (2004) EMBO J , vol.23 , pp. 169-179
    • Lu, P.D.1    Jousse, C.2    Marciniak, S.J.3    Zhang, Y.4    Novoa, I.5    Scheuner, D.6
  • 58
    • 84877578475 scopus 로고    scopus 로고
    • ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death
    • Han J, Back SH, Hur J, Lin YH, Gildersleeve R, Shan J, et al. ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death. Nat Cell Biol (2013) 15:481-90. doi:10.1038/ncb2738
    • (2013) Nat Cell Biol , vol.15 , pp. 481-490
    • Han, J.1    Back, S.H.2    Hur, J.3    Lin, Y.H.4    Gildersleeve, R.5    Shan, J.6
  • 59
    • 55849096988 scopus 로고    scopus 로고
    • Chop deletion reduces oxidative stress, improves beta cell function, and promotes cell survival in multiple mouse models of diabetes
    • Song B, Scheuner D, Ron D, Pennathur S, Kaufman RJ. Chop deletion reduces oxidative stress, improves beta cell function, and promotes cell survival in multiple mouse models of diabetes. J Clin Invest (2008) 118:3378-89. doi:10.1172/JCI34587
    • (2008) J Clin Invest , vol.118 , pp. 3378-3389
    • Song, B.1    Scheuner, D.2    Ron, D.3    Pennathur, S.4    Kaufman, R.J.5
  • 60
    • 10644233167 scopus 로고    scopus 로고
    • CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum
    • Marciniak SJ, Yun CY, Oyadomari S, Novoa I, Zhang Y, Jungreis R, et al. CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. Genes Dev (2004) 18:3066-77. doi:10.1101/gad.1250704
    • (2004) Genes Dev , vol.18 , pp. 3066-3077
    • Marciniak, S.J.1    Yun, C.Y.2    Oyadomari, S.3    Novoa, I.4    Zhang, Y.5    Jungreis, R.6
  • 61
    • 84881117521 scopus 로고    scopus 로고
    • Human endoplasmic reticulum oxidoreductin 1-alpha is a novel predictor for poor prognosis of breast cancer
    • Kutomi G, Tamura Y, Tanaka T, Kajiwara T, Kukita K, Ohmura T, et al. Human endoplasmic reticulum oxidoreductin 1-alpha is a novel predictor for poor prognosis of breast cancer. Cancer Sci (2013) 104:1091-6. doi:10.1111/cas.12177
    • (2013) Cancer Sci , vol.104 , pp. 1091-1096
    • Kutomi, G.1    Tamura, Y.2    Tanaka, T.3    Kajiwara, T.4    Kukita, K.5    Ohmura, T.6
  • 62
    • 77954535031 scopus 로고    scopus 로고
    • PERK promotes cancer cell proliferation and tumor growth by limiting oxidative DNA damage
    • Bobrovnikova-Marjon E, Grigoriadou C, Pytel D, Zhang F, Ye J, Koumenis C, et al. PERK promotes cancer cell proliferation and tumor growth by limiting oxidative DNA damage. Oncogene (2010) 29:3881-95. doi:10.1038/onc.2010.153
    • (2010) Oncogene , vol.29 , pp. 3881-3895
    • Bobrovnikova-Marjon, E.1    Grigoriadou, C.2    Pytel, D.3    Zhang, F.4    Ye, J.5    Koumenis, C.6
  • 63
    • 84867562151 scopus 로고    scopus 로고
    • The unfolded protein response induces the angiogenic switch in human tumor cells through the PERK/ATF4 pathway
    • Wang Y, Alam GN, Ning Y, Visioli F, Dong Z, Nor JE, et al. The unfolded protein response induces the angiogenic switch in human tumor cells through the PERK/ATF4 pathway. Cancer Res (2012) 72:5396-406. doi:10.1158/0008-5472.CAN-12-0474
    • (2012) Cancer Res , vol.72 , pp. 5396-5406
    • Wang, Y.1    Alam, G.N.2    Ning, Y.3    Visioli, F.4    Dong, Z.5    Nor, J.E.6
  • 64
    • 77953565102 scopus 로고    scopus 로고
    • The GCN2-ATF4 pathway is critical for tumour cell survival and proliferation in response to nutrient deprivation
    • Ye J, Kumanova M, Hart LS, Sloane K, Zhang H, De Panis DN, et al. The GCN2-ATF4 pathway is critical for tumour cell survival and proliferation in response to nutrient deprivation. EMBO J (2010) 29:2082-96. doi:10.1038/emboj.2010.81
    • (2010) EMBO J , vol.29 , pp. 2082-2096
    • Ye, J.1    Kumanova, M.2    Hart, L.S.3    Sloane, K.4    Zhang, H.5    De Panis, D.N.6
  • 65
    • 84875235453 scopus 로고    scopus 로고
    • Characterization of a novel PERK kinase inhibitor with antitumor and antiangiogenic activity
    • Atkins C, Liu Q, Minthorn E, Zhang SY, Figueroa DJ, Moss K, et al. Characterization of a novel PERK kinase inhibitor with antitumor and antiangiogenic activity. Cancer Res (2013) 73:1993-2002. doi:10.1158/0008-5472.CAN-12-3109
    • (2013) Cancer Res , vol.73 , pp. 1993-2002
    • Atkins, C.1    Liu, Q.2    Minthorn, E.3    Zhang, S.Y.4    Figueroa, D.J.5    Moss, K.6
  • 66
    • 58349097747 scopus 로고    scopus 로고
    • Synergistic apoptosis induction in leukemic cells by the phosphatase inhibitor salubrinal and proteasome inhibitors
    • Drexler HC. Synergistic apoptosis induction in leukemic cells by the phosphatase inhibitor salubrinal and proteasome inhibitors. PLoS One (2009) 4:e4161. doi:10.1371/journal.pone.0004161
    • (2009) PLoS One , vol.4
    • Drexler, H.C.1
  • 67
    • 68549092781 scopus 로고    scopus 로고
    • Regulated Ire1-dependent decay of messenger RNAs in mammalian cells
    • Hollien J, Lin JH, Li H, Stevens N, Walter P, Weissman JS. Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. J Cell Biol (2009) 186:323-31. doi:10.1083/jcb.200903014
    • (2009) J Cell Biol , vol.186 , pp. 323-331
    • Hollien, J.1    Lin, J.H.2    Li, H.3    Stevens, N.4    Walter, P.5    Weissman, J.S.6
  • 68
    • 69749123786 scopus 로고    scopus 로고
    • Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactome
    • Hetz C, Glimcher LH. Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactome. Mol Cell (2009) 35:551-61. doi:10.1016/j.molcel.2009.08.021
    • (2009) Mol Cell , vol.35 , pp. 551-561
    • Hetz, C.1    Glimcher, L.H.2
  • 69
    • 0026446102 scopus 로고
    • Vascular endothelial growth factor is a potential tumour angiogenesis factor in human gliomas in vivo
    • Plate KH, Breier G, Weich HA, Risau W. Vascular endothelial growth factor is a potential tumour angiogenesis factor in human gliomas in vivo. Nature (1992) 359:845-8. doi:10.1038/359845a0
    • (1992) Nature , vol.359 , pp. 845-848
    • Plate, K.H.1    Breier, G.2    Weich, H.A.3    Risau, W.4
  • 70
    • 84897541350 scopus 로고    scopus 로고
    • XBP1 promotes triple-negative breast cancer by controlling the HIF1alpha pathway
    • Chen X, Iliopoulos D, Zhang Q, Tang Q, Greenblatt MB, Hatziapostolou M, et al. XBP1 promotes triple-negative breast cancer by controlling the HIF1alpha pathway. Nature (2014) 508:103-7. doi:10.1038/nature13119
    • (2014) Nature , vol.508 , pp. 103-107
    • Chen, X.1    Iliopoulos, D.2    Zhang, Q.3    Tang, Q.4    Greenblatt, M.B.5    Hatziapostolou, M.6
  • 71
    • 84872173393 scopus 로고    scopus 로고
    • Autocrine control of glioma cells adhesion and migration through IRE1alpha-mediated cleavage of SPARC mRNA
    • Dejeans N, Pluquet O, Lhomond S, Grise F, Bouchecareilh M, Juin A, et al. Autocrine control of glioma cells adhesion and migration through IRE1alpha-mediated cleavage of SPARC mRNA. J Cell Sci (2012) 125:4278-87. doi:10.1242/jcs.099291
    • (2012) J Cell Sci , vol.125 , pp. 4278-4287
    • Dejeans, N.1    Pluquet, O.2    Lhomond, S.3    Grise, F.4    Bouchecareilh, M.5    Juin, A.6
  • 72
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H, Matsuzawa A, Tobiume K, Saegusa K, Takeda K, Inoue K, et al. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev (2002) 16:1345-55. doi:10.1101/gad.992302
    • (2002) Genes Dev , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6
  • 73
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano F, Wang X, Bertolotti A, Zhang Y, Chung P, Harding HP, et al. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science (2000) 287:664-6. doi:10.1126/science.287.5453.664
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6
  • 74
    • 84856393784 scopus 로고    scopus 로고
    • The transcription factor c-Jun protects against sustained hepatic endoplasmic reticulum stress thereby promoting hepatocyte survival
    • Fuest M, Willim K, Macnelly S, Fellner N, Resch GP, Blum HE, et al. The transcription factor c-Jun protects against sustained hepatic endoplasmic reticulum stress thereby promoting hepatocyte survival. Hepatology (2012) 55:408-18. doi:10.1002/hep.24699
    • (2012) Hepatology , vol.55 , pp. 408-418
    • Fuest, M.1    Willim, K.2    Macnelly, S.3    Fellner, N.4    Resch, G.P.5    Blum, H.E.6
  • 75
    • 54549089088 scopus 로고    scopus 로고
    • c-Jun inhibits thapsigargin-induced ER stress through up-regulation of DSCR1/Adapt78
    • Zhao P, Xiao X, Kim AS, Leite MF, Xu J, Zhu X, et al. c-Jun inhibits thapsigargin-induced ER stress through up-regulation of DSCR1/Adapt78. Exp Biol Med (Maywood) (2008) 233:1289-300. doi:10.3181/0803-RM-84
    • (2008) Exp Biol Med (Maywood) , vol.233 , pp. 1289-1300
    • Zhao, P.1    Xiao, X.2    Kim, A.S.3    Leite, M.F.4    Xu, J.5    Zhu, X.6
  • 76
    • 70449529426 scopus 로고    scopus 로고
    • Paraquat activates the IRE1/ASK1/JNK cascade associated with apoptosis in human neuroblastoma SH-SY5Y cells
    • Yang W, Tiffany-Castiglioni E, Koh HC, Son IH. Paraquat activates the IRE1/ASK1/JNK cascade associated with apoptosis in human neuroblastoma SH-SY5Y cells. Toxicol Lett (2009) 191:203-10. doi:10.1016/j.toxlet.2009.08.024
    • (2009) Toxicol Lett , vol.191 , pp. 203-210
    • Yang, W.1    Tiffany-Castiglioni, E.2    Koh, H.C.3    Son, I.H.4
  • 77
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • 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) 171:513-24. doi:10.2353/ajpath.2007.070188
    • (2007) Am J Pathol , vol.171 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6
  • 78
    • 84870357261 scopus 로고    scopus 로고
    • Divergent allosteric control of the IRE1alpha endoribonuclease using kinase inhibitors
    • Wang L, Perera BG, Hari SB, Bhhatarai B, Backes BJ, Seeliger MA, et al. Divergent allosteric control of the IRE1alpha endoribonuclease using kinase inhibitors. Nat Chem Biol (2012) 8:982-9. doi:10.1038/nchembio.1094
    • (2012) Nat Chem Biol , vol.8 , pp. 982-989
    • Wang, L.1    Perera, B.G.2    Hari, S.B.3    Bhhatarai, B.4    Backes, B.J.5    Seeliger, M.A.6
  • 79
    • 47949100421 scopus 로고    scopus 로고
    • KDEL-retained antigen in B lymphocytes induces a proinflammatory response: a possible role for endoplasmic reticulum stress in adaptive T cell immunity
    • Wheeler MC, Rizzi M, Sasik R, Almanza G, Hardiman G, Zanetti M. KDEL-retained antigen in B lymphocytes induces a proinflammatory response: a possible role for endoplasmic reticulum stress in adaptive T cell immunity. J Immunol (2008) 181:256-64. doi:10.4049/jimmunol.181.1.256
    • (2008) J Immunol , vol.181 , pp. 256-264
    • Wheeler, M.C.1    Rizzi, M.2    Sasik, R.3    Almanza, G.4    Hardiman, G.5    Zanetti, M.6
  • 80
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis RJ. Signal transduction by the JNK group of MAP kinases. Cell (2000) 103:239-52. doi:10.1016/S0092-8674(00)00116-1
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 81
    • 77957308805 scopus 로고    scopus 로고
    • Prostate cancer cells undergoing ER stress in vitro and in vivo activate transcription of pro-inflammatory cytokines
    • Mahadevan NR, Fernandez A, Rodvold JJ, Almanza G, Zanetti M. Prostate cancer cells undergoing ER stress in vitro and in vivo activate transcription of pro-inflammatory cytokines. J Inflamm Res (2010) 3:99-103. doi:10.2147/JIR.S11190
    • (2010) J Inflamm Res , vol.3 , pp. 99-103
    • Mahadevan, N.R.1    Fernandez, A.2    Rodvold, J.J.3    Almanza, G.4    Zanetti, M.5
  • 82
    • 77951290227 scopus 로고    scopus 로고
    • TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages
    • Martinon F, Chen X, Lee AH, Glimcher LH. TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages. Nat Immunol (2010) 11:411-8. doi:10.1038/ni.1857
    • (2010) Nat Immunol , vol.11 , pp. 411-418
    • Martinon, F.1    Chen, X.2    Lee, A.H.3    Glimcher, L.H.4
  • 83
    • 79955632933 scopus 로고    scopus 로고
    • Transmission of endoplasmic reticulum stress and pro-inflammation from tumor cells to myeloid cells
    • Mahadevan NR, Rodvold J, Sepulveda H, Rossi S, Drew AF, Zanetti M. Transmission of endoplasmic reticulum stress and pro-inflammation from tumor cells to myeloid cells. Proc Natl Acad Sci U S A (2011) 108:6561-6. doi:10.1073/pnas.1008942108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 6561-6566
    • Mahadevan, N.R.1    Rodvold, J.2    Sepulveda, H.3    Rossi, S.4    Drew, A.F.5    Zanetti, M.6
  • 85
    • 79952533264 scopus 로고    scopus 로고
    • Restoration of the immunogenicity of cisplatin-induced cancer cell death by endoplasmic reticulum stress
    • Martins I, Kepp O, Schlemmer F, Adjemian S, Tailler M, Shen S, et al. Restoration of the immunogenicity of cisplatin-induced cancer cell death by endoplasmic reticulum stress. Oncogene (2011) 30:1147-58. doi:10.1038/onc.2010.500
    • (2011) Oncogene , vol.30 , pp. 1147-1158
    • Martins, I.1    Kepp, O.2    Schlemmer, F.3    Adjemian, S.4    Tailler, M.5    Shen, S.6
  • 86
    • 33846680250 scopus 로고    scopus 로고
    • Association of elevated GRP78 expression with increased lymph node metastasis and poor prognosis in patients with gastric cancer
    • Zhang J, Jiang Y, Jia Z, Li Q, Gong W, Wang L, et al. Association of elevated GRP78 expression with increased lymph node metastasis and poor prognosis in patients with gastric cancer. Clin Exp Metastasis (2006) 23:401-10. doi:10.1007/s10585-006-9051-9
    • (2006) Clin Exp Metastasis , vol.23 , pp. 401-410
    • Zhang, J.1    Jiang, Y.2    Jia, Z.3    Li, Q.4    Gong, W.5    Wang, L.6
  • 87
    • 33751193479 scopus 로고    scopus 로고
    • Glucose regulated proteins in cancer progression, drug resistance and immunotherapy
    • Fu Y, Lee AS. Glucose regulated proteins in cancer progression, drug resistance and immunotherapy. Cancer Biol Ther (2006) 5:741-4. doi:10.4161/cbt.5.7.2970
    • (2006) Cancer Biol Ther , vol.5 , pp. 741-744
    • Fu, Y.1    Lee, A.S.2
  • 88
    • 0029817451 scopus 로고    scopus 로고
    • Inhibition of tumor progression by suppression of stress protein GRP78/BiP induction in fibrosarcoma B/C10ME
    • Jamora C, Dennert G, Lee AS. Inhibition of tumor progression by suppression of stress protein GRP78/BiP induction in fibrosarcoma B/C10ME. Proc Natl Acad Sci U S A (1996) 93:7690-4. doi:10.1073/pnas.93.15.7690
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 7690-7694
    • Jamora, C.1    Dennert, G.2    Lee, A.S.3
  • 89
    • 77149136381 scopus 로고    scopus 로고
    • Calcium binding chaperones of the endoplasmic reticulum
    • Coe H, Michalak M. Calcium binding chaperones of the endoplasmic reticulum. Gen Physiol Biophys (2009) 28:F96-103.
    • (2009) Gen Physiol Biophys , vol.28 , pp. F96-F103
    • Coe, H.1    Michalak, M.2
  • 90
    • 77957133402 scopus 로고    scopus 로고
    • An intelligent sarco-endoplasmic reticulum Ca2+ store: release and leak channels have differential access to a concealed Ca2+ pool
    • Guerrero-Hernandez A, Dagnino-Acosta A, Verkhratsky A. An intelligent sarco-endoplasmic reticulum Ca2+ store: release and leak channels have differential access to a concealed Ca2+ pool. Cell Calcium (2010) 48:143-9. doi:10.1016/j.ceca.2010.08.001
    • (2010) Cell Calcium , vol.48 , pp. 143-149
    • Guerrero-Hernandez, A.1    Dagnino-Acosta, A.2    Verkhratsky, A.3
  • 91
    • 79952592038 scopus 로고    scopus 로고
    • IP(3) receptors: toward understanding their activation
    • Taylor CW, Tovey SC. IP(3) receptors: toward understanding their activation. Cold Spring Harb Perspect Biol (2010) 2:a004010. doi:10.1101/cshperspect.a004010
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Taylor, C.W.1    Tovey, S.C.2
  • 92
    • 34548644786 scopus 로고    scopus 로고
    • Modulation of the ryanodine receptor and intracellular calcium
    • Zalk R, Lehnart SE, Marks AR. Modulation of the ryanodine receptor and intracellular calcium. Annu Rev Biochem (2007) 76:367-85. doi:10.1146/annurev.biochem.76.053105.094237
    • (2007) Annu Rev Biochem , vol.76 , pp. 367-385
    • Zalk, R.1    Lehnart, S.E.2    Marks, A.R.3
  • 93
    • 0034973680 scopus 로고    scopus 로고
    • Ryanodine receptors/calcium release channels in heart failure and sudden cardiac death
    • Marks AR. Ryanodine receptors/calcium release channels in heart failure and sudden cardiac death. J Mol Cell Cardiol (2001) 33:615-24. doi:10.1006/jmcc.2000.1343
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 615-624
    • Marks, A.R.1
  • 94
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham DE. Calcium signaling. Cell (2007) 131:1047-58. doi:10.1016/j.cell.2007.11.028
    • (2007) Cell , vol.131 , pp. 1047-1058
    • Clapham, D.E.1
  • 96
    • 70349653079 scopus 로고    scopus 로고
    • Calcium pumps in health and disease
    • Brini M, Carafoli E. Calcium pumps in health and disease. Physiol Rev (2009) 89:1341-78. doi:10.1152/physrev.00032.2008
    • (2009) Physiol Rev , vol.89 , pp. 1341-1378
    • Brini, M.1    Carafoli, E.2
  • 97
    • 34047219171 scopus 로고    scopus 로고
    • SERCA pump isoforms: their role in calcium transport and disease
    • Periasamy M, Kalyanasundaram A. SERCA pump isoforms: their role in calcium transport and disease. Muscle Nerve (2007) 35:430-42. doi:10.1002/mus.20745
    • (2007) Muscle Nerve , vol.35 , pp. 430-442
    • Periasamy, M.1    Kalyanasundaram, A.2
  • 98
    • 34247610380 scopus 로고    scopus 로고
    • Sarcolipin and phospholamban as regulators of cardiac sarcoplasmic reticulum Ca2+ ATPase
    • Bhupathy P, Babu GJ, Periasamy M. Sarcolipin and phospholamban as regulators of cardiac sarcoplasmic reticulum Ca2+ ATPase. J Mol Cell Cardiol (2007) 42:903-11. doi:10.1016/j.yjmcc.2007.03.738
    • (2007) J Mol Cell Cardiol , vol.42 , pp. 903-911
    • Bhupathy, P.1    Babu, G.J.2    Periasamy, M.3
  • 99
    • 80053349683 scopus 로고    scopus 로고
    • SUMO1-dependent modulation of SERCA2a in heart failure
    • Kho C, Lee A, Jeong D, Oh JG, Chaanine AH, Kizana E, et al. SUMO1-dependent modulation of SERCA2a in heart failure. Nature (2011) 477:601-5. doi:10.1038/nature10407
    • (2011) Nature , vol.477 , pp. 601-605
    • Kho, C.1    Lee, A.2    Jeong, D.3    Oh, J.G.4    Chaanine, A.H.5    Kizana, E.6
  • 100
    • 25444450030 scopus 로고    scopus 로고
    • 3-Nitrotyrosine modification of SERCA2a in the aging heart: a distinct signature of the cellular redox environment
    • 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. doi:10.1021/bi051226n
    • (2005) Biochemistry , vol.44 , pp. 13071-13081
    • Knyushko, T.V.1    Sharov, V.S.2    Williams, T.D.3    Schoneich, C.4    Bigelow, D.J.5
  • 101
    • 9144266981 scopus 로고    scopus 로고
    • S-glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide
    • Adachi T, Weisbrod RM, Pimentel DR, Ying J, Sharov VS, Schoneich C, et al. S-glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide. Nat Med (2004) 10:1200-7. doi:10.1038/nm1119
    • (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
  • 102
    • 33750986164 scopus 로고    scopus 로고
    • Alterations in the ATP2A2 gene in correlation with colon and lung cancer
    • Korosec B, Glavac D, Rott T, Ravnik-Glavac M. Alterations in the ATP2A2 gene in correlation with colon and lung cancer. Cancer Genet Cytogenet (2006) 171:105-11. doi:10.1016/j.cancergencyto.2006.06.016
    • (2006) Cancer Genet Cytogenet , vol.171 , pp. 105-111
    • Korosec, B.1    Glavac, D.2    Rott, T.3    Ravnik-Glavac, M.4
  • 103
    • 2342528997 scopus 로고    scopus 로고
    • Sarcoendoplasmic reticulum Ca(2+) ATPase type 2 downregulated in human oral squamous cell carcinoma
    • Endo Y, Uzawa K, Mochida Y, Shiiba M, Bukawa H, Yokoe H, et al. Sarcoendoplasmic reticulum Ca(2+) ATPase type 2 downregulated in human oral squamous cell carcinoma. Int J Cancer (2004) 110:225-31. doi:10.1002/ijc.20118
    • (2004) Int J Cancer , vol.110 , pp. 225-231
    • Endo, Y.1    Uzawa, K.2    Mochida, Y.3    Shiiba, M.4    Bukawa, H.5    Yokoe, H.6
  • 104
    • 0037668944 scopus 로고    scopus 로고
    • The expression of the sarco/endoplasmic reticulum Ca2+-ATPases in thyroid and its down-regulation following neoplastic transformation
    • Pacifico F, Ulianich L, De Micheli S, Treglia S, Leonardi A, Vito P, et al. The expression of the sarco/endoplasmic reticulum Ca2+-ATPases in thyroid and its down-regulation following neoplastic transformation. J Mol Endocrinol (2003) 30:399-409. doi:10.1677/jme.0.0300399
    • (2003) J Mol Endocrinol , vol.30 , pp. 399-409
    • Pacifico, F.1    Ulianich, L.2    De Micheli, S.3    Treglia, S.4    Leonardi, A.5    Vito, P.6
  • 106
    • 21244467994 scopus 로고    scopus 로고
    • The loss of sarco/endoplasmic reticulum calcium transport ATPase 3 expression is an early event during the multistep process of colon carcinogenesis
    • Brouland JP, Gelebart P, Kovacs T, Enouf J, Grossmann J, Papp B. The loss of sarco/endoplasmic reticulum calcium transport ATPase 3 expression is an early event during the multistep process of colon carcinogenesis. Am J Pathol (2005) 167:233-42. doi:10.1016/S0002-9440(10)62968-9
    • (2005) Am J Pathol , vol.167 , pp. 233-242
    • Brouland, J.P.1    Gelebart, P.2    Kovacs, T.3    Enouf, J.4    Grossmann, J.5    Papp, B.6
  • 107
    • 0033669884 scopus 로고    scopus 로고
    • Intracellular Ca(2+) release channels in evolution
    • Sorrentino V, Barone V, Rossi D. Intracellular Ca(2+) release channels in evolution. Curr Opin Genet Dev (2000) 10:662-7. doi:10.1016/S0959-437X(00)00139-8
    • (2000) Curr Opin Genet Dev , vol.10 , pp. 662-667
    • Sorrentino, V.1    Barone, V.2    Rossi, D.3
  • 108
    • 0033378368 scopus 로고    scopus 로고
    • Expression of inositol trisphosphate receptors
    • Taylor CW, Genazzani AA, Morris SA. Expression of inositol trisphosphate receptors. Cell Calcium (1999) 26:237-51. doi:10.1054/ceca.1999.0090
    • (1999) Cell Calcium , vol.26 , pp. 237-251
    • Taylor, C.W.1    Genazzani, A.A.2    Morris, S.A.3
  • 109
    • 0037343205 scopus 로고    scopus 로고
    • Signalling specificity in GPCR-dependent Ca2+ signalling
    • Kiselyov K, Shin DM, Muallem S. Signalling specificity in GPCR-dependent Ca2+ signalling. Cell Signal (2003) 15:243-53. doi:10.1016/S0898-6568(02)00074-8
    • (2003) Cell Signal , vol.15 , pp. 243-253
    • Kiselyov, K.1    Shin, D.M.2    Muallem, S.3
  • 110
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • Rhee SG. Regulation of phosphoinositide-specific phospholipase C. Annu Rev Biochem (2001) 70:281-312. doi:10.1146/annurev.biochem.70.1.281
    • (2001) Annu Rev Biochem , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 111
    • 84861762640 scopus 로고    scopus 로고
    • Inositol trisphosphate receptors in smooth muscle cells
    • Narayanan D, Adebiyi A, Jaggar JH. Inositol trisphosphate receptors in smooth muscle cells. Am J Physiol Heart Circ Physiol (2012) 302:H2190-210. doi:10.1152/ajpheart.01146.2011
    • (2012) Am J Physiol Heart Circ Physiol , vol.302 , pp. H2190-H2210
    • Narayanan, D.1    Adebiyi, A.2    Jaggar, J.H.3
  • 112
    • 3943105516 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptors as signal integrators
    • Patterson RL, Boehning D, Snyder SH. Inositol 1,4,5-trisphosphate receptors as signal integrators. Annu Rev Biochem (2004) 73:437-65. doi:10.1146/annurev.biochem.73.071403.161303
    • (2004) Annu Rev Biochem , vol.73 , pp. 437-465
    • Patterson, R.L.1    Boehning, D.2    Snyder, S.H.3
  • 113
    • 40649096621 scopus 로고    scopus 로고
    • Phosphorylation of inositol 1,4,5-trisphosphate receptors by protein kinase B/Akt inhibits Ca2+ release and apoptosis
    • Szado T, Vanderheyden V, Parys JB, De Smedt H, Rietdorf K, Kotelevets L, et al. Phosphorylation of inositol 1,4,5-trisphosphate receptors by protein kinase B/Akt inhibits Ca2+ release and apoptosis. Proc Natl Acad Sci U S A (2008) 105:2427-32. doi:10.1073/pnas.0711324105
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 2427-2432
    • Szado, T.1    Vanderheyden, V.2    Parys, J.B.3    De Smedt, H.4    Rietdorf, K.5    Kotelevets, L.6
  • 114
    • 33645642577 scopus 로고    scopus 로고
    • Akt kinase phosphorylation of inositol 1,4,5-trisphosphate receptors
    • Khan MT, Wagner L II, Yule DI, Bhanumathy C, Joseph SK. Akt kinase phosphorylation of inositol 1,4,5-trisphosphate receptors. J Biol Chem (2006) 281:3731-7. doi:10.1074/jbc.M509262200
    • (2006) J Biol Chem , vol.281 , pp. 3731-3737
    • Khan, M.T.1    Wagner, L.2    Yule, D.I.3    Bhanumathy, C.4    Joseph, S.K.5
  • 115
    • 11844284861 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum
    • Oakes SA, Scorrano L, Opferman JT, Bassik MC, Nishino M, Pozzan T, et al. 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 (2005) 102:105-10. doi:10.1073/pnas.0408352102
    • (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
  • 116
    • 84893142524 scopus 로고    scopus 로고
    • Calcium influx pathways in breast cancer: opportunities for pharmacological intervention
    • Azimi I, Roberts-Thomson SJ, Monteith GR. Calcium influx pathways in breast cancer: opportunities for pharmacological intervention. Br J Pharmacol (2014) 171:945-60. doi:10.1111/bph.12486
    • (2014) Br J Pharmacol , vol.171 , pp. 945-960
    • Azimi, I.1    Roberts-Thomson, S.J.2    Monteith, G.R.3
  • 117
    • 84886785578 scopus 로고    scopus 로고
    • Molecular interaction and functional coupling between type 3 inositol 1,4,5-trisphosphate receptor and BKCa channel stimulate breast cancer cell proliferation
    • Mound A, Rodat-Despoix L, Bougarn S, Ouadid-Ahidouch H, Matifat F. Molecular interaction and functional coupling between type 3 inositol 1,4,5-trisphosphate receptor and BKCa channel stimulate breast cancer cell proliferation. Eur J Cancer (2013) 49:3738-51. doi:10.1016/j.ejca.2013.07.013
    • (2013) Eur J Cancer , vol.49 , pp. 3738-3751
    • Mound, A.1    Rodat-Despoix, L.2    Bougarn, S.3    Ouadid-Ahidouch, H.4    Matifat, F.5
  • 118
    • 77953669483 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate-induced Ca2+ signalling is involved in estradiol-induced breast cancer epithelial cell growth
    • Szatkowski C, Parys JB, Ouadid-Ahidouch H, Matifat F. Inositol 1,4,5-trisphosphate-induced Ca2+ signalling is involved in estradiol-induced breast cancer epithelial cell growth. Mol Cancer (2010) 9:156. doi:10.1186/1476-4598-9-156
    • (2010) Mol Cancer , vol.9 , pp. 156
    • Szatkowski, C.1    Parys, J.B.2    Ouadid-Ahidouch, H.3    Matifat, F.4
  • 120
    • 84880910816 scopus 로고    scopus 로고
    • Assessment of gene expression of intracellular calcium channels, pumps and exchangers with epidermal growth factor-induced epithelial-mesenchymal transition in a breast cancer cell line
    • Davis FM, Parsonage MT, Cabot PJ, Parat MO, Thompson EW, Roberts-Thomson SJ, et al. Assessment of gene expression of intracellular calcium channels, pumps and exchangers with epidermal growth factor-induced epithelial-mesenchymal transition in a breast cancer cell line. Cancer Cell Int (2013) 13:76. doi:10.1186/1475-2867-13-76
    • (2013) Cancer Cell Int , vol.13 , pp. 76
    • Davis, F.M.1    Parsonage, M.T.2    Cabot, P.J.3    Parat, M.O.4    Thompson, E.W.5    Roberts-Thomson, S.J.6
  • 121
    • 10744233873 scopus 로고    scopus 로고
    • Possible involvement of inositol 1,4,5-trisphosphate receptor type 3 (IP3R3) in the peritoneal dissemination of gastric cancers
    • Sakakura C, Hagiwara A, Fukuda K, Shimomura K, Takagi T, Kin S, et al. Possible involvement of inositol 1,4,5-trisphosphate receptor type 3 (IP3R3) in the peritoneal dissemination of gastric cancers. Anticancer Res (2003) 23:3691-7.
    • (2003) Anticancer Res , vol.23 , pp. 3691-3697
    • Sakakura, C.1    Hagiwara, A.2    Fukuda, K.3    Shimomura, K.4    Takagi, T.5    Kin, S.6
  • 122
    • 84897375103 scopus 로고    scopus 로고
    • Oncogenic K-Ras suppresses IP(3)-dependent Ca(2)(+) release through remodelling of the isoform composition of IP(3)Rs and ER luminal Ca(2)(+) levels in colorectal cancer cell lines
    • Pierro C, Cook SJ, Foets TC, Bootman MD, Roderick HL. Oncogenic K-Ras suppresses IP(3)-dependent Ca(2)(+) release through remodelling of the isoform composition of IP(3)Rs and ER luminal Ca(2)(+) levels in colorectal cancer cell lines. J Cell Sci (2014) 127:1607-19. doi:10.1242/jcs.141408
    • (2014) J Cell Sci , vol.127 , pp. 1607-1619
    • Pierro, C.1    Cook, S.J.2    Foets, T.C.3    Bootman, M.D.4    Roderick, H.L.5
  • 123
    • 62149108507 scopus 로고    scopus 로고
    • Endoplasmic reticulum Ca2+-homeostasis is altered in small and non-small cell lung cancer cell lines
    • Bergner A, Kellner J, Tufman A, Huber RM. Endoplasmic reticulum Ca2+-homeostasis is altered in small and non-small cell lung cancer cell lines. J Exp Clin Cancer Res (2009) 28:25. doi:10.1186/1756-9966-28-25
    • (2009) J Exp Clin Cancer Res , vol.28 , pp. 25
    • Bergner, A.1    Kellner, J.2    Tufman, A.3    Huber, R.M.4
  • 124
    • 34249930943 scopus 로고    scopus 로고
    • The inositol 1,4,5-trisphosphate receptor (IP3R) and its regulators: sometimes good and sometimes bad teamwork
    • Choe CU, Ehrlich BE. The inositol 1,4,5-trisphosphate receptor (IP3R) and its regulators: sometimes good and sometimes bad teamwork. Sci STKE (2006) 2006:re15. doi:10.1126/stke.3632006re15
    • (2006) Sci STKE , vol.2006
    • Choe, C.U.1    Ehrlich, B.E.2
  • 125
    • 77954380413 scopus 로고    scopus 로고
    • Exchange protein directly activated by cyclic AMP increases melanoma cell migration by a Ca2+-dependent mechanism
    • Baljinnyam E, De Lorenzo MS, Xie LH, Iwatsubo M, Chen S, Goydos JS, et al. Exchange protein directly activated by cyclic AMP increases melanoma cell migration by a Ca2+-dependent mechanism. Cancer Res (2010) 70:5607-17. doi:10.1158/0008-5472.CAN-10-0056
    • (2010) Cancer Res , vol.70 , pp. 5607-5617
    • Baljinnyam, E.1    De Lorenzo, M.S.2    Xie, L.H.3    Iwatsubo, M.4    Chen, S.5    Goydos, J.S.6
  • 127
    • 0033517826 scopus 로고    scopus 로고
    • Expression of the calcium-sensing receptor in pancreatic islet B-cells
    • Rasschaert J, Malaisse WJ. Expression of the calcium-sensing receptor in pancreatic islet B-cells. Biochem Biophys Res Commun (1999) 264:615-8. doi:10.1006/bbrc.1999.1577
    • (1999) Biochem Biophys Res Commun , vol.264 , pp. 615-618
    • Rasschaert, J.1    Malaisse, W.J.2
  • 128
    • 67949115773 scopus 로고    scopus 로고
    • Peripheral ER structure and function
    • English AR, Zurek N, Voeltz GK. Peripheral ER structure and function. Curr Opin Cell Biol (2009) 21:596-602. doi:10.1016/j.ceb.2009.04.004
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 596-602
    • English, A.R.1    Zurek, N.2    Voeltz, G.K.3
  • 129
    • 70450204007 scopus 로고    scopus 로고
    • An emerging role of mTOR in lipid biosynthesis
    • Laplante M, Sabatini DM. An emerging role of mTOR in lipid biosynthesis. Curr Biol (2009) 19:R1046-52. doi:10.1016/j.cub.2009.09.058
    • (2009) Curr Biol , vol.19 , pp. R1046-R1052
    • Laplante, M.1    Sabatini, D.M.2
  • 130
    • 66349117317 scopus 로고    scopus 로고
    • Membrane phospholipid synthesis and endoplasmic reticulum function
    • Fagone P, Jackowski S. Membrane phospholipid synthesis and endoplasmic reticulum function. J Lipid Res (2009) 50(Suppl):S311-6. doi:10.1194/jlr.R800049-JLR200
    • (2009) J Lipid Res , vol.50 , Issue.SUPPL , pp. S311-S316
    • Fagone, P.1    Jackowski, S.2
  • 131
    • 0029077405 scopus 로고
    • The regulation of stearoyl-CoA desaturase (SCD)
    • Ntambi JM. The regulation of stearoyl-CoA desaturase (SCD). Prog Lipid Res (1995) 34:139-50. doi:10.1016/0163-7827(94)00010-J
    • (1995) Prog Lipid Res , vol.34 , pp. 139-150
    • Ntambi, J.M.1
  • 132
  • 134
    • 70350418625 scopus 로고    scopus 로고
    • mTOR signaling at a glance
    • Laplante M, Sabatini DM. mTOR signaling at a glance. J Cell Sci (2009) 122:3589-94. doi:10.1242/jcs.051011
    • (2009) J Cell Sci , vol.122 , pp. 3589-3594
    • Laplante, M.1    Sabatini, D.M.2
  • 135
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S, Loewith R, Hall MN. TOR signaling in growth and metabolism. Cell (2006) 124:471-84. doi:10.1016/j.cell.2006.01.016
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 136
    • 79955779584 scopus 로고    scopus 로고
    • mTOR links oncogenic signaling to tumor cell metabolism
    • Yecies JL, Manning BD. mTOR links oncogenic signaling to tumor cell metabolism. J Mol Med (Berl) (2011) 89:221-8. doi:10.1007/s00109-011-0726-6
    • (2011) J Mol Med (Berl) , vol.89 , pp. 221-228
    • Yecies, J.L.1    Manning, B.D.2
  • 137
    • 79952104568 scopus 로고    scopus 로고
    • mTOR couples cellular nutrient sensing to organismal metabolic homeostasis
    • Howell JJ, Manning BD. mTOR couples cellular nutrient sensing to organismal metabolic homeostasis. Trends Endocrinol Metab (2011) 22:94-102. doi:10.1016/j.tem.2010.12.003
    • (2011) Trends Endocrinol Metab , vol.22 , pp. 94-102
    • Howell, J.J.1    Manning, B.D.2
  • 138
    • 0034912744 scopus 로고    scopus 로고
    • PTEN and myotubularin: novel phosphoinositide phosphatases
    • Maehama T, Taylor GS, Dixon JE. PTEN and myotubularin: novel phosphoinositide phosphatases. Annu Rev Biochem (2001) 70:247-79. doi:10.1146/annurev.biochem.70.1.247
    • (2001) Annu Rev Biochem , vol.70 , pp. 247-279
    • Maehama, T.1    Taylor, G.S.2    Dixon, J.E.3
  • 139
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama T, Dixon JE. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem (1998) 273:13375-8. doi:10.1074/jbc.273.22.13375
    • (1998) J Biol Chem , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 140
    • 79960050610 scopus 로고    scopus 로고
    • PTEN tumor suppressor network in PI3K-Akt pathway control
    • Georgescu MM. PTEN tumor suppressor network in PI3K-Akt pathway control. Genes Cancer (2010) 1:1170-7. doi:10.1177/1947601911407325
    • (2010) Genes Cancer , vol.1 , pp. 1170-1177
    • Georgescu, M.M.1
  • 142
    • 84874650275 scopus 로고    scopus 로고
    • Development of PI3K inhibitors: lessons learned from early clinical trials
    • Rodon J, Dienstmann R, Serra V, Tabernero J. Development of PI3K inhibitors: lessons learned from early clinical trials. Nat Rev Clin Oncol (2013) 10:143-53. doi:10.1038/nrclinonc.2013.10
    • (2013) Nat Rev Clin Oncol , vol.10 , pp. 143-153
    • Rodon, J.1    Dienstmann, R.2    Serra, V.3    Tabernero, J.4
  • 143
    • 84885910468 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate and cancer: lessons from thyroid cancer cells
    • Tornquist K. Sphingosine 1-phosphate and cancer: lessons from thyroid cancer cells. Biomolecules (2013) 3:303-15. doi:10.3390/biom3020303
    • (2013) Biomolecules , vol.3 , pp. 303-315
    • Tornquist, K.1
  • 145
    • 33644977905 scopus 로고    scopus 로고
    • Sphingolipid targets in cancer therapy
    • Modrak DE, Gold DV, Goldenberg DM. Sphingolipid targets in cancer therapy. Mol Cancer Ther (2006) 5:200-8. doi:10.1158/1535-7163.MCT-05-0420
    • (2006) Mol Cancer Ther , vol.5 , pp. 200-208
    • Modrak, D.E.1    Gold, D.V.2    Goldenberg, D.M.3
  • 146
    • 44949233776 scopus 로고    scopus 로고
    • Sphingosine kinases and sphingosine-1-phosphate are critical for transforming growth factor beta-induced extracellular signal-regulated kinase 1 and 2 activation and promotion of migration and invasion of esophageal cancer cells
    • Miller AV, Alvarez SE, Spiegel S, Lebman DA. Sphingosine kinases and sphingosine-1-phosphate are critical for transforming growth factor beta-induced extracellular signal-regulated kinase 1 and 2 activation and promotion of migration and invasion of esophageal cancer cells. Mol Cell Biol (2008) 28:4142-51. doi:10.1128/MCB.01465-07
    • (2008) Mol Cell Biol , vol.28 , pp. 4142-4151
    • Miller, A.V.1    Alvarez, S.E.2    Spiegel, S.3    Lebman, D.A.4
  • 147
    • 33845982224 scopus 로고    scopus 로고
    • Insulin-like growth factors mediate heterotrimeric G protein-dependent ERK1/2 activation by transactivating sphingosine 1-phosphate receptors
    • El-Shewy HM, Johnson KR, Lee MH, Jaffa AA, Obeid LM, Luttrell LM. Insulin-like growth factors mediate heterotrimeric G protein-dependent ERK1/2 activation by transactivating sphingosine 1-phosphate receptors. J Biol Chem (2006) 281:31399-407. doi:10.1074/jbc.M605339200
    • (2006) J Biol Chem , vol.281 , pp. 31399-31407
    • El-Shewy, H.M.1    Johnson, K.R.2    Lee, M.H.3    Jaffa, A.A.4    Obeid, L.M.5    Luttrell, L.M.6
  • 148
    • 0037458681 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate and platelet-derived growth factor (PDGF) act via PDGF beta receptor-sphingosine 1-phosphate receptor complexes in airway smooth muscle cells
    • Waters C, Sambi B, Kong KC, Thompson D, Pitson SM, Pyne S, et al. Sphingosine 1-phosphate and platelet-derived growth factor (PDGF) act via PDGF beta receptor-sphingosine 1-phosphate receptor complexes in airway smooth muscle cells. J Biol Chem (2003) 278:6282-90. doi:10.1074/jbc.M208560200
    • (2003) J Biol Chem , vol.278 , pp. 6282-6290
    • Waters, C.1    Sambi, B.2    Kong, K.C.3    Thompson, D.4    Pitson, S.M.5    Pyne, S.6
  • 149
    • 57649188727 scopus 로고    scopus 로고
    • Metabolism of sphingolipids in the gut and its relation to inflammation and cancer development
    • Duan RD, Nilsson A. Metabolism of sphingolipids in the gut and its relation to inflammation and cancer development. Prog Lipid Res (2009) 48:62-72. doi:10.1016/j.plipres.2008.04.003
    • (2009) Prog Lipid Res , vol.48 , pp. 62-72
    • Duan, R.D.1    Nilsson, A.2
  • 150
    • 52949143502 scopus 로고    scopus 로고
    • Microarray analysis of altered sphingolipid metabolism reveals prognostic significance of sphingosine kinase 1 in breast cancer
    • Ruckhaberle E, Rody A, Engels K, Gaetje R, Von Minckwitz G, Schiffmann S, et al. Microarray analysis of altered sphingolipid metabolism reveals prognostic significance of sphingosine kinase 1 in breast cancer. Breast Cancer Res Treat (2008) 112:41-52. doi:10.1007/s10549-007-9836-9
    • (2008) Breast Cancer Res Treat , vol.112 , pp. 41-52
    • Ruckhaberle, E.1    Rody, A.2    Engels, K.3    Gaetje, R.4    Von Minckwitz, G.5    Schiffmann, S.6
  • 151
    • 46749153415 scopus 로고    scopus 로고
    • Sphingosine kinase 1 protein and mRNA are overexpressed in non-Hodgkin lymphomas and are attractive targets for novel pharmacological interventions
    • Bayerl MG, Bruggeman RD, Conroy EJ, Hengst JA, King TS, Jimenez M, et al. Sphingosine kinase 1 protein and mRNA are overexpressed in non-Hodgkin lymphomas and are attractive targets for novel pharmacological interventions. Leuk Lymphoma (2008) 49:948-54. doi:10.1080/10428190801911654
    • (2008) Leuk Lymphoma , vol.49 , pp. 948-954
    • Bayerl, M.G.1    Bruggeman, R.D.2    Conroy, E.J.3    Hengst, J.A.4    King, T.S.5    Jimenez, M.6
  • 154
    • 23844498431 scopus 로고    scopus 로고
    • Sphingosine kinase-1 expression correlates with poor survival of patients with glioblastoma multiforme: roles of sphingosine kinase isoforms in growth of glioblastoma cell lines
    • Van Brocklyn JR, Jackson CA, Pearl DK, Kotur MS, Snyder PJ, Prior TW. Sphingosine kinase-1 expression correlates with poor survival of patients with glioblastoma multiforme: roles of sphingosine kinase isoforms in growth of glioblastoma cell lines. J Neuropathol Exp Neurol (2005) 64:695-705. doi:10.1097/01.jnen.0000175329.59092.2c
    • (2005) J Neuropathol Exp Neurol , vol.64 , pp. 695-705
    • Van Brocklyn, J.R.1    Jackson, C.A.2    Pearl, D.K.3    Kotur, M.S.4    Snyder, P.J.5    Prior, T.W.6
  • 156
    • 68149091582 scopus 로고    scopus 로고
    • Gene expression of ceramide kinase, galactosyl ceramide synthase and ganglioside GD3 synthase is associated with prognosis in breast cancer
    • Ruckhaberle E, Karn T, Rody A, Hanker L, Gatje R, Metzler D, et al. Gene expression of ceramide kinase, galactosyl ceramide synthase and ganglioside GD3 synthase is associated with prognosis in breast cancer. J Cancer Res Clin Oncol (2009) 135:1005-13. doi:10.1007/s00432-008-0536-6
    • (2009) J Cancer Res Clin Oncol , vol.135 , pp. 1005-1013
    • Ruckhaberle, E.1    Karn, T.2    Rody, A.3    Hanker, L.4    Gatje, R.5    Metzler, D.6
  • 158
    • 35549006797 scopus 로고    scopus 로고
    • Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival
    • Hayashi T, Su TP. Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival. Cell (2007) 131:596-610. doi:10.1016/j.cell.2007.08.036
    • (2007) Cell , vol.131 , pp. 596-610
    • Hayashi, T.1    Su, T.P.2
  • 159
    • 84857190393 scopus 로고    scopus 로고
    • Palmitoylated TMX and calnexin target to the mitochondria-associated membrane
    • Lynes EM, Bui M, Yap MC, Benson MD, Schneider B, Ellgaard L, et al. Palmitoylated TMX and calnexin target to the mitochondria-associated membrane. EMBO J (2012) 31:457-70. doi:10.1038/emboj.2011.384
    • (2012) EMBO J , vol.31 , pp. 457-470
    • Lynes, E.M.1    Bui, M.2    Yap, M.C.3    Benson, M.D.4    Schneider, B.5    Ellgaard, L.6
  • 160
    • 79952291364 scopus 로고    scopus 로고
    • Molecular mechanisms and physiologic functions of mitochondrial dynamics
    • Otera H, Mihara K. Molecular mechanisms and physiologic functions of mitochondrial dynamics. J Biochem (2011) 149:241-51. doi:10.1093/jb/mvr002
    • (2011) J Biochem , vol.149 , pp. 241-251
    • Otera, H.1    Mihara, K.2
  • 161
    • 67650868959 scopus 로고    scopus 로고
    • Mitochondrial dynamics in mammalian health and disease
    • Liesa M, Palacin M, Zorzano A. Mitochondrial dynamics in mammalian health and disease. Physiol Rev (2009) 89:799-845. doi:10.1152/physrev.00030.2008
    • (2009) Physiol Rev , vol.89 , pp. 799-845
    • Liesa, M.1    Palacin, M.2    Zorzano, A.3
  • 162
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • Hoppins S, Lackner L, Nunnari J. The machines that divide and fuse mitochondria. Annu Rev Biochem (2007) 76:751-80. doi:10.1146/annurev.biochem.76.071905.090048
    • (2007) Annu Rev Biochem , vol.76 , pp. 751-780
    • Hoppins, S.1    Lackner, L.2    Nunnari, J.3
  • 163
    • 33746016268 scopus 로고    scopus 로고
    • Mitochondria: more than just a powerhouse
    • McBride HM, Neuspiel M, Wasiak S. Mitochondria: more than just a powerhouse. Curr Biol (2006) 16:R551-60. doi:10.1016/j.cub.2006.06.054
    • (2006) Curr Biol , vol.16 , pp. R551-R560
    • McBride, H.M.1    Neuspiel, M.2    Wasiak, S.3
  • 165
    • 78649413837 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in cell life and death
    • Westermann B. Mitochondrial fusion and fission in cell life and death. Nat Rev Mol Cell Biol (2010) 11:872-84. doi:10.1038/nrm3013
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 872-884
    • Westermann, B.1
  • 166
    • 45349094984 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis
    • Suen DF, Norris KL, Youle RJ. Mitochondrial dynamics and apoptosis. Genes Dev (2008) 22:1577-90. doi:10.1101/gad.1658508
    • (2008) Genes Dev , vol.22 , pp. 1577-1590
    • Suen, D.F.1    Norris, K.L.2    Youle, R.J.3
  • 167
    • 80051770868 scopus 로고    scopus 로고
    • The role of PML in the control of apoptotic cell fate: a new key player at ER-mitochondria sites
    • Pinton P, Giorgi C, Pandolfi PP. The role of PML in the control of apoptotic cell fate: a new key player at ER-mitochondria sites. Cell Death Differ (2011) 18:1450-6. doi:10.1038/cdd.2011.31
    • (2011) Cell Death Differ , vol.18 , pp. 1450-1456
    • Pinton, P.1    Giorgi, C.2    Pandolfi, P.P.3
  • 168
    • 38549132438 scopus 로고    scopus 로고
    • Degradation of the tumor suppressor PML by Pin1 contributes to the cancer phenotype of breast cancer MDA-MB-231 cells
    • Reineke EL, Lam M, Liu Q, Liu Y, Stanya KJ, Chang KS, et al. Degradation of the tumor suppressor PML by Pin1 contributes to the cancer phenotype of breast cancer MDA-MB-231 cells. Mol Cell Biol (2008) 28:997-1006. doi:10.1128/MCB.01848-07
    • (2008) Mol Cell Biol , vol.28 , pp. 997-1006
    • Reineke, E.L.1    Lam, M.2    Liu, Q.3    Liu, Y.4    Stanya, K.J.5    Chang, K.S.6
  • 170
    • 56849113081 scopus 로고    scopus 로고
    • Role of SERCA1 truncated isoform in the proapoptotic calcium transfer from ER to mitochondria during ER stress
    • Chami M, Oules B, Szabadkai G, Tacine R, Rizzuto R, Paterlini-Brechot P. Role of SERCA1 truncated isoform in the proapoptotic calcium transfer from ER to mitochondria during ER stress. Mol Cell (2008) 32:641-51. doi:10.1016/j.molcel.2008.11.014
    • (2008) Mol Cell , vol.32 , pp. 641-651
    • Chami, M.1    Oules, B.2    Szabadkai, G.3    Tacine, R.4    Rizzuto, R.5    Paterlini-Brechot, P.6
  • 171
    • 84887589243 scopus 로고    scopus 로고
    • Identification of PTEN at the ER and MAMs and its regulation of Ca(2+) signaling and apoptosis in a protein phosphatase-dependent manner
    • Bononi A, Bonora M, Marchi S, Missiroli S, Poletti F, Giorgi C, et al. Identification of PTEN at the ER and MAMs and its regulation of Ca(2+) signaling and apoptosis in a protein phosphatase-dependent manner. Cell Death Differ (2013) 20:1631-43. doi:10.1038/cdd.2013.77
    • (2013) Cell Death Differ , vol.20 , pp. 1631-1643
    • Bononi, A.1    Bonora, M.2    Marchi, S.3    Missiroli, S.4    Poletti, F.5    Giorgi, C.6
  • 172
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder K, Tschopp J. The inflammasomes. Cell (2010) 140:821-32. doi:10.1016/j.cell.2010.01.040
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 174
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • Zhou R, Yazdi AS, Menu P, Tschopp J. A role for mitochondria in NLRP3 inflammasome activation. Nature (2011) 469:221-5. doi:10.1038/nature09663
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 175
    • 77952303410 scopus 로고    scopus 로고
    • The NLRP3 inflammasome functions as a negative regulator of tumorigenesis during colitis-associated cancer
    • Allen IC, Tekippe EM, Woodford RM, Uronis JM, Holl EK, Rogers AB, et al. The NLRP3 inflammasome functions as a negative regulator of tumorigenesis during colitis-associated cancer. J Exp Med (2010) 207:1045-56. doi:10.1084/jem.20100050
    • (2010) J Exp Med , vol.207 , pp. 1045-1056
    • Allen, I.C.1    Tekippe, E.M.2    Woodford, R.M.3    Uronis, J.M.4    Holl, E.K.5    Rogers, A.B.6
  • 176
    • 84891500326 scopus 로고    scopus 로고
    • Deregulation of the NLRP3 inflammasome in hepatic parenchymal cells during liver cancer progression
    • Wei Q, Mu K, Li T, Zhang Y, Yang Z, Jia X, et al. Deregulation of the NLRP3 inflammasome in hepatic parenchymal cells during liver cancer progression. Lab Invest (2014) 94:52-62. doi:10.1038/labinvest.2013.126
    • (2014) Lab Invest , vol.94 , pp. 52-62
    • Wei, Q.1    Mu, K.2    Li, T.3    Zhang, Y.4    Yang, Z.5    Jia, X.6
  • 177
    • 13944253573 scopus 로고    scopus 로고
    • Regulating intracellular antiviral defense and permissiveness to hepatitis C virus RNA replication through a cellular RNA helicase, RIG-I
    • Sumpter R Jr, Loo YM, Foy E, Li K, Yoneyama M, Fujita T, et al. Regulating intracellular antiviral defense and permissiveness to hepatitis C virus RNA replication through a cellular RNA helicase, RIG-I. J Virol (2005) 79:2689-99. doi:10.1128/JVI.79.5.2689-2699.2005
    • (2005) J Virol , vol.79 , pp. 2689-2699
    • Sumpter, R.1    Loo, Y.M.2    Foy, E.3    Li, K.4    Yoneyama, M.5    Fujita, T.6
  • 178
    • 3242813113 scopus 로고    scopus 로고
    • The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
    • Yoneyama M, Kikuchi M, Natsukawa T, Shinobu N, Imaizumi T, Miyagishi M, et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat Immunol (2004) 5:730-7. doi:10.1038/ni1087
    • (2004) Nat Immunol , vol.5 , pp. 730-737
    • Yoneyama, M.1    Kikuchi, M.2    Natsukawa, T.3    Shinobu, N.4    Imaizumi, T.5    Miyagishi, M.6
  • 179
    • 84869233969 scopus 로고    scopus 로고
    • TRAIL and NOXA are selectively upregulated in prostate cancer cells downstream of the RIG-I/MAVS signaling pathway by nonreplicating Sendai virus particles
    • Matsushima-Miyagi T, Hatano K, Nomura M, Li-Wen L, Nishikawa T, Saga K, et al. TRAIL and NOXA are selectively upregulated in prostate cancer cells downstream of the RIG-I/MAVS signaling pathway by nonreplicating Sendai virus particles. Clin Cancer Res (2012) 18:6271-83. doi:10.1158/1078-0432.CCR-12-1595
    • (2012) Clin Cancer Res , vol.18 , pp. 6271-6283
    • Matsushima-Miyagi, T.1    Hatano, K.2    Nomura, M.3    Li-Wen, L.4    Nishikawa, T.5    Saga, K.6
  • 180
    • 84886943336 scopus 로고    scopus 로고
    • The RIG-I/MAVS signaling pathway in cancer cell-selective apoptosis
    • Kaneda Y. The RIG-I/MAVS signaling pathway in cancer cell-selective apoptosis. Oncoimmunology (2013) 2:e23566. doi:10.4161/onci.23566
    • (2013) Oncoimmunology , vol.2
    • Kaneda, Y.1
  • 181
    • 77952503750 scopus 로고    scopus 로고
    • Peroxisomes are signaling platforms for antiviral innate immunity
    • Dixit E, Boulant S, Zhang Y, Lee AS, Odendall C, Shum B, et al. Peroxisomes are signaling platforms for antiviral innate immunity. Cell (2010) 141:668-81. doi:10.1016/j.cell.2010.04.018
    • (2010) Cell , vol.141 , pp. 668-681
    • Dixit, E.1    Boulant, S.2    Zhang, Y.3    Lee, A.S.4    Odendall, C.5    Shum, B.6
  • 182
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3
    • Seth RB, Sun L, Ea CK, Chen ZJ. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell (2005) 122:669-82. doi:10.1016/j.cell.2005.08.012
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 183
    • 80052281413 scopus 로고    scopus 로고
    • Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus
    • Horner SM, Liu HM, Park HS, Briley J, Gale M Jr. Mitochondrial-associated endoplasmic reticulum membranes (MAM) form innate immune synapses and are targeted by hepatitis C virus. Proc Natl Acad Sci U S A (2011) 108:14590-5. doi:10.1073/pnas.1110133108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14590-14595
    • Horner, S.M.1    Liu, H.M.2    Park, H.S.3    Briley, J.4    Gale, M.5
  • 184
    • 77955708533 scopus 로고    scopus 로고
    • Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM)
    • Gilady SY, Bui M, Lynes EM, Benson MD, Watts R, Vance JE, et al. Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM). Cell Stress Chaperones (2010) 15:619-29. doi:10.1007/s12192-010-0174-1
    • (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
  • 186
    • 84870984470 scopus 로고    scopus 로고
    • PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress
    • Verfaillie T, Rubio N, Garg AD, Bultynck G, Rizzuto R, Decuypere JP, et al. PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress. Cell Death Differ (2012) 19:1880-91. doi:10.1038/cdd.2012.74
    • (2012) Cell Death Differ , vol.19 , pp. 1880-1891
    • Verfaillie, T.1    Rubio, N.2    Garg, A.D.3    Bultynck, G.4    Rizzuto, R.5    Decuypere, J.P.6
  • 188
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: renovation of cells and tissues
    • Mizushima N, Komatsu M. Autophagy: renovation of cells and tissues. Cell (2011) 147:728-41. doi:10.1016/j.cell.2011.10.026
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 189
  • 190
  • 191
    • 67349241955 scopus 로고    scopus 로고
    • DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival
    • Peterson TR, Laplante M, Thoreen CC, Sancak Y, Kang SA, Kuehl WM, et al. DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival. Cell (2009) 137:873-86. doi:10.1016/j.cell.2009.03.046
    • (2009) Cell , vol.137 , pp. 873-886
    • Peterson, T.R.1    Laplante, M.2    Thoreen, C.C.3    Sancak, Y.4    Kang, S.A.5    Kuehl, W.M.6
  • 192
    • 84903955288 scopus 로고    scopus 로고
    • mTORC1 signaling controls mammalian skeletal growth through stimulation of protein synthesis
    • Chen J, Long F. mTORC1 signaling controls mammalian skeletal growth through stimulation of protein synthesis. Development (2014) 141:2848-54. doi:10.1242/dev.108811
    • (2014) Development , vol.141 , pp. 2848-2854
    • Chen, J.1    Long, F.2
  • 193
    • 84903437266 scopus 로고    scopus 로고
    • mTORC2 in the center of cancer metabolic reprogramming
    • Masui K, Cavenee WK, Mischel PS. mTORC2 in the center of cancer metabolic reprogramming. Trends Endocrinol Metab (2014) 25:364-73. doi:10.1016/j.tem.2014.04.002
    • (2014) Trends Endocrinol Metab , vol.25 , pp. 364-373
    • Masui, K.1    Cavenee, W.K.2    Mischel, P.S.3
  • 194
    • 84881098989 scopus 로고    scopus 로고
    • Feature article: mTOR complex 2-Akt signaling at mitochondria-associated endoplasmic reticulum membranes (MAM) regulates mitochondrial physiology
    • Betz C, Stracka D, Prescianotto-Baschong C, Frieden M, Demaurex N, Hall MN. Feature article: mTOR complex 2-Akt signaling at mitochondria-associated endoplasmic reticulum membranes (MAM) regulates mitochondrial physiology. Proc Natl Acad Sci U S A (2013) 110:12526-34. doi:10.1073/pnas.1302455110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 12526-12534
    • Betz, C.1    Stracka, D.2    Prescianotto-Baschong, C.3    Frieden, M.4    Demaurex, N.5    Hall, M.N.6


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