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Volumn 1798, Issue 8, 2010, Pages 1465-1473

Oxidative protein folding in the endoplasmic reticulum: Tight links to the mitochondria-associated membrane (MAM)

Author keywords

Apoptosis; Chaperone; Endoplasmic reticulum (ER); Mitochondria; Mitochondria associated membrane (MAM); Oxidative protein folding

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM; CALCIUM CHANNEL; CALNEXIN; CALRETICULIN; CELL PROTEIN; CHAPERONE; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; MITOCHONDRIAL PROTEIN; OXIDOREDUCTASE; PHOSPHOFURIN ACIDIC CLUSTER SORTING PROTEIN 2; PROTEIN ERO1ALPHA; PROTEIN P44; PROTEIN P57; REGULATOR PROTEIN; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SECRETORY PROTEIN; UNCLASSIFIED DRUG;

EID: 77953725586     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.04.009     Document Type: Review
Times cited : (176)

References (201)
  • 1
    • 0021340291 scopus 로고
    • Isolation of plasma membrane, golgi apparatus, and endoplasmic reticulum fractions from single homogenates of mouse liver
    • Croze E.M., Morre D.J. Isolation of plasma membrane, golgi apparatus, and endoplasmic reticulum fractions from single homogenates of mouse liver. J. Cell. Physiol. 1984, 119:46-57.
    • (1984) J. Cell. Physiol. , vol.119 , pp. 46-57
    • Croze, E.M.1    Morre, D.J.2
  • 2
    • 0015610440 scopus 로고
    • Ultrastructural morphometry of the pancreatic β-cell
    • Dean P.M. Ultrastructural morphometry of the pancreatic β-cell. Diabetologia 1973, 9:115-119.
    • (1973) Diabetologia , vol.9 , pp. 115-119
    • Dean, P.M.1
  • 3
    • 0036877142 scopus 로고    scopus 로고
    • The endoplasmic reticulum: a multifunctional signaling organelle
    • Berridge M.J. The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium 2002, 32:235-249.
    • (2002) Cell Calcium , vol.32 , pp. 235-249
    • Berridge, M.J.1
  • 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 M.A., Brostrom C.O. Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability. Cell Calcium 2003, 34:345-363.
    • (2003) Cell Calcium , vol.34 , pp. 345-363
    • Brostrom, M.A.1    Brostrom, C.O.2
  • 5
    • 2342572271 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in mammalian cells
    • Vance J.E., Vance D.E. Phospholipid biosynthesis in mammalian cells. Biochem. Cell. Biol. 2004, 82:113-128.
    • (2004) Biochem. Cell. Biol. , vol.82 , pp. 113-128
    • Vance, J.E.1    Vance, D.E.2
  • 7
    • 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, 16:343-349.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 9
    • 39149109255 scopus 로고    scopus 로고
    • Topology of molecular machines of the endoplasmic reticulum: a compilation of proteomics and cytological data
    • Lavoie C., Paiement J. Topology of molecular machines of the endoplasmic reticulum: a compilation of proteomics and cytological data. Histochem. Cell Biol. 2008, 129:117-128.
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 117-128
    • Lavoie, C.1    Paiement, J.2
  • 10
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport T.A. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 2007, 450:663-669.
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 12
    • 0348103715 scopus 로고    scopus 로고
    • Ultrastructural analysis of transitional endoplasmic reticulum and pre-Golgi intermediates: a highway for cars and trucks
    • Fan J.Y., Roth J., Zuber C. Ultrastructural analysis of transitional endoplasmic reticulum and pre-Golgi intermediates: a highway for cars and trucks. Histochem. Cell Biol. 2003, 120:455-463.
    • (2003) Histochem. Cell Biol. , vol.120 , pp. 455-463
    • Fan, J.Y.1    Roth, J.2    Zuber, C.3
  • 13
    • 68949192292 scopus 로고    scopus 로고
    • Interactions between the endoplasmic reticulum, mitochondria, plasma membrane and other subcellular organelles
    • Lebiedzinska M., Szabadkai G., Jones A.W., Duszynski J., Wieckowski M.R. Interactions between the endoplasmic reticulum, mitochondria, plasma membrane and other subcellular organelles. Int. J. Biochem. Cell Biol. 2009, 41:1805-1816.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1805-1816
    • Lebiedzinska, M.1    Szabadkai, G.2    Jones, A.W.3    Duszynski, J.4    Wieckowski, M.R.5
  • 14
    • 69049098806 scopus 로고    scopus 로고
    • Structural and functional link between the mitochondrial network and the endoplasmic reticulum
    • Giorgi C., De Stefani D., Bononi A., Rizzuto R., Pinton P. Structural and functional link between the mitochondrial network and the endoplasmic reticulum. Int. J. Biochem. Cell Biol. 2009, 41:1817-1827.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1817-1827
    • Giorgi, C.1    De Stefani, D.2    Bononi, A.3    Rizzuto, R.4    Pinton, P.5
  • 15
    • 36248938166 scopus 로고    scopus 로고
    • Reversible interactions between smooth domains of the endoplasmic reticulum and mitochondria are regulated by physiological cytosolic Ca2+ levels
    • Goetz J.G., Genty H., St-Pierre P., Dang T., Joshi B., Sauve R., Vogl W., Nabi I.R. Reversible interactions between smooth domains of the endoplasmic reticulum and mitochondria are regulated by physiological cytosolic Ca2+ levels. J. Cell Sci. 2007, 120:3553-3564.
    • (2007) J. Cell Sci. , vol.120 , pp. 3553-3564
    • Goetz, J.G.1    Genty, H.2    St-Pierre, P.3    Dang, T.4    Joshi, B.5    Sauve, R.6    Vogl, W.7    Nabi, I.R.8
  • 16
    • 0344966647 scopus 로고
    • An association between mitochondria and the endoplasmic reticulum in cells of the pseudobranch gland of a teleost
    • Copeland D.E., Dalton A.J. An association between mitochondria and the endoplasmic reticulum in cells of the pseudobranch gland of a teleost. J. Biophys. Biochem. Cytol. 1959, 5:393-396.
    • (1959) J. Biophys. Biochem. Cytol. , vol.5 , pp. 393-396
    • Copeland, D.E.1    Dalton, A.J.2
  • 17
    • 0014742867 scopus 로고
    • The origin of mitochondrial phosphatidylcholine within the liver cell
    • Jungalwala F.B., Dawson R.M. The origin of mitochondrial phosphatidylcholine within the liver cell. Eur. J. Biochem. 1970, 12:399-402.
    • (1970) Eur. J. Biochem. , vol.12 , pp. 399-402
    • Jungalwala, F.B.1    Dawson, R.M.2
  • 18
    • 0014480903 scopus 로고
    • Phospholipid exchange reactions within the liver cell
    • McMurray W.C., Dawson R.M. Phospholipid exchange reactions within the liver cell. Biochem. J. 1969, 112:91-108.
    • (1969) Biochem. J. , vol.112 , pp. 91-108
    • McMurray, W.C.1    Dawson, R.M.2
  • 19
    • 0014982664 scopus 로고
    • Study of the transfer of phospholipids from the endoplasmic reticulum to the outer and inner mitochondrial membranes
    • Sauner M.T., Levy M. Study of the transfer of phospholipids from the endoplasmic reticulum to the outer and inner mitochondrial membranes. J. Lipid Res. 1971, 12:71-75.
    • (1971) J. Lipid Res. , vol.12 , pp. 71-75
    • Sauner, M.T.1    Levy, M.2
  • 20
    • 0015791478 scopus 로고
    • A rapidly sedimenting fraction of rat liver endoplasmic reticulum
    • Lewis J.A., Tata J.R. A rapidly sedimenting fraction of rat liver endoplasmic reticulum. J. Cell Sci. 1973, 13:447-459.
    • (1973) J. Cell Sci. , vol.13 , pp. 447-459
    • Lewis, J.A.1    Tata, J.R.2
  • 21
    • 0017325162 scopus 로고
    • Two fractions of rough endoplasmic reticulum from rat liver. I. Recovery of rapidly sedimenting endoplasmic reticulum in association with mitochondria
    • Shore G.C., Tata J.R. Two fractions of rough endoplasmic reticulum from rat liver. I. Recovery of rapidly sedimenting endoplasmic reticulum in association with mitochondria. J. Cell Biol. 1977, 72:714-725.
    • (1977) J. Cell Biol. , vol.72 , pp. 714-725
    • Shore, G.C.1    Tata, J.R.2
  • 22
    • 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 A.E., Cui Z., Chen M.H., Vance J.E. 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, 269:27494-27502.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27494-27502
    • Rusinol, A.E.1    Cui, Z.2    Chen, M.H.3    Vance, J.E.4
  • 23
    • 0034602158 scopus 로고    scopus 로고
    • Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes
    • Stone S.J., Vance J.E. Phosphatidylserine synthase-1 and -2 are localized to mitochondria-associated membranes. J. Biol. Chem. 2000, 275:34534-34540.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34534-34540
    • Stone, S.J.1    Vance, J.E.2
  • 24
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance J.E. Phospholipid synthesis in a membrane fraction associated with mitochondria. J. Biol. Chem. 1990, 265:7248-7256.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 25
    • 0032425805 scopus 로고    scopus 로고
    • Electron microscopic tomography of rat-liver mitochondria and their interaction with the endoplasmic reticulum
    • Mannella C.A., Buttle K., Rath B.K., Marko M. Electron microscopic tomography of rat-liver mitochondria and their interaction with the endoplasmic reticulum. Biofactors 1998, 8:225-228.
    • (1998) Biofactors , vol.8 , pp. 225-228
    • Mannella, C.A.1    Buttle, K.2    Rath, B.K.3    Marko, M.4
  • 27
    • 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, 262:744-747.
    • (1993) Science , vol.262 , pp. 744-747
    • Rizzuto, R.1    Brini, M.2    Murgia, M.3    Pozzan, T.4
  • 28
    • 0026659512 scopus 로고
    • Rapid changes of mitochondrial Ca2+ revealed by specifically targeted recombinant aequorin
    • Rizzuto R., Simpson A.W., Brini M., Pozzan T. Rapid changes of mitochondrial Ca2+ revealed by specifically targeted recombinant aequorin. Nature 1992, 358:325-327.
    • (1992) Nature , vol.358 , pp. 325-327
    • Rizzuto, R.1    Simpson, A.W.2    Brini, M.3    Pozzan, T.4
  • 29
    • 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 P.J., 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, 278:39224-39234.
    • (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
  • 30
    • 0033521586 scopus 로고    scopus 로고
    • Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria
    • Csordas G., Thomas A.P., Hajnoczky G. Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria. Embo J. 1999, 18:96-108.
    • (1999) Embo J. , vol.18 , pp. 96-108
    • Csordas, G.1    Thomas, A.P.2    Hajnoczky, G.3
  • 31
    • 84857501714 scopus 로고    scopus 로고
    • The IP3 receptor/Ca2+ channel and its cellular function
    • Mikoshiba K. The IP3 receptor/Ca2+ channel and its cellular function. Biochem. Soc. Symp. 2007, 9-22.
    • (2007) Biochem. Soc. Symp. , pp. 9-22
    • Mikoshiba, K.1
  • 32
    • 0035065493 scopus 로고    scopus 로고
    • Sorting of calcium signals at the junctions of endoplasmic reticulum and mitochondria
    • Csordas G., Hajnoczky G. Sorting of calcium signals at the junctions of endoplasmic reticulum and mitochondria. Cell Calcium 2001, 29:249-262.
    • (2001) Cell Calcium , vol.29 , pp. 249-262
    • Csordas, G.1    Hajnoczky, G.2
  • 33
    • 0035163552 scopus 로고    scopus 로고
    • Calcium signal transmission between ryanodine receptors and mitochondria in cardiac muscle
    • Csordas G., Thomas A.P., Hajnoczky G. Calcium signal transmission between ryanodine receptors and mitochondria in cardiac muscle. Trends Cardiovasc. Med. 2001, 11:269-275.
    • (2001) Trends Cardiovasc. Med. , vol.11 , pp. 269-275
    • Csordas, G.1    Thomas, A.P.2    Hajnoczky, G.3
  • 34
    • 70349653079 scopus 로고    scopus 로고
    • Calcium pumps in health and disease
    • Brini M., Carafoli E. Calcium pumps in health and disease. Physiol. Rev. 2009, 89:1341-1378.
    • (2009) Physiol. Rev. , vol.89 , pp. 1341-1378
    • Brini, M.1    Carafoli, E.2
  • 35
    • 0023391047 scopus 로고
    • Evidence for the presence of a reversible Ca2+-dependent pore activated by oxidative stress in heart mitochondria
    • Crompton M., Costi A., Hayat L. Evidence for the presence of a reversible Ca2+-dependent pore activated by oxidative stress in heart mitochondria. Biochem. J. 1987, 245:915-918.
    • (1987) Biochem. J. , vol.245 , pp. 915-918
    • Crompton, M.1    Costi, A.2    Hayat, L.3
  • 41
    • 0033199506 scopus 로고    scopus 로고
    • Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact
    • Achleitner G., Gaigg B., Krasser A., Kainersdorfer E., Kohlwein S.D., Perktold A., Zellnig G., Daum G. Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact. Eur. J. Biochem. 1999, 264:545-553.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 545-553
    • Achleitner, G.1    Gaigg, B.2    Krasser, A.3    Kainersdorfer, E.4    Kohlwein, S.D.5    Perktold, A.6    Zellnig, G.7    Daum, G.8
  • 42
    • 0037185026 scopus 로고    scopus 로고
    • Phosphatidylserine transport to the mitochondria is regulated by ubiquitination
    • Schumacher M.M., Choi J.Y., Voelker D.R. Phosphatidylserine transport to the mitochondria is regulated by ubiquitination. J. Biol. Chem. 2002, 277:51033-51042.
    • (2002) J. Biol. Chem. , vol.277 , pp. 51033-51042
    • Schumacher, M.M.1    Choi, J.Y.2    Voelker, D.R.3
  • 44
    • 0344392841 scopus 로고    scopus 로고
    • A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery
    • Boldogh I.R., Nowakowski D.W., Yang H.C., Chung H., Karmon S., Royes P., Pon L.A. A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery. Mol. Biol. Cell 2003, 14:4618-4627.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4618-4627
    • Boldogh, I.R.1    Nowakowski, D.W.2    Yang, H.C.3    Chung, H.4    Karmon, S.5    Royes, P.6    Pon, L.A.7
  • 46
    • 33644905848 scopus 로고    scopus 로고
    • Diverse membrane-associated proteins contain a novel SMP domain
    • Lee I., Hong W. Diverse membrane-associated proteins contain a novel SMP domain. Faseb J. 2006, 20:202-206.
    • (2006) Faseb J. , vol.20 , pp. 202-206
    • Lee, I.1    Hong, W.2
  • 47
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito O.M., Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 2008, 456:605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • de Brito, O.M.1    Scorrano, L.2
  • 49
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen H., Detmer S.A., Ewald A.J., Griffin E.E., Fraser S.E., Chan D.C. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 2003, 160:189-200.
    • (2003) J. Cell Biol. , vol.160 , pp. 189-200
    • Chen, H.1    Detmer, S.A.2    Ewald, A.J.3    Griffin, E.E.4    Fraser, S.E.5    Chan, D.C.6
  • 50
    • 13444287961 scopus 로고    scopus 로고
    • Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
    • Ishihara N., Eura Y., Mihara K. Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity. J. Cell Sci. 2004, 117:6535-6546.
    • (2004) J. Cell Sci. , vol.117 , pp. 6535-6546
    • Ishihara, N.1    Eura, Y.2    Mihara, K.3
  • 53
    • 0034640960 scopus 로고    scopus 로고
    • Cytosolic phosphorylation of calnexin controls intracellular Ca(2+) oscillations via an interaction with SERCA2b
    • Roderick H.L., Lechleiter J.D., Camacho P. Cytosolic phosphorylation of calnexin controls intracellular Ca(2+) oscillations via an interaction with SERCA2b. J. Cell Biol. 2000, 149:1235-1248.
    • (2000) J. Cell Biol. , vol.149 , pp. 1235-1248
    • Roderick, H.L.1    Lechleiter, J.D.2    Camacho, P.3
  • 55
    • 0032514917 scopus 로고    scopus 로고
    • Direct monitoring of the calcium concentration in the sarcoplasmic and endoplasmic reticulum of skeletal muscle myotubes
    • Robert V., De Giorgi F., Massimino M.L., Cantini M., Pozzan T. Direct monitoring of the calcium concentration in the sarcoplasmic and endoplasmic reticulum of skeletal muscle myotubes. J. Biol. Chem. 1998, 273:30372-30378.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30372-30378
    • Robert, V.1    De Giorgi, F.2    Massimino, M.L.3    Cantini, M.4    Pozzan, T.5
  • 56
    • 0025313861 scopus 로고
    • Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum
    • Lodish H.F., Kong N. Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum. J. Biol. Chem. 1990, 265:10893-10899.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10893-10899
    • Lodish, H.F.1    Kong, N.2
  • 57
    • 0026654505 scopus 로고
    • Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum
    • Lodish H.F., Kong N., Wikstrom L. Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum. J. Biol. Chem. 1992, 267:12753-12760.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12753-12760
    • Lodish, H.F.1    Kong, N.2    Wikstrom, L.3
  • 58
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: mechanisms and consequences
    • Tu B.P., Weissman J.S. Oxidative protein folding in eukaryotes: mechanisms and consequences. J. Cell Biol. 2004, 164:341-346.
    • (2004) J. Cell Biol. , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 59
  • 60
    • 0033208953 scopus 로고    scopus 로고
    • Role and regulation of the ER chaperone BiP
    • Gething M.J. Role and regulation of the ER chaperone BiP. Semin. Cell Dev. Biol. 1999, 10:465-472.
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 465-472
    • Gething, M.J.1
  • 61
    • 59849120392 scopus 로고    scopus 로고
    • Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
    • Michalak M., Groenendyk J., Szabo E., Gold L.I., Opas M. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem. J. 2009, 417:651-666.
    • (2009) Biochem. J. , vol.417 , pp. 651-666
    • Michalak, M.1    Groenendyk, J.2    Szabo, E.3    Gold, L.I.4    Opas, M.5
  • 62
    • 0036877146 scopus 로고    scopus 로고
    • Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum
    • Michalak M., Robert Parker J.M., Opas M. Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 2002, 32:269-278.
    • (2002) Cell Calcium , vol.32 , pp. 269-278
    • Michalak, M.1    Robert Parker, J.M.2    Opas, M.3
  • 63
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou W.J., Cameron P.H., Thomas D.Y., Bergeron J.J. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 1993, 364:771-776.
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.4
  • 64
    • 0028147528 scopus 로고
    • Retention of unassembled components of integral membrane proteins by calnexin
    • Rajagopalan S., Xu Y., Brenner M.B. Retention of unassembled components of integral membrane proteins by calnexin. Science 1994, 263:387-390.
    • (1994) Science , vol.263 , pp. 387-390
    • Rajagopalan, S.1    Xu, Y.2    Brenner, M.B.3
  • 66
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver J.D., van der Wal F.J., Bulleid N.J., High S. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 1997, 275:86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    van der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 67
    • 33645080188 scopus 로고    scopus 로고
    • Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum
    • Williams D.B. Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. J. Cell Sci. 2006, 119:615-623.
    • (2006) J. Cell Sci. , vol.119 , pp. 615-623
    • Williams, D.B.1
  • 68
    • 38549103628 scopus 로고    scopus 로고
    • Protein quality control in the early secretory pathway
    • Anelli T., Sitia R. Protein quality control in the early secretory pathway. Embo J. 2008, 27:315-327.
    • (2008) Embo J. , vol.27 , pp. 315-327
    • Anelli, T.1    Sitia, R.2
  • 69
    • 2442629457 scopus 로고    scopus 로고
    • Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding
    • Ellgaard L., Frickel E.M. Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding. Cell Biochem. Biophys. 2003, 39:223-247.
    • (2003) Cell Biochem. Biophys. , vol.39 , pp. 223-247
    • Ellgaard, L.1    Frickel, E.M.2
  • 70
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L., Helenius A. Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 2003, 4:181-191.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 71
    • 0033565230 scopus 로고    scopus 로고
    • Calcium binding capacity of the cytosol and endoplasmic reticulum of mouse pancreatic acinar cells
    • Mogami H., Gardner J., Gerasimenko O.V., Camello P., Petersen O.H., Tepikin A.V. Calcium binding capacity of the cytosol and endoplasmic reticulum of mouse pancreatic acinar cells. J Physiol 1999, 518(Pt 2):463-467.
    • (1999) J Physiol , vol.518 , Issue.PART 2 , pp. 463-467
    • Mogami, H.1    Gardner, J.2    Gerasimenko, O.V.3    Camello, P.4    Petersen, O.H.5    Tepikin, A.V.6
  • 73
    • 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, 8:519-529.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 74
    • 43249109174 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses
    • Schroder M. Endoplasmic reticulum stress responses. Cell. Mol. Life Sci. 2008, 65:862-894.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 862-894
    • Schroder, M.1
  • 75
    • 0037338462 scopus 로고    scopus 로고
    • Folding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss of Ca2+ from the endoplasmic reticulum
    • Di Jeso B., Ulianich L., Pacifico F., Leonardi A., Vito P., Consiglio E., Formisano S., Arvan P. Folding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss of Ca2+ from the endoplasmic reticulum. Biochem. J. 2003, 370:449-458.
    • (2003) Biochem. J. , vol.370 , pp. 449-458
    • Di Jeso, B.1    Ulianich, L.2    Pacifico, F.3    Leonardi, A.4    Vito, P.5    Consiglio, E.6    Formisano, S.7    Arvan, P.8
  • 76
    • 0029048360 scopus 로고
    • Conformational changes induced in the endoplasmic reticulum luminal domain of calnexin by Mg-ATP and Ca2+
    • Ou W.J., Bergeron J.J., Li Y., Kang C.Y., Thomas D.Y. Conformational changes induced in the endoplasmic reticulum luminal domain of calnexin by Mg-ATP and Ca2+. J. Biol. Chem. 1995, 270:18051-18059.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18051-18059
    • Ou, W.J.1    Bergeron, J.J.2    Li, Y.3    Kang, C.Y.4    Thomas, D.Y.5
  • 77
    • 0025866855 scopus 로고
    • Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP
    • Suzuki C.K., Bonifacino J.S., Lin A.Y., Davis M.M., Klausner R.D. Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP. J. Cell Biol. 1991, 114:189-205.
    • (1991) J. Cell Biol. , vol.114 , pp. 189-205
    • Suzuki, C.K.1    Bonifacino, J.S.2    Lin, A.Y.3    Davis, M.M.4    Klausner, R.D.5
  • 79
    • 33846223428 scopus 로고    scopus 로고
    • Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress
    • Nadanaka S., Okada T., Yoshida H., Mori K. Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress. Mol. Cell. Biol. 2007, 27:1027-1043.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1027-1043
    • Nadanaka, S.1    Okada, T.2    Yoshida, H.3    Mori, K.4
  • 80
    • 34848860536 scopus 로고    scopus 로고
    • The proprotein convertase SKI-1/S1P: alternate translation and subcellular localization
    • Pullikotil P., Benjannet S., Mayne J., Seidah N.G. The proprotein convertase SKI-1/S1P: alternate translation and subcellular localization. J. Biol. Chem. 2007, 282:27402-27413.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27402-27413
    • Pullikotil, P.1    Benjannet, S.2    Mayne, J.3    Seidah, N.G.4
  • 81
    • 5644244829 scopus 로고    scopus 로고
    • Dependence of site-2 protease cleavage of ATF6 on prior site-1 protease digestion is determined by the size of the luminal domain of ATF6
    • Shen J., Prywes R. Dependence of site-2 protease cleavage of ATF6 on prior site-1 protease digestion is determined by the size of the luminal domain of ATF6. J. Biol. Chem. 2004, 279:43046-43051.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43046-43051
    • Shen, J.1    Prywes, R.2
  • 82
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen J., Chen X., Hendershot L., Prywes R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 2002, 3:99-111.
    • (2002) Dev. Cell , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 83
    • 12844257546 scopus 로고    scopus 로고
    • Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response
    • Shen J., Snapp E.L., Lippincott-Schwartz J., Prywes R. Stable binding of ATF6 to BiP in the endoplasmic reticulum stress response. Mol. Cell. Biol. 2005, 25:921-932.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 921-932
    • Shen, J.1    Snapp, E.L.2    Lippincott-Schwartz, J.3    Prywes, R.4
  • 84
    • 0034968330 scopus 로고    scopus 로고
    • Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival
    • Harding H.P., Zeng H., Zhang Y., Jungries R., Chung P., Plesken H., Sabatini D.D., Ron D. Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival. Mol. Cell 2001, 7:1153-1163.
    • (2001) Mol. Cell , vol.7 , pp. 1153-1163
    • Harding, H.P.1    Zeng, H.2    Zhang, Y.3    Jungries, R.4    Chung, P.5    Plesken, H.6    Sabatini, D.D.7    Ron, D.8
  • 86
    • 0034637605 scopus 로고    scopus 로고
    • Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
    • Liu C.Y., Schroder M., Kaufman R.J. Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. J. Biol. Chem. 2000, 275:24881-24885.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24881-24885
    • Liu, C.Y.1    Schroder, M.2    Kaufman, R.J.3
  • 87
    • 0034312290 scopus 로고    scopus 로고
    • The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response
    • Tirasophon W., Lee K., Callaghan B., Welihinda A., Kaufman R.J. The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response. Genes Dev. 2000, 14:2725-2736.
    • (2000) Genes Dev. , vol.14 , pp. 2725-2736
    • Tirasophon, W.1    Lee, K.2    Callaghan, B.3    Welihinda, A.4    Kaufman, R.J.5
  • 88
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H., Matsui T., Yamamoto A., Okada T., Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001, 107:881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 89
    • 0033739622 scopus 로고    scopus 로고
    • PERK mediates cell-cycle exit during the mammalian unfolded protein response
    • Brewer J.W., Diehl J.A. PERK mediates cell-cycle exit during the mammalian unfolded protein response. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:12625-12630.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 12625-12630
    • Brewer, J.W.1    Diehl, J.A.2
  • 90
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding H.P., Zhang Y., Bertolotti A., Zeng H., Ron D. Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell 2000, 5:897-904.
    • (2000) Mol. Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 91
    • 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 H.P., Ron D. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 2000, 287:664-666.
    • (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    Ron, D.7
  • 92
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • Oyadomari S., Mori M. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ. 2004, 11:381-389.
    • (2004) Cell Death Differ. , vol.11 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 93
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • Ma Y., Brewer J.W., Diehl J.A., Hendershot L.M. Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J. Mol. Biol. 2002, 318:1351-1365.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 94
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state
    • McCullough K.D., Martindale J.L., Klotz L.O., Aw T.Y., Holbrook N.J. Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol. Cell. Biol. 2001, 21:1249-1259.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.O.3    Aw, T.Y.4    Holbrook, N.J.5
  • 96
    • 0032517976 scopus 로고    scopus 로고
    • Termination of cytosolic Ca2+ signals: Ca2+ reuptake into intracellular stores is regulated by the free Ca2+ concentration in the store lumen
    • Mogami H., Tepikin A.V., Petersen O.H. Termination of cytosolic Ca2+ signals: Ca2+ reuptake into intracellular stores is regulated by the free Ca2+ concentration in the store lumen. Embo J. 1998, 17:435-442.
    • (1998) Embo J. , vol.17 , pp. 435-442
    • Mogami, H.1    Tepikin, A.V.2    Petersen, O.H.3
  • 97
    • 0034668946 scopus 로고    scopus 로고
    • Mitochondria as all-round players of the calcium game
    • Rizzuto R., Bernardi P., Pozzan T. Mitochondria as all-round players of the calcium game. J. Physiol. 2000, 529(Pt 1):37-47.
    • (2000) J. Physiol. , vol.529 , Issue.PART 1 , pp. 37-47
    • Rizzuto, R.1    Bernardi, P.2    Pozzan, T.3
  • 98
    • 0034193197 scopus 로고    scopus 로고
    • Regulation of mitochondrial metabolism by ER Ca2+ release: an intimate connection
    • Rutter G.A., Rizzuto R. Regulation of mitochondrial metabolism by ER Ca2+ release: an intimate connection. Trends Biochem. Sci. 2000, 25:215-221.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 215-221
    • Rutter, G.A.1    Rizzuto, R.2
  • 99
    • 0034668931 scopus 로고    scopus 로고
    • The machinery of local Ca2+ signalling between sarco-endoplasmic reticulum and mitochondria
    • Hajnoczky G., Csordas G., Madesh M., Pacher P. The machinery of local Ca2+ signalling between sarco-endoplasmic reticulum and mitochondria. J. Physiol. 2000, 529(Pt 1):69-81.
    • (2000) J. Physiol. , vol.529 , Issue.PART 1 , pp. 69-81
    • Hajnoczky, G.1    Csordas, G.2    Madesh, M.3    Pacher, P.4
  • 100
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Kirichok Y., Krapivinsky G., Clapham D.E. The mitochondrial calcium uniporter is a highly selective ion channel. Nature 2004, 427:360-364.
    • (2004) Nature , vol.427 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 101
    • 24644462789 scopus 로고    scopus 로고
    • Mitochondria and calcium signaling
    • Nicholls D.G. Mitochondria and calcium signaling. Cell Calcium 2005, 38:311-317.
    • (2005) Cell Calcium , vol.38 , pp. 311-317
    • Nicholls, D.G.1
  • 102
    • 35448983147 scopus 로고    scopus 로고
    • Mitochondria and Ca(2+) signaling: old guests, new functions
    • Graier W.F., Frieden M., Malli R. Mitochondria and Ca(2+) signaling: old guests, new functions. Pflugers Arch. 2007, 455:375-396.
    • (2007) Pflugers Arch. , vol.455 , pp. 375-396
    • Graier, W.F.1    Frieden, M.2    Malli, R.3
  • 103
    • 68649120751 scopus 로고    scopus 로고
    • Mitochondrial calcium as a key regulator of mitochondrial ATP production in mammalian cells
    • Griffiths E.J., Rutter G.A. Mitochondrial calcium as a key regulator of mitochondrial ATP production in mammalian cells. Biochim. Biophys. Acta 2009, 1787:1324-1333.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1324-1333
    • Griffiths, E.J.1    Rutter, G.A.2
  • 106
    • 38049155818 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis
    • Deniaud A., Sharaf Test O. Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis. Oncogene 2008, 27:285-299.
    • (2008) Oncogene , vol.27 , pp. 285-299
    • Deniaud, A.1    Sharaf Test, O.2
  • 107
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis
    • Boehning D., Patterson R.L., Sedaghat L., Glebova N.O., Kurosaki T., Snyder S.H. Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis. Nat. Cell Biol. 2003, 5:1051-1061.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1051-1061
    • Boehning, D.1    Patterson, R.L.2    Sedaghat, L.3    Glebova, N.O.4    Kurosaki, T.5    Snyder, S.H.6
  • 108
    • 4544252174 scopus 로고    scopus 로고
    • Apoptosis and calcium: new roles for cytochrome c and inositol 1,4,5-trisphosphate
    • Boehning D., Patterson R.L., Snyder S.H. Apoptosis and calcium: new roles for cytochrome c and inositol 1,4,5-trisphosphate. Cell Cycle 2004, 3:252-254.
    • (2004) Cell Cycle , vol.3 , pp. 252-254
    • Boehning, D.1    Patterson, R.L.2    Snyder, S.H.3
  • 109
    • 46649097078 scopus 로고    scopus 로고
    • Requirement of inositol 1,4,5-trisphosphate receptors for tumor-mediated lymphocyte apoptosis
    • Steinmann C., Landsverk M.L., Barral J.M., Boehning D. Requirement of inositol 1,4,5-trisphosphate receptors for tumor-mediated lymphocyte apoptosis. J. Biol. Chem. 2008, 283:13506-13509.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13506-13509
    • Steinmann, C.1    Landsverk, M.L.2    Barral, J.M.3    Boehning, D.4
  • 110
    • 33845288349 scopus 로고    scopus 로고
    • Requirement of biphasic calcium release from the endoplasmic reticulum for Fas-mediated apoptosis
    • Wozniak A.L., Wang X., Stieren E.S., Scarbrough S.G., Elferink C.J., Boehning D. Requirement of biphasic calcium release from the endoplasmic reticulum for Fas-mediated apoptosis. J. Cell Biol. 2006, 175:709-714.
    • (2006) J. Cell Biol. , vol.175 , pp. 709-714
    • Wozniak, A.L.1    Wang, X.2    Stieren, E.S.3    Scarbrough, S.G.4    Elferink, C.J.5    Boehning, D.6
  • 112
    • 35549006797 scopus 로고    scopus 로고
    • Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival
    • Hayashi T., Su T.P. Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival. Cell 2007, 131:596-610.
    • (2007) Cell , vol.131 , pp. 596-610
    • Hayashi, T.1    Su, T.P.2
  • 113
    • 11844269232 scopus 로고    scopus 로고
    • Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44
    • Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., Mikoshiba K. Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell 2005, 120:85-98.
    • (2005) Cell , vol.120 , pp. 85-98
    • Higo, T.1    Hattori, M.2    Nakamura, T.3    Natsume, T.4    Michikawa, T.5    Mikoshiba, K.6
  • 115
    • 0033570890 scopus 로고    scopus 로고
    • Apoptosis driven by IP(3)-linked mitochondrial calcium signals
    • Szalai G., Krishnamurthy R., Hajnoczky G. Apoptosis driven by IP(3)-linked mitochondrial calcium signals. Embo J. 1999, 18:6349-6361.
    • (1999) Embo J. , vol.18 , pp. 6349-6361
    • Szalai, G.1    Krishnamurthy, R.2    Hajnoczky, G.3
  • 116
    • 34147144002 scopus 로고    scopus 로고
    • Serum-withdrawal-dependent apoptosis of hippocampal neuroblasts involves Ca++ release by endoplasmic reticulum and caspase-12 activation
    • Voccoli V., Mazzoni F., Garcia-Gil M., Colombaioni L. Serum-withdrawal-dependent apoptosis of hippocampal neuroblasts involves Ca++ release by endoplasmic reticulum and caspase-12 activation. Brain Res. 2007, 1147:1-11.
    • (2007) Brain Res. , vol.1147 , pp. 1-11
    • Voccoli, V.1    Mazzoni, F.2    Garcia-Gil, M.3    Colombaioni, L.4
  • 117
    • 59149091608 scopus 로고    scopus 로고
    • Overexpression of mitochondrial Hsp70/Hsp75 in rat brain protects mitochondria, reduces oxidative stress, and protects from focal ischemia
    • Xu L., Voloboueva L.A., Ouyang Y., Emery J.F., Giffard R.G. Overexpression of mitochondrial Hsp70/Hsp75 in rat brain protects mitochondria, reduces oxidative stress, and protects from focal ischemia. J. Cereb. Blood Flow Metab. 2009, 29:365-374.
    • (2009) J. Cereb. Blood Flow Metab. , vol.29 , pp. 365-374
    • Xu, L.1    Voloboueva, L.A.2    Ouyang, Y.3    Emery, J.F.4    Giffard, R.G.5
  • 119
    • 21644455319 scopus 로고    scopus 로고
    • Activated mitofusin 2 signals mitochondrial fusion, interferes with Bax activation, and reduces susceptibility to radical induced depolarization
    • Neuspiel M., Zunino R., Gangaraju S., Rippstein P., McBride H. Activated mitofusin 2 signals mitochondrial fusion, interferes with Bax activation, and reduces susceptibility to radical induced depolarization. J. Biol. Chem. 2005, 280:25060-25070.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25060-25070
    • Neuspiel, M.1    Zunino, R.2    Gangaraju, S.3    Rippstein, P.4    McBride, H.5
  • 122
    • 65849472289 scopus 로고    scopus 로고
    • At the crossroads of homoeostasis and disease: roles of the PACS proteins in membrane traffic and apoptosis
    • Youker R.T., Shinde U., Day R., Thomas G. At the crossroads of homoeostasis and disease: roles of the PACS proteins in membrane traffic and apoptosis. Biochem. J. 2009, 421:1-15.
    • (2009) Biochem. J. , vol.421 , pp. 1-15
    • Youker, R.T.1    Shinde, U.2    Day, R.3    Thomas, G.4
  • 123
    • 69749094274 scopus 로고    scopus 로고
    • A homeostatic switch in PACS-2 links membrane traffic to TRAIL-induced apoptosis
    • You H., Thomas G. A homeostatic switch in PACS-2 links membrane traffic to TRAIL-induced apoptosis. Cell Cycle 2009, 8:2679-2680.
    • (2009) Cell Cycle , vol.8 , pp. 2679-2680
    • You, H.1    Thomas, G.2
  • 125
    • 34248573016 scopus 로고    scopus 로고
    • Both translocon and a cation channel are involved in the passive Ca2+ leak from the endoplasmic reticulum: a mechanistic study on rat liver microsomes
    • Giunti R., Gamberucci A., Fulceri R., Banhegyi G., Benedetti A. Both translocon and a cation channel are involved in the passive Ca2+ leak from the endoplasmic reticulum: a mechanistic study on rat liver microsomes. Arch. Biochem. Biophys. 2007, 462:115-121.
    • (2007) Arch. Biochem. Biophys. , vol.462 , pp. 115-121
    • Giunti, R.1    Gamberucci, A.2    Fulceri, R.3    Banhegyi, G.4    Benedetti, A.5
  • 129
    • 66849138212 scopus 로고    scopus 로고
    • Bax inhibitor 1 regulates ER-stress-induced ROS accumulation through the regulation of cytochrome P450 2E1
    • Kim H.R., Lee G.H., Cho E.Y., Chae S.W., Ahn T., Chae H.J. Bax inhibitor 1 regulates ER-stress-induced ROS accumulation through the regulation of cytochrome P450 2E1. J. Cell Sci. 2009, 122:1126-1133.
    • (2009) J. Cell Sci. , vol.122 , pp. 1126-1133
    • Kim, H.R.1    Lee, G.H.2    Cho, E.Y.3    Chae, S.W.4    Ahn, T.5    Chae, H.J.6
  • 134
    • 33846530584 scopus 로고    scopus 로고
    • Regulation of calnexin sub-cellular localization modulates endoplasmic reticulum stress-induced apoptosis in MCF-7 cells
    • Delom F., Fessart D., Chevet E. Regulation of calnexin sub-cellular localization modulates endoplasmic reticulum stress-induced apoptosis in MCF-7 cells. Apoptosis 2007, 12:293-305.
    • (2007) Apoptosis , vol.12 , pp. 293-305
    • Delom, F.1    Fessart, D.2    Chevet, E.3
  • 135
    • 71749088618 scopus 로고    scopus 로고
    • Calnexin phosphorylation attenuates the release of partially misfolded alpha1-antitrypsin to the secretory pathway
    • Cameron P.H., Chevet E., Pluquet O., Thomas D.Y., Bergeron J.J. Calnexin phosphorylation attenuates the release of partially misfolded alpha1-antitrypsin to the secretory pathway. J. Biol. Chem. 2009, 284:34570-34579.
    • (2009) J. Biol. Chem. , vol.284 , pp. 34570-34579
    • Cameron, P.H.1    Chevet, E.2    Pluquet, O.3    Thomas, D.Y.4    Bergeron, J.J.5
  • 136
    • 0347753252 scopus 로고    scopus 로고
    • Ca2+-dependent redox modulation of SERCA 2b by ERp57
    • Li Y., Camacho P. Ca2+-dependent redox modulation of SERCA 2b by ERp57. J. Cell Biol. 2004, 164:35-46.
    • (2004) J. Cell Biol. , vol.164 , pp. 35-46
    • Li, Y.1    Camacho, P.2
  • 137
    • 0026432666 scopus 로고
    • Bell-shaped calcium-response curves of Ins(1,4,5)P3- and calcium-gated channels from endoplasmic reticulum of cerebellum
    • Bezprozvanny I., Watras J., Ehrlich B.E. Bell-shaped calcium-response curves of Ins(1,4,5)P3- and calcium-gated channels from endoplasmic reticulum of cerebellum. Nature 1991, 351:751-754.
    • (1991) Nature , vol.351 , pp. 751-754
    • Bezprozvanny, I.1    Watras, J.2    Ehrlich, B.E.3
  • 138
    • 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., Forte M., d'Azzo A. GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca(2+)-dependent mitochondrial apoptosis. Mol. Cell 2009, 36:500-511.
    • (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    Forte, M.7    d'Azzo, A.8
  • 139
    • 77950284301 scopus 로고    scopus 로고
    • Detergent-resistant microdomains determine the localization of sigma-1 receptors to the endoplasmic reticulum-mitochondria junction
    • Hayashi T., Fujimoto M. Detergent-resistant microdomains determine the localization of sigma-1 receptors to the endoplasmic reticulum-mitochondria junction. Mol. Pharmacol. 2010.
    • (2010) Mol. Pharmacol.
    • Hayashi, T.1    Fujimoto, M.2
  • 140
    • 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 D.T., Resek M.E., Zajchowski L.D., Robbins S.M. 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, 119:3149-3160.
    • (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
  • 141
    • 67449102905 scopus 로고    scopus 로고
    • An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors
    • Pearce M.M., Wormer D.B., Wilkens S., Wojcikiewicz R.J. An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors. J. Biol. Chem. 2009, 284:10433-10445.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10433-10445
    • Pearce, M.M.1    Wormer, D.B.2    Wilkens, S.3    Wojcikiewicz, R.J.4
  • 142
    • 65549153205 scopus 로고    scopus 로고
    • Distinct regions within the erlins are required for oligomerization and association with high molecular weight complexes
    • Hoegg M.B., Browman D.T., Resek M.E., Robbins S.M. Distinct regions within the erlins are required for oligomerization and association with high molecular weight complexes. J. Biol. Chem. 2009, 284:7766-7776.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7766-7776
    • Hoegg, M.B.1    Browman, D.T.2    Resek, M.E.3    Robbins, S.M.4
  • 143
    • 9444226972 scopus 로고    scopus 로고
    • Control of mitochondrial motility and distribution by the calcium signal: a homeostatic circuit
    • Yi M., Weaver D., Hajnoczky G. Control of mitochondrial motility and distribution by the calcium signal: a homeostatic circuit. J. Cell Biol. 2004, 167:661-672.
    • (2004) J. Cell Biol. , vol.167 , pp. 661-672
    • Yi, M.1    Weaver, D.2    Hajnoczky, G.3
  • 145
    • 0030873452 scopus 로고    scopus 로고
    • Energy turnover of vascular endothelial cells
    • Culic O., Gruwel M.L., Schrader J. Energy turnover of vascular endothelial cells. Am. J. Physiol. 1997, 273:C205-C213.
    • (1997) Am. J. Physiol. , vol.273
    • Culic, O.1    Gruwel, M.L.2    Schrader, J.3
  • 146
    • 0033517058 scopus 로고    scopus 로고
    • Regulation of intracellular ATP concentration under conditions of reduced ATP consumption in pancreatic islets
    • Tsuura Y., Fujimoto S., Kajikawa M., Ishida H., Seino Y. Regulation of intracellular ATP concentration under conditions of reduced ATP consumption in pancreatic islets. Biochem. Biophys. Res. Commun. 1999, 261:439-444.
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 439-444
    • Tsuura, Y.1    Fujimoto, S.2    Kajikawa, M.3    Ishida, H.4    Seino, Y.5
  • 147
    • 27744526809 scopus 로고    scopus 로고
    • Role of sarco/endoplasmic reticulum Ca(2+)-ATPase in thermogenesis
    • de Meis L., Arruda A.P., Carvalho D.P. Role of sarco/endoplasmic reticulum Ca(2+)-ATPase in thermogenesis. Biosci. Rep. 2005, 25:181-190.
    • (2005) Biosci. Rep. , vol.25 , pp. 181-190
    • de Meis, L.1    Arruda, A.P.2    Carvalho, D.P.3
  • 148
    • 34247118887 scopus 로고    scopus 로고
    • Signalling to translation: how signal transduction pathways control the protein synthetic machinery
    • Proud C.G. Signalling to translation: how signal transduction pathways control the protein synthetic machinery. Biochem. J. 2007, 403:217-234.
    • (2007) Biochem. J. , vol.403 , pp. 217-234
    • Proud, C.G.1
  • 149
    • 51249111066 scopus 로고    scopus 로고
    • Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein
    • Awe K., Lambert C., Prange R. Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein. FEBS Lett. 2008, 582:3179-3184.
    • (2008) FEBS Lett. , vol.582 , pp. 3179-3184
    • Awe, K.1    Lambert, C.2    Prange, R.3
  • 150
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP
    • McCracken A.A., Brodsky J.L. Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J. Cell Biol. 1996, 132:291-298.
    • (1996) J. Cell Biol. , vol.132 , pp. 291-298
    • McCracken, A.A.1    Brodsky, J.L.2
  • 151
    • 37649025515 scopus 로고    scopus 로고
    • Dissecting the ER-associated degradation of a misfolded polytopic membrane protein
    • Nakatsukasa K., Huyer G., Michaelis S., Brodsky J.L. Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell 2008, 132:101-112.
    • (2008) Cell , vol.132 , pp. 101-112
    • Nakatsukasa, K.1    Huyer, G.2    Michaelis, S.3    Brodsky, J.L.4
  • 152
    • 0029055754 scopus 로고
    • Evidence that phosphatidylserine is imported into mitochondria via a mitochondria-associated membrane and that the majority of mitochondrial phosphatidylethanolamine is derived from decarboxylation of phosphatidylserine
    • Shiao Y.J., Lupo G., Vance J.E. Evidence that phosphatidylserine is imported into mitochondria via a mitochondria-associated membrane and that the majority of mitochondrial phosphatidylethanolamine is derived from decarboxylation of phosphatidylserine. J. Biol. Chem. 1995, 270:11190-11198.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11190-11198
    • Shiao, Y.J.1    Lupo, G.2    Vance, J.E.3
  • 153
    • 0026508087 scopus 로고
    • Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum
    • Braakman I., Helenius J., Helenius A. Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature 1992, 356:260-262.
    • (1992) Nature , vol.356 , pp. 260-262
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 154
    • 67650882756 scopus 로고    scopus 로고
    • An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells
    • Ostrovsky O., Makarewich C.A., Snapp E.L., Argon Y. An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:11600-11605.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 11600-11605
    • Ostrovsky, O.1    Makarewich, C.A.2    Snapp, E.L.3    Argon, Y.4
  • 155
    • 0028235984 scopus 로고
    • Chaperone function of calnexin for the folding intermediate of gp80, the major secretory protein in MDCK cells; regulation by redox state and ATP
    • Wada I., Ou W.-J., Liu M.-C., Scheele G. Chaperone function of calnexin for the folding intermediate of gp80, the major secretory protein in MDCK cells; regulation by redox state and ATP. JBC 1994, 269:7464-7472.
    • (1994) JBC , vol.269 , pp. 7464-7472
    • Wada, I.1    Ou, W.-J.2    Liu, M.-C.3    Scheele, G.4
  • 156
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi Y., Segal M., Normington K., Gething M.J., Sambrook J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 1988, 332:462-464.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 157
    • 0010625474 scopus 로고
    • Glucose depletion accounts for the induction of two transformation-sensitive membrane proteinsin Rous sarcoma virus-transformed chick embryo fibroblasts
    • Shiu R.P., Pouyssegur J., Pastan I. Glucose depletion accounts for the induction of two transformation-sensitive membrane proteinsin Rous sarcoma virus-transformed chick embryo fibroblasts. Proc. Natl. Acad. Sci. U. S. A. 1977, 74:3840-3844.
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 3840-3844
    • Shiu, R.P.1    Pouyssegur, J.2    Pastan, I.3
  • 158
    • 0027958873 scopus 로고
    • The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications
    • Little E., Ramakrishnan M., Roy B., Gazit G., Lee A.S. The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications. Crit. Rev. Eukaryot. Gene Expr. 1994, 4:1-18.
    • (1994) Crit. Rev. Eukaryot. Gene Expr. , vol.4 , pp. 1-18
    • Little, E.1    Ramakrishnan, M.2    Roy, B.3    Gazit, G.4    Lee, A.S.5
  • 159
    • 0001221508 scopus 로고
    • On respiratory impairment in cancer cells
    • Warburg O. On respiratory impairment in cancer cells. Science 1956, 124:269-270.
    • (1956) Science , vol.124 , pp. 269-270
    • Warburg, O.1
  • 160
    • 1342346592 scopus 로고    scopus 로고
    • Mitochondria provide the main source of cytosolic ATP for activation of outward-rectifying K+ channels in mesophyll protoplast of chlorophyll-deficient mutant rice (OsCHLH) seedlings
    • Goh C.H., Jung K.H., Roberts S.K., McAinsh M.R., Hetherington A.M., Park Y.I., Suh K., An G., Nam H.G. Mitochondria provide the main source of cytosolic ATP for activation of outward-rectifying K+ channels in mesophyll protoplast of chlorophyll-deficient mutant rice (OsCHLH) seedlings. J. Biol. Chem. 2004, 279:6874-6882.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6874-6882
    • Goh, C.H.1    Jung, K.H.2    Roberts, S.K.3    McAinsh, M.R.4    Hetherington, A.M.5    Park, Y.I.6    Suh, K.7    An, G.8    Nam, H.G.9
  • 161
    • 0034782848 scopus 로고    scopus 로고
    • Mitochondria are the main ATP source for a cytosolic pool controlling the activity of ATP-sensitive K(+) channels in mouse cardiac myocytes
    • Knopp A., Thierfelder S., Doepner B., Benndorf K. Mitochondria are the main ATP source for a cytosolic pool controlling the activity of ATP-sensitive K(+) channels in mouse cardiac myocytes. Cardiovasc. Res. 2001, 52:236-245.
    • (2001) Cardiovasc. Res. , vol.52 , pp. 236-245
    • Knopp, A.1    Thierfelder, S.2    Doepner, B.3    Benndorf, K.4
  • 162
    • 33749865859 scopus 로고    scopus 로고
    • Nuclear and mitochondrial genome responses in HeLa cells treated with inhibitors of mitochondrial DNA expression
    • Piechota J., Szczesny R., Wolanin K., Chlebowski A., Bartnik E. Nuclear and mitochondrial genome responses in HeLa cells treated with inhibitors of mitochondrial DNA expression. Acta Biochim. Pol. 2006, 53:485-495.
    • (2006) Acta Biochim. Pol. , vol.53 , pp. 485-495
    • Piechota, J.1    Szczesny, R.2    Wolanin, K.3    Chlebowski, A.4    Bartnik, E.5
  • 163
    • 33646806797 scopus 로고    scopus 로고
    • Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum
    • Osibow K., Frank S., Malli R., Zechner R., Graier W.F. Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum. Biochem. J. 2006, 396:173-182.
    • (2006) Biochem. J. , vol.396 , pp. 173-182
    • Osibow, K.1    Frank, S.2    Malli, R.3    Zechner, R.4    Graier, W.F.5
  • 164
    • 0029782625 scopus 로고    scopus 로고
    • Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia
    • Kuznetsov G., Bush K.T., Zhang P.L., Nigam S.K. Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:8584-8589.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 8584-8589
    • Kuznetsov, G.1    Bush, K.T.2    Zhang, P.L.3    Nigam, S.K.4
  • 166
    • 0027472178 scopus 로고
    • An ATP transporter is required for protein translocation into the yeast endoplasmic reticulum
    • Mayinger P., Meyer D.I. An ATP transporter is required for protein translocation into the yeast endoplasmic reticulum. Embo J. 1993, 12:659-666.
    • (1993) Embo J. , vol.12 , pp. 659-666
    • Mayinger, P.1    Meyer, D.I.2
  • 167
    • 0029866372 scopus 로고    scopus 로고
    • Identification of the ATP transporter of rat liver rough endoplasmic reticulum via photoaffinity labeling and partial purification
    • Kim S.H., Shin S.J., Park J.S. Identification of the ATP transporter of rat liver rough endoplasmic reticulum via photoaffinity labeling and partial purification. Biochemistry 1996, 35:5418-5425.
    • (1996) Biochemistry , vol.35 , pp. 5418-5425
    • Kim, S.H.1    Shin, S.J.2    Park, J.S.3
  • 168
    • 0342844281 scopus 로고    scopus 로고
    • Characterization of the ATP transporter in the reconstituted rough endoplasmic reticulum proteoliposomes
    • Shin S.J., Lee W.K., Lim H.W., Park J. Characterization of the ATP transporter in the reconstituted rough endoplasmic reticulum proteoliposomes. Biochim. Biophys. Acta 2000, 1468:55-62.
    • (2000) Biochim. Biophys. Acta , vol.1468 , pp. 55-62
    • Shin, S.J.1    Lee, W.K.2    Lim, H.W.3    Park, J.4
  • 169
    • 0036862532 scopus 로고    scopus 로고
    • The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum
    • Tu B.P., Weissman J.S. The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol. Cell 2002, 10:983-994.
    • (2002) Mol. Cell , vol.10 , pp. 983-994
    • Tu, B.P.1    Weissman, J.S.2
  • 170
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand A.R., Kaiser C.A. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell 1998, 1:161-170.
    • (1998) Mol. Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 171
    • 41449116766 scopus 로고    scopus 로고
    • Ero1 and redox homeostasis in the endoplasmic reticulum
    • Sevier C.S., Kaiser C.A. Ero1 and redox homeostasis in the endoplasmic reticulum. Biochim. Biophys. Acta 2008, 1783:549-556.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 549-556
    • Sevier, C.S.1    Kaiser, C.A.2
  • 173
    • 0034604675 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response
    • Pagani M., Fabbri M., Benedetti C., Fassio A., Pilati S., Bulleid N.J., Cabibbo A., Sitia R. Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J. Biol. Chem. 2000, 275:23685-23692.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23685-23692
    • Pagani, M.1    Fabbri, M.2    Benedetti, C.3    Fassio, A.4    Pilati, S.5    Bulleid, N.J.6    Cabibbo, A.7    Sitia, R.8
  • 176
    • 0034615941 scopus 로고    scopus 로고
    • Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death
    • Tanaka S., Uehara T., Nomura Y. Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death. J. Biol. Chem. 2000, 275:10388-10393.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10388-10393
    • Tanaka, S.1    Uehara, T.2    Nomura, Y.3
  • 177
    • 13944276380 scopus 로고    scopus 로고
    • Ero1-L alpha plays a key role in a HIF-1-mediated pathway to improve disulfide bond formation and VEGF secretion under hypoxia: implication for cancer
    • May D., Itin A., Gal O., Kalinski H., Feinstein E., Keshet E. Ero1-L alpha plays a key role in a HIF-1-mediated pathway to improve disulfide bond formation and VEGF secretion under hypoxia: implication for cancer. Oncogene 2005, 24:1011-1020.
    • (2005) Oncogene , vol.24 , pp. 1011-1020
    • May, D.1    Itin, A.2    Gal, O.3    Kalinski, H.4    Feinstein, E.5    Keshet, E.6
  • 178
    • 77953703354 scopus 로고    scopus 로고
    • Redox state of the endoplasmic reticulum is controlled by ERO1L-ALPHA and intraluminal calcium
    • Enyedi B., Varnai P., Geiszt M. Redox state of the endoplasmic reticulum is controlled by ERO1L-ALPHA and intraluminal calcium. Antioxid. Redox Signal. 2010.
    • (2010) Antioxid. Redox Signal.
    • Enyedi, B.1    Varnai, P.2    Geiszt, M.3
  • 179
    • 70349352744 scopus 로고    scopus 로고
    • Mechanisms and implications of reactive oxygen species generation during the unfolded protein response: roles of endoplasmic reticulum oxidoreductases, mitochondrial electron transport, and NADPH oxidase
    • Santos C.X., Tanaka L.Y., Wosniak J., Laurindo F.R. Mechanisms and implications of reactive oxygen species generation during the unfolded protein response: roles of endoplasmic reticulum oxidoreductases, mitochondrial electron transport, and NADPH oxidase. Antioxid. Redox Signal. 2009, 11:2409-2427.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2409-2427
    • Santos, C.X.1    Tanaka, L.Y.2    Wosniak, J.3    Laurindo, F.R.4
  • 181
  • 183
    • 0034717179 scopus 로고    scopus 로고
    • NADPH oxidase activation increases the sensitivity of intracellular Ca2+ stores to inositol 1,4,5-trisphosphate in human endothelial cells
    • Hu Q., Zheng G., Zweier J.L., Deshpande S., Irani K., Ziegelstein R.C. NADPH oxidase activation increases the sensitivity of intracellular Ca2+ stores to inositol 1,4,5-trisphosphate in human endothelial cells. J. Biol. Chem. 2000, 275:15749-15757.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15749-15757
    • Hu, Q.1    Zheng, G.2    Zweier, J.L.3    Deshpande, S.4    Irani, K.5    Ziegelstein, R.C.6
  • 184
    • 14244263683 scopus 로고    scopus 로고
    • H2O2-induced changes in mitochondrial activity in isolated mouse pancreatic acinar cells
    • Gonzalez A., Granados M.P., Salido G.M., Pariente J.A. H2O2-induced changes in mitochondrial activity in isolated mouse pancreatic acinar cells. Mol. Cell. Biochem. 2005, 269:165-173.
    • (2005) Mol. Cell. Biochem. , vol.269 , pp. 165-173
    • Gonzalez, A.1    Granados, M.P.2    Salido, G.M.3    Pariente, J.A.4
  • 185
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R., Tabas I. Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J. Cell Biol. 2009, 186:783-792.
    • (2009) J. Cell Biol. , vol.186 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6    Tabas, I.7
  • 186
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu B.P., Ho-Schleyer S.C., Travers K.J., Weissman J.S. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 2000, 290:1571-1574.
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 189
    • 0030721976 scopus 로고    scopus 로고
    • Flavin adenine dinucleotide and flavin mononucleotide metabolism in rat liver-the occurrence of FAD pyrophosphatase and FMN phosphohydrolase in isolated mitochondria
    • Barile M., Brizio C., De Virgilio C., Delfine S., Quagliariello E., Passarella S. Flavin adenine dinucleotide and flavin mononucleotide metabolism in rat liver-the occurrence of FAD pyrophosphatase and FMN phosphohydrolase in isolated mitochondria. Eur. J. Biochem. 1997, 249:777-785.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 777-785
    • Barile, M.1    Brizio, C.2    De Virgilio, C.3    Delfine, S.4    Quagliariello, E.5    Passarella, S.6
  • 190
    • 33746356213 scopus 로고    scopus 로고
    • A screen for genes of heme uptake identifies the FLC family required for import of FAD into the endoplasmic reticulum
    • Protchenko O., Rodriguez-Suarez R., Androphy R., Bussey H., Philpott C.C. A screen for genes of heme uptake identifies the FLC family required for import of FAD into the endoplasmic reticulum. J. Biol. Chem. 2006, 281:21445-21457.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21445-21457
    • Protchenko, O.1    Rodriguez-Suarez, R.2    Androphy, R.3    Bussey, H.4    Philpott, C.C.5
  • 192
    • 33749986033 scopus 로고    scopus 로고
    • Mitochondrial function and toxicity: role of the B vitamin family on mitochondrial energy metabolism
    • Depeint F., Bruce W.R., Shangari N., Mehta R., O'Brien P.J. Mitochondrial function and toxicity: role of the B vitamin family on mitochondrial energy metabolism. Chem. Biol. Interact. 2006, 163:94-112.
    • (2006) Chem. Biol. Interact. , vol.163 , pp. 94-112
    • Depeint, F.1    Bruce, W.R.2    Shangari, N.3    Mehta, R.4    O'Brien, P.J.5
  • 193
    • 18344362133 scopus 로고    scopus 로고
    • Riboflavin deficiency impairs oxidative folding and secretion of apolipoprotein B-100 in HepG2 cells, triggering stress response systems
    • Manthey K.C., Chew Y.C., Zempleni J. Riboflavin deficiency impairs oxidative folding and secretion of apolipoprotein B-100 in HepG2 cells, triggering stress response systems. J. Nutr. 2005, 135:978-982.
    • (2005) J. Nutr. , vol.135 , pp. 978-982
    • Manthey, K.C.1    Chew, Y.C.2    Zempleni, J.3
  • 194
    • 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., Tanzawa H. Sarcoendoplasmic reticulum Ca(2+) ATPase type 2 downregulated in human oral squamous cell carcinoma. Int. J. Cancer 2004, 110:225-231.
    • (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    Tanzawa, H.7
  • 195
    • 25444503742 scopus 로고    scopus 로고
    • Haploinsufficiency of Atp2a2, encoding the sarco(endo)plasmic reticulum Ca2+-ATPase isoform 2 Ca2+ pump, predisposes mice to squamous cell tumors via a novel mode of cancer susceptibility
    • Prasad V., Boivin G.P., Miller M.L., Liu L.H., Erwin C.R., Warner B.W., Shull G.E. Haploinsufficiency of Atp2a2, encoding the sarco(endo)plasmic reticulum Ca2+-ATPase isoform 2 Ca2+ pump, predisposes mice to squamous cell tumors via a novel mode of cancer susceptibility. Cancer Res. 2005, 65:8655-8661.
    • (2005) Cancer Res. , vol.65 , pp. 8655-8661
    • Prasad, V.1    Boivin, G.P.2    Miller, M.L.3    Liu, L.H.4    Erwin, C.R.5    Warner, B.W.6    Shull, G.E.7
  • 196
    • 0035920215 scopus 로고    scopus 로고
    • Squamous cell tumors in mice heterozygous for a null allele of Atp2a2, encoding the sarco(endo)plasmic reticulum Ca2+-ATPase isoform 2 Ca2+ pump
    • Liu L.H., Boivin G.P., Prasad V., Periasamy M., Shull G.E. Squamous cell tumors in mice heterozygous for a null allele of Atp2a2, encoding the sarco(endo)plasmic reticulum Ca2+-ATPase isoform 2 Ca2+ pump. J. Biol. Chem. 2001, 276:26737-26740.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26737-26740
    • Liu, L.H.1    Boivin, G.P.2    Prasad, V.3    Periasamy, M.4    Shull, G.E.5
  • 197
    • 33749343263 scopus 로고    scopus 로고
    • The expression and functional characterization of sigma (sigma) 1 receptors in breast cancer cell lines
    • Aydar E., Onganer P., Perrett R., Djamgoz M.B., Palmer C.P. The expression and functional characterization of sigma (sigma) 1 receptors in breast cancer cell lines. Cancer Lett. 2006, 242:245-257.
    • (2006) Cancer Lett. , vol.242 , pp. 245-257
    • Aydar, E.1    Onganer, P.2    Perrett, R.3    Djamgoz, M.B.4    Palmer, C.P.5
  • 199
    • 0347985694 scopus 로고    scopus 로고
    • Differential downregulation of endoplasmic reticulum-residing chaperones calnexin and calreticulin in human metastatic melanoma
    • Dissemond J., Busch M., Kothen T., Mors J., Weimann T.K., Lindeke A., Goos M., Wagner S.N. Differential downregulation of endoplasmic reticulum-residing chaperones calnexin and calreticulin in human metastatic melanoma. Cancer Lett. 2004, 203:225-231.
    • (2004) Cancer Lett. , vol.203 , pp. 225-231
    • Dissemond, J.1    Busch, M.2    Kothen, T.3    Mors, J.4    Weimann, T.K.5    Lindeke, A.6    Goos, M.7    Wagner, S.N.8


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