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Volumn 358, Issue 1, 2015, Pages 47-58

Mitofusin-2 triggers mitochondria Ca2+ influx from the endoplasmic reticulum to induce apoptosis in hepatocellular carcinoma cells

Author keywords

Heparin; InsP3R; Mitochondrial Ca2+ uniporter; Mitochondrial calcium uptake 2; Mitochondrial calcium uptake1; RU360

Indexed keywords

CALCIUM ION; CASPASE 3; CELL PROTEIN; CYTOCHROME C; INOSITOL TRISPHOSPHATE RECEPTOR; MITOCHONDRIAL CALCIUM UNIPORTER PROTEIN; MITOCHONDRIAL CALCIUM UPTAKE 1 PROTEIN; MITOCHONDRIAL CALCIUM UPTAKE 2 PROTEIN; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; MITOFUSIN 2; PROTEIN BAX; REACTIVE OXYGEN METABOLITE; RECEPTOR; UNCLASSIFIED DRUG; CALCIUM; GUANOSINE TRIPHOSPHATASE; HEPARIN; MFN2 PROTEIN, HUMAN; MITOCHONDRIAL PROTEIN; RU 360; RUTHENIUM DERIVATIVE;

EID: 84921311702     PISSN: 03043835     EISSN: 18727980     Source Type: Journal    
DOI: 10.1016/j.canlet.2014.12.025     Document Type: Article
Times cited : (100)

References (64)
  • 1
    • 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(2):189-200.
    • (2003) J. Cell Biol , vol.160 , Issue.2 , 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
  • 2
    • 33845877961 scopus 로고    scopus 로고
    • Identification of a novel protein that regulates mitochondrial fusion by modulating mitofusin (Mfn) protein function
    • Eura Y., Ishihara N., Oka T., Mihara K. Identification of a novel protein that regulates mitochondrial fusion by modulating mitofusin (Mfn) protein function. J. Cell Sci 2006, 119(Pt 23):4913-4925.
    • (2006) J. Cell Sci , vol.119 , pp. 4913-4925
    • Eura, Y.1    Ishihara, N.2    Oka, T.3    Mihara, K.4
  • 3
    • 4444270915 scopus 로고    scopus 로고
    • Dysregulation of HSG triggers vascular proliferative disorders
    • Chen K.H., Guo X., Ma D., et al. Dysregulation of HSG triggers vascular proliferative disorders. Nat. Cell Biol 2004, 6(9):872-883.
    • (2004) Nat. Cell Biol , vol.6 , Issue.9 , pp. 872-883
    • Chen, K.H.1    Guo, X.2    Ma, D.3
  • 4
    • 36348989007 scopus 로고    scopus 로고
    • Mitofusin 2 triggers vascular smooth muscle cell apoptosis via mitochondrial death pathway
    • Guo X., Chen K.H., Guo Y., Liao H., Tang J., Xiao R.P. Mitofusin 2 triggers vascular smooth muscle cell apoptosis via mitochondrial death pathway. Circ. Res 2007, 101(11):1113-1122.
    • (2007) Circ. Res , vol.101 , Issue.11 , pp. 1113-1122
    • Guo, X.1    Chen, K.H.2    Guo, Y.3    Liao, H.4    Tang, J.5    Xiao, R.P.6
  • 5
    • 0037164813 scopus 로고    scopus 로고
    • Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis
    • Karbowski M., Lee Y.J., Gaume B., et al. Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis. J. Cell Biol 2002, 159(6):931-938.
    • (2002) J. Cell Biol , vol.159 , Issue.6 , pp. 931-938
    • Karbowski, M.1    Lee, Y.J.2    Gaume, B.3
  • 7
    • 34547442346 scopus 로고    scopus 로고
    • Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins
    • Brooks C., Wei Q., Feng L., et al. Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins. Proc. Natl. Acad. Sci. U.S.A. 2007, 104(28):11649-11654.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , Issue.28 , pp. 11649-11654
    • Brooks, C.1    Wei, Q.2    Feng, L.3
  • 8
    • 34249695489 scopus 로고    scopus 로고
    • Mitochondrial clustering induced by overexpression of the mitochondrial fusion protein Mfn2 causes mitochondrial dysfunction and cell death
    • Huang P., Yu T., Yoon Y. Mitochondrial clustering induced by overexpression of the mitochondrial fusion protein Mfn2 causes mitochondrial dysfunction and cell death. Eur. J. Cell Biol 2007, 86(6):289-302.
    • (2007) Eur. J. Cell Biol , vol.86 , Issue.6 , pp. 289-302
    • Huang, P.1    Yu, T.2    Yoon, Y.3
  • 9
    • 77952980581 scopus 로고    scopus 로고
    • HSG provides antitumor efficacy on hepatocellular carcinoma both in vitro and in vivo
    • Wang W., Zhu F., Wang S., et al. HSG provides antitumor efficacy on hepatocellular carcinoma both in vitro and in vivo. Oncol. Rep 2010, 24(1):183-188.
    • (2010) Oncol. Rep , vol.24 , Issue.1 , pp. 183-188
    • Wang, W.1    Zhu, F.2    Wang, S.3
  • 10
    • 84860462092 scopus 로고    scopus 로고
    • Pro-apoptotic and anti-proliferative effects of mitofusin-2 via Bax signaling in hepatocellular carcinoma cells
    • Wang W., Lu J., Zhu F., et al. Pro-apoptotic and anti-proliferative effects of mitofusin-2 via Bax signaling in hepatocellular carcinoma cells. Med. Oncol 2012, 29(1):70-76.
    • (2012) Med. Oncol , vol.29 , Issue.1 , pp. 70-76
    • Wang, W.1    Lu, J.2    Zhu, F.3
  • 11
    • 0033598828 scopus 로고    scopus 로고
    • Regulation of mitochondrial ATP synthesis by calcium: evidence for a long-term metabolic priming
    • Jouaville L.S., Pinton P., Bastianutto C., Rutter G.A., Rizzuto R. Regulation of mitochondrial ATP synthesis by calcium: evidence for a long-term metabolic priming. Proc. Natl. Acad. Sci. U.S.A. 1999, 96(24):13807-13812.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , Issue.24 , pp. 13807-13812
    • Jouaville, L.S.1    Pinton, P.2    Bastianutto, C.3    Rutter, G.A.4    Rizzuto, R.5
  • 13
    • 0034304906 scopus 로고    scopus 로고
    • The versatility and universality of calcium signalling
    • Berridge M.J., Lipp P., Bootman M.D. The versatility and universality of calcium signalling. Nat. Rev. Mol. Cell Biol 2000, 1(1):11-21.
    • (2000) Nat. Rev. Mol. Cell Biol , vol.1 , Issue.1 , pp. 11-21
    • Berridge, M.J.1    Lipp, P.2    Bootman, M.D.3
  • 15
    • 0346880483 scopus 로고    scopus 로고
    • Calcium and apoptosis: facts and hypotheses
    • Rizzuto R., Pinton P., Ferrari D., et al. Calcium and apoptosis: facts and hypotheses. Oncogene 2003, 22(53):8619-8627.
    • (2003) Oncogene , vol.22 , Issue.53 , pp. 8619-8627
    • Rizzuto, R.1    Pinton, P.2    Ferrari, D.3
  • 16
    • 0033044376 scopus 로고    scopus 로고
    • Assessment and validation of a microinjection method for kinetic analysis of [Ca2+]i in individual cells undergoing apoptosis
    • Tombal B., Denmeade S.R., Isaacs J.T. Assessment and validation of a microinjection method for kinetic analysis of [Ca2+]i in individual cells undergoing apoptosis. Cell Calcium 1999, 25(1):19-28.
    • (1999) Cell Calcium , vol.25 , Issue.1 , pp. 19-28
    • Tombal, B.1    Denmeade, S.R.2    Isaacs, J.T.3
  • 17
    • 0033711955 scopus 로고    scopus 로고
    • Basic fibroblast growth factor inhibits apoptosis of spontaneously immortalized granulosa cells by regulating intracellular free calcium levels through a protein kinase Cdelta-dependent pathway
    • Lynch K., Fernandez G., Pappalardo A., Peluso J.J. Basic fibroblast growth factor inhibits apoptosis of spontaneously immortalized granulosa cells by regulating intracellular free calcium levels through a protein kinase Cdelta-dependent pathway. Endocrinology 2000, 141(11):4209-4217.
    • (2000) Endocrinology , vol.141 , Issue.11 , pp. 4209-4217
    • Lynch, K.1    Fernandez, G.2    Pappalardo, A.3    Peluso, J.J.4
  • 18
    • 42049090126 scopus 로고    scopus 로고
    • Mitochondria: the hub of cellular Ca2+ signaling
    • Szabadkai G., Duchen M.R. Mitochondria: the hub of cellular Ca2+ signaling. Physiology (Bethesda) 2008, 23:84-94.
    • (2008) Physiology (Bethesda) , vol.23 , pp. 84-94
    • Szabadkai, G.1    Duchen, M.R.2
  • 19
    • 57649245238 scopus 로고    scopus 로고
    • Mitofusin 2 builds a bridge between ER and mitochondria
    • Merkwirth C., Langer T. Mitofusin 2 builds a bridge between ER and mitochondria. Cell 2008, 135(7):1165-1167.
    • (2008) Cell , vol.135 , Issue.7 , pp. 1165-1167
    • Merkwirth, C.1    Langer, T.2
  • 20
    • 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(7222):605-610.
    • (2008) Nature , vol.456 , Issue.7222 , pp. 605-610
    • de Brito, O.M.1    Scorrano, L.2
  • 21
    • 0035355341 scopus 로고    scopus 로고
    • The Ca2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: significance for the molecular mechanism of Bcl-2 action
    • Pinton P., Ferrari D., Rapizzi E., Di Virgilio F., Pozzan T., Rizzuto R. The Ca2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: significance for the molecular mechanism of Bcl-2 action. EMBO J. 2001, 20(11):2690-2701.
    • (2001) EMBO J. , vol.20 , Issue.11 , pp. 2690-2701
    • Pinton, P.1    Ferrari, D.2    Rapizzi, E.3    Di Virgilio, F.4    Pozzan, T.5    Rizzuto, R.6
  • 22
    • 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(22):6349-6361.
    • (1999) EMBO J. , vol.18 , Issue.22 , pp. 6349-6361
    • Szalai, G.1    Krishnamurthy, R.2    Hajnoczky, G.3
  • 23
    • 0001081063 scopus 로고
    • Ca ion uptake by rat kidney mitochondria and its dependence on respiration and phosphorylation
    • Vasington F.D., Murphy J.V. Ca ion uptake by rat kidney mitochondria and its dependence on respiration and phosphorylation. J. Biol. Chem 1962, 237:2670-2677.
    • (1962) J. Biol. Chem , vol.237 , pp. 2670-2677
    • Vasington, F.D.1    Murphy, J.V.2
  • 24
    • 80051946060 scopus 로고    scopus 로고
    • Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter
    • Baughman J.M., Perocchi F., Girgis H.S., et al. Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter. Nature 2011, 476(7360):341-345.
    • (2011) Nature , vol.476 , Issue.7360 , pp. 341-345
    • Baughman, J.M.1    Perocchi, F.2    Girgis, H.S.3
  • 25
    • 80051936634 scopus 로고    scopus 로고
    • A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
    • De Stefani D., Raffaello A., Teardo E., Szabo I., Rizzuto R. A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter. Nature 2011, 476(7360):336-340.
    • (2011) Nature , vol.476 , Issue.7360 , pp. 336-340
    • De Stefani, D.1    Raffaello, A.2    Teardo, E.3    Szabo, I.4    Rizzuto, R.5
  • 26
    • 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(6972):360-364.
    • (2004) Nature , vol.427 , Issue.6972 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 27
    • 84878796986 scopus 로고    scopus 로고
    • MICU1 controls both the threshold and cooperative activation of the mitochondrial Ca(2)(+) uniporter
    • Csordas G., Golenar T., Seifert E.L., et al. MICU1 controls both the threshold and cooperative activation of the mitochondrial Ca(2)(+) uniporter. Cell Metab 2013, 17(6):976-987.
    • (2013) Cell Metab , vol.17 , Issue.6 , pp. 976-987
    • Csordas, G.1    Golenar, T.2    Seifert, E.L.3
  • 28
    • 84868027665 scopus 로고    scopus 로고
    • MICU1 is an essential gatekeeper for MCU-mediated mitochondrial Ca(2+) uptake that regulates cell survival
    • Mallilankaraman K., Doonan P., Cardenas C., et al. MICU1 is an essential gatekeeper for MCU-mediated mitochondrial Ca(2+) uptake that regulates cell survival. Cell 2012, 151(3):630-644.
    • (2012) Cell , vol.151 , Issue.3 , pp. 630-644
    • Mallilankaraman, K.1    Doonan, P.2    Cardenas, C.3
  • 29
    • 84898665862 scopus 로고    scopus 로고
    • The gatekeepers of mitochondrial calcium influx: MICU1 and MICU2
    • Ahuja M., Muallem S. The gatekeepers of mitochondrial calcium influx: MICU1 and MICU2. EMBO Rep 2014, 15(3):205-206.
    • (2014) EMBO Rep , vol.15 , Issue.3 , pp. 205-206
    • Ahuja, M.1    Muallem, S.2
  • 30
    • 78049509833 scopus 로고    scopus 로고
    • BAG3 protein delocalisation in prostate carcinoma
    • Staibano S., Mascolo M., Di Benedetto M., et al. BAG3 protein delocalisation in prostate carcinoma. Tumour Biol 2010, 31(5):461-469.
    • (2010) Tumour Biol , vol.31 , Issue.5 , pp. 461-469
    • Staibano, S.1    Mascolo, M.2    Di Benedetto, M.3
  • 31
    • 0032562816 scopus 로고    scopus 로고
    • Oxygen-bridged dinuclear ruthenium amine complex specifically inhibits Ca2+ uptake into mitochondria in vitro and in situ in single cardiac myocytes
    • Matlib M.A., Zhou Z., Knight S., et al. Oxygen-bridged dinuclear ruthenium amine complex specifically inhibits Ca2+ uptake into mitochondria in vitro and in situ in single cardiac myocytes. J. Biol. Chem 1998, 273(17):10223-10231.
    • (1998) J. Biol. Chem , vol.273 , Issue.17 , pp. 10223-10231
    • Matlib, M.A.1    Zhou, Z.2    Knight, S.3
  • 32
    • 0028925051 scopus 로고
    • Heparin-insensitive calcium release from intracellular stores triggered by the recombinant human parathyroid hormone receptor
    • Seuwen K., Boddeke H.G. Heparin-insensitive calcium release from intracellular stores triggered by the recombinant human parathyroid hormone receptor. Br. J. Pharmacol 1995, 114(8):1613-1620.
    • (1995) Br. J. Pharmacol , vol.114 , Issue.8 , pp. 1613-1620
    • Seuwen, K.1    Boddeke, H.G.2
  • 33
    • 0242663915 scopus 로고    scopus 로고
    • T cell activation-induced mitochondrial hyperpolarization is mediated by Ca2+- and redox-dependent production of nitric oxide
    • Nagy G., Koncz A., Perl A. T cell activation-induced mitochondrial hyperpolarization is mediated by Ca2+- and redox-dependent production of nitric oxide. J. Immunol 2003, 171(10):5188-5197.
    • (2003) J. Immunol , vol.171 , Issue.10 , pp. 5188-5197
    • Nagy, G.1    Koncz, A.2    Perl, A.3
  • 34
    • 84895732943 scopus 로고    scopus 로고
    • Fus1/Tusc2 is a novel regulator of mitochondrial calcium handling, Ca2+-coupled mitochondrial processes, and Ca2+-dependent NFAT and NF-kappaB pathways in CD4+ T cells
    • Uzhachenko R., Ivanov S.V., Yarbrough W.G., Shanker A., Medzhitov R., Ivanova A.V. Fus1/Tusc2 is a novel regulator of mitochondrial calcium handling, Ca2+-coupled mitochondrial processes, and Ca2+-dependent NFAT and NF-kappaB pathways in CD4+ T cells. Antioxid. Redox Signal 2014, 20(10):1533-1547.
    • (2014) Antioxid. Redox Signal , vol.20 , Issue.10 , pp. 1533-1547
    • Uzhachenko, R.1    Ivanov, S.V.2    Yarbrough, W.G.3    Shanker, A.4    Medzhitov, R.5    Ivanova, A.V.6
  • 35
    • 38349194472 scopus 로고    scopus 로고
    • Cell death in health and disease
    • Lockshin R.A., Zakeri Z. Cell death in health and disease. J. Cell. Mol. Med 2007, 11(6):1214-1224.
    • (2007) J. Cell. Mol. Med , vol.11 , Issue.6 , pp. 1214-1224
    • Lockshin, R.A.1    Zakeri, Z.2
  • 36
    • 0029899181 scopus 로고    scopus 로고
    • Molecular thanatopsis: a discourse on the BCL2 family and cell death
    • Yang E., Korsmeyer S.J. Molecular thanatopsis: a discourse on the BCL2 family and cell death. Blood 1996, 88(2):386-401.
    • (1996) Blood , vol.88 , Issue.2 , pp. 386-401
    • Yang, E.1    Korsmeyer, S.J.2
  • 37
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: the next generation
    • Hanahan D., Weinberg R.A. Hallmarks of cancer: the next generation. Cell 2011, 144(5):646-674.
    • (2011) Cell , vol.144 , Issue.5 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 38
    • 58149296552 scopus 로고    scopus 로고
    • Tumor resistance to apoptosis
    • Fulda S. Tumor resistance to apoptosis. Int. J. Cancer 2009, 124(3):511-515.
    • (2009) Int. J. Cancer , vol.124 , Issue.3 , pp. 511-515
    • Fulda, S.1
  • 39
    • 4544340539 scopus 로고    scopus 로고
    • Antiapoptotic BCL-2 is required for maintenance of a model leukemia
    • Letai A., Sorcinelli M.D., Beard C., Korsmeyer S.J. Antiapoptotic BCL-2 is required for maintenance of a model leukemia. Cancer Cell 2004, 6(3):241-249.
    • (2004) Cancer Cell , vol.6 , Issue.3 , pp. 241-249
    • Letai, A.1    Sorcinelli, M.D.2    Beard, C.3    Korsmeyer, S.J.4
  • 40
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c
    • Liu X., Kim C.N., Yang J., Jemmerson R., Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 1996, 86(1):147-157.
    • (1996) Cell , vol.86 , Issue.1 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 41
    • 0030741528 scopus 로고    scopus 로고
    • Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system
    • Kluck R.M., Martin S.J., Hoffman B.M., Zhou J.S., Green D.R., Newmeyer D.D. Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system. EMBO J. 1997, 16(15):4639-4649.
    • (1997) EMBO J. , vol.16 , Issue.15 , pp. 4639-4649
    • Kluck, R.M.1    Martin, S.J.2    Hoffman, B.M.3    Zhou, J.S.4    Green, D.R.5    Newmeyer, D.D.6
  • 42
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C., Fang M., Li Y., Li L., Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000, 102(1):33-42.
    • (2000) Cell , vol.102 , Issue.1 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 43
    • 0038722727 scopus 로고    scopus 로고
    • Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosis
    • Yang Q.H., Church-Hajduk R., Ren J., Newton M.L., Du C. Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosis. Genes Dev 2003, 17(12):1487-1496.
    • (2003) Genes Dev , vol.17 , Issue.12 , pp. 1487-1496
    • Yang, Q.H.1    Church-Hajduk, R.2    Ren, J.3    Newton, M.L.4    Du, C.5
  • 44
    • 0037562009 scopus 로고    scopus 로고
    • Characterization of a novel and specific inhibitor for the pro-apoptotic protease Omi/HtrA2
    • Cilenti L., Lee Y., Hess S., et al. Characterization of a novel and specific inhibitor for the pro-apoptotic protease Omi/HtrA2. J. Biol. Chem 2003, 278(13):11489-11494.
    • (2003) J. Biol. Chem , vol.278 , Issue.13 , pp. 11489-11494
    • Cilenti, L.1    Lee, Y.2    Hess, S.3
  • 45
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis
    • Kluck R.M., Bossy-Wetzel E., Green D.R., Newmeyer D.D. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 1997, 275(5303):1132-1136.
    • (1997) Science , vol.275 , Issue.5303 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 46
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked
    • Yang J., Liu X., Bhalla K., et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 1997, 275(5303):1129-1132.
    • (1997) Science , vol.275 , Issue.5303 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 48
    • 78149449341 scopus 로고    scopus 로고
    • BH3-triggered structural reorganization drives the activation of proapoptotic BAX
    • Gavathiotis E., Reyna D.E., Davis M.L., Bird G.H., Walensky L.D. BH3-triggered structural reorganization drives the activation of proapoptotic BAX. Mol. Cell 2010, 40(3):481-492.
    • (2010) Mol. Cell , vol.40 , Issue.3 , pp. 481-492
    • Gavathiotis, E.1    Reyna, D.E.2    Davis, M.L.3    Bird, G.H.4    Walensky, L.D.5
  • 49
    • 84879679314 scopus 로고    scopus 로고
    • Three-dimensional structure of Bax-mediated pores in membrane bilayers
    • Xu X.P., Zhai D., Kim E., et al. Three-dimensional structure of Bax-mediated pores in membrane bilayers. Cell Death Dis 2013, 4:e683.
    • (2013) Cell Death Dis , vol.4 , pp. e683
    • Xu, X.P.1    Zhai, D.2    Kim, E.3
  • 50
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M., Shimizu S., Ito T., et al. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc. Natl. Acad. Sci. U.S.A. 1998, 95(25):14681-14686.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , Issue.25 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3
  • 51
    • 33646255246 scopus 로고    scopus 로고
    • The mitochondrial permeability transition from in vitro artifact to disease target
    • Bernardi P., Krauskopf A., Basso E., et al. The mitochondrial permeability transition from in vitro artifact to disease target. FEBS J. 2006, 273(10):2077-2099.
    • (2006) FEBS J. , vol.273 , Issue.10 , pp. 2077-2099
    • Bernardi, P.1    Krauskopf, A.2    Basso, E.3
  • 52
    • 78049474352 scopus 로고    scopus 로고
    • Reactive oxygen species and antioxidant machinery in abiotic stress tolerance in crop plants
    • Gill S.S., Tuteja N. Reactive oxygen species and antioxidant machinery in abiotic stress tolerance in crop plants. Plant Physiol. Biochem 2010, 48(12):909-930.
    • (2010) Plant Physiol. Biochem , vol.48 , Issue.12 , pp. 909-930
    • Gill, S.S.1    Tuteja, N.2
  • 53
    • 0028348251 scopus 로고
    • Complementation of mutant and wild-type human mitochondrial DNAs coexisting since the mutation event and lack of complementation of DNAs introduced separately into a cell within distinct organelles
    • Yoneda M., Miyatake T., Attardi G. Complementation of mutant and wild-type human mitochondrial DNAs coexisting since the mutation event and lack of complementation of DNAs introduced separately into a cell within distinct organelles. Mol. Cell. Biol 1994, 14(4):2699-2712.
    • (1994) Mol. Cell. Biol , vol.14 , Issue.4 , pp. 2699-2712
    • Yoneda, M.1    Miyatake, T.2    Attardi, G.3
  • 54
  • 55
    • 68649092333 scopus 로고    scopus 로고
    • The role of Ca(2+) signaling in the coordination of mitochondrial ATP production with cardiac work
    • Balaban R.S. The role of Ca(2+) signaling in the coordination of mitochondrial ATP production with cardiac work. Biochim. Biophys. Acta 2009, 1787(11):1334-1341.
    • (2009) Biochim. Biophys. Acta , vol.1787 , Issue.11 , pp. 1334-1341
    • Balaban, R.S.1
  • 56
    • 38849119213 scopus 로고    scopus 로고
    • Calcium and cell death: the mitochondrial connection
    • Bernardi P., Rasola A. Calcium and cell death: the mitochondrial connection. Subcell Biochem 2007, 45:481-506.
    • (2007) Subcell Biochem , vol.45 , pp. 481-506
    • Bernardi, P.1    Rasola, A.2
  • 57
    • 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(5134):744-747.
    • (1993) Science , vol.262 , Issue.5134 , pp. 744-747
    • Rizzuto, R.1    Brini, M.2    Murgia, M.3    Pozzan, T.4
  • 58
    • 0032511112 scopus 로고    scopus 로고
    • Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses
    • Rizzuto R., Pinton P., Carrington W., et al. Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses. Science 1998, 280(5370):1763-1766.
    • (1998) Science , vol.280 , Issue.5370 , pp. 1763-1766
    • Rizzuto, R.1    Pinton, P.2    Carrington, W.3
  • 59
    • 77954301751 scopus 로고    scopus 로고
    • Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface
    • Csordas G., Varnai P., Golenar T., et al. Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface. Mol. Cell 2010, 39(1):121-132.
    • (2010) Mol. Cell , vol.39 , Issue.1 , pp. 121-132
    • Csordas, G.1    Varnai, P.2    Golenar, T.3
  • 60
    • 77950888855 scopus 로고    scopus 로고
    • Ca2+ hot spots on the mitochondrial surface are generated by Ca2+ mobilization from stores, but not by activation of store-operated Ca2+ channels
    • Giacomello M., Drago I., Bortolozzi M., et al. Ca2+ hot spots on the mitochondrial surface are generated by Ca2+ mobilization from stores, but not by activation of store-operated Ca2+ channels. Mol. Cell 2010, 38(2):280-290.
    • (2010) Mol. Cell , vol.38 , Issue.2 , pp. 280-290
    • Giacomello, M.1    Drago, I.2    Bortolozzi, M.3
  • 61
    • 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., et al. Structural and functional features and significance of the physical linkage between ER and mitochondria. J. Cell Biol 2006, 174(7):915-921.
    • (2006) J. Cell Biol , vol.174 , Issue.7 , pp. 915-921
    • Csordas, G.1    Renken, C.2    Varnai, P.3
  • 62
    • 24644462789 scopus 로고    scopus 로고
    • Mitochondria and calcium signaling
    • Nicholls D.G. Mitochondria and calcium signaling. Cell Calcium 2005, 38(3-4):311-317.
    • (2005) Cell Calcium , vol.38 , Issue.3-4 , pp. 311-317
    • Nicholls, D.G.1
  • 63
    • 77956928316 scopus 로고    scopus 로고
    • MICU1 encodes a mitochondrial EF hand protein required for Ca(2+) uptake
    • Perocchi F., Gohil V.M., Girgis H.S., et al. MICU1 encodes a mitochondrial EF hand protein required for Ca(2+) uptake. Nature 2010, 467(7313):291-296.
    • (2010) Nature , vol.467 , Issue.7313 , pp. 291-296
    • Perocchi, F.1    Gohil, V.M.2    Girgis, H.S.3
  • 64
    • 84896703008 scopus 로고    scopus 로고
    • MICU1 and MICU2 finely tune the mitochondrial Ca2+ uniporter by exerting opposite effects on MCU activity
    • Patron M., Checchetto V., Raffaello A., et al. MICU1 and MICU2 finely tune the mitochondrial Ca2+ uniporter by exerting opposite effects on MCU activity. Mol. Cell 2014, 53(5):726-737.
    • (2014) Mol. Cell , vol.53 , Issue.5 , pp. 726-737
    • Patron, M.1    Checchetto, V.2    Raffaello, A.3


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