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Volumn 9, Issue , 2011, Pages

Calcium signaling around Mitochondria Associated Membranes (MAMs)

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM CHANNEL; CALCIUM ION; CALMODULIN; CARRIER PROTEIN; DIACYLGLYCEROL; GLUCOSE REGULATED PROTEIN 78; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; INOSITOL 1,4,5 TRISPHOSPHATE; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; LEUCINE ZIPPER EF HAND CONTAINING TRANSMEMBRANE PROTEIN 1; MEMBRANE PROTEIN; MITOCHONDRIAL CALCIUM UNIPORTER; MITOFUSIN 1; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE C; PHOSPHOPROTEIN PHOSPHATASE 2; PLASMA MEMBRANE CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN CCDC109A; PROTEIN NCKX6; PROTEIN NCLX; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SECRETORY PATHWAY CALCIUM ION ATPASE; SIGMA 1 OPIATE RECEPTOR; SODIUM CALCIUM EXCHANGE PROTEIN; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 80053175932     PISSN: None     EISSN: 1478811X     Source Type: Journal    
DOI: 10.1186/1478-811X-9-19     Document Type: Review
Times cited : (319)

References (93)
  • 1
    • 69049098806 scopus 로고    scopus 로고
    • Structural and functional link between the mitochondrial network and the endoplasmic reticulum
    • 10.1016/j.biocel.2009.04.010 19389485
    • Structural and functional link between the mitochondrial network and the endoplasmic reticulum. C Giorgi, D De Stefani, A Bononi, R Rizzuto, P Pinton, Int J Biochem Cell Biol 2009 41 10 1817 27 10.1016/j.biocel.2009.04.010 19389485
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.10 , pp. 1817-1827
    • Giorgi, C.1    De Stefani, D.2    Bononi, A.3    Rizzuto, R.4    Pinton, P.5
  • 2
    • 2442543417 scopus 로고    scopus 로고
    • Respiratory metabolism: Glycolysis, the TCA cycle and mitochondrial electron transport
    • DOI 10.1016/j.pbi.2004.03.007, PII S1369526604000391
    • Respiratory metabolism: glycolysis, the TCA cycle and mitochondrial electron transport. AR Fernie, F Carrari, LJ Sweetlove, Curr Opin Plant Biol 2004 7 3 254 61 10.1016/j.pbi.2004.03.007 15134745 (Pubitemid 38611045)
    • (2004) Current Opinion in Plant Biology , vol.7 , Issue.3 , pp. 254-261
    • Fernie, A.R.1    Carrari, F.2    Sweetlove, L.J.3
  • 5
    • 33746016268 scopus 로고    scopus 로고
    • Mitochondria: More Than Just a Powerhouse
    • DOI 10.1016/j.cub.2006.06.054, PII S0960982206017817
    • Mitochondria: more than just a powerhouse. HM McBride, M Neuspiel, S Wasiak, Curr Biol 2006 16 14 551 60 10.1016/j.cub.2006.06.054 16860735 (Pubitemid 44066793)
    • (2006) Current Biology , vol.16 , Issue.14
    • McBride, H.M.1    Neuspiel, M.2    Wasiak, S.3
  • 6
    • 0347419305 scopus 로고    scopus 로고
    • The molecular machinery of Keilin's respiratory chain
    • The molecular machinery of Keilin's respiratory chain. PR Rich, Biochem Soc Trans 2003 31 Pt 6 1095 105 14641005 (Pubitemid 38030918)
    • (2003) Biochemical Society Transactions , vol.31 , Issue.6 , pp. 1095-1105
    • Rich, P.R.1
  • 7
    • 0018886287 scopus 로고
    • Mitochondrial calcium transport
    • DOI 10.1016/0014-5793(80)80806-4
    • Mitochondrial calcium transport. DG Nicholls, M Crompton, FEBS Lett 1980 111 2 261 8 10.1016/0014-5793(80)80806-4 6987089 (Pubitemid 10121780)
    • (1980) FEBS Letters , vol.111 , Issue.2 , pp. 261-268
    • Nicholls, D.G.1    Crompton, M.2
  • 8
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • DOI 10.1038/nature02246
    • The mitochondrial calcium uniporter is a highly selective ion channel. Y Kirichok, G Krapivinsky, DE Clapham, Nature 2004 427 6972 360 4 10.1038/nature02246 14737170 (Pubitemid 38133664)
    • (2004) Nature , vol.427 , Issue.6972 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 9
    • 80051936634 scopus 로고    scopus 로고
    • A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
    • A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter. D De Stefani, A Raffaello, E Teardo, I Szabò R Rizzuto, Nature 2011
    • (2011) Nature
    • De Stefani, D.1    Raffaello, A.2    Teardo, E.3    Szabò, I.4    Rizzuto, R.5
  • 11
    • 0035038577 scopus 로고    scopus 로고
    • Endoplasmic reticulum of animal cells and its organization into structural and functional domains
    • DOI 10.1016/S0074-7696(01)05004-5
    • Endoplasmic reticulum of animal cells and its organization into structural and functional domains. O Baumann, B Walz, Int Rev Cytol 2001 205 149 214 11336391 (Pubitemid 32390830)
    • (2001) International Review of Cytology , vol.205 , pp. 149-214
    • Baumann, O.1    Walz, B.2
  • 12
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • DOI 10.1016/j.cell.2005.11.047, PII S0092867406000675
    • A class of membrane proteins shaping the tubular endoplasmic reticulum. GK Voeltz, WA Prinz, Y Shibata, JM Rist, TA Rapoport, Cell 2006 124 3 573 86 10.1016/j.cell.2005.11.047 16469703 (Pubitemid 43199442)
    • (2006) Cell , vol.124 , Issue.3 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 13
    • 33746778834 scopus 로고    scopus 로고
    • Rough Sheets and Smooth Tubules
    • DOI 10.1016/j.cell.2006.07.019, PII S0092867406009706
    • Rough sheets and smooth tubules. Y Shibata, GK Voeltz, TA Rapoport, Cell 2006 126 3 435 9 10.1016/j.cell.2006.07.019 16901774 (Pubitemid 44163615)
    • (2006) Cell , vol.126 , Issue.3 , pp. 435-439
    • Shibata, Y.1    Voeltz, G.K.2    Rapoport, T.A.3
  • 14
    • 67949115773 scopus 로고    scopus 로고
    • Peripheral ER structure and function
    • 10.1016/j.ceb.2009.04.004 19447593
    • Peripheral ER structure and function. AR English, N Zurek, GK Voeltz, Curr Opin Cell Biol 2009 21 4 596 602 10.1016/j.ceb.2009.04.004 19447593
    • (2009) Curr Opin Cell Biol , vol.21 , Issue.4 , pp. 596-602
    • English, A.R.1    Zurek, N.2    Voeltz, G.K.3
  • 15
    • 79251471434 scopus 로고    scopus 로고
    • Mechanisms determining the morphology of the peripheral ER
    • 10.1016/j.cell.2010.11.007 21111237
    • Mechanisms determining the morphology of the peripheral ER. Y Shibata, T Shemesh, WA Prinz, AF Palazzo, MM Kozlov, TA Rapoport, Cell 2010 143 5 774 88 10.1016/j.cell.2010.11.007 21111237
    • (2010) Cell , vol.143 , Issue.5 , pp. 774-788
    • Shibata, Y.1    Shemesh, T.2    Prinz, W.A.3    Palazzo, A.F.4    Kozlov, M.M.5    Rapoport, T.A.6
  • 16
    • 0036877145 scopus 로고    scopus 로고
    • The endoplasmic reticulum is a focal point for co-ordination of cellular activity
    • DOI 10.1016/S0143416002002002
    • The endoplasmic reticulum is a focal point for co-ordination of cellular activity. MD Bootman, OH Petersen, A Verkhratsky, Cell Calcium 2002 32 5-6 231 4 10.1016/S0143416002002002 12543085 (Pubitemid 36175746)
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 231-234
    • Bootman, M.D.1    Petersen, O.H.2    Verkhratsky, A.3
  • 17
    • 0035253122 scopus 로고    scopus 로고
    • The endoplasmic reticulum: Integration of protein folding, quality control, signaling and degradation
    • DOI 10.1016/S0959-440X(00)00168-8
    • The endoplasmic reticulum: integration of protein folding, quality control, signaling and degradation. E Chevet, PH Cameron, MF Pelletier, DY Thomas, JJ Bergeron, Curr Opin Struct Biol 2001 11 1 120 4 10.1016/S0959- 440X(00)00168-8 11179901 (Pubitemid 32155561)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.1 , pp. 120-124
    • Chevet, E.1    Cameron, P.H.2    Pelletier, M.F.3    Thomas, D.Y.4    Bergeron, J.J.M.5
  • 18
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • 10.1126/science.1096303 1096303
    • Intracellular aspects of the process of protein synthesis. G Palade, Science 1975 189 4200 347 58 10.1126/science.1096303 1096303
    • (1975) Science , vol.189 , Issue.4200 , pp. 347-358
    • Palade, G.1
  • 19
    • 0037025272 scopus 로고    scopus 로고
    • The endoplasmic reticulum as an integrating signalling organelle: From neuronal signalling to neuronal death
    • DOI 10.1016/S0014-2999(02)01838-1, PII S0014299902018381
    • The endoplasmic reticulum as an integrating signalling organelle: from neuronal signalling to neuronal death. A Verkhratsky, OH Petersen, Eur J Pharmacol 2002 447 2-3 141 54 10.1016/S0014-2999(02)01838-1 12151006 (Pubitemid 34874448)
    • (2002) European Journal of Pharmacology , vol.447 , Issue.2-3 , pp. 141-154
    • Verkhratsky, A.1    Petersen, O.H.2
  • 20
    • 0344966647 scopus 로고
    • An association between mitochondria and the endoplasmic reticulum in cells of the pseudobranch gland of a teleost
    • 10.1083/jcb.5.3.393 13664679
    • An association between mitochondria and the endoplasmic reticulum in cells of the pseudobranch gland of a teleost. DE Copeland, AJ Dalton, J Biophys Biochem Cytol 1959 5 3 393 6 10.1083/jcb.5.3.393 13664679
    • (1959) J Biophys Biochem Cytol , vol.5 , Issue.3 , pp. 393-396
    • Copeland, D.E.1    Dalton, A.J.2
  • 21
    • 0015791478 scopus 로고
    • A rapidly sedimenting fraction of rat liver endoplasmic reticulum
    • 4357366
    • A rapidly sedimenting fraction of rat liver endoplasmic reticulum. JA Lewis, JR Tata, J Cell Sci 1973 13 2 447 59 4357366
    • (1973) J Cell Sci , vol.13 , Issue.2 , pp. 447-459
    • Lewis, J.A.1    Tata, J.R.2
  • 22
    • 0014994920 scopus 로고
    • Connections between mitochondria and endoplasmic reticulum in rat liver and onion stem
    • 10.1007/BF01286410 5112775
    • Connections between mitochondria and endoplasmic reticulum in rat liver and onion stem. DJ Morre, WD Merritt, CA Lembi, Protoplasma 1971 73 1 43 9 10.1007/BF01286410 5112775
    • (1971) Protoplasma , vol.73 , Issue.1 , pp. 43-49
    • Morre, D.J.1    Merritt, W.D.2    Lembi, C.A.3
  • 23
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • 10.1038/nature07534 19052620
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria. OM de Brito, L Scorrano, Nature 2008 456 7222 605 10 10.1038/nature07534 19052620
    • (2008) Nature , vol.456 , Issue.7222 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 25
    • 0031576839 scopus 로고    scopus 로고
    • Abnormalities in mitochondria-associated membranes and phospholipid biosynthetic enzymes in the mnd/mnd mouse model of neuronal ceroid lipofuscinosis
    • DOI 10.1016/S0005-2760(96)00153-1, PII S0005276096001531
    • Abnormalities in mitochondria-associated membranes and phospholipid biosynthetic enzymes in the mnd/mnd mouse model of neuronal ceroid lipofuscinosis. JE Vance, SJ Stone, JR Faust, Biochim Biophys Acta 1997 1344 3 286 99 9059519 (Pubitemid 27079795)
    • (1997) Biochimica et Biophysica Acta - Lipids and Lipid Metabolism , vol.1344 , Issue.3 , pp. 286-299
    • Vance, J.E.1    Stone, S.J.2    Faust, J.R.3
  • 26
    • 70350012303 scopus 로고    scopus 로고
    • Isolation of mitochondria-associated membranes and mitochondria from animal tissues and cells
    • 10.1038/nprot.2009.151 19816421
    • Isolation of mitochondria-associated membranes and mitochondria from animal tissues and cells. MR Wieckowski, C Giorgi, M Lebiedzinska, J Duszynski, P Pinton, Nat Protoc 2009 4 11 1582 90 10.1038/nprot.2009.151 19816421
    • (2009) Nat Protoc , vol.4 , Issue.11 , pp. 1582-1590
    • Wieckowski, M.R.1    Giorgi, C.2    Lebiedzinska, M.3    Duszynski, J.4    Pinton, P.5
  • 27
    • 0034304906 scopus 로고    scopus 로고
    • The versatility and universality of calcium signalling
    • 11413485
    • The versatility and universality of calcium signalling. MJ Berridge, P Lipp, MD Bootman, Nat Rev Mol Cell Biol 2000 1 1 11 21 11413485
    • (2000) Nat Rev Mol Cell Biol , vol.1 , Issue.1 , pp. 11-21
    • Berridge, M.J.1    Lipp, P.2    Bootman, M.D.3
  • 28
    • 0038758748 scopus 로고    scopus 로고
    • 2+ concentration with targeted 'cameleon' fluorescent proteins
    • DOI 10.1016/S0143-4160(03)00081-2
    • 2+concentration with targeted «cameleon» fluorescent proteins. N Demaurex, M Frieden, Cell Calcium 2003 34 2 109 19 10.1016/S0143-4160(03)00081-2 12810053 (Pubitemid 36798394)
    • (2003) Cell Calcium , vol.34 , Issue.2 , pp. 109-119
    • Demaurex, N.1    Frieden, M.2
  • 30
    • 67349089586 scopus 로고    scopus 로고
    • 2+entry by inositol lipids in mammalian cells by multiple mechanisms
    • 10.1016/j.ceca.2009.03.013 19395084
    • 2+entry by inositol lipids in mammalian cells by multiple mechanisms. T Balla, Cell Calcium 2009 45 6 527 34 10.1016/j.ceca.2009.03.013 19395084
    • (2009) Cell Calcium , vol.45 , Issue.6 , pp. 527-534
    • Balla, T.1
  • 33
    • 0030071252 scopus 로고    scopus 로고
    • 2+homeostasis
    • 8522981
    • 2+homeostasis. SL Budd, DG Nicholls, J Neurochem 1996 66 1 403 11 8522981
    • (1996) J Neurochem , vol.66 , Issue.1 , pp. 403-411
    • Budd, S.L.1    Nicholls, D.G.2
  • 34
    • 0033118649 scopus 로고    scopus 로고
    • Contributions of mitochondria to animal physiology: From homeostatic sensor to calcium signalling and cell death
    • Contributions of mitochondria to animal physiology: from homeostatic sensor to calcium signalling and cell death. MR Duchen, J Physiol 1999 516 Pt 1 1 17 10066918 (Pubitemid 29163987)
    • (1999) Journal of Physiology , vol.516 , Issue.1 , pp. 1-17
    • Duchen, M.R.1
  • 35
    • 0029099030 scopus 로고
    • Synchronization of calcium waves by mitochondrial substrates in Xenopus laevis oocytes
    • 10.1038/377438a0 7566122
    • Synchronization of calcium waves by mitochondrial substrates in Xenopus laevis oocytes. LS Jouaville, F Ichas, EL Holmuhamedov, P Camacho, JD Lechleiter, Nature 1995 377 6548 438 41 10.1038/377438a0 7566122
    • (1995) Nature , vol.377 , Issue.6548 , pp. 438-441
    • Jouaville, L.S.1    Ichas, F.2    Holmuhamedov, E.L.3    Camacho, P.4    Lechleiter, J.D.5
  • 36
    • 50549174739 scopus 로고
    • Stoichiometric relationships between mitochondrialion accumulation and oxidative phosphorylation
    • 10.1016/0006-291X(63)90089-5 13975171
    • Stoichiometric relationships between mitochondrialion accumulation and oxidative phosphorylation. CS Rossi, AL Lehninger, Biochem Biophys Res Commun 1963 11 441 6 10.1016/0006-291X(63)90089-5 13975171
    • (1963) Biochem Biophys Res Commun , vol.11 , pp. 441-446
    • Rossi, C.S.1    Lehninger, A.L.2
  • 37
    • 0015724313 scopus 로고
    • 2+uptake by cardiac mitochondria
    • 10.1085/jgp.62.6.756 4548716
    • 2+uptake by cardiac mitochondria. A Scarpa, P Graziotti, J Gen Physiol 1973 62 6 756 72 10.1085/jgp.62.6.756 4548716
    • (1973) J Gen Physiol , vol.62 , Issue.6 , pp. 756-772
    • Scarpa, A.1    Graziotti, P.2
  • 38
    • 0014841199 scopus 로고
    • Mitochondria and calcium ion transport
    • 4922961
    • Mitochondria and calcium ion transport. AL Lehninger, Biochem J 1970 119 2 129 38 4922961
    • (1970) Biochem J , vol.119 , Issue.2 , pp. 129-138
    • Lehninger, A.L.1
  • 39
    • 42049101823 scopus 로고    scopus 로고
    • 2+ signaling, mitochondria and cell death
    • DOI 10.2174/156652408783769571
    • 2+signaling, mitochondria and cell death. C Giorgi, A Romagnoli, P Pinton, R Rizzuto, Curr Mol Med 2008 8 2 119 30 10.2174/156652408783769571 18336292 (Pubitemid 351516831)
    • (2008) Current Molecular Medicine , vol.8 , Issue.2 , pp. 119-130
    • Giorgi, C.1    Romagnoli, A.2    Pinton, P.3    Rizzuto, R.4
  • 40
    • 0018651271 scopus 로고
    • 2+ carrier in rat liver mitochondria
    • 2+carrier in rat liver mitochondria. M Bragadin, T Pozzan, GF Azzone, Biochemistry 1979 18 26 5972 8 10.1021/bi00593a033 42437 (Pubitemid 10137007)
    • (1979) Biochemistry , vol.18 , Issue.26 , pp. 5972-5978
    • Bragadin, M.1    Pozzan, T.2    Azzone, G.F.3
  • 41
    • 33747176845 scopus 로고    scopus 로고
    • 2+ Concentration
    • DOI 10.1016/j.cub.2006.06.059, PII S0960982206018380
    • 2+concentration. B Moreau, C Nelson, AB Parekh, Curr Biol 2006 16 16 1672 7 10.1016/j.cub.2006.06.059 16920631 (Pubitemid 44233269)
    • (2006) Current Biology , vol.16 , Issue.16 , pp. 1672-1677
    • Moreau, B.1    Nelson, C.2    Parekh, A.B.3
  • 45
    • 70349669093 scopus 로고    scopus 로고
    • +antiporter
    • 10.1126/science.1175145 19797662
    • +antiporter. D Jiang, L Zhao, DE Clapham, Science 2009 326 5949 144 7 10.1126/science.1175145 19797662
    • (2009) Science , vol.326 , Issue.5949 , pp. 144-147
    • Jiang, D.1    Zhao, L.2    Clapham, D.E.3
  • 48
    • 70349653079 scopus 로고    scopus 로고
    • Calcium pumps in health and disease
    • 10.1152/physrev.00032.2008 19789383
    • Calcium pumps in health and disease. M Brini, E Carafoli, Physiol Rev 2009 89 4 1341 78 10.1152/physrev.00032.2008 19789383
    • (2009) Physiol Rev , vol.89 , Issue.4 , pp. 1341-1378
    • Brini, M.1    Carafoli, E.2
  • 49
    • 58349111168 scopus 로고    scopus 로고
    • 2+ion extruded
    • 19064619
    • 2+ion extruded. RC Thomas, J Physiol 2009 587 Pt 2 315 27 19064619
    • (2009) J Physiol , vol.587 , Issue.PART 2 , pp. 315-327
    • Thomas, R.C.1
  • 50
    • 0033852625 scopus 로고    scopus 로고
    • Sodium-calcium exchange: A molecular perspective
    • DOI 10.1146/annurev.physiol.62.1.111
    • Sodium-calcium exchange: a molecular perspective. KD Philipson, DA Nicoll, Annu Rev Physiol 2000 62 111 33 10.1146/annurev.physiol.62.1.111 10845086 (Pubitemid 30618258)
    • (2000) Annual Review of Physiology , vol.62 , pp. 111-133
    • Philipson, K.D.1    Nicoll, D.A.2
  • 51
    • 0035815727 scopus 로고    scopus 로고
    • The Golgi PMR1 P-type ATPase of Caenorhabditis elegans: Identification of the gene and demonstration of calcium and manganese transport
    • DOI 10.1074/jbc.M010553200
    • The Golgi PMR1 P-type ATPase of Caenorhabditis elegans. Identification of the gene and demonstration of calcium and manganese transport. K Van Baelen, J Vanoevelen, L Missiaen, L Raeymaekers, F Wuytack, J Biol Chem 2001 276 14 10683 91 10.1074/jbc.M010553200 11134055 (Pubitemid 38089239)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.14 , pp. 10683-10691
    • Van Baelen, K.1    Vanoevelen, J.2    Missiaen, L.3    Raeymaekers, L.4    Wuytack, F.5
  • 53
    • 0027266757 scopus 로고
    • 2+ pump in reconstituted proteoliposomes
    • 2+pump in reconstituted proteoliposomes. X Yu, S Carroll, JL Rigaud, G Inesi, Biophys J 1993 64 4 1232 42 10.1016/S0006-3495(93)81489-9 8388268 (Pubitemid 23143287)
    • (1993) Biophysical Journal , vol.64 , Issue.4 , pp. 1232-1242
    • Yu, X.1    Carroll, S.2    Rigaud, J.-L.3    Inesi, G.4
  • 54
    • 47049101464 scopus 로고    scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum
    • 10.1016/j.abb.2008.04.017 18455499
    • 2+-ATPase of sarcoplasmic reticulum. C Toyoshima, Arch Biochem Biophys 2008 476 1 3 11 10.1016/j.abb.2008.04.017 18455499
    • (2008) Arch Biochem Biophys , vol.476 , Issue.1 , pp. 3-11
    • Toyoshima, C.1
  • 55
    • 0034519503 scopus 로고    scopus 로고
    • Electrical coupling and plasticity of the mitochondrial network
    • DOI 10.1054/ceca.2000.0177
    • Electrical coupling and plasticity of the mitochondrial network. F De Giorgi, L Lartigue, F Ichas, Cell Calcium 2000 28 5-6 365 70 10.1054/ceca.2000.0177 11115375 (Pubitemid 32049119)
    • (2000) Cell Calcium , vol.28 , Issue.5-6 , pp. 365-370
    • De Giorgi, F.1    Lartigue, L.2    Ichas, F.3
  • 56
    • 0034674761 scopus 로고    scopus 로고
    • Characterisation of oxidative phosphorylation in skeletal muscle mitochondria subpopulations in pig: A study using top-down elasticity analysis
    • DOI 10.1016/S0014-5793(00)01633-1, PII S0014579300016331
    • Characterisation of oxidative phosphorylation in skeletal muscle mitochondria subpopulations in pig: a study using top-down elasticity analysis. A Lombardi, M Damon, A Vincent, F Goglia, P Herpin, FEBS Lett 2000 475 2 84 8 10.1016/S0014-5793(00)01633-1 10858493 (Pubitemid 30365055)
    • (2000) FEBS Letters , vol.475 , Issue.2 , pp. 84-88
    • Lombardi, A.1    Damon, M.2    Vincent, A.3    Goglia, F.4    Herpin, P.5
  • 57
    • 0037007227 scopus 로고    scopus 로고
    • Mitochondria are morphologically and functionally heterogeneous within cells
    • DOI 10.1093/emboj/21.7.1616
    • Mitochondria are morphologically and functionally heterogeneous within cells. TJ Collins, MJ Berridge, P Lipp, MD Bootman, EMBO J 2002 21 7 1616 27 10.1093/emboj/21.7.1616 11927546 (Pubitemid 34614618)
    • (2002) EMBO Journal , vol.21 , Issue.7 , pp. 1616-1627
    • Collins, T.J.1    Berridge, M.J.2    Lipp, P.3    Bootman, M.D.4
  • 58
    • 79955623510 scopus 로고    scopus 로고
    • During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
    • 10.1038/ncb2220 21478857
    • During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. LC Gomes, G Di Benedetto, L Scorrano, Nat Cell Biol 2011 13 5 589 98 10.1038/ncb2220 21478857
    • (2011) Nat Cell Biol , vol.13 , Issue.5 , pp. 589-598
    • Gomes, L.C.1    Di Benedetto, G.2    Scorrano, L.3
  • 59
    • 54949110895 scopus 로고    scopus 로고
    • 2+transfer in the control of apoptosis
    • 10.1038/onc.2008.308 18955969
    • 2+transfer in the control of apoptosis. P Pinton, C Giorgi, R Siviero, E Zecchini, R Rizzuto, Oncogene 2008 27 50 6407 18 10.1038/onc.2008.308 18955969
    • (2008) Oncogene , vol.27 , Issue.50 , pp. 6407-6418
    • Pinton, P.1    Giorgi, C.2    Siviero, R.3    Zecchini, E.4    Rizzuto, R.5
  • 60
    • 46649120115 scopus 로고    scopus 로고
    • The versatility of mitochondrial calcium signals: From stimulation of cell metabolism to induction of cell death
    • DOI 10.1016/j.bbabio.2008.05.449, PII S0005272808005987
    • The versatility of mitochondrial calcium signals: from stimulation of cell metabolism to induction of cell death. A Rimessi, C Giorgi, P Pinton, R Rizzuto, Biochim Biophys Acta 2008 1777 7-8 808 16 10.1016/j.bbabio.2008.05.449 18573473 (Pubitemid 351934610)
    • (2008) Biochimica et Biophysica Acta - Bioenergetics , vol.1777 , Issue.7-8 , pp. 808-816
    • Rimessi, A.1    Giorgi, C.2    Pinton, P.3    Rizzuto, R.4
  • 61
    • 0027340729 scopus 로고
    • 3-sensitive channels that are sensed by neighboring mitochondria
    • 2+close to IP3-sensitive channels that are sensed by neighboring mitochondria. R Rizzuto, M Brini, M Murgia, T Pozzan, Science 1993 262 5134 744 7 10.1126/science.8235595 8235595 (Pubitemid 23350694)
    • (1993) Science , vol.262 , Issue.5134 , pp. 744-747
    • Rizzuto, R.1    Brini, M.2    Murgia, M.3    Pozzan, T.4
  • 63
    • 35549006797 scopus 로고    scopus 로고
    • 2+ Signaling and Cell Survival
    • DOI 10.1016/j.cell.2007.08.036, PII S0092867407010999
    • 2+signaling and cell survival. T Hayashi, TP Su, Cell 2007 131 3 596 610 10.1016/j.cell.2007.08.036 17981125 (Pubitemid 350017760)
    • (2007) Cell , vol.131 , Issue.3 , pp. 596-610
    • Hayashi, T.1    Su, T.-P.2
  • 65
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis
    • DOI 10.1038/ncb1063
    • Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis. D Boehning, RL Patterson, L Sedaghat, NO Glebova, T Kurosaki, SH Snyder, Nat Cell Biol 2003 5 12 1051 61 10.1038/ncb1063 14608362 (Pubitemid 37509111)
    • (2003) Nature Cell Biology , vol.5 , Issue.12 , pp. 1051-1061
    • Boehning, D.1    Patterson, R.L.2    Sedaghat, L.3    Glebova, N.O.4    Kurosaki, T.5    Snyder, S.H.6
  • 69
    • 67349112394 scopus 로고    scopus 로고
    • Age-related changes in levels of p66Shc and serine 36-phosphorylated p66Shc in organs and mouse tissues
    • 10.1016/j.abb.2009.03.007 19327338
    • Age-related changes in levels of p66Shc and serine 36-phosphorylated p66Shc in organs and mouse tissues. M Lebiedzinska, J Duszynski, R Rizzuto, P Pinton, MR Wieckowski, Arch Biochem Biophys 2009 486 1 73 80 10.1016/j.abb.2009.03.007 19327338
    • (2009) Arch Biochem Biophys , vol.486 , Issue.1 , pp. 73-80
    • Lebiedzinska, M.1    Duszynski, J.2    Rizzuto, R.3    Pinton, P.4    Wieckowski, M.R.5
  • 72
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • DOI 10.1083/jcb.200212059
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol. DG Breckenridge, M Stojanovic, RC Marcellus, GC Shore, J Cell Biol 2003 160 7 1115 27 10.1083/jcb.200212059 12668660 (Pubitemid 36443879)
    • (2003) Journal of Cell Biology , vol.160 , Issue.7 , pp. 1115-1127
    • Breckenridge, D.G.1    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 73
    • 0032563599 scopus 로고    scopus 로고
    • Differential modulation of SERCA2 isoforms by calreticulin
    • DOI 10.1083/jcb.142.4.963
    • Differential modulation of SERCA2 isoforms by calreticulin. LM John, JD Lechleiter, P Camacho, J Cell Biol 1998 142 4 963 73 10.1083/jcb.142.4.963 9722609 (Pubitemid 28402052)
    • (1998) Journal of Cell Biology , vol.142 , Issue.4 , pp. 963-973
    • John, L.M.1    Lechleiter, J.D.2    Camacho, P.3
  • 74
    • 11844269232 scopus 로고    scopus 로고
    • Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44
    • DOI 10.1016/j.cell.2004.11.048, PII S0092867404011535
    • Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. T Higo, M Hattori, T Nakamura, T Natsume, T Michikawa, K Mikoshiba, Cell 2005 120 1 85 98 10.1016/j.cell.2004.11.048 15652484 (Pubitemid 40094605)
    • (2005) Cell , vol.120 , Issue.1 , pp. 85-98
    • Higo, T.1    Hattori, M.2    Nakamura, T.3    Natsume, T.4    Michikawa, T.5    Mikoshiba, K.6
  • 75
    • 77955708533 scopus 로고    scopus 로고
    • Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM)
    • 10.1007/s12192-010-0174-1 20186508
    • Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM). SY Gilady, M Bui, EM Lynes, MD Benson, R Watts, JE Vance, T Simmen, Cell Stress Chaperones 2010 15 5 619 29 10.1007/s12192-010-0174-1 20186508
    • (2010) Cell Stress Chaperones , vol.15 , Issue.5 , pp. 619-629
    • Gilady, S.Y.1    Bui, M.2    Lynes, E.M.3    Benson, M.D.4    Watts, R.5    Vance, J.E.6    Simmen, T.7
  • 78
    • 0027182769 scopus 로고
    • Cloning and expression of a novel phosphatidylethanolamine N- methyltransferase. A specific biochemical and cytological marker for a unique membrane fraction in rat liver
    • Cloning and expression of a novel phosphatidylethanolamine N-methyltransferase. A specific biochemical and cytological marker for a unique membrane fraction in rat liver. Z Cui, JE Vance, MH Chen, DR Voelker, DE Vance, J Biol Chem 1993 268 22 16655 63 8344945 (Pubitemid 23229978)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.22 , pp. 16655-16663
    • Cui, Z.1    Vance, J.E.2    Chen, M.H.3    Voelker, D.R.4    Vance, D.E.5
  • 79
    • 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
    • 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. AE Rusiñol, Z Cui, MH Chen, JE Vance, J Biol Chem 1994 269 44 27494 502 7961664 (Pubitemid 24346578)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.44 , pp. 27494-27502
    • Rusinol, A.E.1    Cui, Z.2    Chen, M.H.3    Vance, J.E.4
  • 80
    • 0034640960 scopus 로고    scopus 로고
    • 2+ oscillations via an interaction with SERCA2b
    • DOI 10.1083/jcb.149.6.1235
    • 2+oscillations via an interaction with SERCA2b. HL Roderick, JD Lechleiter, P Camacho, J Cell Biol 2000 149 6 1235 48 10.1083/jcb.149.6.1235 10851021 (Pubitemid 30399677)
    • (2000) Journal of Cell Biology , vol.149 , Issue.6 , pp. 1235-1247
    • Roderick, H.L.1    Lechleiter, J.D.2    Camacho, P.3
  • 81
    • 56849113081 scopus 로고    scopus 로고
    • Role of SERCA1 truncated isoform in the proapoptotic calcium transfer from ER to mitochondria during ER stress
    • 10.1016/j.molcel.2008.11.014 19061639
    • Role of SERCA1 truncated isoform in the proapoptotic calcium transfer from ER to mitochondria during ER stress. M Chami, B Oulès, G Szabadkai, R Tacine, R Rizzuto, P Paterlini-Bréchot, Mol Cell 2008 32 5 641 51 10.1016/j.molcel.2008.11.014 19061639
    • (2008) Mol Cell , vol.32 , Issue.5 , pp. 641-651
    • Chami, M.1    Oulès, B.2    Szabadkai, G.3    Tacine, R.4    Rizzuto, R.5    Paterlini-Bréchot, P.6
  • 82
    • 0038662790 scopus 로고    scopus 로고
    • The mitochondria-associated endoplasmic-reticulum subcompartment (MAM fraction) of rat liver contains highly active sphingolipid-specific glycosyltransferases
    • DOI 10.1042/BJ20021834
    • The mitochondria-associated endoplasmic-reticulum subcompartment (MAM fraction) of rat liver contains highly active sphingolipid-specific glycosyltransferases. D Ardail, I Popa, J Bodennec, P Louisot, D Schmitt, J Portoukalian, Biochem J 2003 371 Pt 3 1013 9 12578562 (Pubitemid 36578901)
    • (2003) Biochemical Journal , vol.371 , Issue.3 , pp. 1013-1019
    • Ardail, D.1    Popa, I.2    Bodennec, J.3    Louisot, P.4    Schmitt, D.5    Portoukalian, J.6
  • 83
    • 0035968290 scopus 로고    scopus 로고
    • Enhancement of transport-dependent decarboxylation of phosphatidylserine by S100B protein in permeabilized Chinese hamster ovary cells
    • 10.1074/jbc.M101911200 11320095
    • Enhancement of transport-dependent decarboxylation of phosphatidylserine by S100B protein in permeabilized Chinese hamster ovary cells. O Kuge, Y Yamakawa, M Nishijima, J Biol Chem 2001 276 26 23700 6 10.1074/jbc.M101911200 11320095
    • (2001) J Biol Chem , vol.276 , Issue.26 , pp. 23700-23706
    • Kuge, O.1    Yamakawa, Y.2    Nishijima, M.3
  • 84
    • 21744445061 scopus 로고    scopus 로고
    • Bridging gaps in phospholipid transport
    • DOI 10.1016/j.tibs.2005.05.008, PII S0968000405001532
    • Bridging gaps in phospholipid transport. DR Voelker, Trends Biochem Sci 2005 30 7 396 404 10.1016/j.tibs.2005.05.008 15951180 (Pubitemid 40942035)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.7 , pp. 396-404
    • Voelker, D.R.1
  • 85
    • 0032930120 scopus 로고    scopus 로고
    • Regulated turnover of a cell surface-associated pool of newly synthesized apolipoprotein E in HepG2 cells
    • Regulated turnover of a cell surface-associated pool of newly synthesized apolipoprotein E in HepG2 cells. M Schmitt, T Grand-Perret, J Lipid Res 1999 40 1 39 49 9869648 (Pubitemid 29022584)
    • (1999) Journal of Lipid Research , vol.40 , Issue.1 , pp. 39-49
    • Schmitt, M.1    Grand-Perret, T.2
  • 88
    • 33745958168 scopus 로고    scopus 로고
    • 2+ homeostasis in the endoplasmic reticulum
    • DOI 10.1038/sj.cdd.4401960, PII 4401960
    • 2+homeostasis in the endoplasmic reticulum. P Pinton, R Rizzuto, Cell Death Differ 2006 13 8 1409 18 10.1038/sj.cdd.4401960 16729032 (Pubitemid 44057477)
    • (2006) Cell Death and Differentiation , vol.13 , Issue.8 , pp. 1409-1418
    • Pinton, P.1    Rizzuto, R.2
  • 89
    • 0027377058 scopus 로고
    • Involvement of mitochondrial contact sites in the subcellular compartmentalization of phospholipid biosynthetic enzymes
    • Involvement of mitochondrial contact sites in the subcellular compartmentalization of phospholipid biosynthetic enzymes. D Ardail, F Gasnier, F Lermé C Simonot, P Louisot, O Gateau-Roesch, J Biol Chem 1993 268 34 25985 92 8245031 (Pubitemid 23358220)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.34 , pp. 25985-25992
    • Ardail, D.1    Gasnier, F.2    Lerme, F.3    Simonot, C.4    Louisot, P.5    Gateau-Roesch, O.6
  • 90
    • 0024546684 scopus 로고
    • Adriamycin, a drug interacting with acidic phospholipids, blocks import of precursor proteins by isolated yeast mitochondria
    • Adriamycin, a drug interacting with acidic phospholipids, blocks import of precursor proteins by isolated yeast mitochondria. M Eilers, T Endo, G Schatz, J Biol Chem 1989 264 5 2945 50 2644274 (Pubitemid 19057792)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.5 , pp. 2945-2950
    • Eilers, M.1    Endo, T.2    Schatz, G.3
  • 91
    • 40149104688 scopus 로고    scopus 로고
    • Mitochondrial and secretory human cytomegalovirus UL37 proteins traffic into mitochondrion-associated membranes of human cells
    • DOI 10.1128/JVI.02456-07
    • Mitochondrial and secretory human cytomegalovirus UL37 proteins traffic into mitochondrion-associated membranes of human cells. P Bozidis, CD Williamson, AM Colberg-Poley, J Virol 2008 82 6 2715 26 10.1128/JVI.02456-07 18199645 (Pubitemid 351329163)
    • (2008) Journal of Virology , vol.82 , Issue.6 , pp. 2715-2726
    • Bozidis, P.1    Williamson, C.D.2    Colberg-Poley, A.M.3
  • 92
    • 46249111657 scopus 로고    scopus 로고
    • Hepatitis C virus infection: Molecular pathways to metabolic syndrome
    • DOI 10.1002/hep.22269
    • Hepatitis C virus infection: molecular pathways to metabolic syndrome. MY Sheikh, J Choi, I Qadri, JE Friedman, AJ Sanyal, Hepatology 2008 47 6 2127 33 10.1002/hep.22269 18446789 (Pubitemid 351945577)
    • (2008) Hepatology , vol.47 , Issue.6 , pp. 2127-2133
    • Sheikh, M.Y.1    Choi, J.2    Qadri, I.3    Friedman, J.E.4    Sanyal, A.J.5
  • 93
    • 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
    • 10.1083/jcb.200904060 19752026
    • Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. G Li, M Mongillo, KT Chin, H Harding, D Ron, AR Marks, I Tabas, J Cell Biol 2009 186 6 783 92 10.1083/jcb.200904060 19752026
    • (2009) J Cell Biol , vol.186 , Issue.6 , 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


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