메뉴 건너뛰기




Volumn 32, Issue 4, 2013, Pages 140-146

Calcium and endoplasmic reticulum-mitochondria tethering in neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM;

EID: 84876117473     PISSN: 10445498     EISSN: 15577430     Source Type: Journal    
DOI: 10.1089/dna.2013.2011     Document Type: Article
Times cited : (48)

References (74)
  • 1
    • 80755133370 scopus 로고    scopus 로고
    • Clinical genetics of amyotrophic lateral sclerosis: What do we really know?
    • Andersen, P.M., and Al-Chalabi, A. (2011). Clinical genetics of amyotrophic lateral sclerosis: what do we really know? Nat Rev Neurol 7, 603-615.
    • (2011) Nat Rev Neurol , vol.7 , pp. 603-615
    • Andersen, P.M.1    Al-Chalabi, A.2
  • 2
    • 0141753993 scopus 로고    scopus 로고
    • Thiol-mediated protein retention in the endoplasmic reticulum: The role of ERp44
    • Anelli, T., Alessio, M., Bachi, A., Bergamelli, L., Bertoli, G., Camerini, S., et al. (2003). Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44. EMBO J 22, 5015-5022.
    • (2003) EMBO J , vol.22 , pp. 5015-5022
    • Anelli, T.1    Alessio, M.2    Bachi, A.3    Bergamelli, L.4    Bertoli, G.5    Camerini, S.6
  • 3
    • 84859232387 scopus 로고    scopus 로고
    • Ero1alpha regulates Ca(2+) fluxes at the endoplasmic reticulum- mitochondria interface (MAM)
    • Anelli, T., Bergamelli, L., Margittai, E., Rimessi, A., Fagioli, C., Malgaroli, A., et al. (2012). Ero1alpha regulates Ca(2 +) fluxes at the endoplasmic reticulum-mitochondria interface (MAM). Antioxid Redox Signal 16, 1077-1087.
    • (2012) Antioxid Redox Signal , vol.16 , pp. 1077-1087
    • Anelli, T.1    Bergamelli, L.2    Margittai, E.3    Rimessi, A.4    Fagioli, C.5    Malgaroli, A.6
  • 4
    • 73649098791 scopus 로고    scopus 로고
    • Presenilins are enriched in endoplasmic reticulum membranes associated with mitochondria
    • Area-Gomez, E., de Groof, A.J., Boldogh, I., Bird, T.D., Gibson, G.E., Koehler, C.M., et al. (2009). Presenilins are enriched in endoplasmic reticulum membranes associated with mitochondria. Am J Pathol 175, 1810-1816.
    • (2009) Am J Pathol , vol.175 , pp. 1810-1816
    • Area-Gomez, E.1    De Groof, A.J.2    Boldogh, I.3    Bird, T.D.4    Gibson, G.E.5    Koehler, C.M.6
  • 6
    • 0029128663 scopus 로고
    • Overexpression of calreticulin increases the Ca2 + capacity of rapidly exchanging Ca2 + stores and reveals aspects of their lumenal microenvironment and function
    • Bastianutto, C., Clementi, E., Codazzi, F., Podini, P., De Giorgi, F., Rizzuto, R., et al. (1995). Overexpression of calreticulin increases the Ca2 + capacity of rapidly exchanging Ca2 + stores and reveals aspects of their lumenal microenvironment and function. J Cell Biol 130, 847-855.
    • (1995) J Cell Biol , vol.130 , pp. 847-855
    • Bastianutto, C.1    Clementi, E.2    Codazzi, F.3    Podini, P.4    De Giorgi, F.5    Rizzuto, R.6
  • 7
    • 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., Plovanich, M., Belcher-Timme, C.A., Sancak, Y., et al. (2011). Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter. Nature 476, 341-345.
    • (2011) Nature , vol.476 , pp. 341-345
    • Baughman, J.M.1    Perocchi, F.2    Girgis, H.S.3    Plovanich, M.4    Belcher-Timme, C.A.5    Sancak, Y.6
  • 8
    • 0038125598 scopus 로고    scopus 로고
    • Calcium signalling: Dynamics, homeostasis and remodelling
    • Berridge, M.J., Bootman, M.D., and Roderick, H.L. (2003). Calcium signalling: dynamics, homeostasis and remodelling. Nat Rev Mol Cell Biol 4, 517-529.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 517-529
    • Berridge, M.J.1    Bootman, M.D.2    Roderick, H.L.3
  • 9
    • 84859584667 scopus 로고    scopus 로고
    • The genetics of Alzheimer's disease
    • Bertram, L., and Tanzi, R.E. (2012). The genetics of Alzheimer's disease. Prog Mol Biol Transl Sci 107, 79-100.
    • (2012) Prog Mol Biol Transl Sci , vol.107 , pp. 79-100
    • Bertram, L.1    Tanzi, R.E.2
  • 10
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol (1,4,5) trisphosphate receptors amplifying calciumdependent apoptosis
    • Boehning, D., Patterson, R.L., Sedaghat, L., Glebova, N.O., Kurosaki, T., and Snyder, S.H. (2003). Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calciumdependent apoptosis. Nat Cell Biol 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
  • 11
    • 70349653079 scopus 로고    scopus 로고
    • Calcium pumps in health and disease
    • Brini, M., and Carafoli, E. (2009). Calcium pumps in health and disease. Physiol Rev 89, 1341-1378.
    • (2009) Physiol Rev , vol.89 , pp. 1341-1378
    • Brini, M.1    Carafoli, E.2
  • 12
    • 77449105037 scopus 로고    scopus 로고
    • Presenilin-2 dampens intracellular Ca2 + stores by increasing Ca2 + leakage and reducing Ca2 + uptake
    • Brunello, L., Zampese, E., Florean, C., Pozzan, T., Pizzo, P., and Fasolato, C. (2009). Presenilin-2 dampens intracellular Ca2 + stores by increasing Ca2 + leakage and reducing Ca2 + uptake. J Cell Mol Med 13, 3358-3369.
    • (2009) J Cell Mol Med , vol.13 , pp. 3358-3369
    • Brunello, L.1    Zampese, E.2    Florean, C.3    Pozzan, T.4    Pizzo, P.5    Fasolato, C.6
  • 13
    • 0037269346 scopus 로고    scopus 로고
    • Two pathways for tBID-induced cytochrome c release from rat brain mitochondria: BAK-versus BAX-dependence
    • Brustovetsky, N., Dubinsky, J.M., Antonsson, B., and Jemmerson, R. (2003). Two pathways for tBID-induced cytochrome c release from rat brain mitochondria: BAK-versus BAX-dependence. J Neurochem 84, 196-207.
    • (2003) J Neurochem , vol.84 , pp. 196-207
    • Brustovetsky, N.1    Dubinsky, J.M.2    Antonsson, B.3    Jemmerson, R.4
  • 14
    • 79959500244 scopus 로고    scopus 로고
    • Mitochondria calcium and endoplasmic reticulum stress in Parkinson's disease
    • Cal, T., Ottolini, D., and Brini, M. (2011). Mitochondria, calcium, and endoplasmic reticulum stress in Parkinson's disease. Biofactors 37, 228-240.
    • (2011) Biofactors , vol.37 , pp. 228-240
    • Cal, T.1    Ottolini, D.2    Brini, M.3
  • 15
    • 84888205492 scopus 로고    scopus 로고
    • Mitochondrial Ca(2+) and neurodegeneration
    • Cal, T., Ottolini, D., and Brini, M. (2012a). Mitochondrial Ca(2 +) and neurodegeneration. Cell Calcium 52, 73-85.
    • (2012) Cell Calcium , vol.52 , pp. 73-85
    • Cal, T.1    Ottolini, D.2    Brini, M.3
  • 16
    • 84859894421 scopus 로고    scopus 로고
    • Mitochondrial Ca(2+) as a key regulator of mitochondrial activities
    • Cal, T., Ottolini, D., and Brini, M. (2012b). Mitochondrial Ca(2 +) as a key regulator of mitochondrial activities. Adv Exp Med Biol 942, 53-73.
    • (2012) Adv Exp Med Biol , vol.942 , pp. 53-73
    • Cal, T.1    Ottolini, D.2    Brini, M.3
  • 17
    • 84861554724 scopus 로고    scopus 로고
    • Alpha-Synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions
    • Cal, T., Ottolini, D., Negro, A., and Brini, M. (2012c). alpha-Synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions. J Biol Chem 287, 17914-17929.
    • (2012) J Biol Chem , vol.287 , pp. 17914-17929
    • Cal, T.1    Ottolini, D.2    Negro, A.3    Brini, M.4
  • 18
    • 84873254580 scopus 로고    scopus 로고
    • Enhanced parkin levels favour ER-mitochondria crosstalk and guarantee Ca2 + transfer to sustain cell bioenergetics
    • Cal, T., Ottolini, D., Negro, A., and Brini, M. (2013). Enhanced parkin levels favour ER-mitochondria crosstalk and guarantee Ca2 + transfer to sustain cell bioenergetics. Biochim Biophys Acta -Mol Basis Dis. 1832, 495-508.
    • (2013) Biochim Biophys Acta-Mol Basis Dis , vol.1832 , pp. 495-508
    • Cal, T.1    Ottolini, D.2    Negro, A.3    Brini, M.4
  • 19
    • 0029156597 scopus 로고
    • Calreticulin inhibits repetitive intracellular Ca2 + waves
    • Camacho, P., and Lechleiter, J.D. (1995). Calreticulin inhibits repetitive intracellular Ca2 + waves. Cell 82, 765-771.
    • (1995) Cell , vol.82 , pp. 765-771
    • Camacho, P.1    Lechleiter, J.D.2
  • 20
    • 77955041880 scopus 로고    scopus 로고
    • Essential regulation of cell bioenergetics by constitutive InsP3 receptor Ca+ transfer to mitochondria
    • Cardenas, C., Miller, R.A., Smith, I., Bui, T., Molgo, J., Muller, M., et al. (2010). Essential regulation of cell bioenergetics by constitutive InsP3 receptor Ca+ transfer to mitochondria. Cell 142, 270-283.
    • (2010) Cell , vol.142 , pp. 270-283
    • Cardenas, C.1    Miller, R.A.2    Smith, I.3    Bui, T.4    Molgo, J.5    Muller, M.6
  • 21
    • 34547601410 scopus 로고    scopus 로고
    • Mitochondrial fusion protects against neurodegeneration in the cerebellum
    • Chen, H., McCaffery, J.M., and Chan, D.C. (2007). Mitochondrial fusion protects against neurodegeneration in the cerebellum. Cell 130, 548-562.
    • (2007) Cell , vol.130 , pp. 548-562
    • Chen, H.1    McCaffery, J.M.2    Chan, D.C.3
  • 22
    • 45249117227 scopus 로고    scopus 로고
    • Mechanism of Ca2 + disruption in Alzheimer's disease by presenilin regulation of InsP3 receptor channel gating
    • Cheung, K.H., Shineman, D., Muller, M., Cardenas, C., Mei, L., Yang, J., et al. (2008). Mechanism of Ca2 + disruption in Alzheimer's disease by presenilin regulation of InsP3 receptor channel gating. Neuron 58, 871-883.
    • (2008) Neuron , vol.58 , pp. 871-883
    • Cheung, K.H.1    Shineman, D.2    Muller, M.3    Cardenas, C.4    Mei, L.5    Yang, J.6
  • 23
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham, D.E. (2007). Calcium signaling. Cell 131, 1047-1058.
    • (2007) Cell , vol.131 , pp. 1047-1058
    • Clapham, D.E.1
  • 24
    • 33749022800 scopus 로고    scopus 로고
    • Structural and functional features and significance of the physical linkage between ER and mitochondria
    • Csordas, G., Renken, C., Varnai, P., Walter, L., Weaver, D., Buttle, K.F., et al. (2006). Structural and functional features and significance of the physical linkage between ER and mitochondria. J Cell Biol 174, 915-921.
    • (2006) J Cell Biol , vol.174 , pp. 915-921
    • Csordas, G.1    Renken, C.2    Varnai, P.3    Walter, L.4    Weaver, D.5    Buttle, K.F.6
  • 25
    • 77954301751 scopus 로고    scopus 로고
    • Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface
    • Csordas, G., Varnai, P., Golenar, T., Roy, S., Purkins, G., Schneider, T.G., et al. (2010). Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface. Mol Cell 39, 121-132.
    • (2010) Mol Cell , vol.39 , pp. 121-132
    • Csordas, G.1    Varnai, P.2    Golenar, T.3    Roy, S.4    Purkins, G.5    Schneider, T.G.6
  • 26
    • 70349150536 scopus 로고    scopus 로고
    • Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function
    • Davison, E.J., Pennington, K., Hung, C.C., Peng, J., Rafiq, R., Ostareck-Lederer, A., et al. (2009). Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function. Proteomics 9, 4284-4297.
    • (2009) Proteomics , vol.9 , pp. 4284-4297
    • Davison, E.J.1    Pennington, K.2    Hung, C.C.3    Peng, J.4    Rafiq, R.5    Ostareck-Lederer, A.6
  • 27
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito, O.M., and Scorrano, L. (2008). Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 456, 605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 29
    • 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., and Rizzuto, R. (2011). A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter. Nature 476, 336-340.
    • (2011) Nature , vol.476 , pp. 336-340
    • De Stefani, D.1    Raffaello, A.2    Teardo, E.3    Szabo, I.4    Rizzuto, R.5
  • 30
    • 84863393591 scopus 로고    scopus 로고
    • VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis
    • De Vos, K.J., Morotz, G.M., Stoica, R., Tudor, E.L., Lau, K.F., Ackerley, S., et al. (2012). VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis. Hum Mol Genet 21, 1299-1311.
    • (2012) Hum Mol Genet , vol.21 , pp. 1299-1311
    • De Vos, K.J.1    Morotz, G.M.2    Stoica, R.3    Tudor, E.L.4    Lau, K.F.5    Ackerley, S.6
  • 31
    • 84875730994 scopus 로고    scopus 로고
    • Parkin differently regulates presenilin-1 and presenilin-2 function by direct control of their promoter transcription
    • Epub ahead of print]. DOI: 10. 1093/jmcb/mjt003
    • Duplan, E., Sevalle, J., Viotti, J., Goiran, T., Druon, C., Renbaum, P., et al. (2013). Parkin differently regulates presenilin-1 and presenilin-2 function by direct control of their promoter transcription. J Mol Cell Biol [Epub ahead of print]. DOI: 10. 1093/jmcb/mjt003
    • (2013) J Mol Cell Biol
    • Duplan, E.1    Sevalle, J.2    Viotti, J.3    Goiran, T.4    Druon, C.5    Renbaum, P.6
  • 33
    • 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., Scorzeto, M., Gianelle, A., Pizzo, P., et al. (2010). 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 38, 280-290.
    • (2010) Mol Cell , vol.38 , pp. 280-290
    • Giacomello, M.1    Drago, I.2    Bortolozzi, M.3    Scorzeto, M.4    Gianelle, A.5    Pizzo, P.6
  • 34
    • 78649425814 scopus 로고    scopus 로고
    • PML regulates apoptosis at endoplasmic reticulum by modulating calcium release
    • Giorgi, C., Ito, K., Lin, H.K., Santangelo, C., Wieckowski, M.R., Lebiedzinska, M., et al. (2010). PML regulates apoptosis at endoplasmic reticulum by modulating calcium release. Science 330, 1247-1251.
    • (2010) Science , vol.330 , pp. 1247-1251
    • Giorgi, C.1    Ito, K.2    Lin, H.K.3    Santangelo, C.4    Wieckowski, M.R.5    Lebiedzinska, M.6
  • 35
    • 46249123354 scopus 로고    scopus 로고
    • SERCA pump activity is physiologically regulated by presenilin and regulates amyloid beta production
    • Green, K.N., Demuro, A., Akbari, Y., Hitt, B.D., Smith, I.F., Parker, I., et al. (2008). SERCA pump activity is physiologically regulated by presenilin and regulates amyloid beta production. J Cell Biol 181, 1107-1116.
    • (2008) J Cell Biol , vol.181 , pp. 1107-1116
    • Green, K.N.1    Demuro, A.2    Akbari, Y.3    Hitt, B.D.4    Smith, I.F.5    Parker, I.6
  • 37
    • 35549006797 scopus 로고    scopus 로고
    • Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2 +) signaling and cell survival
    • Hayashi, T., and Su, T.P. (2007). Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2 +) signaling and cell survival. Cell 131, 596-610.
    • (2007) Cell , vol.131 , pp. 596-610
    • Hayashi, T.1    Su, T.P.2
  • 38
    • 7444240833 scopus 로고    scopus 로고
    • The ER function BiP is a master regulator of ER function
    • Hendershot, L.M. (2004). The ER function BiP is a master regulator of ER function. Mt Sinai J Med N Y 71, 289-297.
    • (2004) Mt Sinai J Med N y , vol.71 , pp. 289-297
    • Hendershot, L.M.1
  • 39
    • 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., and Mikoshiba, K. (2005). Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell 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
  • 40
    • 34249704608 scopus 로고    scopus 로고
    • Identification of novel proteins associated with both alphasynuclein and DJ-1
    • Jin, J., Li, G.J., Davis, J., Zhu, D., Wang, Y., Pan, C., et al. (2007). Identification of novel proteins associated with both alphasynuclein and DJ-1. Mol Cell Proteomics 6, 845-859.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 845-859
    • Jin, J.1    Li, G.J.2    Davis, J.3    Zhu, D.4    Wang, Y.5    Pan, C.6
  • 41
    • 84866455663 scopus 로고    scopus 로고
    • Ca2 + dysregulation in neurons from transgenic mice expressing mutant presenilin 2
    • Kipanyula, M.J., Contreras, L., Zampese, E., Lazzari, C., Wong, A.K., Pizzo, P., et al. (2012). Ca2 + dysregulation in neurons from transgenic mice expressing mutant presenilin 2. Aging Cell 11, 885-893.
    • (2012) Aging Cell , vol.11 , pp. 885-893
    • Kipanyula, M.J.1    Contreras, L.2    Zampese, E.3    Lazzari, C.4    Wong, A.K.5    Pizzo, P.6
  • 42
    • 80052172908 scopus 로고    scopus 로고
    • The conserved GTPase Gem1 regulates endoplasmic reticulummitochondria connections
    • Kornmann, B., Osman, C., and Walter, P. (2011). The conserved GTPase Gem1 regulates endoplasmic reticulummitochondria connections. Proc Natl Acad Sci U S A 108, 14151-14156.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14151-14156
    • Kornmann, B.1    Osman, C.2    Walter, P.3
  • 43
    • 77954324616 scopus 로고    scopus 로고
    • AAV-mediated expression of wildtype and ALS-linked mutant VAPB selectively triggers death of motoneurons through a Ca2 + -dependent ER-associated pathway
    • Langou, K., Moumen, A., Pellegrino, C., Aebischer, J., Medina, I., Aebischer, P., et al. (2010). AAV-mediated expression of wildtype and ALS-linked mutant VAPB selectively triggers death of motoneurons through a Ca2 + -dependent ER-associated pathway. J Neurochem 114, 795-809.
    • (2010) J Neurochem , vol.114 , pp. 795-809
    • Langou, K.1    Moumen, A.2    Pellegrino, C.3    Aebischer, J.4    Medina, I.5    Aebischer, P.6
  • 44
    • 63149090431 scopus 로고    scopus 로고
    • Parkinson's disease: From monogenic forms to genetic susceptibility factors
    • Lesage, S., and Brice, A. (2009). Parkinson's disease: from monogenic forms to genetic susceptibility factors. Hum Mol Genet 18, R48-R59.
    • (2009) Hum Mol Genet , vol.18
    • Lesage, S.1    Brice, A.2
  • 45
    • 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., et al. (2009). Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J Cell Biol 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
  • 46
    • 25444514752 scopus 로고    scopus 로고
    • Association of DJ-1 with chaperones and enhanced association and colocalization with mitochondrial Hsp70 by oxidative stress
    • Li, H.M., Niki, T., Taira, T., Iguchi-Ariga, S.M., and Ariga, H. (2005). Association of DJ-1 with chaperones and enhanced association and colocalization with mitochondrial Hsp70 by oxidative stress. Free Radic Res 39, 1091-1099.
    • (2005) Free Radic Res , vol.39 , pp. 1091-1099
    • Li, H.M.1    Niki, T.2    Taira, T.3    Iguchi-Ariga, S.M.4    Ariga, H.5
  • 47
    • 84874386672 scopus 로고    scopus 로고
    • Voltage-dependent anion channel involved in the alphasynuclein-induced dopaminergic neuron toxicity in rats
    • [Epub ahead of print]; DOI: 10. 1093/abbs/gms114
    • Lu, L., Zhang, C., Cai, Q., Lu, Q., Duan, C., Zhu, Y., et al. (2013). Voltage-dependent anion channel involved in the alphasynuclein-induced dopaminergic neuron toxicity in rats. Acta Biochim Biophys Sin [Epub ahead of print]; DOI: 10. 1093/abbs/gms114.
    • (2013) Acta Biochim Biophys Sin
    • Lu, L.1    Zhang, C.2    Cai, Q.3    Lu, Q.4    Duan, C.5    Zhu, Y.6
  • 49
    • 79959505900 scopus 로고    scopus 로고
    • Molecules and roles of mitochondrial calcium signaling
    • Mammucari, C., Patron, M., Granatiero, V., and Rizzuto, R. (2011). Molecules and roles of mitochondrial calcium signaling. Biofactors 37, 219-227.
    • (2011) Biofactors , vol.37 , pp. 219-227
    • Mammucari, C.1    Patron, M.2    Granatiero, V.3    Rizzuto, R.4
  • 50
    • 0025319665 scopus 로고
    • Role of calcium ions in regulation of mammalian intramitochondrial metabolism
    • McCormack, J.G., Halestrap, A.P., and Denton, R.M. (1990). Role of calcium ions in regulation of mammalian intramitochondrial metabolism. Physiol Rev 70, 391-425.
    • (1990) Physiol Rev , vol.70 , pp. 391-425
    • McCormack, J.G.1    Halestrap, A.P.2    Denton, R.M.3
  • 51
    • 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., and Opas, M. (2009). Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem J 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
  • 52
    • 1342334746 scopus 로고    scopus 로고
    • Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control
    • Molinari, M., Eriksson, K.K., Calanca, V., Galli, C., Cresswell, P., Michalak, M., et al. (2004). Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control. Mol Cell 13, 125-135.
    • (2004) Mol Cell , vol.13 , pp. 125-135
    • Molinari, M.1    Eriksson, K.K.2    Calanca, V.3    Galli, C.4    Cresswell, P.5    Michalak, M.6
  • 53
    • 84859246580 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosisassociated mutant VAPBP56S perturbs calcium homeostasis to disrupt axonal transport of mitochondria
    • Morotz, G.M., De Vos, K.J., Vagnoni, A., Ackerley, S., Shaw, C.E., and Miller, C.C. (2012). Amyotrophic lateral sclerosisassociated mutant VAPBP56S perturbs calcium homeostasis to disrupt axonal transport of mitochondria. Hum Mol Genet 21, 1979-1988.
    • (2012) Hum Mol Genet , vol.21 , pp. 1979-1988
    • Morotz, G.M.1    De Vos, K.J.2    Vagnoni, A.3    Ackerley, S.4    Shaw, C.E.5    Miller, C.C.6
  • 55
    • 6344257200 scopus 로고    scopus 로고
    • A mutation in the vesicletrafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis
    • Nishimura, A.L., Mitne-Neto, M., Silva, H.C., Richieri-Costa, A., Middleton, S., Cascio, D., et al. (2004). A mutation in the vesicletrafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis. Am J Hum Genet 75, 822-831.
    • (2004) Am J Hum Genet , vol.75 , pp. 822-831
    • Nishimura, A.L.1    Mitne-Neto, M.2    Silva, H.C.3    Richieri-Costa, A.4    Middleton, S.5    Cascio, D.6
  • 56
    • 84876098997 scopus 로고    scopus 로고
    • The Parkinson disease related protein DJ-1 counteracts mitochondrial impairment induced by the tumor suppressor protein p53 by enhancing Endoplasmic Reticulum-mitochondria tethering
    • [Epub ahead of print]; DOI: 10. 1093/hmg/ddt068
    • Ottolini, D., Cal, T., Negro, A., and Brini, M. (2013). The Parkinson disease related protein DJ-1 counteracts mitochondrial impairment induced by the tumor suppressor protein p53 by enhancing Endoplasmic Reticulum-mitochondria tethering. Hum Mol Genet [Epub ahead of print]; DOI: 10. 1093/hmg/ddt068.
    • (2013) Hum Mol Genet
    • Ottolini, D.1    Cal, T.2    Negro, A.3    Brini, M.4
  • 58
    • 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., Bao, X.R., McCombs, J.E., Palmer, A.E., et al. (2010). MICU1 encodes a mitochondrial EF hand protein required for Ca(2 +) uptake. Nature 467, 291-296.
    • (2010) Nature , vol.467 , pp. 291-296
    • Perocchi, F.1    Gohil, V.M.2    Girgis, H.S.3    Bao, X.R.4    McCombs, J.E.5    Palmer, A.E.6
  • 59
    • 84888198209 scopus 로고    scopus 로고
    • In-depth proteomic analysis of mammalian mitochondria-associated membranes (MAM)
    • Poston, C.N., Krishnan, S.C., and Bazemore-Walker, C.R. (2013). In-depth proteomic analysis of mammalian mitochondria-associated membranes (MAM). J Proteomics pii, S1874-S3919.
    • (2013) J Proteomics Pii
    • Poston, C.N.1    Krishnan, S.C.2    Bazemore-Walker, C.R.3
  • 60
    • 84883281733 scopus 로고    scopus 로고
    • Disruption of cyclophilin Dmediated calcium transfer from the ER to mitochondria contributes to hepatic ER stress and insulin resistance
    • [Epub ahead of print]; DOI: 10. 1002/hep.26189
    • Rieusset, J., Fauconnier, J., Paillard, M., Belaidi, E., Tubbs, E., Chauvin, M.A., et al. (2012). Disruption of cyclophilin Dmediated calcium transfer from the ER to mitochondria contributes to hepatic ER stress and insulin resistance. Hepatology [Epub ahead of print]; DOI: 10. 1002/hep.26189.
    • (2012) Hepatology
    • Rieusset, J.1    Fauconnier, J.2    Paillard, M.3    Belaidi, E.4    Tubbs, E.5    Chauvin, M.A.6
  • 61
    • 0027340729 scopus 로고
    • Microdomains with high Ca2 + close to IP3-sensitive channels that are sensed by neighboring mitochondria
    • Rizzuto, R., Brini, M., Murgia, M., and Pozzan, T. (1993). Microdomains with high Ca2 + close to IP3-sensitive channels that are sensed by neighboring mitochondria. Science 262, 744-747.
    • (1993) Science , vol.262 , pp. 744-747
    • Rizzuto, R.1    Brini, M.2    Murgia, M.3    Pozzan, T.4
  • 63
    • 0032511112 scopus 로고    scopus 로고
    • Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2 + responses
    • Rizzuto, R., Pinton, P., Carrington, W., Fay, F.S., Fogarty, K.E., Lifshitz, L.M., et al. (1998). Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2 + responses. Science 280, 1763-1766.
    • (1998) Science , vol.280 , pp. 1763-1766
    • Rizzuto, R.1    Pinton, P.2    Carrington, W.3    Fay, F.S.4    Fogarty, K.E.5    Lifshitz, L.M.6
  • 64
    • 84866728707 scopus 로고    scopus 로고
    • Endoplasmic reticulummitochondria contacts: Function of the junction
    • Rowland, A.A., and Voeltz, G.K. (2012). Endoplasmic reticulummitochondria contacts: function of the junction. Nat Rev Mol Cell Biol 13, 607-625.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 607-625
    • Rowland, A.A.1    Voeltz, G.K.2
  • 65
    • 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., and Vance, J.E. (1994). 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 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
  • 67
    • 77956203927 scopus 로고    scopus 로고
    • Is Alzheimer's disease a disorder of mitochondria-associated membranes?
    • Schon, E.A., and Area-Gomez, E. (2010). Is Alzheimer's disease a disorder of mitochondria-associated membranes? J Alzheimers Dis 20 Suppl 2, S281-92.
    • (2010) J Alzheimers Dis , vol.20 , Issue.SUPPL. 2
    • Schon, E.A.1    Area-Gomez, E.2
  • 68
    • 79959305691 scopus 로고    scopus 로고
    • Mitochondria: The next (neurode)generation
    • Schon, E.A., and Przedborski, S. (2011). Mitochondria: the next (neurode)generation. Neuron 70, 1033-1053.
    • (2011) Neuron , vol.70 , pp. 1033-1053
    • Schon, E.A.1    Przedborski, S.2
  • 69
    • 0037418843 scopus 로고    scopus 로고
    • BAX and BAK regulation of endoplasmic reticulum Ca2+ : A control point for apoptosis
    • Scorrano, L., Oakes, S.A., Opferman, J.T., Cheng, E.H., Sorcinelli, M.D., Pozzan, T., et al. (2003). BAX and BAK regulation of endoplasmic reticulum Ca2 + : a control point for apoptosis. Science 300, 135-139.
    • (2003) Science , vol.300 , pp. 135-139
    • Scorrano, L.1    Oakes, S.A.2    Opferman, J.T.3    Cheng, E.H.4    Sorcinelli, M.D.5    Pozzan, T.6
  • 70
    • 33845692166 scopus 로고    scopus 로고
    • Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
    • Szabadkai, G., Bianchi, K., Varnai, P., De Stefani, D., Wieckowski, M.R., Cavagna, D., et al. (2006). Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2 + channels. J Cell Biol 175, 901-911.
    • (2006) J Cell Biol , vol.175 , pp. 901-911
    • Szabadkai, G.1    Bianchi, K.2    Varnai, P.3    De Stefani, D.4    Wieckowski, M.R.5    Cavagna, D.6
  • 71
    • 33748140720 scopus 로고    scopus 로고
    • Presenilins form ER Ca2 + leak channels, a function disrupted by familial Alzheimer's disease-linked mutations
    • Tu, H., Nelson, O., Bezprozvanny, A., Wang, Z., Lee, S.F., Hao, Y.H., et al. (2006). Presenilins form ER Ca2 + leak channels, a function disrupted by familial Alzheimer's disease-linked mutations. Cell 126, 981-993.
    • (2006) Cell , vol.126 , pp. 981-993
    • Tu, H.1    Nelson, O.2    Bezprozvanny, A.3    Wang, Z.4    Lee, S.F.5    Hao, Y.H.6
  • 72
    • 84870984470 scopus 로고    scopus 로고
    • PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROSbased ER stress
    • Verfaillie, T., Rubio, N., Garg, A.D., Bultynck, G., Rizzuto, R., Decuypere, J.P., et al. (2012). PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROSbased ER stress. Cell Death Differ 19, 1880-1891.
    • (2012) Cell Death Differ , vol.19 , pp. 1880-1891
    • Verfaillie, T.1    Rubio, N.2    Garg, A.D.3    Bultynck, G.4    Rizzuto, R.5    Decuypere, J.P.6
  • 73
    • 58149091896 scopus 로고    scopus 로고
    • The mechanism of Ca2 + -dependent regulation of kinesin-mediated mitochondrial motility
    • Wang, X., and Schwarz, T.L. (2009). The mechanism of Ca2 + -dependent regulation of kinesin-mediated mitochondrial motility. Cell 136, 163-174.
    • (2009) Cell , vol.136 , pp. 163-174
    • Wang, X.1    Schwarz, T.L.2
  • 74
    • 84859156397 scopus 로고    scopus 로고
    • Presenilin-2 modulation of ER-mitochondria interactions: FAD mutations, mechanisms and pathological consequences
    • Zampese, E., Fasolato, C., Pozzan, T., and Pizzo, P. (2011). Presenilin-2 modulation of ER-mitochondria interactions: FAD mutations, mechanisms and pathological consequences. Commun Integr Biol 4, 357-360.
    • (2011) Commun Integr Biol , vol.4 , pp. 357-360
    • Zampese, E.1    Fasolato, C.2    Pozzan, T.3    Pizzo, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.