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Volumn 15, Issue 10, 2013, Pages 1197-1205

Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells

(26)  Chu, Charleen T a   Ji, Jing b,c,d   Dagda, Ruben K a,e   Jiang, Jian Fei b   Tyurina, Yulia Y b   Kapralov, Alexandr A b   Tyurin, Vladimir A b   Yanamala, Naveena a   Shrivastava, Indira H a   Mohammadyani, Dariush a,f   Qiang Wang, Kent Zhi a   Zhu, Jianhui a   Klein Seetharaman, Judith b,g   Balasubramanian, Krishnakumar b   Amoscato, Andrew A b   Borisenko, Grigory b   Huang, Zhentai b   Gusdon, Aaron M a   Cheikhi, Amin b   Steer, Erin K a   more..


Author keywords

[No Author keywords available]

Indexed keywords

CARDIOLIPIN; CARDIOLIPIN SYNTHASE; MICROTUBULE ASSOCIATED PROTEIN 1; MICROTUBULE ASSOCIATED PROTEIN 1 LIGHT CHAIN 3; OXIDOPAMINE; ROTENONE; SCRAMBLASE; SCRAMBLASE 3; STAUROSPORINE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 84885176082     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb2837     Document Type: Article
Times cited : (821)

References (57)
  • 1
    • 79954622220 scopus 로고    scopus 로고
    • Mitophagy selectively degrades individual damaged mito- chondria after photoirradiation
    • Kim, I. & Lemasters, J. J. Mitophagy selectively degrades individual damaged mito- chondria after photoirradiation. Antioxid. Redox Signal. 14, 1919-1928 (2011).
    • (2011) Antioxid. Redox Signal , vol.14 , pp. 1919-1928
    • Kim, I.1    Lemasters, J.J.2
  • 2
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki, T., Wang, K., Cao, Y., Baba, M. & Klionsky, D. J. Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Dev. Cell 17, 98-109 (2009).
    • (2009) Dev. Cell , vol.17 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3    Baba, M.4    Klionsky, D.J.5
  • 3
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra, D., Tanaka, A., Suen, D. F. & Youle, R. J. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 183, 795-803 (2008).
    • (2008) J. Cell Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 4
    • 84862789618 scopus 로고    scopus 로고
    • Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia- induced mitophagy in mammalian cells
    • Liu, L. et al. Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia- induced mitophagy in mammalian cells. Nat. Cell Biol. 14, 177-185 (2012).
    • (2012) Nat. Cell Biol , vol.14 , pp. 177-185
    • Liu, L.1
  • 5
    • 51449112852 scopus 로고    scopus 로고
    • Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes
    • Schlame, M. Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes. J. Lipid Res. 49, 1607-1620 (2008).
    • (2008) J. Lipid Res , vol.49 , pp. 1607-1620
    • Schlame, M.1
  • 6
    • 0029751960 scopus 로고    scopus 로고
    • Specific cardiolipin binding interferes with labeling of sulfhydryl residues in the adenosine diphosphate/adenosine triphosphate carrier protein from beef heart mitochondria
    • Beyer, K. & Nuscher, B. Specific cardiolipin binding interferes with labeling of sulfhydryl residues in the adenosine diphosphate/adenosine triphosphate carrier protein from beef heart mitochondria. Biochemistry 35, 15784-15790 (1996).
    • (1996) Biochemistry , vol.35 , pp. 15784-15790
    • Beyer, K.1    Nuscher, B.2
  • 7
    • 78649833818 scopus 로고    scopus 로고
    • Human IRGM regulates autophagy and cell-autonomous immunity functions through mitochondria
    • Singh, S. B. et al. Human IRGM regulates autophagy and cell-autonomous immunity functions through mitochondria. Nat. Cell Biol. 12, 1154-1165 (2010).
    • (2010) Nat. Cell Biol , vol.12 , pp. 1154-1165
    • Singh, S.B.1
  • 8
    • 4344696843 scopus 로고    scopus 로고
    • The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8
    • Sugawara, K. et al. The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8. Genes Cells 9, 611-618 (2004).
    • (2004) Genes Cells , vol.9 , pp. 611-618
    • Sugawara, K.1
  • 9
    • 36248944555 scopus 로고    scopus 로고
    • Identification of Tim4 as a phosphatidylserine receptor
    • Miyanishi, M. et al. Identification of Tim4 as a phosphatidylserine receptor. Nature 450, 435-439 (2007).
    • (2007) Nature , vol.450 , pp. 435-439
    • Miyanishi, M.1
  • 10
    • 79959305691 scopus 로고    scopus 로고
    • Mitochondria: The next (neurode)generation
    • Schon, E. A. & Przedborski, S. Mitochondria: the next (neurode)generation. Neuron 70, 1033-1053 (2011).
    • (2011) Neuron , vol.70 , pp. 1033-1053
    • Schon, E.A.1    Przedborski, S.2
  • 11
    • 0242499488 scopus 로고    scopus 로고
    • Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in Lewy body diseases
    • Zhu, J. H., Guo, F., Shelburne, J., Watkins, S. & Chu, C. T. Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in Lewy body diseases. Brain Pathol. 13, 473-481 (2003).
    • (2003) Brain Pathol , vol.13 , pp. 473-481
    • Zhu, J.H.1    Guo, F.2    Shelburne, J.3    Watkins, S.4    Chu, C.T.5
  • 12
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • Wong, E. & Cuervo, A. M. Autophagy gone awry in neurodegenerative diseases. Nat. Neurosci. 13, 805-811 (2010).
    • (2010) Nat. Neurosci , vol.13 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 13
    • 77952766891 scopus 로고    scopus 로고
    • Autophagy: Assays and artifacts
    • Barth, S., Glick, D. & Macleod, K. F. Autophagy: assays and artifacts. J. Pathol. 221, 117-124 (2010).
    • (2010) J. Pathol , vol.221 , pp. 117-124
    • Barth, S.1    Glick, D.2    MacLeod, K.F.3
  • 14
    • 52049116066 scopus 로고    scopus 로고
    • Oxidative lipidomics of programmed cell death
    • Tyurin, V. A. et al. Oxidative lipidomics of programmed cell death. Methods Enzymol. 442, 375-393 (2008).
    • (2008) Methods Enzymol , vol.442 , pp. 375-393
    • Tyurin, V.A.1
  • 15
    • 0036479049 scopus 로고    scopus 로고
    • Mitochondrial intermembrane junctional complexes and their involvement in cell death
    • Crompton, M., Barksby, E., Johnson, N. & Capano, M. Mitochondrial intermembrane junctional complexes and their involvement in cell death. Biochimie 84, 143-152 (2002).
    • (2002) Biochimie , vol.84 , pp. 143-152
    • Crompton, M.1    Barksby, E.2    Johnson, N.3    Capano, M.4
  • 16
    • 0025250043 scopus 로고
    • Binding of vascular anticoagulant alpha (VAC alpha) to planar phospholipid bilayers
    • Andree, H. A. et al. Binding of vascular anticoagulant alpha (VAC alpha) to planar phospholipid bilayers. J. Biol. Chem. 265, 4923-4928 (1990).
    • (1990) J. Biol. Chem , vol.265 , pp. 4923-4928
    • Andree, H.A.1
  • 17
    • 50249168137 scopus 로고    scopus 로고
    • Mitochondrially localized ERK2 regulates mitophagy and autophagic cell stress: Implications for Parkinson's disease
    • Dagda, R. K., Zhu, J., Kulich, S. M. & Chu, C. T. Mitochondrially localized ERK2 regulates mitophagy and autophagic cell stress: implications for Parkinson's disease. Autophagy 4, 770-782 (2008).
    • (2008) Autophagy , vol.4 , pp. 770-782
    • Dagda, R.K.1    Zhu, J.2    Kulich, S.M.3    Chu, C.T.4
  • 18
    • 33745863454 scopus 로고    scopus 로고
    • Functional repression of cAMP response element in 6-hydroxydopamine- treated neuronal cells
    • Chalovich, E. M., Zhu, J. H., Caltagarone, J., Bowser, R. & Chu, C. T. Functional repression of cAMP response element in 6-hydroxydopamine-treated neuronal cells. J. Biol. Chem. 281, 17870-17881 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 17870-17881
    • Chalovich, E.M.1    Zhu, J.H.2    Caltagarone, J.3    Bowser, R.4    Chu, C.T.5
  • 19
    • 42049102578 scopus 로고    scopus 로고
    • Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis
    • Liu, J. et al. Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis. Biochemistry 47, 4518-4529 (2008).
    • (2008) Biochemistry , vol.47 , pp. 4518-4529
    • Liu, J.1
  • 20
    • 43049159564 scopus 로고    scopus 로고
    • Cardiolipin deficiency leads to decreased cardiolipin peroxidation and increased resistance of cells to apoptosis
    • Huang, Z. et al. Cardiolipin deficiency leads to decreased cardiolipin peroxidation and increased resistance of cells to apoptosis. Free Radic. Biol. Med. 44, 1935-1944 (2008).
    • (2008) Free Radic. Biol. Med , vol.44 , pp. 1935-1944
    • Huang, Z.1
  • 21
    • 84866726957 scopus 로고    scopus 로고
    • Lipidomics identifies cardiolipin oxidation as a mitochondrial target for redox therapy of brain injury
    • Ji, J. et al. Lipidomics identifies cardiolipin oxidation as a mitochondrial target for redox therapy of brain injury. Nat. Neurosci. 15, 1407-1413 (2012).
    • (2012) Nat. Neurosci , vol.15 , pp. 1407-1413
    • Ji, J.1
  • 22
    • 84862777560 scopus 로고    scopus 로고
    • Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein
    • Huang, W. et al. Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein. Cell Res. 22, 473-489 (2012).
    • (2012) Cell Res , vol.22 , pp. 473-489
    • Huang, W.1
  • 23
    • 84870013071 scopus 로고    scopus 로고
    • Voltage- dependent anion channels (vdacs) recruit parkin to defective mitochondria to promote mitochondrial autophagy
    • Sun, Y., Vashisht, A. A., Tchieu, J., Wohlschlegel, J. A. & Dreier, L. Voltage- dependent Anion Channels (VDACs) Recruit Parkin to defective mitochondria to promote mitochondrial autophagy. J. Biol. Chem. 287, 40652-40660 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 40652-40660
    • Sun, Y.1    Vashisht, A.A.2    Tchieu, J.3    Wohlschlegel, J.A.4    Dreier, L.5
  • 24
    • 75949130828 scopus 로고    scopus 로고
    • PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
    • Geisler, S. et al. PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nat. Cell Biol. 12, 119-131 (2010).
    • (2010) Nat. Cell Biol , vol.12 , pp. 119-131
    • Geisler, S.1
  • 25
    • 78649636176 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1- induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria
    • Wirawan, E. et al. Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1- induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria. Cell Death Dis. 1, e18 (2010).
    • (2010) Cell Death Dis , vol.1
    • Wirawan, E.1
  • 26
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • Matsuda, N. et al. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J. Cell Biol. 189, 211-221 (2010).
    • (2010) J. Cell Biol , vol.189 , pp. 211-221
    • Matsuda, N.1
  • 27
    • 75949098487 scopus 로고    scopus 로고
    • PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
    • Vives-Bauza, C. et al. PINK1-dependent recruitment of Parkin to mitochondria in mitophagy. Proc. Natl Acad. Sci. USA 107, 378-383 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 378-383
    • Vives-Bauza, C.1
  • 28
    • 75749156257 scopus 로고    scopus 로고
    • PINK1 is selectively stabilized on impaired mitochondria to activate Parkin
    • Narendra, D. P. et al. PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol. 8, e1000298 (2010).
    • (2010) PLoS Biol , vol.8
    • Narendra, D.P.1
  • 29
    • 84864267876 scopus 로고    scopus 로고
    • PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
    • Kondapalli, C. et al. PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65. Open Biol. 2, 120080 (2012).
    • (2012) Open Biol , vol.2 , pp. 120080
    • Kondapalli, C.1
  • 30
    • 77954695260 scopus 로고    scopus 로고
    • P62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria
    • Okatsu, K. et al. p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria. Genes Cells 15, 887-900 (2010).
    • (2010) Genes Cells , vol.15 , pp. 887-900
    • Okatsu, K.1
  • 31
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen, T. & Lamark, T. Selective autophagy mediated by autophagic adapter proteins. Autophagy 7, 279-296 (2011).
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 32
    • 52649121942 scopus 로고    scopus 로고
    • The N-terminus and Phe52 residue of LC3 recruit p62/SQSTM1 into autophagosomes
    • Shvets, E., Fass, E., Scherz-Shouval, R. & Elazar, Z. The N-terminus and Phe52 residue of LC3 recruit p62/SQSTM1 into autophagosomes. J. Cell Sci. 121, 2685-2695 (2008).
    • (2008) J. Cell Sci , vol.121 , pp. 2685-2695
    • Shvets, E.1    Fass, E.2    Scherz-Shouval, R.3    Elazar, Z.4
  • 33
    • 79551603345 scopus 로고    scopus 로고
    • Bioenergetics of neurons inhibit the translocation response of Parkin following rapid mitochondrial depolarization
    • Van Laar, V. S. et al. Bioenergetics of neurons inhibit the translocation response of Parkin following rapid mitochondrial depolarization. Human Mol. Genet. 20, 927-940 (2011).
    • (2011) Human Mol. Genet , vol.20 , pp. 927-940
    • Van Laar, V.S.1
  • 34
    • 84858701257 scopus 로고    scopus 로고
    • Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons
    • Cai, Q., Zakaria, H. M., Simone, A. & Sheng, Z. H. Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons. Curr. Biol. 22, 545-552 (2012).
    • (2012) Curr. Biol , vol.22 , pp. 545-552
    • Cai, Q.1    Zakaria, H.M.2    Simone, A.3    Sheng, Z.H.4
  • 35
    • 74049153002 scopus 로고    scopus 로고
    • Nix is a selective autophagy receptor for mitochondrial clearance
    • Novak, I. et al. Nix is a selective autophagy receptor for mitochondrial clearance. EMBO Rep. 11, 45-51 (2010).
    • (2010) EMBO Rep , vol.11 , pp. 45-51
    • Novak, I.1
  • 36
    • 84861733247 scopus 로고    scopus 로고
    • Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy
    • Hanna, R. A. et al. Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy. J. Biol. Chem. 287, 19094-19104 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 19094-19104
    • Hanna, R.A.1
  • 37
    • 84868596965 scopus 로고    scopus 로고
    • Intramitochondrial transport of phosphatidic acid in yeast by a lipid transfer protein
    • Connerth, M. et al. Intramitochondrial transport of phosphatidic acid in yeast by a lipid transfer protein. Science 338, 815-818 (2012).
    • (2012) Science , vol.338 , pp. 815-818
    • Connerth, M.1
  • 38
    • 0037404152 scopus 로고    scopus 로고
    • Macrophage recognition of externalized phosphatidylserine and phagocytosis of apoptotic Jurkat cells-existence of a threshold
    • Borisenko, G. G. et al. Macrophage recognition of externalized phosphatidylserine and phagocytosis of apoptotic Jurkat cells-existence of a threshold. Arch. Biochem. Biophys. 413, 41-52 (2003).
    • (2003) Arch. Biochem. Biophys , vol.413 , pp. 41-52
    • Borisenko, G.G.1
  • 39
    • 77956255766 scopus 로고    scopus 로고
    • Find-me and eat-me signals in apoptotic cell clearance: Progress and conundrums
    • Ravichandran, K. S. Find-me and eat-me signals in apoptotic cell clearance: progress and conundrums. J. Exp. Med. 207, 1807-1817 (2010).
    • (2010) J. Exp. Med , vol.207 , pp. 1807-1817
    • Ravichandran K., .S.1
  • 40
    • 33845983303 scopus 로고    scopus 로고
    • Voltage gating of VDAC is regulated by nonlamellar lipids of mitochondrial membranes
    • Rostovtseva, T. K., Kazemi, N., Weinrich, M. & Bezrukov, S. M. Voltage gating of VDAC is regulated by nonlamellar lipids of mitochondrial membranes. J. Biol. Chem. 281, 37496-37506 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 37496-37506
    • Rostovtseva, T.K.1    Kazemi, N.2    Weinrich, M.3    Bezrukov, S.M.4
  • 41
    • 33847420521 scopus 로고    scopus 로고
    • AMP-activated protein kinase alpha2 deficiency affects cardiac cardiolipin homeostasis and mitochondrial function
    • Athea, Y. et al. AMP-activated protein kinase alpha2 deficiency affects cardiac cardiolipin homeostasis and mitochondrial function. Diabetes 56, 786-794 (2007).
    • (2007) Diabetes , vol.56 , pp. 786-794
    • Athea, Y.1
  • 42
    • 84862948331 scopus 로고    scopus 로고
    • AMPK directly inhibits NDPK through a phosphoserine switch to maintain cellular homeostasis
    • Onyenwoke, R. U. et al. AMPK directly inhibits NDPK through a phosphoserine switch to maintain cellular homeostasis. Mol. Biol. Cell 23, 381-389 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 381-389
    • Onyenwoke, R.U.1
  • 43
    • 84872094603 scopus 로고    scopus 로고
    • Dual function of mitochondrial Nm23-H4 in phosphotransfer and intermembrane lipid transfer: A cardiolipin-dependent switch
    • Schlattner, U. et al. Dual function of mitochondrial Nm23-H4 in phosphotransfer and intermembrane lipid transfer: a cardiolipin-dependent switch. J. Biol. Chem. 288, 111-121 (2013).
    • (2013) J. Biol. Chem , vol.288 , pp. 111-121
    • Schlattner, U.1
  • 44
    • 0033571223 scopus 로고    scopus 로고
    • Ca(2C) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine
    • Verdaguer, N., Corbalan-Garcia, S., Ochoa, W. F., Fita, I. & Gomez-Fernandez, J. C. Ca(2C) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine. EMBO J. 18, 6329-6338 (1999).
    • (1999) EMBO J. , vol.18 , pp. 6329-6338
    • Verdaguer, N.1    Corbalan-Garcia, S.2    Ochoa, W.F.3    Fita, I.4    Gomez-Fernandez, J.C.5
  • 45
    • 67649399288 scopus 로고    scopus 로고
    • Loss of pink1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission
    • Dagda, R. K. et al. Loss of pink1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J. Biol. Chem. 284, 13843-13855 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 13843-13855
    • Dagda, R.K.1
  • 46
    • 79960804104 scopus 로고    scopus 로고
    • Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth
    • Wild, P. et al. Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. Science 333, 228-233 (2011).
    • (2011) Science , vol.333 , pp. 228-233
    • Wild, P.1
  • 47
    • 27744433524 scopus 로고    scopus 로고
    • Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors
    • Kagan, V. E. et al. Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors. Nat. Chem. Biol. 1, 223-232 (2005).
    • (2005) Nat. Chem. Biol , vol.1 , pp. 223-232
    • Kagan, V.E.1
  • 48
    • 56749103104 scopus 로고    scopus 로고
    • Mass-spectrometric characterization of phospholipids and their primary peroxidation products in rat cortical neurons during staurosporine-induced apoptosis
    • Tyurin, V. A. et al. Mass-spectrometric characterization of phospholipids and their primary peroxidation products in rat cortical neurons during staurosporine-induced apoptosis. J. Neurochem. 107, 1614-1633 (2008).
    • (2008) J. Neurochem , vol.107 , pp. 1614-1633
    • Tyurin, V.A.1
  • 49
    • 80054752820 scopus 로고    scopus 로고
    • Monitoring mitophagy in neuronal cell cultures
    • Zhu, J., Dagda, R. K. & Chu, C. T. Monitoring mitophagy in neuronal cell cultures. Methods Mol. Biol. 793, 325-339 (2011).
    • (2011) Methods Mol. Biol , vol.793 , pp. 325-339
    • Zhu, J.1    Dagda, R.K.2    Chu, C.T.3
  • 50
    • 0034633952 scopus 로고    scopus 로고
    • Structural basis of the anionic interface preference and kcat activation of pancreatic phospholipase A2
    • Yu, B. Z. et al. Structural basis of the anionic interface preference and kcat activation of pancreatic phospholipase A2. Biochemistry 39, 12312-12323 (2000).
    • (2000) Biochemistry , vol.39 , pp. 12312-12323
    • Yu, B.Z.1
  • 51
    • 0017575028 scopus 로고
    • Transverse asymmetry of phospholipids in subcellular membranes of rat liver
    • Nilsson, O. S. & Dallner, G. Transverse asymmetry of phospholipids in subcellular membranes of rat liver. Biochim. Biophys. Acta 464, 453-458 (1977).
    • (1977) Biochim. Biophys. Acta , vol.464 , pp. 453-458
    • Nilsson, O.S.1    Dallner, G.2
  • 52
    • 34347236921 scopus 로고    scopus 로고
    • Organelle isolation: Functional mitochondria from mouse liver, muscle and cultured fibroblasts
    • Frezza, C., Cipolat, S. & Scorrano, L. Organelle isolation: functional mitochondria from mouse liver, muscle and cultured fibroblasts. Nat. Protoc. 2, 287-295 (2007).
    • (2007) Nat. Protoc , vol.2 , pp. 287-295
    • Frezza, C.1    Cipolat, S.2    Scorrano, L.3
  • 53
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O. & Olson, A. J. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31, 455-461 (2010).
    • (2010) J. Comput. Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 54
    • 0033397980 scopus 로고    scopus 로고
    • Python: A programming language for software integration and development
    • Sanner, M. F. Python: a programming language for software integration and development. J. Mol. Graph. Model. 17, 57-61 (1999).
    • (1999) J. Mol. Graph. Model , vol.17 , pp. 57-61
    • Sanner M., .F.1
  • 55
    • 0037255072 scopus 로고    scopus 로고
    • The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003
    • Boeckmann, B. et al. The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003. Nucleic Acids Res. 31, 365-370 (2003).
    • (2003) Nucleic Acids Res , vol.31 , pp. 365-370
    • Boeckmann, B.1
  • 57
    • 2142738304 scopus 로고    scopus 로고
    • Weblogo: A sequence logo generator
    • Crooks, G. E., Hon, G. & Chandonia, J. M. WebLogo: a sequence logo generator. Genome Res. 14, 1188-1190 (2004).
    • (2004) Genome Res , vol.14 , pp. 1188-1190
    • Crooks, G.E.1    Hon, G.2    Chandonia, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.