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Volumn 10, Issue , 2017, Pages

Mitophagy failure in fibroblasts and iPSC-derived neurons of alzheimer’s disease-associated presenilin 1 mutation

Author keywords

Alzheimer s disease; Fibroblasts; IPSC derived neurons; Mitophagy; Presenilin 1 mutation

Indexed keywords

PRESENILIN 1;

EID: 85032360002     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2017.00291     Document Type: Article
Times cited : (86)

References (42)
  • 1
    • 84875831024 scopus 로고    scopus 로고
    • A preliminary study of the whole-genome expression profile of sporadic and monogenic early-onset Alzheimer’s disease
    • Antonell, A., Llado, A., Altirriba, J., Botta-Orfila, T., Balasa, M., Fernández, M., et al. (2013). A preliminary study of the whole-genome expression profile of sporadic and monogenic early-onset Alzheimer’s disease. Neurobiol. Aging 34, 1772–1778. doi: 10.1016/j.neurobiolaging.2012.12.026
    • (2013) Neurobiol. Aging , vol.34 , pp. 1772-1778
    • Antonell, A.1    Llado, A.2    Altirriba, J.3    Botta-Orfila, T.4    Balasa, M.5    Fernández, M.6
  • 2
    • 34548510854 scopus 로고    scopus 로고
    • 2-Amino-3, 4-dihydroquinazolines as inhibitors of BACE-1 (β-site APP cleaving enzyme): Use of structure based design to convert a micromolar hit into a nanomolar lead
    • Baxter, E. W., Conway, K. A., Kennis, L., Bischoff, F., Mercken, M. H., Winter, H. L., et al. (2007). 2-Amino-3, 4-dihydroquinazolines as inhibitors of BACE-1 (β-site APP cleaving enzyme): use of structure based design to convert a micromolar hit into a nanomolar lead. J. Med. Chem. 50, 4261–4264. doi: 10.1021/jm0705408
    • (2007) J. Med. Chem , vol.50 , pp. 4261-4264
    • Baxter, E.W.1    Conway, K.A.2    Kennis, L.3    Bischoff, F.4    Mercken, M.H.5    Winter, H.L.6
  • 3
    • 27944504351 scopus 로고    scopus 로고
    • P62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., et al. (2005). p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171, 603–614. doi: 10.1083/jcb.200507002
    • (2005) J. Cell Biol , vol.171 , pp. 603-614
    • Bjørkøy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Øvervatn, A.6
  • 4
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimer’s disease-linked presenilin 1 variants elevate Aβ1–42/1–40 ratio in vitro and in vivo
    • Borchelt, D. R., Thinakaran, G., Eckman, C. B., Lee, M. K., Davenport, F., Ratovitsky, T., et al. (1996). Familial Alzheimer’s disease-linked presenilin 1 variants elevate Aβ1–42/1–40 ratio in vitro and in vivo. Neuron 17, 1005–1013. doi: 10.1016/s0896-6273(00)80230-5
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1    Thinakaran, G.2    Eckman, C.B.3    Lee, M.K.4    Davenport, F.5    Ratovitsky, T.6
  • 5
    • 0030836345 scopus 로고    scopus 로고
    • Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer’s disease: Neuropathologic evidence for a mechanism of increased β-amyloidogenesis
    • Cataldo, A. M., Barnett, J. L., Pieroni, C., and Nixon, R. A. (1997). Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer’s disease: neuropathologic evidence for a mechanism of increased β-amyloidogenesis. J. Neurosci. 17, 6142–6151.
    • (1997) J. Neurosci , vol.17 , pp. 6142-6151
    • Cataldo, A.M.1    Barnett, J.L.2    Pieroni, C.3    Nixon, R.A.4
  • 6
    • 84865086929 scopus 로고    scopus 로고
    • Lysosomal calcium homeostasis defects, not proton pump defects, cause endo-lysosomal dysfunction in PSEN-deficient cells
    • Coen, K., Flannagan, R. S., Baron, S., Carraro-Lacroix, L. R., Wang, D., Vermeire, W., et al. (2012). Lysosomal calcium homeostasis defects, not proton pump defects, cause endo-lysosomal dysfunction in PSEN-deficient cells. J. Cell Biol. 198, 23–35. doi: 10.1083/jcb.201201076
    • (2012) J. Cell Biol , vol.198 , pp. 23-35
    • Coen, K.1    Flannagan, R.S.2    Baron, S.3    Carraro-Lacroix, L.R.4    Wang, D.5    Vermeire, W.6
  • 7
    • 84896730305 scopus 로고    scopus 로고
    • Lysosomal alkalization and dysfunction in human fibroblasts with the Alzheimer’s disease-linked presenilin 1 A246E mutation can be reversed with cAMP
    • Coffey, E. E., Beckel, J. M., Laties, A. M., and Mitchell, C. H. (2014). Lysosomal alkalization and dysfunction in human fibroblasts with the Alzheimer’s disease-linked presenilin 1 A246E mutation can be reversed with cAMP. Neuroscience 263, 111–124. doi: 10.1016/j.neuroscience.2014.01.001
    • (2014) Neuroscience , vol.263 , pp. 111-124
    • Coffey, E.E.1    Beckel, J.M.2    Laties, A.M.3    Mitchell, C.H.4
  • 8
    • 6844255860 scopus 로고    scopus 로고
    • Estimation of the genetic contribution of presenilin-1 and -2 mutations in a population-based study of presenile Alzheimer disease
    • Cruts, M., van Duijn, C. M., Backhovens, H., Van den Broeck, M., Wehnert, A., Serneels, S., et al. (1998). Estimation of the genetic contribution of presenilin-1 and -2 mutations in a population-based study of presenile Alzheimer disease. Hum. Mol. Genet. 7, 43–51. doi: 10.1093/hmg/7.1.43
    • (1998) Hum. Mol. Genet , vol.7 , pp. 43-51
    • Cruts, M.1    Van Duijn, C.M.2    Backhovens, H.3    Van Den Broeck, M.4    Wehnert, A.5    Serneels, S.6
  • 9
    • 67649399288 scopus 로고    scopus 로고
    • Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission
    • Dagda, R. K., Cherra, S. J. III, Kulich, S. M., Tandon, A., Park, D., and Chu, C. T. (2009). Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J. Biol. Chem. 284, 13843–13855. doi: 10.1074/jbc.M808515200
    • (2009) J. Biol. Chem , vol.284 , pp. 13843-13855
    • Dagda, R.K.1    Cherra, S.2    Kulich, S.M.3    Tandon, A.4    Park, D.5    Chu, C.T.6
  • 10
    • 84867097233 scopus 로고    scopus 로고
    • Diversity of plant evolutionary lineages promotes arthropod diversity
    • Dinnage, R., Cadotte, M. W., Haddad, N. M., Crutsinger, G. M., and Tilman, D. (2012). Diversity of plant evolutionary lineages promotes arthropod diversity. Ecol. Lett. 15, 1308–1317. doi: 10.1111/j.1461-0248.2012.01854.x
    • (2012) Ecol. Lett , vol.15 , pp. 1308-1317
    • Dinnage, R.1    Cadotte, M.W.2    Haddad, N.M.3    Crutsinger, G.M.4    Tilman, D.5
  • 11
    • 0035163347 scopus 로고    scopus 로고
    • Functional γ-secretase inhibitors reduce β-amyloid peptide levels in brain
    • Dovey, H. F., John, V., Anderson, J. P., Chen, L. Z., de Saint Andrieu, P., Fang, L. Y., et al. (2001). Functional γ-secretase inhibitors reduce β-amyloid peptide levels in brain. J. Neurochem. 76, 173–181. doi: 10.1046/j.1471-4159.2001.00012.x
    • (2001) J. Neurochem , vol.76 , pp. 173-181
    • Dovey, H.F.1    John, V.2    Anderson, J.P.3    Chen, L.Z.4    De Saint Andrieu, P.5    Fang, L.Y.6
  • 12
    • 84894599877 scopus 로고    scopus 로고
    • Cytosolic cleaved PINK1 represses Parkin translocation to mitochondria and mitophagy
    • Fedorowicz, M. A., de Vries-Schneider, R. L., Rüb, C., Becker, D., Huang, Y., Zhou, C., et al. (2014). Cytosolic cleaved PINK1 represses Parkin translocation to mitochondria and mitophagy. EMBO Rep. 15, 86–93. doi: 10.1002/embr.201337294
    • (2014) EMBO Rep , vol.15 , pp. 86-93
    • Fedorowicz, M.A.1    De Vries-Schneider, R.L.2    Rüb, C.3    Becker, D.4    Huang, Y.5    Zhou, C.6
  • 13
    • 78649463381 scopus 로고    scopus 로고
    • Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy
    • Gegg, M. E., Cooper, J. M., Chau, K. Y., Rojo, M., Schapira, A. H., and Taanman, J. W. (2010). Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy. Hum. Mol. Genet. 19, 4861–4870. doi: 10.1093/hmg/ddq419
    • (2010) Hum. Mol. Genet , vol.19 , pp. 4861-4870
    • Gegg, M.E.1    Cooper, J.M.2    Chau, K.Y.3    Rojo, M.4    Schapira, A.H.5    Taanman, J.W.6
  • 15
    • 79957850849 scopus 로고    scopus 로고
    • Following autophagy step by step
    • Hansen, T. E., and Johansen, T. (2011). Following autophagy step by step. BMC Biol. 9:39. doi: 10.1186/1741-7007-9-39
    • (2011) BMC Biol , vol.9 , pp. 39
    • Hansen, T.E.1    Johansen, T.2
  • 16
    • 0033844395 scopus 로고    scopus 로고
    • The expression of presenilin 1 mRNA in skin fibroblasts and brains from sporadic Alzheimer’s disease
    • Ikeda, K., Urakami, K., Arai, H., Wada, K., Wakutani, Y., Ji, Y., et al. (2000). The expression of presenilin 1 mRNA in skin fibroblasts and brains from sporadic Alzheimer’s disease. Dement. Geriatr. Cogn. Disord. 11, 245–250. doi: 10.1159/000017246
    • (2000) Dement. Geriatr. Cogn. Disord , vol.11 , pp. 245-250
    • Ikeda, K.1    Urakami, K.2    Arai, H.3    Wada, K.4    Wakutani, Y.5    Ji, Y.6
  • 17
    • 85013763791 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
    • Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., et al. (2016). Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy 12, 1–222. doi: 10.1080/15548627.2015.1100356
    • (2016) Autophagy , vol.12 , pp. 1-222
    • Klionsky, D.J.1    Abdelmohsen, K.2    Abe, A.3    Abedin, M.J.4    Abeliovich, H.5    Acevedo Arozena, A.6
  • 18
    • 0036284021 scopus 로고    scopus 로고
    • Early accumulation of p62 in neurofibrillary tangles in Alzheimer’s disease: Possible role in tangle formation
    • Kuusisto, E., Salminen, A., and Alafuzoff, I. (2002). Early accumulation of p62 in neurofibrillary tangles in Alzheimer’s disease: possible role in tangle formation. Neuropathol. Appl. Neurobiol. 28, 228–237. doi: 10.1046/j.1365-2990.2002.00394.x
    • (2002) Neuropathol. Appl. Neurobiol , vol.28 , pp. 228-237
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 19
    • 0034805395 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells
    • Kuusisto, E., Suuronen, T., and Salminen, A. (2001). Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells. Biochem. Biophys. Res. Commun. 280, 223–228. doi: 10.1006/bbrc.2000.4107
    • (2001) Biochem. Biophys. Res. Commun , vol.280 , pp. 223-228
    • Kuusisto, E.1    Suuronen, T.2    Salminen, A.3
  • 20
    • 84940796652 scopus 로고    scopus 로고
    • Presenilin 1 maintains lysosomal Ca2+ homeostasis via TRPML1 by regulating vATPase-mediated lysosome acidification
    • Lee, J. H., McBrayer, M. K., Wolfe, D. M., Haslett, L. J., Kumar, A., Sato, Y., et al. (2015). Presenilin 1 maintains lysosomal Ca2+ homeostasis via TRPML1 by regulating vATPase-mediated lysosome acidification. Cell Rep. 12, 1430–1444. doi: 10.1016/j.celrep.2015.07.050
    • (2015) Cell Rep , vol.12 , pp. 1430-1444
    • Lee, J.H.1    McBrayer, M.K.2    Wolfe, D.M.3    Haslett, L.J.4    Kumar, A.5    Sato, Y.6
  • 21
    • 10544229795 scopus 로고    scopus 로고
    • Expression of presenilin 1 and 2 (PS1 and PS2) in human and murine tissues
    • Lee, M. K., Slunt, H. H., Martin, L. J., Thinakaran, G., Kim, G., Gandy, S. E., et al. (1996). Expression of presenilin 1 and 2 (PS1 and PS2) in human and murine tissues. J. Neurosci. 16, 7513–7525.
    • (1996) J. Neurosci , vol.16 , pp. 7513-7525
    • Lee, M.K.1    Slunt, H.H.2    Martin, L.J.3    Thinakaran, G.4    Kim, G.5    Gandy, S.E.6
  • 22
    • 77953913051 scopus 로고    scopus 로고
    • Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations
    • Lee, J. H., Yu, W. H., Kumar, A., Lee, S., Mohan, P. S., Peterhoff, C. M., et al. (2010). Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations. Cell 141, 1146–1158. doi: 10.1016/j.cell.2010.05.008
    • (2010) Cell , vol.141 , pp. 1146-1158
    • Lee, J.H.1    Yu, W.H.2    Kumar, A.3    Lee, S.4    Mohan, P.S.5    Peterhoff, C.M.6
  • 23
    • 16844366524 scopus 로고    scopus 로고
    • Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging
    • Lemasters, J. J. (2005). Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging. Rejuvenation Res. 8, 3–5. doi: 10.1089/rej.2005.8.3
    • (2005) Rejuvenation Res , vol.8 , pp. 3-5
    • Lemasters, J.J.1
  • 24
    • 85012845547 scopus 로고    scopus 로고
    • PARK2 enhancement is able to compensate mitophagy alterations found in sporadic Alzheimer’s disease
    • Martín-Maestro, P., Gargini, R., Perry, G., Avila, J., and García-Escudero, V. (2016). PARK2 enhancement is able to compensate mitophagy alterations found in sporadic Alzheimer’s disease. Hum. Mol. Genet. 25, 792–806. doi: 10.1093/hmg/ddv616
    • (2016) Hum. Mol. Genet , vol.25 , pp. 792-806
    • Martín-Maestro, P.1    Gargini, R.2    Perry, G.3    Avila, J.4    García-Escudero, V.5
  • 26
    • 35848931249 scopus 로고    scopus 로고
    • Increased autophagic degradation of mitochondria in Alzheimer disease
    • Moreira, P. I., Siedlak, S. L., Wang, X., Santos, M. S., Oliveira, C. R., Tabaton, M., et al. (2007b). Increased autophagic degradation of mitochondria in Alzheimer disease. Autophagy 3, 614–615. doi: 10.4161/auto.4872
    • (2007) Autophagy , vol.3 , pp. 614-615
    • Moreira, P.I.1    Siedlak, S.L.2    Wang, X.3    Santos, M.S.4    Oliveira, C.R.5    Tabaton, M.6
  • 27
    • 75749156257 scopus 로고    scopus 로고
    • PINK1 is selectively stabilized on impaired mitochondria to activate Parkin
    • Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D. F., Gautier, C. A., Shen, J., et al. (2010). PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol. 8:e1000298. doi: 10.1371/journal.pbio.1000298
    • (2010) Plos Biol , vol.8
    • Narendra, D.P.1    Jin, S.M.2    Tanaka, A.3    Suen, D.F.4    Gautier, C.A.5    Shen, J.6
  • 28
    • 34548259958 scopus 로고    scopus 로고
    • P62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy
    • Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J. A., Outzen, H., et al. (2007). p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J. Biol. Chem. 282, 24131–24145. doi: 10.1074/jbc.M702824200
    • (2007) J. Biol. Chem , vol.282 , pp. 24131-24145
    • Pankiv, S.1    Clausen, T.H.2    Lamark, T.3    Brech, A.4    Bruun, J.A.5    Outzen, H.6
  • 29
    • 84904976176 scopus 로고    scopus 로고
    • A time course analysis of the electrophysiological properties of neurons differentiated from human induced pluripotent stem cells (IPSCs)
    • Prè, D., Nestor, M. W., Sproul, A. A., Jacob, S., Koppensteiner, P., Chinchalongporn, V., et al. (2014). A time course analysis of the electrophysiological properties of neurons differentiated from human induced pluripotent stem cells (iPSCs). PLoS One 9:e103418. doi: 10.1371/journal.pone.0103418
    • (2014) Plos One , vol.9
    • Prè, D.1    Nestor, M.W.2    Sproul, A.A.3    Jacob, S.4    Koppensteiner, P.5    Chinchalongporn, V.6
  • 31
    • 84857029592 scopus 로고    scopus 로고
    • Abnormal accumulation of autophagic vesicles correlates with axonal and synaptic pathology in young Alzheimer’s mice hippocampus
    • Sanchez-Varo, R., Trujillo-Estrada, L., Sanchez-Mejias, E., Torres, M., Baglietto-Vargas, D., Moreno-Gonzalez, I., et al. (2012). Abnormal accumulation of autophagic vesicles correlates with axonal and synaptic pathology in young Alzheimer’s mice hippocampus. Acta Neuropathol.123, 53–70. doi: 10.1007/s00401-011-0896-x
    • (2012) Acta Neuropathol , vol.123 , pp. 53-70
    • Sanchez-Varo, R.1    Trujillo-Estrada, L.2    Sanchez-Mejias, E.3    Torres, M.4    Baglietto-Vargas, D.5    Moreno-Gonzalez, I.6
  • 32
  • 33
    • 84928753296 scopus 로고    scopus 로고
    • Quantification of cellular viability by automated microscopy and flow cytometry
    • Sauvat, A., Wang, Y., Segura, F., Spaggiari, S., Muller, K., Zhou, H., et al. (2015). Quantification of cellular viability by automated microscopy and flow cytometry. Oncotarget 6, 9467–9475. doi: 10.18632/oncotarget.3266
    • (2015) Oncotarget , vol.6 , pp. 9467-9475
    • Sauvat, A.1    Wang, Y.2    Segura, F.3    Spaggiari, S.4    Muller, K.5    Zhou, H.6
  • 34
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early-onset familial Alzheimer’s disease
    • Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., et al. (1995). Cloning of a gene bearing missense mutations in early-onset familial Alzheimer’s disease. Nature 375, 754–760. doi: 10.1038/375754a0
    • (1995) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3    Rogaeva, E.A.4    Levesque, G.5    Ikeda, M.6
  • 35
    • 84943361972 scopus 로고    scopus 로고
    • Being human: The role of pluripotent stem cells in regenerative medicine and humanizing Alzheimer’s disease models
    • Sproul, A. A. (2015). Being human: the role of pluripotent stem cells in regenerative medicine and humanizing Alzheimer’s disease models. Mol. Aspects Med. 43–44, 54–65. doi: 10.1016/j.mam.2015.06.007
    • (2015) Mol. Aspects Med , vol.4344 , pp. 54-65
    • Sproul, A.A.1
  • 36
    • 84897136184 scopus 로고    scopus 로고
    • Characterization and molecular profiling of PSEN1 familial Alzheimer’s disease iPSC-derived neural progenitors
    • Sproul, A. A., Jacob, S., Pre, D., Kim, S. H., Nestor, M. W., Navarro-Sobrino, M., et al. (2014). Characterization and molecular profiling of PSEN1 familial Alzheimer’s disease iPSC-derived neural progenitors. PLoS One 9:e84547. doi: 10.1371/journal.pone.0084547
    • (2014) Plos One , vol.9
    • Sproul, A.A.1    Jacob, S.2    Pre, D.3    Kim, S.H.4    Nestor, M.W.5    Navarro-Sobrino, M.6
  • 37
    • 77950499364 scopus 로고    scopus 로고
    • Parkin-mediated selective mitochondrial autophagy, mitophagy: Parkin purges damaged organelles from the vital mitochondrial network
    • Tanaka, A. (2010). Parkin-mediated selective mitochondrial autophagy, mitophagy: parkin purges damaged organelles from the vital mitochondrial network. FEBS Lett. 584, 1386–1392. doi: 10.1016/j.febslet.2010.02.060
    • (2010) FEBS Lett , vol.584 , pp. 1386-1392
    • Tanaka, A.1
  • 39
    • 84961770670 scopus 로고    scopus 로고
    • Synaptosomal mitochondrial dysfunction in 5xFAD mouse model of Alzheimer’s disease
    • Wang, L., Guo, L., Lu, L., Sun, H., Shao, M., Beck, S. J., et al. (2016). Synaptosomal mitochondrial dysfunction in 5xFAD mouse model of Alzheimer’s disease. PLoS One 11:e0150441. doi: 10.1371/journal.pone.0150441
    • (2016) Plos One , vol.11
    • Wang, L.1    Guo, L.2    Lu, L.3    Sun, H.4    Shao, M.5    Beck, S.J.6
  • 40
    • 84879232282 scopus 로고    scopus 로고
    • Autophagy failure in Alzheimer’s disease and the role of defective lysosomal acidification
    • Wolfe, D. M., Lee, J. H., Kumar, A., Lee, S., Orenstein, S. J., and Nixon, R. A. (2013). Autophagy failure in Alzheimer’s disease and the role of defective lysosomal acidification. Eur. J. Neurosci. 37, 1949–1961. doi: 10.1111/ejn.12169
    • (2013) Eur. J. Neurosci , vol.37 , pp. 1949-1961
    • Wolfe, D.M.1    Lee, J.H.2    Kumar, A.3    Lee, S.4    Orenstein, S.J.5    Nixon, R.A.6
  • 41
    • 84959481890 scopus 로고    scopus 로고
    • The ubiquitin signal and autophagy: An orchestrated dance leading to mitochondrial degradation
    • Yamano, K., Matsuda, N., and Tanaka, K. (2016). The ubiquitin signal and autophagy: an orchestrated dance leading to mitochondrial degradation. EMBO Rep. 17, 300–316. doi: 10.15252/embr.201541486
    • (2016) EMBO Rep , vol.17 , pp. 300-316
    • Yamano, K.1    Matsuda, N.2    Tanaka, K.3
  • 42
    • 84927917189 scopus 로고    scopus 로고
    • Parkin-mediated mitophagy in mutant hAPP neurons and Alzheimer’s disease patient brains
    • Ye, X., Sun, X., Starovoytov, V., and Cai, Q. (2015). Parkin-mediated mitophagy in mutant hAPP neurons and Alzheimer’s disease patient brains. Hum. Mol. Genet. 24, 2938–2951. doi: 10.1093/hmg/ddv056
    • (2015) Hum. Mol. Genet , vol.24 , pp. 2938-2951
    • Ye, X.1    Sun, X.2    Starovoytov, V.3    Cai, Q.4


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