메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

ER-mitochondria associations are regulated by the VAPB-PTPIP51 interaction and are disrupted by ALS/FTD-associated TDP-43

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; GLYCOGEN SYNTHASE KINASE 3BETA; MITOCHONDRIAL PROTEIN; PROTEIN TYROSINE PHOSPHATASE INTERACTING PROTEIN 51; SYNAPTOBREVIN; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG; VESICLE ASSOCIATED MEMBRANE PROTEIN ASSOCIATED PROTEIN B; CALCIUM; DNA BINDING PROTEIN; FAM82A2 PROTEIN, HUMAN; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 BETA; MEMBRANE PROTEIN; PROTEIN TDP-43; PROTEIN TYROSINE PHOSPHATASE; PTPIP51 PROTEIN, MOUSE; TDP-43 PROTEIN, HUMAN; TDP-43 PROTEIN, MOUSE; VAPB PROTEIN, HUMAN; VAPB PROTEIN, MOUSE; VESICULAR TRANSPORT PROTEIN;

EID: 84901925681     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4996     Document Type: Article
Times cited : (469)

References (59)
  • 4
    • 84866728707 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mitochondria contacts: Function of the junction
    • Rowland, A. A. & Voeltz, G. K. Endoplasmic reticulum-mitochondria contacts: function of the junction. Nat. Rev. Mol. Cell Biol. 13, 607-625 (2012).
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 607-625
    • Rowland, A.A.1    Voeltz, G.K.2
  • 5
    • 84883451708 scopus 로고    scopus 로고
    • The molecular hug between the ER and the mitochondria
    • Kornmann, B. The molecular hug between the ER and the mitochondria. Curr. Opin. Cell Biol. 25, 443-448 (2013).
    • (2013) Curr. Opin. Cell Biol. , vol.25 , pp. 443-448
    • Kornmann, B.1
  • 6
    • 77953725586 scopus 로고    scopus 로고
    • Oxidative protein folding in the endoplasmic reticulum: Tight links to the mitochondria-associated membrane (MAM)
    • Simmen, T., Lynes, E. M., Gesson, K. & Thomas, G. Oxidative protein folding in the endoplasmic reticulum: Tight links to the mitochondria-associated membrane (MAM). Biochim. Biophys. Acta 1798, 1465-1473 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1465-1473
    • Simmen, T.1    Lynes, E.M.2    Gesson, K.3    Thomas, G.4
  • 7
    • 84875365804 scopus 로고    scopus 로고
    • Autophagosomes form at ER-mitochondria contact sites
    • Hamasaki, M. et al. Autophagosomes form at ER-mitochondria contact sites. Nature 495, 389-393 (2013).
    • (2013) Nature , vol.495 , pp. 389-393
    • Hamasaki, M.1
  • 8
    • 84872769447 scopus 로고    scopus 로고
    • An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2
    • Korobova, F., Ramabhadran, V. & Higgs, H. N. An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2. Science 339, 464-467 (2013).
    • (2013) Science , vol.339 , pp. 464-467
    • Korobova, F.1    Ramabhadran, V.2    Higgs, H.N.3
  • 9
    • 67749122635 scopus 로고    scopus 로고
    • An ER-mitochondria tethering complex revealed by a synthetic biology screen
    • Kornmann, B. et al. An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science 325, 477-481 (2009).
    • (2009) Science , vol.325 , pp. 477-481
    • Kornmann, B.1
  • 10
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito, O. M. & Scorrano, L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 456, 605-610 (2008).
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 11
    • 84861554724 scopus 로고    scopus 로고
    • Alpha-synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulummitochondria interactions
    • Cali, T., Ottolini, D., Negro, A. & Brini, M. Alpha-synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulummitochondria interactions. J. Biol. Chem. 287, 17914-17929 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 17914-17929
    • Cali, T.1    Ottolini, D.2    Negro, A.3    Brini, M.4
  • 12
    • 84868524156 scopus 로고    scopus 로고
    • Upregulated function of mitochondria-associated ER membranes in Alzheimer disease
    • Area-Gomez, E. et al. Upregulated function of mitochondria-associated ER membranes in Alzheimer disease. EMBO J. 31, 4106-4123 (2012).
    • (2012) EMBO J. , vol.31 , pp. 4106-4123
    • Area-Gomez, E.1
  • 13
    • 79952600977 scopus 로고    scopus 로고
    • Presenilin 2 modulates endoplasmic reticulum (ER)-mitochondria interactions and Ca2 cross-talk
    • USA
    • Zampese, E. et al. Presenilin 2 modulates endoplasmic reticulum (ER)-mitochondria interactions and Ca2 cross-talk. Proc. Natl Acad. Sci. USA 108, 2777-2782 (2011).
    • (2011) Proc. Natl Acad. Sci , vol.108 , pp. 2777-2782
    • Zampese, E.1
  • 14
    • 84877337663 scopus 로고    scopus 로고
    • Modulation of the endoplasmic reticulum-mitochondria interface in Alzheimer's disease and related models
    • USA
    • Hedskog, L. et al. Modulation of the endoplasmic reticulum-mitochondria interface in Alzheimer's disease and related models. Proc. Natl Acad. Sci. USA 110, 7916-7921 (2013).
    • (2013) Proc. Natl Acad. Sci , vol.110 , pp. 7916-7921
    • Hedskog, L.1
  • 15
    • 84891410019 scopus 로고    scopus 로고
    • Alpha-Synuclein is localized to mitochondriaassociated ER membranes
    • Guardia-Laguarta, C. et al. alpha-Synuclein is localized to mitochondriaassociated ER membranes. J. Neurosci. 34, 249-259 (2014).
    • (2014) J. Neurosci. , vol.34 , pp. 249-259
    • Guardia-Laguarta, C.1
  • 16
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann, M. et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314, 130-113 (2006).
    • (2006) Science , vol.314 , pp. 130-113
    • Neumann, M.1
  • 17
    • 84864981763 scopus 로고    scopus 로고
    • Advances in understanding the molecular basis of frontotemporal dementia
    • Rademakers, R., Neumann, M. & Mackenzie, I. R. Advances in understanding the molecular basis of frontotemporal dementia. Nat. Rev. Neurol. 8, 423-434 (2012).
    • (2012) Nat. Rev. Neurol. , vol.8 , pp. 423-434
    • Rademakers, R.1    Neumann, M.2    Mackenzie, I.R.3
  • 18
    • 84861929838 scopus 로고    scopus 로고
    • TDP-43: Gumming up neurons through proteinprotein and protein-RNA interactions
    • Buratti, E. & Baralle, F. E. TDP-43: gumming up neurons through proteinprotein and protein-RNA interactions. Trends Biochem. Sci. 37, 237-247 (2012).
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 237-247
    • Buratti, E.1    Baralle, F.E.2
  • 19
    • 80755153025 scopus 로고    scopus 로고
    • TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies
    • Cohen, T. J., Lee, V. M. & Trojanowski, J. Q. TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies. Trends Mol. Med. 17, 659-667 (2011).
    • (2011) Trends Mol. Med. , vol.17 , pp. 659-667
    • Cohen, T.J.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 20
    • 84863393591 scopus 로고    scopus 로고
    • VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis
    • De Vos, K. J. et al. VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis. Hum. Mol. Genet. 21, 1299-1311 (2012).
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1299-1311
    • De Vos, K.J.1
  • 21
    • 84867003433 scopus 로고    scopus 로고
    • Mitofusin-2 independent juxtaposition of endoplasmic reticulum and mitochondria: An ultrastructural study
    • Cosson, P., Marchetti, A., Ravazzola, M. & Orci, L. Mitofusin-2 independent juxtaposition of endoplasmic reticulum and mitochondria: an ultrastructural study. PLoS ONE 7, e46293 (2012).
    • (2012) PLoS ONE , vol.7 , pp. 46293
    • Cosson, P.1    Marchetti, A.2    Ravazzola, M.3    Orci, L.4
  • 22
    • 77954301751 scopus 로고    scopus 로고
    • Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface
    • Csordas, G. et al. Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface. Mol. Cell 39, 121-132 (2010).
    • (2010) Mol. Cell , vol.39 , pp. 121-132
    • Csordas, G.1
  • 23
    • 2142765951 scopus 로고    scopus 로고
    • o, and N-Type Calcium Channel Complex at a Presynaptic Nerve Terminal: Analysis by Quantitative Immunocolocalization
    • DOI 10.1523/JNEUROSCI.0346-04.2004
    • Li, Q. et al. A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: analysis by quantitative immunocolocalization. J. Neurosci. 24, 4070-4081 (2004). (Pubitemid 38544233)
    • (2004) Journal of Neuroscience , vol.24 , Issue.16 , pp. 4070-4081
    • Li, Q.1    Lau, A.2    Morris, T.J.3    Guo, L.4    Fordyce, C.B.5    Stanley, E.F.6
  • 25
    • 77649269011 scopus 로고    scopus 로고
    • TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration
    • USA
    • Wils, H. et al. TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration. Proc. Natl Acad. Sci. USA 107, 3858-3863 (2010).
    • (2010) Proc. Natl Acad. Sci , vol.107 , pp. 3858-3863
    • Wils, H.1
  • 26
    • 77956199371 scopus 로고    scopus 로고
    • Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice
    • Xu, Y. F. et al. Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice. J. Neurosci. 30, 10851-10859 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 10851-10859
    • Xu, Y.F.1
  • 27
    • 80052936462 scopus 로고    scopus 로고
    • Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments
    • Swarup, V. et al. Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments. Brain 134, 2610-2626 (2011).
    • (2011) Brain , vol.134 , pp. 2610-2626
    • Swarup, V.1
  • 28
    • 77958022745 scopus 로고    scopus 로고
    • Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice
    • USA
    • Shan, X., Chiang, P. M., Price, D. L. & Wong, P. C. Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice. Proc. Natl Acad. Sci. USA 107, 16325-16330 (2010).
    • (2010) Proc. Natl Acad. Sci , vol.107 , pp. 16325-16330
    • Shan, X.1    Chiang, P.M.2    Price, D.L.3    Wong, P.C.4
  • 29
    • 81255127258 scopus 로고    scopus 로고
    • ALS-linked mutant VAPB enhances TDP-43-induced motor neuronal toxicity
    • Suzuki, H. & Matsuoka, M. ALS-linked mutant VAPB enhances TDP-43-induced motor neuronal toxicity. J. Neurochem. 119, 1099-1107 (2011).
    • (2011) J. Neurochem. , vol.119 , pp. 1099-1107
    • Suzuki, H.1    Matsuoka, M.2
  • 30
    • 81855172495 scopus 로고    scopus 로고
    • Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation
    • Ambegaokar, S. S. & Jackson, G. R. Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation. Hum. Mol. Genet. 20, 4947-4977 (2011).
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 4947-4977
    • Ambegaokar, S.S.1    Jackson, G.R.2
  • 32
    • 77950421249 scopus 로고    scopus 로고
    • Transgenic rat model of neurodegeneration caused by mutation in the TDP Gene
    • Zhou, H. et al. Transgenic rat model of neurodegeneration caused by mutation in the TDP Gene. PLoS Genet. 6, e1000887 (2010).
    • (2010) PLoS Genet. , vol.6 , pp. 1000887
    • Zhou, H.1
  • 33
    • 77953019135 scopus 로고    scopus 로고
    • Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration
    • Nishimura, A. L. et al. Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration. Brain 133, 1763-1771 (2010).
    • (2010) Brain , vol.133 , pp. 1763-1771
    • Nishimura, A.L.1
  • 34
    • 84865063851 scopus 로고    scopus 로고
    • The ALS disease protein TDP-43 is actively transported in motor neuron axons and regulates axon outgrowth
    • Fallini, C., Bassell, G. J. & Rossoll, W. The ALS disease protein TDP-43 is actively transported in motor neuron axons and regulates axon outgrowth. Hum. Mol. Genet. 21, 3703-3718 (2012).
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 3703-3718
    • Fallini, C.1    Bassell, G.J.2    Rossoll, W.3
  • 35
    • 84887540422 scopus 로고    scopus 로고
    • The ALS disease associated mutant TDP-43 impairs mitochondrial dynamics and function in motor neurons
    • Wang, W. et al. The ALS disease associated mutant TDP-43 impairs mitochondrial dynamics and function in motor neurons. Hum. Mol. Genet. 22, 4706-4719 (2013).
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 4706-4719
    • Wang, W.1
  • 36
    • 84896710448 scopus 로고    scopus 로고
    • ALS-associated TDP-43 Induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation
    • Walker, A. K. et al. ALS-associated TDP-43 Induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation. PLoS ONE 8, e81170 (2013).
    • (2013) PLoS ONE , vol.8
    • Walker, A.K.1
  • 37
    • 84867289633 scopus 로고    scopus 로고
    • XBP1 depletion precedes ubiquitin aggregation and Golgi fragmentation in TDP-43 transgenic rats
    • Tong, J. et al. XBP1 depletion precedes ubiquitin aggregation and Golgi fragmentation in TDP-43 transgenic rats. J. Neurochem. 123, 406-416 (2012).
    • (2012) J. Neurochem. , vol.123 , pp. 406-416
    • Tong, J.1
  • 38
    • 84855889048 scopus 로고    scopus 로고
    • TDP-43 toxicity is mediated by the unfolded protein response-unrelated induction of C/EBP homologous protein expression
    • Suzuki, H. & Matsuoka, M. TDP-43 toxicity is mediated by the unfolded protein response-unrelated induction of C/EBP homologous protein expression. J. Neurosci. Res. 90, 641-647 (2011).
    • (2011) J. Neurosci. Res. , vol.90 , pp. 641-647
    • Suzuki, H.1    Matsuoka, M.2
  • 39
    • 84864606276 scopus 로고    scopus 로고
    • TDP-1/TDP-43 regulates stress signaling and age-dependent proteotoxicity in Caenorhabditis elegans
    • Vaccaro, A. et al. TDP-1/TDP-43 regulates stress signaling and age-dependent proteotoxicity in Caenorhabditis elegans. PLoS Genet. 8, e1002806 (2012).
    • (2012) PLoS Genet. , vol.8
    • Vaccaro, A.1
  • 40
    • 79957583304 scopus 로고    scopus 로고
    • Neurotoxic 43-kDa TAR DNA-binding protein (TDP-43) triggers mitochondrion-dependent programmed cell death in yeast
    • Braun, R. J. et al. Neurotoxic 43-kDa TAR DNA-binding protein (TDP-43) triggers mitochondrion-dependent programmed cell death in yeast. J. Biol. Chem. 286, 19958-19972 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 19958-19972
    • Braun, R.J.1
  • 41
    • 84862118369 scopus 로고    scopus 로고
    • Rodent models of TDP-43: Recent advances
    • Tsao, W. et al. Rodent models of TDP-43: recent advances. Brain Res. 1462, 26-39 (2012).
    • (2012) Brain Res. , vol.1462 , pp. 26-39
    • Tsao, W.1
  • 42
    • 39849110726 scopus 로고    scopus 로고
    • The GSK3 hypothesis of Alzheimer's disease
    • DOI 10.1111/j.1471-4159.2007.05194.x
    • Hooper, C., Killick, R. & Lovestone, S. The GSK3 hypothesis of Alzheimer's disease. J. Neurochem. 104, 1433-1439 (2008). (Pubitemid 351316776)
    • (2008) Journal of Neurochemistry , vol.104 , Issue.6 , pp. 1433-1439
    • Hooper, C.1    Killick, R.2    Lovestone, S.3
  • 43
    • 79959948402 scopus 로고    scopus 로고
    • The potential role of glycogen synthase kinase 3 inhibitors as amyotrophic lateral sclerosis pharmacological therapy
    • Palomo, V., Perez, D. I., Gil, C. & Martinez, A. The potential role of glycogen synthase kinase 3 inhibitors as amyotrophic lateral sclerosis pharmacological therapy. Curr. Med. Chem. 18, 3028-3034 (2011).
    • (2011) Curr. Med. Chem. , vol.18 , pp. 3028-3034
    • Palomo, V.1    Perez, D.I.2    Gil, C.3    Martinez, A.4
  • 44
  • 45
    • 68649120751 scopus 로고    scopus 로고
    • Mitochondrial calcium as a key regulator of mitochondrial ATP production in mammalian cells
    • Griffiths, E. J. & Rutter, G. A. Mitochondrial calcium as a key regulator of mitochondrial ATP production in mammalian cells. Biochim. Biophys. Acta 1787, 1324-1333 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1324-1333
    • Griffiths, E.J.1    Rutter, G.A.2
  • 46
    • 84876079328 scopus 로고    scopus 로고
    • Pathogenic VCP mutations induce mitochondrial uncoupling and reduced ATP levels
    • Bartolome, F. et al. Pathogenic VCP mutations induce mitochondrial uncoupling and reduced ATP levels. Neuron 78, 57-64 (2013).
    • (2013) Neuron , vol.78 , pp. 57-64
    • Bartolome, F.1
  • 47
    • 84862870271 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Saxton, W. M. & Hollenbeck, P. J. The axonal transport of mitochondria. J. Cell Sci. 125, 2095-2104 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 2095-2104
    • Saxton, W.M.1    Hollenbeck, P.J.2
  • 48
    • 77955459468 scopus 로고    scopus 로고
    • ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules
    • Friedman, J. R., Webster, B. M., Mastronarde, D. N., Verhey, K. J. & Voeltz, G. K. ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules. J. Cell Biol. 190, 363-375 (2010).
    • (2010) J. Cell Biol. , vol.190 , pp. 363-375
    • Friedman, J.R.1    Webster, B.M.2    Mastronarde, D.N.3    Verhey, K.J.4    Voeltz, G.K.5
  • 49
    • 80052172908 scopus 로고    scopus 로고
    • The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections
    • USA
    • Kornmann, B., Osman, C. & Walter, P. The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections. Proc. Natl Acad. Sci. USA 108, 14151-14156 (2011).
    • (2011) Proc. Natl Acad. Sci , vol.108 , pp. 14151-14156
    • Kornmann, B.1    Osman, C.2    Walter, P.3
  • 50
    • 83455243339 scopus 로고    scopus 로고
    • Autophagy dysregulation in amyotrophic lateral sclerosis
    • Chen, S., Zhang, X., Song, L. & Le, W. Autophagy dysregulation in amyotrophic lateral sclerosis. Brain Pathol. 22, 110-116 (2012).
    • (2012) Brain Pathol. , vol.22 , pp. 110-116
    • Chen, S.1    Zhang, X.2    Song, L.3    Le, W.4
  • 51
    • 84866289381 scopus 로고    scopus 로고
    • Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43
    • USA
    • Wang, I. F. et al. Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43. Proc. Natl Acad. Sci. USA 109, 15024-15029 (2012).
    • (2012) Proc. Natl Acad. Sci , vol.109 , pp. 15024-15029
    • Wang, I.F.1
  • 53
    • 66149156941 scopus 로고    scopus 로고
    • ER Stress and unfolded protein response in amyotrophic lateral sclerosis
    • Kanekura, K., Suzuki, H., Aiso, S. & Matsuoka, M. ER Stress and unfolded protein response in amyotrophic lateral sclerosis. Mol. Neurobiol. 39, 81-89 (2009).
    • (2009) Mol. Neurobiol. , vol.39 , pp. 81-89
    • Kanekura, K.1    Suzuki, H.2    Aiso, S.3    Matsuoka, M.4
  • 54
    • 84897504097 scopus 로고    scopus 로고
    • Familial Alzheimer's disease-associated presenilin-1 alters cerebellar activity and calcium homeostasis
    • Sepulveda-Falla, D. et al. Familial Alzheimer's disease-associated presenilin-1 alters cerebellar activity and calcium homeostasis. J. Clin. Invest. 124, 1552-1567 (2014).
    • (2014) J. Clin. Invest. , vol.124 , pp. 1552-1567
    • Sepulveda-Falla, D.1
  • 55
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Sreedharan, J. et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319, 1688-1672 (2008).
    • (2008) Science , vol.319 , pp. 1688-1672
    • Sreedharan, J.1
  • 56
    • 84859246580 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated mutant VAPBP56S perturbs calcium homeostasis to disrupt axonal transport of mitochondria
    • Morotz, G. M. et al. Amyotrophic lateral sclerosis-associated mutant VAPBP56S perturbs calcium homeostasis to disrupt axonal transport of mitochondria. Hum. Mol. Genet. 21, 1979-1988 (2012).
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1979-1988
    • Morotz, G.M.1
  • 57
    • 79953141458 scopus 로고    scopus 로고
    • Phosphorylation of kinesin light chain-1 at serine-460 modulates binding and trafficking of calsyntenin-1
    • Vagnoni, A., Rodriguez, L., Manser, C., De Vos, K. J. & Miller, C. C. J. Phosphorylation of kinesin light chain-1 at serine-460 modulates binding and trafficking of calsyntenin-1. J. Cell Sci. 124, 1032-1042 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 1032-1042
    • Vagnoni, A.1    Rodriguez, L.2    Manser, C.3    De Vos, K.J.4    Miller, C.C.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.