메뉴 건너뛰기




Volumn 8, Issue 11, 2013, Pages

ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 2ALPHA; PROTEIN DISULFIDE ISOMERASE; SALUBRINAL; TAR DNA BINDING PROTEIN; CINNAMIC ACID DERIVATIVE; DNA BINDING PROTEIN; PROTEIN TDP-43; THIOUREA;

EID: 84896710448     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0081170     Document Type: Article
Times cited : (137)

References (69)
  • 3
    • 0035794665 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
    • DOI 10.1093/emboj/20.7.1774
    • Buratti E, Dork T, Zuccato E, Pagani F, Romano M, et al. (2001) Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. Embo J 20: 1774-1784. (Pubitemid 32299413)
    • (2001) EMBO Journal , vol.20 , Issue.7 , pp. 1774-1784
    • Buratti, E.1    Dork, T.2    Zuccato, E.3    Pagani, F.4    Romano, M.5    Baralle, F.E.6
  • 4
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton MJ, Igaz LM, Wong MM, Kwong LK, Trojanowski JQ, et al. (2008) Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J Biol Chem 283: 13302-13309.
    • (2008) J Biol Chem , vol.283 , pp. 13302-13309
    • Winton, M.J.1    Igaz, L.M.2    Wong, M.M.3    Kwong, L.K.4    Trojanowski, J.Q.5
  • 6
    • 58149498300 scopus 로고    scopus 로고
    • Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells
    • Nonaka T, Arai T, Buratti E, Baralle FE, Akiyama H, et al. (2009) Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells. FEBS Lett 583: 394-400.
    • (2009) FEBS Lett , vol.583 , pp. 394-400
    • Nonaka, T.1    Arai, T.2    Buratti, E.3    Baralle, F.E.4    Akiyama, H.5
  • 7
    • 78149461229 scopus 로고    scopus 로고
    • Tar DNA binding protein-43 (TDP-43) associates with stress granules: Analysis of cultured cells and pathological brain tissue
    • Liu-Yesucevitz L, Bilgutay A, Zhang YJ, Vanderweyde T, Citro A, et al. (2010) Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue. PLoS ONE 5: e13250.
    • (2010) PLoS ONE , vol.5
    • Liu-Yesucevitz, L.1    Bilgutay, A.2    Zhang, Y.J.3    Vanderweyde, T.4    Citro, A.5
  • 8
    • 79952589652 scopus 로고    scopus 로고
    • TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1
    • McDonald KK, Aulas A, Destroismaisons L, Pickles S, Beleac E, et al. (2011) TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1. Hum Mol Genet 20: 1400-1410.
    • (2011) Hum Mol Genet , vol.20 , pp. 1400-1410
    • McDonald, K.K.1    Aulas, A.2    Destroismaisons, L.3    Pickles, S.4    Beleac, E.5
  • 9
    • 79952268025 scopus 로고    scopus 로고
    • TDP- 43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor
    • Dewey CM, Cenik B, Sephton CF, Dries DR, Mayer P, 3rd, et al. (2011) TDP- 43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor. Mol Cell Biol 31: 1098-1108.
    • (2011) Mol Cell Biol , vol.31 , pp. 1098-1108
    • Dewey, C.M.1    Cenik, B.2    Sephton, C.F.3    Dries, D.R.4    Mayer III, P.5
  • 10
    • 84857124994 scopus 로고    scopus 로고
    • Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates
    • Parker SJ, Meyerowitz J, James JL, Liddell JR, Crouch PJ, et al. (2012) Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates. Neurochem Int 60: 415-424.
    • (2012) Neurochem Int , vol.60 , pp. 415-424
    • Parker, S.J.1    Meyerowitz, J.2    James, J.L.3    Liddell, J.R.4    Crouch, P.J.5
  • 12
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules
    • Kedersha NL, Gupta M, Li W, Miller I, Anderson P (1999) RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J Cell Biol 147: 1431-1442.
    • (1999) J Cell Biol , vol.147 , pp. 1431-1442
    • Kedersha, N.L.1    Gupta, M.2    Li, W.3    Miller, I.4    Anderson, P.5
  • 13
    • 77952628837 scopus 로고    scopus 로고
    • Regulation of translation by stress granules and processing bodies
    • Kedersha N, Anderson P (2009) Regulation of translation by stress granules and processing bodies. Prog Mol Biol Transl Sci 90: 155-185.
    • (2009) Prog Mol Biol Transl Sci , vol.90 , pp. 155-185
    • Kedersha, N.1    Anderson, P.2
  • 14
    • 84862128438 scopus 로고    scopus 로고
    • TDP-43 aggregation in neurodegeneration: Are stress granules the key?
    • Dewey CM, Cenik B, Sephton CF, Johnson BA, Herz J, et al. (2012) TDP-43 aggregation in neurodegeneration: are stress granules the key? Brain Res 1462: 16-25.
    • (2012) Brain Res , vol.1462 , pp. 16-25
    • Dewey, C.M.1    Cenik, B.2    Sephton, C.F.3    Johnson, B.A.4    Herz, J.5
  • 15
    • 80054714793 scopus 로고    scopus 로고
    • Cell stress induces TDP-43 pathological changes associated with ERK1/2 dysfunction: Implications in ALS
    • Ayala V, Granado-Serrano AB, Cacabelos D, Naudi A, Ilieva EV, et al. (2011) Cell stress induces TDP-43 pathological changes associated with ERK1/2 dysfunction: implications in ALS. Acta Neuropathol 122: 259-270.
    • (2011) Acta Neuropathol , vol.122 , pp. 259-270
    • Ayala, V.1    Granado-Serrano, A.B.2    Cacabelos, D.3    Naudi, A.4    Ilieva, E.V.5
  • 16
    • 80052081196 scopus 로고    scopus 로고
    • Stress signaling from the endoplasmic reticulum: A central player in the pathogenesis of amyotrophic lateral sclerosis
    • Walker AK, Atkin JD (2011) Stress signaling from the endoplasmic reticulum: A central player in the pathogenesis of amyotrophic lateral sclerosis. IUBMB life 63: 754-763.
    • (2011) IUBMB Life , vol.63 , pp. 754-763
    • Walker, A.K.1    Atkin, J.D.2
  • 17
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • DOI 10.1126/science.287.5453.664
    • Urano F, Wang X, Bertolotti A, Zhang Y, Chung P, et al. (2000) Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287: 664-666. (Pubitemid 30070916)
    • (2000) Science , vol.287 , Issue.5453 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 18
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K, Yoshida H, Yanagi H, Yura T, Mori K (1999) Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 10: 3787-3799. (Pubitemid 29534025)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.11 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 19
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic- reticulum-resident kinase
    • DOI 10.1038/16729
    • Harding HP, Zhang Y, Ron D (1999) Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397: 271-274. (Pubitemid 29051178)
    • (1999) Nature , vol.397 , Issue.6716 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 20
    • 43249109174 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses
    • Schroder M (2008) Endoplasmic reticulum stress responses. Cell Mol Life Sci 65: 862-894.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 862-894
    • Schroder, M.1
  • 21
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • DOI 10.1016/S0022-2836(02)00234-6
    • Ma Y, Brewer JW, Diehl JA, Hendershot LM (2002) Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J Mol Biol 318: 1351-1365. (Pubitemid 34754003)
    • (2002) Journal of Molecular Biology , vol.318 , Issue.5 , pp. 1351-1365
    • Ma, Y.1    Brewer, J.W.2    Alan, D.J.3    Hendershot, L.M.4
  • 22
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • DOI 10.1146/annurev.biochem.73.011303.074134
    • Schroder M, Kaufman RJ (2005) The mammalian unfolded protein response. Annu Rev Biochem 74: 739-789. (Pubitemid 40995523)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 23
    • 43649100018 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis
    • Atkin JD, Farg MA, Walker AK, McLean C, Tomas D, et al. (2008) Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis. Neurobiol Dis 30: 400-407.
    • (2008) Neurobiol Dis , vol.30 , pp. 400-407
    • Atkin, J.D.1    Farg, M.A.2    Walker, A.K.3    McLean, C.4    Tomas, D.5
  • 24
    • 70349627027 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
    • Hetz C, Thielen P, Matus S, Nassif M, Court F, et al. (2009) XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes Dev 23: 2294-2306.
    • (2009) Genes Dev , vol.23 , pp. 2294-2306
    • Hetz, C.1    Thielen, P.2    Matus, S.3    Nassif, M.4    Court, F.5
  • 25
    • 79551584057 scopus 로고    scopus 로고
    • The unfolded protein response in familial amyotrophic lateral sclerosis
    • Wang L, Popko B, Roos RP (2011) The unfolded protein response in familial amyotrophic lateral sclerosis. Hum Mol Genet 20: 1008-1015.
    • (2011) Hum Mol Genet , vol.20 , pp. 1008-1015
    • Wang, L.1    Popko, B.2    Roos, R.P.3
  • 26
    • 84866748196 scopus 로고    scopus 로고
    • Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase
    • Farg MA, Soo KY, Walker AK, Pham H, Orian J, et al. (2012) Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase. Neurobiol Aging 33: 2855-2868.
    • (2012) Neurobiol Aging , vol.33 , pp. 2855-2868
    • Farg, M.A.1    Soo, K.Y.2    Walker, A.K.3    Pham, H.4    Orian, J.5
  • 27
    • 74249084267 scopus 로고    scopus 로고
    • Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis
    • Walker AK, Farg MA, Bye CR, McLean CA, Horne MK, et al. (2010) Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis. Brain 133: 105-116.
    • (2010) Brain , vol.133 , pp. 105-116
    • Walker, A.K.1    Farg, M.A.2    Bye, C.R.3    McLean, C.A.4    Horne, M.K.5
  • 28
    • 79953894390 scopus 로고    scopus 로고
    • Mutant HFE H63D protein is associated with prolonged endoplasmic reticulum stress and increased neuronal vulnerability
    • Liu Y, Lee SY, Neely E, Nandar W, Moyo M, et al. (2011) Mutant HFE H63D protein is associated with prolonged endoplasmic reticulum stress and increased neuronal vulnerability. J Biol Chem 286: 13161-13170.
    • (2011) J Biol Chem , vol.286 , pp. 13161-13170
    • Liu, Y.1    Lee, S.Y.2    Neely, E.3    Nandar, W.4    Moyo, M.5
  • 29
    • 79953855830 scopus 로고    scopus 로고
    • TDP-43-induced death is associated with altered regulation of BIM and Bcl-xL and attenuated by caspase-mediated TDP-43 cleavage
    • Suzuki H, Lee K, Matsuoka M (2011) TDP-43-induced death is associated with altered regulation of BIM and Bcl-xL and attenuated by caspase-mediated TDP-43 cleavage. J Biol Chem 286: 13171-13183.
    • (2011) J Biol Chem , vol.286 , pp. 13171-13183
    • Suzuki, H.1    Lee, K.2    Matsuoka, M.3
  • 30
    • 84867289633 scopus 로고    scopus 로고
    • XBP1 depletion precedes ubiquitin aggregation and Golgi fragmentation in TDP-43 transgenic rats
    • Tong J, Huang C, Bi F, Wu Q, Huang B, et al. (2012) XBP1 depletion precedes ubiquitin aggregation and Golgi fragmentation in TDP-43 transgenic rats. J Neurochem 123: 406-416.
    • (2012) J Neurochem , vol.123 , pp. 406-416
    • Tong, J.1    Huang, C.2    Bi, F.3    Wu, Q.4    Huang, B.5
  • 31
    • 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 (2012) TDP-43 toxicity is mediated by the unfolded protein response-unrelated induction of C/EBP homologous protein expression. J Neurosci Res 90: 641-647.
    • (2012) J Neurosci Res , vol.90 , pp. 641-647
    • Suzuki, H.1    Matsuoka, M.2
  • 34
    • 33645108336 scopus 로고    scopus 로고
    • Mapping superoxide dismutase 1 domains of non-native interaction: Roles of intra- and intermolecular disulfide bonding in aggregation
    • Wang J, Xu G, Borchelt DR (2006) Mapping superoxide dismutase 1 domains of non-native interaction: roles of intra- and intermolecular disulfide bonding in aggregation. J Neurochem 96: 1277-1288.
    • (2006) J Neurochem , vol.96 , pp. 1277-1288
    • Wang, J.1    Xu, G.2    Borchelt, D.R.3
  • 35
    • 70449377144 scopus 로고    scopus 로고
    • Reticulon-4A (Nogo-A) redistributes protein disulfide isomerase to protect mice from SOD1-dependent amyotrophic lateral sclerosis
    • Yang YS, Harel NY, Strittmatter SM (2009) Reticulon-4A (Nogo-A) redistributes protein disulfide isomerase to protect mice from SOD1-dependent amyotrophic lateral sclerosis. J Neurosci 29: 13850-13859.
    • (2009) J Neurosci , vol.29 , pp. 13850-13859
    • Yang, Y.S.1    Harel, N.Y.2    Strittmatter, S.M.3
  • 36
    • 80055031464 scopus 로고    scopus 로고
    • Protein disulfide isomerase-immunopositive inclusions in patients with amyotrophic lateral sclerosis
    • Honjo Y, Kaneko S, Ito H, Horibe T, Nagashima M, et al. (2011) Protein disulfide isomerase-immunopositive inclusions in patients with amyotrophic lateral sclerosis. Amyotroph Lateral Scler 12: 444-450.
    • (2011) Amyotroph Lateral Scler , vol.12 , pp. 444-450
    • Honjo, Y.1    Kaneko, S.2    Ito, H.3    Horibe, T.4    Nagashima, M.5
  • 37
    • 84857997227 scopus 로고    scopus 로고
    • Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide crosslinking
    • Cohen TJ, Hwang AW, Unger T, Trojanowski JQ, Lee VM (2012) Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide crosslinking. Embo J 31: 1241-1252.
    • (2012) Embo J , vol.31 , pp. 1241-1252
    • Cohen, T.J.1    Hwang, A.W.2    Unger, T.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 41
    • 52949094629 scopus 로고    scopus 로고
    • Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis
    • Rutherford NJ, Zhang YJ, Baker M, Gass JM, Finch NA, et al. (2008) Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis. PLoS Genet 4: e1000193.
    • (2008) PLoS Genet , vol.4
    • Rutherford, N.J.1    Zhang, Y.J.2    Baker, M.3    Gass, J.M.4    Finch, N.A.5
  • 42
    • 63749096466 scopus 로고    scopus 로고
    • High frequency of TARDBP gene mutations in Italian patients with amyotrophic lateral sclerosis
    • Corrado L, Ratti A, Gellera C, Buratti E, Castellotti B, et al. (2009) High frequency of TARDBP gene mutations in Italian patients with amyotrophic lateral sclerosis. Hum Mutat 30: 688-694.
    • (2009) Hum Mutat , vol.30 , pp. 688-694
    • Corrado, L.1    Ratti, A.2    Gellera, C.3    Buratti, E.4    Castellotti, B.5
  • 43
    • 77749331305 scopus 로고    scopus 로고
    • TDP-43 M337V mutation in familial amyotrophic lateral sclerosis in Japan
    • Tamaoka A, Arai M, Itokawa M, Arai T, Hasegawa M, et al. (2010) TDP-43 M337V mutation in familial amyotrophic lateral sclerosis in Japan. Intern Med 49: 331-334.
    • (2010) Intern Med , vol.49 , pp. 331-334
    • Tamaoka, A.1    Arai, M.2    Itokawa, M.3    Arai, T.4    Hasegawa, M.5
  • 45
    • 0037066741 scopus 로고    scopus 로고
    • The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the er to the Golgi
    • DOI 10.1074/jbc.M110636200
    • Chen X, Shen J, Prywes R (2002) The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi. J Biol Chem 277: 13045-13052. (Pubitemid 34952673)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 13045-13052
    • Chen, X.1    Shen, J.2    Prywes, R.3
  • 46
    • 70849101711 scopus 로고    scopus 로고
    • Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins
    • Jessop CE, Watkins RH, Simmons JJ, Tasab M, Bulleid NJ (2009) Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. J Cell Sci 122: 4287-4295.
    • (2009) J Cell Sci , vol.122 , pp. 4287-4295
    • Jessop, C.E.1    Watkins, R.H.2    Simmons, J.J.3    Tasab, M.4    Bulleid, N.J.5
  • 47
    • 67049109264 scopus 로고    scopus 로고
    • Activation of the endoplasmic reticulum stress-associated transcription factor x box-binding protein-1 occurs in a subset of normal germinal-center B cells and in aggressive B-cell lymphomas with prognostic implications
    • Balague O, Mozos A, Martinez D, Hernandez L, Colomo L, et al. (2009) Activation of the endoplasmic reticulum stress-associated transcription factor x box-binding protein-1 occurs in a subset of normal germinal-center B cells and in aggressive B-cell lymphomas with prognostic implications. Am J Pathol 174: 2337-2346.
    • (2009) Am J Pathol , vol.174 , pp. 2337-2346
    • Balague, O.1    Mozos, A.2    Martinez, D.3    Hernandez, L.4    Colomo, L.5
  • 48
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska I, Bell S, Cairns NJ, Miller TM, Baloh RH (2009) TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc Natl Acad Sci U S A 106: 18809-18814.
    • (2009) Proc Natl Acad Sci U S a , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 49
    • 59549094064 scopus 로고    scopus 로고
    • Structural determinants of the cellular localization and shuttling of TDP-43
    • Ayala YM, Zago P, D'Ambrogio A, Xu YF, Petrucelli L, et al. (2008) Structural determinants of the cellular localization and shuttling of TDP-43. J Cell Sci 121: 3778-3785.
    • (2008) J Cell Sci , vol.121 , pp. 3778-3785
    • Ayala, Y.M.1    Zago, P.2    D'Ambrogio, A.3    Xu, Y.F.4    Petrucelli, L.5
  • 50
    • 75649135319 scopus 로고    scopus 로고
    • Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6
    • Fiesel FC, Voigt A, Weber SS, Van den Haute C, Waldenmaier A, et al. (2010) Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6. Embo J 29: 209-221.
    • (2010) Embo J , vol.29 , pp. 209-221
    • Fiesel, F.C.1    Voigt, A.2    Weber, S.S.3    Van Den Haute, C.4    Waldenmaier, A.5
  • 51
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • DOI 10.1016/S0962-8924(98)01346-4
    • Lee DH, Goldberg AL (1998) Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol 8: 397-403. (Pubitemid 28458705)
    • (1998) Trends in Cell Biology , vol.8 , Issue.10 , pp. 397-403
    • Lee, D.H.1
  • 53
    • 77950686223 scopus 로고    scopus 로고
    • OGFOD1, a novel modulator of eukaryotic translation initiation factor 2alpha phosphorylation and the cellular response to stress
    • Wehner KA, Schutz S, Sarnow P (2010) OGFOD1, a novel modulator of eukaryotic translation initiation factor 2alpha phosphorylation and the cellular response to stress. Mol Cell Biol 30: 2006-2016.
    • (2010) Mol Cell Biol , vol.30 , pp. 2006-2016
    • Wehner, K.A.1    Schutz, S.2    Sarnow, P.3
  • 54
    • 55549130760 scopus 로고    scopus 로고
    • Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways
    • Arimoto K, Fukuda H, Imajoh-Ohmi S, Saito H, Takekawa M (2008) Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways. Nat Cell Biol 10: 1324-1332.
    • (2008) Nat Cell Biol , vol.10 , pp. 1324-1332
    • Arimoto, K.1    Fukuda, H.2    Imajoh-Ohmi, S.3    Saito, H.4    Takekawa, M.5
  • 56
    • 38449116842 scopus 로고    scopus 로고
    • Superoxide dismutase 1 mutants related to amyotrophic lateral sclerosis induce endoplasmic stress in neuro2a cells
    • DOI 10.1111/j.1471-4159.2007.05053.x
    • Oh YK, Shin KS, Yuan J, Kang SJ (2008) Superoxide dismutase 1 mutants related to amyotrophic lateral sclerosis induce endoplasmic stress in neuro2a cells. J Neurochem 104: 993-1005. (Pubitemid 351143647)
    • (2008) Journal of Neurochemistry , vol.104 , Issue.4 , pp. 993-1005
    • Oh, Y.K.1    Shin, K.S.2    Yuan, J.3    Kang, S.J.4
  • 57
    • 84859867839 scopus 로고    scopus 로고
    • Bim Links ER Stress and Apoptosis in Cells Expressing Mutant SOD1 Associated with Amyotrophic Lateral Sclerosis
    • Soo KY, Atkin JD, Farg M, Walker AK, Horne MK, et al. (2012) Bim Links ER Stress and Apoptosis in Cells Expressing Mutant SOD1 Associated with Amyotrophic Lateral Sclerosis. PLoS ONE 7: e35413.
    • (2012) PLoS ONE , vol.7
    • Soo, K.Y.1    Atkin, J.D.2    Farg, M.3    Walker, A.K.4    Horne, M.K.5
  • 58
    • 84873033993 scopus 로고    scopus 로고
    • Ataxin-2 interacts with FUS and intermediate-length polyglutamine expansions enhance FUS-related pathology in amyotrophic lateral sclerosis
    • Farg MA, Soo KY, Warraich ST, Sundaramoorthy V, Blair IP, et al. (2013) Ataxin-2 interacts with FUS and intermediate-length polyglutamine expansions enhance FUS-related pathology in amyotrophic lateral sclerosis. Hum Mol Genet 22: 717-728.
    • (2013) Hum Mol Genet , vol.22 , pp. 717-728
    • Farg, M.A.1    Soo, K.Y.2    Warraich, S.T.3    Sundaramoorthy, V.4    Blair, I.P.5
  • 59
    • 58549088349 scopus 로고    scopus 로고
    • ALS-linked P56S-VAPB, an aggregated loss-of-function mutant of VAPB, predisposes motor neurons to ER stress-related death by inducing aggregation of co-expressed wild-type VAPB
    • Suzuki H, Kanekura K, Levine TP, Kohno K, Olkkonen VM, et al. (2009) ALS-linked P56S-VAPB, an aggregated loss-of-function mutant of VAPB, predisposes motor neurons to ER stress-related death by inducing aggregation of co-expressed wild-type VAPB. J Neurochem 108: 973-985.
    • (2009) J Neurochem , vol.108 , pp. 973-985
    • Suzuki, H.1    Kanekura, K.2    Levine, T.P.3    Kohno, K.4    Olkkonen, V.M.5
  • 60
    • 66449134941 scopus 로고    scopus 로고
    • VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death
    • Gitcho MA, Strider J, Carter D, Taylor-Reinwald L, Forman MS, et al. (2009) VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death. J Biol Chem 284: 12384-12398.
    • (2009) J Biol Chem , vol.284 , pp. 12384-12398
    • Gitcho, M.A.1    Strider, J.2    Carter, D.3    Taylor-Reinwald, L.4    Forman, M.S.5
  • 61
    • 67349164383 scopus 로고    scopus 로고
    • A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice
    • Saxena S, Cabuy E, Caroni P (2009) A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nat Neurosci 12: 627-636.
    • (2009) Nat Neurosci , vol.12 , pp. 627-636
    • Saxena, S.1    Cabuy, E.2    Caroni, P.3
  • 62
    • 84877075803 scopus 로고    scopus 로고
    • Pharmacological reduction of ER stress protects against TDP-43 neuronal toxicity in vivo
    • Vaccaro A, Patten SA, Aggad D, Julien C, Maios C, et al. (2013) Pharmacological reduction of ER stress protects against TDP-43 neuronal toxicity in vivo. Neurobiol Dis 55: 64-75.
    • (2013) Neurobiol Dis , vol.55 , pp. 64-75
    • Vaccaro, A.1    Patten, S.A.2    Aggad, D.3    Julien, C.4    Maios, C.5
  • 63
    • 79961117695 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase controls TDP-43 accumulation in stress granules induced by oxidative stress
    • Meyerowitz J, Parker SJ, Vella LJ, Ng D, Price KA, et al. (2011) C-Jun N-terminal kinase controls TDP-43 accumulation in stress granules induced by oxidative stress. Molecular neurodegeneration 6: 57.
    • (2011) Molecular Neurodegeneration , vol.6 , pp. 57
    • Meyerowitz, J.1    Parker, S.J.2    Vella, L.J.3    Ng, D.4    Price, K.A.5
  • 65
    • 33646486372 scopus 로고    scopus 로고
    • Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice
    • Furukawa Y, Fu R, Deng HX, Siddique T, O'Halloran TV (2006) Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice. Proc Natl Acad Sci U S A 103: 7148-7153.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7148-7153
    • Furukawa, Y.1    Fu, R.2    Deng, H.X.3    Siddique, T.4    O'Halloran, T.V.5
  • 66
    • 84875991370 scopus 로고    scopus 로고
    • Association studies indicate that protein disulfide isomerase is a risk factor in amyotrophic lateral sclerosis
    • Kwok CT, Morris AG, Frampton J, Smith B, Shaw CE, et al. (2013) Association studies indicate that protein disulfide isomerase is a risk factor in amyotrophic lateral sclerosis. Free Radic Biol Med 58: 81-86.
    • (2013) Free Radic Biol Med , vol.58 , pp. 81-86
    • Kwok, C.T.1    Morris, A.G.2    Frampton, J.3    Smith, B.4    Shaw, C.E.5
  • 67
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: Unpredicted non-ER locations and functions
    • Turano C, Coppari S, Altieri F, Ferraro A (2002) Proteins of the PDI family: unpredicted non-ER locations and functions. J Cell Physiol 193: 154-163.
    • (2002) J Cell Physiol , vol.193 , pp. 154-163
    • Turano, C.1    Coppari, S.2    Altieri, F.3    Ferraro, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.