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Volumn 1822, Issue 6, 2012, Pages 885-896

Oxidative stress increases BACE1 protein levels through activation of the PKR-eIF2α pathway

Author keywords

Alzheimer's disease; BACE1; EIF2 ; Neuroblastoma cell cultures; Oxidative stress; PKR

Indexed keywords

BETA SECRETASE 1; DOUBLE STRANDED RNA DEPENDANT PROTEIN KINASE; HYDROGEN PEROXIDE; INITIATION FACTOR 2ALPHA; JANUS KINASE; PROTEIN KINASE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84859073666     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2012.01.009     Document Type: Article
Times cited : (140)

References (75)
  • 1
    • 67349143998 scopus 로고    scopus 로고
    • Classification and basic pathology of Alzheimer disease
    • Duyckaerts C., Delatour B., Potier M.C. Classification and basic pathology of Alzheimer disease. Acta Neuropathol. 2009, 118:5-36.
    • (2009) Acta Neuropathol. , vol.118 , pp. 5-36
    • Duyckaerts, C.1    Delatour, B.2    Potier, M.C.3
  • 5
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 8
    • 0036718272 scopus 로고    scopus 로고
    • Beta-secretase protein and activity are increased in the neocortex in Alzheimer disease
    • Fukumoto H., Cheung B.S., Hyman B.T., Irizarry M.C. Beta-secretase protein and activity are increased in the neocortex in Alzheimer disease. Arch. Neurol. 2002, 59:1381-1389.
    • (2002) Arch. Neurol. , vol.59 , pp. 1381-1389
    • Fukumoto, H.1    Cheung, B.S.2    Hyman, B.T.3    Irizarry, M.C.4
  • 10
    • 34147120073 scopus 로고    scopus 로고
    • Beta-site amyloid precursor protein cleaving enzyme 1 levels become elevated in neurons around amyloid plaques: implications for Alzheimer's disease pathogenesis
    • Zhao J., Fu Y., Yasvoina M., Shao P., Hitt B., O'Connor T., Logan S., Maus E., Citron M., Berry R., Binder L., Vassar R. Beta-site amyloid precursor protein cleaving enzyme 1 levels become elevated in neurons around amyloid plaques: implications for Alzheimer's disease pathogenesis. J. Neurosci. 2007, 27:3639-3649.
    • (2007) J. Neurosci. , vol.27 , pp. 3639-3649
    • Zhao, J.1    Fu, Y.2    Yasvoina, M.3    Shao, P.4    Hitt, B.5    O'Connor, T.6    Logan, S.7    Maus, E.8    Citron, M.9    Berry, R.10    Binder, L.11    Vassar, R.12
  • 11
    • 0036260892 scopus 로고    scopus 로고
    • Increased expression of the amyloid precursor beta-secretase in Alzheimer's disease
    • Holsinger R.M., McLean C.A., Beyreuther K., Masters C.L., Evin G. Increased expression of the amyloid precursor beta-secretase in Alzheimer's disease. Ann. Neurol. 2002, 51:783-786.
    • (2002) Ann. Neurol. , vol.51 , pp. 783-786
    • Holsinger, R.M.1    McLean, C.A.2    Beyreuther, K.3    Masters, C.L.4    Evin, G.5
  • 13
    • 0347356360 scopus 로고    scopus 로고
    • Transcriptional regulation of BACE1, the beta-amyloid precursor protein beta-secretase, by Sp1
    • Christensen M.A., Zhou W., Qing H., Lehman A., Philipsen S., Song W. Transcriptional regulation of BACE1, the beta-amyloid precursor protein beta-secretase, by Sp1. Mol. Cell. Biol. 2004, 24:865-874.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 865-874
    • Christensen, M.A.1    Zhou, W.2    Qing, H.3    Lehman, A.4    Philipsen, S.5    Song, W.6
  • 14
    • 77952604395 scopus 로고    scopus 로고
    • Tyk2/STAT3 signaling mediates beta-amyloid-induced neuronal cell death: implications in Alzheimer's disease
    • Wan J., Fu A.K., Ip F.C., Ng H.K., Hugon J., Page G., Wang J.H., Lai K.O., Wu Z., Ip N.Y. Tyk2/STAT3 signaling mediates beta-amyloid-induced neuronal cell death: implications in Alzheimer's disease. J. Neurosci. 2011, 30:6873-6881.
    • (2011) J. Neurosci. , vol.30 , pp. 6873-6881
    • Wan, J.1    Fu, A.K.2    Ip, F.C.3    Ng, H.K.4    Hugon, J.5    Page, G.6    Wang, J.H.7    Lai, K.O.8    Wu, Z.9    Ip, N.Y.10
  • 18
    • 1642345964 scopus 로고    scopus 로고
    • Cleavage of amyloid-beta precursor protein and amyloid-beta precursor-like protein by BACE 1
    • Li Q., Sudhof T.C. Cleavage of amyloid-beta precursor protein and amyloid-beta precursor-like protein by BACE 1. J. Biol. Chem. 2004, 279:10542-10550.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10542-10550
    • Li, Q.1    Sudhof, T.C.2
  • 20
    • 78650287763 scopus 로고    scopus 로고
    • Biogenesis and regulation of microRNA: implication in Alzheimer's disease
    • Mouton-Liger F., Paquet C., Hugon J. Biogenesis and regulation of microRNA: implication in Alzheimer's disease. Futur. Neurol. 2010, 5:839-850.
    • (2010) Futur. Neurol. , vol.5 , pp. 839-850
    • Mouton-Liger, F.1    Paquet, C.2    Hugon, J.3
  • 21
    • 71749094769 scopus 로고    scopus 로고
    • Down-regulation of seladin-1 increases BACE1 levels and activity through enhanced GGA3 depletion during apoptosis
    • Sarajarvi T., Haapasalo A., Viswanathan J., Makinen P., Laitinen M., Soininen H., Hiltunen M. Down-regulation of seladin-1 increases BACE1 levels and activity through enhanced GGA3 depletion during apoptosis. J. Biol. Chem. 2009, 284:34433-34443.
    • (2009) J. Biol. Chem. , vol.284 , pp. 34433-34443
    • Sarajarvi, T.1    Haapasalo, A.2    Viswanathan, J.3    Makinen, P.4    Laitinen, M.5    Soininen, H.6    Hiltunen, M.7
  • 23
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • Dever T.E. Gene-specific regulation by general translation factors. Cell 2002, 108:545-556.
    • (2002) Cell , vol.108 , pp. 545-556
    • Dever, T.E.1
  • 24
    • 12344305214 scopus 로고    scopus 로고
    • EIF2 and the control of cell physiology
    • Proud C.G. eIF2 and the control of cell physiology. Semin. Cell Dev. Biol. 2005, 16:3-12.
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 3-12
    • Proud, C.G.1
  • 25
    • 0030992545 scopus 로고    scopus 로고
    • A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis
    • Der S.D., Yang Y.L., Weissmann C., Williams B.R. A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:3279-3283.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 3279-3283
    • Der, S.D.1    Yang, Y.L.2    Weissmann, C.3    Williams, B.R.4
  • 26
    • 56149097715 scopus 로고    scopus 로고
    • Oxidative stress induces PKR-dependent apoptosis via IFN-gamma activation signaling in Jurkat T cells
    • Pyo C.W., Lee S.H., Choi S.Y. Oxidative stress induces PKR-dependent apoptosis via IFN-gamma activation signaling in Jurkat T cells. Biochem. Biophys. Res. Commun. 2008, 377:1001-1006.
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 1001-1006
    • Pyo, C.W.1    Lee, S.H.2    Choi, S.Y.3
  • 27
    • 0033056848 scopus 로고    scopus 로고
    • RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling
    • Ito T., Yang M., May W.S. RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling. J. Biol. Chem. 1999, 274:15427-15432.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15427-15432
    • Ito, T.1    Yang, M.2    May, W.S.3
  • 28
    • 36448942200 scopus 로고    scopus 로고
    • Activation of double-stranded RNA-activated protein kinase by mild impairment of oxidative metabolism in neurons
    • Wang X., Fan Z., Wang B., Luo J., Ke Z.J. Activation of double-stranded RNA-activated protein kinase by mild impairment of oxidative metabolism in neurons. J. Neurochem. 2007, 103:2380-2390.
    • (2007) J. Neurochem. , vol.103 , pp. 2380-2390
    • Wang, X.1    Fan, Z.2    Wang, B.3    Luo, J.4    Ke, Z.J.5
  • 30
    • 0034531395 scopus 로고    scopus 로고
    • PACT, a stress-modulated cellular activator of interferon-induced double-stranded RNA-activated protein kinase, PKR
    • Patel C.V., Handy I., Goldsmith T., Patel R.C. PACT, a stress-modulated cellular activator of interferon-induced double-stranded RNA-activated protein kinase, PKR. J. Biol. Chem. 2000, 275:37993-37998.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37993-37998
    • Patel, C.V.1    Handy, I.2    Goldsmith, T.3    Patel, R.C.4
  • 31
    • 0036892618 scopus 로고    scopus 로고
    • Involvement of double-stranded RNA-dependent protein kinase and phosphorylation of eukaryotic initiation factor-2alpha in neuronal degeneration
    • Chang R.C., Suen K.C., Ma C.H., Elyaman W., Ng H.K., Hugon J. Involvement of double-stranded RNA-dependent protein kinase and phosphorylation of eukaryotic initiation factor-2alpha in neuronal degeneration. J. Neurochem. 2002, 83:1215-1225.
    • (2002) J. Neurochem. , vol.83 , pp. 1215-1225
    • Chang, R.C.1    Suen, K.C.2    Ma, C.H.3    Elyaman, W.4    Ng, H.K.5    Hugon, J.6
  • 32
    • 0041833464 scopus 로고    scopus 로고
    • Activation of the cell stress kinase PKR in Alzheimer's disease and human amyloid precursor protein transgenic mice
    • Peel A.L., Bredesen D.E. Activation of the cell stress kinase PKR in Alzheimer's disease and human amyloid precursor protein transgenic mice. Neurobiol. Dis. 2003, 14:52-62.
    • (2003) Neurobiol. Dis. , vol.14 , pp. 52-62
    • Peel, A.L.1    Bredesen, D.E.2
  • 33
    • 0037147666 scopus 로고    scopus 로고
    • Phosphorylation of eukaryotic initiation factor-2alpha (eIF2alpha) is associated with neuronal degeneration in Alzheimer's disease
    • Chang R.C., Wong A.K., Ng H.K., Hugon J. Phosphorylation of eukaryotic initiation factor-2alpha (eIF2alpha) is associated with neuronal degeneration in Alzheimer's disease. Neuroreport 2002, 13:2429-2432.
    • (2002) Neuroreport , vol.13 , pp. 2429-2432
    • Chang, R.C.1    Wong, A.K.2    Ng, H.K.3    Hugon, J.4
  • 34
    • 70350167138 scopus 로고    scopus 로고
    • Could PKR inhibition modulate human neurodegeneration?
    • Hugon J., Paquet C., Chang R.C. Could PKR inhibition modulate human neurodegeneration?. Expert. Rev. Neurother. 2009, 9:1455-1457.
    • (2009) Expert. Rev. Neurother. , vol.9 , pp. 1455-1457
    • Hugon, J.1    Paquet, C.2    Chang, R.C.3
  • 35
    • 79251575329 scopus 로고    scopus 로고
    • Modulation of tau phosphorylation by the kinase PKR: implications in Alzheimer's disease
    • Bose A., Mouton-Liger F., Paquet C., Mazot P., Vigny M., Gray F., Hugon J. Modulation of tau phosphorylation by the kinase PKR: implications in Alzheimer's disease. Brain Pathol. 2011, 21:189-200.
    • (2011) Brain Pathol. , vol.21 , pp. 189-200
    • Bose, A.1    Mouton-Liger, F.2    Paquet, C.3    Mazot, P.4    Vigny, M.5    Gray, F.6    Hugon, J.7
  • 37
    • 77958530620 scopus 로고    scopus 로고
    • Phospho-eIF2alpha level is important for determining abilities of BACE1 reduction to rescue cholinergic neurodegeneration and memory defects in 5XFAD mice
    • Devi L., Ohno M. Phospho-eIF2alpha level is important for determining abilities of BACE1 reduction to rescue cholinergic neurodegeneration and memory defects in 5XFAD mice. PLoS One 2010, 5:e12974.
    • (2010) PLoS One , vol.5
    • Devi, L.1    Ohno, M.2
  • 39
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding H.P., Zhang Y., Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 1999, 397:271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 40
    • 3843117589 scopus 로고    scopus 로고
    • Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells
    • Vattem K.M., Wek R.C. Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:11269-11274.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11269-11274
    • Vattem, K.M.1    Wek, R.C.2
  • 42
    • 4344681535 scopus 로고    scopus 로고
    • Expression of the Alzheimer protease BACE1 is suppressed via its 5'-untranslated region
    • Lammich S., Schobel S., Zimmer A.K., Lichtenthaler S.F., Haass C. Expression of the Alzheimer protease BACE1 is suppressed via its 5'-untranslated region. EMBO Rep. 2004, 5:620-625.
    • (2004) EMBO Rep. , vol.5 , pp. 620-625
    • Lammich, S.1    Schobel, S.2    Zimmer, A.K.3    Lichtenthaler, S.F.4    Haass, C.5
  • 43
    • 34250641977 scopus 로고    scopus 로고
    • Complex translational regulation of BACE1 involves upstream AUGs and stimulatory elements within the 5' untranslated region
    • Mihailovich M., Thermann R., Grohovaz F., Hentze M.W., Zacchetti D. Complex translational regulation of BACE1 involves upstream AUGs and stimulatory elements within the 5' untranslated region. Nucleic Acids Res. 2007, 35:2975-2985.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2975-2985
    • Mihailovich, M.1    Thermann, R.2    Grohovaz, F.3    Hentze, M.W.4    Zacchetti, D.5
  • 44
    • 0037096193 scopus 로고    scopus 로고
    • The relationship between oxidative/nitrative stress and pathological inclusions in Alzheimer's and Parkinson's diseases
    • Giasson B.I., Ischiropoulos H., Lee V.M., Trojanowski J.Q. The relationship between oxidative/nitrative stress and pathological inclusions in Alzheimer's and Parkinson's diseases. Free Radic. Biol. Med. 2002, 32:1264-1275.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1264-1275
    • Giasson, B.I.1    Ischiropoulos, H.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 47
    • 33644845279 scopus 로고    scopus 로고
    • Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease
    • Reddy P.H. Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease. J. Neurochem. 2006, 96:1-13.
    • (2006) J. Neurochem. , vol.96 , pp. 1-13
    • Reddy, P.H.1
  • 52
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 2001, 29:e45.
    • (2001) Nucleic Acids Res. , vol.29
    • Pfaffl, M.W.1
  • 54
    • 13844265969 scopus 로고    scopus 로고
    • BACE overexpression alters the subcellular processing of APP and inhibits Abeta deposition in vivo
    • Lee E.B., Zhang B., Liu K., Greenbaum E.A., Doms R.W., Trojanowski J.Q., Lee V.M. BACE overexpression alters the subcellular processing of APP and inhibits Abeta deposition in vivo. J. Cell Biol. 2005, 168:291-302.
    • (2005) J. Cell Biol. , vol.168 , pp. 291-302
    • Lee, E.B.1    Zhang, B.2    Liu, K.3    Greenbaum, E.A.4    Doms, R.W.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 55
    • 0035231288 scopus 로고    scopus 로고
    • Initiation factor eIF2 alpha phosphorylation in stress responses and apoptosis
    • Clemens M.J. Initiation factor eIF2 alpha phosphorylation in stress responses and apoptosis. Prog. Mol. Subcell. Biol. 2001, 27:57-89.
    • (2001) Prog. Mol. Subcell. Biol. , vol.27 , pp. 57-89
    • Clemens, M.J.1
  • 56
    • 0035231980 scopus 로고    scopus 로고
    • Regulation of eukaryotic initiation factor eIF2B
    • Proud C.G. Regulation of eukaryotic initiation factor eIF2B. Prog. Mol. Subcell. Biol. 2001, 26:95-114.
    • (2001) Prog. Mol. Subcell. Biol. , vol.26 , pp. 95-114
    • Proud, C.G.1
  • 57
    • 38949167101 scopus 로고    scopus 로고
    • Activation of protein kinase C modulates BACE1-mediated beta-secretase activity
    • Wang L., Shim H., Xie C., Cai H. Activation of protein kinase C modulates BACE1-mediated beta-secretase activity. Neurobiol. Aging 2008, 29:357-367.
    • (2008) Neurobiol. Aging , vol.29 , pp. 357-367
    • Wang, L.1    Shim, H.2    Xie, C.3    Cai, H.4
  • 58
    • 34347225099 scopus 로고    scopus 로고
    • The dsRNA protein kinase PKR: virus and cell control
    • Garcia M.A., Meurs E.F., Esteban M. The dsRNA protein kinase PKR: virus and cell control. Biochimie 2007, 89:799-811.
    • (2007) Biochimie , vol.89 , pp. 799-811
    • Garcia, M.A.1    Meurs, E.F.2    Esteban, M.3
  • 59
    • 33645650679 scopus 로고    scopus 로고
    • Activation of the RNA-dependent protein kinase PKR promoter in the absence of interferon is dependent upon Sp proteins
    • Das S., Ward S.V., Tacke R.S., Suske G., Samuel C.E. Activation of the RNA-dependent protein kinase PKR promoter in the absence of interferon is dependent upon Sp proteins. J. Biol. Chem. 2006, 281:3244-3253.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3244-3253
    • Das, S.1    Ward, S.V.2    Tacke, R.S.3    Suske, G.4    Samuel, C.E.5
  • 60
    • 18844457095 scopus 로고    scopus 로고
    • Mechanisms of type-I- and type-II-interferon-mediated signalling
    • Platanias L.C. Mechanisms of type-I- and type-II-interferon-mediated signalling. Nat. Rev. Immunol. 2005, 5:375-386.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 375-386
    • Platanias, L.C.1
  • 61
    • 33644920657 scopus 로고    scopus 로고
    • Control of APP processing and Abeta generation level by BACE1 enzymatic activity and transcription
    • Li Y., Zhou W., Tong Y., He G., Song W. Control of APP processing and Abeta generation level by BACE1 enzymatic activity and transcription. FASEB J. 2006, 20:285-292.
    • (2006) FASEB J. , vol.20 , pp. 285-292
    • Li, Y.1    Zhou, W.2    Tong, Y.3    He, G.4    Song, W.5
  • 65
    • 33646171699 scopus 로고    scopus 로고
    • Divergent roles of IRE1alpha and PERK in the unfolded protein response
    • Schroder M., Kaufman R.J. Divergent roles of IRE1alpha and PERK in the unfolded protein response. Curr. Mol. Med. 2006, 6:5-36.
    • (2006) Curr. Mol. Med. , vol.6 , pp. 5-36
    • Schroder, M.1    Kaufman, R.J.2
  • 66
    • 0028695223 scopus 로고
    • The eIF-2 alpha kinases: regulators of protein synthesis in starvation and stress
    • Hinnebusch A.G. The eIF-2 alpha kinases: regulators of protein synthesis in starvation and stress. Semin. Cell Biol. 1994, 5:417-426.
    • (1994) Semin. Cell Biol. , vol.5 , pp. 417-426
    • Hinnebusch, A.G.1
  • 67
    • 5444264022 scopus 로고    scopus 로고
    • Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response
    • Lu P.D., Harding H.P., Ron D. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J. Cell Biol. 2004, 167:27-33.
    • (2004) J. Cell Biol. , vol.167 , pp. 27-33
    • Lu, P.D.1    Harding, H.P.2    Ron, D.3
  • 69
    • 28844478867 scopus 로고    scopus 로고
    • EIF2B, a mediator of general and gene-specific translational control
    • Pavitt G.D. eIF2B, a mediator of general and gene-specific translational control. Biochem. Soc. Trans. 2005, 33:1487-1492.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1487-1492
    • Pavitt, G.D.1
  • 70
    • 69349091132 scopus 로고    scopus 로고
    • Oxidative stress promotes JNK-dependent amyloidogenic processing of normally expressed human APP by differential modification of alpha-, beta- and gamma-secretase expression
    • Quiroz-Baez R., Rojas E., Arias C. Oxidative stress promotes JNK-dependent amyloidogenic processing of normally expressed human APP by differential modification of alpha-, beta- and gamma-secretase expression. Neurochem. Int. 2009, 55:662-670.
    • (2009) Neurochem. Int. , vol.55 , pp. 662-670
    • Quiroz-Baez, R.1    Rojas, E.2    Arias, C.3
  • 71
    • 79952106055 scopus 로고    scopus 로고
    • Differential regulation of BACE1 expression by oxidative and nitrosative signals
    • Kwak Y.D., Wang R., Li J.J., Zhang Y.W., Xu H., Liao F.F. Differential regulation of BACE1 expression by oxidative and nitrosative signals. Mol. Neurodegener. 2011, 6:17.
    • (2011) Mol. Neurodegener. , vol.6 , pp. 17
    • Kwak, Y.D.1    Wang, R.2    Li, J.J.3    Zhang, Y.W.4    Xu, H.5    Liao, F.F.6
  • 72
    • 0034663942 scopus 로고    scopus 로고
    • The protein kinase PKR is required for p38 MAPK activation and the innate immune response to bacterial endotoxin
    • Goh K.C., deVeer M.J., Williams B.R. The protein kinase PKR is required for p38 MAPK activation and the innate immune response to bacterial endotoxin. EMBO J. 2000, 19:4292-4297.
    • (2000) EMBO J. , vol.19 , pp. 4292-4297
    • Goh, K.C.1    deVeer, M.J.2    Williams, B.R.3
  • 73
    • 0033970937 scopus 로고    scopus 로고
    • Activation of p38 mitogen-activated protein kinase and c-Jun NH(2)-terminal kinase by double-stranded RNA and encephalomyocarditis virus: involvement of RNase L, protein kinase R, and alternative pathways
    • Iordanov M.S., Paranjape J.M., Zhou A., Wong J., Williams B.R., Meurs E.F., Silverman R.H., Magun B.E. Activation of p38 mitogen-activated protein kinase and c-Jun NH(2)-terminal kinase by double-stranded RNA and encephalomyocarditis virus: involvement of RNase L, protein kinase R, and alternative pathways. Mol. Cell. Biol. 2000, 20:617-627.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 617-627
    • Iordanov, M.S.1    Paranjape, J.M.2    Zhou, A.3    Wong, J.4    Williams, B.R.5    Meurs, E.F.6    Silverman, R.H.7    Magun, B.E.8
  • 74
    • 78650176190 scopus 로고    scopus 로고
    • Doxorubicin bypasses the cytoprotective effects of eIF2alpha phosphorylation and promotes PKR-mediated cell death
    • Peidis P., Papadakis A.I., Muaddi H., Richard S., Koromilas A.E. Doxorubicin bypasses the cytoprotective effects of eIF2alpha phosphorylation and promotes PKR-mediated cell death. Cell Death Differ. 2010, 18:145-154.
    • (2010) Cell Death Differ. , vol.18 , pp. 145-154
    • Peidis, P.1    Papadakis, A.I.2    Muaddi, H.3    Richard, S.4    Koromilas, A.E.5
  • 75
    • 0041589432 scopus 로고    scopus 로고
    • Role of double-stranded RNA-activated protein kinase R (PKR) in deoxynivalenol-induced ribotoxic stress response
    • Zhou H.R., Lau A.S., Pestka J.J. Role of double-stranded RNA-activated protein kinase R (PKR) in deoxynivalenol-induced ribotoxic stress response. Toxicol. Sci. 2003, 74:335-344.
    • (2003) Toxicol. Sci. , vol.74 , pp. 335-344
    • Zhou, H.R.1    Lau, A.S.2    Pestka, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.