메뉴 건너뛰기




Volumn 112, Issue 1, 2010, Pages 238-245

Activation of PERK kinase in neural cells by proteasome inhibitor treatment

Author keywords

Aging; Neurotoxicity; P38 kinase; Proteolysis; Ubiquitin

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BETA ACTIN; BORTEZOMIB; MG 115; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN KINASE; PROTEIN PERK; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 71649104120     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2009.06448.x     Document Type: Article
Times cited : (13)

References (67)
  • 1
    • 2642551603 scopus 로고    scopus 로고
    • Development of the proteasome inhibitor Velcade (Bortezomib)
    • Adams J. Kauffman M. (2004) Development of the proteasome inhibitor Velcade (Bortezomib). Cancer Invest. 22, 304 311.
    • (2004) Cancer Invest. , vol.22 , pp. 304-311
    • Adams, J.1    Kauffman, M.2
  • 2
    • 0033324249 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis in learning and memory
    • Chain D. G., Schwartz J. H. Hegde A. N. (1999) Ubiquitin-mediated proteolysis in learning and memory. Mol. Neurobiol. 20, 125 142.
    • (1999) Mol. Neurobiol. , vol.20 , pp. 125-142
    • Chain, D.G.1    Schwartz, J.H.2    Hegde, A.N.3
  • 3
    • 0042346327 scopus 로고    scopus 로고
    • Central role of the proteasome in senescence and survival of human fibroblasts: Induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation
    • Chondrogianni N., Stratford F. L., Trougakos I. P., Friguet B., Rivett A. J. Gonos E. S. (2003) Central role of the proteasome in senescence and survival of human fibroblasts: induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation. J. Biol. Chem. 278, 28026 28037.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28026-28037
    • Chondrogianni, N.1    Stratford, F.L.2    Trougakos, I.P.3    Friguet, B.4    Rivett, A.J.5    Gonos, E.S.6
  • 4
    • 17144414925 scopus 로고    scopus 로고
    • Overexpression of proteasome beta5 assembled subunit increases the amount of proteasome and confers ameliorated response to oxidative stress and higher survival rates
    • Chondrogianni N., Tzavelas C., Pemberton A. J., Nezis I. P., Rivett A. J. Gonos E. S. (2005) Overexpression of proteasome beta5 assembled subunit increases the amount of proteasome and confers ameliorated response to oxidative stress and higher survival rates. J. Biol. Chem. 280, 11840 11850.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11840-11850
    • Chondrogianni, N.1    Tzavelas, C.2    Pemberton, A.J.3    Nezis, I.P.4    Rivett, A.J.5    Gonos, E.S.6
  • 5
    • 0142250840 scopus 로고    scopus 로고
    • Lack of p53 delays apoptosis, but increases ubiquitinated inclusions, in proteasomal inhibitor-treated cultured cortical neurons
    • Dietrich P., Rideout H. J., Wang Q. Stefanis L. (2003) Lack of p53 delays apoptosis, but increases ubiquitinated inclusions, in proteasomal inhibitor-treated cultured cortical neurons. Mol. Cell. Neurosci. 24, 430 441.
    • (2003) Mol. Cell. Neurosci. , vol.24 , pp. 430-441
    • Dietrich, P.1    Rideout, H.J.2    Wang, Q.3    Stefanis, L.4
  • 6
    • 0142074304 scopus 로고    scopus 로고
    • Does proteasome inhibition play a role in mediating neuropathology and neuron death in Alzheimer's disease?
    • Ding Q. Keller J. N. (2003) Does proteasome inhibition play a role in mediating neuropathology and neuron death in Alzheimer's disease? J. Alzheimers Dis. 5, 241 245.
    • (2003) J. Alzheimers Dis. , vol.5 , pp. 241-245
    • Ding, Q.1    Keller, J.N.2
  • 7
    • 33644652951 scopus 로고    scopus 로고
    • Proteasome regulation of oxidative stress in aging and age-related diseases of the CNS
    • Ding Q., Dimayuga E. Keller J. N. (2006a) Proteasome regulation of oxidative stress in aging and age-related diseases of the CNS. Antioxid. Redox Signal. 8, 163 172.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 163-172
    • Ding, Q.1    Dimayuga, E.2    Keller, J.N.3
  • 8
    • 33745977756 scopus 로고    scopus 로고
    • Proteasome inhibition induces reversible impairments in protein synthesis
    • Ding Q., Dimayuga E., Markesbery W. R. Keller J. N. (2006b) Proteasome inhibition induces reversible impairments in protein synthesis. FASEB J. 20, 1055 1063.
    • (2006) FASEB J. , vol.20 , pp. 1055-1063
    • Ding, Q.1    Dimayuga, E.2    Markesbery, W.R.3    Keller, J.N.4
  • 9
    • 33845610586 scopus 로고    scopus 로고
    • Interplay between protein synthesis and degradation in the CNS: Physiological and pathological implications
    • Ding Q., Cecarini V. Keller J. N. (2007) Interplay between protein synthesis and degradation in the CNS: physiological and pathological implications. Trends Neurosci. 30, 31 36.
    • (2007) Trends Neurosci. , vol.30 , pp. 31-36
    • Ding, Q.1    Cecarini, V.2    Keller, J.N.3
  • 10
    • 35048833816 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase is required for central nervous system myelination
    • Fragoso G., Haines J. D., Roberston J., Pedraza L., Mushynski W. E. Almazan G. (2007) p38 mitogen-activated protein kinase is required for central nervous system myelination. Glia 55, 1531 1541.
    • (2007) Glia , vol.55 , pp. 1531-1541
    • Fragoso, G.1    Haines, J.D.2    Roberston, J.3    Pedraza, L.4    Mushynski, W.E.5    Almazan, G.6
  • 11
    • 7644242953 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 induces apoptosis through induction of endoplasmic reticulum stress-reactive oxygen species in head and neck squamous cell carcinoma cells
    • Fribley A., Zeng Q. Wang C. Y. (2004) Proteasome inhibitor PS-341 induces apoptosis through induction of endoplasmic reticulum stress-reactive oxygen species in head and neck squamous cell carcinoma cells. Mol. Cell. Biol. 24, 9695 9704.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9695-9704
    • Fribley, A.1    Zeng, Q.2    Wang, C.Y.3
  • 12
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A. L. (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895 899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 14
    • 0036268224 scopus 로고    scopus 로고
    • Hypothesis: Proteasomal dysfunction a primary event in neurodegeneration that leads to nitrative and oxidative stress and subsequent neuron death
    • Halliwell B. (2002) Hypothesis: proteasomal dysfunction a primary event in neurodegeneration that leads to nitrative and oxidative stress and subsequent neuron death. Ann. N Y Acad. Sci. 962, 182 194.
    • (2002) Ann. N y Acad. Sci. , vol.962 , pp. 182-194
    • Halliwell, B.1
  • 15
    • 28644441875 scopus 로고    scopus 로고
    • PERK and GCN2 contribute to eIF2alpha phosphorylation and cell cycle arrest after activation of the unfolded protein response pathway
    • Hamanaka R. B., Bennett B. S., Cullinan S. B. Diehl J. A. (2005) PERK and GCN2 contribute to eIF2alpha phosphorylation and cell cycle arrest after activation of the unfolded protein response pathway. Mol. Biol. Cell 16, 5493 5501.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5493-5501
    • Hamanaka, R.B.1    Bennett, B.S.2    Cullinan, S.B.3    Diehl, J.A.4
  • 16
    • 34547212349 scopus 로고    scopus 로고
    • The pathways to tumor suppression via route p38
    • Han J. Sun P. (2007) The pathways to tumor suppression via route p38. Trends Biochem. Sci. 32, 364 371.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 364-371
    • Han, J.1    Sun, P.2
  • 17
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding H. P., Novoa I., Zhang Y., Zeng H., Wek R., Schapira M. Ron D. (2000a) Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6, 1099 1108.
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 18
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding H. P., Zhang Y., Bertolotti A., Zeng H. Ron D. (2000b) Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell 5, 897 904.
    • (2000) Mol. Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 20
    • 33750057386 scopus 로고    scopus 로고
    • Ubiquitin proteasome system as a pharmacological target in neurodegeneration
    • Hol E. M., Fischer D. F., Ovaa H. Scheper W. (2006) Ubiquitin proteasome system as a pharmacological target in neurodegeneration. Expert Rev. Neurother. 6, 1337 1347.
    • (2006) Expert Rev. Neurother. , vol.6 , pp. 1337-1347
    • Hol, E.M.1    Fischer, D.F.2    Ovaa, H.3    Scheper, W.4
  • 23
    • 35848938280 scopus 로고    scopus 로고
    • P38alpha: A suppressor of cell proliferation and tumorigenesis
    • Hui L., Bakiri L., Stepniak E. Wagner E. F. (2007) p38alpha: a suppressor of cell proliferation and tumorigenesis. Cell Cycle 6, 2429 2433.
    • (2007) Cell Cycle , vol.6 , pp. 2429-2433
    • Hui, L.1    Bakiri, L.2    Stepniak, E.3    Wagner, E.F.4
  • 24
    • 33847149663 scopus 로고    scopus 로고
    • Reduced eIF2alpha phosphorylation and increased proapoptotic proteins in aging
    • Hussain S. G. Ramaiah K. V. (2007) Reduced eIF2alpha phosphorylation and increased proapoptotic proteins in aging. Biochem. Biophys. Res. Commun. 355, 365 370.
    • (2007) Biochem. Biophys. Res. Commun. , vol.355 , pp. 365-370
    • Hussain, S.G.1    Ramaiah, K.V.2
  • 25
    • 0038155130 scopus 로고    scopus 로고
    • Proteasomal inhibition causes the formation of protein aggregates containing a wide range of proteins, including nitrated proteins
    • Hyun D. H., Lee M., Halliwell B. Jenner P. (2003) Proteasomal inhibition causes the formation of protein aggregates containing a wide range of proteins, including nitrated proteins. J. Neurochem. 86, 363 367.
    • (2003) J. Neurochem. , vol.86 , pp. 363-367
    • Hyun, D.H.1    Lee, M.2    Halliwell, B.3    Jenner, P.4
  • 26
    • 17344371804 scopus 로고    scopus 로고
    • Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: Suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction
    • Keller J. N., Kindy M. S., Holtsberg F. W., St Clair D. K., Yen H. C., Germeyer A., Steiner S. M., Bruce-Keller A. J., Hutchins J. B. Mattson M. P. (1998) Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction. J. Neurosci. 18, 687 697.
    • (1998) J. Neurosci. , vol.18 , pp. 687-697
    • Keller, J.N.1    Kindy, M.S.2    Holtsberg, F.W.3    St Clair, D.K.4    Yen, H.C.5    Germeyer, A.6    Steiner, S.M.7    Bruce-Keller, A.J.8    Hutchins, J.B.9    Mattson, M.P.10
  • 27
    • 0033614712 scopus 로고    scopus 로고
    • Oxidized lipoproteins increase reactive oxygen species formation in microglia and astrocyte cell lines
    • Keller J. N., Hanni K. B., Gabbita S. P., Friebe V., Mattson M. P. Kindy M. S. (1999a) Oxidized lipoproteins increase reactive oxygen species formation in microglia and astrocyte cell lines. Brain Res. 830, 10 15.
    • (1999) Brain Res. , vol.830 , pp. 10-15
    • Keller, J.N.1    Hanni, K.B.2    Gabbita, S.P.3    Friebe, V.4    Mattson, M.P.5    Kindy, M.S.6
  • 28
    • 0033051325 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein induces neuronal death: Implications for calcium, reactive oxygen species, and caspases
    • Keller J. N., Hanni K. B. Markesbery W. R. (1999b) Oxidized low-density lipoprotein induces neuronal death: implications for calcium, reactive oxygen species, and caspases. J. Neurochem. 72, 2601 2609.
    • (1999) J. Neurochem. , vol.72 , pp. 2601-2609
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 29
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller J. N., Hanni K. B. Markesbery W. R. (2000) Impaired proteasome function in Alzheimer's disease. J. Neurochem. 75, 436 439.
    • (2000) J. Neurochem. , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 31
    • 31444449462 scopus 로고    scopus 로고
    • Role of the unfolded protein response in cell death
    • DOI 10.1007/s10495-005-3088-0
    • Kim R., Emi M., Tanabe K. Murakami S. (2006) Role of the unfolded protein response in cell death. Apoptosis 11, 5 13. (Pubitemid 43151639)
    • (2006) Apoptosis , vol.11 , Issue.1 , pp. 5-13
    • Kim, R.1    Emi, M.2    Tanabe, K.3    Murakami, S.4
  • 32
    • 18144363161 scopus 로고    scopus 로고
    • Proteasome inhibition alters glucose-stimulated (pro)insulin secretion and turnover in pancreatic {beta}-cells
    • Kitiphongspattana K., Mathews C. E., Leiter E. H. Gaskins H. R. (2005) Proteasome inhibition alters glucose-stimulated (pro)insulin secretion and turnover in pancreatic {beta}-cells. J. Biol. Chem. 280, 15727 15734.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15727-15734
    • Kitiphongspattana, K.1    Mathews, C.E.2    Leiter, E.H.3    Gaskins, H.R.4
  • 33
    • 34247391127 scopus 로고    scopus 로고
    • Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins
    • Lam Y. W., Lamond A. I., Mann M. Andersen J. S. (2007) Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins. Curr. Biol. 17, 749 760.
    • (2007) Curr. Biol. , vol.17 , pp. 749-760
    • Lam, Y.W.1    Lamond, A.I.2    Mann, M.3    Andersen, J.S.4
  • 34
    • 54449091703 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase mediates lactacystin-induced dopamine neuron degeneration
    • Li X., Du Y., Fan X., Yang D., Luo G. Le W. (2008) c-Jun N-terminal kinase mediates lactacystin-induced dopamine neuron degeneration. J. Neuropathol. Exp. Neurol. 67, 933 944.
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 933-944
    • Li, X.1    Du, Y.2    Fan, X.3    Yang, D.4    Luo, G.5    Le, W.6
  • 35
    • 0037072813 scopus 로고    scopus 로고
    • Apoptotic changes in the aged brain are triggered by interleukin-1beta- induced activation of p38 and reversed by treatment with eicosapentaenoic acid
    • Martin D. S., Lonergan P. E., Boland B., Fogarty M. P., Brady M., Horrobin D. F., Campbell V. A. Lynch M. A. (2002) Apoptotic changes in the aged brain are triggered by interleukin-1beta-induced activation of p38 and reversed by treatment with eicosapentaenoic acid. J. Biol. Chem. 277, 34239 34246.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34239-34246
    • Martin, D.S.1    Lonergan, P.E.2    Boland, B.3    Fogarty, M.P.4    Brady, M.5    Horrobin, D.F.6    Campbell, V.A.7    Lynch, M.A.8
  • 36
    • 16544362156 scopus 로고    scopus 로고
    • Proteolytic dysfunction in neurodegenerative disorders
    • McNaught K. S. (2004) Proteolytic dysfunction in neurodegenerative disorders. Int. Rev. Neurobiol. 62, 95 119.
    • (2004) Int. Rev. Neurobiol. , vol.62 , pp. 95-119
    • McNaught, K.S.1
  • 37
    • 48549090526 scopus 로고    scopus 로고
    • Aging impairs the unfolded protein response to sleep deprivation and leads to proapoptotic signaling
    • Naidoo N., Ferber M., Master M., Zhu Y. Pack A. I. (2008) Aging impairs the unfolded protein response to sleep deprivation and leads to proapoptotic signaling. J. Neurosci. 28, 6539 6548.
    • (2008) J. Neurosci. , vol.28 , pp. 6539-6548
    • Naidoo, N.1    Ferber, M.2    Master, M.3    Zhu, Y.4    Pack, A.I.5
  • 38
    • 29244470510 scopus 로고    scopus 로고
    • Bortezomib inhibits PKR-like endoplasmic reticulum (ER) kinase and induces apoptosis via ER stress in human pancreatic cancer cells
    • Nawrocki S. T., Carew J. S., Dunner K. Jr., Boise L. H., Chiao P. J., Huang P., Abbruzzese J. L. McConkey D. J. (2005) Bortezomib inhibits PKR-like endoplasmic reticulum (ER) kinase and induces apoptosis via ER stress in human pancreatic cancer cells. Cancer Res. 65, 11510 11519.
    • (2005) Cancer Res. , vol.65 , pp. 11510-11519
    • Nawrocki, S.T.1    Carew, J.S.2    Dunner Jr., K.3    Boise, L.H.4    Chiao, P.J.5    Huang, P.6    Abbruzzese, J.L.7    McConkey, D.J.8
  • 39
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng E. A., Carlson L. M., Gutman D. M., Harrington W. J. Jr., Lee K. P. Boise L. H. (2006) Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood 107, 4907 4916.
    • (2006) Blood , vol.107 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3    Harrington, Jr.W.J.4    Lee, K.P.5    Boise, L.H.6
  • 40
    • 33748345432 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system and Parkinson's disease
    • Olanow C. W. McNaught K. S. (2006) Ubiquitin-proteasome system and Parkinson's disease. Mov. Disord. 21, 1806 1823.
    • (2006) Mov. Disord. , vol.21 , pp. 1806-1823
    • Olanow, C.W.1    McNaught, K.S.2
  • 41
    • 1842843855 scopus 로고    scopus 로고
    • Roles of CHOP/GADD153 in endoplasmic reticulum stress
    • Oyadomari S. Mori M. (2004) Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ. 11, 381 389.
    • (2004) Cell Death Differ. , vol.11 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 42
    • 3042730216 scopus 로고    scopus 로고
    • Endoplasmic reticulum dysfunction in brain pathology: Critical role of protein synthesis
    • Paschen W. (2004) Endoplasmic reticulum dysfunction in brain pathology: critical role of protein synthesis. Curr. Neurovasc. Res. 1, 173 181.
    • (2004) Curr. Neurovasc. Res. , vol.1 , pp. 173-181
    • Paschen, W.1
  • 44
    • 36348961452 scopus 로고    scopus 로고
    • HIV-1 protease inhibitors nelfinavir and atazanavir induce malignant glioma death by triggering endoplasmic reticulum stress
    • Pyrko P., Kardosh A., Wang W., Xiong W., Schönthal A. H. Chen T. C. (2007) HIV-1 protease inhibitors nelfinavir and atazanavir induce malignant glioma death by triggering endoplasmic reticulum stress. Cancer Res. 67, 10920 10928.
    • (2007) Cancer Res. , vol.67 , pp. 10920-10928
    • Pyrko, P.1    Kardosh, A.2    Wang, W.3    Xiong, W.4    Schönthal, A.H.5    Chen, T.C.6
  • 45
    • 44349125754 scopus 로고    scopus 로고
    • PERK and PKR: Old kinases learn new tricks
    • Raven J. F. Koromilas A. E. (2008) PERK and PKR: old kinases learn new tricks. Cell Cycle 7, 1146 1150.
    • (2008) Cell Cycle , vol.7 , pp. 1146-1150
    • Raven, J.F.1    Koromilas, A.E.2
  • 46
    • 0034884622 scopus 로고    scopus 로고
    • Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein- immunoreactive inclusions in PC12 cells
    • Rideout H. J., Larsen K. E., Sulzer D. Stefanis L. (2001) Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells. J. Neurochem. 78, 899 908.
    • (2001) J. Neurochem. , vol.78 , pp. 899-908
    • Rideout, H.J.1    Larsen, K.E.2    Sulzer, D.3    Stefanis, L.4
  • 47
    • 0037442820 scopus 로고    scopus 로고
    • Cyclin-dependent kinase activity is required for apoptotic death but not inclusion formation in cortical neurons after proteasomal inhibition
    • Rideout H. J., Wang Q., Park D. S. Stefanis L. (2003) Cyclin-dependent kinase activity is required for apoptotic death but not inclusion formation in cortical neurons after proteasomal inhibition. J. Neurosci. 23, 1237 1245.
    • (2003) J. Neurosci. , vol.23 , pp. 1237-1245
    • Rideout, H.J.1    Wang, Q.2    Park, D.S.3    Stefanis, L.4
  • 48
    • 0037114971 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease
    • Ryu E. J., Harding H. P., Angelastro J. M., Vitolo O. V., Ron D. Greene L. A. (2002) Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J. Neurosci. 22, 10690 10698.
    • (2002) J. Neurosci. , vol.22 , pp. 10690-10698
    • Ryu, E.J.1    Harding, H.P.2    Angelastro, J.M.3    Vitolo, O.V.4    Ron, D.5    Greene, L.A.6
  • 49
    • 33646171699 scopus 로고    scopus 로고
    • Divergent roles of IRE1alpha and PERK in the unfolded protein response
    • Schröder M. Kaufman R. J. (2006) Divergent roles of IRE1alpha and PERK in the unfolded protein response. Curr. Mol. Med. 6, 35 36.
    • (2006) Curr. Mol. Med. , vol.6 , pp. 35-36
    • Schröder, M.1    Kaufman, R.J.2
  • 50
    • 58049088976 scopus 로고    scopus 로고
    • Think locally: Control of ubiquitin-dependent protein degradation in neurons
    • Segref A. Hoppe T. (2009) Think locally: control of ubiquitin-dependent protein degradation in neurons. EMBO Rep. 10, 44 50.
    • (2009) EMBO Rep. , vol.10 , pp. 44-50
    • Segref, A.1    Hoppe, T.2
  • 51
    • 4444303263 scopus 로고    scopus 로고
    • Generalized brain and skin proteasome inhibition in Huntington's disease
    • Seo H., Sonntag K. C. Isacson O. (2004) Generalized brain and skin proteasome inhibition in Huntington's disease. Ann. Neurol. 56, 319 328.
    • (2004) Ann. Neurol. , vol.56 , pp. 319-328
    • Seo, H.1    Sonntag, K.C.2    Isacson, O.3
  • 52
    • 0036591853 scopus 로고    scopus 로고
    • Protein turnover by the proteasome in aging and disease
    • Shringarpure R. Davies K. J. (2002) Protein turnover by the proteasome in aging and disease. Free Radic. Biol. Med. 32, 84 88.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 84-88
    • Shringarpure, R.1    Davies, K.J.2
  • 53
    • 33745169658 scopus 로고    scopus 로고
    • Gene expression analysis of B-lymphoma cells resistant and sensitive to bortezomib
    • Shringarpure R., Catley L., Bhole D. et al. (2006) Gene expression analysis of B-lymphoma cells resistant and sensitive to bortezomib. Br. J. Haematol. 134, 145 156.
    • (2006) Br. J. Haematol. , vol.134 , pp. 145-156
    • Shringarpure, R.1    Catley, L.2    Bhole, D.3
  • 54
    • 59149095868 scopus 로고    scopus 로고
    • Transducing neuronal activity into dendritic spine morphology: New roles for p38 MAP kinase and N-cadherin
    • Sugiura H., Tanaka H., Yasuda S., Takemiya T. Yamagata K. (2009) Transducing neuronal activity into dendritic spine morphology: new roles for p38 MAP kinase and N-cadherin. Neuroscientist 15, 90 104.
    • (2009) Neuroscientist , vol.15 , pp. 90-104
    • Sugiura, H.1    Tanaka, H.2    Yasuda, S.3    Takemiya, T.4    Yamagata, K.5
  • 55
    • 0034846004 scopus 로고    scopus 로고
    • Age-specific changes in expression, activity, and activation of the c-Jun NH(2)-terminal kinase and p38 mitogen-activated protein kinases by methyl methanesulfonate in rats
    • Suh Y. (2001) Age-specific changes in expression, activity, and activation of the c-Jun NH(2)-terminal kinase and p38 mitogen-activated protein kinases by methyl methanesulfonate in rats. Mech. Ageing Dev. 122, 1797 1811.
    • (2001) Mech. Ageing Dev. , vol.122 , pp. 1797-1811
    • Suh, Y.1
  • 57
    • 66249133081 scopus 로고    scopus 로고
    • Proteasome inhibition potentiates antitumor effects of photodynamic therapy in mice through induction of endoplasmic reticulum stress and unfolded protein response
    • Szokalska A., Makowski M., Nowis D. et al. (2009) Proteasome inhibition potentiates antitumor effects of photodynamic therapy in mice through induction of endoplasmic reticulum stress and unfolded protein response. Cancer Res. 69, 4235 4243.
    • (2009) Cancer Res. , vol.69 , pp. 4235-4243
    • Szokalska, A.1    Makowski, M.2    Nowis, D.3
  • 58
    • 1342289413 scopus 로고    scopus 로고
    • MAPK cascade signalling and synaptic plasticity
    • Thomas G. M. Huganir R. L. (2004) MAPK cascade signalling and synaptic plasticity. Nat. Rev. Neurosci. 5, 173 183.
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 173-183
    • Thomas, G.M.1    Huganir, R.L.2
  • 59
    • 60149093582 scopus 로고    scopus 로고
    • Non-classical p38 map kinase functions: Cell cycle checkpoints and survival
    • Thornton T. M. Rincon M. (2008) Non-classical p38 map kinase functions: cell cycle checkpoints and survival. Int. J. Biol. Sci. 5, 44 51.
    • (2008) Int. J. Biol. Sci. , vol.5 , pp. 44-51
    • Thornton, T.M.1    Rincon, M.2
  • 61
    • 0026786503 scopus 로고
    • Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex
    • Vinitsky A., Michaud C., Powers J. C. Orlowski M. (1992) Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry 31, 9421 9428.
    • (1992) Biochemistry , vol.31 , pp. 9421-9428
    • Vinitsky, A.1    Michaud, C.2    Powers, J.C.3    Orlowski, M.4
  • 62
    • 34247172998 scopus 로고    scopus 로고
    • Expanding insights on the involvement of endoplasmic reticulum stress in Parkinson's disease
    • Wang H. Q. Takahashi R. (2007) Expanding insights on the involvement of endoplasmic reticulum stress in Parkinson's disease. Antioxid. Redox Signal. 9, 553 561.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 553-561
    • Wang, H.Q.1    Takahashi, R.2
  • 63
    • 23844516979 scopus 로고    scopus 로고
    • Proteasome inhibition by lactacystin in primary neuronal cells induces both potentially neuroprotective and pro-apoptotic transcriptional responses: A microarray analysis
    • Yew E. H., Cheung N. S., Choy M. S. et al. (2005) Proteasome inhibition by lactacystin in primary neuronal cells induces both potentially neuroprotective and pro-apoptotic transcriptional responses: a microarray analysis. J. Neurochem. 94, 943 956.
    • (2005) J. Neurochem. , vol.94 , pp. 943-956
    • Yew, E.H.1    Cheung, N.S.2    Choy, M.S.3
  • 64
    • 70449465063 scopus 로고    scopus 로고
    • Proteasome inhibition modulates kinase activation in neural cells: Relevance to ubiquitination, ribosomes, and survival
    • Zhang L., Ebenezer P. J., Dasuri K., Bruce-Keller A. J., Liu Y. Keller J. N. (2009) Proteasome inhibition modulates kinase activation in neural cells: Relevance to ubiquitination, ribosomes, and survival. J. Neurosci. Res. 87, 3231 3238.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 3231-3238
    • Zhang, L.1    Ebenezer, P.J.2    Dasuri, K.3    Bruce-Keller, A.J.4    Liu, Y.5    Keller, J.N.6
  • 65
    • 41449095062 scopus 로고    scopus 로고
    • Phosphorylation of eIF2 directs ATF5 translational control in response to diverse stress conditions
    • Zhou D., Palam L. R., Jiang L., Narasimhan J., Staschke K. A. Wek R. C. (2008) Phosphorylation of eIF2 directs ATF5 translational control in response to diverse stress conditions. J. Biol. Chem. 283, 7064 7073.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7064-7073
    • Zhou, D.1    Palam, L.R.2    Jiang, L.3    Narasimhan, J.4    Staschke, K.A.5    Wek, R.C.6
  • 66
    • 0036770144 scopus 로고    scopus 로고
    • The role of mitogen-activated protein kinase pathways in Alzheimer's disease
    • Zhu X., Lee H. G., Raina A. K., Perry G. Smith M. A. (2002) The role of mitogen-activated protein kinase pathways in Alzheimer's disease. Neurosignals 11, 270 281.
    • (2002) Neurosignals , vol.11 , pp. 270-281
    • Zhu, X.1    Lee, H.G.2    Raina, A.K.3    Perry, G.4    Smith, M.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.