메뉴 건너뛰기




Volumn 5, Issue 10, 2010, Pages

Yokukansan inhibits neuronal death during ER stress by regulating the unfolded protein response

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 4; CCAAT ENHANCER BINDING PROTEIN; FERULIC ACID; GLUCOSE REGULATED PROTEIN 78; HERBACEOUS AGENT; NEUROPROTECTIVE AGENT; PRESENILIN 1; TJ 54; UNCLASSIFIED DRUG; YOKUKANSAN; YI GAN SAN; YI-GAN SAN;

EID: 78149429507     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0013280     Document Type: Article
Times cited : (33)

References (49)
  • 1
    • 67049173445 scopus 로고    scopus 로고
    • A randomized cross-over study of a traditional Japanese medicine (kampo), yokukansan, in the treatment of the behavioural and psychological symptoms of dementia
    • Mizukami K, Asada T, Kinoshita T, Tanaka K, Sonohara K, et al. (2009) A randomized cross-over study of a traditional Japanese medicine (kampo), yokukansan, in the treatment of the behavioural and psychological symptoms of dementia. Int J Neuropsychopharmacol 12(2): 191-199.
    • (2009) Int J Neuropsychopharmacol , vol.12 , Issue.2 , pp. 191-199
    • Mizukami, K.1    Asada, T.2    Kinoshita, T.3    Tanaka, K.4    Sonohara, K.5
  • 2
    • 60049099127 scopus 로고    scopus 로고
    • Effect of yokukansan on the behavioral and psychological symptoms of dementia in elderly patients with Alzheimer's disease
    • Monji A, Takita M, Samejima T, Takaishi T, Hashimoto K, et al. (2009) Effect of yokukansan on the behavioral and psychological symptoms of dementia in elderly patients with Alzheimer's disease. Prog Neuropsychopharmacol Biol Psychiatry 33(2): 308-311.
    • (2009) Prog Neuropsychopharmacol Biol Psychiatry , vol.33 , Issue.2 , pp. 308-311
    • Monji, A.1    Takita, M.2    Samejima, T.3    Takaishi, T.4    Hashimoto, K.5
  • 4
    • 0037036053 scopus 로고    scopus 로고
    • Evaluation of betaamyloid peptide 25-35 on calcium homeostasis in cultured rat dorsal root ganglion neurons
    • He LM, Chen LY, Lou XL, Qu AL, Zhou Z, et al. (2002) Evaluation of betaamyloid peptide 25-35 on calcium homeostasis in cultured rat dorsal root ganglion neurons. Brain Res 939(1-2): 65-75.
    • (2002) Brain Res , vol.939 , Issue.1-2 , pp. 65-75
    • He, L.M.1    Chen, L.Y.2    Lou, X.L.3    Qu, A.L.4    Zhou, Z.5
  • 5
    • 4344669435 scopus 로고    scopus 로고
    • Cell degeneration induced by amyloid-beta peptides: Implications for Alzheimer's disease
    • Pereira C, Ferreiro E, Cardoso SM, de Oliveira CR (2004) Cell degeneration induced by amyloid-beta peptides: implications for Alzheimer's disease. J Mol Neurosci 23(1-2): 97-104.
    • (2004) J Mol Neurosci , vol.23 , Issue.1-2 , pp. 97-104
    • Pereira, C.1    Ferreiro, E.2    Cardoso, S.M.3    de Oliveira, C.R.4
  • 6
    • 33745019916 scopus 로고    scopus 로고
    • Beta-amyloid peptides induces neuronal apoptosis via a mechanism independent of unfolded protein responses
    • Yu MS, Suen KC, Kwok NS, So KF, Hugon J, et al. (2006) Beta-amyloid peptides induces neuronal apoptosis via a mechanism independent of unfolded protein responses. Apoptosis 11(5): 687-700.
    • (2006) Apoptosis , vol.11 , Issue.5 , pp. 687-700
    • Yu, M.S.1    Suen, K.C.2    Kwok, N.S.3    So, K.F.4    Hugon, J.5
  • 7
    • 0033258544 scopus 로고    scopus 로고
    • Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response
    • Katayama T, Imaizumi K, Sato N, Miyoshi K, Kudo T, et al. (1999) Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response. Nat Cell Biol 1(8): 479-485.
    • (1999) Nat Cell Biol , vol.1 , Issue.8 , pp. 479-485
    • Katayama, T.1    Imaizumi, K.2    Sato, N.3    Miyoshi, K.4    Kudo, T.5
  • 8
    • 0035900779 scopus 로고    scopus 로고
    • Disturbed activation of endoplasmic reticulum stress transducers by familial Alzheimer's disease-linked presenilin-1 mutations
    • Katayama T, Imaizumi K, Honda A, Yoneda T, Kudo T, et al. (2001) Disturbed activation of endoplasmic reticulum stress transducers by familial Alzheimer's disease-linked presenilin-1 mutations. J Biol Chem 276(46): 43446-43454.
    • (2001) J Biol Chem , vol.276 , Issue.46 , pp. 43446-43454
    • Katayama, T.1    Imaizumi, K.2    Honda, A.3    Yoneda, T.4    Kudo, T.5
  • 9
    • 0032973469 scopus 로고    scopus 로고
    • A novel presenilin-2 splice variant in human Alzheimer's disease brain tissue
    • Sato N, Hori O, Yamaguchi A, Lambert JC, Chartier-Harlin MC, et al. (1999) A novel presenilin-2 splice variant in human Alzheimer's disease brain tissue. J Neurochem 72(6): 2498-2505.
    • (1999) J Neurochem , vol.72 , Issue.6 , pp. 2498-2505
    • Sato, N.1    Hori, O.2    Yamaguchi, A.3    Lambert, J.C.4    Chartier-Harlin, M.C.5
  • 10
    • 0035910471 scopus 로고    scopus 로고
    • Increased production of beta-amyloid and vulnerability to endoplasmic reticulum stress by an aberrant spliced form of presenilin 2
    • Sato N, Imaizumi K, Manabe T, Taniguchi M, Hitomi J, et al. (2001) Increased production of beta-amyloid and vulnerability to endoplasmic reticulum stress by an aberrant spliced form of presenilin 2. J Biol Chem 276(3): 2108-2114.
    • (2001) J Biol Chem , vol.276 , Issue.3 , pp. 2108-2114
    • Sato, N.1    Imaizumi, K.2    Manabe, T.3    Taniguchi, M.4    Hitomi, J.5
  • 11
    • 12144288051 scopus 로고    scopus 로고
    • Metals accelerate production of the aberrant splicing isoform of the presenilin-2
    • Matsuzaki S, Manabe T, Katayama T, Nishikawa A, Yanagita T, et al. (2004) Metals accelerate production of the aberrant splicing isoform of the presenilin-2. J Neurochem 88(6): 1345-51.
    • (2004) J Neurochem , vol.88 , Issue.6 , pp. 1345-1351
    • Matsuzaki, S.1    Manabe, T.2    Katayama, T.3    Nishikawa, A.4    Yanagita, T.5
  • 12
    • 0037636434 scopus 로고    scopus 로고
    • Induced HMGA1a expression causes aberrant splicing of Presenilin-2 pre-mRNA in sporadic Alzheimer's disease
    • Manabe T, Katayama T, Sato N, Gomi F, Hitomi J, et al. (2003) Induced HMGA1a expression causes aberrant splicing of Presenilin-2 pre-mRNA in sporadic Alzheimer's disease. Cell Death Differ 10(6): 698-708.
    • (2003) Cell Death Differ , vol.10 , Issue.6 , pp. 698-708
    • Manabe, T.1    Katayama, T.2    Sato, N.3    Gomi, F.4    Hitomi, J.5
  • 13
    • 0032101239 scopus 로고    scopus 로고
    • The unfolded protein response: An intracellular signaling pathway with many surprising features
    • Sidrauski C, Chapman R, Walter P (1998) The unfolded protein response: an intracellular signaling pathway with many surprising features. Trends Cell Biol 8: 245-249.
    • (1998) Trends Cell Biol , vol.8 , pp. 245-249
    • Sidrauski, C.1    Chapman, R.2    Walter, P.3
  • 14
    • 0032525990 scopus 로고    scopus 로고
    • A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells
    • Tirasophon W, Welihinda AA, Kaufman RJ (1998) A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev 12: 1812-1824.
    • (1998) Genes Dev , vol.12 , pp. 1812-1824
    • Tirasophon, W.1    Welihinda, A.A.2    Kaufman, R.J.3
  • 15
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi Y, Segal M, Normington K, Gething MJ, Sambrook JF (1988) The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332: 462-464.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.F.5
  • 16
    • 0036022403 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells
    • Oyadomari S, Araki E, Mori M (2002) Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells. Apoptosis 7(4): 335-45.
    • (2002) Apoptosis , vol.7 , Issue.4 , pp. 335-345
    • Oyadomari, S.1    Araki, E.2    Mori, M.3
  • 17
    • 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(4): 381-9.
    • (2004) Cell Death Differ , vol.11 , Issue.4 , pp. 381-389
    • Oyadomari, S.1    Mori, M.2
  • 18
    • 2442432416 scopus 로고    scopus 로고
    • Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death
    • Hitomi J, Katayama T, Eguchi Y, Kudo T, Taniguchi M, et al. (2004) Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death. J Cell Biol 165(3): 347-356.
    • (2004) J Cell Biol , vol.165 , Issue.3 , pp. 347-356
    • Hitomi, J.1    Katayama, T.2    Eguchi, Y.3    Kudo, T.4    Taniguchi, M.5
  • 19
    • 38349169247 scopus 로고    scopus 로고
    • Presenilin-1 mutation activates the signaling pathway of caspase-4 in endoplasmic reticulum stress-induced apoptosis
    • Yukioka F, Matsuzaki S, Kawamoto K, Koyama Y, Hitomi J, et al. (2008) Presenilin-1 mutation activates the signaling pathway of caspase-4 in endoplasmic reticulum stress-induced apoptosis. Neurochem Int 52(4-5): 683-687.
    • (2008) Neurochem Int , vol.52 , Issue.4-5 , pp. 683-687
    • Yukioka, F.1    Matsuzaki, S.2    Kawamoto, K.3    Koyama, Y.4    Hitomi, J.5
  • 20
    • 34247230858 scopus 로고    scopus 로고
    • Ferulic Acid: Therapeutic potential through its antioxidant property
    • Srinivasan M, Sudheer AR, Menon VP (2007) Ferulic Acid: therapeutic potential through its antioxidant property, J Clin Biochem Nutr 40: 92-100.
    • (2007) J Clin Biochem Nutr , vol.40 , pp. 92-100
    • Srinivasan, M.1    Sudheer, A.R.2    Menon, V.P.3
  • 21
    • 0020450453 scopus 로고
    • Anti-inflammatory and irritant activities of curcumin analogues in rats
    • Mukhopadhyay A, Basu, Ghatak N, Gujral PK (1982) Anti-inflammatory and irritant activities of curcumin analogues in rats, Agents Actions 12: 508-515.
    • (1982) Agents Actions , vol.12 , pp. 508-515
    • Mukhopadhyay, A.1    Basu2    Ghatak, N.3    Gujral, P.K.4
  • 22
    • 0034739333 scopus 로고    scopus 로고
    • Modifying effects of ferulic acid on azoxymethane-induced colon carcinogenesis in F344 rats
    • Kawabata K, Yamamoto T, Hara A, Shimizu M, Yamada Y, et al. (2000) Modifying effects of ferulic acid on azoxymethane-induced colon carcinogenesis in F344 rats, Cancer Lett 157: 15-21.
    • (2000) Cancer Lett , vol.157 , pp. 15-21
    • Kawabata, K.1    Yamamoto, T.2    Hara, A.3    Shimizu, M.4    Yamada, Y.5
  • 24
    • 13644265462 scopus 로고    scopus 로고
    • Ferulic acid ethyl ester protects neurons against amyloid beta-peptide(1- 42)-induced oxidative stress and neurotoxicity: Relationship to antioxidant activity
    • Sultana R, Ravagna A, Mohmmad-Abdul H, Calabrese V, Butterfield DA (2005) Ferulic acid ethyl ester protects neurons against amyloid beta-peptide(1- 42)-induced oxidative stress and neurotoxicity: relationship to antioxidant activity, J Neurochem 92: 749-758.
    • (2005) J Neurochem , vol.92 , pp. 749-758
    • Sultana, R.1    Ravagna, A.2    Mohmmad-Abdul, H.3    Calabrese, V.4    Butterfield, D.A.5
  • 25
    • 33646246958 scopus 로고    scopus 로고
    • Attenuation of abnormalities in the lipid metabolism during experimental myocardial infarction induced by isoproterenol in rats: Beneficial effect of ferulic acid and ascorbic acid
    • Yogeeta SK, Hanumantra RB, Gnanapragasam A, Senthilkumar S, Subhashini R et al (2006) Attenuation of abnormalities in the lipid metabolism during experimental myocardial infarction induced by isoproterenol in rats: beneficial effect of ferulic acid and ascorbic acid, Basic Clin Pharmacol Toxicol 98: 467-472.
    • (2006) Basic Clin Pharmacol Toxicol , vol.98 , pp. 467-472
    • Yogeeta, S.K.1    Hanumantra, R.B.2    Gnanapragasam, A.3    Senthilkumar, S.4    Subhashini, R.5
  • 26
    • 0034986151 scopus 로고    scopus 로고
    • Protection against betaamyloid peptide toxicity in vivo with long-term administration of ferulic acid
    • Yan JJ, Cho JY, Kim HS, Kim KL, Jung JS, et al. (2001) Protection against betaamyloid peptide toxicity in vivo with long-term administration of ferulic acid. Br J Pharmacol 133(1): 89-96.
    • (2001) Br J Pharmacol , vol.133 , Issue.1 , pp. 89-96
    • Yan, J.J.1    Cho, J.Y.2    Kim, H.S.3    Kim, K.L.4    Jung, J.S.5
  • 27
    • 70350534700 scopus 로고    scopus 로고
    • Ferulic acid inhibits oxidative stress and cell death induced by Ab oligomers: Improved delivery by solid lipid nanoparticles
    • Picone P, Bondi ML, Montana G, Bruno A, Pitarresi G, et al. (2009) Ferulic acid inhibits oxidative stress and cell death induced by Ab oligomers: improved delivery by solid lipid nanoparticles. Free Radic Res 43(11): 1133-45.
    • (2009) Free Radic Res , vol.43 , Issue.11 , pp. 1133-1145
    • Picone, P.1    Bondi, M.L.2    Montana, G.3    Bruno, A.4    Pitarresi, G.5
  • 28
    • 33845742025 scopus 로고    scopus 로고
    • Thiamine deficiency induces endoplasmic reticulum stress in neurons
    • Wang X, Wang B, Fan Z, Shi X, Ke ZJ, et al. (2006) Thiamine deficiency induces endoplasmic reticulum stress in neurons. Neuroscience 144(3): 1045-56.
    • (2006) Neuroscience , vol.144 , Issue.3 , pp. 1045-1056
    • Wang, X.1    Wang, B.2    Fan, Z.3    Shi, X.4    Ke, Z.J.5
  • 29
    • 70349960037 scopus 로고    scopus 로고
    • Effects of yokukansan, a traditional Japanese medicine, on memory disturbance and behavioral and psychological symptoms of dementia in thiamine-deficient rats
    • Ikarashi Y, Iizuka S, Imamura S, Yamaguchi T, Sekiguchi K, et al. (2009) Effects of yokukansan, a traditional Japanese medicine, on memory disturbance and behavioral and psychological symptoms of dementia in thiamine-deficient rats. Biol Pharm Bull 32(10): 1701-9.
    • (2009) Biol Pharm Bull , vol.32 , Issue.10 , pp. 1701-1709
    • Ikarashi, Y.1    Iizuka, S.2    Imamura, S.3    Yamaguchi, T.4    Sekiguchi, K.5
  • 30
    • 77957322358 scopus 로고    scopus 로고
    • Electron-microscopic examination of effects of yokukansan, a traditional Japanese medicine, on degeneration of cerebral cells in thiamine-deficient rats
    • In press
    • Iizuka S, Kawakami Z, Imamura S, Yamaguchi T, Sekiguchi K, et al. (2010) Electron-microscopic examination of effects of yokukansan, a traditional Japanese medicine, on degeneration of cerebral cells in thiamine-deficient rats. Neuropathology, In press.
    • (2010) Neuropathology
    • Iizuka, S.1    Kawakami, Z.2    Imamura, S.3    Yamaguchi, T.4    Sekiguchi, K.5
  • 31
    • 51349169371 scopus 로고    scopus 로고
    • Neuroprotective effects of Yi-Gan San against beta amyloid-induced cytotoxicity on rat cortical neurons
    • Tateno M, Ukai W, Ono T, Saito S, Hashimoto E, et al. (2008) Neuroprotective effects of Yi-Gan San against beta amyloid-induced cytotoxicity on rat cortical neurons. Prog Neuropsychopharmacol Biol Psychiatry 32(7): 1704-1707.
    • (2008) Prog Neuropsychopharmacol Biol Psychiatry , vol.32 , Issue.7 , pp. 1704-1707
    • Tateno, M.1    Ukai, W.2    Ono, T.3    Saito, S.4    Hashimoto, E.5
  • 32
    • 68049097888 scopus 로고    scopus 로고
    • Effects of yokukansan, a traditional Japanese medicine, on aggressiveness induced by intracerebroventricular injection of amyloid beta protein into mice
    • Sekiguchi K, Yamaguchi T, Tabuchi M, Ikarashi Y, Kase Y (2009) Effects of yokukansan, a traditional Japanese medicine, on aggressiveness induced by intracerebroventricular injection of amyloid beta protein into mice. Phytother Res 23(8): 1175-81.
    • (2009) Phytother Res , vol.23 , Issue.8 , pp. 1175-1181
    • Sekiguchi, K.1    Yamaguchi, T.2    Tabuchi, M.3    Ikarashi, Y.4    Kase, Y.5
  • 33
    • 21144453720 scopus 로고    scopus 로고
    • The effects of Choto-san on the mRNA expression of Alzheimer's disease related factors in the permanent ischemic rat brain
    • Hayashi H, Tohda M, Watanabe H, Murakami Y, Matsumoto K (2005) The effects of Choto-san on the mRNA expression of Alzheimer's disease related factors in the permanent ischemic rat brain. Biol Pharm Bull 28(4): 744-746.
    • (2005) Biol Pharm Bull , vol.28 , Issue.4 , pp. 744-746
    • Hayashi, H.1    Tohda, M.2    Watanabe, H.3    Murakami, Y.4    Matsumoto, K.5
  • 34
    • 1442323991 scopus 로고    scopus 로고
    • Intraneuronal amyloidbeta1-42 production triggered by sustained increase of cytosolic calcium concentration induces neuronal death
    • Pierrot N, Ghisdal P, Caumont AS, Octave JN (2004) Intraneuronal amyloidbeta1-42 production triggered by sustained increase of cytosolic calcium concentration induces neuronal death. J Neurochem 88: 1140-1150.
    • (2004) J Neurochem , vol.88 , pp. 1140-1150
    • Pierrot, N.1    Ghisdal, P.2    Caumont, A.S.3    Octave, J.N.4
  • 35
    • 0347479364 scopus 로고    scopus 로고
    • A slowly formed transient conformer of Abeta(1-40) is toxic to inward channels of dissociated hippocampal and cortical neurons of rats
    • Sun XD, Mo ZL, Taylor BM, Epps DE (2003) A slowly formed transient conformer of Abeta(1-40) is toxic to inward channels of dissociated hippocampal and cortical neurons of rats. Neurobiol Dis 14: 567-578.
    • (2003) Neurobiol Dis , vol.14 , pp. 567-578
    • Sun, X.D.1    Mo, Z.L.2    Taylor, B.M.3    Epps, D.E.4
  • 36
    • 35848951621 scopus 로고    scopus 로고
    • Abeta 1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner
    • Chafekar SM, Hoozemans JJ, Zwart R, Baas F, Scheper W (2007) Abeta 1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner. Antioxid Redox Signal 9: 2245-2254.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 2245-2254
    • Chafekar, S.M.1    Hoozemans, J.J.2    Zwart, R.3    Baas, F.4    Scheper, W.5
  • 37
    • 41049111771 scopus 로고    scopus 로고
    • Effectiveness of cholinesterase inhibitors and memantine for treating dementia: Evidence review for a clinical practice guideline
    • Raina P, Santaguida P, Ismaila A, Patterson C, Cowan D, et al. (2008) Effectiveness of cholinesterase inhibitors and memantine for treating dementia: evidence review for a clinical practice guideline. Ann Intern Med 148(5): 379-397.
    • (2008) Ann Intern Med , vol.148 , Issue.5 , pp. 379-397
    • Raina, P.1    Santaguida, P.2    Ismaila, A.3    Patterson, C.4    Cowan, D.5
  • 38
    • 36749094556 scopus 로고    scopus 로고
    • NICE cost-effectiveness appraisal of cholinesterase inhibitors: Was the right question posed? Were the best tools used?
    • Getsios D, Migliaccio-Walle K, Caro JJ (2007) NICE cost-effectiveness appraisal of cholinesterase inhibitors: was the right question posed? Were the best tools used? Pharmacoeconomics 25(12): 997-1006.
    • (2007) Pharmacoeconomics , vol.25 , Issue.12 , pp. 997-1006
    • Getsios, D.1    Migliaccio-Walle, K.2    Caro, J.J.3
  • 39
    • 36048939845 scopus 로고    scopus 로고
    • Is long-term treatment of Alzheimer's disease with cholinesterase inhibitor therapy justified?
    • Seltzer B (2007) Is long-term treatment of Alzheimer's disease with cholinesterase inhibitor therapy justified? Drugs Aging 24(11): 881-890.
    • (2007) Drugs Aging , vol.24 , Issue.11 , pp. 881-890
    • Seltzer, B.1
  • 41
    • 34548570017 scopus 로고    scopus 로고
    • One hundred years after the discovery of Alzheimer's disease A turning point for therapy?
    • Giacobini E, Becker RE (2007) One hundred years after the discovery of Alzheimer's disease. A turning point for therapy? J Alzheimers Dis 12(1): 37-52.
    • (2007) J Alzheimers Dis , vol.12 , Issue.1 , pp. 37-52
    • Giacobini, E.1    Becker, R.E.2
  • 42
    • 47949132196 scopus 로고    scopus 로고
    • Active and passive immunotherapy for neurodegenerative disorders
    • Brody DL, Holtzman DM (2008) Active and passive immunotherapy for neurodegenerative disorders. Annu Rev Neurosci 31: 175-193.
    • (2008) Annu Rev Neurosci , vol.31 , pp. 175-193
    • Brody, D.L.1    Holtzman, D.M.2
  • 43
    • 34548681841 scopus 로고    scopus 로고
    • A novel immunotherapy for Alzheimer's disease: Antibodies against the beta-secretase cleavage site of APP
    • Arbel M, Solomon B (2007) A novel immunotherapy for Alzheimer's disease: antibodies against the beta-secretase cleavage site of APP. Curr Alzheimer Res 4(4): 437-445.
    • (2007) Curr Alzheimer Res , vol.4 , Issue.4 , pp. 437-445
    • Arbel, M.1    Solomon, B.2
  • 44
    • 34047117766 scopus 로고    scopus 로고
    • Intravenous immunoglobulin and Alzheimer's disease immunotherapy
    • Solomon B (2007) Intravenous immunoglobulin and Alzheimer's disease immunotherapy. Curr Opin Mol Ther 9(1): 79-85.
    • (2007) Curr Opin Mol Ther , vol.9 , Issue.1 , pp. 79-85
    • Solomon, B.1
  • 45
    • 4043177726 scopus 로고    scopus 로고
    • Clearing tau pathology with Abeta immunotherapy- reversible and irreversible stages revealed
    • Hutton M, McGowan E (2004) Clearing tau pathology with Abeta immunotherapy- reversible and irreversible stages revealed. Neuron 43(3): 293-294.
    • (2004) Neuron , vol.43 , Issue.3 , pp. 293-294
    • Hutton, M.1    McGowan, E.2
  • 46
    • 54249156984 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau protein in Alzheimer's disease and related tauopathies
    • Sigurdsson EM (2008) Immunotherapy targeting pathological tau protein in Alzheimer's disease and related tauopathies. J Alzheimers Dis 15(2): 157-168.
    • (2008) J Alzheimers Dis , vol.15 , Issue.2 , pp. 157-168
    • Sigurdsson, E.M.1
  • 47
    • 0031960313 scopus 로고    scopus 로고
    • A tool coming of age: Thapsigargin as an inhibitor of sarco-endoplasmic reticulum Ca 2 +-ATPases
    • Treiman M, Caspersen C, Christensen SB (1998) A tool coming of age: thapsigargin as an inhibitor of sarco-endoplasmic reticulum Ca 2 +-ATPases. Trends Pharmacol Sci 19: 131-135.
    • (1998) Trends Pharmacol Sci , vol.19 , pp. 131-135
    • Treiman, M.1    Caspersen, C.2    Christensen, S.B.3
  • 48
    • 0023695237 scopus 로고
    • A novel tumour promoter, thapsigargin, transiently increases cytoplasmic free Ca2+ without generation of inositol phosphates in NG115-401L neuronal cells
    • Jackson TR, Patterson SI, Thastrup O, Hanley MR (1988) A novel tumour promoter, thapsigargin, transiently increases cytoplasmic free Ca2+ without generation of inositol phosphates in NG115-401L neuronal cells. Biochem J 253: 81-86.
    • (1988) Biochem J , vol.253 , pp. 81-86
    • Jackson, T.R.1    Patterson, S.I.2    Thastrup, O.3    Hanley, M.R.4
  • 49
    • 0035423875 scopus 로고    scopus 로고
    • The glucose-regulated proteins: Stress induction and clinical applications
    • Lee AS (2001) The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem Sci 26: 504-510.
    • (2001) Trends Biochem Sci , vol.26 , pp. 504-510
    • Lee, A.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.