메뉴 건너뛰기




Volumn 2, Issue , 2010, Pages 197-210

Role of glycogen synthase kinase-3B on tau phosphorylation in alzheimer’s disease

Author keywords

Amyloid beta; Glycogen synthase kinase 3 ; Tau; Tauopathies

Indexed keywords


EID: 85017063867     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (1)

References (96)
  • 1
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer’s disease
    • Alonso, A. C., Zaidi, T., Grundke-Iqbal, I. & Iqbal, K. (1994). Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer’s disease. Proc. Natl. Acad. Sci., U S A., 91, 5562-5566.
    • (1994) Proc. Natl. Acad. Sci., U S A. , vol.91 , pp. 5562-5566
    • Alonso, A.C.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 2
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer’s disease
    • Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T. & Hyman, B. T. (1992). Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer’s disease. Neurology, 42, 631-639.
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 3
    • 33747425960 scopus 로고    scopus 로고
    • Tau protein, the main component of paired helical filaments
    • Avila, J. (2006). Tau protein, the main component of paired helical filaments. J. Alzheimers Dis, 9, 171-175.
    • (2006) J. Alzheimers Dis , vol.9 , pp. 171-175
    • Avila, J.1
  • 4
    • 38349014705 scopus 로고    scopus 로고
    • Wild-type but not FAD mutant presenilin-1 prevents neuronal degeneration by promoting phosphatidylinositol 3-kinase neuroprotective signaling
    • Baki, L., Neve, R. L., Shao, Z., Shioi, J., Georgakopoulos, A. & Robakis, N. K. (2008). Wild-type but not FAD mutant presenilin-1 prevents neuronal degeneration by promoting phosphatidylinositol 3-kinase neuroprotective signaling. J. Neurosci, 28, 483-490.
    • (2008) J. Neurosci , vol.28 , pp. 483-490
    • Baki, L.1    Neve, R.L.2    Shao, Z.3    Shioi, J.4    Georgakopoulos, A.5    Robakis, N.K.6
  • 5
    • 33745301487 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta and Alzheimer’s disease: Pathophysiological and therapeutic significance
    • Balaraman, Y., Limaye, A. R., Levey, A. I. & Srinivasan, S. (2006). Glycogen synthase kinase 3beta and Alzheimer’s disease: pathophysiological and therapeutic significance. Cell. Mol. Life Sci., 63, 1226-1235.
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 1226-1235
    • Balaraman, Y.1    Limaye, A.R.2    Levey, A.I.3    Srinivasan, S.4
  • 6
    • 53749102630 scopus 로고    scopus 로고
    • Therapeutic strategies for Alzheimer’s disease
    • Barten, D. M. & Albright, C. F. (2008). Therapeutic strategies for Alzheimer’s disease. Mol. Neurobiol, 37, 171-186.
    • (2008) Mol. Neurobiol , vol.37 , pp. 171-186
    • Barten, D.M.1    Albright, C.F.2
  • 8
    • 1242341923 scopus 로고    scopus 로고
    • Incipient Alzheimer’s disease: Microarray correlation analyses reveal major Rosa Resende, Catarina Resende Oliveira and Cláudia MF Pereira 204 transcriptional and tumor suppressor responses
    • Blalock, E. M., Geddes, J. W., Chen, K. C., Porter, N. M., Markesbery, W. R. & Landfield, P. W. (2004). Incipient Alzheimer’s disease: microarray correlation analyses reveal major Rosa Resende, Catarina Resende Oliveira and Cláudia MF Pereira 204 transcriptional and tumor suppressor responses. Proc. Natl. Acad. Sci. U S A, 10, 2173-2178.
    • (2004) Proc. Natl. Acad. Sci. U S A , vol.10 , pp. 2173-2178
    • Blalock, E.M.1    Geddes, J.W.2    Chen, K.C.3    Porter, N.M.4    Markesbery, W.R.5    Landfield, P.W.6
  • 10
    • 10944244158 scopus 로고    scopus 로고
    • Cultured cell and transgenic mouse models for tau pathology linked to beta-amyloid
    • Bloom, G. S., Ren, K. & Glabe, C. G. (2005). Cultured cell and transgenic mouse models for tau pathology linked to beta-amyloid. Biochim. Biophys. Acta, 1739, 116-124.
    • (2005) Biochim. Biophys. Acta , vol.1739 , pp. 116-124
    • Bloom, G.S.1    Ren, K.2    Glabe, C.G.3
  • 11
    • 33846047004 scopus 로고    scopus 로고
    • Pathways by which Abeta facilitates tau pathology
    • Blurton-Jones, M. & Laferla, F. M. (2006). Pathways by which Abeta facilitates tau pathology. Curr. Alzheimer. Res., 3, 437-448.
    • (2006) Curr. Alzheimer. Res , vol.3 , pp. 437-448
    • Blurton-Jones, M.1    Laferla, F.M.2
  • 12
    • 33745747085 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and trophic factor withdrawal activate distinct signaling cascades that induce glycogen synthase kinase-3 beta and a caspase-9-dependent apoptosis in cerebellar granule neurons
    • Brewster, J. L., Linseman, D. A., Bouchard, R. J., Loucks, F. A., Precht, T. A., Esch, E. A. & Heidenreich, K. A. (2006). Endoplasmic reticulum stress and trophic factor withdrawal activate distinct signaling cascades that induce glycogen synthase kinase-3 beta and a caspase-9-dependent apoptosis in cerebellar granule neurons. Mol. Cell Neurosci, 32, 242-253.
    • (2006) Mol. Cell Neurosci , vol.32 , pp. 242-253
    • Brewster, J.L.1    Linseman, D.A.2    Bouchard, R.J.3    Loucks, F.A.4    Precht, T.A.5    Esch, E.A.6    Heidenreich, K.A.7
  • 14
    • 0029417023 scopus 로고
    • Apoptosis and increased generation of reactive oxygen species in Down’s syndrome neurons in vitro
    • Busciglio, J. & Yankner, B. A. (1995). Apoptosis and increased generation of reactive oxygen species in Down’s syndrome neurons in vitro. Nature, 378, 776-779.
    • (1995) Nature , vol.378 , pp. 776-779
    • Busciglio, J.1    Yankner, B.A.2
  • 15
    • 34250818767 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation but not A beta or working memory deficits in a transgenic model with both plaques and tangles
    • Caccamo, A., Oddo, S., Tran, L. X. & LaFerla, F. M. (2007). Lithium reduces tau phosphorylation but not A beta or working memory deficits in a transgenic model with both plaques and tangles. Am. J. Pathol, 170, 1669-1675.
    • (2007) Am. J. Pathol , vol.170 , pp. 1669-1675
    • Caccamo, A.1    Oddo, S.2    Tran, L.X.3    LaFerla, F.M.4
  • 17
    • 0035087123 scopus 로고    scopus 로고
    • Selective small-molecule inhibitors of glycogen synthase kinase-3 activity protect primary neurones from death
    • Cross, D. A., Culbert, A. A., Chalmers, K. A., Facci, L., Skaper, S. D. & Reith, A. D. (2001). Selective small-molecule inhibitors of glycogen synthase kinase-3 activity protect primary neurones from death. J. Neurochem, 77, 94-102.
    • (2001) J. Neurochem , vol.77 , pp. 94-102
    • Cross, D.A.1    Culbert, A.A.2    Chalmers, K.A.3    Facci, L.4    Skaper, S.D.5    Reith, A.D.6
  • 20
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3: Tricks of the trade for a multi-tasking kinase
    • Doble, B. W. & Woodgett, J. R. (2003). GSK-3: tricks of the trade for a multi-tasking kinase. J. Cell Sci., 116, 1175-1186.
    • (2003) J. Cell Sci , vol.116 , pp. 1175-1186
    • Doble, B.W.1    Woodgett, J.R.2
  • 21
    • 16844363453 scopus 로고    scopus 로고
    • Does lithium therapy protect against the onset of dementia?
    • Dunn, N., Holmes, C. & Mullee, M. (2005). Does lithium therapy protect against the onset of dementia? Alzheimer Dis. Assoc. Disord, 19, 20-22.
    • (2005) Alzheimer Dis. Assoc. Disord , vol.19 , pp. 20-22
    • Dunn, N.1    Holmes, C.2    Mullee, M.3
  • 22
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer’s disease
    • Ebneth, A., Godemann, R., Stamer, K., Illenberger, S., Trinczek, B. & Mandelkow, E. (1998). Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer’s disease. J. Cell Biol., 143, 777-794.
    • (1998) J. Cell Biol , vol.143 , pp. 777-794
    • Ebneth, A.1    Godemann, R.2    Stamer, K.3    Illenberger, S.4    Trinczek, B.5    Mandelkow, E.6
  • 23
    • 33845530335 scopus 로고    scopus 로고
    • Chronic lithium administration to FTDP-17 tau and GSK-3beta overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillary tangles do not revert
    • Engel, T., Goñi-Oliver, P., Lucas, J. J., Avila, J. & Hernández, F. (2006). Chronic lithium administration to FTDP-17 tau and GSK-3beta overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillary tangles do not revert. J. Neurochem, 99, 1445-1455.
    • (2006) J. Neurochem , vol.99 , pp. 1445-1455
    • Engel, T.1    Goñi-Oliver, P.2    Lucas, J.J.3    Avila, J.4    Hernández, F.5
  • 25
    • 2642541799 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum Ca2+ release through ryanodine and inositol 1,4,5-triphosphate receptors in the neurotoxic effects induced by the amyloid-β peptide
    • Ferreiro, E., Oliveira, C. R. & Pereira, C. (2004). Involvement of endoplasmic reticulum Ca2+ release through ryanodine and inositol 1,4,5-triphosphate receptors in the neurotoxic effects induced by the amyloid-β peptide. J. Neurosci. Res., 76, 872-880.
    • (2004) J. Neurosci. Res , vol.76 , pp. 872-880
    • Ferreiro, E.1    Oliveira, C.R.2    Pereira, C.3
  • 26
    • 43649083316 scopus 로고    scopus 로고
    • The release of calcium from the Endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway
    • Ferreiro, E., Oliveira, C. R. & Pereira C. (2008). The release of calcium from the Endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway. Neurobiol. Dis., 30, 331-342.
    • (2008) Neurobiol. Dis , vol.30 , pp. 331-342
    • Ferreiro, E.1    Oliveira, C.R.2    Pereira, C.3
  • 27
    • 33747195017 scopus 로고    scopus 로고
    • An endoplasmicreticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity
    • Ferreiro, E., Resende, R., Costa, R., Oliveira, C. R. & Pereira, C. (2006). An endoplasmicreticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity. Neurobiol. Dis., 23, 669-678.
    • (2006) Neurobiol. Dis , vol.23 , pp. 669-678
    • Ferreiro, E.1    Resende, R.2    Costa, R.3    Oliveira, C.R.4    Pereira, C.5
  • 28
    • 55249086251 scopus 로고    scopus 로고
    • Hyperphosphorylation of microtubule-associated protein tau: A promising therapeutic target for Alzheimer disease
    • Gong, C. X. & Iqbal, K. (2008). Hyperphosphorylation of microtubule-associated protein tau: a promising therapeutic target for Alzheimer disease. Curr. Med. Chem., 15, 2321-2328.
    • (2008) Curr. Med. Chem , vol.15 , pp. 2321-2328
    • Gong, C.X.1    Iqbal, K.2
  • 29
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling
    • Grimes, C. A. & Jope, R. S. (2001). The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling. Prog. Neurobiol, 65, 391-426.
    • (2001) Prog. Neurobiol , vol.65 , pp. 391-426
    • Grimes, C.A.1    Jope, R.S.2
  • 31
    • 32444432146 scopus 로고    scopus 로고
    • Abeta and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer’s disease
    • Guo, J. P., Arai, T., Miklossy, J. & McGeer, P. L. (2006). Abeta and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer’s disease. Proc. Natl. Acad. Sci. U S A, 103, 1953-1958.
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 1953-1958
    • Guo, J.P.1    Arai, T.2    Miklossy, J.3    McGeer, P.L.4
  • 32
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer’s amyloid beta-peptide
    • Haass, C. & Selkoe, D. J. (2007). Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid beta-peptide. Nat. Rev. Mol. Cell Biol., 8, 101-112.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 33
    • 0034612636 scopus 로고    scopus 로고
    • Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation
    • Hoeflich, K. P., Luo, J., Rubie, E. A., Tsao, M. S., Jin, O. & Woodgett, J. R. (2000). Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation. Nature, 406, 86-90.
    • (2000) Nature , vol.406 , pp. 86-90
    • Hoeflich, K.P.1    Luo, J.2    Rubie, E.A.3    Tsao, M.S.4    Jin, O.5    Woodgett, J.R.6
  • 34
    • 39849110726 scopus 로고    scopus 로고
    • The GSK3 hypothesis of Alzheimer’s disease
    • Hooper, C., Killick, R. & Lovestone, S. (2008). The GSK3 hypothesis of Alzheimer’s disease. J. Neurochem, 104, 1433-1439.
    • (2008) J. Neurochem , vol.104 , pp. 1433-1439
    • Hooper, C.1    Killick, R.2    Lovestone, S.3
  • 36
    • 0027475421 scopus 로고
    • Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation
    • Hughes, K., Nikolakaki, E., Plyte, S. E., Totty, N. F. & Woodgett, J. R. (1993). Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation. EMBO J, 12, 803-808.
    • (1993) EMBO J , vol.12 , pp. 803-808
    • Hughes, K.1    Nikolakaki, E.2    Plyte, S.E.3    Totty, N.F.4    Woodgett, J.R.5
  • 37
    • 0026619472 scopus 로고
    • Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments
    • Ishiguro, K., Omori, A., Takamatsu, M., Sato, K., Arioka, M., Uchida, T. & Imahori, K. (1992). Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments. Neurosci. Lett, 148, 202-206.
    • (1992) Neurosci. Lett , vol.148 , pp. 202-206
    • Ishiguro, K.1    Omori, A.2    Takamatsu, M.3    Sato, K.4    Arioka, M.5    Uchida, T.6    Imahori, K.7
  • 38
    • 0027255817 scopus 로고
    • Glycogen synthase kinase 3 beta is identical to tau protein kinase I generating several epitopes of paired helical filaments
    • Ishiguro, K., Shiratsuchi, A., Sato, S., Omori, A., Arioka, M., Kobayashi, S., Uchida, T. & Imahori, K. (1993). Glycogen synthase kinase 3 beta is identical to tau protein kinase I generating several epitopes of paired helical filaments. FEBS Lett, 325, 167-172.
    • (1993) FEBS Lett , vol.325 , pp. 167-172
    • Ishiguro, K.1    Shiratsuchi, A.2    Sato, S.3    Omori, A.4    Arioka, M.5    Kobayashi, S.6    Uchida, T.7    Imahori, K.8
  • 39
    • 0042425738 scopus 로고    scopus 로고
    • Co-localization of glycogen synthase kinase-3 with neurofibrillary tangles and granulovacuolar degeneration in transgenic mice
    • Ishizawa, T., Sahara, N., Ishiguro, K., Kersh, J., McGowan, E., Lewis, J., Hutton, M., Dickson, D. W. & Yen, S. H. (2003). Co-localization of glycogen synthase kinase-3 with neurofibrillary tangles and granulovacuolar degeneration in transgenic mice. Am. J. Pathol, 163, 1057-1067.
    • (2003) Am. J. Pathol , vol.163 , pp. 1057-1067
    • Ishizawa, T.1    Sahara, N.2    Ishiguro, K.3    Kersh, J.4    McGowan, E.5    Lewis, J.6    Hutton, M.7    Dickson, D.W.8    Yen, S.H.9
  • 40
    • 33947597084 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 (GSK3): Inflammation, diseases, and therapeutics
    • Jope, R. S., Yuskaitis, C. J. & Beurel, E. (2007). Glycogen synthase kinase-3 (GSK3): inflammation, diseases, and therapeutics. Neurochem. Res., 32, 577-595.
    • (2007) Neurochem. Res , vol.32 , pp. 577-595
    • Jope, R.S.1    Yuskaitis, C.J.2    Beurel, E.3
  • 41
    • 29244456731 scopus 로고    scopus 로고
    • Long-term treatment with novel glycogen synthase kinase-3 inhibitor improves glucose homeostasis in ob/ob mice: Molecular characterization in liver and muscle
    • Kaidanovich-Beilin, O. & Eldar-Finkelman, H. (2006). Long-term treatment with novel glycogen synthase kinase-3 inhibitor improves glucose homeostasis in ob/ob mice: molecular characterization in liver and muscle. J. Pharmacol. Exp. Ther., 316, 17-24.
    • (2006) J. Pharmacol. Exp. Ther , vol.316 , pp. 17-24
    • Kaidanovich-Beilin, O.1    Eldar-Finkelman, H.2
  • 42
    • 0033151570 scopus 로고    scopus 로고
    • Presenilin 1 facilitates the constitutive turnover of beta-catenin: Differential activity of Alzheimer’s disease-linked PS1 mutants in the beta-catenin-signaling pathway
    • Kang, D. E., Soriano, S., Frosch, M. P., Collins, T., Naruse, S., Sisodia, S. S., Leibowitz, G., Levine, F. & Koo, E. H. (1999). Presenilin 1 facilitates the constitutive turnover of beta-catenin: differential activity of Alzheimer’s disease-linked PS1 mutants in the beta-catenin-signaling pathway. J. Neurosci, 19, 4229-4237.
    • (1999) J. Neurosci , vol.19 , pp. 4229-4237
    • Kang, D.E.1    Soriano, S.2    Frosch, M.P.3    Collins, T.4    Naruse, S.5    Sisodia, S.S.6    Leibowitz, G.7    Levine, F.8    Koo, E.H.9
  • 43
    • 37349109154 scopus 로고    scopus 로고
    • Amyloid-beta-induced neurotoxicity is reduced by inhibition of glycogen synthase kinase-3
    • Koh, S. H., Noh, M. Y. & Kim, S. H. (2008). Amyloid-beta-induced neurotoxicity is reduced by inhibition of glycogen synthase kinase-3. Brain Res., 1188, 254-262.
    • (2008) Brain Res , vol.1188 , pp. 254-262
    • Koh, S.H.1    Noh, M.Y.2    Kim, S.H.3
  • 45
    • 37049008884 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-kinase activation blocks amyloid beta-induced neurotoxicity
    • Lee, K. Y., Koh, S. H., Noh, M. Y., Kim, S. H. & Lee, Y. J. (2008). Phosphatidylinositol-3-kinase activation blocks amyloid beta-induced neurotoxicity. Toxicology, 243, 43-50.
    • (2008) Toxicology , vol.243 , pp. 43-50
    • Lee, K.Y.1    Koh, S.H.2    Noh, M.Y.3    Kim, S.H.4    Lee, Y.J.5
  • 46
    • 33846129434 scopus 로고    scopus 로고
    • Increased level of active GSK-3beta in Alzheimer’s disease and accumulation in argyrophilic grains and in neurones at different stages of neurofibrillary degeneration
    • Leroy, K., Yilmaz, Z. & Brion, J. P. (2007). Increased level of active GSK-3beta in Alzheimer’s disease and accumulation in argyrophilic grains and in neurones at different stages of neurofibrillary degeneration. Neuropathol. Appl. Neurobiol, 33, 43-55.
    • (2007) Neuropathol. Appl. Neurobiol , vol.33 , pp. 43-55
    • Leroy, K.1    Yilmaz, Z.2    Brion, J.P.3
  • 47
    • 0346434153 scopus 로고    scopus 로고
    • Overactivation of glycogen synthase kinase-3 by inhibition of phosphoinositol-3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory
    • Liu, S. J., Zhang, A. H., Li, H. L., Wang, Q., Deng, H. M., Netzer, W. J., Xu, H. & Wang, J. Z. (2003). Overactivation of glycogen synthase kinase-3 by inhibition of phosphoinositol-3 kinase and protein kinase C leads to hyperphosphorylation of tau and impairment of spatial memory. J. Neurochem, 87, 1333-1344.
    • (2003) J. Neurochem , vol.87 , pp. 1333-1344
    • Liu, S.J.1    Zhang, A.H.2    Li, H.L.3    Wang, Q.4    Deng, H.M.5    Netzer, W.J.6    Xu, H.7    Wang, J.Z.8
  • 48
    • 37549015597 scopus 로고    scopus 로고
    • Role of cyclin-dependent kinase 5 in the neurodegenerative process triggered by amyloid-Beta and prion peptides: Implications for Alzheimer’s disease and prion-related encephalopathies
    • Lopes, J. P., Oliveira, C. R. & Agostinho, P. (2007). Role of cyclin-dependent kinase 5 in the neurodegenerative process triggered by amyloid-Beta and prion peptides: implications for Alzheimer’s disease and prion-related encephalopathies. Cell Mol. Neurobiol, 27, 943-957.
    • (2007) Cell Mol. Neurobiol , vol.27 , pp. 943-957
    • Lopes, J.P.1    Oliveira, C.R.2    Agostinho, P.3
  • 49
    • 0028675873 scopus 로고
    • Alzheimer’s disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells
    • Lovestone, S., Reynolds, C. H., Latimer, D., Davis, D. R., Anderton, B. H., Gallo, J. M., Hanger, D., Mulot, S., Marquardt, B. & Stabel, S., et al. (1994). Alzheimer’s disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells. Curr. Biol., 4, 1077-1086.
    • (1994) Curr. Biol , vol.4 , pp. 1077-1086
    • Lovestone, S.1    Reynolds, C.H.2    Latimer, D.3    Davis, D.R.4    Anderton, B.H.5    Gallo, J.M.6    Hanger, D.7    Mulot, S.8    Marquardt, B.9    Stabel, S.10
  • 50
  • 52
    • 28044446528 scopus 로고    scopus 로고
    • Intraneuronal beta-amyloid expression downregulates the Akt survival pathway and blunts the stress response
    • Magrané, J., Rosen, K. M., Smith, R. C., Walsh, K., Gouras, G. K. & Querfurth, H. W. (2005). Intraneuronal beta-amyloid expression downregulates the Akt survival pathway and blunts the stress response. J. Neurosci, 25, 10960-10969.
    • (2005) J. Neurosci , vol.25 , pp. 10960-10969
    • Magrané, J.1    Rosen, K.M.2    Smith, R.C.3    Walsh, K.4    Gouras, G.K.5    Querfurth, H.W.6
  • 53
    • 5444273804 scopus 로고    scopus 로고
    • MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons
    • Mandelkow, E. M., Thies, E., Trinczek, B., Biernat, J. & Mandelkow, E. (2004). MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons. J. Cell Biol., 167, 99-110.
    • (2004) J. Cell Biol , vol.167 , pp. 99-110
    • Mandelkow, E.M.1    Thies, E.2    Trinczek, B.3    Biernat, J.4    Mandelkow, E.5
  • 54
    • 46249120721 scopus 로고    scopus 로고
    • Inhibition of Wnt and P13K signaling modulates GSK-3beta activity and induces morphological changes in cortical neurons: Role of tau phosphorylation
    • Mercado-Gómez, O., Hernández-Fonseca, K., Villavicencio-Queijeiro, A., Massieu, L., Chimal-Monroy, J. & Arias, C. (2008). Inhibition of Wnt and P13K signaling modulates GSK-3beta activity and induces morphological changes in cortical neurons: role of tau phosphorylation. Neurochem. Res., 33, 1599-1609.
    • (2008) Neurochem. Res , vol.33 , pp. 1599-1609
    • Mercado-Gómez, O.1    Hernández-Fonseca, K.2    Villavicencio-Queijeiro, A.3    Massieu, L.4    Chimal-Monroy, J.5    Arias, C.6
  • 56
    • 4043167747 scopus 로고    scopus 로고
    • Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • Oddo, S., Billings, L., Kesslak, J. P., Cribbs, D. H. & LaFerla, F. M. (2004). Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron, 43, 321-332.
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 57
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer’s disease
    • Oddo, S., Caccamo, A., Kitazawa, M., Tseng, B. P. & LaFerla, F. M. (2003). Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer’s disease. Neurobiol. Aging, 24, 1063-1070.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3    Tseng, B.P.4    LaFerla, F.M.5
  • 59
    • 58149388879 scopus 로고    scopus 로고
    • Blocking Abeta42 accumulation delays the onset and progression of tau pathology via the C terminus of heat shock protein70-interacting protein: A mechanistic link between Abeta and tau pathology
    • Oddo, S., Caccamo, A., Tseng, B., Cheng, D., Vasilevko, V., Cribbs, D. H. & LaFerla, F. M. (2008). Blocking Abeta42 accumulation delays the onset and progression of tau pathology via the C terminus of heat shock protein70-interacting protein: a mechanistic link between Abeta and tau pathology. J. Neurosci, 28, 12163-12175.
    • (2008) J. Neurosci , vol.28 , pp. 12163-12175
    • Oddo, S.1    Caccamo, A.2    Tseng, B.3    Cheng, D.4    Vasilevko, V.5    Cribbs, D.H.6    LaFerla, F.M.7
  • 60
    • 33144487701 scopus 로고    scopus 로고
    • Temporal profile of amyloid-beta (Abeta) oligomerization in an in vivo model of Alzheimer’s disease. A link between Abeta and tau pathology
    • Oddo, S., Caccamo, A., Tran, L., Lambert, M. P., Glabe, C. G., Klein, W. L. & LaFerla, F. M. (2006a). Temporal profile of amyloid-beta (Abeta) oligomerization in an in vivo model of Alzheimer’s disease. A link between Abeta and tau pathology. J Biol Chem., 281, 1599-1604.
    • (2006) J Biol Chem , vol.281 , pp. 1599-1604
    • Oddo, S.1    Caccamo, A.2    Tran, L.3    Lambert, M.P.4    Glabe, C.G.5    Klein, W.L.6    LaFerla, F.M.7
  • 61
    • 33846015514 scopus 로고    scopus 로고
    • Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles
    • Oddo, S., Vasilevko, V., Caccamo, A., Kitazawa, M., Cribbs, D. H. & LaFerla, F. M. (2006b). Reduction of soluble Abeta and tau, but not soluble Abeta alone, ameliorates cognitive decline in transgenic mice with plaques and tangles. J. Biol. Chem., 281, 39413-39423.
    • (2006) J. Biol. Chem , vol.281 , pp. 39413-39423
    • Oddo, S.1    Vasilevko, V.2    Caccamo, A.3    Kitazawa, M.4    Cribbs, D.H.5    LaFerla, F.M.6
  • 62
    • 0032850599 scopus 로고    scopus 로고
    • Distribution of active glycogen synthase kinase 3beta (GSK-3beta) in brains staged for Alzheimer’s disease neurofibrillary changes
    • Pei, J. J., Braak, E., Braak, H., Grundke-Iqbal, I., Iqbal, K., Winblad, B. & Cowburn, R. F. (1997). Distribution of active glycogen synthase kinase 3beta (GSK-3beta) in brains staged for Alzheimer’s disease neurofibrillary changes. J. Neuropathol. Exp. Neurol, 58, 1010-1019.
    • (1997) J. Neuropathol. Exp. Neurol , vol.58 , pp. 1010-1019
    • Pei, J.J.1    Braak, E.2    Braak, H.3    Grundke-Iqbal, I.4    Iqbal, K.5    Winblad, B.6    Cowburn, R.F.7
  • 63
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3alpha regulates production of Alzheimer’s disease amyloid-beta peptides
    • Phiel, C. J., Wilson, C. A., Lee, V. M. & Klein, P. S. (2003). GSK-3alpha regulates production of Alzheimer’s disease amyloid-beta peptides. Nature, 423, 435-439.
    • (2003) Nature , vol.423 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.3    Klein, P.S.4
  • 64
    • 33748752882 scopus 로고    scopus 로고
    • The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation
    • Plattner, F., Angelo, M. & Giese, K. P. (2006). The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation. J. Biol. Chem., 281, 25457-25465.
    • (2006) J. Biol. Chem , vol.281 , pp. 25457-25465
    • Plattner, F.1    Angelo, M.2    Giese, K.P.3
  • 65
    • 58149314221 scopus 로고    scopus 로고
    • Valproic acid inhibits Abeta production, neuritic plaque formation, and behavioral deficits in Alzheimer’s disease mouse models
    • Qing, H., He, G., Ly, P. T., Fox, C. J., Staufenbiel, M., Cai, F., Zhang, Z., Wei, S., Sun, X., Chen, C. H., Zhou, W., Wang, K. & Song, W. (2008). Valproic acid inhibits Abeta production, neuritic plaque formation, and behavioral deficits in Alzheimer’s disease mouse models. J. Exp. Med, 205, 2781-2789.
    • (2008) J. Exp. Med , vol.205 , pp. 2781-2789
    • Qing, H.1    He, G.2    Ly, P.T.3    Fox, C.J.4    Staufenbiel, M.5    Cai, F.6    Zhang, Z.7    Wei, S.8    Sun, X.9    Chen, C.H.10    Zhou, W.11    Wang, K.12    Song, W.13
  • 66
    • 40849095832 scopus 로고    scopus 로고
    • Lithium down-regulates tau in cultured cortical neurons: A possible mechanism of neuroprotection
    • Rametti, A., Esclaire, F., Yardin, C., Cogné, N. & Terro, F. (2008). Lithium down-regulates tau in cultured cortical neurons: a possible mechanism of neuroprotection. Neurosci. Lett, 434, 93-98.
    • (2008) Neurosci. Lett , vol.434 , pp. 93-98
    • Rametti, A.1    Esclaire, F.2    Yardin, C.3    Cogné, N.4    Terro, F.5
  • 67
    • 49349110485 scopus 로고    scopus 로고
    • Pre-assembled tau filaments phosphorylated by GSK-3b form large tangle-like structures
    • Rankin, C. A., Sun, Q. & Gamblin, T. C. (2008). Pre-assembled tau filaments phosphorylated by GSK-3b form large tangle-like structures. Neurobiol. Dis., 31, 368-377.
    • (2008) Neurobiol. Dis , vol.31 , pp. 368-377
    • Rankin, C.A.1    Sun, Q.2    Gamblin, T.C.3
  • 69
    • 48249157930 scopus 로고    scopus 로고
    • ER stress is involved in Abeta-induced GSK-3beta activation and tau phosphorylation
    • Resende, R., Ferreiro, E., Pereira, C. & Oliveira, C. R. (2008a). ER stress is involved in Abeta-induced GSK-3beta activation and tau phosphorylation. J. Neurosci. Res., 86, 2091-2099.
    • (2008) J. Neurosci. Res , vol.86 , pp. 2091-2099
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    Oliveira, C.R.4
  • 70
    • 49249118742 scopus 로고    scopus 로고
    • Neurotoxic effect of oligomeric and fibrillar species of Aβ1-42 peptide. Involvement of ER calcium release in oligomers-induced cell death
    • Resende, R., Ferreiro, E., Pereira, C. & Oliveira, C. R. (2008b). Neurotoxic effect of oligomeric and fibrillar species of Aβ1-42 peptide. Involvement of ER calcium release in oligomers-induced cell death. Neuroscience, 155, 725-737.
    • (2008) Neuroscience , vol.155 , pp. 725-737
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    Oliveira, C.R.4
  • 71
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer’s disease mouse model
    • Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G. Q. & Mucke, L. (2007). Reducing endogenous tau ameliorates amyloid beta-induced deficits in an Alzheimer’s disease mouse model. Science, 316, 750-754.
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6    Gerstein, H.7    Yu, G.Q.8    Mucke, L.9
  • 72
    • 33847214486 scopus 로고    scopus 로고
    • Neuroprotective effects of regulators of the glycogen synthase kinase-3beta signaling pathway in a transgenic model of Alzheimer’s disease are associated with reduced amyloid precursor protein phosphorylation
    • Rockenstein, E., Torrance, M., Adame, A., Mante, M., Baron, P., Rose, J. B., Crews, L. & Masliah, E. (2007). Neuroprotective effects of regulators of the glycogen synthase kinase-3beta signaling pathway in a transgenic model of Alzheimer’s disease are associated with reduced amyloid precursor protein phosphorylation. J. Neurosci, 27, 1981-1991.
    • (2007) J. Neurosci , vol.27 , pp. 1981-1991
    • Rockenstein, E.1    Torrance, M.2    Adame, A.3    Mante, M.4    Baron, P.5    Rose, J.B.6    Crews, L.7    Masliah, E.8
  • 73
    • 33749854516 scopus 로고    scopus 로고
    • Acute impairment of mitochondrial trafficking by beta-amyloid peptides in hippocampal neurons
    • Rui, Y., Tiwari, P., Xie, Z. & Zheng, J. Q. (2006). Acute impairment of mitochondrial trafficking by beta-amyloid peptides in hippocampal neurons. J. Neurosci, 26, 10480-10487.
    • (2006) J. Neurosci , vol.26 , pp. 10480-10487
    • Rui, Y.1    Tiwari, P.2    Xie, Z.3    Zheng, J.Q.4
  • 74
    • 1642269125 scopus 로고    scopus 로고
    • Cyclin-dependent kinase-5 in neurodegeneration
    • Shelton, S. B. & Johnson, G. V. (2004). Cyclin-dependent kinase-5 in neurodegeneration. J. Neurochem, 88, 1313-1326.
    • (2004) J. Neurochem , vol.88 , pp. 1313-1326
    • Shelton, S.B.1    Johnson, G.V.2
  • 75
    • 0037160134 scopus 로고    scopus 로고
    • Central role of glycogen synthase kinase-3beta in endoplasmic reticulum stress-induced caspase-3 activation
    • Song, L., De Sarno, P. & Jope, R. S. (2002). Central role of glycogen synthase kinase-3beta in endoplasmic reticulum stress-induced caspase-3 activation. J. Biol. Chem., 277, 44701-44708.
    • (2002) J. Biol. Chem , vol.277 , pp. 44701-44708
    • Song, L.1    De Sarno, P.2    Jope, R.S.3
  • 76
    • 1842510667 scopus 로고    scopus 로고
    • Altered expression levels of the protein phosphatase 2A ABalphaC enzyme are associated with Alzheimer’s disease pathology
    • Sontag, E., Luangpirom, A., Hladik, C., Mudrak, I., Ogris, E., Speciale, S. & White, CL 3rd. (2004). Altered expression levels of the protein phosphatase 2A ABalphaC enzyme are associated with Alzheimer’s disease pathology. J. Neuropathol. Exp. Neurol, 63, 287-301.
    • (2004) J. Neuropathol. Exp. Neurol , vol.63 , pp. 287-301
    • Sontag, E.1    Luangpirom, A.2    Hladik, C.3    Mudrak, I.4    Ogris, E.5    Speciale, S.6    White, C.L.7
  • 77
    • 15944375438 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced apoptosis is partly mediated by reduced insulin signaling through phosphatidylinositol 3-kinase/Akt and increased glycogen synthase kinase-3beta in mouse insulinoma cells
    • Srinivasan, S., Ohsugi, M., Liu, Z., Fatrai, S., Bernal-Mizrachi, E. & Permutt, M. A. (2005). Endoplasmic reticulum stress-induced apoptosis is partly mediated by reduced insulin signaling through phosphatidylinositol 3-kinase/Akt and increased glycogen synthase kinase-3beta in mouse insulinoma cells. Diabetes, 54, 968-975.
    • (2005) Diabetes , vol.54 , pp. 968-975
    • Srinivasan, S.1    Ohsugi, M.2    Liu, Z.3    Fatrai, S.4    Bernal-Mizrachi, E.5    Permutt, M.A.6
  • 78
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • Stamer, K., Vogel, R., Thies, E., Mandelkow, E. & Mandelkow, E. M. (2002). Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J. Cell Biol., 156, 1051-1063.
    • (2002) J. Cell Biol , vol.156 , pp. 1051-1063
    • Stamer, K.1    Vogel, R.2    Thies, E.3    Mandelkow, E.4    Mandelkow, E.M.5
  • 79
    • 0037087220 scopus 로고    scopus 로고
    • Lithium inhibits amyloid secretion in COS7 cells transfected with amyloid precursor protein C100
    • Sun, X., Sato, S., Murayama, O., Murayama, M., Park, J. M., Yamaguchi, H. & Takashima, A. (2002). Lithium inhibits amyloid secretion in COS7 cells transfected with amyloid precursor protein C100. Neuroscience Lett, 321, 61-64.
    • (2002) Neuroscience Lett , vol.321 , pp. 61-64
    • Sun, X.1    Sato, S.2    Murayama, O.3    Murayama, M.4    Park, J.M.5    Yamaguchi, H.6    Takashima, A.7
  • 80
    • 34250792792 scopus 로고    scopus 로고
    • Caspase-dependent apoptosis induced by thapsigargin was prevented by glycogen synthase kinase-3 inhibitors in cultured rat cortical neurons
    • Takadera, T., Fujibayashi, M., Kaniyu, H., Sakota, N. & Ohyashiki, T. (2007). Caspase-dependent apoptosis induced by thapsigargin was prevented by glycogen synthase kinase-3 inhibitors in cultured rat cortical neurons. Neurochem. Res., 32, 1336-1342.
    • (2007) Neurochem. Res , vol.32 , pp. 1336-1342
    • Takadera, T.1    Fujibayashi, M.2    Kaniyu, H.3    Sakota, N.4    Ohyashiki, T.5
  • 81
    • 33749359060 scopus 로고    scopus 로고
    • Thapsigargin-induced apoptosis was prevented by glycogen synthase kinase-3 inhibitors in PC12 cells
    • Takadera, T., Yoshikawa, R. & Ohyashiki, T. (2006). Thapsigargin-induced apoptosis was prevented by glycogen synthase kinase-3 inhibitors in PC12 cells. Neurosci. Lett, 408, 124-128.
    • (2006) Neurosci. Lett , vol.408 , pp. 124-128
    • Takadera, T.1    Yoshikawa, R.2    Ohyashiki, T.3
  • 83
    • 0030044463 scopus 로고    scopus 로고
    • Exposure of rat hippocampal neurons to amyloid beta peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3 beta
    • Takashima, A., Noguchi, K., Michel, G., Mercken, M., Hoshi, M., Ishiguro, K. & Imahori, K. (1996). Exposure of rat hippocampal neurons to amyloid beta peptide (25-35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3 beta. Neurosci. Lett, 203, 33-36.
    • (1996) Neurosci. Lett , vol.203 , pp. 33-36
    • Takashima, A.1    Noguchi, K.2    Michel, G.3    Mercken, M.4    Hoshi, M.5    Ishiguro, K.6    Imahori, K.7
  • 87
    • 2342549202 scopus 로고    scopus 로고
    • Glycogen synthase kinase3 beta phosphorylates serine 33 of p53 and activates p53‘s transcriptional activity
    • Turenne, G. A. & Price, B. D. (2001). Glycogen synthase kinase3 beta phosphorylates serine 33 of p53 and activates p53‘s transcriptional activity. BMC Cell Biol, 2, 12-20.
    • (2001) BMC Cell Biol , vol.2 , pp. 12-20
    • Turenne, G.A.1    Price, B.D.2
  • 88
    • 0032746701 scopus 로고    scopus 로고
    • Cell-extracellular matrix interactions stimulate the AP-1 transcription factor in an integrin-linked kinase- and glycogen synthase kinase 3-dependent manner
    • Troussard, A. A., Tan, C., Yoganathan, T. N. & Dedhar, S. (1999). Cell-extracellular matrix interactions stimulate the AP-1 transcription factor in an integrin-linked kinase- and glycogen synthase kinase 3-dependent manner. Mol. Cell Biol., 19, 7420-7427.
    • (1999) Mol. Cell Biol , vol.19 , pp. 7420-7427
    • Troussard, A.A.1    Tan, C.2    Yoganathan, T.N.3    Dedhar, S.4
  • 89
  • 91
    • 0035075793 scopus 로고    scopus 로고
    • PP2A mRNA expression is quantitatively decreased in Alzheimer’s disease hippocampus
    • Vogelsberg-Ragaglia, V., Schuck, T., Trojanowski, J. Q. & Lee, V. M. (2001). PP2A mRNA expression is quantitatively decreased in Alzheimer’s disease hippocampus. Exp. Neurol, 168, 402-412.
    • (2001) Exp. Neurol , vol.168 , pp. 402-412
    • Vogelsberg-Ragaglia, V.1    Schuck, T.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 92
    • 33846212717 scopus 로고    scopus 로고
    • Kinases and phosphatases and tau sites involved in Alzheimer’s neurofibrillary degeneration
    • Wang, J. Z., Grundke-Iqbal, I. & Iqbal, K. (2007). Kinases and phosphatases and tau sites involved in Alzheimer’s neurofibrillary degeneration. Eur. J. Neurosci, 25, 59-68.
    • (2007) Eur. J. Neurosci , vol.25 , pp. 59-68
    • Wang, J.Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 93
    • 0027430039 scopus 로고
    • Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B
    • Welsh, G. I. & Proud, C. G. (1993). Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. Biochem. J, 294, 625-629.
    • (1993) Biochem. J , vol.294 , pp. 625-629
    • Welsh, G.I.1    Proud, C.G.2
  • 94
    • 40449087334 scopus 로고    scopus 로고
    • Interplay between cyclin-dependent kinase 5 and glycogen synthase kinase 3 beta mediated by neuregulin signaling leads to differential effects on tau phosphorylation and amyloid precursor protein processing
    • Wen, Y., Planel, E., Herman, M., Figueroa, H. Y., Wang, L., Liu, L., Lau, L. F., Yu, W. H. & Duff, K. E. (2008). Interplay between cyclin-dependent kinase 5 and glycogen synthase kinase 3 beta mediated by neuregulin signaling leads to differential effects on tau phosphorylation and amyloid precursor protein processing. J. Neurosci, 28, 2624-2632.
    • (2008) J. Neurosci , vol.28 , pp. 2624-2632
    • Wen, Y.1    Planel, E.2    Herman, M.3    Figueroa, H.Y.4    Wang, L.5    Liu, L.6    Lau, L.F.7    Yu, W.H.8    Duff, K.E.9
  • 95
    • 0029737421 scopus 로고    scopus 로고
    • Preferential labeling of Alzheimer’s neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3 beta and cyclin-dependent kinase 5, a component of TPK II
    • Yamaguchi, H., Ishiguro, K., Uchida, T., Takashima, A., Lemere, C. A. & Imahori, K. (1996). Preferential labeling of Alzheimer’s neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3 beta and cyclin-dependent kinase 5, a component of TPK II. Acta Neuropathol, 92, 232-241.
    • (1996) Acta Neuropathol , vol.92 , pp. 232-241
    • Yamaguchi, H.1    Ishiguro, K.2    Uchida, T.3    Takashima, A.4    Lemere, C.A.5    Imahori, K.6
  • 96
    • 33646121053 scopus 로고    scopus 로고
    • Depletion of intracellular Ca2+ store itself may be a major factor in thapsigargin-induced ER stress and apoptosis in PC12 cells
    • Yoshida, I., Monji, A., Tashiro, K., Nakamura, K., Inoue, R. & Kanba, S. (2006). Depletion of intracellular Ca2+ store itself may be a major factor in thapsigargin-induced ER stress and apoptosis in PC12 cells. Neurochem. Int., 48, 696-702.
    • (2006) Neurochem. Int , vol.48 , pp. 696-702
    • Yoshida, I.1    Monji, A.2    Tashiro, K.3    Nakamura, K.4    Inoue, R.5    Kanba, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.