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Volumn 30, Issue 3, 2009, Pages 377-387

Insulin rescues amyloid β-induced impairment of hippocampal long-term potentiation

Author keywords

Alzheimer's disease; Amyloid ; Hemoglobin; Hippocampus; Insulin; Long term potentiation

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-42]; DIMER; DITHIOTHREITOL; HEMOGLOBIN; INSULIN; OLIGOMER; SOMATOMEDIN C;

EID: 58549102356     PISSN: 01974580     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neurobiolaging.2007.06.014     Document Type: Article
Times cited : (71)

References (63)
  • 1
    • 13244292389 scopus 로고    scopus 로고
    • Protective effects of insulin-like growth factor-I on the somatostatinergic system in the temporal cortex of β-amyloid-treated rats
    • Aguado-Llera D., Arilla-Ferreiro E., Campos-Barros A., Puebla-Jimenez L., and Barrios V. Protective effects of insulin-like growth factor-I on the somatostatinergic system in the temporal cortex of β-amyloid-treated rats. J. Neurochem. 92 3 (2005) 607-615
    • (2005) J. Neurochem. , vol.92 , Issue.3 , pp. 607-615
    • Aguado-Llera, D.1    Arilla-Ferreiro, E.2    Campos-Barros, A.3    Puebla-Jimenez, L.4    Barrios, V.5
  • 2
    • 0032859938 scopus 로고    scopus 로고
    • Inhibition of tau phosphorylating protein kinase cdk5 prevents β-amyloid-induced neuronal death
    • Alvarez A., Toro R., Caceres A., and Maccioni R.B. Inhibition of tau phosphorylating protein kinase cdk5 prevents β-amyloid-induced neuronal death. FEBS Lett. 459 3 (1999) 421-426
    • (1999) FEBS Lett. , vol.459 , Issue.3 , pp. 421-426
    • Alvarez, A.1    Toro, R.2    Caceres, A.3    Maccioni, R.B.4
  • 3
    • 0030664286 scopus 로고    scopus 로고
    • Transport of insulin across the blood-brain barrier: saturability at euglycemic doses of insulin
    • Banks W.A., Jaspan J.B., Huang W., and Kastin A.J. Transport of insulin across the blood-brain barrier: saturability at euglycemic doses of insulin. Peptides 18 9 (1997) 1423-1429
    • (1997) Peptides , vol.18 , Issue.9 , pp. 1423-1429
    • Banks, W.A.1    Jaspan, J.B.2    Huang, W.3    Kastin, A.J.4
  • 7
    • 0034069795 scopus 로고    scopus 로고
    • Impairment of hippocampal long-term potentiation by Alzheimer amyloid β-peptides
    • Chen Q.S., Kagan B.L., Hirakura Y., and Xie C.W. Impairment of hippocampal long-term potentiation by Alzheimer amyloid β-peptides. J. Neurosci. Res. 60 1 (2000) 65-72
    • (2000) J. Neurosci. Res. , vol.60 , Issue.1 , pp. 65-72
    • Chen, Q.S.1    Kagan, B.L.2    Hirakura, Y.3    Xie, C.W.4
  • 8
    • 0031907459 scopus 로고    scopus 로고
    • Cerebrospinal fluid and plasma insulin levels in Alzheimer's disease: relationship to severity of dementia and apolipoprotein E genotype
    • Craft S., Peskind E., Schwartz M.W., Schellenberg G.D., Raskind M., and Porte Jr. D. Cerebrospinal fluid and plasma insulin levels in Alzheimer's disease: relationship to severity of dementia and apolipoprotein E genotype. Neurology 50 1 (1998) 164-168
    • (1998) Neurology , vol.50 , Issue.1 , pp. 164-168
    • Craft, S.1    Peskind, E.2    Schwartz, M.W.3    Schellenberg, G.D.4    Raskind, M.5    Porte Jr., D.6
  • 9
    • 1042265187 scopus 로고    scopus 로고
    • Neuropathology and pathogenesis of encephalitis following amyloid-β immunization in Alzheimer's disease
    • Ferrer I., Boada Rovira M., Sanchez Guerra M.L., Rey M.J., and Costa-Jussa F. Neuropathology and pathogenesis of encephalitis following amyloid-β immunization in Alzheimer's disease. Brain Pathol. 14 1 (2004) 11-20
    • (2004) Brain Pathol. , vol.14 , Issue.1 , pp. 11-20
    • Ferrer, I.1    Boada Rovira, M.2    Sanchez Guerra, M.L.3    Rey, M.J.4    Costa-Jussa, F.5
  • 10
    • 0038581893 scopus 로고    scopus 로고
    • 1-40 on long-term potentiation in the rat hippocampal CA1 region in vivo
    • 1-40 on long-term potentiation in the rat hippocampal CA1 region in vivo. J. Neurophysiol. 89 6 (2003) 2917-2922
    • (2003) J. Neurophysiol. , vol.89 , Issue.6 , pp. 2917-2922
    • Freir, D.B.1    Herron, C.E.2
  • 11
    • 0035128734 scopus 로고    scopus 로고
    • Blockade of long-term potentiation by β-amyloid peptides in the CA1 region of the rat hippocampus in vivo
    • Freir D.B., Holscher C., and Herron C.E. Blockade of long-term potentiation by β-amyloid peptides in the CA1 region of the rat hippocampus in vivo. J. Neurophysiol. 85 2 (2001) 708-713
    • (2001) J. Neurophysiol. , vol.85 , Issue.2 , pp. 708-713
    • Freir, D.B.1    Holscher, C.2    Herron, C.E.3
  • 12
    • 0035871641 scopus 로고    scopus 로고
    • Stimulation of β-amyloid precursor protein trafficking by insulin reduces intraneuronal β-amyloid and requires mitogen-activated protein kinase signaling
    • Gasparini L., Gouras G.K., Wang R., Gross R.S., Beal M.F., Greengard P., and Xu H. Stimulation of β-amyloid precursor protein trafficking by insulin reduces intraneuronal β-amyloid and requires mitogen-activated protein kinase signaling. J. Neurosci. 21 8 (2001) 2561-2570
    • (2001) J. Neurosci. , vol.21 , Issue.8 , pp. 2561-2570
    • Gasparini, L.1    Gouras, G.K.2    Wang, R.3    Gross, R.S.4    Beal, M.F.5    Greengard, P.6    Xu, H.7
  • 13
    • 0036591657 scopus 로고    scopus 로고
    • Does insulin dysfunction play a role in Alzheimer's disease?
    • Gasparini L., Netzer W.J., Greengard P., and Xu H. Does insulin dysfunction play a role in Alzheimer's disease?. Trends Pharmacol. Sci. 23 6 (2002) 288-293
    • (2002) Trends Pharmacol. Sci. , vol.23 , Issue.6 , pp. 288-293
    • Gasparini, L.1    Netzer, W.J.2    Greengard, P.3    Xu, H.4
  • 14
    • 0142026832 scopus 로고    scopus 로고
    • Potential roles of insulin and IGF-1 in Alzheimer's disease
    • Gasparini L., and Xu H. Potential roles of insulin and IGF-1 in Alzheimer's disease. Trends Neurosci. 26 8 (2003) 404-406
    • (2003) Trends Neurosci. , vol.26 , Issue.8 , pp. 404-406
    • Gasparini, L.1    Xu, H.2
  • 15
    • 34249024370 scopus 로고    scopus 로고
    • Impairments of hippocampal synaptic plasticity induced by aggregated beta-amyloid (25-35) are dependent on stimulation-protocol and genetic background
    • Gengler S., Gault V.A., Harriott P., and Holscher C. Impairments of hippocampal synaptic plasticity induced by aggregated beta-amyloid (25-35) are dependent on stimulation-protocol and genetic background. Exp. Brain Res. 179 4 (2007) 621-630
    • (2007) Exp. Brain Res. , vol.179 , Issue.4 , pp. 621-630
    • Gengler, S.1    Gault, V.A.2    Harriott, P.3    Holscher, C.4
  • 16
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner G.G., and Wong C.W. Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem. Biophys. Res. Commun. 122 3 (1984) 1131-1135
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , Issue.3 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 17
    • 0023009658 scopus 로고
    • Microtubule-associated protein tau. A component of Alzheimer paired helical filaments
    • Grundke-Iqbal I., Iqbal K., Quinlan M., Tung Y.C., Zaidi M.S., and Wisniewski H.M. Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J. Biol. Chem. 261 13 (1986) 6084-6089
    • (1986) J. Biol. Chem. , vol.261 , Issue.13 , pp. 6084-6089
    • Grundke-Iqbal, I.1    Iqbal, K.2    Quinlan, M.3    Tung, Y.C.4    Zaidi, M.S.5    Wisniewski, H.M.6
  • 19
    • 0022510796 scopus 로고
    • Autoradiographic localization of insulin receptors in rat brain: prominence in olfactory and limbic areas
    • Hill J.M., Lesniak M.A., Pert C.B., and Roth J. Autoradiographic localization of insulin receptors in rat brain: prominence in olfactory and limbic areas. Neuroscience 17 4 (1986) 1127-1138
    • (1986) Neuroscience , vol.17 , Issue.4 , pp. 1127-1138
    • Hill, J.M.1    Lesniak, M.A.2    Pert, C.B.3    Roth, J.4
  • 20
    • 0033571910 scopus 로고    scopus 로고
    • A role for extracellular adenosine in time-dependent reversal of long-term potentiation by low-frequency stimulation at hippocampal CA1 synapses
    • Huang C.C., Liang Y.C., and Hsu K.S. A role for extracellular adenosine in time-dependent reversal of long-term potentiation by low-frequency stimulation at hippocampal CA1 synapses. J. Neurosci. 19 22 (1999) 9728-9738
    • (1999) J. Neurosci. , vol.19 , Issue.22 , pp. 9728-9738
    • Huang, C.C.1    Liang, Y.C.2    Hsu, K.S.3
  • 21
    • 1842562359 scopus 로고    scopus 로고
    • An investigation into signal transduction mechanisms involved in insulin-induced long-term depression in the CA1 region of the hippocampus
    • Huang C.C., Lee C.C., and Hsu K.S. An investigation into signal transduction mechanisms involved in insulin-induced long-term depression in the CA1 region of the hippocampus. J. Neurochem. 89 1 (2004) 217-231
    • (2004) J. Neurochem. , vol.89 , Issue.1 , pp. 217-231
    • Huang, C.C.1    Lee, C.C.2    Hsu, K.S.3
  • 22
    • 32644483115 scopus 로고    scopus 로고
    • Sustained activation of metabotropic glutamate receptor 5 and protein tyrosine phosphatases mediate the expression of (S)-3,5-dihydroxyphenylglycine-induced long-term depression in the hippocampal CA1 region
    • Huang C.C., and Hsu K.S. Sustained activation of metabotropic glutamate receptor 5 and protein tyrosine phosphatases mediate the expression of (S)-3,5-dihydroxyphenylglycine-induced long-term depression in the hippocampal CA1 region. J. Neurochem. 96 1 (2006) 179-194
    • (2006) J. Neurochem. , vol.96 , Issue.1 , pp. 179-194
    • Huang, C.C.1    Hsu, K.S.2
  • 23
    • 25844477102 scopus 로고    scopus 로고
    • Current concepts in therapeutic strategies targeting cognitive decline and disease modification in Alzheimer's disease
    • Jacobsen J.S., Reinhart P., and Pangalos M.N. Current concepts in therapeutic strategies targeting cognitive decline and disease modification in Alzheimer's disease. NeuroRx 2 4 (2005) 612-626
    • (2005) NeuroRx , vol.2 , Issue.4 , pp. 612-626
    • Jacobsen, J.S.1    Reinhart, P.2    Pangalos, M.N.3
  • 24
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., and Glabe C.G. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300 5618 (2003) 486-489
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 26
    • 0032496368 scopus 로고    scopus 로고
    • Amyloidogenic determinant as a substrate recognition motif of insulin-degrading enzyme
    • Kurochkin I.V. Amyloidogenic determinant as a substrate recognition motif of insulin-degrading enzyme. FEBS Lett. 427 2 (1998) 153-156
    • (1998) FEBS Lett. , vol.427 , Issue.2 , pp. 153-156
    • Kurochkin, I.V.1
  • 27
    • 17044439021 scopus 로고    scopus 로고
    • Alzheimer's disease: Aβ, tau and synaptic dysfunction
    • LaFerla F.M., and Oddo S. Alzheimer's disease: Aβ, tau and synaptic dysfunction. Trends Mol. Med. 11 4 (2005) 170-176
    • (2005) Trends Mol. Med. , vol.11 , Issue.4 , pp. 170-176
    • LaFerla, F.M.1    Oddo, S.2
  • 29
    • 0034682414 scopus 로고    scopus 로고
    • Neurotoxicity induces cleavage of p35 to p25 by calpain
    • Lee M.S., Kwon Y.T., Li M., Peng J., Friedlander R.M., and Tsai L.H. Neurotoxicity induces cleavage of p35 to p25 by calpain. Nature 405 6784 (2000) 360-364
    • (2000) Nature , vol.405 , Issue.6784 , pp. 360-364
    • Lee, M.S.1    Kwon, Y.T.2    Li, M.3    Peng, J.4    Friedlander, R.M.5    Tsai, L.H.6
  • 31
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution
    • LeVine III H. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2 3 (1993) 404-410
    • (1993) Protein Sci. , vol.2 , Issue.3 , pp. 404-410
    • LeVine III, H.1
  • 32
    • 0033695663 scopus 로고    scopus 로고
    • Distinct molecular mechanisms and divergent endocytotic pathways of AMPA receptor internalization
    • Lin J.W., Ju W., Foster K., Lee S.H., Ahmadian G., Wyszynski M., Wang Y.T., and Sheng M. Distinct molecular mechanisms and divergent endocytotic pathways of AMPA receptor internalization. Nat. Neurosci. 3 12 (2000) 1282-1290
    • (2000) Nat. Neurosci. , vol.3 , Issue.12 , pp. 1282-1290
    • Lin, J.W.1    Ju, W.2    Foster, K.3    Lee, S.H.4    Ahmadian, G.5    Wyszynski, M.6    Wang, Y.T.7    Sheng, M.8
  • 33
    • 0346099098 scopus 로고    scopus 로고
    • Residues 17-20 and 30-35 of β-amyloid play critical roles in aggregation
    • Liu R., McAllister C., Lyubchenko Y., and Sierks M.R. Residues 17-20 and 30-35 of β-amyloid play critical roles in aggregation. J. Neurosci. Res. 75 2 (2004) 162-171
    • (2004) J. Neurosci. Res. , vol.75 , Issue.2 , pp. 162-171
    • Liu, R.1    McAllister, C.2    Lyubchenko, Y.3    Sierks, M.R.4
  • 34
    • 0033681557 scopus 로고    scopus 로고
    • Regulation of AMPA receptor-mediated synaptic transmission by clathrin-dependent receptor internalization
    • Man H.Y., Lin J.W., Ju W.H., Ahmadian G., Liu L., Becker L.E., Sheng M., and Wang Y.T. Regulation of AMPA receptor-mediated synaptic transmission by clathrin-dependent receptor internalization. Neuron 25 3 (2000) 649-662
    • (2000) Neuron , vol.25 , Issue.3 , pp. 649-662
    • Man, H.Y.1    Lin, J.W.2    Ju, W.H.3    Ahmadian, G.4    Liu, L.5    Becker, L.E.6    Sheng, M.7    Wang, Y.T.8
  • 36
    • 0032526423 scopus 로고    scopus 로고
    • β-Amyloid fibrils activate parallel mitogen-activated protein kinase pathways in microglia and THP1 monocytes
    • McDonald D.R., Bamberger M.E., Combs C.K., and Landreth G.E. β-Amyloid fibrils activate parallel mitogen-activated protein kinase pathways in microglia and THP1 monocytes. J. Neurosci. 18 12 (1998) 4451-4460
    • (1998) J. Neurosci. , vol.18 , Issue.12 , pp. 4451-4460
    • McDonald, D.R.1    Bamberger, M.E.2    Combs, C.K.3    Landreth, G.E.4
  • 38
    • 0037393454 scopus 로고    scopus 로고
    • Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: a case report
    • Nicoll J.A., Wilkinson D., Holmes C., Steart P., Markham H., and Weller R.O. Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: a case report. Nat. Med. 9 4 (2003) 448-452
    • (2003) Nat. Med. , vol.9 , Issue.4 , pp. 448-452
    • Nicoll, J.A.1    Wilkinson, D.2    Holmes, C.3    Steart, P.4    Markham, H.5    Weller, R.O.6
  • 40
    • 0028981219 scopus 로고
    • Structure-activity analyses of β-amyloid peptides: contributions of the β 25-35 region to aggregation and neurotoxicity
    • Pike C.J., Walencewicz-Wasserman A.J., Kosmoski J., Cribbs D.H., Glabe C.G., and Cotman C.W. Structure-activity analyses of β-amyloid peptides: contributions of the β 25-35 region to aggregation and neurotoxicity. J. Neurochem. 64 1 (1995) 253-265
    • (1995) J. Neurochem. , vol.64 , Issue.1 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 41
    • 13944272576 scopus 로고    scopus 로고
    • The role of insulin receptor signaling in the brain
    • Plum L., Schubert M., and Bruning J.C. The role of insulin receptor signaling in the brain. Trends Endocrinol. Metab. 16 2 (2005) 59-65
    • (2005) Trends Endocrinol. Metab. , vol.16 , Issue.2 , pp. 59-65
    • Plum, L.1    Schubert, M.2    Bruning, J.C.3
  • 42
    • 0028301348 scopus 로고
    • Macromolecular permeability across the blood-nerve and blood-brain barriers
    • Poduslo J.F., Curran G.L., and Berg C.T. Macromolecular permeability across the blood-nerve and blood-brain barriers. Proc. Natl. Acad. Sci. U.S.A. 91 12 (1994) 5705-5709
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , Issue.12 , pp. 5705-5709
    • Poduslo, J.F.1    Curran, G.L.2    Berg, C.T.3
  • 43
    • 29844432266 scopus 로고    scopus 로고
    • Insulin, insulin-degrading enzyme and amyloid-β peptide in Alzheimer's disease: review and hypothesis
    • Qiu W.Q., and Folstein M.F. Insulin, insulin-degrading enzyme and amyloid-β peptide in Alzheimer's disease: review and hypothesis. Neurobiol. Aging 27 2 (2006) 190-198
    • (2006) Neurobiol. Aging , vol.27 , Issue.2 , pp. 190-198
    • Qiu, W.Q.1    Folstein, M.F.2
  • 48
    • 0035950225 scopus 로고    scopus 로고
    • Clearing the brain's amyloid cobwebs
    • Selkoe D.J. Clearing the brain's amyloid cobwebs. Neuron 32 2 (2001) 177-180
    • (2001) Neuron , vol.32 , Issue.2 , pp. 177-180
    • Selkoe, D.J.1
  • 49
    • 0001181116 scopus 로고    scopus 로고
    • Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics
    • Selkoe D.J., and Schenk D. Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics. Annu. Rev. Pharmacol. Toxicol. 43 (2003) 545-584
    • (2003) Annu. Rev. Pharmacol. Toxicol. , vol.43 , pp. 545-584
    • Selkoe, D.J.1    Schenk, D.2
  • 52
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: a potent role for trimers
    • Townsend M., Shankar G.M., Mehta T., Walsh D.M., and Selkoe D.J. Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: a potent role for trimers. J. Physiol. 572 2 (2006) 477-492
    • (2006) J. Physiol. , vol.572 , Issue.2 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Mehta, T.3    Walsh, D.M.4    Selkoe, D.J.5
  • 54
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., and Selkoe D.J. Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 6880 (2002) 535-539
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 55
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate
    • Walsh D.M., Lomakin A., Benedek G.B., Condron M.M., and Teplow D.B. Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 272 35 (1997) 22364-22372
    • (1997) J. Biol. Chem. , vol.272 , Issue.35 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 56
    • 14944378094 scopus 로고    scopus 로고
    • Certain inhibitors of synthetic amyloid β-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation
    • Walsh D.M., Townsend M., Podlisny M.B., Shankar G.M., Fadeeva J.V., Agnaf O.E., Hartley D.M., and Selkoe D.J. Certain inhibitors of synthetic amyloid β-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation. J. Neurosci. 25 10 (2005) 2455-2462
    • (2005) J. Neurosci. , vol.25 , Issue.10 , pp. 2455-2462
    • Walsh, D.M.1    Townsend, M.2    Podlisny, M.B.3    Shankar, G.M.4    Fadeeva, J.V.5    Agnaf, O.E.6    Hartley, D.M.7    Selkoe, D.J.8
  • 57
    • 1842610852 scopus 로고    scopus 로고
    • Block of long-term potentiation by naturally secreted and synthetic amyloid β-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5
    • Wang Q., Walsh D.M., Rowan M.J., Selkoe D.J., and Anwyl R. Block of long-term potentiation by naturally secreted and synthetic amyloid β-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5. J. Neurosci. 24 13 (2004) 3370-3378
    • (2004) J. Neurosci. , vol.24 , Issue.13 , pp. 3370-3378
    • Wang, Q.1    Walsh, D.M.2    Rowan, M.J.3    Selkoe, D.J.4    Anwyl, R.5
  • 58
    • 0032562694 scopus 로고    scopus 로고
    • Tracking insulin to the mind
    • Wickelgren I. Tracking insulin to the mind. Science 280 5363 (1998) 517-519
    • (1998) Science , vol.280 , Issue.5363 , pp. 517-519
    • Wickelgren, I.1
  • 59
    • 0027391758 scopus 로고
    • The cellular and physiological actions of insulin in the central nervous system
    • Wozniak M., Rydzewski B., Baker S.P., and Raizada M.K. The cellular and physiological actions of insulin in the central nervous system. Neurochem. Int. 22 1 (1993) 1-10
    • (1993) Neurochem. Int. , vol.22 , Issue.1 , pp. 1-10
    • Wozniak, M.1    Rydzewski, B.2    Baker, S.P.3    Raizada, M.K.4
  • 60
    • 9644302450 scopus 로고    scopus 로고
    • Hemoglobin promotes Aβ oligomer formation and localizes in neurons and amyloid deposits
    • Wu C.W., Liao P.C., Yu L., Wang S.T., Chen S.T., Wu C.M., and Kuo Y.M. Hemoglobin promotes Aβ oligomer formation and localizes in neurons and amyloid deposits. Neurobiol. Dis. 17 3 (2004) 367-377
    • (2004) Neurobiol. Dis. , vol.17 , Issue.3 , pp. 367-377
    • Wu, C.W.1    Liao, P.C.2    Yu, L.3    Wang, S.T.4    Chen, S.T.5    Wu, C.M.6    Kuo, Y.M.7
  • 63
    • 0035142804 scopus 로고    scopus 로고
    • Activation and redistribution of c-jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease
    • Zhu X., Raina A.K., Rottkamp C.A., Aliev G., Perry G., Boux H., and Smith M.A. Activation and redistribution of c-jun N-terminal kinase/stress activated protein kinase in degenerating neurons in Alzheimer's disease. J. Neurochem. 76 2 (2001) 435-441
    • (2001) J. Neurochem. , vol.76 , Issue.2 , pp. 435-441
    • Zhu, X.1    Raina, A.K.2    Rottkamp, C.A.3    Aliev, G.4    Perry, G.5    Boux, H.6    Smith, M.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.