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Volumn , Issue , 2011, Pages

The pathological roles of ganglioside metabolism in Alzheimer's disease: Effects of gangliosides on neurogenesis

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; ANTIGEN; CHOLESTEROL; CHOLINERGIC SPECIFIC ANTIGEN 1 ALPHA; GANGLIOSIDE; GANGLIOSIDE GM1; PHOSPHOLIPID; UNCLASSIFIED DRUG;

EID: 79952176116     PISSN: None     EISSN: 20900252     Source Type: Journal    
DOI: 10.4061/2011/193618     Document Type: Review
Times cited : (42)

References (138)
  • 1
    • 48549100652 scopus 로고    scopus 로고
    • Role of ganglioside metabolism in the pathogenesis of Alzheimer's diseasea review
    • Ariga T., McDonald M. P., Yu R. K., Role of ganglioside metabolism in the pathogenesis of Alzheimer's diseasea review Journal of Lipid Research 2008 49 6 1157 1175
    • (2008) Journal of Lipid Research , vol.49 , Issue.6 , pp. 1157-1175
    • Ariga, T.1    McDonald, M.P.2    Yu, R.K.3
  • 2
    • 77955364852 scopus 로고    scopus 로고
    • Role of proteoglycans and glycosaminoglycans in the pathogenesis of Alzheimer's disease and related disorders: Amyloidogenesis and therapeutic strategiesa review
    • Ariga T., Miyatake T., Yu R. K., Role of proteoglycans and glycosaminoglycans in the pathogenesis of Alzheimer's disease and related disorders: amyloidogenesis and therapeutic strategiesa review Journal of Neuroscience Research 2010 88 11 2303 2315
    • (2010) Journal of Neuroscience Research , vol.88 , Issue.11 , pp. 2303-2315
    • Ariga, T.1    Miyatake, T.2    Yu, R.K.3
  • 3
    • 66349103103 scopus 로고    scopus 로고
    • The role of glycosphingolipid metabolism in the developing brain
    • Yu R. K., Nakatani Y., Yanagisawa M., The role of glycosphingolipid metabolism in the developing brain Journal of Lipid Research 2009 50 S440 S445
    • (2009) Journal of Lipid Research , vol.50
    • Yu, R.K.1    Nakatani, Y.2    Yanagisawa, M.3
  • 4
    • 36448995805 scopus 로고    scopus 로고
    • Developmental changes of glycosphingolipids and expression of glycogenes in mouse brains
    • DOI 10.1111/j.1471-4159.2007.04910.x
    • Ngamukote S., Yanagisawa M., Ariga T., Ando S., Yu R. K., Developmental changes of glycosphingolipids and expression of glycog (Pubitemid 350173557)
    • (2007) Journal of Neurochemistry , vol.103 , Issue.6 , pp. 2327-2341
    • Ngamukote, S.1    Yanagisawa, M.2    Ariga, T.3    Ando, S.4    Yu, R.K.5
  • 5
    • 34447304629 scopus 로고    scopus 로고
    • The expression and functions of glycoconjugates in neural stem cells
    • DOI 10.1093/glycob/cwm018
    • Yanagisawa M., Yu R. K., The expression and functions of glycoconjugates in neural stem cells Glycobiology 2007 17 7 57R 74R (Pubitemid 47050656)
    • (2007) Glycobiology , vol.17 , Issue.7
    • Yanagisawa, M.1    Yu, R.K.2
  • 6
    • 0028212835 scopus 로고
    • Development regulation of ganglioside metabolism
    • Yu R. K., Development regulation of ganglioside metabolism Progress in Brain Research 1994 101 31 44 (Pubitemid 24084736)
    • (1994) Progress in Brain Research , vol.101 , pp. 31-44
    • Yu, R.K.1
  • 8
    • 24044519084 scopus 로고    scopus 로고
    • GM1 ganglioside prevented the decline of hippocampal neurogenesis associated with D-galactose
    • DOI 10.1097/01.wnr.0000174405.24763.bc
    • Zhang Q., Huang Y., Li X., Cui X., Zuo P., Li J., GM1 ganglioside prevented the decline of hippocampal neurogenesis associated with D-galactose NeuroReport 2005 16 12 1297 1301 (Pubitemid 41225199)
    • (2005) NeuroReport , vol.16 , Issue.12 , pp. 1297-1301
    • Zhang, Q.1    Huang, Y.2    Li, X.3    Cui, X.4    Zuo, P.5    Li, J.6
  • 9
    • 33947222694 scopus 로고    scopus 로고
    • Effects of gangliosides on ethanol-induced neurodegeneration in the developing mouse brain
    • DOI 10.1111/j.1530-0277.2007.00351.x
    • Saito M., Mao R. F., Wang R., Vadasz C., Saito M., Effects of gangliosides on ethanol-induced neurodegeneration in the developing mouse brain Alcoholism: Clinical and Experimental Research 2007 31 4 665 674 (Pubitemid 46434903)
    • (2007) Alcoholism: Clinical and Experimental Research , vol.31 , Issue.4 , pp. 665-674
    • Saito, M.1    Mao, R.-F.2    Wang, R.3    Vadasz, C.4    Saito, M.5
  • 10
    • 0036361744 scopus 로고    scopus 로고
    • Alzheimer diseaseeffect of continuous intracerebroventricular treatment with GM1 ganglioside and a systematic activation programme
    • Svennerholm L., Brne G., Karlsson I., Lekman A., Ramstrm I., Wikkels C., Alzheimer diseaseeffect of continuous intracerebroventricular treatment with GM1 ganglioside and a systematic activation programme Dementia and Geriatric Cognitive Disorders 2002 14 3 128 136
    • (2002) Dementia and Geriatric Cognitive Disorders , vol.14 , Issue.3 , pp. 128-136
    • Svennerholm, L.1    Brne, G.2    Karlsson, I.3    Lekman, A.4    Ramstrm, I.5    Wikkels, C.6
  • 11
  • 13
    • 0031798568 scopus 로고    scopus 로고
    • Parkinson's disease improved function with GM1 ganglioside treatment in a randomized placebo-controlled study
    • Schneider J. S., Roeltgen D. P., Mancall E. L., Chapas-Crilly J., Rothblat D. S., Tatarian G. T., Parkinson's disease improved function with GM1 ganglioside treatment in a randomized placebo-controlled study Neurology 1998 50 6 1630 1636 (Pubitemid 28283228)
    • (1998) Neurology , vol.50 , Issue.6 , pp. 1630-1636
    • Schneider, J.S.1    Roeltgen, D.P.2    Mancall, E.L.3    Chapas-Crilly, J.4    Rothblat, D.S.5    Tatarian, G.T.6
  • 15
    • 27644558148 scopus 로고    scopus 로고
    • Guillain-Barr syndrome
    • Hughes R. A., Cornblath D. R., Guillain-Barr syndrome The Lancet 2005 366 9497 1653 1666
    • (2005) The Lancet , vol.366 , Issue.9497 , pp. 1653-1666
    • Hughes, R.A.1    Cornblath, D.R.2
  • 16
    • 1442351177 scopus 로고    scopus 로고
    • Binding sites of amyloid β-peptide in cell plasma membrane and implications for Alzheimer's disease
    • DOI 10.2174/1389203043486937
    • Verdier Y., Penke B., Binding sites of amyloid -peptide in cell plasma membrane and implications for Alzheimer's disease Current Protein and Peptide Science 2004 5 1 19 31 (Pubitemid 38279402)
    • (2004) Current Protein and Peptide Science , vol.5 , Issue.1 , pp. 19-31
    • Verdier, Y.1    Penke, B.2
  • 18
    • 78649790233 scopus 로고    scopus 로고
    • Sphingolipids in neurodegeneration
    • Haughey N. J., Sphingolipids in neurodegeneration NeuroMolecular Medicine 2010 12 4 301 305
    • (2010) NeuroMolecular Medicine , vol.12 , Issue.4 , pp. 301-305
    • Haughey, N.J.1
  • 19
    • 77953268102 scopus 로고    scopus 로고
    • Roles for dysfunctional sphingolipid metabolism in Alzheimer's disease neuropathogenesis
    • Haughey N. J., Bandaru V. V. R., Bae M., Mattson M. P., Roles for dysfunctional sphingolipid metabolism in Alzheimer's disease neuropathogenesis Biochimica et Biophysica Acta 2010 1801 8 878 886
    • (2010) Biochimica et Biophysica Acta , vol.1801 , Issue.8 , pp. 878-886
    • Haughey, N.J.1    Bandaru, V.V.R.2    Bae, M.3    Mattson, M.P.4
  • 21
    • 33646557678 scopus 로고    scopus 로고
    • The role of lipid-protein interactions in amyloid-type protein fibril formation
    • DOI 10.1016/j.chemphyslip.2006.02.006, PII S0009308406000260
    • Gorbenko G. P., Kinnunen P. K. J., The role of lipid-protein interactions in amyloid-type protein fibril formation Chemistry and Physics of Lipids 2006 141 1-2 72 82 (Pubitemid 43728804)
    • (2006) Chemistry and Physics of Lipids , vol.141 , Issue.1-2 , pp. 72-82
    • Gorbenko, G.P.1    Kinnunen, P.K.J.2
  • 22
    • 33745754350 scopus 로고    scopus 로고
    • Altered membrane fluidity and lipid raft composition in presenilin-deficient cells
    • DOI 10.1111/j.1600-0404.2006.00682.x
    • Grimm M. O. W., Tschpe J. A., Grimm H. S., Zinser E. G., Hartmann T., Altered membrane fluidity and lipid raft composition in presenilin-deficient cells Acta Neurologica Scandinavica 2006 114 185 27 32 (Pubitemid 44015222)
    • (2006) Acta Neurologica Scandinavica , vol.114 , Issue.SUPPL. 185 , pp. 27-32
    • Grimm, M.O.W.1    Tschape, J.-A.2    Grimm, H.S.3    Zinser, E.G.4    Hartmann, T.5
  • 23
    • 58549084816 scopus 로고    scopus 로고
    • Amyloid- membrane binding and permeabilization are distinct processes influenced separately by membrane charge and fluidity
    • Wong P. T., Schauerte J. A., Wisser K. C., Ding H., Lee E. L., Steel D. G., Gafni A., Amyloid- membrane binding and permeabilization are distinct processes influenced separately by membrane charge and fluidity Journal of Molecular Biology 2009 386 1 81 96
    • (2009) Journal of Molecular Biology , vol.386 , Issue.1 , pp. 81-96
    • Wong, P.T.1    Schauerte, J.A.2    Wisser, K.C.3    Ding, H.4    Lee, E.L.5    Steel, D.G.6    Gafni, A.7
  • 24
    • 0025328363 scopus 로고
    • 1 membranous ganglioside
    • DOI 10.1016/0006-8993(90)91592-5
    • Iwamoto N., Suzuki Y., Makino Y., Haga C., Kosaka K., Iizuka R., Cell membrane changes in brains manifesting senile plaques: an immunohistochemical study of GM membranous ganglioside Brain Research 1990 522 1 152 156 (Pubitemid 20208800)
    • (1990) Brain Research , vol.522 , Issue.1 , pp. 152-156
    • Iwamoto, N.1    Suzuki, Y.2    Makino, Y.3    Haga, C.4    Kosaka, K.5    Iizuka, R.6
  • 25
    • 0025846971 scopus 로고
    • Immunohistological study on brains of Alzheimer's disease using antibodies to fetal antigens, C-series gangliosides and microtubule-associated protein 5
    • Takahashi H., Hirokawa K., Ando S., Obata K., Immunohistological study on brains of Alzheimer's disease using antibodies to fetal antigens, C-series gangliosides and microtubule-associated protein 5 Acta Neuropathologica 1991 81 6 626 631
    • (1991) Acta Neuropathologica , vol.81 , Issue.6 , pp. 626-631
    • Takahashi, H.1    Hirokawa, K.2    Ando, S.3    Obata, K.4
  • 26
    • 0027216957 scopus 로고
    • Anti-ganglioside GD1a monoclonal antibody recognizes senile plaques in the brains of patients with Alzheimer-type dementia
    • DOI 10.1016/0168-0102(93)90093-6
    • Nishinaka T., Iwata D., Shimada S., Kosaka K., Suzuki Y., Anti-ganglioside GD1a monoclonal antibody recognizes senile plaques in the brains of patients with Alzheimer-type dementia Neuroscience Research 1993 17 2 171 176 (Pubitemid 23266174)
    • (1993) Neuroscience Research , vol.17 , Issue.2 , pp. 171-176
    • Nishinaka, T.1    Iwata, D.2    Shimada, S.3    Kosaka, K.4    Suzuki, Y.5
  • 27
    • 0028982292 scopus 로고
    • Self-association of -amyloid peptide (140) in solution and binding to lipid membranes
    • Terzi E., Holzemann G., Seelig J., Self-association of -amyloid peptide (140) in solution and binding to lipid membranes Journal of Molecular Biology 1995 252 5 633 642
    • (1995) Journal of Molecular Biology , vol.252 , Issue.5 , pp. 633-642
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 28
    • 0030823756 scopus 로고    scopus 로고
    • Acceleration of amyloid fibril formation by specific binding of Aβ-(1- 40) peptide to ganglioside-containing membrane vesicles
    • DOI 10.1074/jbc.272.37.22987
    • Choo-Smith L. P., Garzon-Rodriguez W., Glabe C. G., Surewicz W. K., Acceleration of amyloid fibril formation by specific binding of A -(140) peptide to ganglioside-containing membrane vesicles Journal of Biological Chemistry 1997 272 37 22987 22990 (Pubitemid 27392420)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.37 , pp. 22987-22990
    • Choo-Smith, L.-P.1    Garzon-Rodriguez, W.2    Glabe, C.G.3    Surewicz, W.K.4
  • 29
    • 0033616779 scopus 로고    scopus 로고
    • Interactions of amyloid -peptide (140) with ganglioside-containing membranes
    • Matsuzaki K., Horikiri C., Interactions of amyloid -peptide (140) with ganglioside-containing membranes Biochemistry 1999 38 13 4137 4142
    • (1999) Biochemistry , vol.38 , Issue.13 , pp. 4137-4142
    • Matsuzaki, K.1    Horikiri, C.2
  • 30
    • 0029861772 scopus 로고    scopus 로고
    • Membrane disruption by Alzheimer β-amyloid peptides mediated through specific binding to either phospholipids or gangliosides. Implications for neurotoxicity
    • DOI 10.1074/jbc.271.43.26482
    • McLaurin J., Chakrabartty A., Membrane disruption by Alzheimer -amyloid peptides mediated through specific binding to either phospholipids or gangliosides. Implications for neurotoxicity Journal of Biological Chemistry 1996 271 43 26482 26489 (Pubitemid 26359045)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.43 , pp. 26482-26489
    • McLaurin, J.1    Chakrabartty, A.2
  • 31
    • 0032548943 scopus 로고    scopus 로고
    • Structural transitions associated with the interaction of Alzheimer β- amyloid peptides with gangliosides
    • DOI 10.1074/jbc.273.8.4506
    • McLaurin J., Franklin T., Fraser P. E., Chakrabartty A., Structural transitions associated with the interaction of Alzheimer -amyloid peptides with gangliosides Journal of Biological Chemistry 1998 273 8 4506 4515 (Pubitemid 28103191)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.8 , pp. 4506-4515
    • McLaurin, J.1    Franklin, T.2    Fraser, P.E.3    Chakrabartty, A.4
  • 32
    • 0031054785 scopus 로고    scopus 로고
    • The interaction between Alzheimer amyloid β(1-40) peptide and ganglioside G(M1)-containing membranes
    • DOI 10.1016/S0014-5793(96)01504-9, PII S0014579396015049
    • Choo-Smith L. P., Surewicz W. K., The interaction between Alzheimer amyloid (140) peptide and ganglioside G(M1)-containing membranes FEBS Letters 1997 402 2-3 95 98 (Pubitemid 27078236)
    • (1997) FEBS Letters , vol.402 , Issue.2-3 , pp. 95-98
    • Choo-Smith, L.-P.1    Surewicz, W.K.2
  • 34
    • 1242269212 scopus 로고    scopus 로고
    • Alzheimer's Disease: NMR Studies of Asialo (GM1) and Trisialo (GT1b) Ganglioside Interactions with Aβ(1-40) Peptide in a Membrane Mimic Environment
    • DOI 10.1023/B:NERE.0000013750.80925.25
    • Mandal P. K., Pettegrew J. W., Alzheimer's disease: NMR studies of asialo (GM1) and Trisialo (GT1b) ganglioside interactions with A (140) peptide in a membrane mimic environment Neurochemical Research 2004 29 2 447 453 (Pubitemid 38223028)
    • (2004) Neurochemical Research , vol.29 , Issue.2 , pp. 447-453
    • Mandal, P.K.1    Pettegrew, J.W.2
  • 35
    • 60249099854 scopus 로고    scopus 로고
    • The interaction of amyloid A (140) with lipid bilayers and ganglioside as studied by P solid-state NMR
    • Nakazawa Y., Suzuki Y., Williamson M. P., Sait H., Asakura T., The interaction of amyloid A (140) with lipid bilayers and ganglioside as studied by P solid-state NMR Chemistry and Physics of Lipids 2009 158 1 54 60
    • (2009) Chemistry and Physics of Lipids , vol.158 , Issue.1 , pp. 54-60
    • Nakazawa, Y.1    Suzuki, Y.2    Williamson, M.P.3    Sait, H.4    Asakura, T.5
  • 37
    • 33745675123 scopus 로고    scopus 로고
    • The effect of Aβ conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy
    • DOI 10.1093/jb/mvj083
    • Chen Y. R., Huang H. B., Chyan C. L., Shiao M. S., Lin T. H., Chen Y. C., The effect of A conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy Journal of Biochemistry 2006 139 4 733 740 (Pubitemid 43973920)
    • (2006) Journal of Biochemistry , vol.139 , Issue.4 , pp. 733-740
    • Chen, Y.R.1    Huang, H.B.2    Chyan, C.L.3    Shiao, M.S.4    Lin, T.H.5    Chen, Y.C.6
  • 38
    • 33746925586 scopus 로고    scopus 로고
    • Binding of amyloid β-peptide to ganglioside micelles is dependent on histidine-13
    • DOI 10.1042/BJ20060293
    • Williamson M. P., Suzuki Y., Bourne N. T., Asakura T., Binding of amyloid -peptide to ganglioside micelles is dependent on histidine-13 Biochemical Journal 2006 397 3 483 490 (Pubitemid 44187506)
    • (2006) Biochemical Journal , vol.397 , Issue.3 , pp. 483-490
    • Williamson, M.P.1    Suzuki, Y.2    Bourne, N.T.3    Asakura, T.4
  • 40
    • 72649096531 scopus 로고    scopus 로고
    • Up-and-down topological mode of amyloid -peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters
    • Utsumi M., Yamaguchi Y., Sasakawa H., Yamamoto N., Yanagisawa K., Kato K., Up-and-down topological mode of amyloid -peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters Glycoconjugate Journal 2009 26 8 999 1006
    • (2009) Glycoconjugate Journal , vol.26 , Issue.8 , pp. 999-1006
    • Utsumi, M.1    Yamaguchi, Y.2    Sasakawa, H.3    Yamamoto, N.4    Yanagisawa, K.5    Kato, K.6
  • 41
    • 77649270452 scopus 로고    scopus 로고
    • NMR characterization of the interactions between lyso-GM1 aqueous micelles and amyloid
    • Yagi-Utsumi M., Kameda T., Yamaguchi Y., Kato K., NMR characterization of the interactions between lyso-GM1 aqueous micelles and amyloid FEBS Letters 2010 584 4 831 836
    • (2010) FEBS Letters , vol.584 , Issue.4 , pp. 831-836
    • Yagi-Utsumi, M.1    Kameda, T.2    Yamaguchi, Y.3    Kato, K.4
  • 42
    • 0028885854 scopus 로고
    • GM1 ganglioside-bound amyloid -protein (AB): A possible form of preamyloid in Alzheimer's disease
    • Yanagisawa K., Odaka A., Suzuki N., Ihara Y., GM1 ganglioside-bound amyloid -protein (AB): a possible form of preamyloid in Alzheimer's disease Nature Medicine 1995 1 10 1062 1066
    • (1995) Nature Medicine , vol.1 , Issue.10 , pp. 1062-1066
    • Yanagisawa, K.1    Odaka, A.2    Suzuki, N.3    Ihara, Y.4
  • 43
    • 34547152918 scopus 로고    scopus 로고
    • Role of gangliosides in Alzheimer's disease
    • DOI 10.1016/j.bbamem.2007.01.018, PII S0005273607000302
    • Yanagisawa K., Role of gangliosides in Alzheimer's disease Biochimica et Biophysica Acta 2007 1768 8 1943 1951 (Pubitemid 47125848)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.8 , pp. 1943-1951
    • Yanagisawa, K.1
  • 44
    • 0031957080 scopus 로고    scopus 로고
    • GM1 ganglioside-bound amyloid -protein in Alzheimer's disease brain
    • Yanagisawa K., Ihara Y., GM1 ganglioside-bound amyloid -protein in Alzheimer's disease brain Neurobiology of Aging 1998 19 1 S65 S67
    • (1998) Neurobiology of Aging , vol.19 , Issue.1
    • Yanagisawa, K.1    Ihara, Y.2
  • 45
    • 35148816608 scopus 로고    scopus 로고
    • Endosomal accumulation of GM1 ganglioside-bound amyloid β-protein in neurons of aged monkey brains
    • DOI 10.1097/WNR.0b013e3282f0d2ab, PII 0000175620071029000007
    • Kimura N., Yanagisawa K., Endosomal accumulation of GM1 ganglioside-bound amyloid -protein in neurons of aged monkey brains NeuroReport 2007 18 16 1669 1673 (Pubitemid 47549131)
    • (2007) NeuroReport , vol.18 , Issue.16 , pp. 1669-1673
    • Kimura, N.1    Yanagisawa, K.2
  • 46
    • 1942420641 scopus 로고    scopus 로고
    • M1 ganglioside
    • DOI 10.1016/j.peptides.2004.01.001, PII S0196978104000038
    • Kurganov B., Doh M., Arispe N., Aggregation of liposomes induced by the toxic peptides Alzheimer's A s, human amylin and prion (106126): facilitation by membrane-bound GM1 ganglioside Peptides 2004 25 2 217 232 (Pubitemid 38520052)
    • (2004) Peptides , vol.25 , Issue.2 , pp. 217-232
    • Kurganov, B.1    Doh, M.2    Arispe, N.3
  • 47
    • 16344382167 scopus 로고    scopus 로고
    • Assembly of hereditary amyloid β-protein variants in the presence of favorable gangliosides
    • DOI 10.1016/j.febslet.2005.03.013
    • Yamamoto N., Hirabayashi Y., Amari M., Yamaguchi H., Romanov G., Van Nostrand W. E., Yanagisawa K., Assembly of hereditary amyloid -protein variants in the presence of favorable gangliosides FEBS Letters 2005 579 10 2185 2190 (Pubitemid 40469690)
    • (2005) FEBS Letters , vol.579 , Issue.10 , pp. 2185-2190
    • Yamamoto, N.1    Hirabayashi, Y.2    Amari, M.3    Yamaguchi, H.4    Romanov, G.5    Van Nostrand, W.E.6    Yanagisawa, K.7
  • 48
    • 51249115821 scopus 로고    scopus 로고
    • Formation of toxic A (140) fibrils on GM1 ganglioside-containing membranes mimicking lipid rafts: Polymorphisms in A (140) fibrils
    • Okada T., Ikeda K., Wakabayashi M., Ogawa M., Matsuzaki K., Formation of toxic A (140) fibrils on GM1 ganglioside-containing membranes mimicking lipid rafts: polymorphisms in A (140) fibrils Journal of Molecular Biology 2008 382 4 1066 1074
    • (2008) Journal of Molecular Biology , vol.382 , Issue.4 , pp. 1066-1074
    • Okada, T.1    Ikeda, K.2    Wakabayashi, M.3    Ogawa, M.4    Matsuzaki, K.5
  • 49
    • 0642348930 scopus 로고    scopus 로고
    • Cholesterol and A aggregation
    • Yanagisawa K., Cholesterol and A aggregation Pharmacopsychiatry 2003 36 2 S127 S129
    • (2003) Pharmacopsychiatry , vol.36 , Issue.2
    • Yanagisawa, K.1
  • 51
    • 34547118151 scopus 로고    scopus 로고
    • Formation of Amyloids by Aβ-(1-42) on NGF-differentiated PC12 Cells: Roles of Gangliosides and Cholesterol
    • DOI 10.1016/j.jmb.2007.06.008, PII S0022283607007905
    • Wakabayashi M., Matsuzaki K., Formation of amyloids by A -(1-42) on NGF-differentiated PC12 cells: roles of gangliosides and cholesterol Journal of Molecular Biology 2007 371 4 924 933 (Pubitemid 47101820)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.4 , pp. 924-933
    • Wakabayashi, M.1    Matsuzaki, K.2
  • 52
    • 0035834692 scopus 로고    scopus 로고
    • Reduction in cholesterol and sialic acid content protects cells from the toxic effects of -amyloid peptides
    • Wang S. S. S., Rymer D. L., Good T. A., Reduction in cholesterol and sialic acid content protects cells from the toxic effects of -amyloid peptides Journal of Biological Chemistry 2001 276 45 42027 42034
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.45 , pp. 42027-42034
    • Wang, S.S.S.1    Rymer, D.L.2    Good, T.A.3
  • 53
    • 46149092957 scopus 로고    scopus 로고
    • Examining the levels of ganglioside and cholesterol in cell membrane on attenuation the cytotoxicity of beta-amyloid peptide
    • Lin M. S., Chen L. Y., Wang S. S. S., Chang Y., Chen W. Y., Examining the levels of ganglioside and cholesterol in cell membrane on attenuation the cytotoxicity of beta-amyloid peptide Colloids and Surfaces B 2008 65 2 172 177
    • (2008) Colloids and Surfaces B , vol.65 , Issue.2 , pp. 172-177
    • Lin, M.S.1    Chen, L.Y.2    Wang, S.S.S.3    Chang, Y.4    Chen, W.Y.5
  • 54
    • 6044221306 scopus 로고    scopus 로고
    • GM1 ganglioside regulates the proteolysis of amyloid precursor protein
    • DOI 10.1038/sj.mp.4001509
    • Zha Q., Ruan Y., Hartmann T., Beyreuther K., Zhang D., GM1 ganglioside regulates the proteolysis of amyloid precursor protein Molecular Psychiatry 2004 9 10 946 952 (Pubitemid 39381958)
    • (2004) Molecular Psychiatry , vol.9 , Issue.10 , pp. 946-952
    • Zha, Q.1    Ruan, Y.2    Hartmann, T.3    Beyreuther, K.4    Zhang, D.5
  • 56
    • 65549129594 scopus 로고    scopus 로고
    • Late endocytic dysfunction as a putative cause of amyloid fibril formation in Alzheimer's disease
    • Yuyama K., Yanagisawa K., Late endocytic dysfunction as a putative cause of amyloid fibril formation in Alzheimer's disease Journal of Neurochemistry 2009 109 5 1250 1260
    • (2009) Journal of Neurochemistry , vol.109 , Issue.5 , pp. 1250-1260
    • Yuyama, K.1    Yanagisawa, K.2
  • 57
    • 55749095544 scopus 로고    scopus 로고
    • Age-dependent high-density clustering of GM1 ganglioside at presynaptic neuritic terminals promotes amyloid -protein fibrillogenesis
    • Yamamoto N., Matsubara T., Sato T., Yanagisawa K., Age-dependent high-density clustering of GM1 ganglioside at presynaptic neuritic terminals promotes amyloid -protein fibrillogenesis Biochimica et Biophysica Acta 2008 1778 12 2717 2726
    • (2008) Biochimica et Biophysica Acta , vol.1778 , Issue.12 , pp. 2717-2726
    • Yamamoto, N.1    Matsubara, T.2    Sato, T.3    Yanagisawa, K.4
  • 58
    • 25144505865 scopus 로고    scopus 로고
    • Suppression of Aβ deposition in brain by peripheral administration of Fab fragments of anti-seed antibody
    • DOI 10.1016/j.bbrc.2005.06.208, PII S0006291X05014786
    • Yamamoto N., Yokoseki T., Shibata M., Yamaguchi H., Yanagisawa K., Suppression of A deposition in brain by peripheral administration of Fab fragments of anti-seed antibody Biochemical and Biophysical Research Communications 2005 335 1 45 47 (Pubitemid 41350761)
    • (2005) Biochemical and Biophysical Research Communications , vol.335 , Issue.1 , pp. 45-47
    • Yamamoto, N.1    Yokoseki, T.2    Shibata, M.3    Yamaguchi, H.4    Yanagisawa, K.5
  • 59
    • 77955341552 scopus 로고    scopus 로고
    • Sphingomyelin accumulation provides a favorable milieu for GM1 ganglioside-induced assembly of amyloid -protein
    • Yuyama K., Yanagisawa K., Sphingomyelin accumulation provides a favorable milieu for GM1 ganglioside-induced assembly of amyloid -protein Neuroscience Letters 2010 481 3 168 172
    • (2010) Neuroscience Letters , vol.481 , Issue.3 , pp. 168-172
    • Yuyama, K.1    Yanagisawa, K.2
  • 60
    • 18844428601 scopus 로고    scopus 로고
    • GM1 ganglioside and the seeding of amyloid in Alzheimer's disease: Endogenous seed for Alzheimer amyloid
    • DOI 10.1177/1073858405275177
    • Yanagisawa K., GM1 ganglioside and the seeding of amyloid in Alzheimer's disease: endogenous seed for Alzheimer amyloid Neuroscientist 2005 11 3 250 260 (Pubitemid 40686726)
    • (2005) Neuroscientist , vol.11 , Issue.3 , pp. 250-260
    • Yanagisawa, K.1
  • 61
    • 33847738814 scopus 로고    scopus 로고
    • Lipid rafts: Structure, function and role in HIV, Alzheimer's and prion diseases
    • Fantini J., Garmy N., Mahfoud R., Yahi N., Lipid rafts: structure, function and role in HIV, Alzheimer's and prion diseases Expert Reviews in Molecular Medicine 2002 4 27 1 22
    • (2002) Expert Reviews in Molecular Medicine , vol.4 , Issue.27 , pp. 1-22
    • Fantini, J.1    Garmy, N.2    Mahfoud, R.3    Yahi, N.4
  • 62
    • 0037062582 scopus 로고    scopus 로고
    • Interactions of amyloid β-protein with various gangliosides in raft-like membranes: Importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid
    • DOI 10.1021/bi0255874
    • Kakio A., Nishimoto S. I., Yanagisawa K., Kozutsumi Y., Matsuzaki K., Interactions of amyloid -protein with various gangliosides in raft-like membranes: importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid Biochemistry 2002 41 23 7385 7390 (Pubitemid 34602456)
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7385-7390
    • Kakio, A.1    Nishimoto, S.-I.2    Yanagisawa, K.3    Kozutsumi, Y.4    Matsuzaki, K.5
  • 63
    • 77952510090 scopus 로고    scopus 로고
    • Surface-induced phase separation of a sphingomyelin/cholesterol/ ganglioside GM1-planar bilayer on mica surfaces and microdomain molecular conformation that accelerates A oligomerization
    • Mao Y., Shang Z., Imai Y., Hoshino T., Tero R., Tanaka M., Yamamoto N., Yanagisawa K., Urisu T., Surface-induced phase separation of a sphingomyelin/cholesterol/ganglioside GM1-planar bilayer on mica surfaces and microdomain molecular conformation that accelerates A oligomerization Biochimica et Biophysica Acta 2010 1798 6 1090 1099
    • (2010) Biochimica et Biophysica Acta , vol.1798 , Issue.6 , pp. 1090-1099
    • Mao, Y.1    Shang, Z.2    Imai, Y.3    Hoshino, T.4    Tero, R.5    Tanaka, M.6    Yamamoto, N.7    Yanagisawa, K.8    Urisu, T.9
  • 64
    • 77953235479 scopus 로고    scopus 로고
    • A polymerization through interaction with membrane gangliosides
    • Matsuzaki K., Kato K., Yanagisawa K., A polymerization through interaction with membrane gangliosides Biochimica et Biophysica Acta 2010 1801 8 868 877
    • (2010) Biochimica et Biophysica Acta , vol.1801 , Issue.8 , pp. 868-877
    • Matsuzaki, K.1    Kato, K.2    Yanagisawa, K.3
  • 65
    • 0036516378 scopus 로고    scopus 로고
    • Interactions between amyloid betaprotein and gangliosides
    • Matsuzaki K., Interactions between amyloid betaprotein and gangliosides Tanpakushitsu Kakusan Koso 2002 47 4 351 356
    • (2002) Tanpakushitsu Kakusan Koso , vol.47 , Issue.4 , pp. 351-356
    • Matsuzaki, K.1
  • 66
    • 33749467048 scopus 로고    scopus 로고
    • Amyloid oligomerization is induced by brain lipid rafts
    • Kim S. I., Yi J. S., Ko Y. G., Amyloid oligomerization is induced by brain lipid rafts Journal of Cellular Biochemistry 2006 99 3 878 889
    • (2006) Journal of Cellular Biochemistry , vol.99 , Issue.3 , pp. 878-889
    • Kim, S.I.1    Yi, J.S.2    Ko, Y.G.3
  • 67
    • 69249209894 scopus 로고    scopus 로고
    • Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts
    • Wakabayashi M., Matsuzaki K., Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts FEBS Letters 2009 583 17 2854 2858
    • (2009) FEBS Letters , vol.583 , Issue.17 , pp. 2854-2858
    • Wakabayashi, M.1    Matsuzaki, K.2
  • 69
    • 16344382167 scopus 로고    scopus 로고
    • Assembly of hereditary amyloid β-protein variants in the presence of favorable gangliosides
    • DOI 10.1016/j.febslet.2005.03.013
    • Yamamoto N., Hirabayashi Y., Amari M., Yamaguchi H., Romanov G., Van Nostrand W. E., Yanagisawa K., Assembly of hereditary amyloid -protein variants in the presence of favorable gangliosides FEBS Letters 2005 579 10 2185 2190 (Pubitemid 40469690)
    • (2005) FEBS Letters , vol.579 , Issue.10 , pp. 2185-2190
    • Yamamoto, N.1    Hirabayashi, Y.2    Amari, M.3    Yamaguchi, H.4    Romanov, G.5    Van Nostrand, W.E.6    Yanagisawa, K.7
  • 70
    • 33750328015 scopus 로고    scopus 로고
    • Further evidence of local ganglioside-dependent amyloid β-protein assembly in brain
    • DOI 10.1097/01.wnr.0000239958.53072.14, PII 0000175620061106000015
    • Yamamoto N., Van Nostrand W. E., Yanagisawa K., Further evidence of local ganglioside-dependent amyloid -protein assembly in brain NeuroReport 2006 17 16 1735 1737 (Pubitemid 44621574)
    • (2006) NeuroReport , vol.17 , Issue.16 , pp. 1735-1737
    • Yamamoto, N.1    Van Nostrand, W.E.2    Yanagisawa, K.3
  • 72
    • 33750475909 scopus 로고    scopus 로고
    • Fucosyl-GM1 expression and amyloid-β protein accumulation in PC12 cells
    • DOI 10.1002/jnr.21031
    • Yanagisawa M., Ariga T., Yu R. K., Fucosyl-GM1 expression and amyloid- protein accumulation in PC12 cells Journal of Neuroscience Research 2006 84 6 1343 1349 (Pubitemid 44654457)
    • (2006) Journal of Neuroscience Research , vol.84 , Issue.6 , pp. 1343-1349
    • Yanagisawa, M.1    Ariga, T.2    Yu, R.K.3
  • 74
    • 35148846513 scopus 로고    scopus 로고
    • M1: A novel member of lipid membrane microdomain components involved in PC12 cell neuritogenesis
    • DOI 10.1042/BJ20070090
    • Yamazaki Y., Horibata Y., Magatsuka Y., Hirabayashi Y., Hashikawa T., Fucoganglioside -fucosyl( -galactosyl)-GM1: a novel member of lipid membrane microdomain components involved in PC12 cell neuritogenesis Biochemical Journal 2007 407 1 31 40 (Pubitemid 47535578)
    • (2007) Biochemical Journal , vol.407 , Issue.1 , pp. 31-40
    • Yamazaki, Y.1    Horibata, Y.2    Magatsuka, Y.3    Hirabayashi, Y.4    Hashikawa, T.5
  • 75
    • 0023872609 scopus 로고
    • Lipid composition of PC12 pheochromocytoma cells: Characterization of globoside as a major neutral glycolipid
    • Ariga T., Macala L. J., Saito M., Margolis R. K., Greene L. A., Margolis R. U., Yu R. K., Lipid composition of PC12 pheochromocytoma cells: characterization of globoside as a major neutral glycolipid Biochemistry 1988 27 1 52 58 (Pubitemid 18036284)
    • (1988) Biochemistry , vol.27 , Issue.1 , pp. 52-58
    • Ariga, T.1    Macala, L.J.2    Saito, M.3    Margolis, R.K.4    Greene, L.A.5    Margolis, R.U.6    Yu, R.K.7
  • 76
    • 13244272410 scopus 로고    scopus 로고
    • Structural membrane alterations in Alzheimer brains found to be associated with regional disease development; increased density of gangliosides GM1 and GM2 and loss of cholesterol in detergent-resistant membrane domains
    • DOI 10.1111/j.1471-4159.2004.02849.x
    • Molander-Melin M., Blennow K., Bogdanovic N., Dellheden B., Mnsson J. E., Fredman P., Structural membrane alterations in Alzheimer brains found to be associated with regional disease development; increased density of gangliosides GM1 and GM2 and loss of cholesterol in detergent-resistant membrane domains Journal of Neurochemistry 2005 92 1 171 182 (Pubitemid 40193519)
    • (2005) Journal of Neurochemistry , vol.92 , Issue.1 , pp. 171-182
    • Molander-Melin, M.1    Blennow, K.2    Bogdanovic, N.3    Dellheden, B.4    Mansson, J.-E.5    Fredman, P.6
  • 78
    • 0026279740 scopus 로고
    • Regional distribution of brain gangliosides in Alzheimer's disease
    • Kalanj S., Kracun I., Rosner H., Cosovi C., Regional distribution of brain gangliosides in Alzheimer's disease Neurologia Croatica 1991 40 4 269 281
    • (1991) Neurologia Croatica , vol.40 , Issue.4 , pp. 269-281
    • Kalanj, S.1    Kracun, I.2    Rosner, H.3    Cosovi, C.4
  • 79
    • 33745973005 scopus 로고    scopus 로고
    • Ganglioside catabolism is altered in fibroblasts and leukocytes from Alzheimer's disease patients
    • DOI 10.1016/j.neurobiolaging.2005.06.012, PII S0197458005001843
    • Kalanj-Bognar S., Ganglioside catabolism is altered in fibroblasts and leukocytes from Alzheimer's disease patients Neurobiology of Aging 2006 27 9 1354 1356 (Pubitemid 44067301)
    • (2006) Neurobiology of Aging , vol.27 , Issue.9 , pp. 1354-1356
    • Kalanj-Bognar, S.1
  • 80
    • 0028157335 scopus 로고
    • Membrane lipids, selectively diminished in Alzheimer brains, suggest synapse loss as a primary event in early-onset form (type I) and demyelination in late-onset form (type II)
    • Svennerholm L., Gottfries C. G., Membrane lipids, selectively diminished in Alzheimer brains, suggest synapse loss as a primary event in early-onset form (type I) and demyelination in late-onset form (type II) Journal of Neurochemistry 1994 62 3 1039 1047 (Pubitemid 24064516)
    • (1994) Journal of Neurochemistry , vol.62 , Issue.3 , pp. 1039-1047
    • Svennerholm, L.1    Gottfries, C.-G.2
  • 83
    • 0024794215 scopus 로고
    • Gangliosides in the brain in adult Down's syndrome and Alzheimer's disease
    • Brooksbank B. W. L., McGovern J., Gangliosides in the brain in adult Down's syndrome and Alzheimer's disease Molecular and Chemical Neuropathology 1989 11 3 143 156 (Pubitemid 20322833)
    • (1989) Molecular and Chemical Neuropathology , vol.11 , Issue.3 , pp. 143-156
    • Brooksbank, B.W.L.1    McGovern, J.2
  • 85
    • 77958476883 scopus 로고    scopus 로고
    • Ganglioside metabolism in a transgenic mouse model of alzheimer's disease: Expression of Chol-1 antigens in the brain
    • Ariga T., Yanagisawa M., Wakade C., Ando S., Buccafusco J. J., McDonald M. P., Yu R. K., Ganglioside metabolism in a transgenic mouse model of alzheimer's disease: expression of Chol-1 antigens in the brain ASN Neuro 2010 2 4 233 241
    • (2010) ASN Neuro , vol.2 , Issue.4 , pp. 233-241
    • Ariga, T.1    Yanagisawa, M.2    Wakade, C.3    Ando, S.4    Buccafusco, J.J.5    McDonald, M.P.6    Yu, R.K.7
  • 88
    • 35148814075 scopus 로고    scopus 로고
    • Genotype-related changes of ganglioside composition in brain regions of transgenic mouse models of Alzheimer's disease
    • DOI 10.1016/j.neurobiolaging.2006.08.002, PII S0197458006002971
    • Barrier L., Ingrand S., Damjanac M., Rioux Bilan A., Hugon J., Page G., Genotype-related changes of ganglioside composition in brain regions of transgenic mouse models of Alzheimer's disease Neurobiology of Aging 2007 28 12 1863 1872 (Pubitemid 47539690)
    • (2007) Neurobiology of Aging , vol.28 , Issue.12 , pp. 1863-1872
    • Barrier, L.1    Ingrand, S.2    Damjanac, M.3    Rioux Bilan, A.4    Hugon, J.5    Page, G.6
  • 89
    • 0026576050 scopus 로고
    • A trisialoganglioside containing a sialyl 2-6 N-acetylgalactosamine residue is a cholinergic-specific antigen, Chol-1
    • Ando S., Hirabayashi Y., Kon K., Inagaki F., Tate S., Whittaker V. P., A trisialoganglioside containing a sialyl 2-6 N-acetylgalactosamine residue is a cholinergic-specific antigen, Chol-1 Journal of Biochemistry 1992 111 3 287 290
    • (1992) Journal of Biochemistry , vol.111 , Issue.3 , pp. 287-290
    • Ando, S.1    Hirabayashi, Y.2    Kon, K.3    Inagaki, F.4    Tate, S.5    Whittaker, V.P.6
  • 90
    • 0026688825 scopus 로고
    • Structural characterization of a novel cholinergic neuron-specific ganglioside in bovine brain
    • Hirabayashi Y., Nakao T., Irie F., Whittaker V. P., Kon K., Ando S., Structural characterization of a novel cholinergic neuron-specific ganglioside in bovine brain Journal of Biological Chemistry 1992 267 18 12973 12978
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.18 , pp. 12973-12978
    • Hirabayashi, Y.1    Nakao, T.2    Irie, F.3    Whittaker, V.P.4    Kon, K.5    Ando, S.6
  • 91
    • 0025139276 scopus 로고
    • The developmental expression of the cholinergic-specific antigen Chol-1 in the central and peripheral nervous system of the rat
    • Derrington E. A., Borroni E., The developmental expression of the cholinergic-specific antigen Chol-1 in the central and peripheral nervous system of the rat Developmental Brain Research 1990 52 1-2 131 140 (Pubitemid 20081070)
    • (1990) Developmental Brain Research , vol.52 , Issue.1-2 , pp. 131-140
    • Derrington, E.A.1    Borroni, E.2
  • 95
    • 67650735603 scopus 로고    scopus 로고
    • Effect of voluntary running on adult hippocampal neurogenesis in cholinergic lesioned mice
    • Ho N. F., Han S., Dawe G. S., Effect of voluntary running on adult hippocampal neurogenesis in cholinergic lesioned mice BMC Neuroscience 2009 10, article 57
    • (2009) BMC Neuroscience , vol.1057
    • Ho, N.F.1    Han, S.2    Dawe, G.S.3
  • 96
    • 33645882245 scopus 로고    scopus 로고
    • Neurodegeneration and neurogenesis: Focus on Alzheimer's disease
    • Greenberg D. A., Jin K., Neurodegeneration and neurogenesis: focus on Alzheimer's disease Current Alzheimer Research 2006 3 1 25 28
    • (2006) Current Alzheimer Research , vol.3 , Issue.1 , pp. 25-28
    • Greenberg, D.A.1    Jin, K.2
  • 102
    • 31944450386 scopus 로고    scopus 로고
    • Differences in regional brain atrophy in genetic forms of Alzheimer's disease
    • DOI 10.1016/j.neurobiolaging.2005.03.011, PII S0197458005001016
    • Gregory G. C., Macdonald V., Schofield P. R., Kril J. J., Halliday G. M., Differences in regional brain atrophy in genetic forms of Alzheimer's disease Neurobiology of Aging 2006 27 3 387 393 (Pubitemid 43186040)
    • (2006) Neurobiology of Aging , vol.27 , Issue.3 , pp. 387-393
    • Gregory, G.C.1    Macdonald, V.2    Schofield, P.R.3    Kril, J.J.4    Halliday, G.M.5
  • 103
    • 77953892400 scopus 로고    scopus 로고
    • Molecular mechanisms of neurodegeneration in Alzheimer's disease
    • Crews L., Masliah E., Molecular mechanisms of neurodegeneration in Alzheimer's disease Human Molecular Genetics 2010 19 1 R12 R20
    • (2010) Human Molecular Genetics , vol.19 , Issue.1
    • Crews, L.1    Masliah, E.2
  • 104
    • 39049157397 scopus 로고    scopus 로고
    • Therapeutic potential of adult neural stem cells
    • Taupin P., Therapeutic potential of adult neural stem cells Recent Patents on CNS Drug Discovery 2006 1 3 299 303
    • (2006) Recent Patents on CNS Drug Discovery , vol.1 , Issue.3 , pp. 299-303
    • Taupin, P.1
  • 105
    • 78649993950 scopus 로고    scopus 로고
    • Neurogenesis in the aged and neurodegenerative brain
    • Shruster A., Melamed E., Offen D., Neurogenesis in the aged and neurodegenerative brain Apoptosis 2010 15 11 1415 1421
    • (2010) Apoptosis , vol.15 , Issue.11 , pp. 1415-1421
    • Shruster, A.1    Melamed, E.2    Offen, D.3
  • 106
    • 77950461116 scopus 로고    scopus 로고
    • APP transgenic modeling of Alzheimer's disease: Mechanisms of neurodegeneration and aberrant neurogenesis
    • Crews L., Rockenstein E., Masliah E., APP transgenic modeling of Alzheimer's disease: mechanisms of neurodegeneration and aberrant neurogenesis Brain Structure and Function 2010 214 2-3 111 126
    • (2010) Brain Structure and Function , vol.214 , Issue.23 , pp. 111-126
    • Crews, L.1    Rockenstein, E.2    Masliah, E.3
  • 107
    • 33748790666 scopus 로고    scopus 로고
    • Increased proliferation reflects glial and vascular-associated changes, but not neurogenesis in the presenile Alzheimer hippocampus
    • DOI 10.1016/j.nbd.2006.04.017, PII S0969996106000957
    • Boekhoorn K., Joels M., Lucassen P. J., Increased proliferation reflects glial and vascular-associated changes, but not neurogenesis in the presenile Alzheimer hippocampus Neurobiology of Disease 2006 24 1 1 14 (Pubitemid 44416208)
    • (2006) Neurobiology of Disease , vol.24 , Issue.1 , pp. 1-14
    • Boekhoorn, K.1    Joels, M.2    Lucassen, P.J.3
  • 108
    • 32544460592 scopus 로고    scopus 로고
    • Decreased adult hippocampal neurogenesis in the PDAPP mouse model of Alzheimer's disease
    • DOI 10.1002/cne.20840
    • Donovan M. H., Yazdani U., Norris R. D., Games D., German D. C., Eisch A. J., Decreased adult hippocampal neurogenesis in the PDAPP mouse model of Alzheimer's disease Journal of Comparative Neurology 2006 495 1 70 83 (Pubitemid 43238052)
    • (2006) Journal of Comparative Neurology , vol.495 , Issue.1 , pp. 70-83
    • Donovan, M.H.1    Yazdani, U.2    Norris, R.D.3    Games, D.4    German, D.C.5    Eisch, A.J.6
  • 109
    • 0036358623 scopus 로고    scopus 로고
    • Disruption of neurogenesis in the subventricular zone of adult mice, and in human cortical neuronal precursor cells in culture, by amyloid β-peptide: Implications for the pathogenesis of Alzheimer's disease
    • DOI 10.1385/NMM:1:2:125
    • Haughey N. J., Liu D., Nath A., Borchard A. C., Mattson M. P., Disruption of neurogenesis in the subventricular zone of adult mice, and in human cortical neuronal precursor cells in culture, by amyloid -peptide: implications for the pathogenesis of Alzheimer's disease NeuroMolecular Medicine 2002 1 2 125 135 (Pubitemid 37012521)
    • (2002) NeuroMolecular Medicine , vol.1 , Issue.2 , pp. 125-135
    • Haughey, N.J.1    Liu, D.2    Nath, A.3    Borchard, A.C.4    Mattson, M.P.5
  • 110
    • 0042362874 scopus 로고    scopus 로고
    • Disruption of neurogenesis by amyloid β-peptide, and perturbed neural progenitor cell homeostasis, in models of Alzheimer's disease
    • DOI 10.1046/j.1471-4159.2002.01267.x
    • Haughey N. J., Nath A., Chan S. L., Borchard A. C., Rao M. S., Mattson M. P., Disruption of neurogenesis by amyloid -peptide, and perturbed neural progenitor cell homeostasis, in models of Alzheimer's disease Journal of Neurochemistry 2002 83 6 1509 1524 (Pubitemid 35477489)
    • (2002) Journal of Neurochemistry , vol.83 , Issue.6 , pp. 1509-1524
    • Haughey, N.J.1    Nath, A.2    Chan, S.L.3    Borchard, A.C.4    Rao, M.S.5    Mattson, M.P.6
  • 112
    • 33847258237 scopus 로고    scopus 로고
    • Long-lasting impairment in hippocampal neurogenesis associated with amyloid deposition in a knock-in mouse model of familial Alzheimer's disease
    • DOI 10.1016/j.expneurol.2006.09.018, PII S0014488606005565
    • Zhang C., McNeil E., Dressler L., Siman R., Long-lasting impairment in hippocampal neurogenesis associated with amyloid deposition in a knock-in mouse model of familial Alzheimer's disease Experimental Neurology 2007 204 1 77 87 (Pubitemid 46330258)
    • (2007) Experimental Neurology , vol.204 , Issue.1 , pp. 77-87
    • Zhang, C.1    McNeil, E.2    Dressler, L.3    Siman, R.4
  • 113
    • 71249160061 scopus 로고    scopus 로고
    • O-linked -N-acetylglucosaminylation in mouse embryonic neural precursor cells
    • Yanagisawa M., Yu R. K., O-linked -N-acetylglucosaminylation in mouse embryonic neural precursor cells Journal of Neuroscience Research 2009 87 16 3535 3545
    • (2009) Journal of Neuroscience Research , vol.87 , Issue.16 , pp. 3535-3545
    • Yanagisawa, M.1    Yu, R.K.2
  • 114
    • 26644433655 scopus 로고    scopus 로고
    • Glycosphingolipid synthesis inhibitor represses cytokine-induced activation of the Ras-MAPK pathway in embryonic neural precursor cells
    • DOI 10.1093/jb/mvi129
    • Yanagisawa M., Nakamura K., Taga T., Glycosphingolipid synthesis inhibitor represses cytokine-induced activation of the Ras-MAPK pathway in embryonic neural precursor cells Journal of Biochemistry 2005 138 3 285 291 (Pubitemid 41441960)
    • (2005) Journal of Biochemistry , vol.138 , Issue.3 , pp. 285-291
    • Yanagisawa, M.1    Nakamura, K.2    Taga, T.3
  • 115
    • 60849095497 scopus 로고    scopus 로고
    • A 40 promotes neuronal cell fate in neural progenitor cells
    • Chen Y., Dong C., A 40 promotes neuronal cell fate in neural progenitor cells Cell Death and Differentiation 2009 16 3 386 394
    • (2009) Cell Death and Differentiation , vol.16 , Issue.3 , pp. 386-394
    • Chen, Y.1    Dong, C.2
  • 116
    • 1842555337 scopus 로고    scopus 로고
    • Alzheimer's amyloid-beta (Aβ) is an essential synaptic protein, not neurotoxic junk
    • Koudinov A. R., Berezov T. T., Alzheimer's amyloid-beta (A ) is an essential synaptic protein, not neurotoxic junk Acta Neurobiologiae Experimentalis 2004 64 1 71 79 (Pubitemid 38453807)
    • (2004) Acta Neurobiologiae Experimentalis , vol.64 , Issue.1 , pp. 71-79
    • Koudinov, A.R.1    Berezov, T.T.2
  • 117
    • 2942530513 scopus 로고    scopus 로고
    • Neurogenic effect of β-amyloid peptide in the development of neural stem cells
    • DOI 10.1523/JNEUROSCI.0974-04.2004
    • Lpez-Toledano M. A., Shelanski M. L., Neurogenic effect of -amyloid peptide in the development of neural stem cells Journal of Neuroscience 2004 24 23 5439 5444 (Pubitemid 38747685)
    • (2004) Journal of Neuroscience , vol.24 , Issue.23 , pp. 5439-5444
    • Lopez-Toledano, M.A.1    Shelanski, M.L.2
  • 118
    • 33344460074 scopus 로고    scopus 로고
    • Progenitor cells from the adult mouse brain acquire a neuronal phenotype in response to β-amyloid
    • DOI 10.1016/j.neurobiolaging.2005.03.019, PII S0197458005001089, Protein Misfolding in Alzheimer's and Other Age-Related Neurodegenerative Diseases
    • Calafiore M., Battaglia G., Zappal A., Trovato-Salinaro E., Caraci F., Caruso M., Vancheri C., Sortino M. A., Nicoletti F., Copani A., Progenitor cells from the adult mouse brain acquire a neuronal phenotype in response to -amyloid Neurobiology of Aging 2006 27 4 606 613 (Pubitemid 43290529)
    • (2006) Neurobiology of Aging , vol.27 , Issue.4 , pp. 606-613
    • Calafiore, M.1    Battaglia, G.2    Zappala, A.3    Trovato-Salinaro, E.4    Caraci, F.5    Caruso, M.6    Vancheri, C.7    Sortino, M.A.8    Nicoletti, F.9    Copani, A.10
  • 119
    • 70349876742 scopus 로고    scopus 로고
    • A 1-42 stimulates adult SVZ neurogenesis through the p75 neurotrophin receptor
    • Sotthibundhu A., Li Q.-X., Thangnipon W., Coulson E. J., A 1-42 stimulates adult SVZ neurogenesis through the p75 neurotrophin receptor Neurobiology of Aging 2009 30 12 1975 1985
    • (2009) Neurobiology of Aging , vol.30 , Issue.12 , pp. 1975-1985
    • Sotthibundhu, A.1    Li, Q.-X.2    Thangnipon, W.3    Coulson, E.J.4
  • 124
    • 34347220924 scopus 로고    scopus 로고
    • 42 peptides on the proliferation and differentiation of adult neural stem cells from subventricular zone
    • DOI 10.1111/j.1471-4159.2007.04499.x
    • Heo C., Chang K.-A., Choi H. S., Kim H.-S., Kim S., Liew H., Kim J. A., Yu E., Ma J., Suh Y.-H., Effects of the monomeric, oligomeric, and fibrillar A 42 peptides on the proliferation and differentiation of adult neural stem cells from subventricular zone Journal of Neurochemistry 2007 102 2 493 500 (Pubitemid 47000592)
    • (2007) Journal of Neurochemistry , vol.102 , Issue.2 , pp. 493-500
    • Heo, C.1    Chang, K.-A.2    Choi, H.S.3    Kim, H.-S.4    Kim, S.5    Liew, H.6    Kim, J.A.7    Yu, E.8    Ma, J.9    Suh, Y.-H.10
  • 125
    • 0347122965 scopus 로고    scopus 로고
    • Amyloid-β peptide induces oligodendrocyte death by activating the neutral sphingomyelinase-ceramide pathway
    • DOI 10.1083/jcb.200307017
    • Lee J. T., Xu J., Lee J. M., Ku G., Han X., Yang D. I., Chen S., Hsu C. Y., Amyloid- peptide induces oligodendrocyte death by activating the neutral sphingomyelinase-ceramide pathway Journal of Cell Biology 2004 164 1 123 131 (Pubitemid 38082463)
    • (2004) Journal of Cell Biology , vol.164 , Issue.1 , pp. 123-131
    • Lee, J.-T.1    Xu, J.2    Lee, J.-M.3    Ku, G.4    Han, X.5    Yang, D.-I.6    Chen, S.7    Hsu, C.Y.8
  • 126
    • 17444413787 scopus 로고    scopus 로고
    • Amyloid-β peptide triggers Fas-independent apoptosis and differentiation of neural progenitor cells
    • DOI 10.1016/j.nbd.2004.11.006
    • Millet P., Silva Lages C., Hak S., Nowak E., Allemand I., Granotier C., Boussin F. D., Amyloid- peptide triggers Fas-independent apoptosis and differentiation of neural progenitor cells Neurobiology of Disease 2005 19 1-2 57 65 (Pubitemid 40544723)
    • (2005) Neurobiology of Disease , vol.19 , Issue.1-2 , pp. 57-65
    • Millet, P.1    Silva Lages, C.2    Haik, S.3    Nowak, E.4    Allemand, I.5    Granotier, C.6    Boussin, F.D.7
  • 127
    • 15244342663 scopus 로고    scopus 로고
    • 25-35 on neurogenesis in the adult mouse subventricular zone and dentate gyrus
    • DOI 10.1179/016164105X35585
    • Li X., Zuo P., Effects of A on neurogenesis in the adult mouse subventricular zone and dentate gyrus Neurological Research 2005 27 2 218 222 (Pubitemid 40388429)
    • (2005) Neurological Research , vol.27 , Issue.2 , pp. 218-222
    • Li, X.1    Zuo, P.2
  • 130
    • 77953372048 scopus 로고    scopus 로고
    • Cytotoxic effects of GM1 ganglioside and amyloid -peptide on mouse embryonic neural stem cells
    • Yanagisawa M., Ariga T., Yu R. K., Cytotoxic effects of GM1 ganglioside and amyloid -peptide on mouse embryonic neural stem cells ASN Neuro 2010 2 1 49 56
    • (2010) ASN Neuro , vol.2 , Issue.1 , pp. 49-56
    • Yanagisawa, M.1    Ariga, T.2    Yu, R.K.3
  • 131
    • 0030887669 scopus 로고    scopus 로고
    • Gangliosides inhibit growth factor-stimulated neurite outgrowth in SH- SY5Y human neuroblastoma cells
    • DOI 10.1002/(SICI)1097-4547(19970315)47:6<617::AID-JNR7>3.0.CO;2-G
    • Hynds D. L., Burry R. W., Yates A. J., Gangliosides inhibit growth factor-stimulated neurite outgrowth in SH-SY5Y human neuroblastoma cells Journal of Neuroscience Research 1997 47 6 617 625 (Pubitemid 27138744)
    • (1997) Journal of Neuroscience Research , vol.47 , Issue.6 , pp. 617-625
    • Hynds, D.L.1    Burry, R.W.2    Yates, A.J.3
  • 132
    • 0021178727 scopus 로고
    • 1 effects on neuronal repair
    • Leon A., Benvegnu D., Dal Toso R., Dorsal root ganglia and nerve growth factor: a model for understanding the mechanism of GM1 effects on neuronal repair Journal of Neuroscience Research 1984 12 2-3 277 287 (Pubitemid 14023220)
    • (1984) Journal of Neuroscience Research , vol.12 , Issue.2-3 , pp. 277-287
    • Leon, A.1    Benvegnu, D.2    Dal Toso, R.3
  • 134
    • 0023737884 scopus 로고
    • A novel, carbohydrate signal-mediated cell surface protein phosphorylation: Ganglioside GQ1b stimulates ecto-protein kinase activity on the cell surface of a human neuroblastoma cell line, GOTO
    • Tsuji S., Yamashita T., Nagai Y., A novel, carbohydrate signal-mediated cell surface protein phosphorylation: ganglioside GQ1b stimulates ecto-protein kinase activity on the cell surface of a human neuroblastoma cell line, GOTO Journal of Biochemistry 1988 104 4 498 503
    • (1988) Journal of Biochemistry , vol.104 , Issue.4 , pp. 498-503
    • Tsuji, S.1    Yamashita, T.2    Nagai, Y.3
  • 135
    • 0035049961 scopus 로고    scopus 로고
    • Co-expression of multiple transgenes in mouse CNS: A comparison of strategies
    • DOI 10.1016/S1389-0344(01)00067-3, PII S1389034401000673
    • Jankowsky J. L., Slunt H. H., Ratovitski T., Jenkins N. A., Copeland N. G., Borchelt D. R., Co-expression of multiple transgenes in mouse CNS: a comparison of strategies Biomolecular Engineering 2001 17 6 157 165 (Pubitemid 32409891)
    • (2001) Biomolecular Engineering , vol.17 , Issue.6 , pp. 157-165
    • Jankowsky, J.L.1    Slunt, H.H.2    Ratovitski, T.3    Jenkins, N.A.4    Copeland, N.G.5    Borchelt, D.R.6


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