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Volumn 16, Issue 1, 2015, Pages

Neuronal response in Alzheimer's and Parkinson's disease: The effect of toxic proteins on intracellular pathways

Author keywords

Alpha synuclein; Alzheimer's disease; Beta amyloid; Intracellular signalling; Neurodegeneration; Neurotoxicity; Parkinson's disease

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; APOLIPOPROTEIN E; GLYCOGEN SYNTHASE KINASE 3BETA; MITOGEN ACTIVATED PROTEIN KINASE;

EID: 84944890971     PISSN: None     EISSN: 14712202     Source Type: Journal    
DOI: 10.1186/s12868-015-0211-1     Document Type: Review
Times cited : (62)

References (211)
  • 1
    • 0141861067 scopus 로고    scopus 로고
    • Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go?
    • Uversky VN. Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go? Cell Mol Life Sci. 2003;60(9):1852-71.
    • (2003) Cell Mol Life Sci , vol.60 , Issue.9 , pp. 1852-1871
    • Uversky, V.N.1
  • 2
    • 84888406392 scopus 로고    scopus 로고
    • Protein folding and aggregation into amyloid: the interference by natural phenolic compounds
    • Stefani M, Rigacci S. Protein folding and aggregation into amyloid: the interference by natural phenolic compounds. Int J Mol Sci. 2013;14(6):12411-57.
    • (2013) Int J Mol Sci , vol.14 , Issue.6 , pp. 12411-12457
    • Stefani, M.1    Rigacci, S.2
  • 3
    • 0031761706 scopus 로고    scopus 로고
    • Protein precipitation: a common etiology in neuro-degenerative disorders?
    • Kakizuka A. Protein precipitation: a common etiology in neuro-degenerative disorders? Trends Genet. 1998;14(10):396-402.
    • (1998) Trends Genet , vol.14 , Issue.10 , pp. 396-402
    • Kakizuka, A.1
  • 4
    • 0033773935 scopus 로고    scopus 로고
    • Conformational disease
    • Kopito RR, Ron D. Conformational disease. Nat Cell Biol. 2000;2(11):E207-9.
    • (2000) Nat Cell Biol , vol.2 , Issue.11 , pp. E207-E209
    • Kopito, R.R.1    Ron, D.2
  • 7
    • 79959366068 scopus 로고    scopus 로고
    • Prions and protein-folding diseases
    • Norrby E. Prions and protein-folding diseases. J Intern Med. 2011;270(1):1-14.
    • (2011) J Intern Med , vol.270 , Issue.1 , pp. 1-14
    • Norrby, E.1
  • 8
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world
    • Stefani M. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim Biophys Acta. 2004;1739(1):5-25.
    • (2004) Biochim Biophys Acta , vol.1739 , Issue.1 , pp. 5-25
    • Stefani, M.1
  • 9
    • 38549169530 scopus 로고    scopus 로고
    • The two faces of protein misfolding: gain- and loss-of-function in neurodegenerative diseases
    • Winklhofer KF, Tatzelt J, Haass C. The two faces of protein misfolding: gain- and loss-of-function in neurodegenerative diseases. EMBO J. 2008;27(2):336-49.
    • (2008) EMBO J , vol.27 , Issue.2 , pp. 336-349
    • Winklhofer, K.F.1    Tatzelt, J.2    Haass, C.3
  • 10
    • 84856873078 scopus 로고    scopus 로고
    • Hydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid beta self-assembly
    • Abelein A, Bolognesi B, Dobson CM, Graslund A, Lendel C. Hydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid beta self-assembly. Biochemistry. 2012;51(1):126-37.
    • (2012) Biochemistry , vol.51 , Issue.1 , pp. 126-137
    • Abelein, A.1    Bolognesi, B.2    Dobson, C.M.3    Graslund, A.4    Lendel, C.5
  • 12
    • 0034516988 scopus 로고    scopus 로고
    • Toward a comprehensive theory for Alzheimer's disease. Hypothesis: Alzheimer's disease is caused by the cerebral accumulation and cytotoxicity of amyloid beta-protein
    • Selkoe DJ. Toward a comprehensive theory for Alzheimer's disease. Hypothesis: Alzheimer's disease is caused by the cerebral accumulation and cytotoxicity of amyloid beta-protein. Ann N Y Acad Sci. 2000;924:17-25.
    • (2000) Ann N Y Acad Sci , vol.924 , pp. 17-25
    • Selkoe, D.J.1
  • 13
    • 84886703257 scopus 로고    scopus 로고
    • Early intraneuronal accumulation and increased aggregation of phosphorylated Abeta in a mouse model of Alzheimer's disease
    • Kumar S, Wirths O, Theil S, Gerth J, Bayer TA, Walter J. Early intraneuronal accumulation and increased aggregation of phosphorylated Abeta in a mouse model of Alzheimer's disease. Acta Neuropathol. 2013;125(5):699-709.
    • (2013) Acta Neuropathol , vol.125 , Issue.5 , pp. 699-709
    • Kumar, S.1    Wirths, O.2    Theil, S.3    Gerth, J.4    Bayer, T.A.5    Walter, J.6
  • 14
    • 0344431341 scopus 로고    scopus 로고
    • Structural neurology: are seeds at the root of neuronal degeneration?
    • Lansbury PT Jr. Structural neurology: are seeds at the root of neuronal degeneration? Neuron. 1997;19(6):1151-4.
    • (1997) Neuron , vol.19 , Issue.6 , pp. 1151-1154
    • Lansbury, P.T.1
  • 15
    • 33749521100 scopus 로고    scopus 로고
    • Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation
    • Oakley H, Cole SL, Logan S, Maus E, Shao P, Craft J, Guillozet-Bongaarts A, Ohno M, Disterhoft J, Van Eldik L, et al. Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: potential factors in amyloid plaque formation. J Neurosci. 2006;26(40):10129-40.
    • (2006) J Neurosci , vol.26 , Issue.40 , pp. 10129-10140
    • Oakley, H.1    Cole, S.L.2    Logan, S.3    Maus, E.4    Shao, P.5    Craft, J.6    Guillozet-Bongaarts, A.7    Ohno, M.8    Disterhoft, J.9    Eldik, L.10
  • 16
    • 0032902647 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease and the Abeta peptide
    • Storey E, Cappai R. The amyloid precursor protein of Alzheimer's disease and the Abeta peptide. Neuropathol Appl Neurobiol. 1999;25(2):81-97.
    • (1999) Neuropathol Appl Neurobiol , vol.25 , Issue.2 , pp. 81-97
    • Storey, E.1    Cappai, R.2
  • 17
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of APP cleavage by alpha-, beta- and gamma- secretases
    • Nunan J, Small DH. Regulation of APP cleavage by alpha-, beta- and gamma- secretases. FEBS Lett. 2000;483(1):6-10.
    • (2000) FEBS Lett , vol.483 , Issue.1 , pp. 6-10
    • Nunan, J.1    Small, D.H.2
  • 18
    • 1442306058 scopus 로고    scopus 로고
    • Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage
    • Ho A, Sudhof TC. Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage. Proc Natl Acad Sci USA. 2004;101(8):2548-53.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.8 , pp. 2548-2553
    • Ho, A.1    Sudhof, T.C.2
  • 20
    • 0033636136 scopus 로고    scopus 로고
    • Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I
    • Kamal A, Stokin GB, Yang Z, Xia CH, Goldstein LS. Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I. Neuron. 2000;28(2):449-59.
    • (2000) Neuron , vol.28 , Issue.2 , pp. 449-459
    • Kamal, A.1    Stokin, G.B.2    Yang, Z.3    Xia, C.H.4    Goldstein, L.S.5
  • 22
    • 40849097929 scopus 로고    scopus 로고
    • Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons
    • Schneider A, Rajendran L, Honsho M, Gralle M, Donnert G, Wouters F, Hell SW, Simons M. Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons. J Neurosci. 2008;28(11):2874-82.
    • (2008) J Neurosci , vol.28 , Issue.11 , pp. 2874-2882
    • Schneider, A.1    Rajendran, L.2    Honsho, M.3    Gralle, M.4    Donnert, G.5    Wouters, F.6    Hell, S.W.7    Simons, M.8
  • 24
    • 84991569148 scopus 로고    scopus 로고
    • Dysregulation of protein trafficking in neurodegeneration
    • Wang X, Huang T, Bu G, Xu H. Dysregulation of protein trafficking in neurodegeneration. Mol Neurodegenr. 2014;9(31):1-9.
    • (2014) Mol Neurodegenr. , vol.9 , Issue.31 , pp. 1-9
    • Wang, X.1    Huang, T.2    Bu, G.3    Xu, H.4
  • 25
    • 80053209344 scopus 로고    scopus 로고
    • Interactions of pathological hallmark proteins: tubulin polymerization promoting protein/p25, beta-amyloid, and alpha-synuclein
    • Olah J, Vincze O, Virok D, Simon D, Bozso Z, Tokesi N, Horvath I, Hlavanda E, Kovacs J, Magyar A, et al. Interactions of pathological hallmark proteins: tubulin polymerization promoting protein/p25, beta-amyloid, and alpha-synuclein. J Biol Chem. 2011;286(39):34088-100.
    • (2011) J Biol Chem , vol.286 , Issue.39 , pp. 34088-34100
    • Olah, J.1    Vincze, O.2    Virok, D.3    Simon, D.4    Bozso, Z.5    Tokesi, N.6    Horvath, I.7    Hlavanda, E.8    Kovacs, J.9    Magyar, A.10
  • 26
    • 0034333041 scopus 로고    scopus 로고
    • In search of an enzyme: the beta-secretase of Alzheimer's disease is an aspartic proteinase
    • Howlett DR, Simmons DL, Dingwall C, Christie G. In search of an enzyme: the beta-secretase of Alzheimer's disease is an aspartic proteinase. Trends Neurosci. 2000;23(11):565-70.
    • (2000) Trends Neurosci , vol.23 , Issue.11 , pp. 565-570
    • Howlett, D.R.1    Simmons, D.L.2    Dingwall, C.3    Christie, G.4
  • 27
    • 70350451482 scopus 로고    scopus 로고
    • gamma-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment
    • Takami M, Nagashima Y, Sano Y, Ishihara S, Morishima-Kawashima M, Funamoto S, Ihara Y. gamma-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment. J Neurosci. 2009;29(41):13042-52.
    • (2009) J Neurosci , vol.29 , Issue.41 , pp. 13042-13052
    • Takami, M.1    Nagashima, Y.2    Sano, Y.3    Ishihara, S.4    Morishima-Kawashima, M.5    Funamoto, S.6    Ihara, Y.7
  • 28
    • 24144451760 scopus 로고    scopus 로고
    • Familial Alzheimer's disease mutations inhibit gamma-secretase-mediated liberation of beta-amyloid precursor protein carboxy-terminal fragment
    • Wiley JC, Hudson M, Kanning KC, Schecterson LC, Bothwell M. Familial Alzheimer's disease mutations inhibit gamma-secretase-mediated liberation of beta-amyloid precursor protein carboxy-terminal fragment. J Neurochem. 2005;94(5):1189-201.
    • (2005) J Neurochem , vol.94 , Issue.5 , pp. 1189-1201
    • Wiley, J.C.1    Hudson, M.2    Kanning, K.C.3    Schecterson, L.C.4    Bothwell, M.5
  • 29
    • 0028983336 scopus 로고
    • Amyloid beta-protein induces its own production in cultured degenerating cerebrovascular smooth muscle cells
    • Davis-Salinas J, Saporito-Irwin SM, Cotman CW, Van Nostrand WE. Amyloid beta-protein induces its own production in cultured degenerating cerebrovascular smooth muscle cells. J Neurochem. 1995;65(2):931-4.
    • (1995) J Neurochem , vol.65 , Issue.2 , pp. 931-934
    • Davis-Salinas, J.1    Saporito-Irwin, S.M.2    Cotman, C.W.3    Nostrand, W.E.4
  • 30
    • 36448953934 scopus 로고    scopus 로고
    • Fibrillar beta-amyloid (Abeta) (1-42) elevates extracellular Abeta in cultured hippocampal neurons of adult rats
    • Majd S, Rastegar K, Zarifkar A, Takhshid MA. Fibrillar beta-amyloid (Abeta) (1-42) elevates extracellular Abeta in cultured hippocampal neurons of adult rats. Brain Res. 2007;1185:321-7.
    • (2007) Brain Res , vol.1185 , pp. 321-327
    • Majd, S.1    Rastegar, K.2    Zarifkar, A.3    Takhshid, M.A.4
  • 31
    • 4644276796 scopus 로고    scopus 로고
    • Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Abeta42 accumulation in a novel Alzheimer transgenic model
    • Casas C, Sergeant N, Itier JM, Blanchard V, Wirths O, van der Kolk N, Vingtdeux V, van de Steeg E, Ret G, Canton T, et al. Massive CA1/2 neuronal loss with intraneuronal and N-terminal truncated Abeta42 accumulation in a novel Alzheimer transgenic model. Am J Pathol. 2004;165(4):1289-300.
    • (2004) Am J Pathol , vol.165 , Issue.4 , pp. 1289-1300
    • Casas, C.1    Sergeant, N.2    Itier, J.M.3    Blanchard, V.4    Wirths, O.5    Kolk, N.6    Vingtdeux, V.7    Steeg, E.8    Ret, G.9    Canton, T.10
  • 32
    • 84904975199 scopus 로고    scopus 로고
    • Serum levels of albumin-amyloid beta complexes are decreased in Alzheimer's disease
    • Yamamoto K, Shimada H, Koh H, Ataka S, Miki T. Serum levels of albumin-amyloid beta complexes are decreased in Alzheimer's disease. Geriatr Gerontol Int. 2014;14(3):716-23.
    • (2014) Geriatr Gerontol Int , vol.14 , Issue.3 , pp. 716-723
    • Yamamoto, K.1    Shimada, H.2    Koh, H.3    Ataka, S.4    Miki, T.5
  • 33
    • 0031825554 scopus 로고    scopus 로고
    • From the globular to the fibrous state: protein structure and structural conversion in amyloid formation
    • Sunde M, Blake CC. From the globular to the fibrous state: protein structure and structural conversion in amyloid formation. Q Rev Biophys. 1998;31:1-39.
    • (1998) Q Rev Biophys , vol.31 , pp. 1-39
    • Sunde, M.1    Blake, C.C.2
  • 35
    • 0037465708 scopus 로고    scopus 로고
    • Insights into the amyloid folding problem from solid-state NMR
    • Tycko R. Insights into the amyloid folding problem from solid-state NMR. Biochemistry. 2003;42:3151-9.
    • (2003) Biochemistry , vol.42 , pp. 3151-3159
    • Tycko, R.1
  • 36
    • 0037174998 scopus 로고    scopus 로고
    • Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling
    • Torok M, Milton S, Kayed R, Wu P, McIntire T, Glabe CG, Langen R. Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling. J Biol Chem. 2002;277:40810-5.
    • (2002) J Biol Chem , vol.277 , pp. 40810-40815
    • Torok, M.1    Milton, S.2    Kayed, R.3    Wu, P.4    McIntire, T.5    Glabe, C.G.6    Langen, R.7
  • 37
    • 34547152918 scopus 로고    scopus 로고
    • Role of gangliosides in Alzheimer's disease
    • Yanagisawa K. Role of gangliosides in Alzheimer's disease. Biochim Biophys Acta. 2002;1768:1943-51.
    • (2002) Biochim Biophys Acta , vol.1768 , pp. 1943-1951
    • Yanagisawa, K.1
  • 38
    • 34249672242 scopus 로고    scopus 로고
    • Abeta oligomers induce neuronal oxidative stress through an N-methyl-d-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice FG, Velasco PT, Lambert MP, Viola K, Fernandez SJ, Ferreira ST, Klein WL. Abeta oligomers induce neuronal oxidative stress through an N-methyl-d-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem. 2002;282:11590-601.
    • (2002) J Biol Chem , vol.282 , pp. 11590-11601
    • Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5    Ferreira, S.T.6    Klein, W.L.7
  • 39
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • Laferla FM, Green KN, Oddo S. Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci. 2007;8:499-509.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • Laferla, F.M.1    Green, K.N.2    Oddo, S.3
  • 40
    • 33646461282 scopus 로고    scopus 로고
    • Beta-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system
    • Almeida CG, Takahashi RH, Gouras GK. Beta-amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J Neurosci. 2006;26:4277-88.
    • (2006) J Neurosci , vol.26 , pp. 4277-4288
    • Almeida, C.G.1    Takahashi, R.H.2    Gouras, G.K.3
  • 41
    • 0034966403 scopus 로고    scopus 로고
    • Closing in on the amyloid cascade: recent insights into the cell biology of Alzheimer's disease
    • Huse JT, Doms RW. Closing in on the amyloid cascade: recent insights into the cell biology of Alzheimer's disease. Mol Neurobiol. 2000;22(1-3):81-98.
    • (2000) Mol Neurobiol , vol.22 , Issue.1-3 , pp. 81-98
    • Huse, J.T.1    Doms, R.W.2
  • 43
    • 0027361386 scopus 로고
    • Human neurons derived from a teratocarcinoma cell line express solely the 695-amino acid amyloid precursor protein and produce intracellular beta- amyloid or A4 peptides
    • Wertkin AM, Turner RS, Pleasure SJ, Golde TE, Younkin SG, Trojanowski JQ, Lee VM. Human neurons derived from a teratocarcinoma cell line express solely the 695-amino acid amyloid precursor protein and produce intracellular beta- amyloid or A4 peptides. Proc Natl Acad Sci USA. 1993;90(20):9513-7.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.20 , pp. 9513-9517
    • Wertkin, A.M.1    Turner, R.S.2    Pleasure, S.J.3    Golde, T.E.4    Younkin, S.G.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 46
    • 34748897213 scopus 로고    scopus 로고
    • Amyloid precursor protein regulates brain apolipoprotein E and cholesterol metabolism through lipoprotein receptor LRP1
    • Liu Q, Zerbinatti CV, Zhang J, Hoe HS, Wang B, Cole SL, Herz J, Muglia L, Bu G. Amyloid precursor protein regulates brain apolipoprotein E and cholesterol metabolism through lipoprotein receptor LRP1. Neuron. 2007;56(1):66-78.
    • (2007) Neuron , vol.56 , Issue.1 , pp. 66-78
    • Liu, Q.1    Zerbinatti, C.V.2    Zhang, J.3    Hoe, H.S.4    Wang, B.5    Cole, S.L.6    Herz, J.7    Muglia, L.8    Bu, G.9
  • 47
    • 84866464632 scopus 로고    scopus 로고
    • LRP-1 and LRP-2 receptors function in the membrane neuron. Trafficking mechanisms and proteolytic processing in Alzheimer's disease
    • Spuch C, Ortolano S, Navarro C. LRP-1 and LRP-2 receptors function in the membrane neuron. Trafficking mechanisms and proteolytic processing in Alzheimer's disease. Front Physiol. 2012;3:269.
    • (2012) Front Physiol , vol.3 , pp. 269
    • Spuch, C.1    Ortolano, S.2    Navarro, C.3
  • 49
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's Abeta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Cook DG, Forman MS, Sung JC, Leight S, Kolson DL, Iwatsubo T, Lee VM, Doms RW. Alzheimer's Abeta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat Med. 1997;3(9):1021-3.
    • (1997) Nat Med , vol.3 , Issue.9 , pp. 1021-1023
    • Cook, D.G.1    Forman, M.S.2    Sung, J.C.3    Leight, S.4    Kolson, D.L.5    Iwatsubo, T.6    Lee, V.M.7    Doms, R.W.8
  • 51
    • 0031686460 scopus 로고    scopus 로고
    • Presenilin 1 mutations linked to familial Alzheimer's disease increase the intracellular levels of amyloid beta-protein 1-42 and its N-terminally truncated variant(s) which are generated at distinct sites
    • Sudoh S, Kawamura Y, Sato S, Wang R, Saido TC, Oyama F, Sakaki Y, Komano H, Yanagisawa K. Presenilin 1 mutations linked to familial Alzheimer's disease increase the intracellular levels of amyloid beta-protein 1-42 and its N-terminally truncated variant(s) which are generated at distinct sites. J Neurochem. 1998;71(4):1535-43.
    • (1998) J Neurochem , vol.71 , Issue.4 , pp. 1535-1543
    • Sudoh, S.1    Kawamura, Y.2    Sato, S.3    Wang, R.4    Saido, T.C.5    Oyama, F.6    Sakaki, Y.7    Komano, H.8    Yanagisawa, K.9
  • 52
    • 84938997554 scopus 로고    scopus 로고
    • Autophagy in neurodegenerative diseases: from mechanism to therapeutic approach
    • Nah J, Yuan J, Jung YK. Autophagy in neurodegenerative diseases: from mechanism to therapeutic approach. Mol Cells. 2015;38(5):381-9.
    • (2015) Mol Cells , vol.38 , Issue.5 , pp. 381-389
    • Nah, J.1    Yuan, J.2    Jung, Y.K.3
  • 54
    • 84858336588 scopus 로고    scopus 로고
    • Aβ-induced formation of autophagosomes is mediated by RAGECaMKK β-AMPK signaling
    • Son SM, Jung ES, Shin HJ, Byun J, Mook-Jung I. Aβ-induced formation of autophagosomes is mediated by RAGECaMKK β-AMPK signaling. Neurobiol Aging. 2012;33:1006.e11-23.
    • (2012) Neurobiol Aging , vol.33 , pp. 1006e11-1006e23
    • Son, S.M.1    Jung, E.S.2    Shin, H.J.3    Byun, J.4    Mook-Jung, I.5
  • 55
    • 0035203662 scopus 로고    scopus 로고
    • Key factors in Alzheimer's disease: beta-amyloid precursor protein processing, metabolism and intraneuronal transport
    • Bayer TA, Wirths O, Majtenyi K, Hartmann T, Multhaup G, Beyreuther K, Czech C. Key factors in Alzheimer's disease: beta-amyloid precursor protein processing, metabolism and intraneuronal transport. Brain Pathol. 2001;11(1):1-11.
    • (2001) Brain Pathol , vol.11 , Issue.1 , pp. 1-11
    • Bayer, T.A.1    Wirths, O.2    Majtenyi, K.3    Hartmann, T.4    Multhaup, G.5    Beyreuther, K.6    Czech, C.7
  • 58
    • 3042833662 scopus 로고    scopus 로고
    • Alzheimer's disease pathogenesis and therapeutic interventions
    • Parihar MS, Hemnani T. Alzheimer's disease pathogenesis and therapeutic interventions. J Clin Neurosci. 2004;11(5):456-67.
    • (2004) J Clin Neurosci , vol.11 , Issue.5 , pp. 456-467
    • Parihar, M.S.1    Hemnani, T.2
  • 60
    • 0442276554 scopus 로고    scopus 로고
    • The glamour and gloom of glycogen synthase kinase-3
    • Jope RS, Johnson GV. The glamour and gloom of glycogen synthase kinase-3. Trends Biochem Sci. 2004;29(2):95-102.
    • (2004) Trends Biochem Sci , vol.29 , Issue.2 , pp. 95-102
    • Jope, R.S.1    Johnson, G.V.2
  • 61
    • 39849110726 scopus 로고    scopus 로고
    • The GSK3 hypothesis of Alzheimer's disease
    • Hooper C, Killick R, Lovestone S. The GSK3 hypothesis of Alzheimer's disease. J Neurochem. 2008;104(6):1433-9.
    • (2008) J Neurochem , vol.104 , Issue.6 , pp. 1433-1439
    • Hooper, C.1    Killick, R.2    Lovestone, S.3
  • 63
    • 0032850599 scopus 로고    scopus 로고
    • Distribution of active glycogen synthase kinase 3beta (GSK-3beta) in brains staged for Alzheimer disease neurofibrillary changes
    • Pei JJ, Braak E, Braak H, Grundke-Iqbal I, Iqbal K, Winblad B, Cowburn RF. Distribution of active glycogen synthase kinase 3beta (GSK-3beta) in brains staged for Alzheimer disease neurofibrillary changes. J Neuropathol Exp Neurol. 1999;58(9):1010-9.
    • (1999) J Neuropathol Exp Neurol , vol.58 , Issue.9 , 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
  • 64
    • 0029737421 scopus 로고    scopus 로고
    • Preferential labeling of Alzheimer 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 CA, Imahori K. Preferential labeling of Alzheimer 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. 1996;92(3):232-41.
    • (1996) Acta Neuropathol , vol.92 , Issue.3 , pp. 232-241
    • Yamaguchi, H.1    Ishiguro, K.2    Uchida, T.3    Takashima, A.4    Lemere, C.A.5    Imahori, K.6
  • 66
    • 0034731461 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta phosphorylates protein tau and rescues the axonopathy in the central nervous system of human four-repeat tau transgenic mice
    • Spittaels K, Van den Haute C, Van Dorpe J, Geerts H, Mercken M, Bruynseels K, Lasrado R, Vandezande K, Laenen I, Boon T, et al. Glycogen synthase kinase-3beta phosphorylates protein tau and rescues the axonopathy in the central nervous system of human four-repeat tau transgenic mice. J Biol Chem. 2000;275(52):41340-9.
    • (2000) J Biol Chem , vol.275 , Issue.52 , pp. 41340-41349
    • Spittaels, K.1    Haute, C.2    Dorpe, J.3    Geerts, H.4    Mercken, M.5    Bruynseels, K.6    Lasrado, R.7    Vandezande, K.8    Laenen, I.9    Boon, T.10
  • 67
    • 0035863188 scopus 로고    scopus 로고
    • Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice
    • Lucas JJ, Hernandez F, Gomez-Ramos P, Moran MA, Hen R, Avila J. Decreased nuclear beta-catenin, tau hyperphosphorylation and neurodegeneration in GSK-3beta conditional transgenic mice. EMBO J. 2001;20(1-2):27-39.
    • (2001) EMBO J , vol.20 , Issue.1-2 , pp. 27-39
    • Lucas, J.J.1    Hernandez, F.2    Gomez-Ramos, P.3    Moran, M.A.4    Hen, R.5    Avila, J.6
  • 68
    • 1842452043 scopus 로고    scopus 로고
    • GSK-3beta reduces cAMP-induced cholecystokinin gene expression by inhibiting CREB binding
    • Hansen T, Rehfeld JF, Nielsen FC. GSK-3beta reduces cAMP-induced cholecystokinin gene expression by inhibiting CREB binding. NeuroReport. 2004;15(5):841-5.
    • (2004) NeuroReport , vol.15 , Issue.5 , pp. 841-845
    • Hansen, T.1    Rehfeld, J.F.2    Nielsen, F.C.3
  • 69
    • 33947597084 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 (GSK3): inflammation, diseases, and therapeutics
    • Jope RS, Yuskaitis CJ, Beurel E. Glycogen synthase kinase-3 (GSK3): inflammation, diseases, and therapeutics. Neurochem Res. 2007;32(4-5):577-95.
    • (2007) Neurochem Res , vol.32 , Issue.4-5 , pp. 577-595
    • Jope, R.S.1    Yuskaitis, C.J.2    Beurel, E.3
  • 70
    • 36348935683 scopus 로고    scopus 로고
    • Soluble Abeta inhibits specific signal transduction cascades common to the insulin receptor pathway
    • Townsend M, Mehta T, Selkoe DJ. Soluble Abeta inhibits specific signal transduction cascades common to the insulin receptor pathway. J Biol Chem. 2007;282(46):33305-12.
    • (2007) J Biol Chem , vol.282 , Issue.46 , pp. 33305-33312
    • Townsend, M.1    Mehta, T.2    Selkoe, D.J.3
  • 72
    • 84920505804 scopus 로고    scopus 로고
    • Blockage of GSK3β-mediated Drp1 phosphorylation provides neuroprotection in neuronal and mouse models of Alzheimer's disease
    • Yan J, Liu XH, Han MZ, Wang YM, Sun XL, Yu N, Li T, Su B, Chen ZY. Blockage of GSK3β-mediated Drp1 phosphorylation provides neuroprotection in neuronal and mouse models of Alzheimer's disease. Neurobiol Aging. 2015;36(1):211-27.
    • (2015) Neurobiol Aging. , vol.36 , Issue.1 , pp. 211-227
    • Yan, J.1    Liu, X.H.2    Han, M.Z.3    Wang, Y.M.4    Sun, X.L.5    Yu, N.6    Li, T.7    Su, B.8    Chen, Z.Y.9
  • 73
    • 0031045216 scopus 로고    scopus 로고
    • Physiology and pathology of tau protein kinases in relation to Alzheimer's disease
    • Imahori K, Uchida T. Physiology and pathology of tau protein kinases in relation to Alzheimer's disease. J Biochem. 1997;121(2):179-88.
    • (1997) J Biochem , vol.121 , Issue.2 , pp. 179-188
    • Imahori, K.1    Uchida, T.2
  • 74
    • 8444233219 scopus 로고    scopus 로고
    • Altered mitogen-activated protein kinase signaling, tau hyperphosphorylation and mild spatial learning dysfunction in transgenic rats expressing the beta-amyloid peptide intracellularly in hippocampal and cortical neurons
    • Echeverria V, Ducatenzeiler A, Dowd E, Janne J, Grant SM, Szyf M, Wandosell F, Avila J, Grimm H, Dunnett SB, et al. Altered mitogen-activated protein kinase signaling, tau hyperphosphorylation and mild spatial learning dysfunction in transgenic rats expressing the beta-amyloid peptide intracellularly in hippocampal and cortical neurons. Neuroscience. 2004;129(3):583-92.
    • (2004) Neuroscience , vol.129 , Issue.3 , pp. 583-592
    • Echeverria, V.1    Ducatenzeiler, A.2    Dowd, E.3    Janne, J.4    Grant, S.M.5    Szyf, M.6    Wandosell, F.7    Avila, J.8    Grimm, H.9    Dunnett, S.B.10
  • 76
    • 0027284385 scopus 로고
    • Localization of the mitogen activated protein kinase ERK2 in Alzheimer's disease neurofibrillary tangles and senile plaque neurites
    • Trojanowski JQ, Mawal-Dewan M, Schmidt ML, Martin J, Lee VM. Localization of the mitogen activated protein kinase ERK2 in Alzheimer's disease neurofibrillary tangles and senile plaque neurites. Brain Res. 1993;618(2):333-7.
    • (1993) Brain Res , vol.618 , Issue.2 , pp. 333-337
    • Trojanowski, J.Q.1    Mawal-Dewan, M.2    Schmidt, M.L.3    Martin, J.4    Lee, V.M.5
  • 77
    • 12244279939 scopus 로고    scopus 로고
    • Up- regulation of mitogen-activated protein kinases ERK1/2 and MEK1/2 is associated with the progression of neurofibrillary degeneration in Alzheimer's disease
    • Pei JJ, Braak H, An WL, Winblad B, Cowburn RF, Iqbal K, Grundke-Iqbal I. Up- regulation of mitogen-activated protein kinases ERK1/2 and MEK1/2 is associated with the progression of neurofibrillary degeneration in Alzheimer's disease. Brain Res Mol Brain Res. 2002;109(1-2):45-55.
    • (2002) Brain Res Mol Brain Res , vol.109 , Issue.1-2 , pp. 45-55
    • Pei, J.J.1    Braak, H.2    An, W.L.3    Winblad, B.4    Cowburn, R.F.5    Iqbal, K.6    Grundke-Iqbal, I.7
  • 78
    • 0035021950 scopus 로고    scopus 로고
    • ERK induces p35, a neuron-specific activator of Cdk5, through induction of Egr1
    • Harada T, Morooka T, Ogawa S, Nishida E. ERK induces p35, a neuron-specific activator of Cdk5, through induction of Egr1. Nat Cell Biol. 2001;3(5):453-9.
    • (2001) Nat Cell Biol , vol.3 , Issue.5 , pp. 453-459
    • Harada, T.1    Morooka, T.2    Ogawa, S.3    Nishida, E.4
  • 79
    • 2942530310 scopus 로고    scopus 로고
    • ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions
    • Roux PP, Blenis J. ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions. Microbiol Mol Biol Rev. 2004;68(2):320-44.
    • (2004) Microbiol Mol Biol Rev , vol.68 , Issue.2 , pp. 320-344
    • Roux, P.P.1    Blenis, J.2
  • 80
    • 11144356304 scopus 로고    scopus 로고
    • S6K1(-/-)/S6K2(-/-) mice exhibit perinatal lethality and rapamycin-sensitive 5'-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent S6 kinase pathway
    • Pende M, Um SH, Mieulet V, Sticker M, Goss VL, Mestan J, Mueller M, Fumagalli S, Kozma SC, Thomas G. S6K1(-/-)/S6K2(-/-) mice exhibit perinatal lethality and rapamycin-sensitive 5'-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent S6 kinase pathway. Mol Cell Biol. 2004;24(8):3112-24.
    • (2004) Mol Cell Biol , vol.24 , Issue.8 , pp. 3112-3124
    • Pende, M.1    Um, S.H.2    Mieulet, V.3    Sticker, M.4    Goss, V.L.5    Mestan, J.6    Mueller, M.7    Fumagalli, S.8    Kozma, S.C.9    Thomas, G.10
  • 81
    • 0035668350 scopus 로고    scopus 로고
    • Active, phosphorylation-dependent mitogen-activated protein kinase (MAPK/ERK), stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK), and p38 kinase expression in Parkinson's disease and Dementia with Lewy bodies
    • Ferrer I, Blanco R, Carmona M, Puig B, Barrachina M, Gomez C, Ambrosio S. Active, phosphorylation-dependent mitogen-activated protein kinase (MAPK/ERK), stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK), and p38 kinase expression in Parkinson's disease and Dementia with Lewy bodies. J Neural Transm. 2001;108(12):1383-96.
    • (2001) J Neural Transm , vol.108 , Issue.12 , pp. 1383-1396
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3    Puig, B.4    Barrachina, M.5    Gomez, C.6    Ambrosio, S.7
  • 82
    • 0035659377 scopus 로고    scopus 로고
    • Phosphorylated mitogen-activated protein kinase (MAPK/ERK-P), protein kinase of 38 kDa (p38-P), stress- activated protein kinase (SAPK/JNK-P), and calcium/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies
    • Ferrer I, Blanco R, Carmona M, Puig B. Phosphorylated mitogen-activated protein kinase (MAPK/ERK-P), protein kinase of 38 kDa (p38-P), stress- activated protein kinase (SAPK/JNK-P), and calcium/calmodulin-dependent kinase II (CaM kinase II) are differentially expressed in tau deposits in neurons and glial cells in tauopathies. J Neural Transm. 2001;108(12):1397-415.
    • (2001) J Neural Transm , vol.108 , Issue.12 , pp. 1397-1415
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3    Puig, B.4
  • 83
    • 10944273982 scopus 로고    scopus 로고
    • Phosphorylated tau and the neurodegenerative foldopathies
    • Kosik KS, Shimura H. Phosphorylated tau and the neurodegenerative foldopathies. Biochim Biophys Acta. 2005;1739(2-3):298-310.
    • (2005) Biochim Biophys Acta , vol.1739 , Issue.2-3 , pp. 298-310
    • Kosik, K.S.1    Shimura, H.2
  • 84
    • 11144249896 scopus 로고    scopus 로고
    • Increased tau phosphorylation on mitogen-activated protein kinase consensus sites and cognitive decline in transgenic models for Alzheimer's disease and FTDP-17: evidence for distinct molecular processes underlying tau abnormalities
    • Lambourne SL, Sellers LA, Bush TG, Choudhury SK, Emson PC, Suh YH, Wilkinson LS. Increased tau phosphorylation on mitogen-activated protein kinase consensus sites and cognitive decline in transgenic models for Alzheimer's disease and FTDP-17: evidence for distinct molecular processes underlying tau abnormalities. Mol Cell Biol. 2005;25(1):278-93.
    • (2005) Mol Cell Biol , vol.25 , Issue.1 , pp. 278-293
    • Lambourne, S.L.1    Sellers, L.A.2    Bush, T.G.3    Choudhury, S.K.4    Emson, P.C.5    Suh, Y.H.6    Wilkinson, L.S.7
  • 85
    • 0034641936 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • Yuan J, Yankner BA. Apoptosis in the nervous system. Nature. 2000;407(6805):802-9.
    • (2000) Nature , vol.407 , Issue.6805 , pp. 802-809
    • Yuan, J.1    Yankner, B.A.2
  • 86
    • 0037451130 scopus 로고    scopus 로고
    • Axonal transport of membranous and nonmembranous cargoes: a unified perspective
    • Brown A. Axonal transport of membranous and nonmembranous cargoes: a unified perspective. J Cell Biol. 2003;160(6):817-21.
    • (2003) J Cell Biol , vol.160 , Issue.6 , pp. 817-821
    • Brown, A.1
  • 89
    • 0031711244 scopus 로고    scopus 로고
    • Neurofibrillary tangles and Alzheimer's disease
    • Brion JP. Neurofibrillary tangles and Alzheimer's disease. Eur Neurol. 1998;40(3):130-40.
    • (1998) Eur Neurol , vol.40 , Issue.3 , pp. 130-140
    • Brion, J.P.1
  • 90
    • 0033066239 scopus 로고    scopus 로고
    • Neurochemical diversity of dystrophic neurites in the early and late stages of Alzheimer's disease
    • Dickson TC, King CE, McCormack GH, Vickers JC. Neurochemical diversity of dystrophic neurites in the early and late stages of Alzheimer's disease. Exp Neurol. 1999;156(1):100-10.
    • (1999) Exp Neurol , vol.156 , Issue.1 , pp. 100-110
    • Dickson, T.C.1    King, C.E.2    McCormack, G.H.3    Vickers, J.C.4
  • 92
    • 0024364877 scopus 로고
    • Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease
    • Masliah E, Terry RD, DeTeresa RM, Hansen LA. Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease. Neurosci Lett. 1989;103(2):234-9.
    • (1989) Neurosci Lett , vol.103 , Issue.2 , pp. 234-239
    • Masliah, E.1    Terry, R.D.2    DeTeresa, R.M.3    Hansen, L.A.4
  • 93
    • 0029813177 scopus 로고    scopus 로고
    • Comparison of neurodegenerative pathology in transgenic mice overexpressing V717F beta-amyloid precursor protein and Alzheimer's disease
    • Masliah E, Sisk A, Mallory M, Mucke L, Schenk D, Games D. Comparison of neurodegenerative pathology in transgenic mice overexpressing V717F beta-amyloid precursor protein and Alzheimer's disease. J Neurosci. 1996;16(18):5795-811.
    • (1996) J Neurosci , vol.16 , Issue.18 , pp. 5795-5811
    • Masliah, E.1    Sisk, A.2    Mallory, M.3    Mucke, L.4    Schenk, D.5    Games, D.6
  • 94
    • 77950632324 scopus 로고    scopus 로고
    • Abeta promotes Alzheimer's disease-like cytoskeleton abnormalities with consequences to APP processing in neurons
    • Henriques AG, Vieira SI, da Cruz ESEF, da Cruz ESOA. Abeta promotes Alzheimer's disease-like cytoskeleton abnormalities with consequences to APP processing in neurons. J Neurochem. 2010;113(3):761-71.
    • (2010) J Neurochem , vol.113 , Issue.3 , pp. 761-771
    • Henriques, A.G.1    Vieira, S.I.2    Cruz, E.S.E.F.3    Cruz, E.S.O.A.4
  • 95
    • 2542567240 scopus 로고    scopus 로고
    • Alzheimer's disease: intraneuronal alterations precede insoluble amyloid-beta formation
    • Braak H, Del Tredici K. Alzheimer's disease: intraneuronal alterations precede insoluble amyloid-beta formation. Neurobiol Aging. 2004;25(6):713-8 (discussion 743-716).
    • (2004) Neurobiol Aging , vol.25 , Issue.6 , pp. 713-718
    • Braak, H.1    Del Tredici, K.2
  • 98
    • 0036150827 scopus 로고    scopus 로고
    • Alzheimer's disease-do tauists and baptists finally shake hands?
    • Mudher A, Lovestone S. Alzheimer's disease-do tauists and baptists finally shake hands? Trends Neurosci. 2002;25(1):22-6.
    • (2002) Trends Neurosci , vol.25 , Issue.1 , pp. 22-26
    • Mudher, A.1    Lovestone, S.2
  • 99
    • 67650729973 scopus 로고    scopus 로고
    • Beta-amyloid oligomers induce phosphorylation of tau and inactivation of insulin receptor substrate via c-Jun N-terminal kinase signalling: suppression by omega-3 fatty acids and curcumin
    • Ma QL, Yang F, Rosario ER, Ubeda OJ, Beech W, Gant DJ, Chen PP, Hudspeth B, Chen C, Zhao Y, et al. Beta-amyloid oligomers induce phosphorylation of tau and inactivation of insulin receptor substrate via c-Jun N-terminal kinase signalling: suppression by omega-3 fatty acids and curcumin. J Neurosci. 2009;29(28):9078-89.
    • (2009) J Neurosci , vol.29 , Issue.28 , pp. 9078-9089
    • Ma, Q.L.1    Yang, F.2    Rosario, E.R.3    Ubeda, O.J.4    Beech, W.5    Gant, D.J.6    Chen, P.P.7    Hudspeth, B.8    Chen, C.9    Zhao, Y.10
  • 100
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils
    • Gotz J, Chen F, van Dorpe J, Nitsch RM. Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils. Science. 2001;293(5534):1491-5.
    • (2001) Science , vol.293 , Issue.5534 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Dorpe, J.3    Nitsch, R.M.4
  • 101
    • 0035134081 scopus 로고    scopus 로고
    • Age-dependent induction of congophilic neurofibrillary tau inclusions in tau transgenic mice
    • Ishihara T, Zhang B, Higuchi M, Yoshiyama Y, Trojanowski JQ, Lee VM. Age-dependent induction of congophilic neurofibrillary tau inclusions in tau transgenic mice. Am J Pathol. 2001;158(2):555-62.
    • (2001) Am J Pathol , vol.158 , Issue.2 , pp. 555-562
    • Ishihara, T.1    Zhang, B.2    Higuchi, M.3    Yoshiyama, Y.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 102
    • 0033795279 scopus 로고    scopus 로고
    • Apolipoprotein E and Alzheimer disease: an update on genetic and functional analyses
    • Saunders AM. Apolipoprotein E and Alzheimer disease: an update on genetic and functional analyses. J Neuropathol Exp Neurol. 2000;59(9):751-8.
    • (2000) J Neuropathol Exp Neurol , vol.59 , Issue.9 , pp. 751-758
    • Saunders, A.M.1
  • 103
    • 0026542786 scopus 로고
    • Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid
    • Wisniewski T, Frangione B. Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid. Neurosci Lett. 1992;135(2):235-8.
    • (1992) Neurosci Lett , vol.135 , Issue.2 , pp. 235-238
    • Wisniewski, T.1    Frangione, B.2
  • 104
  • 105
    • 84876894324 scopus 로고    scopus 로고
    • Binding of apolipoprotein E inhibits the oligomer growth of amyloid-beta peptide in solution as determined by fluorescence cross-correlation spectroscopy
    • Ly S, Altman R, Petrlova J, Lin Y, Hilt S, Huser T, Laurence TA, Voss JC. Binding of apolipoprotein E inhibits the oligomer growth of amyloid-beta peptide in solution as determined by fluorescence cross-correlation spectroscopy. J Biol Chem. 2013;288(17):11628-35.
    • (2013) J Biol Chem , vol.288 , Issue.17 , pp. 11628-11635
    • Ly, S.1    Altman, R.2    Petrlova, J.3    Lin, Y.4    Hilt, S.5    Huser, T.6    Laurence, T.A.7    Voss, J.C.8
  • 106
    • 0034100794 scopus 로고    scopus 로고
    • Apolipoprotein E4: an allele associated with many diseases
    • Smith JD. Apolipoprotein E4: an allele associated with many diseases. Ann Med. 2000;32(2):118-27.
    • (2000) Ann Med , vol.32 , Issue.2 , pp. 118-127
    • Smith, J.D.1
  • 109
    • 0035065367 scopus 로고    scopus 로고
    • Role of individual amino acids of apolipoprotein A-I in the activation of lecithin: cholesterol acyltransferase and in HDL rearrangements
    • Cho KH, Durbin DM, Jonas A. Role of individual amino acids of apolipoprotein A-I in the activation of lecithin: cholesterol acyltransferase and in HDL rearrangements. J Lipid Res. 2001;42(3):379-89.
    • (2001) J Lipid Res , vol.42 , Issue.3 , pp. 379-389
    • Cho, K.H.1    Durbin, D.M.2    Jonas, A.3
  • 110
    • 0033860372 scopus 로고    scopus 로고
    • Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity
    • Varadarajan S, Yatin S, Aksenova M, Butterfield DA. Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity. J Struct Biol. 2000;130(2-3):184-208.
    • (2000) J Struct Biol , vol.130 , Issue.2-3 , pp. 184-208
    • Varadarajan, S.1    Yatin, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 111
    • 0036905921 scopus 로고    scopus 로고
    • Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review
    • Butterfield DA. Amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity: implications for neurodegeneration in Alzheimer's disease brain. A review. Free Radic Res. 2002;36(12):1307-13.
    • (2002) Free Radic Res , vol.36 , Issue.12 , pp. 1307-1313
    • Butterfield, D.A.1
  • 112
    • 0036592636 scopus 로고    scopus 로고
    • Amyloid beta-peptide and amyloid pathology are central to the oxidative stress and inflammatory cascades under which Alzheimer's disease brain exists
    • Butterfield DA, Griffin S, Munch G, Pasinetti GM. Amyloid beta-peptide and amyloid pathology are central to the oxidative stress and inflammatory cascades under which Alzheimer's disease brain exists. J Alzheimers Dis. 2002;4(3):193-201.
    • (2002) J Alzheimers Dis , vol.4 , Issue.3 , pp. 193-201
    • Butterfield, D.A.1    Griffin, S.2    Munch, G.3    Pasinetti, G.M.4
  • 114
    • 84868286870 scopus 로고    scopus 로고
    • New insights in the amyloid-Beta interaction with mitochondria
    • Spuch C, Ortolano S, Navarro C. New insights in the amyloid-Beta interaction with mitochondria. J Aging Res. 2012;2012:324968.
    • (2012) J Aging Res , vol.2012 , pp. 324968
    • Spuch, C.1    Ortolano, S.2    Navarro, C.3
  • 115
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells
    • Anandatheerthavarada HK, Biswas G, Robin MA, Avadhani NG. Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells. J Cell Biol. 2003;161(1):41-54.
    • (2003) J Cell Biol , vol.161 , Issue.1 , pp. 41-54
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Robin, M.A.3    Avadhani, N.G.4
  • 117
    • 0343090436 scopus 로고    scopus 로고
    • Lipid peroxidation and nitrite plus nitrate levels in brain tissue from patients with Alzheimer's disease
    • DiCiero Miranda M, de Bruin VM, Vale MR, Viana GS. Lipid peroxidation and nitrite plus nitrate levels in brain tissue from patients with Alzheimer's disease. Gerontology. 2000;46(4):179-84.
    • (2000) Gerontology , vol.46 , Issue.4 , pp. 179-184
    • DiCiero Miranda, M.1    de Bruin, V.M.2    Vale, M.R.3    Viana, G.S.4
  • 118
    • 77956197971 scopus 로고    scopus 로고
    • Mitochondrial amyloid-beta levels are associated with the extent of mitochondrial dysfunction in different brain regions and the degree of cognitive impairment in Alzheimer's transgenic mice
    • Dragicevic N, Mamcarz M, Zhu Y, Buzzeo R, Tan J, Arendash GW, Bradshaw PC. Mitochondrial amyloid-beta levels are associated with the extent of mitochondrial dysfunction in different brain regions and the degree of cognitive impairment in Alzheimer's transgenic mice. J Alzheimers Dis. 2010;20(Suppl 2):S535-50.
    • (2010) J Alzheimers Dis , vol.20 , pp. S535-S550
    • Dragicevic, N.1    Mamcarz, M.2    Zhu, Y.3    Buzzeo, R.4    Tan, J.5    Arendash, G.W.6    Bradshaw, P.C.7
  • 119
    • 84927602807 scopus 로고    scopus 로고
    • Molecular mechanisms linking amyloid β toxicity and Tau hyperphosphorylation in Alzheimer's disease
    • Lloret A, Fuchsberger T, Giraldo E, Vina J. Molecular mechanisms linking amyloid β toxicity and Tau hyperphosphorylation in Alzheimer's disease. Free Radic Biol Med. 2015;83:186-91.
    • (2015) Free Radic Biol Med , vol.83 , pp. 186-191
    • Lloret, A.1    Fuchsberger, T.2    Giraldo, E.3    Vina, J.4
  • 120
    • 33644845279 scopus 로고    scopus 로고
    • Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease
    • Reddy PH. Amyloid precursor protein-mediated free radicals and oxidative damage: implications for the development and progression of Alzheimer's disease. J Neurochem. 2006;96(1):1-13.
    • (2006) J Neurochem , vol.96 , Issue.1 , pp. 1-13
    • Reddy, P.H.1
  • 121
    • 33744935554 scopus 로고    scopus 로고
    • Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in Mild Cognitive Impairment and early Alzheimer's disease
    • Williams TI, Lynn BC, Markesbery WR, Lovell MA. Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in Mild Cognitive Impairment and early Alzheimer's disease. Neurobiol Aging. 2006;27(8):1094-9.
    • (2006) Neurobiol Aging , vol.27 , Issue.8 , pp. 1094-1099
    • Williams, T.I.1    Lynn, B.C.2    Markesbery, W.R.3    Lovell, M.A.4
  • 122
    • 84930082960 scopus 로고    scopus 로고
    • Anti-oxidative effects produced by environmental enrichment in the hippocampus and cerebral cortex of male and female rats
    • Marmol F, Rodriguez CA, Sanchez J, Chamizo VD. Anti-oxidative effects produced by environmental enrichment in the hippocampus and cerebral cortex of male and female rats. Brain Res. 2015;10(1613):120-9.
    • (2015) Brain Res , vol.10 , Issue.1613 , pp. 120-129
    • Marmol, F.1    Rodriguez, C.A.2    Sanchez, J.3    Chamizo, V.D.4
  • 123
    • 0035880007 scopus 로고    scopus 로고
    • Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins
    • Butterfield DA, Kanski J. Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins. Mech Ageing Dev. 2001;122(9):945-62.
    • (2001) Mech Ageing Dev , vol.122 , Issue.9 , pp. 945-962
    • Butterfield, D.A.1    Kanski, J.2
  • 124
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller JN, Hanni KB, Markesbery WR. Impaired proteasome function in Alzheimer's disease. J Neurochem. 2000;75(1):436-9.
    • (2000) J Neurochem , vol.75 , Issue.1 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 125
    • 0034798361 scopus 로고    scopus 로고
    • Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells
    • Shringarpure R, Grune T, Davies KJ. Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells. Cell Mol Life Sci. 2001;58(10):1442-50.
    • (2001) Cell Mol Life Sci , vol.58 , Issue.10 , pp. 1442-1450
    • Shringarpure, R.1    Grune, T.2    Davies, K.J.3
  • 126
    • 0033765735 scopus 로고    scopus 로고
    • Oxidative injury in diseases of the central nervous system: focus on Alzheimer's disease
    • Pratico D, Delanty N. Oxidative injury in diseases of the central nervous system: focus on Alzheimer's disease. Am J Med. 2000;109(7):577-85.
    • (2000) Am J Med , vol.109 , Issue.7 , pp. 577-585
    • Pratico, D.1    Delanty, N.2
  • 128
    • 0033637884 scopus 로고    scopus 로고
    • Beta-amyloid activated microglia induce cell cycling and cell death in cultured cortical neurons
    • Wu Q, Combs C, Cannady SB, Geldmacher DS, Herrup K. Beta-amyloid activated microglia induce cell cycling and cell death in cultured cortical neurons. Neurobiol Aging. 2000;21(6):797-806.
    • (2000) Neurobiol Aging , vol.21 , Issue.6 , pp. 797-806
    • Wu, Q.1    Combs, C.2    Cannady, S.B.3    Geldmacher, D.S.4    Herrup, K.5
  • 129
    • 0034802570 scopus 로고    scopus 로고
    • Immunological aspects of microglia: relevance to Alzheimer's disease
    • Benveniste EN, Nguyen VT, O'Keefe GM. Immunological aspects of microglia: relevance to Alzheimer's disease. Neurochem Int. 2001;39(5-6):381-91.
    • (2001) Neurochem Int , vol.39 , Issue.5-6 , pp. 381-391
    • Benveniste, E.N.1    Nguyen, V.T.2    O'Keefe, G.M.3
  • 130
    • 0035255055 scopus 로고    scopus 로고
    • IL-4, IL-10 and IL-13 modulate A beta(1-42)-induced cytokine and chemokine production in primary murine microglia and a human monocyte cell line
    • Szczepanik AM, Funes S, Petko W, Ringheim GE. IL-4, IL-10 and IL-13 modulate A beta(1-42)-induced cytokine and chemokine production in primary murine microglia and a human monocyte cell line. J Neuroimmunol. 2001;113(1):49-62.
    • (2001) J Neuroimmunol , vol.113 , Issue.1 , pp. 49-62
    • Szczepanik, A.M.1    Funes, S.2    Petko, W.3    Ringheim, G.E.4
  • 132
    • 0034661784 scopus 로고    scopus 로고
    • Cyclin' toward dementia: cell cycle abnormalities and abortive oncogenesis in Alzheimer disease
    • Raina AK, Zhu X, Rottkamp CA, Monteiro M, Takeda A, Smith MA. Cyclin' toward dementia: cell cycle abnormalities and abortive oncogenesis in Alzheimer disease. J Neurosci Res. 2000;61(2):128-33.
    • (2000) J Neurosci Res , vol.61 , Issue.2 , pp. 128-133
    • Raina, A.K.1    Zhu, X.2    Rottkamp, C.A.3    Monteiro, M.4    Takeda, A.5    Smith, M.A.6
  • 133
    • 0031737550 scopus 로고    scopus 로고
    • Neuronal expression of cycline dependent kinase inhibitors of the INK4 family in Alzheimer's disease
    • Arendt T, Holzer M, Gartner U. Neuronal expression of cycline dependent kinase inhibitors of the INK4 family in Alzheimer's disease. J Neural Transm. 1998;105(8-9):949-60.
    • (1998) J Neural Transm , vol.105 , Issue.8-9 , pp. 949-960
    • Arendt, T.1    Holzer, M.2    Gartner, U.3
  • 134
    • 0032522911 scopus 로고    scopus 로고
    • Ectopic cell cycle proteins predict the sites of neuronal cell death in Alzheimer's disease brain
    • Busser J, Geldmacher DS, Herrup K. Ectopic cell cycle proteins predict the sites of neuronal cell death in Alzheimer's disease brain. J Neurosci. 1998;18(8):2801-7.
    • (1998) J Neurosci , vol.18 , Issue.8 , pp. 2801-2807
    • Busser, J.1    Geldmacher, D.S.2    Herrup, K.3
  • 135
    • 0033516567 scopus 로고    scopus 로고
    • Involvement of cell cycle elements, cyclin-dependent kinases, pRb, and E2F × DP, B-amyloid-induced neuronal death
    • Giovanni A, Wirtz-Brugger F, Keramaris E, Slack R, Park DS. Involvement of cell cycle elements, cyclin-dependent kinases, pRb, and E2F × DP, B-amyloid-induced neuronal death. J Biol Chem. 1999;274(27):19011-6.
    • (1999) J Biol Chem , vol.274 , Issue.27 , pp. 19011-19016
    • Giovanni, A.1    Wirtz-Brugger, F.2    Keramaris, E.3    Slack, R.4    Park, D.S.5
  • 136
    • 0035871660 scopus 로고    scopus 로고
    • DNA replication precedes neuronal cell death in Alzheimer's disease
    • Yang Y, Geldmacher DS, Herrup K. DNA replication precedes neuronal cell death in Alzheimer's disease. J Neurosci. 2001;21(8):2661-8.
    • (2001) J Neurosci , vol.21 , Issue.8 , pp. 2661-2668
    • Yang, Y.1    Geldmacher, D.S.2    Herrup, K.3
  • 137
    • 0344241479 scopus 로고    scopus 로고
    • Neuronal cell death is preceded by cell cycle events at all stages of Alzheimer's disease
    • Yang Y, Mufson EJ, Herrup K. Neuronal cell death is preceded by cell cycle events at all stages of Alzheimer's disease. J Neurosci. 2003;23(7):2557-63.
    • (2003) J Neurosci , vol.23 , Issue.7 , pp. 2557-2563
    • Yang, Y.1    Mufson, E.J.2    Herrup, K.3
  • 138
    • 0032892435 scopus 로고    scopus 로고
    • The role of cell cycle-mediated events in Alzheimer's disease
    • Raina AK, Monteiro MJ, McShea A, Smith MA. The role of cell cycle-mediated events in Alzheimer's disease. Int J Exp Pathol. 1999;80(2):71-6.
    • (1999) Int J Exp Pathol , vol.80 , Issue.2 , pp. 71-76
    • Raina, A.K.1    Monteiro, M.J.2    McShea, A.3    Smith, M.A.4
  • 139
    • 0034237405 scopus 로고    scopus 로고
    • Activation of oncogenic pathways in degenerating neurons in Alzheimer disease
    • Zhu X, Raina AK, Boux H, Simmons ZL, Takeda A, Smith MA. Activation of oncogenic pathways in degenerating neurons in Alzheimer disease. Int J Dev Neurosci. 2000;18(4-5):433-7.
    • (2000) Int J Dev Neurosci , vol.18 , Issue.4-5 , pp. 433-437
    • Zhu, X.1    Raina, A.K.2    Boux, H.3    Simmons, Z.L.4    Takeda, A.5    Smith, M.A.6
  • 141
    • 0035058466 scopus 로고    scopus 로고
    • Activation of cell-cycle-associated proteins in neuronal death: a mandatory or dispensable path?
    • Copani A, Uberti D, Sortino MA, Bruno V, Nicoletti F, Memo M. Activation of cell-cycle-associated proteins in neuronal death: a mandatory or dispensable path? Trends Neurosci. 2001;24(1):25-31.
    • (2001) Trends Neurosci , vol.24 , Issue.1 , pp. 25-31
    • Copani, A.1    Uberti, D.2    Sortino, M.A.3    Bruno, V.4    Nicoletti, F.5    Memo, M.6
  • 142
    • 46349093667 scopus 로고    scopus 로고
    • Different fibrillar Abeta 1-42 concentrations induce adult hippocampal neurons to reenter various phases of the cell cycle
    • Majd S, Zarifkar A, Rastegar K, Takhshid MA. Different fibrillar Abeta 1-42 concentrations induce adult hippocampal neurons to reenter various phases of the cell cycle. Brain Res. 2008;1218:224-9.
    • (2008) Brain Res , vol.1218 , pp. 224-229
    • Majd, S.1    Zarifkar, A.2    Rastegar, K.3    Takhshid, M.A.4
  • 143
    • 4344637728 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitors attenuate protein hyperphosphorylation, cytoskeletal lesion formation, and motor defects in Niemann-Pick Type C mice
    • Zhang M, Li J, Chakrabarty P, Bu B, Vincent I. Cyclin-dependent kinase inhibitors attenuate protein hyperphosphorylation, cytoskeletal lesion formation, and motor defects in Niemann-Pick Type C mice. Am J Pathol. 2004;165(3):843-53.
    • (2004) Am J Pathol , vol.165 , Issue.3 , pp. 843-853
    • Zhang, M.1    Li, J.2    Chakrabarty, P.3    Bu, B.4    Vincent, I.5
  • 144
    • 84871660526 scopus 로고    scopus 로고
    • Reciprocal induction between alpha-synuclein and beta-amyloid in adult rat neurons
    • Majd S, Chegini F, Chataway T, Zhou XF, Gai W. Reciprocal induction between alpha-synuclein and beta-amyloid in adult rat neurons. Neurotox Res. 2013;23(1):69-78.
    • (2013) Neurotox Res , vol.23 , Issue.1 , pp. 69-78
    • Majd, S.1    Chegini, F.2    Chataway, T.3    Zhou, X.F.4    Gai, W.5
  • 145
    • 27744536440 scopus 로고    scopus 로고
    • The last neuronal division: a unifying hypothesis for the pathogenesis of Alzheimer's disease
    • Nagy Z. The last neuronal division: a unifying hypothesis for the pathogenesis of Alzheimer's disease. J Cell Mol Med. 2005;9(3):531-41.
    • (2005) J Cell Mol Med , vol.9 , Issue.3 , pp. 531-541
    • Nagy, Z.1
  • 146
    • 84893714992 scopus 로고    scopus 로고
    • Autophagy in aging and neurodegenerative diseases: implications for pathogenesis and therapy
    • Tan CC, Yu JT, Tan MS, Jiang T, Zhu XC, Tan L. Autophagy in aging and neurodegenerative diseases: implications for pathogenesis and therapy. Neurobiol Aging. 2014;35:941-57.
    • (2014) Neurobiol Aging , vol.35 , pp. 941-957
    • Tan, C.C.1    Yu, J.T.2    Tan, M.S.3    Jiang, T.4    Zhu, X.C.5    Tan, L.6
  • 148
    • 0036278335 scopus 로고    scopus 로고
    • Dopamine-dependent neurotoxicity of alpha-synuclein: a mechanism for selective neurodegeneration in Parkinson disease
    • Xu J, Kao SY, Lee FJ, Song W, Jin LW, Yankner BA. Dopamine-dependent neurotoxicity of alpha-synuclein: a mechanism for selective neurodegeneration in Parkinson disease. Nat Med. 2002;8(6):600-6.
    • (2002) Nat Med , vol.8 , Issue.6 , pp. 600-606
    • Xu, J.1    Kao, S.Y.2    Lee, F.J.3    Song, W.4    Jin, L.W.5    Yankner, B.A.6
  • 149
    • 0029981526 scopus 로고    scopus 로고
    • Neuropathology of Parkinson's disease
    • Forno LS. Neuropathology of Parkinson's disease. J Neuropathol Exp Neurol. 1996;55(3):259-72.
    • (1996) J Neuropathol Exp Neurol , vol.55 , Issue.3 , pp. 259-272
    • Forno, L.S.1
  • 151
    • 0029127954 scopus 로고
    • Characterization of a novel protein regulated during the critical period for song learning in the zebra finch
    • George JM, Jin H, Woods WS, Clayton DF. Characterization of a novel protein regulated during the critical period for song learning in the zebra finch. Neuron. 1995;15(2):361-72.
    • (1995) Neuron , vol.15 , Issue.2 , pp. 361-372
    • George, J.M.1    Jin, H.2    Woods, W.S.3    Clayton, D.F.4
  • 153
    • 0036315240 scopus 로고    scopus 로고
    • Demonstration of alpha-synuclein immunoreactivity in neuronal and glial cytoplasm in normal human brain tissue using proteinase K and formic acid pretreatment
    • Mori F, Tanji K, Yoshimoto M, Takahashi H, Wakabayashi K. Demonstration of alpha-synuclein immunoreactivity in neuronal and glial cytoplasm in normal human brain tissue using proteinase K and formic acid pretreatment. Exp Neurol. 2002;176(1):98-104.
    • (2002) Exp Neurol , vol.176 , Issue.1 , pp. 98-104
    • Mori, F.1    Tanji, K.2    Yoshimoto, M.3    Takahashi, H.4    Wakabayashi, K.5
  • 155
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis
    • Perrin RJ, Woods WS, Clayton DF, George JM. Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis. J Biol Chem. 2000;275(44):34393-8.
    • (2000) J Biol Chem , vol.275 , Issue.44 , pp. 34393-34398
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 156
    • 0037109727 scopus 로고    scopus 로고
    • Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein
    • Cabin DE, Shimazu K, Murphy D, Cole NB, Gottschalk W, McIlwain KL, Orrison B, Chen A, Ellis CE, Paylor R, et al. Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein. J Neurosci. 2002;22(20):8797-807.
    • (2002) J Neurosci , vol.22 , Issue.20 , pp. 8797-8807
    • Cabin, D.E.1    Shimazu, K.2    Murphy, D.3    Cole, N.B.4    Gottschalk, W.5    McIlwain, K.L.6    Orrison, B.7    Chen, A.8    Ellis, C.E.9    Paylor, R.10
  • 157
    • 27544507306 scopus 로고    scopus 로고
    • Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration
    • Chandra S, Gallardo G, Fernandez-Chacon R, Schluter OM, Sudhof TC. Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration. Cell. 2005;123(3):383-96.
    • (2005) Cell , vol.123 , Issue.3 , pp. 383-396
    • Chandra, S.1    Gallardo, G.2    Fernandez-Chacon, R.3    Schluter, O.M.4    Sudhof, T.C.5
  • 159
  • 162
    • 77956966416 scopus 로고    scopus 로고
    • Molecular interaction of alpha-synuclein with tubulin influences on the polymerization of microtubule in vitro and structure of microtubule in cells
    • Zhou RM, Huang YX, Li XL, Chen C, Shi Q, Wang GR, Tian C, Wang ZY, Jing YY, Gao C, et al. Molecular interaction of alpha-synuclein with tubulin influences on the polymerization of microtubule in vitro and structure of microtubule in cells. Mol Biol Rep. 2010;37(7):3183-92.
    • (2010) Mol Biol Rep , vol.37 , Issue.7 , pp. 3183-3192
    • Zhou, R.M.1    Huang, Y.X.2    Li, X.L.3    Chen, C.4    Shi, Q.5    Wang, G.R.6    Tian, C.7    Wang, Z.Y.8    Jing, Y.Y.9    Gao, C.10
  • 164
    • 34548620297 scopus 로고    scopus 로고
    • Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation
    • Uversky VN. Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation. J Neurochem. 2007;103(1):17-37.
    • (2007) J Neurochem , vol.103 , Issue.1 , pp. 17-37
    • Uversky, V.N.1
  • 166
    • 84899894003 scopus 로고    scopus 로고
    • c-Abl phosphorylates alpha-synuclein and regulates its degradation, implication for alpha-synuclein clearance and contribution to the pathogenesis of Parkinson's Disease
    • Mahul-Mellier AL, Fauvet B, Gysbers A, Dikiy I, Oueslati A, Georgeon S, Lamontanara AJ, Bisquertt A, Eliezer D, Masliah E, et al. c-Abl phosphorylates alpha-synuclein and regulates its degradation, implication for alpha-synuclein clearance and contribution to the pathogenesis of Parkinson's Disease. Hum Mol Genet. 2014;23(11):2858-79.
    • (2014) Hum Mol Genet , vol.23 , Issue.11 , pp. 2858-2879
    • Mahul-Mellier, A.L.1    Fauvet, B.2    Gysbers, A.3    Dikiy, I.4    Oueslati, A.5    Georgeon, S.6    Lamontanara, A.J.7    Bisquertt, A.8    Eliezer, D.9    Masliah, E.10
  • 169
    • 0033564726 scopus 로고    scopus 로고
    • Copper(II)-induced self-oligomerization of alpha-synuclein
    • Paik SR, Shin HJ, Lee JH, Chang CS, Kim J. Copper(II)-induced self-oligomerization of alpha-synuclein. Biochem J. 1999;340(Pt 3):821-8.
    • (1999) Biochem J , vol.340 , pp. 821-828
    • Paik, S.R.1    Shin, H.J.2    Lee, J.H.3    Chang, C.S.4    Kim, J.5
  • 170
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro
    • Hashimoto M, Hsu LJ, Xia Y, Takeda A, Sisk A, Sundsmo M, Masliah E. Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro. Neuroreport. 1999;10(4):717-21.
    • (1999) Neuroreport , vol.10 , Issue.4 , pp. 717-721
    • Hashimoto, M.1    Hsu, L.J.2    Xia, Y.3    Takeda, A.4    Sisk, A.5    Sundsmo, M.6    Masliah, E.7
  • 171
    • 0034193399 scopus 로고    scopus 로고
    • Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons
    • Murphy DD, Rueter SM, Trojanowski JQ, Lee VM. Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J Neurosci. 2000;20(9):3214-20.
    • (2000) J Neurosci , vol.20 , Issue.9 , pp. 3214-3220
    • Murphy, D.D.1    Rueter, S.M.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 172
    • 0141891097 scopus 로고    scopus 로고
    • The association of alpha-synuclein with membranes affects bilayer structure, stability, and fibril formation
    • Zhu M, Li J, Fink AL. The association of alpha-synuclein with membranes affects bilayer structure, stability, and fibril formation. J Biol Chem. 2003;278(41):40186-97.
    • (2003) J Biol Chem , vol.278 , Issue.41 , pp. 40186-40197
    • Zhu, M.1    Li, J.2    Fink, A.L.3
  • 173
    • 3242879787 scopus 로고    scopus 로고
    • alpha-Synuclein-synaptosomal membrane interactions: implications for fibrillogenesis
    • Jo E, Darabie AA, Han K, Tandon A, Fraser PE, McLaurin J. alpha-Synuclein-synaptosomal membrane interactions: implications for fibrillogenesis. Eur J Biochem. 2004;271(15):3180-9.
    • (2004) Eur J Biochem , vol.271 , Issue.15 , pp. 3180-3189
    • Jo, E.1    Darabie, A.A.2    Han, K.3    Tandon, A.4    Fraser, P.E.5    McLaurin, J.6
  • 174
    • 84864258151 scopus 로고    scopus 로고
    • alpha-Synuclein inhibits intersynaptic vesicle mobility and maintains recycling-pool homeostasis
    • Scott D, Roy S. alpha-Synuclein inhibits intersynaptic vesicle mobility and maintains recycling-pool homeostasis. J Neurosci. 2012;32(30):10129-35.
    • (2012) J Neurosci , vol.32 , Issue.30 , pp. 10129-10135
    • Scott, D.1    Roy, S.2
  • 176
    • 84887963355 scopus 로고    scopus 로고
    • Genetic causes of Parkinson's disease and their links to autophagy regulation
    • Pan PY, Yue Z. Genetic causes of Parkinson's disease and their links to autophagy regulation. Parkinsonism Relat Disord. 2014;20(Suppl 1):S154-7.
    • (2014) Parkinsonism Relat Disord. , vol.20 , pp. S154-S157
    • Pan, P.Y.1    Yue, Z.2
  • 177
    • 0035076647 scopus 로고    scopus 로고
    • alpha-Synuclein forms a complex with transcription factor Elk-1
    • Iwata A, Miura S, Kanazawa I, Sawada M, Nukina N. alpha-Synuclein forms a complex with transcription factor Elk-1. J Neurochem. 2001;77(1):239-52.
    • (2001) J Neurochem , vol.77 , Issue.1 , pp. 239-252
    • Iwata, A.1    Miura, S.2    Kanazawa, I.3    Sawada, M.4    Nukina, N.5
  • 178
    • 1842454976 scopus 로고    scopus 로고
    • Does alpha-synuclein modulate dopaminergic synaptic content and tone at the synapse?
    • Sidhu A, Wersinger C, Vernier P. Does alpha-synuclein modulate dopaminergic synaptic content and tone at the synapse? FASEB J. 2004;18(6):637-47.
    • (2004) FASEB J , vol.18 , Issue.6 , pp. 637-647
    • Sidhu, A.1    Wersinger, C.2    Vernier, P.3
  • 179
    • 0035976959 scopus 로고    scopus 로고
    • alpha-Synuclein affects the MAPK pathway and accelerates cell death
    • Iwata A, Maruyama M, Kanazawa I, Nukina N. alpha-Synuclein affects the MAPK pathway and accelerates cell death. J Biol Chem. 2001;276(48):45320-9.
    • (2001) J Biol Chem , vol.276 , Issue.48 , pp. 45320-45329
    • Iwata, A.1    Maruyama, M.2    Kanazawa, I.3    Nukina, N.4
  • 180
    • 0142154275 scopus 로고    scopus 로고
    • Alpha-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies
    • Iwata A, Maruyama M, Akagi T, Hashikawa T, Kanazawa I, Tsuji S, Nukina N. Alpha-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies. Hum Mol Genet. 2003;12(20):2625-35.
    • (2003) Hum Mol Genet , vol.12 , Issue.20 , pp. 2625-2635
    • Iwata, A.1    Maruyama, M.2    Akagi, T.3    Hashikawa, T.4    Kanazawa, I.5    Tsuji, S.6    Nukina, N.7
  • 183
    • 62449129138 scopus 로고    scopus 로고
    • Cell death pathways in Parkinson's disease: proximal triggers, distal effectors, and final steps
    • Levy OA, Malagelada C, Greene LA. Cell death pathways in Parkinson's disease: proximal triggers, distal effectors, and final steps. Apoptosis. 2009;14(4):478-500.
    • (2009) Apoptosis , vol.14 , Issue.4 , pp. 478-500
    • Levy, O.A.1    Malagelada, C.2    Greene, L.A.3
  • 184
    • 34347369328 scopus 로고    scopus 로고
    • Activation of apoptosis signal regulating kinase 1 (ASK1) and translocation of death-associated protein, Daxx, in substantia nigra pars compacta in a mouse model of Parkinson's disease: protection by alpha-lipoic acid
    • Karunakaran S, Diwakar L, Saeed U, Agarwal V, Ramakrishnan S, Iyengar S, Ravindranath V. Activation of apoptosis signal regulating kinase 1 (ASK1) and translocation of death-associated protein, Daxx, in substantia nigra pars compacta in a mouse model of Parkinson's disease: protection by alpha-lipoic acid. FASEB J. 2007;21(9):2226-36.
    • (2007) FASEB J , vol.21 , Issue.9 , pp. 2226-2236
    • Karunakaran, S.1    Diwakar, L.2    Saeed, U.3    Agarwal, V.4    Ramakrishnan, S.5    Iyengar, S.6    Ravindranath, V.7
  • 187
    • 84902535538 scopus 로고    scopus 로고
    • The centrality of mitochondria in the pathogenesis and treatment of Parkinson's disease
    • Camilleri A, Vassallo N. The centrality of mitochondria in the pathogenesis and treatment of Parkinson's disease. CNS Neurosci Ther. 2014;20(7):591-602.
    • (2014) CNS Neurosci Ther. , vol.20 , Issue.7 , pp. 591-602
    • Camilleri, A.1    Vassallo, N.2
  • 188
    • 84878614977 scopus 로고    scopus 로고
    • Alpha-synuclein and intracellular trafficking: impact on the spreading of Parkinson's disease pathology
    • Eisbach SE, Outeiro TF. Alpha-synuclein and intracellular trafficking: impact on the spreading of Parkinson's disease pathology. J Mol Med (Berl). 2013;91(6):693-703.
    • (2013) J Mol Med (Berl) , vol.91 , Issue.6 , pp. 693-703
    • Eisbach, S.E.1    Outeiro, T.F.2
  • 189
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia
    • Sian J, Dexter DT, Lees AJ, Daniel S, Agid Y, Javoy-Agid F, Jenner P, Marsden CD. Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia. Ann Neurol. 1994;36(3):348-55.
    • (1994) Ann Neurol , vol.36 , Issue.3 , pp. 348-355
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3    Daniel, S.4    Agid, Y.5    Javoy-Agid, F.6    Jenner, P.7    Marsden, C.D.8
  • 190
    • 0024356620 scopus 로고
    • Increased nigral iron content and alterations in other metal ions occurring in brain in Parkinson's disease
    • Dexter DT, Wells FR, Lees AJ, Agid F, Agid Y, Jenner P, Marsden CD. Increased nigral iron content and alterations in other metal ions occurring in brain in Parkinson's disease. J Neurochem. 1989;52(6):1830-6.
    • (1989) J Neurochem , vol.52 , Issue.6 , pp. 1830-1836
    • Dexter, D.T.1    Wells, F.R.2    Lees, A.J.3    Agid, F.4    Agid, Y.5    Jenner, P.6    Marsden, C.D.7
  • 191
    • 0345724066 scopus 로고
    • Dopamine turnover and glutathione oxidation: implications for Parkinson disease
    • Spina MB, Cohen G. Dopamine turnover and glutathione oxidation: implications for Parkinson disease. Proc Natl Acad Sci USA. 1989;86(4):1398-400.
    • (1989) Proc Natl Acad Sci USA , vol.86 , Issue.4 , pp. 1398-1400
    • Spina, M.B.1    Cohen, G.2
  • 193
    • 34748826792 scopus 로고    scopus 로고
    • Localization of alpha-synuclein to mitochondria within midbrain of mice
    • Li WW, Yang R, Guo JC, Ren HM, Zha XL, Cheng JS, Cai DF. Localization of alpha-synuclein to mitochondria within midbrain of mice. Neuroreport. 2007;18(15):1543-6.
    • (2007) Neuroreport , vol.18 , Issue.15 , pp. 1543-1546
    • Li, W.W.1    Yang, R.2    Guo, J.C.3    Ren, H.M.4    Zha, X.L.5    Cheng, J.S.6    Cai, D.F.7
  • 196
    • 84928485187 scopus 로고    scopus 로고
    • Mitochondrial Dysfunction and aα-synuclein Synaptic Pathology in Parkinson's Disease: Who's on First
    • Zaltieri M, Longhena F, Pizzi M, Missale C, Spano P, Bellucci A. Mitochondrial Dysfunction and aα-synuclein Synaptic Pathology in Parkinson's Disease: Who's on First. Parkinsons Dis. 2015;108029:1-10.
    • (2015) Parkinsons Dis. , pp. 1-10
    • Zaltieri, M.1    Longhena, F.2    Pizzi, M.3    Missale, C.4    Spano, P.5    Bellucci, A.6
  • 197
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell. 1996;86(1):147-57.
    • (1996) Cell , vol.86 , Issue.1 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 198
    • 77952900626 scopus 로고    scopus 로고
    • Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs
    • Thayanidhi N, Helm JR, Nycz DC, Bentley M, Liang Y, Hay JC. Alpha-synuclein delays endoplasmic reticulum (ER)-to-Golgi transport in mammalian cells by antagonizing ER/Golgi SNAREs. Mol Biol Cell. 2010;21(11):1850-63.
    • (2010) Mol Biol Cell , vol.21 , Issue.11 , pp. 1850-1863
    • Thayanidhi, N.1    Helm, J.R.2    Nycz, D.C.3    Bentley, M.4    Liang, Y.5    Hay, J.C.6
  • 199
    • 84863229691 scopus 로고    scopus 로고
    • Accumulation of toxic alpha-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo
    • Colla E, Jensen PH, Pletnikova O, Troncoso JC, Glabe C, Lee MK. Accumulation of toxic alpha-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo. J Neurosci. 2012;32(10):3301-5.
    • (2012) J Neurosci , vol.32 , Issue.10 , pp. 3301-3305
    • Colla, E.1    Jensen, P.H.2    Pletnikova, O.3    Troncoso, J.C.4    Glabe, C.5    Lee, M.K.6
  • 200
    • 0037428398 scopus 로고    scopus 로고
    • Evaluation of the therapeutic usefulness of botulinum neurotoxin B, C1, E, and F compared with the long lasting type A. Basis for distinct durations of inhibition of exocytosis in central neurons
    • Foran PG, Mohammed N, Lisk GO, Nagwaney S, Lawrence GW, Johnson E, Smith L, Aoki KR, Dolly JO. Evaluation of the therapeutic usefulness of botulinum neurotoxin B, C1, E, and F compared with the long lasting type A. Basis for distinct durations of inhibition of exocytosis in central neurons. J Biol Chem. 2003;278(2):1363-71.
    • (2003) J Biol Chem , vol.278 , Issue.2 , pp. 1363-1371
    • Foran, P.G.1    Mohammed, N.2    Lisk, G.O.3    Nagwaney, S.4    Lawrence, G.W.5    Johnson, E.6    Smith, L.7    Aoki, K.R.8    Dolly, J.O.9
  • 203
    • 0037073748 scopus 로고    scopus 로고
    • Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion
    • Gosavi N, Lee HJ, Lee JS, Patel S, Lee SJ. Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion. J Biol Chem. 2002;277(50):48984-92.
    • (2002) J Biol Chem , vol.277 , Issue.50 , pp. 48984-48992
    • Gosavi, N.1    Lee, H.J.2    Lee, J.S.3    Patel, S.4    Lee, S.J.5
  • 204
    • 33845656077 scopus 로고    scopus 로고
    • Impairment of microtubule-dependent trafficking by overexpression of alpha-synuclein
    • Lee HJ, Khoshaghideh F, Lee S, Lee SJ. Impairment of microtubule-dependent trafficking by overexpression of alpha-synuclein. Eur J Neurosci. 2006;24(11):3153-62.
    • (2006) Eur J Neurosci , vol.24 , Issue.11 , pp. 3153-3162
    • Lee, H.J.1    Khoshaghideh, F.2    Lee, S.3    Lee, S.J.4
  • 205
    • 73549085595 scopus 로고    scopus 로고
    • Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis
    • Nemani VM, Lu W, Berge V, Nakamura K, Onoa B, Lee MK, Chaudhry FA, Nicoll RA, Edwards RH. Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron. 2010;65(1):66-79.
    • (2010) Neuron , vol.65 , Issue.1 , pp. 66-79
    • Nemani, V.M.1    Lu, W.2    Berge, V.3    Nakamura, K.4    Onoa, B.5    Lee, M.K.6    Chaudhry, F.A.7    Nicoll, R.A.8    Edwards, R.H.9
  • 208
    • 33847649977 scopus 로고    scopus 로고
    • Extensive nuclear localization of alpha-synuclein in normal rat brain neurons revealed by a novel monoclonal antibody
    • Yu S, Li X, Liu G, Han J, Zhang C, Li Y, Xu S, Liu C, Gao Y, Yang H, et al. Extensive nuclear localization of alpha-synuclein in normal rat brain neurons revealed by a novel monoclonal antibody. Neuroscience. 2007;145(2):539-55.
    • (2007) Neuroscience , vol.145 , Issue.2 , pp. 539-555
    • Yu, S.1    Li, X.2    Liu, G.3    Han, J.4    Zhang, C.5    Li, Y.6    Xu, S.7    Liu, C.8    Gao, Y.9    Yang, H.10
  • 209
    • 65249162241 scopus 로고    scopus 로고
    • Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies
    • Paleologou KE, Kragh CL, Mann DM, Salem SA, Al-Shami R, Allsop D, Hassan AH, Jensen PH, El-Agnaf OM. Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies. Brain. 2009;132(Pt 4):1093-101.
    • (2009) Brain , vol.132 , pp. 1093-1101
    • Paleologou, K.E.1    Kragh, C.L.2    Mann, D.M.3    Salem, S.A.4    Al-Shami, R.5    Allsop, D.6    Hassan, A.H.7    Jensen, P.H.8    El-Agnaf, O.M.9
  • 210
    • 32544459388 scopus 로고    scopus 로고
    • Ectopic cell cycle events link human Alzheimer's disease and amyloid precursor protein transgenic mouse models
    • Yang Y, Varvel NH, Lamb BT, Herrup K. Ectopic cell cycle events link human Alzheimer's disease and amyloid precursor protein transgenic mouse models. J Neurosci. 2006;26(3):775-84.
    • (2006) J Neurosci , vol.26 , Issue.3 , pp. 775-784
    • Yang, Y.1    Varvel, N.H.2    Lamb, B.T.3    Herrup, K.4
  • 211
    • 39749185957 scopus 로고    scopus 로고
    • A molecular pathway of neurodegeneration linking alpha-synuclein to ApoE and Abeta peptides
    • Gallardo G, Schluter OM, Sudhof TC. A molecular pathway of neurodegeneration linking alpha-synuclein to ApoE and Abeta peptides. Nat Neurosci. 2008;11(3):301-8.
    • (2008) Nat Neurosci , vol.11 , Issue.3 , pp. 301-308
    • Gallardo, G.1    Schluter, O.M.2    Sudhof, T.C.3


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