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Volumn 56, Issue 3, 2002, Pages 282-292

Progress in the development of new treatments for combined Alzheimer's and Parkinson's diseases

Author keywords

synuclein; synuclein; Alzheimer's disease; Lewy body disease; Parkinson's disease; Transgenic mouse

Indexed keywords

2,3,4,5 TETRAHYDRO 7,8 DIHYDROXY 1 PHENYL 1H 3 BENZAZEPINE; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; ANTIOXIDANT; ATROPINE; BETA SYNUCLEIN; BROMOCRIPTINE; CHOLINERGIC RECEPTOR BLOCKING AGENT; CYTOCHROME C; DOPAMINE RECEPTOR STIMULATING AGENT; FENCLONINE; LEVODOPA; METIROSINE; NEUROTROPHIC FACTOR; PERGOLIDE; PLATELET DERIVED GROWTH FACTOR B;

EID: 0036660268     PISSN: 02724391     EISSN: None     Source Type: Journal    
DOI: 10.1002/ddr.10082     Document Type: Review
Times cited : (4)

References (108)
  • 1
    • 0034604583 scopus 로고    scopus 로고
    • Wild-type but not Parkinson's disease-related ala-53→ Thr mutant alpha synuclein protects neuronal cells from apoptotic stimuli
    • Alves Da Costa C, Ancolio K, Cheeler F. 2000. Wild-type but not Parkinson's disease-related ala-53→ Thr mutant alpha synuclein protects neuronal cells from apoptotic stimuli. J Biol Chem 275:24065-24069.
    • (2000) J Biol Chem , vol.275 , pp. 24065-24069
    • Alves Da Costa, C.1    Ancolio, K.2    Cheeler, F.3
  • 2
    • 0034047021 scopus 로고    scopus 로고
    • Beta-amyloid deposition in the temporal lobe of patients with dementia with Lewy bodies: Comparison with non-demented cases and Alzheimer's disease
    • Armstrong R, Cairns N, Lantos P. 2000. Beta-amyloid deposition in the temporal lobe of patients with dementia with Lewy bodies: comparison with non-demented cases and Alzheimer's disease. Dement Geriatr Cogn Disord 11:187-192.
    • (2000) Dement Geriatr Cogn Disord , vol.11 , pp. 187-192
    • Armstrong, R.1    Cairns, N.2    Lantos, P.3
  • 3
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck PK, Chan HY, Trojanowski JQ, Lee VM, Bonini NM. 2002. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295:865-868.
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 6
    • 0027451313 scopus 로고
    • Molecular genetics of Alzheimer's disease
    • Clark R, Goate A. 1993. Molecular genetics of Alzheimer's disease. Arch Neurol 50:1164-1172.
    • (1993) Arch Neurol , vol.50 , pp. 1164-1172
    • Clark, R.1    Goate, A.2
  • 7
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
    • Conway K, Harper J, Lansbury P. 1998. Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nature Med 4:1318-1320.
    • (1998) Nature Med , vol.4 , pp. 1318-1320
    • Conway, K.1    Harper, J.2    Lansbury, P.3
  • 8
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization not fibrillization, is a shared property of both alpha-synuclein mutations linked to earlyonset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway KA, Lee SJ, Rochet JC, Ding TT, Williamson RE, Lansbury PT, Jr. 2000. Acceleration of oligomerization not fibrillization, is a shared property of both alpha-synuclein mutations linked to earlyonset Parkinson's disease: implications for pathogenesis and therapy. Proc Natl Acad Sci USA 97:571-576.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury P.T., Jr.6
  • 9
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway KA, Rochet JC, Bieganski RM, Lansbury PT, Jr. 2001. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294:1346-1349.
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury P.T., Jr.4
  • 10
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson W, Jonas A, Clayton D, George J. 1998. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J Biol Chem 273:9443-9449.
    • (1998) J Biol Chem , vol.273 , pp. 9443-9449
    • Davidson, W.1    Jonas, A.2    Clayton, D.3    George, J.4
  • 12
    • 0025943418 scopus 로고
    • Hippocampal degeneration differentiates diffuse Lewy body disease (DLBD) from Alzheimer's disease: Light and electron microscopic immunocytochemistry of CA2-3 neurites specific to DLBD
    • Dickson D, Ruan D, Crystal H, Mark M, Davies P, Kress Y, Yen S-H. 1991. Hippocampal degeneration differentiates diffuse Lewy body disease (DLBD) from Alzheimer's disease: Light and electron microscopic immunocytochemistry of CA2-3 neurites specific to DLBD. Neurology 41:1402-1409.
    • (1991) Neurology , vol.41 , pp. 1402-1409
    • Dickson, D.1    Ruan, D.2    Crystal, H.3    Mark, M.4    Davies, P.5    Kress, Y.6    Yen, S.-H.7
  • 13
    • 0033850190 scopus 로고    scopus 로고
    • Review: Formation and properties of amyloid-like fibrils derived from alpha-synuclein and related proteins
    • El-Agnaf O, Irvine G. 2000. Review: Formation and properties of amyloid-like fibrils derived from alpha-synuclein and related proteins. J Struct Biol 130:300-309.
    • (2000) J Struct Biol , vol.130 , pp. 300-309
    • El-Agnaf, O.1    Irvine, G.2
  • 14
    • 0034647786 scopus 로고    scopus 로고
    • Oligomerization and toxicity of beta-amyloid-42 implicated in Alzheimer's disease
    • El-Agnaf O, Mahil D, Patel B, Austen B. 2000. Oligomerization and toxicity of beta-amyloid-42 implicated in Alzheimer's disease. Biochem Biophys Res Commun 273:1003-1007.
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 1003-1007
    • El-Agnaf, O.1    Mahil, D.2    Patel, B.3    Austen, B.4
  • 15
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • Feany M, Bender W. 2000. A Drosophila model of Parkinson's disease. Nature 404:394-398.
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.1    Bender, W.2
  • 16
    • 0033679283 scopus 로고    scopus 로고
    • Polyglutamine expansions: Proteolysis, chaperones, and the dangers of promiscuity
    • Ferrigno P, Silver P. 2000. Polyglutamine expansions: proteolysis, chaperones, and the dangers of promiscuity. Neuron 26:9-12.
    • (2000) Neuron , vol.26 , pp. 9-12
    • Ferrigno, P.1    Silver, P.2
  • 17
    • 0034017710 scopus 로고    scopus 로고
    • Alphasynuclein and Parkinson's disease: Selective neurodegenerative effect of alpha-synuclein fragment on dopaminergic neurons in vitro and in vivo
    • Forloni G, Bertani I, Calella A, Thaler F, Invernizzi R. 2000. Alphasynuclein and Parkinson's disease: selective neurodegenerative effect of alpha-synuclein fragment on dopaminergic neurons in vitro and in vivo. Ann Neurol 47:632-640.
    • (2000) Ann Neurol , vol.47 , pp. 632-640
    • Forloni, G.1    Bertani, I.2    Calella, A.3    Thaler, F.4    Invernizzi, R.5
  • 19
    • 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. 2001. Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Abeta 42 fibrils. Science 293:1491-1495.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 20
    • 0030950055 scopus 로고    scopus 로고
    • Further evidence for an association between a mutation in the APP gene and Lewy body formation
    • Halliday G, Brooks W, Arthur H, Creasey H, Broe G. 1997. Further evidence for an association between a mutation in the APP gene and Lewy body formation. Neurosci Lett 227:49-52.
    • (1997) Neurosci Lett , vol.227 , pp. 49-52
    • Halliday, G.1    Brooks, W.2    Arthur, H.3    Creasey, H.4    Broe, G.5
  • 21
    • 0033919992 scopus 로고    scopus 로고
    • Lewy bodies in Alzheimer's disease: A neuropatbological review of 145 cases using alpha-synuclein immunohistochemistry
    • Hamilton RL, 2000. Lewy bodies in Alzheimer's disease: a neuropatbological review of 145 cases using alpha-synuclein immunohistochemistry. Brain Pathol 10:378-384.
    • (2000) Brain Pathol , vol.10 , pp. 378-384
    • Hamilton, R.L.1
  • 22
    • 0031283220 scopus 로고    scopus 로고
    • The Lewy body variant of Alzheimer disease
    • Hansen L. 1997. The Lewy body variant of Alzheimer disease. J Neural Transm 51:111-121.
    • (1997) J Neural Transm , vol.51 , pp. 111-121
    • Hansen, L.1
  • 23
    • 0024406472 scopus 로고
    • A neuropathologic subset of Alzheimer's disease with concomitant Lewy body disease and spongiform change
    • Hansen L, Masliah E, Terry R. 1989. A neuropathologic subset of Alzheimer's disease with concomitant Lewy body disease and spongiform change. Acta Neuropathol 78:194-201.
    • (1989) Acta Neuropathol , vol.78 , pp. 194-201
    • Hansen, L.1    Masliah, E.2    Terry, R.3
  • 25
    • 0025878695 scopus 로고
    • Entorhinal neurofibrillary tangles in Alzheimer disease with Lewy bodies
    • Hansen L, Masliah E, Quijada-Fawcett S, Rexin D. 1991. Entorhinal neurofibrillary tangles in Alzheimer disease with Lewy bodies. NeurosciLett 129:269-272.
    • (1991) Neurosci Lett , vol.129 , pp. 269-272
    • Hansen, L.1    Masliah, E.2    Quijada-Fawcett, S.3    Rexin, D.4
  • 26
    • 0033598697 scopus 로고    scopus 로고
    • Interaction between Abeta(1-42) and Abeta(1-40) in Alzheimer's beta-amyloid fibril formation in vitro
    • Hasegawa K, Yamaguchi I, Omata S, Gejyo F, Naiki H. 1999. Interaction between Abeta(1-42) and Abeta(1-40) in Alzheimer's beta-amyloid fibril formation in vitro. Biochemistry 38:15514-15521.
    • (1999) Biochemistry , vol.38 , pp. 15514-15521
    • Hasegawa, K.1    Yamaguchi, I.2    Omata, S.3    Gejyo, F.4    Naiki, H.5
  • 27
    • 0032888789 scopus 로고    scopus 로고
    • Alpha-synuclein in Lewy body disease and Alzheimer's disease
    • Hashimoto M, Masliah E, 1999. Alpha-synuclein in Lewy body disease and Alzheimer's disease. Brain Pathol 9:707-720.
    • (1999) Brain Pathol , vol.9 , pp. 707-720
    • Hashimoto, M.1    Masliah, E.2
  • 28
    • 0032551656 scopus 로고    scopus 로고
    • Human recombinant NACP/a-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease
    • Hashimoto M, Hernandez-Ruiz S, Hsu L, Sisk A, Xia Y, Takeda A, Sundsmo M, Masliah E. 1998. Human recombinant NACP/a-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease. Brain Res 799:301-306.
    • (1998) Brain Res , vol.799 , pp. 301-306
    • Hashimoto, M.1    Hernandez-Ruiz, S.2    Hsu, L.3    Sisk, A.4    Xia, Y.5    Takeda, A.6    Sundsmo, M.7    Masliah, E.8
  • 29
    • 0032879452 scopus 로고    scopus 로고
    • Role of cytochrome c as a stimulator of α-synuclein aggregation in Lewy body disease
    • Hashimoto M, Takeda A, Hsu LJ, Takenouchi T, Masliah E. 1999a. Role of cytochrome c as a stimulator of α-synuclein aggregation in Lewy body disease. J Biol Chem 274:28849-28852.
    • (1999) J Biol Chem , vol.274 , pp. 28849-28852
    • Hashimoto, M.1    Takeda, A.2    Hsu, L.J.3    Takenouchi, T.4    Masliah, E.5
  • 30
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/a-synuclein in vitro
    • Hashimoto M, Hsu L, Xia Y, Takeda A, Sundsmo M, Masliah E. 1999b. Oxidative stress induces amyloid-like aggregate formation of NACP/a-synuclein in vitro. Neuro report 10:717-721.
    • (1999) Neuro report , vol.10 , pp. 717-721
    • Hashimoto, M.1    Hsu, L.2    Xia, Y.3    Takeda, A.4    Sundsmo, M.5    Masliah, E.6
  • 31
    • 0035950270 scopus 로고    scopus 로고
    • beta-synuclein inhibits alpha-synuclein aggregation. A possible role as an anti-Parkinsonian factor
    • Hashimnoto M, Rockenstein E, Mante M, Mallory M, Masliah E. 2001. beta-synuclein inhibits alpha-synuclein aggregation. A possible role as an anti-Parkinsonian factor. Neuron 32:213-223.
    • (2001) Neuron , vol.32 , pp. 213-223
    • Hashimnoto, M.1    Rockenstein, E.2    Mante, M.3    Mallory, M.4    Masliah, E.5
  • 34
    • 0031944830 scopus 로고    scopus 로고
    • Nigral and cortical Lewy, bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity
    • Irizarry M, Growdon W, Gomez-Isla T, Newell K, George J; Clayton D, Hyman B. 1998. Nigral and cortical Lewy, bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain alpha-synuclein immunoreactivity. J Neuropathol Exp NeuroI 57:334-337.
    • (1998) J Neuropathol Exp NeuroI , vol.57 , pp. 334-337
    • Irizarry, M.1    Growdon, W.2    Gomez-Isla, T.3    Newell, K.4    George, J.5    Clayton, D.6    Hyman, B.7
  • 35
    • 0034718160 scopus 로고    scopus 로고
    • Properties of NACP/alpha-synuclein and its role in Alzheimer's disease
    • Iwai A. 2000. Properties of NACP/alpha-synuclein and its role in Alzheimer's disease. Biochim Biophys Acta 1502:95-109.
    • (2000) Biochim Biophys Acta , vol.1502 , pp. 95-109
    • Iwai, A.1
  • 36
    • 0028277520 scopus 로고
    • Identification of two distinct synucleins from human brain
    • Jakes R, Spillantini M, Goedert M. 1994. Identification of two distinct synucleins from human brain. FEBS Lett 345:27-32.
    • (1994) FEBS Lett , vol.345 , pp. 27-32
    • Jakes, R.1    Spillantini, M.2    Goedert, M.3
  • 37
    • 0030932673 scopus 로고    scopus 로고
    • Binding of Ab to a- and b-synucleins: Identification of segments in a-synuclein/NAC precursor that bind Ab and NAC
    • Jensen P, Hojrup P, Hager H, Nielsen M, Jacobsen L, Olesen O, Gliemann J, Jakes R. 1997. Binding of Ab to a- and b-synucleins: identification of segments in a-synuclein/NAC precursor that bind Ab and NAC. Biochem J 323:539-546.
    • (1997) Biochem J , vol.323 , pp. 539-546
    • Jensen, P.1    Hojrup, P.2    Hager, H.3    Nielsen, M.4    Jacobsen, L.5    Olesen, O.6    Gliemann, J.7    Jakes, R.8
  • 38
    • 0033083049 scopus 로고    scopus 로고
    • Stimulation of breast cancer invasion and metastasis by synuclein gamma
    • Jia T, Liu YE, Liu J, Shi YE. 1999. Stimulation of breast cancer invasion and metastasis by synuclein gamma. Cancer Res 59:742-747.
    • (1999) Cancer Res , vol.59 , pp. 742-747
    • Jia, T.1    Liu, Y.E.2    Liu, J.3    Shi, Y.E.4
  • 41
    • 0035815285 scopus 로고    scopus 로고
    • Release and aggregation of cytochrome c and alpha-synuclein are inhibited by the antiparkinsonian drugs, talipexole and pramipexole
    • Kakimura J, Kitamura Y, Takata K, Kohno Y, Nomura Y, Taniguchi T. 2001. Release and aggregation of cytochrome c and alpha-synuclein are inhibited by the antiparkinsonian drugs, talipexole and pramipexole. Eur J Pharmacol 417:59-67.
    • (2001) Eur J Pharmacol , vol.417 , pp. 59-67
    • Kakimura, J.1    Kitamura, Y.2    Takata, K.3    Kohno, Y.4    Nomura, Y.5    Taniguchi, T.6
  • 42
    • 0034008852 scopus 로고    scopus 로고
    • Enhanced vulnerability to oxidative stress by alpha-synuclein mutations and C-terminal truncation
    • Kanda S, Bishop J, Eglitis M, Yang Y, Mouradian M. 2000. Enhanced vulnerability to oxidative stress by alpha-synuclein mutations and C-terminal truncation. Neuroscience 97:279-284.
    • (2000) Neuroscience , vol.97 , pp. 279-284
    • Kanda, S.1    Bishop, J.2    Eglitis, M.3    Yang, Y.4    Mouradian, M.5
  • 43
    • 0025911018 scopus 로고
    • Advances in Alzheimer's disease
    • Katzman R, Saitoh T, 1991. Advances in Alzheimer's disease. FASEB J 5:278-286.
    • (1991) FASEB J , vol.5 , pp. 278-286
    • Katzman, R.1    Saitoh, T.2
  • 45
    • 0033385632 scopus 로고    scopus 로고
    • Neurotoxicity and oxidative damage of beta amyloid 1-42 versus beta amyloid 1-40 in the mouse cerebral cortex
    • Klein A, Kowall N, Ferrante R. 1999. Neurotoxicity and oxidative damage of beta amyloid 1-42 versus beta amyloid 1-40 in the mouse cerebral cortex. Ann NY Acad Sci 893:314-320.
    • (1999) Ann NY Acad Sci , vol.893 , pp. 314-320
    • Klein, A.1    Kowall, N.2    Ferrante, R.3
  • 46
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • Koo E, Lansbury PJ, Kelly J, 1999. Amyloid diseases: Abnormal protein aggregation in neurodegeneration. Proc Natl Acad Sci USA 96:9989-9990.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9989-9990
    • Koo, E.1    Lansbury, P.J.2    Kelly, J.3
  • 47
    • 0018145267 scopus 로고
    • Lewy bodies in cerebral cortex. Report of three cases
    • Kosaka K. 1978. Lewy bodies in cerebral cortex. Report of three cases. Acta Neuropathol (Berl) 42:127-134.
    • (1978) Acta Neuropathol (Berl) , vol.42 , pp. 127-134
    • Kosaka, K.1
  • 48
    • 0021636665 scopus 로고
    • Diffuse type of Lewy body disease. Progressive dementia with abundant cortical Lewy bodies and senile changes of varying degree: A new disease?
    • Kosaka K, Yoshimura M, Ikeda K, Budka H. 1984. Diffuse type of Lewy body disease. Progressive dementia with abundant cortical Lewy bodies and senile changes of varying degree: a new disease? Clin Neuropathol 3:183-192.
    • (1984) Clin Neuropathol , vol.3 , pp. 183-192
    • Kosaka, K.1    Yoshimura, M.2    Ikeda, K.3    Budka, H.4
  • 50
    • 0021155228 scopus 로고
    • MPTP-induced parkinsonism in human and non-human primates: Clinical and experimental aspects
    • Langston JW, Langston EB, Irwin I, 1984. MPTP-induced parkinsonism in human and non-human primates: clinical and experimental aspects. Acta Neurol Scand Suppl 100:49-54.
    • (1984) Acta Neurol Scand Suppl , vol.100 , pp. 49-54
    • Langston, J.W.1    Langston, E.B.2    Irwin, I.3
  • 51
    • 0037085288 scopus 로고    scopus 로고
    • Formation and removal of alpha-synuclein aggregates in cells exposed to mitochondrial inhibitors
    • Lee HJ, Shin SY, Choi C, Lee YH, Lee SJ. 2002. Formation and removal of alpha-synuclein aggregates in cells exposed to mitochondrial inhibitors. J Biol Chem 277:5411-5417.
    • (2002) J Biol Chem , vol.277 , pp. 5411-5417
    • Lee, H.J.1    Shin, S.Y.2    Choi, C.3    Lee, Y.H.4    Lee, S.J.5
  • 52
    • 0035958973 scopus 로고    scopus 로고
    • Muscarinic receptor stimulation induces translocation of an alpha-synuclein oligomer from plasma membrane to a light vesicle fraction in cytoplasm
    • Leng Y, Chase TN, Bennett MC. 2001. Muscarinic receptor stimulation induces translocation of an alpha-synuclein oligomer from plasma membrane to a light vesicle fraction in cytoplasm. J Biol Chem 276:28212-28218:
    • (2001) J Biol Chem , vol.276 , pp. 28212-28218
    • Leng, Y.1    Chase, T.N.2    Bennett, M.C.3
  • 54
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid beta protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • Lin H, Bhatia R, Lal R. 2001. Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology. Faseb J 15:2433-2444.
    • (2001) Faseb J , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 56
    • 0032887165 scopus 로고    scopus 로고
    • Deposition of beta-amyloid subtypes 40 and 42 differentiates dementia with Lewy bodies from Alzheimer diseaes
    • Lippa C, Ozawa K, Mann D, Ishii K, Smith T, Arawaka S, Mori H. 1999. Deposition of beta-amyloid subtypes 40 and 42 differentiates dementia with Lewy bodies from Alzheimer diseaes. Arch Neurol 56:1111-1118.
    • (1999) Arch Neurol , vol.56 , pp. 1111-1118
    • Lippa, C.1    Ozawa, K.2    Mann, D.3    Ishii, K.4    Smith, T.5    Arawaka, S.6    Mori, H.7
  • 57
    • 0031824433 scopus 로고    scopus 로고
    • Amyloid beta protein (A beta) deposition in dementia Lewy bodies: Predominance of A beta 42(43) and paucity of A beta 40 compared with sporadic Alzheimer's disease
    • Mann D, Brown S, Owen F, Baba M, Iwatsubo T. 1998. Amyloid beta protein (A beta) deposition in dementia Lewy bodies: predominance of A beta 42(43) and paucity of A beta 40 compared with sporadic Alzheimer's disease. NeuropathoI Appl Neurobiol 24:187-194.
    • (1998) NeuropathoI Appl Neurobiol , vol.24 , pp. 187-194
    • Mann, D.1    Brown, S.2    Owen, F.3    Baba, M.4    Iwatsubo, T.5
  • 58
    • 0034509452 scopus 로고    scopus 로고
    • The role of synaptic proteins in Alzheimer's disease
    • Masliah E, 2000a. The role of synaptic proteins in Alzheimer's disease. Ann NY Acad Sci 924:68-75.
    • (2000) Ann NY Acad Sci , vol.924 , pp. 68-75
    • Masliah, E.1
  • 59
    • 0030025635 scopus 로고    scopus 로고
    • Altered presynaptic protein NACP is associated with plaque formation and neurodegeneration in Alzheimer's disease
    • Masliah E, Iwai A, Mallory M, Ueda K, Saitoh T. 1996. Altered presynaptic protein NACP is associated with plaque formation and neurodegeneration in Alzheimer's disease. Am J Pathol 148:201-210.
    • (1996) Am J Pathol , vol.148 , pp. 201-210
    • Masliah, E.1    Iwai, A.2    Mallory, M.3    Ueda, K.4    Saitoh, T.5
  • 60
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders
    • Masliah E, Rockenstein E, Veinbergs I, Mallory M, Hashimoto M, Takeda A, Sagara, Sisk A, Mucke L. 2000b. Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders. Science 287:1265-1269.
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5    Takeda, A.6    Sagara7    Sisk, A.8    Mucke, L.9
  • 61
    • 0035834076 scopus 로고    scopus 로고
    • beta-Amyloid peptides enhance alpha-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease
    • Masliah E, Rockenstein E, Veinbergs I, Sagara Y, Mallory M, Hashimoto M, Mucke L, 2001. beta-Amyloid peptides enhance alpha-synuclein accumulation and neuronal deficits in a transgenic mouse model linking Alzheimer's disease and Parkinson's disease. Proc Natl Acad Sci USA 98:12245-12250
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12245-12250
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Sagara, Y.4    Mallory, M.5    Hashimoto, M.6    Mucke, L.7
  • 62
    • 0030609125 scopus 로고    scopus 로고
    • Abeta25-35 induces rapid lysis of red blood cells: Contrast with Abeta1-42 and examination of underlying mechanisms
    • Mattson M, Begley J, Mark R, Furukawa K. 1997. Abeta25-35 induces rapid lysis of red blood cells: contrast with Abeta1-42 and examination of underlying mechanisms. Brain Res 771:147-153.
    • (1997) Brain Res , vol.771 , pp. 147-153
    • Mattson, M.1    Begley, J.2    Mark, R.3    Furukawa, K.4
  • 64
    • 0027429156 scopus 로고
    • A new brain-specific 14-kDa protein is a phosphoprotein. Its complete amino acid sequence and evidence for phosphorylation
    • Nakajo S, Tsukada K, Omata K, Nakamura Y, Nakaya K. 1993. A new brain-specific 14-kDa protein is a phosphoprotein. Its complete amino acid sequence and evidence for phosphorylation. Eur J Biochem 217:1057-1063.
    • (1993) Eur J Biochem , vol.217 , pp. 1057-1063
    • Nakajo, S.1    Tsukada, K.2    Omata, K.3    Nakamura, Y.4    Nakaya, K.5
  • 65
    • 0035928748 scopus 로고    scopus 로고
    • Membrane binding and selfassociation of alpha-synucleins
    • Narayanan V, Scarlata S. 2001. Membrane binding and selfassociation of alpha-synucleins. Biochemistry 40:9927-9934.
    • (2001) Biochemistry , vol.40 , pp. 9927-9934
    • Narayanan, V.1    Scarlata, S.2
  • 68
    • 0034663039 scopus 로고    scopus 로고
    • The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity
    • Osterova-Golts N, Petrucelli L, Hardy J, Lee J, Farer M, Wolozin B, 2000. The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity. J Neurosci 20:6048-6054.
    • (2000) J Neurosci , vol.20 , pp. 6048-6054
    • Osterova-Golts, N.1    Petrucelli, L.2    Hardy, J.3    Lee, J.4    Farer, M.5    Wolozin, B.6
  • 69
    • 0032472212 scopus 로고    scopus 로고
    • Self-oligomerization of NACP, the precursor protien of the non-amyloid beta/A4 protein (A beta) component of Alzheimer's disease amyloid, observed in the presence of a C-terminal A beta fragment (residues 25-35)
    • Paik S, Lee J, Kim D, Chang C, Kim Y. 1998a. Self-oligomerization of NACP, the precursor protien of the non-amyloid beta/A4 protein (A beta) component of Alzheimer's disease amyloid, observed in the presence of a C-terminal A beta fragment (residues 25-35). FEBS Lett 421:73-76.
    • (1998) FEBS Lett , vol.421 , pp. 73-76
    • Paik, S.1    Lee, J.2    Kim, D.3    Chang, C.4    Kim, Y.5
  • 70
    • 0032472212 scopus 로고    scopus 로고
    • Self-oligomerization of NACP, the precursor protein of the non-amyloid beta/A4 protein (A beta) component of Alzheimer's disease amyloid observed in the presence of C-terminal A beta fragment (residues 25-35)
    • Paik S, Lee J, Kim D, Chang C, Kim Y. 1998b. Self-oligomerization of NACP, the precursor protein of the non-amyloid beta/A4 protein (A beta) component of Alzheimer's disease amyloid observed in the presence of C-terminal A beta fragment (residues 25-35). FEBS Lett 421:73-76.
    • (1998) FEBS Lett , vol.421 , pp. 73-76
    • Paik, S.1    Lee, J.2    Kim, D.3    Chang, C.4    Kim, Y.5
  • 71
    • 0033564726 scopus 로고    scopus 로고
    • Copper(II) induced self-oligomerization of alpha-synuclein
    • Paik SR, Shin HJ, Lee JH, Chang CS, Kim J. 1999. Copper(II) induced self-oligomerization of alpha-synuclein. Biochem J 340:821-828.
    • (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
  • 72
    • 0036137083 scopus 로고    scopus 로고
    • Effects of pharmacological agents upon a transgenic model of Parkinson's disease in Drosophila melanogaster
    • Pendleton RC, Parvez F, Sayed M, Hillman R. 2002. Effects of pharmacological agents upon a transgenic model of Parkinson's disease in Drosophila melanogaster. J Pharmacol Exp Ther 300:91-96.
    • (2002) J Pharmacol Exp Ther , vol.300 , pp. 91-96
    • Pendleton, R.C.1    Parvez, F.2    Sayed, M.3    Hillman, R.4
  • 73
    • 0034602271 scopus 로고    scopus 로고
    • Interaction of human alpha-synuclein and Parkinson's disease variants with phospholipids: Structural analysis using site0directed mutagenesis
    • Perrin R, Woods W, Clayton D, George J. 2000. Interaction of human alpha-synuclein and Parkinson's disease variants with phospholipids: structural analysis using site0directed mutagenesis. J Biol Chem 275:34393-34398.
    • (2000) J Biol Chem , vol.275 , pp. 34393-34398
    • Perrin, R.1    Woods, W.2    Clayton, D.3    George, J.4
  • 77
    • 0034609561 scopus 로고    scopus 로고
    • Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein
    • Rochet J, Conway K, Lansbury PJ. 2000. Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein. Biochemistry 39:10619-10626.
    • (2000) Biochemistry , vol.39 , pp. 10619-10626
    • Rochet, J.1    Conway, K.2    Lansbury, P.J.3
  • 78
    • 0036605566 scopus 로고    scopus 로고
    • Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the PDGF and Thy-1 promoters
    • Rockenstein E, Mallory, M, Hashimoto M, Song D, Shults C, Lang I, Masliah E. 2002. Differential neuropathological alterations in transgenic mice expressing alpha-synuclein from the PDGF and Thy-1 promoters. J Neurosci Res 68:568-578.
    • (2002) J Neurosci Res , vol.68 , pp. 568-578
    • Rockenstein, E.1    Mallory, M.2    Hashimoto, M.3    Song, D.4    Shults, C.5    Lang, I.6    Masliah, E.7
  • 81
    • 0030781194 scopus 로고    scopus 로고
    • Dementia with Lewy bodies versus pure Alzheimer's disease: Differences in cognition, neurpathology; cholinergic dysfunction and synapse density
    • Samuel W, Alford M, Hofstetter R, Hansen L. 1997. Dementia with Lewy bodies versus pure Alzheimer's disease: differences in cognition, neurpathology; cholinergic dysfunction and synapse density. J Neuropathol Exp Neurol 56:499-508.
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 499-508
    • Samuel, W.1    Alford, M.2    Hofstetter, R.3    Hansen, L.4
  • 82
    • 0024314702 scopus 로고
    • Amyloid β protein precursor and the pathogenesis of Alzheimer's disease
    • Selkoe D. 1989. Amyloid β protein precursor and the pathogenesis of Alzheimer's disease. Cell 58:611-612.
    • (1989) Cell , vol.58 , pp. 611-612
    • Selkoe, D.1
  • 84
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic a-synuclein filaments shows amyloid-like cross-β conformation
    • Serpell L, Berriman J, Jakes R, Goedert M, Crowther R. 2000. Fiber diffraction of synthetic a-synuclein filaments shows amyloid-like cross-β conformation. Proc Natl Acad Sci 97:4897-4902.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 4897-4902
    • Serpell, L.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.5
  • 85
    • 0034882629 scopus 로고    scopus 로고
    • Parkinson disease: Etiology, pathogenesis and future of gene therapy
    • Shastry BS. 2001. Parkinson disease: etiology, pathogenesis and future of gene therapy. Neurosci Res 41:5-12.
    • (2001) Neurosci Res , vol.41 , pp. 5-12
    • Shastry, B.S.1
  • 87
    • 0028985799 scopus 로고
    • Role of the beta-amyloid protein in Alzheimer's disease
    • Sisodia S, Price D. 1995. Role of the beta-amyloid protein in Alzheimer's disease. FASEB J 9:366-370.
    • (1995) FASEB J , vol.9 , pp. 366-370
    • Sisodia, S.1    Price, D.2
  • 88
    • 0034674652 scopus 로고    scopus 로고
    • Dityrosine cross-linking promotes formation of stable alphasynuclein polymers
    • Souza J, Giasson B, Chen Q, Lee V-Y, Ischiropoulos H. 2000. Dityrosine cross-linking promotes formation of stable alphasynuclein polymers. J Biol Chem 275:18344-18349.
    • (2000) J Biol Chem , vol.275 , pp. 18344-18349
    • Souza, J.1    Giasson, B.2    Chen, Q.3    Lee, V.-Y.4    Ischiropoulos, H.5
  • 90
    • 0030851944 scopus 로고    scopus 로고
    • Superoxide free radical and intracellular calcium mediate Abeta (1-42) induced endothelial toxicity
    • Suo Z, Fang C, Crawford F, Mullan M. 1997. Superoxide free radical and intracellular calcium mediate Abeta (1-42) induced endothelial toxicity. Brain Res 762:144-152.
    • (1997) Brain Res , vol.762 , pp. 144-152
    • Suo, Z.1    Fang, C.2    Crawford, F.3    Mullan, M.4
  • 94
    • 0031661141 scopus 로고    scopus 로고
    • Abnormal distribution of the non-Ab component of Alzheimer's disease amyloid precursor/a-synuclein in Lewy body disease as revealed by proteinase K and formic acid pretreatment
    • Takeda A, Hashimoto M, Mallory M, Sundsmo M, Hansen L, Sisk A, Masliah E. 1998b. Abnormal distribution of the non-Ab component of Alzheimer's disease amyloid precursor/a-synuclein in Lewy body disease as revealed by proteinase K and formic acid pretreatment. Lab Invest 78:1169-1177.
    • (1998) Lab Invest , vol.78 , pp. 1169-1177
    • Takeda, A.1    Hashimoto, M.2    Mallory, M.3    Sundsmo, M.4    Hansen, L.5    Sisk, A.6    Masliah, E.7
  • 95
    • 0033954218 scopus 로고    scopus 로고
    • C-terminal a-synuclein immunoreactivity in structures other than Lewy bodies in neurodegenerative disorders
    • Takeda A, Hashimoto M, Mallory M, Sundsmo M, Hansen L, Masliah E. 2000. C-terminal a-synuclein immunoreactivity in structures other than Lewy bodies in neurodegenerative disorders, Acta Neuropathol 99:296-304.
    • (2000) Acta Neuropathol , vol.99 , pp. 296-304
    • Takeda, A.1    Hashimoto, M.2    Mallory, M.3    Sundsmo, M.4    Hansen, L.5    Masliah, E.6
  • 96
    • 0031910093 scopus 로고    scopus 로고
    • Aggregation of neurofilament and alpha-synuclein proteins in Lewy bodies: Implications for pathogenesis of Parkinson disease and Lewy body dementia
    • Trojanowski J, Lee V. 1998. Aggregation of neurofilament and alpha-synuclein proteins in Lewy bodies: implications for pathogenesis of Parkinson disease and Lewy body dementia. Arch Neurol 55:151-152.
    • (1998) Arch Neurol , vol.55 , pp. 151-152
    • Trojanowski, J.1    Lee, V.2
  • 97
    • 0010862444 scopus 로고
    • Novel amyloid component (NAC) differentiates Alzheimer's disease from normal aging plaques
    • Ueda K, Masliah E, Xia Y, Iwai A, Yoshimoto M, Saitoh T, 1993. Novel amyloid component (NAC) differentiates Alzheimer's disease from normal aging plaques. Soc Neurosei Abstr 19:1254.
    • (1993) Soc Neurosei Abstr , vol.19 , pp. 1254
    • Ueda, K.1    Masliah, E.2    Xia, Y.3    Iwai, A.4    Yoshimoto, M.5    Saitoh, T.6
  • 98
    • 0037023699 scopus 로고    scopus 로고
    • Biophysical properties of the synucleins and their propensities to fibrillate: Inhibition of alpha-synuclein assembly by beta- and gamma-synucleins
    • Uversky VN, Li J, Souillac P, Jakes R, Goedert M, Fink AL. 2002. Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins. J Biol Chem 277:11970-11978.
    • (2002) J Biol Chem , vol.277 , pp. 11970-11978
    • Uversky, V.N.1    Li, J.2    Souillac, P.3    Jakes, R.4    Goedert, M.5    Fink, A.L.6
  • 100
    • 0028908034 scopus 로고
    • Amyloid precursor protein accumulation in Lewy dody dementia and Alzheimer's disease
    • Van Gool D, De Strooper B, Van Leuven F, Dom R, 1995. Amyloid precursor protein accumulation in Lewy dody dementia and Alzheimer's disease. Dementia 6:63-68.
    • (1995) Dementia , vol.6 , pp. 63-68
    • Van Gool, D.1    De Strooper, B.2    Van Leuven, F.3    Dom, R.4
  • 101
    • 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, 2000. Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity. J Struct Biol 130:184-208.
    • (2000) J Struct Biol , vol.130 , pp. 184-208
    • Varadarajan, S.1    Yatin, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 102
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein implications for the pathogenesis and treatment of Parkinson's disease
    • Volles MJ, Lee SJ, Rochet JC, Shtilerman MD, Ding TT, Kessler JC, Lansbury PT, Jr. 2001. Vesicle permeabilization by protofibrillar alpha-synuclein implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry 40:7812-7819.
    • (2001) Biochemistry , vol.40 , pp. 7812-7819
    • Volles, M.J.1    Lee, S.J.2    Rochet, J.C.3    Shtilerman, M.D.4    Ding, T.T.5    Kessler, J.C.6    Lansbury P.T., Jr.7
  • 103
    • 0028915739 scopus 로고
    • Cortical Lewy body-containing neurons are pyramidal cells: Laser confocal imaging of double-immunolabeled sections with anti-ubiquitin and SMI32
    • Wakabayashi K, Hansen L, Masliah E. 1995. Cortical Lewy body-containing neurons are pyramidal cells: laser confocal imaging of double-immunolabeled sections with anti-ubiquitin and SMI32. Acta Neuropathol 89:404-408.
    • (1995) Acta Neuropathol , vol.89 , pp. 404-408
    • Wakabayashi, K.1    Hansen, L.2    Masliah, E.3
  • 104
    • 0030639022 scopus 로고    scopus 로고
    • Neurofibrillary tangles in the dentate granule cells in Alzheimer's disease. Lewy body disease and progressive supranuclear palsy
    • Wakabayashi K, Hansen L, Vincent I, Mallory M, Masliah E. 1997. Neurofibrillary tangles in the dentate granule cells in Alzheimer's disease, Lewy body disease and progressive supranuclear palsy. Acta Neuropathol 93:7-12.
    • (1997) Acta Neuropathol , vol.93 , pp. 7-12
    • Wakabayashi, K.1    Hansen, L.2    Vincent, I.3    Mallory, M.4    Masliah, E.5
  • 105
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb P, Zhen W, Pooh A, Conway K, Lansbury PJ. 1996. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochem 35:13709-13715.
    • (1996) Biochem , vol.35 , pp. 13709-13715
    • Weinreb, P.1    Zhen, W.2    Pooh, A.3    Conway, K.4    Lansbury, P.J.5
  • 106
    • 0033538541 scopus 로고    scopus 로고
    • alpha-Synuclein fibrillogenesis is nucleation dependent. Implications for the pathogenesis of Parkinson's disease
    • Wood SJ, Wypych J, Steavenson S, Louis JC, Citron M, Biere AL. 1999. alpha-Synuclein fibrillogenesis is nucleation dependent. Implications for the pathogenesis of Parkinson's disease. J Biol Chem 274:19509-19512.
    • (1999) J Biol Chem , vol.274 , pp. 19509-19512
    • Wood, S.J.1    Wypych, J.2    Steavenson, S.3    Louis, J.C.4    Citron, M.5    Biere, A.L.6
  • 107
    • 0029056115 scopus 로고
    • NACP, the precursor protein of non-amyloid b/A4 protein (Ab) component of Alzheimer disease amyloid, binds Ab and stimulates Ab aggregation
    • Yoshimoto M. Iwai A, Kang D, Otero D, Xia Y, Saitoh T. 1995 NACP, the precursor protein of non-amyloid b/A4 protein (Ab) component of Alzheimer disease amyloid, binds Ab and stimulates Ab aggregation. Proc Natl Acad Sci USA 92:9141-9145.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9141-9145
    • Yoshimoto, M.1    Iwai, A.2    Kang, D.3    Otero, D.4    Xia, Y.5    Saitoh, T.6
  • 108
    • 0034595728 scopus 로고    scopus 로고
    • Overexpression of human alpha-synuclein causes dopmaine neuron death in rat primary culture and immortalized mesence phalon-derived cells
    • Zhou W, Hurlbert M, Schaack J, Prasad K, Freed C. 2000. Overexpression of human alpha-synuclein causes dopmaine neuron death in rat primary culture and immortalized mesence phalon-derived cells. Brain Res 866:33-4:3.
    • (2000) Brain Res , vol.866 , pp. 33-34
    • Zhou, W.1    Hurlbert, M.2    Schaack, J.3    Prasad, K.4    Freed, C.5


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