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Volumn 66, Issue 2 SUPPL. 1, 2006, Pages

Inclusion-body myositis and Alzheimer disease: Two sides of the same coin, or different currencies altogether?

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN ANTIBODY; AMYLOID BETA PROTEIN[1-42]; AMYLOID PRECURSOR PROTEIN; CLIOQUINOL; GAMMA SECRETASE INHIBITOR; GREEN TEA EXTRACT; IBUPROFEN; MESSENGER RNA; NONSTEROID ANTIINFLAMMATORY AGENT; ASPARTIC PROTEINASE; BACE1 PROTEIN, HUMAN; BACE1 PROTEIN, MOUSE; MUSCLE PROTEIN; NERVE PROTEIN; PROTEINASE; SECRETASE;

EID: 33644869496     PISSN: 00283878     EISSN: None     Source Type: Journal    
DOI: 10.1212/01.wnl.0000192108.02654.ac     Document Type: Conference Paper
Times cited : (14)

References (49)
  • 2
    • 0031728797 scopus 로고    scopus 로고
    • Sporadic inclusion-body myositis and its similarities to Alzheimer disease brain. Recent approaches to diagnosis and pathogenesis, and relation to aging
    • Askanas V, Engel WK. Sporadic inclusion-body myositis and its similarities to Alzheimer disease brain. Recent approaches to diagnosis and pathogenesis, and relation to aging. Scand J Rheumatol 1998;27:389-405.
    • (1998) Scand J Rheumatol , vol.27 , pp. 389-405
    • Askanas, V.1    Engel, W.K.2
  • 3
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001;81:741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 4
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002;297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 5
    • 0027444952 scopus 로고
    • Beta-amyloid precursor epitopes in muscle fibers of inclusion body myositis
    • Askanas V, Alvarez RB, Engel WK. Beta-amyloid precursor epitopes in muscle fibers of inclusion body myositis. Ann Neurol 1993;34:551-560.
    • (1993) Ann Neurol , vol.34 , pp. 551-560
    • Askanas, V.1    Alvarez, R.B.2    Engel, W.K.3
  • 6
    • 0035145398 scopus 로고    scopus 로고
    • Inclusion-body myositis: Newest concepts of pathogenesis and relation to aging and Alzheimer disease
    • Askanas V, Engel WK. Inclusion-body myositis: newest concepts of pathogenesis and relation to aging and Alzheimer disease. J Neuropathol Exp Neurol 2001;60:1-14.
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 1-14
    • Askanas, V.1    Engel, W.K.2
  • 7
    • 0036778097 scopus 로고    scopus 로고
    • Newest pathogenetic considerations in inclusion-body myositis: Possible role of amyloid-beta, cholesterol, relation to aging and to Alzheimer's disease
    • Askanas V, Engel WK. Newest pathogenetic considerations in inclusion-body myositis: possible role of amyloid-beta, cholesterol, relation to aging and to Alzheimer's disease. Curr Rheumatol Rep 2002;4:427-433.
    • (2002) Curr Rheumatol Rep , vol.4 , pp. 427-433
    • Askanas, V.1    Engel, W.K.2
  • 8
    • 0026695045 scopus 로고
    • Light and electron microscopic localization of beta-amyloid protein in muscle biopsies of patients with inclusion-body myositis
    • Askanas V, Engel WK, Alvarez RB. Light and electron microscopic localization of beta-amyloid protein in muscle biopsies of patients with inclusion-body myositis. Am J Pathol 1992;141:31-36.
    • (1992) Am J Pathol , vol.141 , pp. 31-36
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3
  • 9
    • 0027232988 scopus 로고
    • Beta-amyloid precursor protein mRNA is increased in inclusion-body myositis muscle
    • Sarkozi E, Askanas V, Johnson SA, Engel WK, Alvarez RB. Beta-amyloid precursor protein mRNA is increased in inclusion-body myositis muscle. Neuroreport 1993;4:815-818.
    • (1993) Neuroreport , vol.4 , pp. 815-818
    • Sarkozi, E.1    Askanas, V.2    Johnson, S.A.3    Engel, W.K.4    Alvarez, R.B.5
  • 10
    • 0029671441 scopus 로고    scopus 로고
    • Transfer of beta-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle
    • U S A
    • Askanas V, McFerrin J, Baque S, Alvarez RB, Sarkozi E, Engel WK. Transfer of beta-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle. Proc Natl Acad Sci U S A 1996;93:1314-1319.
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 1314-1319
    • Askanas, V.1    McFerrin, J.2    Baque, S.3    Alvarez, R.B.4    Sarkozi, E.5    Engel, W.K.6
  • 11
    • 0031772229 scopus 로고    scopus 로고
    • Amyloid-beta deposition in skeletal muscle of transgenic mice: Possible model of inclusion body myopathy
    • Fukuchi K, Pham D, Hart M, Li L, Lindsey JR. Amyloid-beta deposition in skeletal muscle of transgenic mice: possible model of inclusion body myopathy. Am J Pathol 1998;153:1687-1693.
    • (1998) Am J Pathol , vol.153 , pp. 1687-1693
    • Fukuchi, K.1    Pham, D.2    Hart, M.3    Li, L.4    Lindsey, J.R.5
  • 12
    • 0031740915 scopus 로고    scopus 로고
    • Transgenic mice over-expressing the C-99 fragment of betaPP with an alpha-secretase site mutation develop a myopathy similar to human inclusion body myositis
    • Jin LW, Hearn MG, Ogburn CE, et al. Transgenic mice over-expressing the C-99 fragment of betaPP with an alpha-secretase site mutation develop a myopathy similar to human inclusion body myositis. Am J Pathol 1998;153:1679-1686.
    • (1998) Am J Pathol , vol.153 , pp. 1679-1686
    • Jin, L.W.1    Hearn, M.G.2    Ogburn, C.E.3
  • 13
    • 0037197835 scopus 로고    scopus 로고
    • Inclusion body myositis-like phenotype induced by transgenic overexpression of beta APP in skeletal muscle
    • U S A
    • Sugarman MC, Yamasaki TR, Oddo S, et al. Inclusion body myositis-like phenotype induced by transgenic overexpression of beta APP in skeletal muscle. Proc Natl Acad Sci U S A 2002;99:6334-6339.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 6334-6339
    • Sugarman, M.C.1    Yamasaki, T.R.2    Oddo, S.3
  • 14
    • 0036700809 scopus 로고    scopus 로고
    • Gamma-Secretase: Substrates and inhibitors
    • Rochette MJ, Murphy MP. Gamma-Secretase: substrates and inhibitors. Mol Neurobiol 2002;26:81-95.
    • (2002) Mol Neurobiol , vol.26 , pp. 81-95
    • Rochette, M.J.1    Murphy, M.P.2
  • 15
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X, Sudhof TC. A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 2001;293:115-120.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 16
    • 0035909901 scopus 로고    scopus 로고
    • The gamma-secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus
    • U S A
    • Gao Y, Pimplikar SW. The gamma-secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus. Proc Natl Acad Sci U S A 2001;98:14979-14984.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 14979-14984
    • Gao, Y.1    Pimplikar, S.W.2
  • 17
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner
    • Kimberly WT, Zheng JB, Guenette SY, Selkoe DJ. The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner. J Biol Chem 2001;276:40288-40292.
    • (2001) J Biol Chem , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guenette, S.Y.3    Selkoe, D.J.4
  • 18
    • 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;293:1491-1495.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    Van Dorpe, J.3    Nitsch, R.M.4
  • 19
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J, Dickson DW, Lin WL, et al. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 2001;293:1487-1491.
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3
  • 20
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003;300:486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3
  • 21
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002;416:535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3
  • 22
    • 0027526419 scopus 로고
    • Release of excess amyloid β protein from a mutant amyloid A protein precursor
    • Cai X-D, Golde TE, Younkin SG. Release of excess amyloid β protein from a mutant amyloid A protein precursor. Science 1993;259:514-517.
    • (1993) Science , vol.259 , pp. 514-517
    • Cai, X.-D.1    Golde, T.E.2    Younkin, S.G.3
  • 23
    • 0026745610 scopus 로고
    • Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production
    • Citron M, Oltersdorf T, Haass C, et al. Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production. Nature 1992;360:672-674.
    • (1992) Nature , vol.360 , pp. 672-674
    • Citron, M.1    Oltersdorf, T.2    Haass, C.3
  • 24
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner D, Eckman C, Jensen M, et al. Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nat Med 1996;2:864-870.
    • (1996) Nat Med , vol.2 , pp. 864-870
    • Scheuner, D.1    Eckman, C.2    Jensen, M.3
  • 26
    • 17944368176 scopus 로고    scopus 로고
    • The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced protofibril formation
    • Nilsberth C, Westlind-Danielsson A, Eckman CB, et al. The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced protofibril formation. Nat Neurosci 2001;4:887-893.
    • (2001) Nat Neurosci , vol.4 , pp. 887-893
    • Nilsberth, C.1    Westlind-Danielsson, A.2    Eckman, C.B.3
  • 27
    • 0032491494 scopus 로고    scopus 로고
    • Genetic neurodegenerative diseases: The human illness and transgenic models
    • Price DL, Sisodia SS, Borchelt DR. Genetic neurodegenerative diseases: the human illness and transgenic models. Science 1998;282:1079-1083.
    • (1998) Science , vol.282 , pp. 1079-1083
    • Price, D.L.1    Sisodia, S.S.2    Borchelt, D.R.3
  • 28
    • 0029811901 scopus 로고    scopus 로고
    • Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: A review of 17 epidemiologic studies
    • McGeer PL, Schulzer M, McGeer EG. Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: a review of 17 epidemiologic studies. Neurology 1996;47:425-432.
    • (1996) Neurology , vol.47 , pp. 425-432
    • McGeer, P.L.1    Schulzer, M.2    McGeer, E.G.3
  • 29
    • 85047691727 scopus 로고    scopus 로고
    • NSAIDs and enantiomers of flurbiprofen target gamma-secretase and lower Abeta 42 in vivo
    • Eriksen JL, Sagi SA, Smith TE, et al. NSAIDs and enantiomers of flurbiprofen target gamma-secretase and lower Abeta 42 in vivo. J Clin Invest 2003;112:440-449.
    • (2003) J Clin Invest , vol.112 , pp. 440-449
    • Eriksen, J.L.1    Sagi, S.A.2    Smith, T.E.3
  • 30
    • 0034254924 scopus 로고    scopus 로고
    • Ibuprofen suppresses plaque pathology and inflammation in a mouse model for Alzheimer's disease
    • Lim GP, Yang F, Chu T, et al. Ibuprofen suppresses plaque pathology and inflammation in a mouse model for Alzheimer's disease. J Neurosci 2000;20:5709-5714.
    • (2000) J Neurosci , vol.20 , pp. 5709-5714
    • Lim, G.P.1    Yang, F.2    Chu, T.3
  • 31
    • 0035829592 scopus 로고    scopus 로고
    • A subset of NSAIDs lower amyloidogenic Ab42 independently of cyclooxygenase activity
    • Weggen S, Eriksen JL, Das P, et al. A subset of NSAIDs lower amyloidogenic Ab42 independently of cyclooxygenase activity. Nature 2001;414:212-216.
    • (2001) Nature , vol.414 , pp. 212-216
    • Weggen, S.1    Eriksen, J.L.2    Das, P.3
  • 32
    • 0042878457 scopus 로고    scopus 로고
    • The non-cyclooxygenase targets of non-steroidal anti-inflammatory drugs, lipoxygenases, peroxisome proliferator-activated receptor, inhibitor of kappa B kinase, and NF kappa B, do not reduce amyloid beta 42 production
    • Sagi SA, Weggen S, Eriksen J, Golde TE, Koo EH. The non-cyclooxygenase targets of non-steroidal anti-inflammatory drugs, lipoxygenases, peroxisome proliferator-activated receptor, inhibitor of kappa B kinase, and NF kappa B, do not reduce amyloid beta 42 production. J Biol Chem 2003;278:31825-31830.
    • (2003) J Biol Chem , vol.278 , pp. 31825-31830
    • Sagi, S.A.1    Weggen, S.2    Eriksen, J.3    Golde, T.E.4    Koo, E.H.5
  • 33
    • 0041876229 scopus 로고    scopus 로고
    • Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid beta 42 production by direct modulation of gamma-secretase activity
    • Weggen S, Eriksen JL, Sagi SA, et al. Evidence that nonsteroidal anti-inflammatory drugs decrease amyloid beta 42 production by direct modulation of gamma-secretase activity. J Biol Chem 2003;278:31831-31837.
    • (2003) J Biol Chem , vol.278 , pp. 31831-31837
    • Weggen, S.1    Eriksen, J.L.2    Sagi, S.A.3
  • 34
    • 6344233805 scopus 로고    scopus 로고
    • Selected Non-steroidal Anti-inflammatory Drugs and Their Derivatives Target (gamma)-Secretase at a Novel Site: Evidence for al allosteric mechanism
    • Beher D, Clarke EE, Wrigley JD, et al. Selected Non-steroidal Anti-inflammatory Drugs and Their Derivatives Target (gamma)-Secretase at a Novel Site: evidence for al allosteric mechanism. J Biol Chem 2004;279:43419-43426.
    • (2004) J Biol Chem , vol.279 , pp. 43419-43426
    • Beher, D.1    Clarke, E.E.2    Wrigley, J.D.3
  • 35
    • 7044254509 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs lower Abeta(42) and change presenilin 1 conformation
    • Lleo A, Berezovska O, Herl L, et al. Nonsteroidal anti-inflammatory drugs lower Abeta(42) and change presenilin 1 conformation. Nat Med 2004;10:1065-1066.
    • (2004) Nat Med , vol.10 , pp. 1065-1066
    • Lleo, A.1    Berezovska, O.2    Herl, L.3
  • 36
    • 21044458540 scopus 로고    scopus 로고
    • Diverse compounds mimic Alzheimer disease-causing mutations by augmenting Abeta42 production
    • Kukar T, Murphy MP, Eriksen JL, et al. Diverse compounds mimic Alzheimer disease-causing mutations by augmenting Abeta42 production. Nat Med 2005;11:545-550.
    • (2005) Nat Med , vol.11 , pp. 545-550
    • Kukar, T.1    Murphy, M.P.2    Eriksen, J.L.3
  • 37
    • 0034714316 scopus 로고    scopus 로고
    • Presenilin 1 regulates pharmacologically distinct gamma -secretase activities. Implications for the role of presenilin in gamma -secretase cleavage
    • Murphy MP, Uljon SN, Fraser PE, et al. Presenilin 1 regulates pharmacologically distinct gamma -secretase activities. Implications for the role of presenilin in gamma -secretase cleavage. J Biol Chem 2000;275:26277-26284.
    • (2000) J Biol Chem , vol.275 , pp. 26277-26284
    • Murphy, M.P.1    Uljon, S.N.2    Fraser, P.E.3
  • 38
    • 0033835996 scopus 로고    scopus 로고
    • Peripherally adminstered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer's disease
    • Bard F, Cannon C, Barbour R, et al. Peripherally adminstered antibodies against amyloid beta-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer's disease. Nat Med 2000;6:916-919.
    • (2000) Nat Med , vol.6 , pp. 916-919
    • Bard, F.1    Cannon, C.2    Barbour, R.3
  • 39
    • 0034700471 scopus 로고    scopus 로고
    • A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
    • Janus C, Pearson J, McLaurin J, et al. A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature 2000;408:979-982.
    • (2000) Nature , vol.408 , pp. 979-982
    • Janus, C.1    Pearson, J.2    McLaurin, J.3
  • 40
    • 0035106780 scopus 로고    scopus 로고
    • Imaging of amyloid-beta deposits in brains of living mice permits direct observation of clearance of plaques with immunotherapy
    • Bacskai BJ, Kajdasz ST, Christie RH, et al. Imaging of amyloid-beta deposits in brains of living mice permits direct observation of clearance of plaques with immunotherapy. Nat Med 2001;7:369-372.
    • (2001) Nat Med , vol.7 , pp. 369-372
    • Bacskai, B.J.1    Kajdasz, S.T.2    Christie, R.H.3
  • 41
    • 0034746897 scopus 로고    scopus 로고
    • Reduced effectiveness of Abeta1-42 immunization in APP transgenic mice with significant amyloid deposition
    • Das P, Murphy MP, Younkin LH, Younkin SG, Golde TE. Reduced effectiveness of Abeta1-42 immunization in APP transgenic mice with significant amyloid deposition. Neurobiol Aging 2001;22:721-727.
    • (2001) Neurobiol Aging , vol.22 , pp. 721-727
    • Das, P.1    Murphy, M.P.2    Younkin, L.H.3    Younkin, S.G.4    Golde, T.E.5
  • 42
    • 0035902619 scopus 로고    scopus 로고
    • Peripheral anti-A beta antibody alters CNS and plasma a beta clearance and decreases brain a beta burden in a mouse model of Alzheimer's disease
    • U S A
    • DeMattos RB, Bales KR, Cummins DJ, Dodart JC, Paul SM, Holtzman DM. Peripheral anti-A beta antibody alters CNS and plasma A beta clearance and decreases brain A beta burden in a mouse model of Alzheimer's disease. Proc Natl Acad Sci U S A 2001;98:8850-8855.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 8850-8855
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3    Dodart, J.C.4    Paul, S.M.5    Holtzman, D.M.6
  • 43
    • 84984755327 scopus 로고    scopus 로고
    • A beta peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
    • Morgan D, Diamond DM, Gottschall PE, et al. A beta peptide vaccination prevents memory loss in an animal model of Alzheimer's disease. Nature 2000;408:982-985.
    • (2000) Nature , vol.408 , pp. 982-985
    • Morgan, D.1    Diamond, D.M.2    Gottschall, P.E.3
  • 44
    • 0033622324 scopus 로고    scopus 로고
    • Intraneuronal Abeta42 accumulation in human brain
    • Gouras GK, Tsai J, Naslund J, et al. Intraneuronal Abeta42 accumulation in human brain. Am J Pathol 2000;156:15-20.
    • (2000) Am J Pathol , vol.156 , pp. 15-20
    • Gouras, G.K.1    Tsai, J.2    Naslund, J.3
  • 45
    • 0030793522 scopus 로고    scopus 로고
    • Neuronal cell death in Alzheimer's disease correlates with apoE uptake and intracellular Abeta stabilization
    • LaFerla FM, Troncoso JC, Strickland DK, Kawas CH, Jay G. Neuronal cell death in Alzheimer's disease correlates with apoE uptake and intracellular Abeta stabilization. J Clin Invest 1997;100:310-320.
    • (1997) J Clin Invest , vol.100 , pp. 310-320
    • LaFerla, F.M.1    Troncoso, J.C.2    Strickland, D.K.3    Kawas, C.H.4    Jay, G.5
  • 46
    • 0029057814 scopus 로고
    • Intracellular A beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells
    • Yang AJ, Knauer M, Burdick DA, Glabe C. Intracellular A beta 1-42 aggregates stimulate the accumulation of stable, insoluble amyloidogenic fragments of the amyloid precursor protein in transfected cells. J Biol Chem 1995;270:14786-14792.
    • (1995) J Biol Chem , vol.270 , pp. 14786-14792
    • Yang, A.J.1    Knauer, M.2    Burdick, D.A.3    Glabe, C.4
  • 47
    • 4043167747 scopus 로고    scopus 로고
    • Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome
    • Oddo S, Billings L, Kesslak JP, Cribbs DH, LaFerla FM. Abeta immunotherapy leads to clearance of early, but not late, hyperphosphorylated tau aggregates via the proteasome. Neuron 2004;43:321-332.
    • (2004) Neuron , vol.43 , pp. 321-332
    • Oddo, S.1    Billings, L.2    Kesslak, J.P.3    Cribbs, D.H.4    LaFerla, F.M.5
  • 48
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice
    • Cherny RA, Atwood CS, Xilinas ME, et al. Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 2001;30:665-676.
    • (2001) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1    Atwood, C.S.2    Xilinas, M.E.3
  • 49
    • 0038661168 scopus 로고    scopus 로고
    • Neuroprotection and neurorescue against Abeta toxicity and PKC-dependent release of nonamyloidogenic soluble precursor protein by green tea polyphenol (-)-epigallocatechin-3-gallate
    • Levites Y, Amit T, Mandel S, Youdim MB. Neuroprotection and neurorescue against Abeta toxicity and PKC-dependent release of nonamyloidogenic soluble precursor protein by green tea polyphenol (-)-epigallocatechin-3-gallate. Faseb J 2003;17:952-954.
    • (2003) Faseb J , vol.17 , pp. 952-954
    • Levites, Y.1    Amit, T.2    Mandel, S.3    Youdim, M.B.4


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