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Volumn 2, Issue 1, 2006, Pages 43-55

Synaptic targeting by Aβ oligomers (ADDLS) as a basis for memory loss in early Alzheimer's disease

Author keywords

Actin; Arc; Diagnostics; Glutamate receptors; Plasticity; ROS; Spines; Tau phosphorylation; Therapeutics

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; DONEPEZIL; LIGAND; MEMANTINE; OLIGOMER;

EID: 33144484368     PISSN: 15525260     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jalz.2005.11.003     Document Type: Review
Times cited : (110)

References (98)
  • 1
    • 0030801772 scopus 로고    scopus 로고
    • Diagnosis and treatment of Alzheimer disease and related disorders. Consensus statement of the American Association for Geriatric Psychiatry, the Alzheimer's Association, and the American Geriatrics Society
    • G.W. Small P.V. Rabins P.P. Barry N.S. Buckholtz S.T. DeKosky S.H. Ferris et al. Diagnosis and treatment of Alzheimer disease and related disorders. Consensus statement of the American Association for Geriatric Psychiatry, the Alzheimer's Association, and the American Geriatrics Society JAMA 278 16 1997 1363-1371
    • (1997) JAMA , vol.278 , Issue.16 , pp. 1363-1371
    • Small, G.W.1    Rabins, P.V.2    Barry, P.P.3    Buckholtz, N.S.4    DeKosky, S.T.5    Ferris, S.H.6
  • 2
    • 0346656621 scopus 로고    scopus 로고
    • A clinical review of current and emerging indications
    • G.C. Roman S.J. Rogers Donepezil A clinical review of current and emerging indications Expert Opin Pharmacother 5 1 2004 161-180
    • (2004) Expert Opin Pharmacother , vol.5 , Issue.1 , pp. 161-180
    • Roman, G.C.1    Rogers, S.J.2    Donepezil3
  • 4
    • 0026758654 scopus 로고
    • Alzheimer's debate boils over
    • J. Marx Alzheimer's debate boils over Science 257 5075 1992 1336-1338
    • (1992) Science , vol.257 , Issue.5075 , pp. 1336-1338
    • Marx, J.1
  • 5
    • 0027447286 scopus 로고
    • Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state
    • C.J. Pike D. Burdick A.J. Walencewicz C.G. Glabe C.W. Cotman Neurodegeneration induced by beta-amyloid peptides in vitro: The role of peptide assembly state J Neurosci 13 4 1993 1676-1687
    • (1993) J Neurosci , vol.13 , Issue.4 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 6
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red
    • A. Lorenzo B.A. Yankner Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red Proc Natl Acad Sci U S A 91 25 1994 12243-12247
    • (1994) Proc Natl Acad Sci U S A , vol.91 , Issue.25 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 7
    • 0002665739 scopus 로고    scopus 로고
    • Aβ toxicity in Alzheimer's disease
    • M.F. Chesselet Humana Press, Inc Totowa, New Jersey
    • W.L. Klein Aβ toxicity in Alzheimer's disease M.F. Chesselet Molecular mechanisms of neurodegenerative diseases 2001 Humana Press, Inc Totowa, New Jersey 1-49
    • (2001) Molecular Mechanisms of Neurodegenerative Diseases , pp. 1-49
    • Klein, W.L.1
  • 8
    • 0027944208 scopus 로고
    • Beta/A4-evoked degeneration of differentiated SH-SY5Y human neuroblastoma cells
    • M.P. Lambert G. Stevens S. Sabo K. Barber G. Wang W. Wade et al. Beta/ A4-evoked degeneration of differentiated SH-SY5Y human neuroblastoma cells J Neurosci Res 39 4 1994 377-385
    • (1994) J Neurosci Res , vol.39 , Issue.4 , pp. 377-385
    • Lambert, M.P.1    Stevens, G.2    Sabo, S.3    Barber, K.4    Wang, G.5    Wade, W.6
  • 9
    • 0028986916 scopus 로고
    • Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • J. Busciglio A. Lorenzo J. Yeh B.A. Yankner beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding Neuron 14 4 1995 879-888
    • (1995) Neuron , vol.14 , Issue.4 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 11
    • 0027988046 scopus 로고
    • Focal adhesion kinase expressed by nerve cell lines shows increased tyrosine phosphorylation in response to Alzheimer's A beta peptide
    • C. Zhang M.P. Lambert C. Bunch K. Barber W.S. Wade G.A. Krafft et al. Focal adhesion kinase expressed by nerve cell lines shows increased tyrosine phosphorylation in response to Alzheimer's A beta peptide J Biol Chem 269 41 1994 25247-25250
    • (1994) J Biol Chem , vol.269 , Issue.41 , pp. 25247-25250
    • Zhang, C.1    Lambert, M.P.2    Bunch, C.3    Barber, K.4    Wade, W.S.5    Krafft, G.A.6
  • 12
    • 0030604667 scopus 로고    scopus 로고
    • A beta peptide enhances focal adhesion kinase/Fyn association in a rat CNS nerve cell line
    • C. Zhang H.E. Qiu G.A. Krafft W.L. Klein A beta peptide enhances focal adhesion kinase/Fyn association in a rat CNS nerve cell line Neurosci Lett 211 3 1996 187-190
    • (1996) Neurosci Lett , vol.211 , Issue.3 , pp. 187-190
    • Zhang, C.1    Qiu, H.E.2    Krafft, G.A.3    Klein, W.L.4
  • 13
    • 0032955426 scopus 로고    scopus 로고
    • Insulin transiently increases tau phosphorylation: Involvement of glycogen synthase kinase-3beta and Fyn tyrosine kinase
    • M. Lesort R.S. Jope G.V. Johnson Insulin transiently increases tau phosphorylation: Involvement of glycogen synthase kinase-3beta and Fyn tyrosine kinase J Neurochem 72 2 1999 576-584
    • (1999) J Neurochem , vol.72 , Issue.2 , pp. 576-584
    • Lesort, M.1    Jope, R.S.2    Johnson, G.V.3
  • 14
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • J.A. Hardy G.A. Higgins Alzheimer's disease: The amyloid cascade hypothesis Science 256 5054 1992 184-185
    • (1992) Science , vol.256 , Issue.5054 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 15
    • 0033536163 scopus 로고    scopus 로고
    • Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse
    • D. Schenk R. Barbour W. Dunn G. Gordon H. Grajeda T. Guido Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse Nature 400 6740 1999 173-177
    • (1999) Nature , vol.400 , Issue.6740 , pp. 173-177
    • Schenk, D.1    Barbour, R.2    Dunn, W.3    Gordon, G.4    Grajeda, H.5    Guido, T.6
  • 16
    • 0036240395 scopus 로고    scopus 로고
    • Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model
    • J.C. Dodart K.R. Bales K.S. Gannon S.J. Greene R.B. DeMattos C. Mathis et al. Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model Nat Neurosci 5 (5) 2002 452-457
    • (2002) Nat Neurosci , vol.5 , Issue.5 , pp. 452-457
    • Dodart, J.C.1    Bales, K.R.2    Gannon, K.S.3    Greene, S.J.4    DeMattos, R.B.5    Mathis, C.6
  • 18
    • 0023905906 scopus 로고
    • Clinical, pathological, and neurochemical changes in dementia: A subgroup with preserved mental status and numerous neocortical plaques
    • R. Katzman R. Terry R. DeTeresa T. Brown P. Davies P. Fuld et al. Clinical, pathological, and neurochemical changes in dementia: A subgroup with preserved mental status and numerous neocortical plaques Ann Neurol 23 2 1988 138-144
    • (1988) Ann Neurol , vol.23 , Issue.2 , pp. 138-144
    • Katzman, R.1    Terry, R.2    DeTeresa, R.3    Brown, T.4    Davies, P.5    Fuld, P.6
  • 19
    • 0002080057 scopus 로고    scopus 로고
    • The neuropathology of Alzheimer disease and the structural basis of its cognitive alterations
    • R.D. Terry R. Katzman K.L. Bick S.S. Sisodia Lippincott Williams, & Wilkins Philadelphia, PA
    • R.D. Terry The neuropathology of Alzheimer disease and the structural basis of its cognitive alterations R.D. Terry R. Katzman K.L. Bick S.S. Sisodia Alzheimer disease 1999 Lippincott Williams, & Wilkins Philadelphia, PA 187-206
    • (1999) Alzheimer Disease , pp. 187-206
    • Terry, R.D.1
  • 20
    • 0006325405 scopus 로고    scopus 로고
    • Alzheimer's disease A re-examination of the amyloid hypothesis
    • R.L. Neve N.K. Robakis Alzheimer's disease A re-examination of the amyloid hypothesis Trends Neurosci 21 1 1998 15-19
    • (1998) Trends Neurosci , vol.21 , Issue.1 , pp. 15-19
    • Neve, R.L.1    Robakis, N.K.2
  • 21
    • 2442664058 scopus 로고    scopus 로고
    • Amyloid-beta deposition is associated with decreased hippocampal glucose metabolism and spatial memory impairment in APP/PS1 mice
    • M. Sadowski J. Pankiewicz H. Scholtzova Y. Ji D. Quartermain C.H. Jensen Amyloid-beta deposition is associated with decreased hippocampal glucose metabolism and spatial memory impairment in APP/PS1 mice J Neuropathol Exp Neurol 63 5 2004 418-428
    • (2004) J Neuropathol Exp Neurol , vol.63 , Issue.5 , pp. 418-428
    • Sadowski, M.1    Pankiewicz, J.2    Scholtzova, H.3    Ji, Y.4    Quartermain, D.5    Jensen, C.H.6
  • 23
    • 0028828044 scopus 로고
    • Clusterin (apoJ) alters the aggregation of amyloid beta-peptide (A beta 1-42) and forms slowly sedimenting A beta complexes that cause oxidative stress
    • T. Oda P. Wals H.H. Osterburg S.A. Johnson G.M. Pasinetti T.E. Morgan et al. Clusterin (apoJ) alters the aggregation of amyloid beta-peptide (A beta 1-42) and forms slowly sedimenting A beta complexes that cause oxidative stress Exp Neurol 136 1 1995 22-31
    • (1995) Exp Neurol , vol.136 , Issue.1 , pp. 22-31
    • Oda, T.1    Wals, P.2    Osterburg, H.H.3    Johnson, S.A.4    Pasinetti, G.M.5    Morgan, T.E.6
  • 24
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins
    • M.P. Lambert A.K. Barlow B.A. Chromy C. Edwards R. Freed M. Liosatos et al. Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins Proc Natl Acad Sci U S A 95 11 1998 6448-6453
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.11 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 25
    • 0029670277 scopus 로고    scopus 로고
    • The nanometer-scale structure of amyloid-beta visualized by atomic force microscopy
    • W.B. Stine Jr S.W. Snyder U.S. Ladror W.S. Wade M.F. Miller T.J. Perun et al. The nanometer-scale structure of amyloid-beta visualized by atomic force microscopy J Protein Chem 15 2 1996 193-203
    • (1996) J Protein Chem , vol.15 , Issue.2 , pp. 193-203
    • Stine, W.B.1    Snyder, S.W.2    Ladror, U.S.3    Wade, W.S.4    Miller, M.F.5    Perun, T.J.6
  • 26
    • 0035993237 scopus 로고    scopus 로고
    • Aβ toxicity in Alzheimer's disease Globular oligomers (ADDLs) as new vaccine and drug targets
    • W.L. Klein Aβ toxicity in Alzheimer's disease Globular oligomers (ADDLs) as new vaccine and drug targets Neurochem Int 41 5 2002 345
    • (2002) Neurochem Int , vol.41 , Issue.5 , pp. 345
    • Klein, W.L.1
  • 27
    • 0034740197 scopus 로고    scopus 로고
    • Vaccination with soluble Aβ oligomers generates toxicity-neutralizing antibodies
    • M.P. Lambert K.L. Viola B.A. Chromy L. Chang T.E. Morgan J. Yu et al. Vaccination with soluble Aβ oligomers generates toxicity-neutralizing antibodies J Neurochem 79 3 2001 595-605
    • (2001) J Neurochem , vol.79 , Issue.3 , pp. 595-605
    • Lambert, M.P.1    Viola, K.L.2    Chromy, B.A.3    Chang, L.4    Morgan, T.E.5    Yu, J.6
  • 29
    • 0028832472 scopus 로고
    • Soluble multimeric Alzheimer beta(1-40) pre-amyloid complexes in dilute solution
    • H. Levine III Soluble multimeric Alzheimer beta(1-40) pre-amyloid complexes in dilute solution Neurobiol Aging 16 5 1995 755-764
    • (1995) Neurobiol Aging , vol.16 , Issue.5 , pp. 755-764
    • Levine III, H.1
  • 31
    • 7444247272 scopus 로고    scopus 로고
    • Alzheimer's beta-peptide oligomer formation at physiologic concentrations
    • H. Levine III Alzheimer's beta-peptide oligomer formation at physiologic concentrations Anal Biochem 335 1 2004 81-90
    • (2004) Anal Biochem , vol.335 , Issue.1 , pp. 81-90
    • Levine III, H.1
  • 32
    • 0242479694 scopus 로고    scopus 로고
    • Femtomole immunodetection of synthetic and endogenous Amyloid-β oligomers and its application to Alzheimer's Disease drug candidate screening
    • L. Chang L. Bakhos Z. Wang D.L. Venton W.L. Klein Femtomole immunodetection of synthetic and endogenous Amyloid-β oligomers and its application to Alzheimer's Disease drug candidate screening J Mol Neurosci 20 3 2003 305-313
    • (2003) J Mol Neurosci , vol.20 , Issue.3 , pp. 305-313
    • Chang, L.1    Bakhos, L.2    Wang, Z.3    Venton, D.L.4    Klein, W.L.5
  • 33
    • 12144282992 scopus 로고    scopus 로고
    • Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Aβ peptides
    • X. Huang C.S. Atwood R.D. Moir M.A. Hartshorn R.E. Tanzi A.I. Bush Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Aβ peptides J Biol Inorg Chem 9 8 2004 954-960
    • (2004) J Biol Inorg Chem , vol.9 , Issue.8 , pp. 954-960
    • Huang, X.1    Atwood, C.S.2    Moir, R.D.3    Hartshorn, M.A.4    Tanzi, R.E.5    Bush, A.I.6
  • 35
    • 0037059598 scopus 로고    scopus 로고
    • Soluble oligomers of beta amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus
    • H.W. Wang J.F. Pasternak H. Kuo H. Ristic M.P. Lambert B. Chromy et al. Soluble oligomers of beta amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus Brain Res 924 2 2002 133-140
    • (2002) Brain Res , vol.924 , Issue.2 , pp. 133-140
    • Wang, H.W.1    Pasternak, J.F.2    Kuo, H.3    Ristic, H.4    Lambert, M.P.5    Chromy, B.6
  • 36
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Y. Gong L. Chang K.L. Viola P.N. Lacor M.P. Lambert C.E. Finch Alzheimer's disease-affected brain Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss Proc Natl Acad Sci U S A 100 18 2003 10417-10422
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.18 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6
  • 38
    • 0035967909 scopus 로고    scopus 로고
    • AMPA receptor trafficking and the control of synaptic transmission
    • M. Sheng S.H. Lee AMPA receptor trafficking and the control of synaptic transmission Cell 105 7 2001 825-828
    • (2001) Cell , vol.105 , Issue.7 , pp. 825-828
    • Sheng, M.1    Lee, S.H.2
  • 39
    • 33144468050 scopus 로고    scopus 로고
    • ADDLs (Aβ oligomers) alter structure and function of synaptic spines
    • 2004 Abstract Viewer/Itinerary Planner Washington, DC: Society for Neuroscience[Online], Program No. 218.3
    • P.N. Lacor M.C. Buniel W.L. Klein ADDLs (Aβ oligomers) alter structure and function of synaptic spines 2004 2004 Abstract Viewer/ Itinerary Planner Washington, DC: Society for Neuroscience[Online], Program No. 218.3
    • (2004)
    • Lacor, P.N.1    Buniel, M.C.2    Klein, W.L.3
  • 40
    • 33144468800 scopus 로고    scopus 로고
    • Changes in NMDA receptor subunit 1 and 2B expression in ADDL-treated hippocampal neurons
    • 2005 Abstract Viewer/Itinerary Planner Washington, DC: Society for Neuroscience[Online], Program No. 786.17
    • P.N. Lacor A. Sanz-Clemente K.L. Viola W.L. Klein Changes in NMDA receptor subunit 1 and 2B expression in ADDL-treated hippocampal neurons 2005 2005 Abstract Viewer/Itinerary Planner Washington, DC: Society for Neuroscience[Online], Program No. 786.17
    • (2005)
    • Lacor, P.N.1    Sanz-Clemente, A.2    Viola, K.L.3    Klein, W.L.4
  • 42
    • 0037271080 scopus 로고    scopus 로고
    • Selective neuronal degeneration induced by soluble oligomeric amyloid beta protein
    • H.J. Kim S.C. Chae D.K. Lee B. Chromy S.C. Lee Y.C. Park et al. Selective neuronal degeneration induced by soluble oligomeric amyloid beta protein FASEB J 17 1 2003 118-120
    • (2003) FASEB J , vol.17 , Issue.1 , pp. 118-120
    • Kim, H.J.1    Chae, S.C.2    Lee, D.K.3    Chromy, B.4    Lee, S.C.5    Park, Y.C.6
  • 43
    • 27844510969 scopus 로고    scopus 로고
    • Mechanism of impairment of long-term potentiation by amyloid beta is independent of NMDA receptors or voltage-dependent calcium channels in hippocampal CA1 pyramidal neurons
    • I. Nomura N. Kato T. Kita H. Takechi Mechanism of impairment of long-term potentiation by amyloid beta is independent of NMDA receptors or voltage-dependent calcium channels in hippocampal CA1 pyramidal neurons Neurosci Lett 2005
    • (2005) Neurosci Lett
    • Nomura, I.1    Kato, N.2    Kita, T.3    Takechi, H.4
  • 44
    • 22544485048 scopus 로고    scopus 로고
    • Amyloid-beta peptide inhibits activation of the nitric oxide/cGMP/ cAMP-responsive element-binding protein pathway during hippocampal synaptic plasticity
    • D. Puzzo O. Vitolo F. Trinchese J.P. Jacob A. Palmeri O. Arancio Amyloid-beta peptide inhibits activation of the nitric oxide/cGMP/ cAMP-responsive element-binding protein pathway during hippocampal synaptic plasticity J Neurosci 25 29 2005 6887-6897
    • (2005) J Neurosci , vol.25 , Issue.29 , pp. 6887-6897
    • Puzzo, D.1    Vitolo, O.2    Trinchese, F.3    Jacob, J.P.4    Palmeri, A.5    Arancio, O.6
  • 45
    • 21044453723 scopus 로고    scopus 로고
    • Amyloid beta protein immunotherapy neutralizes Aβ oligomers that disrupt synaptic plasticity in vivo
    • I. Klyubin D.M. Walsh C.A. Lemere W.K. Cullen G.M. Shankar V. Betts et al. Amyloid beta protein immunotherapy neutralizes Aβ oligomers that disrupt synaptic plasticity in vivo Nat Med 11 5 2005 556-561
    • (2005) Nat Med , vol.11 , Issue.5 , pp. 556-561
    • Klyubin, I.1    Walsh, D.M.2    Lemere, C.A.3    Cullen, W.K.4    Shankar, G.M.5    Betts, V.6
  • 46
    • 14944378094 scopus 로고    scopus 로고
    • Certain inhibitors of synthetic amyloid beta-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation
    • D.M. Walsh M. Townsend M.B. Podlisny G.M. Shankar J.V. Fadeeva O.E. Agnaf et al. Certain inhibitors of synthetic amyloid beta-peptide (Aβ) fibrillogenesis block oligomerization of natural Aβ and thereby rescue long-term potentiation J Neurosci 25 10 2005 2455-2462
    • (2005) J Neurosci , vol.25 , Issue.10 , pp. 2455-2462
    • Walsh, D.M.1    Townsend, M.2    Podlisny, M.B.3    Shankar, G.M.4    Fadeeva, J.V.5    Agnaf, O.E.6
  • 48
    • 2942626182 scopus 로고    scopus 로고
    • Soluble Arctic amyloid beta protein inhibits hippocampal long-term potentiation in vivo
    • I. Klyubin D.M. Walsh W.K. Cullen J.V. Fadeeva R. Anwyl D.J. Selkoe et al. Soluble Arctic amyloid beta protein inhibits hippocampal long-term potentiation in vivo Eur J Neurosci 19 10 2004 2839-2846
    • (2004) Eur J Neurosci , vol.19 , Issue.10 , pp. 2839-2846
    • Klyubin, I.1    Walsh, D.M.2    Cullen, W.K.3    Fadeeva, J.V.4    Anwyl, R.5    Selkoe, D.J.6
  • 49
    • 1842610852 scopus 로고    scopus 로고
    • Block of long-term potentiation by naturally secreted and synthetic amyloid beta-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5
    • Q. Wang D.M. Walsh M.J. Rowan D.J. Selkoe R. Anwyl Block of long-term potentiation by naturally secreted and synthetic amyloid beta-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5 J Neurosci 24 13 2004 3370-3378
    • (2004) J Neurosci , vol.24 , Issue.13 , pp. 3370-3378
    • Wang, Q.1    Walsh, D.M.2    Rowan, M.J.3    Selkoe, D.J.4    Anwyl, R.5
  • 50
    • 0036792096 scopus 로고    scopus 로고
    • Amyloid beta -peptide inhibition of the PKA/CREB pathway and long-term potentiation: Reversibility by drugs that enhance cAMP signaling
    • O.V. Vitolo A. Sant'Angelo V. Costanzo F. Battaglia O. Arancio M. Shelanski Amyloid beta -peptide inhibition of the PKA/CREB pathway and long-term potentiation: Reversibility by drugs that enhance cAMP signaling Proc Natl Acad Sci U S A 99 20 2002 13217-13221
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.20 , pp. 13217-13221
    • Vitolo, O.V.1    Sant'Angelo, A.2    Costanzo, V.3    Battaglia, F.4    Arancio, O.5    Shelanski, M.6
  • 51
    • 0034069795 scopus 로고    scopus 로고
    • Impairment of hippocampal long-term potentiation by Alzheimer amyloid beta-peptides
    • Q.S. Chen B.L. Kagan Y. Hirakura C.W. Xie Impairment of hippocampal long-term potentiation by Alzheimer amyloid beta-peptides J Neurosci Res 60 1 2000 65-72
    • (2000) J Neurosci Res , vol.60 , Issue.1 , pp. 65-72
    • Chen, Q.S.1    Kagan, B.L.2    Hirakura, Y.3    Xie, C.W.4
  • 52
    • 23444433225 scopus 로고    scopus 로고
    • Agonists of peroxisome proliferator-activated receptor-gamma attenuate the Aβ-mediated impairment of LTP in the hippocampus in vitro
    • D.A. Costello D.M. O'Leary C.E. Herron Agonists of peroxisome proliferator-activated receptor-gamma attenuate the Aβ-mediated impairment of LTP in the hippocampus in vitro Neuropharmacology 49 3 2005 359-366
    • (2005) Neuropharmacology , vol.49 , Issue.3 , pp. 359-366
    • Costello, D.A.1    O'Leary, D.M.2    Herron, C.E.3
  • 53
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • D.M. Walsh I. Klyubin J.V. Fadeeva W.K. Cullen R. Anwyl M.S. Wolfe et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo Nature 416 6880 2002 535-539
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6
  • 54
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • J. Hardy D.J. Selkoe The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics Science 297 5580 2002 353-356
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 55
    • 47549083199 scopus 로고    scopus 로고
    • Cytotoxic intermediates in the fibrillation pathway Aβ oligomers in Alzheimer's disease as a case study
    • Uversky V, (editors) Kluwer Academic/Plenum Publishers New York, NY
    • W.L. Klein Cytotoxic intermediates in the fibrillation pathway Aβ oligomers in Alzheimer's disease as a case study V. Uversky Protein misfolding, aggregation, and conformational diseases 2005 Kluwer Academic/Plenum Publishers New York, NY
    • (2005) Protein Misfolding, Aggregation, and Conformational Diseases
    • Klein, W.L.1
  • 56
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset: Parkinson's disease Implications for pathogenesis and therapy
    • K.A. Conway S.J. Lee J.C. Rochet T.T. Ding R.E. Williamson P.T. Lansbury Jr Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease Implications for pathogenesis and therapy Proc Natl Acad Sci U S A 97 2 2000 571-576
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.2 , 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.6
  • 57
    • 1542357685 scopus 로고    scopus 로고
    • Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture
    • N. Reixach S. Deechongkit X. Jiang J.W. Kelly J.N. Buxbaum Tissue damage in the amyloidoses Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture Proc Natl Acad Sci U S A 101 9 2004 2817-2822
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.9 , pp. 2817-2822
    • Reixach, N.1    Deechongkit, S.2    Jiang, X.3    Kelly, J.W.4    Buxbaum, J.N.5
  • 58
    • 0042822112 scopus 로고    scopus 로고
    • Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: Evidence for role of islet amyloid formation rather than direct action of amyloid
    • A.E. Butler J. Janson W.C. Soeller P.C. Butler Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes Evidence for role of islet amyloid formation rather than direct action of amyloid Diabetes 52 9 2003 2304-2314
    • (2003) Diabetes , vol.52 , Issue.9 , pp. 2304-2314
    • Butler, A.E.1    Janson, J.2    Soeller, W.C.3    Butler, P.C.4
  • 60
    • 0028171110 scopus 로고
    • Non-fibrillar beta-amyloid protein is associated with smooth muscle cells of vessel walls in Alzheimer disease
    • J. Frackowiak A. Zoltowska H.M. Wisniewski Non-fibrillar beta-amyloid protein is associated with smooth muscle cells of vessel walls in Alzheimer disease J Neuropathol Exp Neurol 53 6 1994 637-645
    • (1994) J Neuropathol Exp Neurol , vol.53 , Issue.6 , pp. 637-645
    • Frackowiak, J.1    Zoltowska, A.2    Wisniewski, H.M.3
  • 61
    • 33144484915 scopus 로고    scopus 로고
    • ADDL-generated monoclonal antibodies target epitopes specific to Aβ oligomers
    • 2003 Abstract Viewer/Itinerary Planner Washington, DC: Society for Neuroscience[Online], Program No. 527.16
    • M.P. Lambert P.N. Lacor L. Chang K.L. Viola P.T. Velasco D.K. Richardson et al. ADDL-generated monoclonal antibodies target epitopes specific to Aβ oligomers 2003 2003 Abstract Viewer/Itinerary Planner Washington, DC: Society for Neuroscience[Online], Program No. 527.16
    • (2003)
    • Lambert, M.P.1    Lacor, P.N.2    Chang, L.3    Viola, K.L.4    Velasco, P.T.5    Richardson, D.K.6
  • 63
  • 64
    • 0042697305 scopus 로고    scopus 로고
    • Triple-transgenic model of Alzheimer's disease with plaques and tangles: Intracellular Aβ and synaptic dysfunction
    • S. Oddo A. Caccamo J.D. Shepherd M.P. Murphy T.E. Golde R. Kayed Triple-transgenic model of Alzheimer's disease with plaques and tangles Intracellular Aβ and synaptic dysfunction Neuron 39 3 2003 409-421
    • (2003) Neuron , vol.39 , Issue.3 , pp. 409-421
    • Oddo, S.1    Caccamo, A.2    Shepherd, J.D.3    Murphy, M.P.4    Golde, T.E.5    Kayed, R.6
  • 65
    • 33144487701 scopus 로고    scopus 로고
    • Temporal profile of Aβ oligomerization in an in vivo model of Alzheimer's disease: A link between Aβ and tau pathology
    • S. Oddo A. Caccamo L. Tram M.P. Lambert C.G. Glabe W.L. Klein et al. Temporal profile of Aβ oligomerization in an in vivo model of Alzheimer's disease: A link between Aβ and tau pathology J Biol Chem 281 3 2006 1599-1604
    • (2006) J Biol Chem , vol.281 , Issue.3 , pp. 1599-1604
    • Oddo, S.1    Caccamo, A.2    Tram, L.3    Lambert, M.P.4    Glabe, C.G.5    Klein, W.L.6
  • 67
    • 0033230623 scopus 로고    scopus 로고
    • Neuroplasticity failure in Alzheimer's disease: Bridging the gap between plaques and tangles
    • M.M. Mesulam Neuroplasticity failure in Alzheimer's disease: Bridging the gap between plaques and tangles Neuron 24 3 1999 521-529
    • (1999) Neuron , vol.24 , Issue.3 , pp. 521-529
    • Mesulam, M.M.1
  • 68
    • 33144469349 scopus 로고    scopus 로고
    • Temporal memory deficits in Alzheimer's mouse models: Rescue by genetic deletion of BACE1 with reduced amyloid-β oligomers
    • In press
    • Ohno M, Chang L, Tseng W, Oakley H, Citron M, Klein WL, et al. Temporal memory deficits in Alzheimer's mouse models: Rescue by genetic deletion of BACE1 with reduced amyloid-β oligomers. Eur J Neurosci. In press.
    • Eur J Neurosci.
    • Ohno, M.1    Chang, L.2    Tseng, W.3    Oakley, H.4    Citron, M.5    Klein, W.L.6
  • 70
    • 1842732209 scopus 로고    scopus 로고
    • Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain
    • R.H. Takahashi C.G. Almeida P.F. Kearney F. Yu M.T. Lin T.A. Milner et al. Oligomerization of Alzheimer's beta-amyloid within processes and synapses of cultured neurons and brain J Neurosci 24 14 2004 3592-3599
    • (2004) J Neurosci , vol.24 , Issue.14 , pp. 3592-3599
    • Takahashi, R.H.1    Almeida, C.G.2    Kearney, P.F.3    Yu, F.4    Lin, M.T.5    Milner, T.A.6
  • 71
    • 10744232413 scopus 로고    scopus 로고
    • Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound-B
    • W.E. Klunk H. Engler A. Nordberg Y. Wang G. Blomqvist D.P. Holt et al. Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound-B Ann Neurol 55 3 2004 306-319
    • (2004) Ann Neurol , vol.55 , Issue.3 , pp. 306-319
    • Klunk, W.E.1    Engler, H.2    Nordberg, A.3    Wang, Y.4    Blomqvist, G.5    Holt, D.P.6
  • 72
    • 33144487132 scopus 로고    scopus 로고
    • Composition and methods for non-invasive imaging of soluble beta-amyloid
    • New York/USA patent US 2004/0223909 A1. 2004 Nov 2004
    • Montalto MC, Agdeppa ED, Siclovan TM, Williams AC. Composition and methods for non-invasive imaging of soluble beta-amyloid. New York/USA patent US 2004/0223909 A1. 2004 Nov 2004.
    • Montalto, M.C.1    Agdeppa, E.D.2    Siclovan, T.M.3    Williams, A.C.4
  • 73
    • 14044279957 scopus 로고    scopus 로고
    • Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer's disease
    • D.G. Georganopoulou L. Chang J.M. Nam C.S. Thaxton E.J. Mufson W.L. Klein et al. Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer's disease Proc Natl Acad Sci U S A 102 7 2005 2273-2276
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.7 , pp. 2273-2276
    • Georganopoulou, D.G.1    Chang, L.2    Nam, J.M.3    Thaxton, C.S.4    Mufson, E.J.5    Klein, W.L.6
  • 74
    • 0034659732 scopus 로고    scopus 로고
    • Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons: Maintenance of core components independent of actin filaments and microtubules
    • D.W. Allison A.S. Chervin V.I. Gelfand A.M. Craig Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons: maintenance of core components independent of actin filaments and microtubules J Neurosci 20 12 2000 4545-4554
    • (2000) J Neurosci , vol.20 , Issue.12 , pp. 4545-4554
    • Allison, D.W.1    Chervin, A.S.2    Gelfand, V.I.3    Craig, A.M.4
  • 75
    • 15944369335 scopus 로고    scopus 로고
    • Spine architecture and synaptic plasticity
    • H.J. Carlisle M.B. Kennedy Spine architecture and synaptic plasticity Trends Neurosci 28 4 2005 182-187
    • (2005) Trends Neurosci , vol.28 , Issue.4 , pp. 182-187
    • Carlisle, H.J.1    Kennedy, M.B.2
  • 76
    • 0035708355 scopus 로고    scopus 로고
    • Dendritic spine geometry is critical for AMPA receptor expression in hippocampal CA1 pyramidal neurons
    • M. Matsuzaki G.C. Ellis-Davies T. Nemoto Y. Miyashita M. Iino H. Kasai Dendritic spine geometry is critical for AMPA receptor expression in hippocampal CA1 pyramidal neurons Nat Neurosci 4 11 2001 1086-1092
    • (2001) Nat Neurosci , vol.4 , Issue.11 , pp. 1086-1092
    • Matsuzaki, M.1    Ellis-Davies, G.C.2    Nemoto, T.3    Miyashita, Y.4    Iino, M.5    Kasai, H.6
  • 77
    • 0036082812 scopus 로고    scopus 로고
    • Dendritic spine pathology: Cause or consequence of neurological disorders?
    • J.C. Fiala J. Spacek K.M. Harris Dendritic spine pathology: Cause or consequence of neurological disorders? Brain Res Brain Res Rev 39 1 2002 29-54
    • (2002) Brain Res Brain Res Rev , vol.39 , Issue.1 , pp. 29-54
    • Fiala, J.C.1    Spacek, J.2    Harris, K.M.3
  • 78
    • 4444223956 scopus 로고    scopus 로고
    • Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model mouse model
    • F. Calon G.P. Lim F. Yang T. Morihara B. Teter O. Ubeda et al. Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model Neuron 43 5 2004 633-645
    • (2004) Neuron , vol.43 , Issue.5 , pp. 633-645
    • Calon, F.1    Lim, G.P.2    Yang, F.3    Morihara, T.4    Teter, B.5    Ubeda, O.6
  • 79
    • 0344329878 scopus 로고    scopus 로고
    • Health benefits of docosahexaenoic acid (DHA)
    • L.A. Horrocks Y.K. Yeo Health benefits of docosahexaenoic acid (DHA) Pharmacol Res 40 3 1999 211-225
    • (1999) Pharmacol Res , vol.40 , Issue.3 , pp. 211-225
    • Horrocks, L.A.1    Yeo, Y.K.2
  • 80
    • 0037650162 scopus 로고    scopus 로고
    • Low serum cholesteryl ester-docosahexaenoic acid levels in Alzheimer's disease
    • A.M. Tully H.M. Roche R. Doyle C. Fallon I. Bruce B. Lawlor et al. Low serum cholesteryl ester-docosahexaenoic acid levels in Alzheimer's disease A case-control study Br J Nutr 89 4 2003 483-489
    • (2003) Br J Nutr , vol.89 , Issue.4 , pp. 483-489
    • Tully, A.M.1    Roche, H.M.2    Doyle, R.3    Fallon, C.4    Bruce, I.5    Lawlor, B.6
  • 81
    • 0034213297 scopus 로고    scopus 로고
    • Inhibition of activity-dependent arc protein expression in the rat hippocampus impairs the maintenance of long-term potentiation and the consolidation of long-term memory
    • J.F. Guzowski G.L. Lyford G.D. Stevenson F.P. Houston J.L. McGaugh P.F. Worley et al. Inhibition of activity-dependent arc protein expression in the rat hippocampus impairs the maintenance of long-term potentiation and the consolidation of long-term memory J Neurosci 20 11 2000 3993-4001
    • (2000) J Neurosci , vol.20 , Issue.11 , pp. 3993-4001
    • Guzowski, J.F.1    Lyford, G.L.2    Stevenson, G.D.3    Houston, F.P.4    McGaugh, J.L.5    Worley, P.F.6
  • 82
    • 0036881893 scopus 로고    scopus 로고
    • Local synthesis of proteins at synaptic sites on dendrites Role in synaptic plasticity and memory consolidation?
    • O. Steward P. Worley Local synthesis of proteins at synaptic sites on dendrites Role in synaptic plasticity and memory consolidation? Neurobiol Learn Mem 78 3 2002 508-527
    • (2002) Neurobiol Learn Mem , vol.78 , Issue.3 , pp. 508-527
    • Steward, O.1    Worley, P.2
  • 83
    • 0036200702 scopus 로고    scopus 로고
    • Insights into immediate-early gene function in hippocampal memory consolidation using antisense oligonucleotide and fluorescent imaging approaches
    • J.F. Guzowski Insights into immediate-early gene function in hippocampal memory consolidation using antisense oligonucleotide and fluorescent imaging approaches Hippocampus 12 1 2002 86-104
    • (2002) Hippocampus , vol.12 , Issue.1 , pp. 86-104
    • Guzowski, J.F.1
  • 84
    • 0041342036 scopus 로고    scopus 로고
    • Experience-dependent regulation of the immediate-early gene arc differs across brain regions
    • M.P. Kelly S.A. Deadwyler Experience-dependent regulation of the immediate-early gene arc differs across brain regions J Neurosci 23 16 2003 6443-6451
    • (2003) J Neurosci , vol.23 , Issue.16 , pp. 6443-6451
    • Kelly, M.P.1    Deadwyler, S.A.2
  • 86
    • 27144530643 scopus 로고    scopus 로고
    • Vulnerability of dentate granule cells to disruption of arc expression in human amyloid precursor protein transgenic mice
    • J.J. Palop J. Chin N. Bien-Ly C. Massaro B.Z. Yeung G.Q. Yu et al. Vulnerability of dentate granule cells to disruption of arc expression in human amyloid precursor protein transgenic mice J Neurosci 25 42 2005 9686-9693
    • (2005) J Neurosci , vol.25 , Issue.42 , pp. 9686-9693
    • Palop, J.J.1    Chin, J.2    Bien-Ly, N.3    Massaro, C.4    Yeung, B.Z.5    Yu, G.Q.6
  • 87
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of Aβ 1-42 in wild-type human amyloid protein precursor transgenic mice Synaptotoxicity without plaque formation
    • L. Mucke E. Masliah G.Q. Yu M. Mallory E.M. Rockenstein G. Tatsuno et al. High-level neuronal expression of Aβ 1-42 in wild-type human amyloid protein precursor transgenic mice Synaptotoxicity without plaque formation J Neurosci 20 11 2000 4050-4058
    • (2000) J Neurosci , vol.20 , Issue.11 , pp. 4050-4058
    • Mucke, L.1    Masliah, E.2    Yu, G.Q.3    Mallory, M.4    Rockenstein, E.M.5    Tatsuno, G.6
  • 88
    • 0035907325 scopus 로고    scopus 로고
    • Beta -amyloid-(1-42) impairs activity-dependent cAMP-response element-binding protein signaling in neurons at concentrations in which cell survival Is not compromised
    • L. Tong P.L. Thornton R. Balazs C.W. Cotman Beta -amyloid-(1-42) impairs activity-dependent cAMP-response element-binding protein signaling in neurons at concentrations in which cell survival Is not compromised J Biol Chem 276 20 2001 17301-17306
    • (2001) J Biol Chem , vol.276 , Issue.20 , pp. 17301-17306
    • Tong, L.1    Thornton, P.L.2    Balazs, R.3    Cotman, C.W.4
  • 89
    • 0033794593 scopus 로고    scopus 로고
    • Reversible inactivation of superoxide-sensitive aconitase in Aβ1-42-treated neuronal cell lines
    • V.D. Longo K.L. Viola W.L. Klein C.E. Finch Reversible inactivation of superoxide-sensitive aconitase in Aβ1-42-treated neuronal cell lines J Neurochem 75 5 2000 1977-1985
    • (2000) J Neurochem , vol.75 , Issue.5 , pp. 1977-1985
    • Longo, V.D.1    Viola, K.L.2    Klein, W.L.3    Finch, C.E.4
  • 90
    • 0036602967 scopus 로고    scopus 로고
    • Exercise: A behavioral intervention to enhance brain health and plasticity
    • C.W. Cotman N.C. Berchtold Exercise A behavioral intervention to enhance brain health and plasticity Trends Neurosci 25 6 2002 295-301
    • (2002) Trends Neurosci , vol.25 , Issue.6 , pp. 295-301
    • Cotman, C.W.1    Berchtold, N.C.2
  • 91
    • 0037133172 scopus 로고    scopus 로고
    • The brain-derived neurotrophic factor enhances synthesis of Arc in synaptoneurosomes
    • Y. Yin G.M. Edelman P.W. Vanderklish The brain-derived neurotrophic factor enhances synthesis of Arc in synaptoneurosomes Proc Natl Acad Sci U S A 99 4 2002 2368-2373
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.4 , pp. 2368-2373
    • Yin, Y.1    Edelman, G.M.2    Vanderklish, P.W.3
  • 92
    • 20044373636 scopus 로고    scopus 로고
    • Endurance exercise training increases insulin responsiveness in isolated adipocytes through IRS/PI3-kinase/Akt pathway
    • S.B. Peres S.M. de Moraes C.E. Costa L.C. Brito J. Takada S. Andreotti et al. Endurance exercise training increases insulin responsiveness in isolated adipocytes through IRS/PI3-kinase/Akt pathway J Appl Physiol 98 3 2005 1037-1043
    • (2005) J Appl Physiol , vol.98 , Issue.3 , pp. 1037-1043
    • Peres, S.B.1    de Moraes, S.M.2    Costa, C.E.3    Brito, L.C.4    Takada, J.5    Andreotti, S.6
  • 93
    • 0028267440 scopus 로고
    • Normal and abnormal biologyof the beta-amyloid precursor protein
    • D.J. Selkoe Normal and abnormal biologyof the beta-amyloid precursor protein Annu Rev Neurosci 17 1994 489-517
    • (1994) Annu Rev Neurosci , vol.17 , pp. 489-517
    • Selkoe, D.J.1
  • 94
    • 12544258201 scopus 로고    scopus 로고
    • Secretase inhibitors for Alzheimer's disease: Challenges of a promiscuous protease
    • S.J. Pollack H. Lewis Secretase inhibitors for Alzheimer's disease challenges of a promiscuous protease Curr Opin Investig Drugs 6 1 2005 35-47
    • (2005) Curr Opin Investig Drugs , vol.6 , Issue.1 , pp. 35-47
    • Pollack, S.J.1    Lewis, H.2
  • 95
    • 1042265187 scopus 로고    scopus 로고
    • Neuropathology and pathogenesis of encephalitis following amyloid-beta immunization in Alzheimer's disease
    • I. Ferrer R.M. Boada M.L. Sanchez Guerra M.J. Rey F. Costa-Jussa Neuropathology and pathogenesis of encephalitis following amyloid-beta immunization in Alzheimer's disease Brain Pathol 14 1 2004 11-20
    • (2004) Brain Pathol , vol.14 , Issue.1 , pp. 11-20
    • Ferrer, I.1    Boada, R.M.2    Sanchez Guerra, M.L.3    Rey, M.J.4    Costa-Jussa, F.5
  • 96
    • 0035297712 scopus 로고    scopus 로고
    • Targeting small Aβ oligomers The solution to an Alzheimer's disease conundrum?
    • W.L. Klein G.A. Krafft C.E. Finch Targeting small Aβ oligomers The solution to an Alzheimer's disease conundrum? Trends Neurosci 24 4 2001 219-224
    • (2001) Trends Neurosci , vol.24 , Issue.4 , pp. 219-224
    • Klein, W.L.1    Krafft, G.A.2    Finch, C.E.3
  • 98
    • 2942544246 scopus 로고    scopus 로고
    • Per-6-substituted-per-6-deoxy beta-cyclodextrins inhibit the formation of beta-amyloid peptide derived soluble oligomers
    • Z. Wang L. Chang W.L. Klein G.R. Thatcher D.L. Venton Per-6-substituted-per-6-deoxy beta-cyclodextrins inhibit the formation of beta-amyloid peptide derived soluble oligomers J Med Chem 47 13 2004 3329-3333
    • (2004) J Med Chem , vol.47 , Issue.13 , pp. 3329-3333
    • Wang, Z.1    Chang, L.2    Klein, W.L.3    Thatcher, G.R.4    Venton, D.L.5


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