메뉴 건너뛰기




Volumn 39, Issue 2, 2006, Pages 167-201

Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; AMYLOID BETA PROTEIN; BACTERIAL TOXIN; HUNTINGTIN; ION CHANNEL; POLYGLUTAMINE; PRION PROTEIN; SUPEROXIDE DISMUTASE; VIRULENCE FACTOR;

EID: 33750365052     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583506004422     Document Type: Review
Times cited : (347)

References (308)
  • 1
    • 33644543761 scopus 로고    scopus 로고
    • Expanding insights of mitochondrial dysfunction in Parkinson's disease
    • ABOU-SLEIMAN, P. M., MUQIT, M. M. & WOOD, N. W. (2006). Expanding insights of mitochondrial dysfunction in Parkinson's disease. Nature Reviews Neuroscience 7, 207-219.
    • (2006) Nature Reviews Neuroscience , vol.7 , pp. 207-219
    • Abou-Sleiman, P.M.1    Muqit, M.M.2    Wood, N.W.3
  • 3
    • 0029661902 scopus 로고    scopus 로고
    • Alpha-1-antichymotrypsin interaction with a beta (1-40) inhibits fibril formation but does not affect the peptide toxicity
    • AKSENOVA, M. V., AKSENOV, M. Y., BUTTERFIELD, D. A. & CARNEY, J. M. (1996). alpha-1-antichymotrypsin interaction with A beta (1-40) inhibits fibril formation but does not affect the peptide toxicity. Neuroscience Letters 211, 45-48.
    • (1996) Neuroscience Letters , vol.211 , pp. 45-48
    • Aksenova, M.V.1    Aksenov, M.Y.2    Butterfield, D.A.3    Carney, J.M.4
  • 4
    • 30344445381 scopus 로고    scopus 로고
    • Ion channel formation by Alzheimer's disease amyloid beta-peptide (Abeta40) in unilamellar liposomes is determined by anionic phospholipids
    • ALARCON, J. M., BRITO, J. A., HERMOSILLA, T., ATWATER, I., MEARS, D. & ROJAS, E. (2006). Ion channel formation by Alzheimer's disease amyloid beta-peptide (Abeta40) in unilamellar liposomes is determined by anionic phospholipids. Peptides 27, 95-104.
    • (2006) Peptides , vol.27 , pp. 95-104
    • Alarcon, J.M.1    Brito, J.A.2    Hermosilla, T.3    Atwater, I.4    Mears, D.5    Rojas, E.6
  • 5
    • 0037167613 scopus 로고    scopus 로고
    • Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes
    • ANGUIANO, M., NOWAK, R. J. & LANSBURY JR., P. T. (2002). Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. Biochemistry 41, 11338-11343.
    • (2002) Biochemistry , vol.41 , pp. 11338-11343
    • Anguiano, M.1    Nowak, R.J.2    Lansbury Jr., P.T.3
  • 6
    • 0036793543 scopus 로고    scopus 로고
    • Plasma membrane cholesterol controls the cytotoxicity of Alzheimer's disease AbetaP (1-40) and (1-42) Peptides
    • ARISPE, N. & DOH, M. (2002). Plasma membrane cholesterol controls the cytotoxicity of Alzheimer's disease AbetaP (1-40) and (1-42) Peptides. Faseb Journal 16, 1526-1536.
    • (2002) Faseb Journal , vol.16 , pp. 1526-1536
    • Arispe, N.1    Doh, M.2
  • 7
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes
    • ARISPE, N., POLLARD, H. B. & ROJAS, E. (1993a). Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes. Proceedings of the National Academy of Sciences USA 90, 10573-10577.
    • (1993) Proceedings of the National Academy of Sciences USA , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 10
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum
    • ARISPE, N., ROJAS, E. & POLLARD, H. B. (1993b). Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. Proceedings of the National Academy of Sciences USA 90, 567-571.
    • (1993) Proceedings of the National Academy of Sciences USA , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 14
    • 0141679530 scopus 로고    scopus 로고
    • Ion channels formed with a synthetic mutant prion protein (PrP[[LB]]82-146[[RB]]) homologous to a 7 kDa fragment found in the diseased brain of Gerstmann-Straussler-Scheinker syndrome
    • BAHADI, R., FARRELLY, P. V., KENNA, B. L., KOURIE, J. I., TAGLIAVINI, F., FORLONI, G. & SALMONA, M. (2003c). Ion channels formed with a synthetic mutant prion protein (PrP[[LB]]82-146[[RB]]) homologous to a 7 kDa fragment found in the diseased brain of Gerstmann-Straussler-Scheinker syndrome. American Journal of Physiology - Cell Physiology 285, C862-C872.
    • (2003) American Journal of Physiology - Cell Physiology , vol.285
    • Bahadi, R.1    Farrelly, P.V.2    Kenna, B.L.3    Kourie, J.I.4    Tagliavini, F.5    Forloni, G.6    Salmona, M.7
  • 19
    • 0036498430 scopus 로고    scopus 로고
    • Small is not beautiful: Antagonizing functions for the prion protein PrP(C) and its homologue Dpl
    • BEHRENS, A. & AGUZZI, A. (2002). Small is not beautiful: antagonizing functions for the prion protein PrP(C) and its homologue Dpl. Trends in Neurosciences 25, 150-154.
    • (2002) Trends in Neurosciences , vol.25 , pp. 150-154
    • Behrens, A.1    Aguzzi, A.2
  • 20
    • 4444288866 scopus 로고    scopus 로고
    • Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones
    • BEN-ZVI, A., DE LOS RIOS, P., DIETLER, G. & GOLOUBINOFF, P. (2004). Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones. Journal of Biological Chemistry 279, 37298-37303.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 37298-37303
    • Ben-Zvi, A.1    De Los Rios, P.2    Dietler, G.3    Goloubinoff, P.4
  • 21
    • 0035783169 scopus 로고    scopus 로고
    • Review: Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones
    • BEN-ZVI, A. P. & GOLOUBINOFF, P. (2001). Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones. Journal of Structural Biology 135, 84-93.
    • (2001) Journal of Structural Biology , vol.135 , pp. 84-93
    • Ben-Zvi, A.P.1    Goloubinoff, P.2
  • 22
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • BENNETT, E. J., BENCE, N. F., JAYAKUMAR, R. & KOPITO, R. R. (2005). Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Molecular Cell 17, 351-365.
    • (2005) Molecular Cell , vol.17 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 23
    • 0038689039 scopus 로고    scopus 로고
    • Protein aggregation and the ubiquitin proteasome pathway: Gaining the upper hand on neurodegeneration
    • BERKE, S. J. & PAULSON, H. L. (2003). Protein aggregation and the ubiquitin proteasome pathway: gaining the upper hand on neurodegeneration. Current Opinion in Genetics & Development 13, 253-261.
    • (2003) Current Opinion in Genetics & Development , vol.13 , pp. 253-261
    • Berke, S.J.1    Paulson, H.L.2
  • 24
    • 0034087948 scopus 로고    scopus 로고
    • Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: Evidence for AbetaP channel-mediated cellular toxicity
    • BHATIA, R., LIN, H. & LAL, R. (2000). Fresh and globular amyloid beta protein (1-42) induces rapid cellular degeneration: evidence for AbetaP channel-mediated cellular toxicity. FASEB Journal 14, 1233-1243.
    • (2000) FASEB Journal , vol.14 , pp. 1233-1243
    • Bhatia, R.1    Lin, H.2    Lal, R.3
  • 25
    • 14444268768 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis. Insights from genetics
    • BROWN JR., R. H. (1997). Amyotrophic lateral sclerosis. Insights from genetics. Archives of Neurology 54, 1246-1250.
    • (1997) Archives of Neurology , vol.54 , pp. 1246-1250
    • Brown Jr., R.H.1
  • 28
    • 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
    • BUTLER, A. E., JANSON, J., SOELLER, W. C. & BUTLER, P. C. (2003). 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, 2304-2314.
    • (2003) Diabetes , vol.52 , pp. 2304-2314
    • Butler, A.E.1    Janson, J.2    Soeller, W.C.3    Butler, P.C.4
  • 31
    • 0036295080 scopus 로고    scopus 로고
    • Transthyretin fibrillogenesis entails the assembly of monomers: A molecular model for in vitro assembled transthyretin amyloid-like fibrils
    • CARDOSO, I., GOLDSBURY, C. S., MULLER, S. A., OLIVIERI, V., WIRTZ, S., DAMAS, A. M., AEBI, U. & SARAIVA, M. J. (2002a). Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils. Journal of Molecular Biology 317, 683-695.
    • (2002) Journal of Molecular Biology , vol.317 , pp. 683-695
    • Cardoso, I.1    Goldsbury, C.S.2    Muller, S.A.3    Olivieri, V.4    Wirtz, S.5    Damas, A.M.6    Aebi, U.7    Saraiva, M.J.8
  • 32
    • 0036440686 scopus 로고    scopus 로고
    • Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase
    • CARDOSO, R. M., THAYER, M. M., DIDONATO, M., LO, T. P., BRUNS, C. K., GETZOFF, E. D. & TAINER, J. A. (2002b). Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase. Journal of Molecular Biology 324, 247-256.
    • (2002) Journal of Molecular Biology , vol.324 , pp. 247-256
    • Cardoso, R.M.1    Thayer, M.M.2    Didonato, M.3    Lo, T.P.4    Bruns, C.K.5    Getzoff, E.D.6    Tainer, J.A.7
  • 33
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • CAUGHEY, B. & LANSBURY, P. T. (2003). Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annual Review of Neuroscience 26, 267-298.
    • (2003) Annual Review of Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 34
    • 17844406856 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
    • CHEN, L. & FEANY, M. B. (2005). Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nature Neuroscience 8, 657-663.
    • (2005) Nature Neuroscience , vol.8 , pp. 657-663
    • Chen, L.1    Feany, M.B.2
  • 35
    • 0035168351 scopus 로고    scopus 로고
    • Prion diseases: What is the neurotoxic molecule?
    • CHIESA, R. & HARRIS, D. A. (2001). Prion diseases: what is the neurotoxic molecule? Neurobiology of Disease Journal 8, 743-763.
    • (2001) Neurobiology of Disease Journal , vol.8 , pp. 743-763
    • Chiesa, R.1    Harris, D.A.2
  • 42
    • 0031787871 scopus 로고    scopus 로고
    • Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
    • CONWAY, K. A., HARPER, J. D. & LANSBURY, P. T. (1998). Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nature Medicine 4, 1318-1320.
    • (1998) Nature Medicine , vol.4 , pp. 1318-1320
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 43
    • 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
    • CONWAY, K. A., LEE, S. J., ROCHET, J. C., DING, T. T., WILLIAMSON, R. E. & LANSBURY JR., P. T. (2000). 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. Proceedings of the National Academy of Sciences USA 97, 571-576.
    • (2000) Proceedings of the National Academy of Sciences 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 Jr., P.T.6
  • 44
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • CONWAY, K. A., ROCHET, J. C., BIEGANSKI, R. M. & LANSBURY JR., P. T. (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 Jr., P.T.4
  • 45
    • 22244442489 scopus 로고    scopus 로고
    • The biochemistry of Parkinson's disease
    • COOKSON, M. R. (2005). The biochemistry of Parkinson's disease. Annual Review of Biochemistry 74, 29-52.
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 29-52
    • Cookson, M.R.1
  • 47
    • 0037474240 scopus 로고    scopus 로고
    • Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid
    • CURTAIN, C. C., ALI, F. E., SMITH, D. G., BUSH, A. I., MASTERS, C. L. & BARNHAM, K. J. (2003). Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid. Journal of Biological Chemistry 278, 2977-2982.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 2977-2982
    • Curtain, C.C.1    Ali, F.E.2    Smith, D.G.3    Bush, A.I.4    Masters, C.L.5    Barnham, K.J.6
  • 49
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • DAUER, W. & PRZEDBORSKI, S. (2003). Parkinson's disease: mechanisms and models. Neuron 39, 889-909.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 51
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • DEMURO, A., MINA, E., KAYED, R., MILTON, S. C., PARKER, I. & GLABE, C. G. (2005). Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. Journal of Biological Chemistry 280, 17294-17300.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 52
    • 0037072284 scopus 로고    scopus 로고
    • Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes
    • DING, T. T., LEE, S. J., ROCHET, J. C. & LANSBURY JR., P. T. (2002). Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. Biochemistry 41, 10209-10217.
    • (2002) Biochemistry , vol.41 , pp. 10209-10217
    • Ding, T.T.1    Lee, S.J.2    Rochet, J.C.3    Lansbury Jr., P.T.4
  • 55
    • 0242351798 scopus 로고    scopus 로고
    • Cholesterol modulates amyloid beta-peptide's membrane interactions
    • ECKERT, G. P., KIRSCH, C., LEUTZ, S., WOOD, W. G. & MULLER, W. E. (2003). Cholesterol modulates amyloid beta-peptide's membrane interactions. Pharmacopsychiatry 36 (Suppl. 2), S136-S143.
    • (2003) Pharmacopsychiatry , vol.36 , Issue.SUPPL. 2
    • Eckert, G.P.1    Kirsch, C.2    Leutz, S.3    Wood, W.G.4    Muller, W.E.5
  • 56
    • 0032573289 scopus 로고    scopus 로고
    • Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's disease
    • EL-AGNAF, O. M., JAKES, R., CURRAN, M.D. & WALLACE, A. (1998). Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's disease. FEBS Letters 440, 67-70.
    • (1998) FEBS Letters , vol.440 , pp. 67-70
    • El-Agnaf, O.M.1    Jakes, R.2    Curran, M.D.3    Wallace, A.4
  • 58
    • 0035967889 scopus 로고    scopus 로고
    • Non-fibrillar oligomeric species of the amyloid ABri peptide, implicated in familial British dementia, are more potent at inducing apoptotic cell death than protofibrils or mature fibrils
    • EL-AGNAF, O. M., NAGALA, S., PATEL, B. P. & AUSTEN, B. M. (2001a). Non-fibrillar oligomeric species of the amyloid ABri peptide, implicated in familial British dementia, are more potent at inducing apoptotic cell death than protofibrils or mature fibrils. Journal of Molecular Biology 310, 157-168.
    • (2001) Journal of Molecular Biology , vol.310 , pp. 157-168
    • El-Agnaf, O.M.1    Nagala, S.2    Patel, B.P.3    Austen, B.M.4
  • 60
    • 0035957220 scopus 로고    scopus 로고
    • Effect of the disulfide bridge and the C-terminal extension on the oligomerization of the amyloid peptide ABri implicated in familial British dementia
    • EL-AGNAF, O. M., SHERIDAN, J. M., SIDERA, C., SILIGARDI, G., HUSSAIN, R., HARIS, P. I. & AUSTEN, B. M. (2001b). Effect of the disulfide bridge and the C-terminal extension on the oligomerization of the amyloid peptide ABri implicated in familial British dementia. Biochemistry 40, 3449-3457.
    • (2001) Biochemistry , vol.40 , pp. 3449-3457
    • El-Agnaf, O.M.1    Sheridan, J.M.2    Sidera, C.3    Siligardi, G.4    Hussain, R.5    Haris, P.I.6    Austen, B.M.7
  • 63
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • FEANY, M. B. & BENDER, W. W. (2000). A Drosophila model of Parkinson's disease. Nature 404, 394-398.
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 64
    • 16344363800 scopus 로고    scopus 로고
    • Altered proteasome structure, function, and oxidation in aged muscle
    • FERRINGTON, D. A., HUSOM, A. D. & THOMPSON, L. V. (2005). Altered proteasome structure, function, and oxidation in aged muscle. FASEB Journal 19, 644-646.
    • (2005) FASEB Journal , vol.19 , pp. 644-646
    • Ferrington, D.A.1    Husom, A.D.2    Thompson, L.V.3
  • 65
    • 0032791073 scopus 로고    scopus 로고
    • Pharmacologic management of Alzheimer disease part III: Nonsteroidal antiinflammatory drugs - Emerging protective evidence?
    • FLYNN, B. L. & THEESEN, K. A. (1999). Pharmacologic management of Alzheimer disease part III: nonsteroidal antiinflammatory drugs - emerging protective evidence? Annals of Pharmacotherapy 33, 840-849.
    • (1999) Annals of Pharmacotherapy , vol.33 , pp. 840-849
    • Flynn, B.L.1    Theesen, K.A.2
  • 67
    • 0032983254 scopus 로고    scopus 로고
    • Presence of sodium dodecyl sulfate-stable amyloid beta-protein dimers in the hippocampus CA1 not exhibiting neurofibrillary tangle formation
    • FUNATO, H., ENYA, M., YOSHIMURA, M., MORISHIMA-KAWASHIMA, M. & IHARA, Y. (1999). Presence of sodium dodecyl sulfate-stable amyloid beta-protein dimers in the hippocampus CA1 not exhibiting neurofibrillary tangle formation. American Journal of Pathology 155, 23-28.
    • (1999) American Journal of Pathology , vol.155 , pp. 23-28
    • Funato, H.1    Enya, M.2    Yoshimura, M.3    Morishima-Kawashima, M.4    Ihara, Y.5
  • 70
    • 0028835989 scopus 로고
    • Fatal familial insomnia and familial Creutzfeldt-Jakob disease: Clinical, pathological and molecular features
    • GAMBETTI, P., PARCHI, P., PETERSEN, R. B., CHEN, S. G. & LUGARESI, E. (1995). Fatal familial insomnia and familial Creutzfeldt-Jakob disease: clinical, pathological and molecular features. Brain Pathology 5, 43-51.
    • (1995) Brain Pathology , vol.5 , pp. 43-51
    • Gambetti, P.1    Parchi, P.2    Petersen, R.B.3    Chen, S.G.4    Lugaresi, E.5
  • 72
    • 0038784529 scopus 로고    scopus 로고
    • Are ubiquitination pathways central to Parkinson's disease?
    • GIASSON, B. I. & LEE, V. M. (2003). Are ubiquitination pathways central to Parkinson's disease? Cell 114, 1-8.
    • (2003) Cell , vol.114 , pp. 1-8
    • Giasson, B.I.1    Lee, V.M.2
  • 73
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • GLENNER, G.G. & WONG, C. W. (1984). Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochemical and Biophysical Research Communications 120, 885-890.
    • (1984) Biochemical and Biophysical Research Communications , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 74
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    • GOLDBERG, M. S. & LANSBURY JR., P. T. (2000). Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nature Cell Biology 2, E115-E119.
    • (2000) Nature Cell Biology , vol.2
    • Goldberg, M.S.1    Lansbury Jr., P.T.2
  • 77
    • 0037073748 scopus 로고    scopus 로고
    • Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion
    • GOSAVI, N., LEE, H. J., LEE, J. S., PATEL, S. & LEE, S. J. (2002). Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion. Journal of Biological Chemistry 277, 48984-48992.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 48984-48992
    • Gosavi, N.1    Lee, H.J.2    Lee, J.S.3    Patel, S.4    Lee, S.J.5
  • 79
    • 1842425710 scopus 로고    scopus 로고
    • Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation
    • GREEN, J. D., GOLDSBURY, C., KISTLER, J., COOPER, G. S. & AEBI, U. (2004). Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation. Journal of Biological Chemistry 279, 12206-12212.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 12206-12212
    • Green, J.D.1    Goldsbury, C.2    Kistler, J.3    Cooper, G.S.4    Aebi, U.5
  • 81
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • HARDY, J. & SELKOE, D. J. (2002). The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 82
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • HARDY, J. A. & HIGGINS, G. A. (1992). Alzheimer's disease: the amyloid cascade hypothesis. Science 256, 184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 83
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein
    • HARPER, J. D., LIEBER, C. M. & LANSBURY JR., P. T. (1997a). Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein. Chemistry & Biology 4, 951-959.
    • (1997) Chemistry & Biology , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury Jr., P.T.3
  • 84
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Abeta amyloid protofibrils by atomic force microscopy
    • HARPER, J. D., WONG, S. S., LIEBER, C. M. & LANSBURY, P. T. (1997b). Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chemistry & Biology 4, 119-125.
    • (1997) Chemistry & Biology , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 85
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of a beta amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease
    • HARPER, J. D., WONG, S. S., LIEBER, C. M. & LANSBURY JR., P. T. (1999). Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease. Biochemistry 38, 8972-8980.
    • (1999) Biochemistry , vol.38 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury Jr., P.T.4
  • 87
    • 0035955455 scopus 로고    scopus 로고
    • Inhibitors can arrest the membrane activity of human islet amyloid polypeptide independently of amyloid formation
    • HARROUN, T. A., BRADSHAW, J. P. & ASHLEY, R. H. (2001). Inhibitors can arrest the membrane activity of human islet amyloid polypeptide independently of amyloid formation. FEBS Letters 507, 200-204.
    • (2001) FEBS Letters , vol.507 , pp. 200-204
    • Harroun, T.A.1    Bradshaw, J.P.2    Ashley, R.H.3
  • 88
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • HARTLEY, D. M., WALSH, D. M., YE, C. P., DIEHL, T., VASQUEZ, S., VASSILEV, P. M., TEPLOW, D. B. & SELKOE, D. J. (1999). Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. Journal of Neuroscience 19, 8876-8884.
    • (1999) Journal of Neuroscience , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3    Diehl, T.4    Vasquez, S.5    Vassilev, P.M.6    Teplow, D.B.7    Selkoe, D.J.8
  • 89
    • 0035950270 scopus 로고    scopus 로고
    • Beta-Synuclein inhibits alpha-synuclein aggregation: A possible role as an antiparkinsonian factor
    • HASHIMOTO, M., ROCKENSTEIN, E., MANTE, M., MALLORY, M. & MASLIAH, E. (2001). beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an antiparkinsonian factor. Neuron 32, 213-223.
    • (2001) Neuron , vol.32 , pp. 213-223
    • Hashimoto, M.1    Rockenstein, E.2    Mante, M.3    Mallory, M.4    Masliah, E.5
  • 91
    • 0033576323 scopus 로고    scopus 로고
    • Transmissible and genetic prion diseases share a common pathway of neurodegeneration
    • HEGDE, R. S., TREMBLAY, P., GROTH, D., DEARMOND, S. J., PRUSINER, S. B. & LINGAPPA, V. R. (1999). Transmissible and genetic prion diseases share a common pathway of neurodegeneration. Nature 402, 822-826.
    • (1999) Nature , vol.402 , pp. 822-826
    • Hegde, R.S.1    Tremblay, P.2    Groth, D.3    Dearmond, S.J.4    Prusiner, S.B.5    Lingappa, V.R.6
  • 92
    • 0029966282 scopus 로고    scopus 로고
    • Specificity of abnormal assembly in immunoglobulin light chain deposition disease and amyloidosis
    • HELMS, L. R. & WETZEL, R. (1996). Specificity of abnormal assembly in immunoglobulin light chain deposition disease and amyloidosis. Journal of Molecular Biology 257, 77-86.
    • (1996) Journal of Molecular Biology , vol.257 , pp. 77-86
    • Helms, L.R.1    Wetzel, R.2
  • 93
    • 0035822706 scopus 로고    scopus 로고
    • Beta-barrel pore-forming toxins: Intriguing dimorphic proteins
    • HEUCK, A. P., TWETEN, R. K. & JOHNSON, A. E. (2001). Beta-barrel pore-forming toxins: intriguing dimorphic proteins. Biochemistry 40, 9065-9073.
    • (2001) Biochemistry , vol.40 , pp. 9065-9073
    • Heuck, A.P.1    Tweten, R.K.2    Johnson, A.E.3
  • 94
    • 0043234285 scopus 로고    scopus 로고
    • Assembly and topography of the prepore complex in cholesterol-dependent cytolysins
    • HEUCK, A. P., TWETEN, R. K. & JOHNSON, A. E. (2003). Assembly and topography of the prepore complex in cholesterol-dependent cytolysins. Journal of Biological Chemistry 278, 31218-31225.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 31218-31225
    • Heuck, A.P.1    Tweten, R.K.2    Johnson, A.E.3
  • 95
    • 0028842285 scopus 로고
    • Expression of heat shock genes in hepatocytes is affected by age and food restriction in rats
    • HEYDARI, A. R., CONRAD, C. C. & RICHARDSON, A. (1995). Expression of heat shock genes in hepatocytes is affected by age and food restriction in rats. Journal of Nutrition 125, 410-418.
    • (1995) Journal of Nutrition , vol.125 , pp. 410-418
    • Heydari, A.R.1    Conrad, C.C.2    Richardson, A.3
  • 96
    • 0034657229 scopus 로고    scopus 로고
    • Polyglutamine-induced ion channels: A possible mechanism for the neurotoxicity of Huntington and other CAG repeat diseases
    • HIRAKURA, Y., AZIMOV, R., AZIMOVA, R. & KAGAN, B. L. (2000a). Polyglutamine-induced ion channels: a possible mechanism for the neurotoxicity of Huntington and other CAG repeat diseases. Journal of Neuroscience Research 60, 490-494.
    • (2000) Journal of Neuroscience Research , vol.60 , pp. 490-494
    • Hirakura, Y.1    Azimov, R.2    Azimova, R.3    Kagan, B.L.4
  • 97
    • 0036131408 scopus 로고    scopus 로고
    • Channel formation by serum amyloid A: A potential mechanism for amyloid pathogenesis and host defense
    • HIRAKURA, Y., CARRERAS, I., SIPE, J. D. & KAGAN, B. L. (2002). Channel formation by serum amyloid A: a potential mechanism for amyloid pathogenesis and host defense. Amyloid 9, 13-23.
    • (2002) Amyloid , vol.9 , pp. 13-23
    • Hirakura, Y.1    Carreras, I.2    Sipe, J.D.3    Kagan, B.L.4
  • 98
    • 0034994097 scopus 로고    scopus 로고
    • Pore formation by beta-2-microglobulin: A mechanism for the pathogenesis of dialysis associated amyloidosis
    • HIRAKURA, Y. & KAGAN, B. L. (2001). Pore formation by beta-2-microglobulin: a mechanism for the pathogenesis of dialysis associated amyloidosis. Amyloid 8, 94-100.
    • (2001) Amyloid , vol.8 , pp. 94-100
    • Hirakura, Y.1    Kagan, B.L.2
  • 99
    • 0033566369 scopus 로고    scopus 로고
    • Alzheimer amyloid abeta 1-42 channels: Effects of solvent, pH, and Congo Red
    • HIRAKURA, Y., LIN, M. C. & KAGAN, B. L. (1999). Alzheimer amyloid abeta 1-42 channels: effects of solvent, pH, and Congo Red. Journal of Neuroscience Research 57, 458-466.
    • (1999) Journal of Neuroscience Research , vol.57 , pp. 458-466
    • Hirakura, Y.1    Lin, M.C.2    Kagan, B.L.3
  • 100
    • 0033808530 scopus 로고    scopus 로고
    • Amyloid peptide channels: Blockade by zinc and inhibition by Congo red (amyloid channel block)
    • HIRAKURA, Y., YIU, W. W., YAMAMOTO, A. & KAGAN, B. L. (2000b). Amyloid peptide channels: blockade by zinc and inhibition by Congo red (amyloid channel block). Amyloid 7, 194-199.
    • (2000) Amyloid , vol.7 , pp. 194-199
    • Hirakura, Y.1    Yiu, W.W.2    Yamamoto, A.3    Kagan, B.L.4
  • 103
    • 0037975676 scopus 로고    scopus 로고
    • Spherical aggregates of beta-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3beta
    • HOSHI, M., SATO, M., MATSUMOTO, S., NOGUCHI, A., YASUTAKE, K., YOSHIDA, N. & SATO, K. (2003). Spherical aggregates of beta-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3beta. Proceedings of the National Academy of Sciences USA 100, 6370-6375.
    • (2003) Proceedings of the National Academy of Sciences USA , vol.100 , pp. 6370-6375
    • Hoshi, M.1    Sato, M.2    Matsumoto, S.3    Noguchi, A.4    Yasutake, K.5    Yoshida, N.6    Sato, K.7
  • 104
    • 0035896507 scopus 로고    scopus 로고
    • Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate
    • HOTZE, E. M., WILSON-KUBALEK, E. M., ROSSJOHN, J., PARKER, M. W., JOHNSON, A. E. & TWETEN, R.K. (2001). Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate. Journal of Biological Chemistry 276, 8261-8268.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 8261-8268
    • Hotze, E.M.1    Wilson-Kubalek, E.M.2    Rossjohn, J.3    Parker, M.W.4    Johnson, A.E.5    Tweten, R.K.6
  • 108
    • 0033048453 scopus 로고    scopus 로고
    • The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles
    • JANSON, J., ASHLEY, R. H., HARRISON, D., MCINTYRE, S. & BUTLER, P. C. (1999). The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes 48, 491-498.
    • (1999) Diabetes , vol.48 , pp. 491-498
    • Janson, J.1    Ashley, R.H.2    Harrison, D.3    McIntyre, S.4    Butler, P.C.5
  • 111
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • JARRETT, J. T., BERGER, E. P. & LANSBURY JR., P. T. (1993). The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 112
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • JARRETT, J. T. & LANSBURY JR., P. T. (1993). Seeding 'one-dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 113
    • 0033749379 scopus 로고    scopus 로고
    • Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
    • JOHNSTON, J. A., DALTON, M. J., GURNEY, M. E. & KOPITO, R. R. (2000). Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proceedings of the National Academy of Sciences USA 97, 12571-12576.
    • (2000) Proceedings of the National Academy of Sciences USA , vol.97 , pp. 12571-12576
    • Johnston, J.A.1    Dalton, M.J.2    Gurney, M.E.3    Kopito, R.R.4
  • 114
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • JOHNSTON, J. A., WARD, C. L. & KOPITO, R. R. (1998). Aggresomes: a cellular response to misfolded proteins. Journal of Cell Biology 143, 1883-1898.
    • (1998) Journal of Cell Biology , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 115
    • 0035936804 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis. unfolding the toxicity of the misfolded
    • JULIEN, J. P. (2001). Amyotrophic lateral sclerosis. unfolding the toxicity of the misfolded. Cell 104, 581-591.
    • (2001) Cell , vol.104 , pp. 581-591
    • Julien, J.P.1
  • 117
  • 119
    • 0035997234 scopus 로고    scopus 로고
    • The channel hypothesis of Alzheimer's disease: Current status
    • KAGAN, B. L., HIRAKURA, Y., AZIMOV, R., AZIMOVA, R. & LIN, M. C. (2002). The channel hypothesis of Alzheimer's disease: current status. Peptides 23, 1311-1315.
    • (2002) Peptides , vol.23 , pp. 1311-1315
    • Kagan, B.L.1    Hirakura, Y.2    Azimov, R.3    Azimova, R.4    Lin, M.C.5
  • 120
    • 0030966536 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid beta-protein forms Zn (2+)-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons
    • KAWAHARA, M., ARISPE, N., KURODA, Y. & ROJAS, E. (1997). Alzheimer's disease amyloid beta-protein forms Zn (2+)-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons. Biophysical Journal 73, 67-75.
    • (1997) Biophysical Journal , vol.73 , pp. 67-75
    • Kawahara, M.1    Arispe, N.2    Kuroda, Y.3    Rojas, E.4
  • 121
    • 0034319190 scopus 로고    scopus 로고
    • Molecular mechanism of neurodegeneration induced by Alzheimer's beta-amyloid protein: Channel formation and disruption of calcium homeostasis
    • KAWAHARA, M. & KURODA, Y. (2000). Molecular mechanism of neurodegeneration induced by Alzheimer's beta-amyloid protein: channel formation and disruption of calcium homeostasis. Brain Research Bulletin 53, 389-397.
    • (2000) Brain Research Bulletin , vol.53 , pp. 389-397
    • Kawahara, M.1    Kuroda, Y.2
  • 122
    • 0034980106 scopus 로고    scopus 로고
    • Intracellular calcium changes in neuronal cells induced by Alzheimer's beta-amyloid protein are blocked by estradiol and cholesterol
    • KAWAHARA, M. & KURODA, Y. (2001). Intracellular calcium changes in neuronal cells induced by Alzheimer's beta-amyloid protein are blocked by estradiol and cholesterol. Cellular and Molecular Neurobiology 21, 1-13.
    • (2001) Cellular and Molecular Neurobiology , vol.21 , pp. 1-13
    • Kawahara, M.1    Kuroda, Y.2
  • 123
    • 0034640372 scopus 로고    scopus 로고
    • Alzheimer's beta-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line
    • KAWAHARA, M., KURODA, Y., ARISPE, N. & ROJAS, E. (2000). Alzheimer's beta-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line. Journal of Biological Chemistry 275, 14077-14083.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 14077-14083
    • Kawahara, M.1    Kuroda, Y.2    Arispe, N.3    Rojas, E.4
  • 124
    • 33750824600 scopus 로고    scopus 로고
    • Formation, stability and toxicity of annular protofibrils from different amyloid forming proteins
    • KAYED, R. & GLABE, C. G. (2004). Formation, stability and toxicity of annular protofibrils from different amyloid forming proteins. Neurobiology of Aging 25 (Suppl. 2), S144.
    • (2004) Neurobiology of Aging , vol.25 , Issue.SUPPL. 2
    • Kayed, R.1    Glabe, C.G.2
  • 125
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • KAYED, R., HEAD, E., THOMPSON, J. L., MCINTIRE, T. M., MILTON, S. C., COTMAN, C. W. & GLABE, C. G. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 126
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • KAYED, R., SOKOLOV, Y., EDMONDS, B., MCINTIRE, T. M., MILTON, S. C., HALL, J. E. & GLABE, C. G. (2004). Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. Journal of Biological Chemistry 279, 46363-46366.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 127
    • 25444433798 scopus 로고    scopus 로고
    • Characterization of oligomeric intermediates in alpha-synuclein fibrillation: FRET studies of Y125W/Y133F/Y136F alpha-synuclein
    • KAYLOR, J., BODNER, N., EDRIDGE, S., YAMIN, G., HONG, D. P. & FINK, A. L. (2005). Characterization of oligomeric intermediates in alpha-synuclein fibrillation: FRET studies of Y125W/Y133F/Y136F alpha-synuclein. Journal of Molecular Biology 353, 357-372.
    • (2005) Journal of Molecular Biology , vol.353 , pp. 357-372
    • Kaylor, J.1    Bodner, N.2    Edridge, S.3    Yamin, G.4    Hong, D.P.5    Fink, A.L.6
  • 128
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • KELLY, J. W. (1998). The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Current Opinion in Structural Biology 8, 101-106.
    • (1998) Current Opinion in Structural Biology , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 129
    • 0345060507 scopus 로고    scopus 로고
    • Aβ proto.brils possess a stable core structure resistant to hydrogen exchange
    • KHETERPAL, I., LASHUEL, H., HARTLEY, D., WALZ, T., LANSBURY JR., P. & WETZEL, R. (2003). Aβ proto.brils possess a stable core structure resistant to hydrogen exchange. Biochemistry 42, 14092-14098.
    • (2003) Biochemistry , vol.42 , pp. 14092-14098
    • Kheterpal, I.1    Lashuel, H.2    Hartley, D.3    Walz, T.4    Lansbury Jr., P.5    Wetzel, R.6
  • 131
    • 0345269757 scopus 로고    scopus 로고
    • Nigrostriatal alpha-synucleinopathy induced by viral vector-mediated overexpression of human alpha-synuclein: A new primate model of Parkinson's disease
    • KIRIK, D., ANNETT, L. E., BURGER, C., MUZYCZKA, N., MANDEL, R. J. & BJORKLUND, A. (2003). Nigrostriatal alpha-synucleinopathy induced by viral vector-mediated overexpression of human alpha-synuclein: a new primate model of Parkinson's disease. Proceedings of the National Academy of Sciences USA 100, 2884-2889.
    • (2003) Proceedings of the National Academy of Sciences USA , vol.100 , pp. 2884-2889
    • Kirik, D.1    Annett, L.E.2    Burger, C.3    Muzyczka, N.4    Mandel, R.J.5    Bjorklund, A.6
  • 134
    • 0242362596 scopus 로고    scopus 로고
    • Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH
    • KLUG, G. M., LOSIC, D., SUBASINGHE, S. S., AGUILAR, M. I., MARTIN, L. L. & SMALL, D. H. (2003). Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH. European Journal of Biochemistry 270, 4282-4293.
    • (2003) European Journal of Biochemistry , vol.270 , pp. 4282-4293
    • Klug, G.M.1    Losic, D.2    Subasinghe, S.S.3    Aguilar, M.I.4    Martin, L.L.5    Small, D.H.6
  • 135
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • KOPITO, R. R. (2000). Aggresomes, inclusion bodies and protein aggregation. Trends in Cell Biology 10, 524-530.
    • (2000) Trends in Cell Biology , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 136
    • 0036735015 scopus 로고    scopus 로고
    • Prion channel proteins and their role in vacuolation and neurodegenerative diseases
    • KOURIE, J. I. (2002). Prion channel proteins and their role in vacuolation and neurodegenerative diseases. European Biophysics Journal 31, 409-416.
    • (2002) European Biophysics Journal , vol.31 , pp. 409-416
    • Kourie, J.I.1
  • 137
    • 0033774525 scopus 로고    scopus 로고
    • Prion peptide fragment PrP[106-126] forms distinct cation channel types
    • KOURIE, J. I. & CULVERSON, A. (2000). Prion peptide fragment PrP[106-126] forms distinct cation channel types. Journal of Neuroscience Research 62, 120-133.
    • (2000) Journal of Neuroscience Research , vol.62 , pp. 120-133
    • Kourie, J.I.1    Culverson, A.2
  • 138
    • 0035888283 scopus 로고    scopus 로고
    • Channel activity of deamidated isoforms of prion protein fragment 106-126 in planar lipid bilayers
    • KOURIE, J. I., FARRELLY, P. V. & HENRY, C. L. (2001a). Channel activity of deamidated isoforms of prion protein fragment 106-126 in planar lipid bilayers. Journal of Neuroscience Research 66, 214-220.
    • (2001) Journal of Neuroscience Research , vol.66 , pp. 214-220
    • Kourie, J.I.1    Farrelly, P.V.2    Henry, C.L.3
  • 146
    • 0036591668 scopus 로고    scopus 로고
    • Genetics of Parkinson's disease and biochemical studies of implicated gene products
    • LANSBURY JR., P. T. & BRICE, A. (2002). Genetics of Parkinson's disease and biochemical studies of implicated gene products. Current Opinion in Genetics & Development 12, 299-306.
    • (2002) Current Opinion in Genetics & Development , vol.12 , pp. 299-306
    • Lansbury Jr., P.T.1    Brice, A.2
  • 147
    • 0041825430 scopus 로고    scopus 로고
    • Mixtures of wild-type and 'Arctic' Abeta40 in vitro accumulate protofibrils, including amyloid pores
    • LASHUEL, H., HARTLEY, D., PETRE, B., WALL, J., SIMON, M., WALZ, T. & LANSBURY, P. (2003). Mixtures of wild-type and 'Arctic' Abeta40 in vitro accumulate protofibrils, including amyloid pores. Journal of Molecular Biology 332, 795-808.
    • (2003) Journal of Molecular Biology , vol.332 , pp. 795-808
    • Lashuel, H.1    Hartley, D.2    Petre, B.3    Wall, J.4    Simon, M.5    Walz, T.6    Lansbury, P.7
  • 148
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • LASHUEL, H., PETRE, B., WALL, J., SIMON, M., NOWAK, R., WALZ, T. & LANSBURY, P. (2002a). alpha-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils. Journal of Molecular Biology 322, 1089.
    • (2002) Journal of Molecular Biology , vol.322 , pp. 1089
    • Lashuel, H.1    Petre, B.2    Wall, J.3    Simon, M.4    Nowak, R.5    Walz, T.6    Lansbury, P.7
  • 149
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • LASHUEL, H. A., HARTLEY, D., PETRE, B. M., WALZ, T. & LANSBURY JR., P. T. (2002b). Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 418, 291.
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 150
    • 0032558978 scopus 로고    scopus 로고
    • Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: Implications for wild-type, V30M, and L55P amyloid fibril formation
    • LASHUEL, H. A., LAI, Z. & KELLY, J. W. (1998). Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation. Biochemistry 37, 17851-17864.
    • (1998) Biochemistry , vol.37 , pp. 17851-17864
    • Lashuel, H.A.1    Lai, Z.2    Kelly, J.W.3
  • 151
    • 0033550075 scopus 로고    scopus 로고
    • The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions
    • LASHUEL, H. A., WURTH, C., WOO, L. & KELLY, J. W. (1999). The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions. Biochemistry 38, 13560-13573.
    • (1999) Biochemistry , vol.38 , pp. 13560-13573
    • Lashuel, H.A.1    Wurth, C.2    Woo, L.3    Kelly, J.W.4
  • 152
    • 1442275729 scopus 로고    scopus 로고
    • Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway
    • LEE, H. J., KHOSHAGHIDEH, F., PATEL, S. & LEE, S. J. (2004). Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway. Journal of Neuroscience 24, 1888-1896.
    • (2004) Journal of Neuroscience , vol.24 , pp. 1888-1896
    • Lee, H.J.1    Khoshaghideh, F.2    Patel, S.3    Lee, S.J.4
  • 153
    • 0037073747 scopus 로고    scopus 로고
    • Characterization of cytoplasmic alpha-synuclein aggregates: Fibril formation is tightly linked to the inclusion forming process in cells
    • LEE, H. J. & LEE, S. J. (2002). Characterization of cytoplasmic alpha-synuclein aggregates: Fibril formation is tightly linked to the inclusion forming process in cells. Journal of Biological Chemistry 277, 48976-48983.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 48976-48983
    • Lee, H.J.1    Lee, S.J.2
  • 154
    • 0037085288 scopus 로고    scopus 로고
    • Formation and removal of alpha-synuclein aggregates in cells exposed to mitochondrial inhibitors
    • LEE, H. J., SHIN, S. Y., CHOI, C., LEE, Y. H. & LEE, S. J. (2002). Formation and removal of alpha-synuclein aggregates in cells exposed to mitochondrial inhibitors. Journal of Biological Chemistry 277, 5411-5417.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 5411-5417
    • Lee, H.J.1    Shin, S.Y.2    Choi, C.3    Lee, Y.H.4    Lee, S.J.5
  • 155
    • 0042320356 scopus 로고    scopus 로고
    • Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process
    • LEE, S. & EISENBERG, D. (2003). Seeded conversion of recombinant prion protein to a disulfide-bonded oligomer by a reduction-oxidation process. Nature Structural Biology 10, 725-730.
    • (2003) Nature Structural Biology , vol.10 , pp. 725-730
    • Lee, S.1    Eisenberg, D.2
  • 156
    • 0030050733 scopus 로고    scopus 로고
    • Mutant and infectious prion proteins display common biochemical properties in cultured cells
    • LEHMANN, S. & HARRIS, D. A. (1996). Mutant and infectious prion proteins display common biochemical properties in cultured cells. Journal of Biological Chemistry 271, 1633-1637.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 1633-1637
    • Lehmann, S.1    Harris, D.A.2
  • 157
    • 0030007964 scopus 로고    scopus 로고
    • Sequence of deposition of heterogeneous amyloid beta-peptides and APO e in Down syndrome: Implications for initial events in amyloid plaque formation
    • LEMERE, C. A., BLUSZTAJN, J. K., YAMAGUCHI, H., WISNIEWSKI, T., SAIDO, T. C. & SELKOE, D. J. (1996). Sequence of deposition of heterogeneous amyloid beta-peptides and APO E in Down syndrome: implications for initial events in amyloid plaque formation. Neurobiology of Disease Journal 3, 16-32.
    • (1996) Neurobiology of Disease Journal , vol.3 , pp. 16-32
    • Lemere, C.A.1    Blusztajn, J.K.2    Yamaguchi, H.3    Wisniewski, T.4    Saido, T.C.5    Selkoe, D.J.6
  • 159
    • 0035949542 scopus 로고    scopus 로고
    • Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein
    • LI, J., UVERSKY, V. N. & FINK, A. L. (2001). Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein. Biochemistry 40, 11604-11613.
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 160
    • 4344650564 scopus 로고    scopus 로고
    • Dopamine and L-dopa disaggregate amyloid fibrils: Implications for Parkinson's and Alzheimer's disease
    • LI, J., ZHU, M., MANNING-BOG, A. B., DI MONTE, D. A. & FINK, A. L. (2004). Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease. FASEB Journal 18, 962-964.
    • (2004) FASEB Journal , vol.18 , pp. 962-964
    • Li, J.1    Zhu, M.2    Manning-Bog, A.B.3    Di Monte, D.A.4    Fink, A.L.5
  • 161
    • 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 Journal 15, 2433-2444.
    • (2001) FASEB Journal , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 162
    • 0033600590 scopus 로고    scopus 로고
    • 2+-sensitive channel in reconstituted lipid vesicles
    • 2+-sensitive channel in reconstituted lipid vesicles. Biochemistry 38, 11189-11196.
    • (1999) Biochemistry , vol.38 , pp. 11189-11196
    • Lin, H.1    Zhu, Y.J.2    Lal, R.3
  • 163
    • 0035997224 scopus 로고    scopus 로고
    • Electrophysiologic properties of channels induced by Abeta25-35 in planar lipid bilayers
    • LIN, M. C. & KAGAN, B. L. (2002). Electrophysiologic properties of channels induced by Abeta25-35 in planar lipid bilayers. Peptides 23, 1215-1228.
    • (2002) Peptides , vol.23 , pp. 1215-1228
    • Lin, M.C.1    Kagan, B.L.2
  • 165
    • 0037168643 scopus 로고    scopus 로고
    • Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state
    • LINDBERG, M. J., TIBELL, L. & OLIVEBERG, M. (2002). Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state. Proceedings of the National Academy of Sciences USA 99, 16607-16612.
    • (2002) Proceedings of the National Academy of Sciences USA , vol.99 , pp. 16607-16612
    • Lindberg, M.J.1    Tibell, L.2    Oliveberg, M.3
  • 168
    • 0036884733 scopus 로고    scopus 로고
    • Pathogenesis of Parkinson's disease: Dopamine, vesicles and alphasynuclein
    • LOTHARIUS, J. & BRUNDIN, P. (2002). Pathogenesis of Parkinson's disease: dopamine, vesicles and alphasynuclein. Nature Reviews Neuroscience 3, 932-942.
    • (2002) Nature Reviews Neuroscience , vol.3 , pp. 932-942
    • Lotharius, J.1    Brundin, P.2
  • 169
    • 9344233839 scopus 로고    scopus 로고
    • Calcium(II) selectively induces alpha-synuclein annular oligomers via interaction with the C-terminal domain
    • LOWE, R., POUNTNEY, D. L., JENSEN, P. H., GAI, W. P. & VOELCKER, N. H. (2004). Calcium(II) selectively induces alpha-synuclein annular oligomers via interaction with the C-terminal domain. Protein Science 13, 3245-3252.
    • (2004) Protein Science , vol.13 , pp. 3245-3252
    • Lowe, R.1    Pountney, D.L.2    Jensen, P.H.3    Gai, W.P.4    Voelcker, N.H.5
  • 170
    • 0037093432 scopus 로고    scopus 로고
    • Isolation and characterization of a polymerized prion protein
    • LU, B. Y. & CHANG, J. Y. (2002). Isolation and characterization of a polymerized prion protein. Biochemical Journal 364, 81-87.
    • (2002) Biochemical Journal , vol.364 , pp. 81-87
    • Lu, B.Y.1    Chang, J.Y.2
  • 172
    • 0037195617 scopus 로고    scopus 로고
    • Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol
    • MA, J. & LINDQUIST, S. (2002). Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science 298, 1785-1788.
    • (2002) Science , vol.298 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 173
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • MA, J., WOLLMANN, R. & LINDQUIST, S. (2002). Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298, 1781-1785.
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 174
    • 0026437675 scopus 로고
    • Morphology of cerebral plaque-like lesions in hereditary cerebral hemorrhage with amyloidosis
    • in Dutch
    • MAAT-SCHIEMAN, M. L., VAN DUINEN, S. G., HAAN, J. & ROOS, R. A. (1992). Morphology of cerebral plaque-like lesions in hereditary cerebral hemorrhage with amyloidosis [in Dutch]. Acta Neuropathologica (Berlin) 84, 674-679.
    • (1992) Acta Neuropathologica (Berlin) , vol.84 , pp. 674-679
    • Maat-Schieman, M.L.1    Van Duinen, S.G.2    Haan, J.3    Roos, R.A.4
  • 175
    • 0042744699 scopus 로고    scopus 로고
    • Amyloid protofilaments from the calcium-binding protein equine lysozyme: Formation of ring and linear structures depends on pH and metal ion concentration
    • MALISAUSKAS, M., ZAMOTIN, V., JASS, J., NOPPE, W., DOBSON, C. M. & MOROZOVA-ROCHE, L. A. (2003). Amyloid protofilaments from the calcium-binding protein equine lysozyme: formation of ring and linear structures depends on pH and metal ion concentration. Journal of Molecular Biology 330, 879-890.
    • (2003) Journal of Molecular Biology , vol.330 , pp. 879-890
    • Malisauskas, M.1    Zamotin, V.2    Jass, J.3    Noppe, W.4    Dobson, C.M.5    Morozova-Roche, L.A.6
  • 176
    • 0036777590 scopus 로고    scopus 로고
    • Development of new treatments for Parkinson's disease in transgenic animal models: A role for beta-synuclein
    • MASLIAH, E. & HASHIMOTO, M. (2002). Development of new treatments for Parkinson's disease in transgenic animal models: a role for beta-synuclein. Neurotoxicology 23, 461-468.
    • (2002) Neurotoxicology , vol.23 , pp. 461-468
    • Masliah, E.1    Hashimoto, M.2
  • 177
    • 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, Y., SISK, A. & MUCKE, L. (2000). 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    Sagara, Y.7    Sisk, A.8    Mucke, L.9
  • 178
    • 23144443884 scopus 로고    scopus 로고
    • Protein quality control: Chaperones culling corrupt conformations
    • MCCLELLAN, A. J., TAM, S., KAGANOVICH, D. & FRYDMAN, J. (2005). Protein quality control: chaperones culling corrupt conformations. Nature Cell Biology 7, 736-741.
    • (2005) Nature Cell Biology , vol.7 , pp. 736-741
    • McClellan, A.J.1    Tam, S.2    Kaganovich, D.3    Frydman, J.4
  • 180
    • 0036316947 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures
    • MCNAUGHT, K. S., MYTILINEOU, C., JNOBAPTISTE, R., YABUT, J., SHASHIDHARAN, P., JENNERT, P. & OLANOW, C. W. (2002). Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures. Journal of Neurochemistry 81, 301-306.
    • (2002) Journal of Neurochemistry , vol.81 , pp. 301-306
    • McNaught, K.S.1    Mytilineou, C.2    Jnobaptiste, R.3    Yabut, J.4    Shashidharan, P.5    Jennert, P.6    Olanow, C.W.7
  • 181
    • 0034869444 scopus 로고    scopus 로고
    • Mode of action of beta-barrel pore-forming toxins of the staphylococcal alpha-hemolysin family
    • MENESTRINA, G., SERRA, M. D. & PREVOST, G. (2001). Mode of action of beta-barrel pore-forming toxins of the staphylococcal alpha-hemolysin family. Toxicon 39, 1661-1672.
    • (2001) Toxicon , vol.39 , pp. 1661-1672
    • Menestrina, G.1    Serra, M.D.2    Prevost, G.3
  • 182
    • 0036176613 scopus 로고    scopus 로고
    • Mitochondrial involvement in amyotrophic lateral sclerosis
    • MENZIES, F. M., INCE, P. G. & SHAW, P. J. (2002). Mitochondrial involvement in amyotrophic lateral sclerosis. Neurochemistry International 40, 543-551.
    • (2002) Neurochemistry International , vol.40 , pp. 543-551
    • Menzies, F.M.1    Ince, P.G.2    Shaw, P.J.3
  • 183
  • 185
    • 0029088140 scopus 로고
    • New tubular single-stranded helix of poly-L-amino acids suggested by molecular mechanics calculations: I. Homopolypeptides in isolated environments
    • MONOI, H. (1995). New tubular single-stranded helix of poly-L-amino acids suggested by molecular mechanics calculations: I. Homopolypeptides in isolated environments. Biophysical Journal 69, 1130-1141.
    • (1995) Biophysical Journal , vol.69 , pp. 1130-1141
    • Monoi, H.1
  • 186
    • 0034125918 scopus 로고    scopus 로고
    • Poly-L-glutamine forms cation channels: Relevance to the pathogenesis of the polyglutamine diseases
    • MONOI, H., FUTAKI, S., KUGIMIYA, S., MINAKATA, H. & YOSHIHARA, K. (2000). Poly-L-glutamine forms cation channels: relevance to the pathogenesis of the polyglutamine diseases. Biophysical Journal 78, 2892-2899.
    • (2000) Biophysical Journal , vol.78 , pp. 2892-2899
    • Monoi, H.1    Futaki, S.2    Kugimiya, S.3    Minakata, H.4    Yoshihara, K.5
  • 189
    • 0032480771 scopus 로고    scopus 로고
    • The presence of amyloid beta-protein in the detergent-insoluble membrane compartment of human neuroblastoma cells
    • MORISHIMA-KAWASHIMA, M. & IHARA, Y. (1998). The presence of amyloid beta-protein in the detergent-insoluble membrane compartment of human neuroblastoma cells. Biochemistry 37, 15247-15253.
    • (1998) Biochemistry , vol.37 , pp. 15247-15253
    • Morishima-Kawashima, M.1    Ihara, Y.2
  • 190
    • 0037014426 scopus 로고    scopus 로고
    • Protein misfolding, amyloid formation, and neurodegeneration: A critical role for molecular chaperones?
    • MUCHOWSKI, P. J. (2002). Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones? Neuron 35, 9-12.
    • (2002) Neuron , vol.35 , pp. 9-12
    • Muchowski, P.J.1
  • 195
    • 0028123618 scopus 로고
    • Islet amyloid polypeptide in human insulinomas. Evidence for intracellular amyloidogenesis
    • O'BRIEN, T. D., BUTLER, A. E., ROCHE, P. C., JOHNSON, K. H. & BUTLER, P. C. (1994). Islet amyloid polypeptide in human insulinomas. Evidence for intracellular amyloidogenesis. Diabetes 43, 329-336.
    • (1994) Diabetes , vol.43 , pp. 329-336
    • O'Brien, T.D.1    Butler, A.E.2    Roche, P.C.3    Johnson, K.H.4    Butler, P.C.5
  • 197
    • 0027526035 scopus 로고
    • The projection structure of perfringolysin O (Clostridium perfringens theta-toxin)
    • OLOFSSON, A., HEBERT, H. & THELESTAM, M. (1993). The projection structure of perfringolysin O (Clostridium perfringens theta-toxin). FEBS Letters 319, 125-127.
    • (1993) FEBS Letters , vol.319 , pp. 125-127
    • Olofsson, A.1    Hebert, H.2    Thelestam, M.3
  • 199
    • 30444457574 scopus 로고    scopus 로고
    • The alpha-synuclein mutation E46K promotes aggregation in cultured cells
    • PANDEY, N., SCHMIDT, R. E. & GALVIN, J. E. (2006). The alpha-synuclein mutation E46K promotes aggregation in cultured cells. Experimental Neurology 197, 515-520.
    • (2006) Experimental Neurology , vol.197 , pp. 515-520
    • Pandey, N.1    Schmidt, R.E.2    Galvin, J.E.3
  • 201
    • 0035997230 scopus 로고    scopus 로고
    • Imaging real-time aggregation of amyloid beta protein (1-42) by atomic force microscopy
    • PARBHU, A., LIN, H., THIMM, J. & LAL, R. (2002). Imaging real-time aggregation of amyloid beta protein (1-42) by atomic force microscopy. Peptides 23, 1265-1270.
    • (2002) Peptides , vol.23 , pp. 1265-1270
    • Parbhu, A.1    Lin, H.2    Thimm, J.3    Lal, R.4
  • 202
    • 0037426346 scopus 로고    scopus 로고
    • Beta-synuclein inhibits formation of alpha-synuclein protofibrils: A possible therapeutic strategy against Parkinson's disease
    • PARK, J. Y. & LANSBURY JR., P. T. (2003). Beta-synuclein inhibits formation of alpha-synuclein protofibrils: a possible therapeutic strategy against Parkinson's disease. Biochemistry 42, 3696-3700.
    • (2003) Biochemistry , vol.42 , pp. 3696-3700
    • Park, J.Y.1    Lansbury Jr., P.T.2
  • 203
    • 0033769044 scopus 로고    scopus 로고
    • A nonfibrillar form of the fusogenic prion protein fragment [118-135] induces apoptotic cell death in rat cortical neurons
    • PILLOT, T., DROUET, B., PINCON-RAYMOND, M., VANDEKERCKHOVE, J., ROSSENEU, M. & CHAMBAZ, J. (2000). A nonfibrillar form of the fusogenic prion protein fragment [118-135] induces apoptotic cell death in rat cortical neurons. Journal of Neurochemistry 75, 2298-2308.
    • (2000) Journal of Neurochemistry , vol.75 , pp. 2298-2308
    • Pillot, T.1    Drouet, B.2    Pincon-Raymond, M.3    Vandekerckhove, J.4    Rosseneu, M.5    Chambaz, J.6
  • 205
    • 0031871740 scopus 로고    scopus 로고
    • Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy
    • PITSCHKE, M., PRIOR, R., HAUPT, M. & RIESNER, D. (1998). Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy. Nature Medicine 4, 832-834.
    • (1998) Nature Medicine , vol.4 , pp. 832-834
    • Pitschke, M.1    Prior, R.2    Haupt, M.3    Riesner, D.4
  • 207
  • 210
    • 0141653970 scopus 로고    scopus 로고
    • The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies
    • PORAT, Y., KOLUSHEVA, S., JELINEK, R. & GAZIT, E. (2003). The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies. Biochemistry 42, 10971-10977.
    • (2003) Biochemistry , vol.42 , pp. 10971-10977
    • Porat, Y.1    Kolusheva, S.2    Jelinek, R.3    Gazit, E.4
  • 214
    • 2442624720 scopus 로고    scopus 로고
    • Monomeric Cu/Zn superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial ALS
    • RAKHIT, R., CROW, J. P., LEPOCK, J. R., KONDEJEWSKI, L. H., CASHMAN, N.R. & CHAKRABARTTY, A. (2004). Monomeric Cu/Zn superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial ALS. Journal of Biological Chemistry 279, 15499-15504.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 15499-15504
    • Rakhit, R.1    Crow, J.P.2    Lepock, J.R.3    Kondejewski, L.H.4    Cashman, N.R.5    Chakrabartty, A.6
  • 216
    • 2142761528 scopus 로고    scopus 로고
    • An inter-subunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis
    • RAY, S. S., NOWAK, R. J., STROKOVICH, K., BROWN JR., R. H, WALZ, T. & LANSBURY JR., P. T. (2004). An inter-subunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis. Biochemistry 43, 4899-4905.
    • (2004) Biochemistry , vol.43 , pp. 4899-4905
    • Ray, S.S.1    Nowak, R.J.2    Strokovich, K.3    Brown Jr., R.H.4    Walz, T.5    Lansbury Jr., P.T.6
  • 217
    • 1542357685 scopus 로고    scopus 로고
    • Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture
    • REIXACH, N., DEECHONGKIT, S., JIANG, X., KELLY, J. W. & BUXBAUM, J. N. (2004). Tissue damage in the amyloidoses: transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture. Proceedings of the National Academy of Sciences USA 101, 2817-2822.
    • (2004) Proceedings of the National Academy of Sciences USA , vol.101 , pp. 2817-2822
    • Reixach, N.1    Deechongkit, S.2    Jiang, X.3    Kelly, J.W.4    Buxbaum, J.N.5
  • 219
    • 0037960271 scopus 로고    scopus 로고
    • Micelle formation by a fragment of human islet amyloid polypeptide
    • RHOADES, E. & GAFNI, A. (2003). Micelle formation by a fragment of human islet amyloid polypeptide. Biophysical Journal 84, 3480-3487.
    • (2003) Biophysical Journal , vol.84 , pp. 3480-3487
    • Rhoades, E.1    Gafni, A.2
  • 220
    • 0030026759 scopus 로고    scopus 로고
    • Disruption of prion rods generates 10-nm spherical particles having high alpha-helical content and lacking scrapie infectivity
    • RIESNER, D., KELLINGS, K., POST, K., WILLE, H., SERBAN, H., GROTH, D., BALDWIN, M. A. & PRUSINER, S. B. (1996). Disruption of prion rods generates 10-nm spherical particles having high alpha-helical content and lacking scrapie infectivity. Journal of Virology 70, 1714-1722.
    • (1996) Journal of Virology , vol.70 , pp. 1714-1722
    • Riesner, D.1    Kellings, K.2    Post, K.3    Wille, H.4    Serban, H.5    Groth, D.6    Baldwin, M.A.7    Prusiner, S.B.8
  • 221
    • 0034609561 scopus 로고    scopus 로고
    • Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein
    • ROCHET, J. C., CONWAY, K. A. & LANSBURY JR., P. T. (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.C.1    Conway, K.A.2    Lansbury Jr., P.T.3
  • 224
    • 0037013224 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase
    • RODRIGUEZ, J. A., VALENTINE, J. S., EGGERS, D. K., ROE, J. A., TIWARI, A., BROWN JR., R. H. & HAYWARD, L. J. (2002). Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase. Journal of Biological Chemistry 277, 15932-15937.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 15932-15937
    • Rodriguez, J.A.1    Valentine, J.S.2    Eggers, D.K.3    Roe, J.A.4    Tiwari, A.5    Brown Jr., R.H.6    Hayward, L.J.7
  • 226
    • 0017867105 scopus 로고
    • Amyotrophic lateral sclerosis. Clinical features and prognosis
    • ROSEN, A. D. (1978). Amyotrophic lateral sclerosis. Clinical features and prognosis. Archives of Neurology 35, 638-642.
    • (1978) Archives of Neurology , vol.35 , pp. 638-642
    • Rosen, A.D.1
  • 228
    • 3142604036 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases
    • ROSS, C. A. & PICKART, C. M. (2004). The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases. Trends in Cell Biology 14, 703-711.
    • (2004) Trends in Cell Biology , vol.14 , pp. 703-711
    • Ross, C.A.1    Pickart, C.M.2
  • 229
    • 0035865398 scopus 로고    scopus 로고
    • Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain
    • ROSSI, D., COZZIO, A., FLECHSIG, E., KLEIN, M. A., RULICKE, T., AGUZZI, A. & WEISSMANN, C. (2001). Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain. EMBO Journal 20, 694-702.
    • (2001) EMBO Journal , vol.20 , pp. 694-702
    • Rossi, D.1    Cozzio, A.2    Flechsig, E.3    Klein, M.A.4    Rulicke, T.5    Aguzzi, A.6    Weissmann, C.7
  • 231
    • 0031035836 scopus 로고    scopus 로고
    • Aggregates of a beta-amyloid peptide are required to induce calcium currents in neuron-like human teratocarcinoma cells: Relation to Alzheimer's disease
    • SANDERSON, K. L., BUTLER, L. & INGRAM, V. M. (1997). Aggregates of a beta-amyloid peptide are required to induce calcium currents in neuron-like human teratocarcinoma cells: relation to Alzheimer's disease. Brain Research 744, 7-14.
    • (1997) Brain Research , vol.744 , pp. 7-14
    • Sanderson, K.L.1    Butler, L.2    Ingram, V.M.3
  • 232
    • 0036306046 scopus 로고    scopus 로고
    • Binding of prion protein to lipid membranes and implications for prion conversion
    • SANGHERA, N. & PINHEIRO, T. J. (2002). Binding of prion protein to lipid membranes and implications for prion conversion. Journal of Molecular Biology 315, 1241-1256.
    • (2002) Journal of Molecular Biology , vol.315 , pp. 1241-1256
    • Sanghera, N.1    Pinheiro, T.J.2
  • 234
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • SCHUBERT, U., ANTON, L. C., GIBBS, J., NORBURY, C. C., YEWDELL, J. W. & BENNINK, J. R. (2000). Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404, 770-774.
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 235
    • 0027169048 scopus 로고
    • A ring-shaped structure with a crown formed by streptolysin O on the erythrocyte membrane
    • SEKIYA, K., SATOH, R., DANBARA, H. & FUTAESAKU, Y. (1993). A ring-shaped structure with a crown formed by streptolysin O on the erythrocyte membrane. Journal of Bacteriology 175, 5953-5961.
    • (1993) Journal of Bacteriology , vol.175 , pp. 5953-5961
    • Sekiya, K.1    Satoh, R.2    Danbara, H.3    Futaesaku, Y.4
  • 236
    • 0028170818 scopus 로고
    • Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease
    • SELKOE, D. J. (1994). Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease. Annual Reviews of Cell Biology 10, 373-403.
    • (1994) Annual Reviews of Cell Biology , vol.10 , pp. 373-403
    • Selkoe, D.J.1
  • 237
    • 0031025916 scopus 로고    scopus 로고
    • Generation of a membrane-bound, oligomerized prepore complex is necessary for pore formation by Clostridium septicum alpha toxin
    • SELLMAN, B. R., KAGAN, B. L. & TWETEN, R. K. (1997). Generation of a membrane-bound, oligomerized prepore complex is necessary for pore formation by Clostridium septicum alpha toxin. Molecular Microbiology 23, 551-558.
    • (1997) Molecular Microbiology , vol.23 , pp. 551-558
    • Sellman, B.R.1    Kagan, B.L.2    Tweten, R.K.3
  • 239
    • 0037456578 scopus 로고    scopus 로고
    • The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease
    • SHARON, R., BAR-JOSEPH, I., FROSCH, M. P., WALSH, D. M., HAMILTON, J. A. & SELKOE, D. J. (2003a). The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease. Neuron 37, 583-595.
    • (2003) Neuron , vol.37 , pp. 583-595
    • Sharon, R.1    Bar-Joseph, I.2    Frosch, M.P.3    Walsh, D.M.4    Hamilton, J.A.5    Selkoe, D.J.6
  • 240
    • 0347379922 scopus 로고    scopus 로고
    • Altered fatty acid composition of dopaminergic neurons expressing alpha-synuclein and human brains with alpha-synucleinopathies
    • SHARON, R., BAR-JOSEPH, I., MIRICK, G. E., SERHAN, C.N. & SELKOE, D. J. (2003b). Altered fatty acid composition of dopaminergic neurons expressing alpha-synuclein and human brains with alpha-synucleinopathies. Journal of Biological Chemistry 278, 49874-49881.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 49874-49881
    • Sharon, R.1    Bar-Joseph, I.2    Mirick, G.E.3    Serhan, C.N.4    Selkoe, D.J.5
  • 241
    • 0035979233 scopus 로고    scopus 로고
    • Alpha-Synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins
    • SHARON, R., GOLDBERG, M. S., BAR-JOSEF, I., BETENSKY, R. A., SHEN, J. & SELKOE, D. J. (2001). alpha-Synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins. Proceedings of the National Academy of Sciences USA 98, 9110-9115.
    • (2001) Proceedings of the National Academy of Sciences USA , vol.98 , pp. 9110-9115
    • Sharon, R.1    Goldberg, M.S.2    Bar-Josef, I.3    Betensky, R.A.4    Shen, J.5    Selkoe, D.J.6
  • 242
    • 0033215457 scopus 로고    scopus 로고
    • Diphtheria toxin forms pores of different sizes depending on its concentration in membranes: Probable relationship to oligomerization
    • SHARPE, J. C. & LONDON, E. (1999). Diphtheria toxin forms pores of different sizes depending on its concentration in membranes: probable relationship to oligomerization. Journal of Membrane Biology 171, 209-221.
    • (1999) Journal of Membrane Biology , vol.171 , pp. 209-221
    • Sharpe, J.C.1    London, E.2
  • 243
    • 0029927679 scopus 로고    scopus 로고
    • Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement
    • SHIBATA, N., HIRANO, A., KOBAYASHI, M., SIDDIQUE, T., DENG, H. X., HUNG, W. Y., KATO, T. & ASAYAMA, K. (1996). Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement. Journal of Neuropathology & Experimental Neurology 55, 481-490.
    • (1996) Journal of Neuropathology & Experimental Neurology , vol.55 , pp. 481-490
    • Shibata, N.1    Hirano, A.2    Kobayashi, M.3    Siddique, T.4    Deng, H.X.5    Hung, W.Y.6    Kato, T.7    Asayama, K.8
  • 245
    • 0037177250 scopus 로고    scopus 로고
    • Molecular crowding accelerates fibrillization of alpha-synuclein: Could an increase in the cytoplasmic protein concentration induce Parkinson's disease?
    • SHTILERMAN, M. D., DING, T. T. & LANSBURY JR., P. T. (2002). Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease? Biochemistry 41, 3855-3860.
    • (2002) Biochemistry , vol.41 , pp. 3855-3860
    • Shtilerman, M.D.1    Ding, T.T.2    Lansbury Jr., P.T.3
  • 248
    • 31944449691 scopus 로고    scopus 로고
    • Evidence that Perutz's double-beta-stranded subunit structure for beta-amyloids also applies to their channel-forming structures in membranes
    • SINGER, S. J. & DEWJI, N. N. (2006). Evidence that Perutz's double-beta-stranded subunit structure for beta-amyloids also applies to their channel-forming structures in membranes. Proceedings of the National Academy of Sciences USA 103, 1546-1550.
    • (2006) Proceedings of the National Academy of Sciences USA , vol.103 , pp. 1546-1550
    • Singer, S.J.1    Dewji, N.N.2
  • 249
    • 1842507639 scopus 로고    scopus 로고
    • The law of mass action applied to neurodegenerative disease: A hypothesis concerning the aetiology and pathogenesis of complex diseases
    • SINGLETON, A., MYERS, A. & HARDY, J. (2004). The law of mass action applied to neurodegenerative disease: a hypothesis concerning the aetiology and pathogenesis of complex diseases. Human Molecular Genetics 13, R123-R126.
    • (2004) Human Molecular Genetics , vol.13
    • Singleton, A.1    Myers, A.2    Hardy, J.3
  • 252
    • 0038413759 scopus 로고    scopus 로고
    • Aggregated and monomeric alpha-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function
    • SNYDER, H., MENSAH, K., THEISLER, C., LEE, J., MATOUSCHEK, A. & WOLOZIN, B. (2003). Aggregated and monomeric alpha-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function. Journal of Biological Chemistry 278, 11753-11759.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 11753-11759
    • Snyder, H.1    Mensah, K.2    Theisler, C.3    Lee, J.4    Matouschek, A.5    Wolozin, B.6
  • 254
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • SONG, L., HOBAUGH, M. R., SHUSTAK, C., CHELEY, S., BAYLEY, H. & GOUAUX, J. E. (1996). Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274, 1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 255
    • 0036883535 scopus 로고    scopus 로고
    • Chaperones and aging: Role in neurodegeneration and in other civilizational diseases
    • SOTI, C. & CSERMELY, P. (2002). Chaperones and aging: role in neurodegeneration and in other civilizational diseases. Neurochemistry International 41, 383-389.
    • (2002) Neurochemistry International , vol.41 , pp. 383-389
    • Soti, C.1    Csermely, P.2
  • 256
    • 0035180285 scopus 로고    scopus 로고
    • Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: Evidence for toxicity of nonfibrillar aggregates
    • SOUSA, M. M., CARDOSO, I., FERNANDES, R., GUIMARAES, A. & SARAIVA, M. J. (2001). Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates. American Journal of Pathology 159, 1993-2000.
    • (2001) American Journal of Pathology , vol.159 , pp. 1993-2000
    • Sousa, M.M.1    Cardoso, I.2    Fernandes, R.3    Guimaraes, A.4    Saraiva, M.J.5
  • 258
    • 0032584686 scopus 로고    scopus 로고
    • Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies
    • SPILLANTINI, M. G., CROWTHER, R. A., JAKES, R., CAIRNS, N. J., LANTOS, P. L. & GOEDERT, M. (1998a). Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies. Neuroscience Letters 251, 205-208.
    • (1998) Neuroscience Letters , vol.251 , pp. 205-208
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Cairns, N.J.4    Lantos, P.L.5    Goedert, M.6
  • 261
    • 2542483823 scopus 로고    scopus 로고
    • ABri peptide associated with familial British dementia forms pore-like protofibrillar structures
    • SRINIVASAN, R., MARCHANT, R. & ZAGORSKI, M. (2004). ABri peptide associated with familial British dementia forms pore-like protofibrillar structures. Amyloid 11, 10-13.
    • (2004) Amyloid , vol.11 , pp. 10-13
    • Srinivasan, R.1    Marchant, R.2    Zagorski, M.3
  • 262
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • STEFANI, M. & DOBSON, C. M. (2003). Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. Journal of Molecular Medicine 81, 678-699.
    • (2003) Journal of Molecular Medicine , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 264
    • 0038176528 scopus 로고    scopus 로고
    • In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis
    • STINE JR., W. B., DAHLGREN, K. N., KRAFFT, G. A. & LADU, M. J. (2003). In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis. Journal of Biological Chemistry 278, 11612-11622.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 11612-11622
    • Stine Jr., W.B.1    Dahlgren, K.N.2    Krafft, G.A.3    Ladu, M.J.4
  • 267
    • 0034714236 scopus 로고    scopus 로고
    • Flammutoxin, a cytolysin from the edible mushroom Flammulina velutipes, forms two different types of voltage-gated channels in lipid bilayer membranes
    • TADJIBAEVA, G., SABIROV, R. & TOMITA, T. (2000). Flammutoxin, a cytolysin from the edible mushroom Flammulina velutipes, forms two different types of voltage-gated channels in lipid bilayer membranes. Biochimica et Biophysica Acta 1467, 431-443.
    • (2000) Biochimica et Biophysica Acta , vol.1467 , pp. 431-443
    • Tadjibaeva, G.1    Sabirov, R.2    Tomita, T.3
  • 271
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • TERRY, R. D., MASLIAH, E., SALMON, D. P., BUTTERS, N., DETERESA, R., HILL, R., HANSEN, L. A. & KATZMAN, R. (1991). Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment. Annals of Neurology 30, 572-580.
    • (1991) Annals of Neurology , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3    Butters, N.4    Deteresa, R.5    Hill, R.6    Hansen, L.A.7    Katzman, R.8
  • 272
    • 0037458564 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction
    • TIWARI, A. & HAYWARD, L. J. (2003). Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction. Journal of Biological Chemistry 278, 5984-5992.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 5984-5992
    • Tiwari, A.1    Hayward, L.J.2
  • 273
    • 0031474418 scopus 로고    scopus 로고
    • Contribution of somal Lewy bodies to neuronal death
    • TOMPKINS, M. M. & HILL, W. D. (1997). Contribution of somal Lewy bodies to neuronal death. Brain Research 775, 24-29.
    • (1997) Brain Research , vol.775 , pp. 24-29
    • Tompkins, M.M.1    Hill, W.D.2
  • 274
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: A potent role for trimers
    • TOWNSEND, M., SHANKAR, G. M., MEHTA, T., WALSH, D. M. & SELKOE, D. J. (2006). Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: a potent role for trimers. Journal of Physiology 572, 477-492.
    • (2006) Journal of Physiology , vol.572 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Mehta, T.3    Walsh, D.M.4    Selkoe, D.J.5
  • 275
    • 0042827316 scopus 로고    scopus 로고
    • Neuromuscular accumulation of mutant superoxide dismutase 1 aggregates in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • TURNER, B. J., LOPES, E. C. & CHEEMA, S. S. (2003). Neuromuscular accumulation of mutant superoxide dismutase 1 aggregates in a transgenic mouse model of familial amyotrophic lateral sclerosis. Neuroscience Letters 350, 132-136.
    • (2003) Neuroscience Letters , vol.350 , pp. 132-136
    • Turner, B.J.1    Lopes, E.C.2    Cheema, S.S.3
  • 276
    • 0036892683 scopus 로고    scopus 로고
    • Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis
    • URUSHITANI, M., KURISU, J., TSUKITA, K. & TAKAHASHI, R. (2002). Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis. Journal of Neurochemistry 83, 1030-1042.
    • (2002) Journal of Neurochemistry , vol.83 , pp. 1030-1042
    • Urushitani, M.1    Kurisu, J.2    Tsukita, K.3    Takahashi, R.4
  • 278
    • 0030735356 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin: Formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages
    • VALEVA, A., PALMER, M. & BHAKDI, S. (1997). Staphylococcal alpha-toxin: formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages. Biochemistry 36, 13298-13304.
    • (1997) Biochemistry , vol.36 , pp. 13298-13304
    • Valeva, A.1    Palmer, M.2    Bhakdi, S.3
  • 280
    • 0033600228 scopus 로고    scopus 로고
    • A stop-codon mutation in the BRI gene associated with familial British dementia
    • VIDAL, R., FRANGIONE, B., ROSTAGNO, A., MEAD, S., REVESZ, T., PLANT, G. & GHISO, J. (1999). A stop-codon mutation in the BRI gene associated with familial British dementia. Nature 399, 776-781.
    • (1999) Nature , vol.399 , pp. 776-781
    • Vidal, R.1    Frangione, B.2    Rostagno, A.3    Mead, S.4    Revesz, T.5    Plant, G.6    Ghiso, J.7
  • 281
    • 0037046163 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism
    • VOLLES, M. J. & LANSBURY JR., P. T. (2002). Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism. Biochemistry 41, 4595-4602.
    • (2002) Biochemistry , vol.41 , pp. 4595-4602
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 282
    • 0038386274 scopus 로고    scopus 로고
    • Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease
    • VOLLES, M. J. & LANSBURY JR., P. T. (2003). Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease. Biochemistry 42, 7871-7878.
    • (2003) Biochemistry , vol.42 , pp. 7871-7878
    • Volles, M.J.1    Lansbury Jr., P.T.2
  • 283
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar alpha-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease
    • VOLLES, M. J., LEE, S. J., ROCHET, J. C., SHTILERMAN, M. D., DING, T. T., KESSLER, J. C. & LANSBURY JR., P. T. (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 Jr., P.T.7
  • 284
    • 16544383250 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer
    • WACKER, J. L., ZAREIE, M. H., FONG, H., SARIKAYA, M. & MUCHOWSKI, P. J. (2004). Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer. Nature Structural & Molecular Biology 11, 1215-1222.
    • (2004) Nature Structural & Molecular Biology , vol.11 , pp. 1215-1222
    • Wacker, J.L.1    Zareie, M.H.2    Fong, H.3    Sarikaya, M.4    Muchowski, P.J.5
  • 285
    • 0026785678 scopus 로고
    • Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis
    • WALKER, B., KRISHNASASTRY, M., ZORN, L. & BAYLEY, H. (1992). Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis. Journal of Biological Chemistry 267, 21782-21786.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 21782-21786
    • Walker, B.1    Krishnasastry, M.2    Zorn, L.3    Bayley, H.4
  • 286
    • 0034695613 scopus 로고    scopus 로고
    • E. coli hemolysin e (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy
    • WALLACE, A. J., STILLMAN, T. J., ATKINS, A., JAMIESON, S. J., BULLOUGH, P. A., GREEN, J. & ARTYMIUK, P. J. (2000). E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy. Cell 100, 265-276.
    • (2000) Cell , vol.100 , pp. 265-276
    • Wallace, A.J.1    Stillman, T.J.2    Atkins, A.3    Jamieson, S.J.4    Bullough, P.A.5    Green, J.6    Artymiuk, P.J.7
  • 288
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • WALSH, D. M., KLYUBIN, I., FADEEVA, J. V., CULLEN, W. K., ANWYL, R., WOLFE, M. S., ROWAN, M. J. & SELKOE, D. J. (2002). Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416, 535-539.
    • (2002) Nature , vol.416 , 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    Rowan, M.J.7    Selkoe, D.J.8
  • 290
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain
    • WALSH, D. M., TSENG, B. P., RYDEL, R. E., PODLISNY, M. B. & SELKOE, D. J. (2000). The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain. Biochemistry 39, 10831-10839.
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 292
    • 0037058997 scopus 로고    scopus 로고
    • Murine apolipoprotein serum amyloid a in solution forms a hexamer containing a central channel
    • WANG, L., LASHUEL, H. A., WALZ, T. & COLON, W. (2002b). Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel. Proceedings of the National Academy of Sciences USA 99, 15947-15952.
    • (2002) Proceedings of the National Academy of Sciences USA , vol.99 , pp. 15947-15952
    • Wang, L.1    Lashuel, H.A.2    Walz, T.3    Colon, W.4
  • 293
    • 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
    • WANG, Q., WALSH, D. M., ROWAN, M. J., SELKOE, D. J. & ANWYL, R. (2004). 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. Journal of Neuroscience 24, 3370-3378.
    • (2004) Journal of Neuroscience , vol.24 , pp. 3370-3378
    • Wang, Q.1    Walsh, D.M.2    Rowan, M.J.3    Selkoe, D.J.4    Anwyl, R.5
  • 294
    • 0035664213 scopus 로고    scopus 로고
    • Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues
    • WATANABE, M., DYKES-HOBERG, M., CULOTTA, V. C., PRICE, D. L., WONG, P. C. & ROTHSTEIN, J. D. (2001). Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiology of Disease Journal 8, 933-941.
    • (2001) Neurobiology of Disease Journal , vol.8 , pp. 933-941
    • Watanabe, M.1    Dykes-Hoberg, M.2    Culotta, V.C.3    Price, D.L.4    Wong, P.C.5    Rothstein, J.D.6
  • 296
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • WEINREB, P. H., ZHEN, W., POON, A. W., CONWAY, K. A. & LANSBURY JR., P. T. (1996). NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35, 13709-13715.
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury Jr., P.T.5
  • 297
    • 0028298127 scopus 로고
    • Mutations and off-pathway aggregation of proteins
    • WETZEL, R. (1994). Mutations and off-pathway aggregation of proteins. Trends in Biotechnology 12, 193-198.
    • (1994) Trends in Biotechnology , vol.12 , pp. 193-198
    • Wetzel, R.1
  • 298
    • 26944437967 scopus 로고    scopus 로고
    • Small non-fibrillar assemblies of amyloid beta-protein bearing the Arctic mutation induce rapid neuritic degeneration
    • WHALEN, B. M., SELKOE, D. J. & HARTLEY, D. M. (2005). Small non-fibrillar assemblies of amyloid beta-protein bearing the Arctic mutation induce rapid neuritic degeneration. Neurobiology of Disease Journal 20, 254-266.
    • (2005) Neurobiology of Disease Journal , vol.20 , pp. 254-266
    • Whalen, B.M.1    Selkoe, D.J.2    Hartley, D.M.3
  • 299
    • 14744283139 scopus 로고    scopus 로고
    • Differential effects of oligomeric and fibrillar amyloid-beta 1-42 on astrocyte-mediated inflammation
    • WHITE, J. A., MANELLI, A. M., HOLMBERG, K. H., VAN ELDIK, L. J. & LADU, M. J. (2005). Differential effects of oligomeric and fibrillar amyloid-beta 1-42 on astrocyte-mediated inflammation. Neurobiology of Disease Journal 18, 459-465.
    • (2005) Neurobiology of Disease Journal , vol.18 , pp. 459-465
    • White, J.A.1    Manelli, A.M.2    Holmberg, K.H.3    Van Eldik, L.J.4    Ladu, M.J.5
  • 301
    • 0036278335 scopus 로고    scopus 로고
    • Dopamine-dependent neurotoxicity of alpha-synuclein: A mechanism for selective neurodegeneration in Parkinson disease
    • XU, J., KAO, S. Y., LEE, F. J., SONG, W., JIN, L.W. & YANKNER, B. A. (2002). Dopamine-dependent neurotoxicity of alpha-synuclein: a mechanism for selective neurodegeneration in Parkinson disease. Nature Medicine 8, 600-606.
    • (2002) Nature Medicine , vol.8 , pp. 600-606
    • Xu, J.1    Kao, S.Y.2    Lee, F.J.3    Song, W.4    Jin, L.W.5    Yankner, B.A.6
  • 304
    • 0037017399 scopus 로고    scopus 로고
    • Selective cytotoxicity of intracellular amyloid beta peptide 1-42 through p53 and Bax in cultured primary human neurons
    • ZHANG, Y., MCLAUGHLIN, R., GOODYER, C. & LEBLANC, A. (2002). Selective cytotoxicity of intracellular amyloid beta peptide 1-42 through p53 and Bax in cultured primary human neurons. Journal of Cell Biology 156, 519-529.
    • (2002) Journal of Cell Biology , vol.156 , pp. 519-529
    • Zhang, Y.1    McLaughlin, R.2    Goodyer, C.3    Leblanc, A.4
  • 305
    • 33750835937 scopus 로고    scopus 로고
    • Washington, DC: Society for Neuroscience, Program No. 132.12
    • ZHU, M. & FINK, A. L. (2003). Abstract Viewer/Itinerary Planner. Washington, DC: Society for Neuroscience, Program No. 132.12.
    • (2003) Abstract Viewer/Itinerary Planner
    • Zhu, M.1    Fink, A.L.2
  • 306
    • 3042547187 scopus 로고    scopus 로고
    • The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils
    • ZHU, M., RAJMANI, S., KAYLOR, J., HAN, S., ZHOU, F. & FINK, A. L. (2004). The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils. Journal of Biological Chemistry 279, 26846-26857.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 26846-26857
    • Zhu, M.1    Rajmani, S.2    Kaylor, J.3    Han, S.4    Zhou, F.5    Fink, A.L.6
  • 307
    • 0029004327 scopus 로고
    • Characterization of Vibrio cholerae El Tor cytolysin as an oligomerizing pore-forming toxin
    • ZITZER, A., WALEV, I., PALMER, M. & BHAKDI, S. (1995). Characterization of Vibrio cholerae El Tor cytolysin as an oligomerizing pore-forming toxin. Medical Microbiology and Immunology (Berlin) 184, 37-44.
    • (1995) Medical Microbiology and Immunology (Berlin) , vol.184 , pp. 37-44
    • Zitzer, A.1    Walev, I.2    Palmer, M.3    Bhakdi, S.4
  • 308


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.