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Volumn 648, Issue , 2010, Pages 25-41

Protein aggregation diseases: Toxicity of soluble prefibrillar aggregates and their clinical significance

(1)  Stefani, Massimo a  

a NONE

Author keywords

Amyloid; Amyloid cytotoxicity; Amyloid fibrils; Amyloid oligomers

Indexed keywords

PROTEIN; AMYLOID;

EID: 78649310717     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-60761-756-3_2     Document Type: Chapter
Times cited : (23)

References (105)
  • 1
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity, new insights into protein folding, misfolding diseases and biological evolution
    • Stefani M, Dobson CM (2003) Protein aggregation and aggregate toxicity, new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 81:678–699
    • (2003) J Mol Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333–366
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: New examples in medicine and biology of the dark side of the protein world
    • Stefani M (2004) Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim Biophys Acta 1739:5–25
    • (2004) Biochim Biophys Acta , vol.1739 , pp. 5-25
    • Stefani, M.1
  • 4
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe DJ (2003) Folding proteins in fatal ways. Nature 426:900–904
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 5
    • 0031934267 scopus 로고    scopus 로고
    • Genetically determined neuropathies
    • Reilly MM (1998) Genetically determined neuropathies. J Neurol 245:6–13
    • (1998) J Neurol , vol.245 , pp. 6-13
    • Reilly, M.M.1
  • 6
    • 0032006678 scopus 로고    scopus 로고
    • Alternative conformation of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly J (1998) Alternative conformation of amyloidogenic proteins and their multi-step assembly pathways. Curr Opin Struct Biol 8:101–106
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 101-106
    • Kelly, J.1
  • 7
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson CM (2001) The structural basis of protein folding and its links with human disease. Phil Trans R Soc Lond B 356:133–145
    • (2001) Phil Trans R Soc Lond B , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 10
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, Wolfe MS, Rowan MJ, Selkoe DJ (2002) Naturally secreted oligomers of amyloid β 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
  • 11
    • 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. Implication for pathogenesis and therapy
    • Conway KA, Lee S-J, Rochet JC, Ding TT, Williamson RE, Lansbury PT (2000) Acceleration of oligomerization not fibrillization is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson’s disease. Implication for pathogenesis and therapy. Proc Natl Acad Sci USA 97:571–576
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.-J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 12
    • 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, Deechingkit S, Jiang X, Kelly JW, Buxbaum JN (2004) Tissue damage in the amyloidoses: transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture. Proc Natl Acad Sci USA 101:2817–2822
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2817-2822
    • Reixach, N.1    Deechingkit, S.2    Jiang, X.3    Kelly, J.W.4    Buxbaum, J.N.5
  • 14
    • 0035849879 scopus 로고    scopus 로고
    • Cause of neuronal death in neurodegenerative diseases attributable to expansion of glutamine repeats
    • Perutz MF, Windle AH (2001) Cause of neuronal death in neurodegenerative diseases attributable to expansion of glutamine repeats. Nature 412:143–144
    • (2001) Nature , vol.412 , pp. 143-144
    • Perutz, M.F.1    Windle, A.H.2
  • 15
    • 0032503933 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by self-asso-ciation of a partially unfolded fibronectin type III module
    • Litvinovich SV, Brew SA, Aota S, Akiyama SK, Haudenschild C, Ingham KC (1998) Formation of amyloid-like fibrils by self-asso-ciation of a partially unfolded fibronectin type III module. J Mol Biol 280:245–258
    • (1998) J Mol Biol , vol.280 , pp. 245-258
    • Litvinovich, S.V.1    Brew, S.A.2    Aota, S.3    Akiyama, S.K.4    Haudenschild, C.5    Ingham, K.C.6
  • 18
    • 0035187228 scopus 로고    scopus 로고
    • Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain
    • Chiti F, Bucciantini M, Capanni C, Taddei N, Dobson CM, Stefani M (2001) Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain. Protein Sci 10:2541–2547
    • (2001) Protein Sci , vol.10 , pp. 2541-2547
    • Chiti, F.1    Bucciantini, M.2    Capanni, C.3    Taddei, N.4    Dobson, C.M.5    Stefani, M.6
  • 19
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fändrich M, Dobson CM (2002) The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J 21:5682–5690
    • (2002) EMBO J , vol.21 , pp. 5682-5690
    • Fändrich, M.1    Dobson, C.M.2
  • 20
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM (2003) Protein folding and misfolding. Nature 426:884–890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 21
    • 34547631623 scopus 로고    scopus 로고
    • Prevention of amyloid-like aggregation as a driving force of protein evolution
    • Monsellier E, Chiti F (2007) Prevention of amyloid-like aggregation as a driving force of protein evolution. EMBO Rep 8:737–742
    • (2007) EMBO Rep , vol.8 , pp. 737-742
    • Monsellier, E.1    Chiti, F.2
  • 22
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM (1999) Protein misfolding, evolution and disease. Trends Biochem Sci 24:329–332
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 23
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424:805–808
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 27
    • 0035920156 scopus 로고    scopus 로고
    • Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants
    • Quintas A, Vaz DC, Cardoso I, Saraiva MJM, Brito RMM (2001) Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants. J Biol Chem 276: 27207–27213
    • (2001) J Biol Chem , vol.276 , pp. 27207-27213
    • Quintas, A.1    Vaz, D.C.2    Cardoso, I.3    Saraiva, M.J.M.4    Brito, R.M.M.5
  • 29
    • 0036415838 scopus 로고    scopus 로고
    • α-Synuclein, especially the Parkinson’s disease-associated mutants, forms pore-like annular and tubular protofibrils
    • Lashuel HA, Petre BM, Wall J, Simon M, Nowak RJ, Walz T, Lansbury PT (2002) α-Synuclein, especially the Parkinson’s disease-associated mutants, forms pore-like annular and tubular protofibrils. J Mol Biol 322: 1089–1102
    • (2002) J Mol Biol , vol.322 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3    Simon, M.4    Nowak, R.J.5    Walz, T.6    Lansbury, P.T.7
  • 30
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrillization
    • Poirier MA, Li H, Macosko J, Cail S, Amzel M, Ross CA (2002) Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrillization. J Biol Chem 277:41032–41037
    • (2002) J Biol Chem , vol.277 , pp. 41032-41037
    • Poirier, M.A.1    Li, H.2    Macosko, J.3    Cail, S.4    Amzel, M.5    Ross, C.A.6
  • 31
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT (2003) Protofibrils, pores, fibrils and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26:267–298
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 32
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid β protein forms ion channels: Implications for Alzheimer’s disease pathophysiology
    • Lin H, Bhatia R, Lal R (2001) Amyloid β protein forms ion channels: implications for Alzheimer’s disease pathophysiology. FASEB J 15:2433–2444
    • (2001) FASEB J , vol.15 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 36
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • O’Nuallain B, Wetzel R (2002) Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci USA 99: 1485–1490
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1485-1490
    • O’Nuallain, B.1    Wetzel, R.2
  • 38
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren P-H, Laucker JE, Kachirskaia I, Heuser JE, Melki R, Kopito RR (2009) Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 11:219–225
    • (2009) Nat Cell Biol , vol.11 , pp. 219-225
    • Ren, P.-H.1    Laucker, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 39
    • 27644528932 scopus 로고    scopus 로고
    • A single disulfide bond differentiates aggregation pathways of β2-microglobulin
    • Chen Y, Kokholyan N (2005) A single disulfide bond differentiates aggregation pathways of β2-microglobulin. J Mol Biol 354: 473–482
    • (2005) J Mol Biol , vol.354 , pp. 473-482
    • Chen, Y.1    Kokholyan, N.2
  • 43
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Novitskaya V, Bocharova OV, Bronstein I, Baskakov IV (2006) Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J Biol Chem 281:13828–13836
    • (2006) J Biol Chem , vol.281 , pp. 13828-13836
    • Novitskaya, V.1    Bocharova, O.V.2    Bronstein, I.3    Baskakov, I.V.4
  • 45
    • 0034994097 scopus 로고    scopus 로고
    • Pore formation by beta-2-microglobulin: A mechanism for the pathogenesis of dialysis-associated amyloidosis
    • Hirakura Y, Kagan BL (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
  • 47
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers on the brain, the emerging role of soluble protein aggregates in neurodegeneration
    • Walsh DM, Selkoe DJ (2004) Oligomers on the brain, the emerging role of soluble protein aggregates in neurodegeneration. Protein Peptide Lett 11:1–16
    • (2004) Protein Peptide Lett , vol.11 , pp. 1-16
    • Walsh, D.M.1    Selkoe, D.J.2
  • 49
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers on amyloid β-protein on hippocampal synaptic plasticity: A potent role for trimers
    • Townsend M, Shankar GM, Mehta T, Walsh DM, Selkoe DJ (2006) Effects of secreted oligomers on amyloid β-protein on hippocampal synaptic plasticity: a potent role for trimers. J Physiol 572(2):477–492
    • (2006) J Physiol , vol.572 , Issue.2 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Mehta, T.3    Walsh, D.M.4    Selkoe, D.J.5
  • 51
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer’s disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong Y, Chang I, Viola KI, Lacor PN, Lambert MP, Finch CE, Krafft GA, Klein WI (2003) Alzheimer’s disease-affected brain: presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc Natl Acad Sci USA 100:10417–10422
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, I.2    Viola, K.I.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6    Krafft, G.A.7    Klein, W.I.8
  • 54
    • 0037975676 scopus 로고    scopus 로고
    • Spherical aggregates of β-amyloid (Amylo-spheroid show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β
    • Hoshi M, Sato M, Matsumoto S, Noguchi A, Yasutake K, Yoshida N, Sato K (2003) Spherical aggregates of β-amyloid (amylo-spheroid show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3β. Proc Natl Acad Sci USA 100:6370–6375
    • (2003) Proc Natl Acad Sci 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
  • 55
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid β-protein begins intracellularly in cell derived from human brain
    • Walsh DM, Tseng BP, Rydel RE, Podlisny MB, Selkoe DJ (2000) The oligomerization of amyloid β-protein begins intracellularly in cell 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
  • 56
    • 14644442872 scopus 로고    scopus 로고
    • Intraneuronal Aβ causes the onset of early Alzheimer’s disease-related cognitive deficits in transgenic mice
    • Billings LM, Oddo S, Green KN, McGaugh JL, LaFerla F (2005) Intraneuronal Aβ causes the onset of early Alzheimer’s disease-related cognitive deficits in transgenic mice. Neuron 45:675–688
    • (2005) Neuron , vol.45 , pp. 675-688
    • Billings, L.M.1    Oddo, S.2    Green, K.N.3    McGaugh, J.L.4    Laferla, F.5
  • 57
    • 0029078972 scopus 로고
    • Correlation of synaptic and pathological markers with cognition of the elderly
    • Dickson DW (1995) Correlation of synaptic and pathological markers with cognition of the elderly. Neurobiol Aging 16:285–298
    • (1995) Neurobiol Aging , vol.16 , pp. 285-298
    • Dickson, D.W.1
  • 63
    • 0000694354 scopus 로고
    • Wheaterall DJ, Ledingham JG, Warrel DA (eds), 3rd Edition, Oxford University Press, Oxford
    • Pepys MB (1995) In: Wheaterall DJ, Ledingham JG, Warrel DA (eds) Oxford textbook of medicine, 3rd Edition, Oxford University Press, Oxford, pp 1512–1524.
    • (1995) Oxford Textbook of Medicine , pp. 1512-1524
    • Pepys, M.B.1
  • 64
    • 0007862386 scopus 로고
    • Alzheimer’s disease amyloid beta protein forms calcium channels in bilayer membranes: Blockade by tromethamine and alu-minium
    • Arispe N, Rojas E, Pollard HD (1993) Alzheimer’s disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and alu-minium. Proc Natl Acad Sci USA 89: 10940–10944
    • (1993) Proc Natl Acad Sci USA , vol.89 , pp. 10940-10944
    • Arispe, N.1    Rojas, E.2    Pollard, H.D.3
  • 65
    • 0030044018 scopus 로고    scopus 로고
    • Pore formation by the cytotoxic islet amyloid peptide amylin
    • Mirzabekov TA, Lin MC, Kagan BL (1996) Pore formation by the cytotoxic islet amyloid peptide amylin. J Biol Chem 271:1988–1992
    • (1996) J Biol Chem , vol.271 , pp. 1988-1992
    • Mirzabekov, T.A.1    Lin, M.C.2    Kagan, B.L.3
  • 66
    • 0033028498 scopus 로고    scopus 로고
    • Synthetic C-type mammalian natriuretic peptide forms large cation selective channels
    • Kourie JI (1999) Synthetic C-type mammalian natriuretic peptide forms large cation selective channels. FEBS Lett 445:57–62
    • (1999) FEBS Lett , vol.445 , pp. 57-62
    • Kourie, J.I.1
  • 67
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar α-synuclein: Comparison of wild-type with Parkinson’s disease linked mutants and insights in the mechanisms
    • Volles MJ, Lansbury PT (2001) Vesicle permeabilization by protofibrillar α-synuclein: comparison of wild-type with Parkinson’s disease linked mutants and insights in the mechanisms. Biochemistry 40:7812–7819
    • (2001) Biochemistry , vol.40 , pp. 7812-7819
    • Volles, M.J.1    Lansbury, P.T.2
  • 68
    • 0034089960 scopus 로고    scopus 로고
    • Fresh and nonfibrillar amyloid β protein (1-40) induces rapid cellular degeneration in aged human fibroblasts: Evidence for AβP-channel-mediated cellular toxicity
    • Zhu YJ, Lin H, Lal R (2000) Fresh and nonfibrillar amyloid β protein (1-40) induces rapid cellular degeneration in aged human fibroblasts: evidence for AβP-channel-mediated cellular toxicity. FASEB J 14:1244–1254
    • (2000) FASEB J , vol.14 , pp. 1244-1254
    • Zhu, Y.J.1    Lin, H.2    Lal, R.3
  • 69
    • 33747195017 scopus 로고    scopus 로고
    • An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity
    • Ferreiro E, Resende R, Costa R, Oliveira C, Pereira CMF (2006) An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity. Neurobiol Dis 23:669–678
    • (2006) Neurobiol Dis , vol.23 , pp. 669-678
    • Ferreiro, E.1    Resende, R.2    Costa, R.3    Oliveira, C.4    Pereira, C.M.F.5
  • 70
    • 26444588771 scopus 로고    scopus 로고
    • Gradual alteration of mitochondrial structure and function by beta-amyloids: Importance of membrane viscosity changes, energy deprivation, reactive oxygen species production, and cytochrome c release
    • Aleardi AM, Bernard G, Augereau O, Malgat M, Talbot JC, Mazat JP, Letellier T, Dachary-Prigent J, Solaini GC, Rossignol R (2005) Gradual alteration of mitochondrial structure and function by beta-amyloids: importance of membrane viscosity changes, energy deprivation, reactive oxygen species production, and cytochrome c release. J Bioenerg Biomem 37:207–225
    • (2005) J Bioenerg Biomem , vol.37 , pp. 207-225
    • Aleardi, A.M.1    Bernard, G.2    Augereau, O.3    Malgat, M.4    Talbot, J.C.5    Mazat, J.P.6    Letellier, T.7    Dachary-Prigent, J.8    Solaini, G.C.9    Rossignol, R.10
  • 71
    • 33751218015 scopus 로고    scopus 로고
    • Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid
    • King ME, Kan H-M, Baas PW, Erisir A, Glabe CG, Bloom S (2006) Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid. J Cell Biol 175:541–546
    • (2006) J Cell Biol , vol.175 , pp. 541-546
    • King, M.E.1    Kan, H.-M.2    Baas, P.W.3    Erisir, A.4    Glabe, C.G.5    Bloom, S.6
  • 73
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defences against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman MY, Goldberg AL (2001) Cellular defences against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29:15–32
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 74
    • 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, Sokolow Y, Edmonds B, McIntire TM, Milton SC, Hall JE, Glabe CG (2004) Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J Biol Chem 279:46363–46366
    • (2004) J Biol Chem , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolow, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 75
    • 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 SC, Parker I, Glabe CG (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280:17294–17300
    • (2005) J Biol Chem , 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
  • 76
    • 0033946014 scopus 로고    scopus 로고
    • Properties of cytotoxic peptide-induced ion channels
    • Kourie JI, Shorthouse AA (2000) Properties of cytotoxic peptide-induced ion channels. Am J Physiol Cell Physiol 278:C1063–C1087
    • (2000) Am J Physiol Cell Physiol , vol.278 , pp. C1063-C1087
    • Kourie, J.I.1    Shorthouse, A.A.2
  • 77
    • 0037058997 scopus 로고    scopus 로고
    • Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel
    • Wang L, Lashuel HA, Walz T, Colòn W (2002) Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel. Proc Natl Acad Sci USA 99:15947–15952
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15947-15952
    • Wang, L.1    Lashuel, H.A.2    Walz, T.3    Colòn, W.4
  • 79
    • 2542483823 scopus 로고    scopus 로고
    • ABri peptide associated with familial British dementia forms annular and ring-like protofibrillar structures
    • Srinivasan R, Marchant RE, Zagorski MG (2004) ABri peptide associated with familial British dementia forms annular and ring-like protofibrillar structures. Amyloid 11:10–13
    • (2004) Amyloid , vol.11 , pp. 10-13
    • Srinivasan, R.1    Marchant, R.E.2    Zagorski, M.G.3
  • 81
    • 0035478618 scopus 로고    scopus 로고
    • Beta-amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand
    • Morishima Y, Gotoh Y, Zieg J, Barrett T, Takano H, Flavell R, Davis RJ, Shirasaki Y, Greenberg ME (2001) Beta-amyloid induces neuronal apoptosis via a mechanism that involves the c-Jun N-terminal kinase pathway and the induction of Fas ligand. J Neurosci 21:7551–7560
    • (2001) J Neurosci , vol.21 , pp. 7551-7560
    • Morishima, Y.1    Gotoh, Y.2    Zieg, J.3    Barrett, T.4    Takano, H.5    Flavell, R.6    Davis, R.J.7    Shirasaki, Y.8    Greenberg, M.E.9
  • 82
    • 0034853813 scopus 로고    scopus 로고
    • Ultrastructure evidence of necrotic neural cell death in familial Alzheimer’s disease brains bearing presenilin-1 E280A mutation
    • Velez-Pardo C, Arroyave ST, Lopera F, Castano AD, Jimenez Del Rio M (2001) Ultrastructure evidence of necrotic neural cell death in familial Alzheimer’s disease brains bearing presenilin-1 E280A mutation. J Alzheimer’s Dis 3:409–415
    • (2001) J Alzheimer’s Dis , vol.3 , pp. 409-415
    • Velez-Pardo, C.1    Arroyave, S.T.2    Lopera, F.3    Castano, A.D.4    Jimenez Del Rio, M.5
  • 84
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington’s disease and related disorders
    • Ross CA (2002) Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington’s disease and related disorders. Neuron 35:819–822
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.A.1
  • 85
    • 33845411954 scopus 로고    scopus 로고
    • AMPAR removal underlies Aβ-induced synaptic depression and dendritic spine loss
    • Hsieh H, Boehm J, Sato C, Iwatsubo T, Tomita T, Sisodia S, Malinow R (2006) AMPAR removal underlies Aβ-induced synaptic depression and dendritic spine loss. Neuron 52:831–843
    • (2006) Neuron , vol.52 , pp. 831-843
    • Hsieh, H.1    Boehm, J.2    Sato, C.3    Iwatsubo, T.4    Tomita, T.5    Sisodia, S.6    Malinow, R.7
  • 86
    • 34249672242 scopus 로고    scopus 로고
    • Aβ oligomers induce neuronal oxidative stress through an N-methyl-d-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice FG, Velasco PT, Lambert MP, Viola K, Fernandez SJ, Ferreira ST, Klein WL (2007) Aβ oligomers induce neuronal oxidative stress through an N-methyl-d-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J Biol Chem 282:11590–11601
    • (2007) J Biol Chem , vol.282 , pp. 11590-11601
    • de Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5    Ferreira, S.T.6    Klein, W.L.7
  • 88
    • 10944241542 scopus 로고    scopus 로고
    • Tau alteration and neuronal degeneration in tauopathies: Mechanisms and models
    • Brandt R, Hundelt M, Shahani N (2004) Tau alteration and neuronal degeneration in tauopathies: mechanisms and models. Biochim Biophys Acta 1739:331–354
    • (2004) Biochim Biophys Acta , vol.1739 , pp. 331-354
    • Brandt, R.1    Hundelt, M.2    Shahani, N.3
  • 89
    • 33751172145 scopus 로고    scopus 로고
    • Distinct destructive signal pathways of neuronal death in Alzheimer’s disease
    • Shen Y, He P, Zhong Z, McAllister C, Lindholm K (2006) Distinct destructive signal pathways of neuronal death in Alzheimer’s disease. Trends Mol Med 12:574–579
    • (2006) Trends Mol Med , vol.12 , pp. 574-579
    • Shen, Y.1    He, P.2    Zhong, Z.3    McAllister, C.4    Lindholm, K.5
  • 91
    • 0035955513 scopus 로고    scopus 로고
    • α-Lipoic acid protects rat cortical neurons against cell death induced by amyloid and hydrogen peroxide through the Akt signalling pathway
    • Zhang L, Xing Gq, Barker JL, Chang Y, Maric D, Ma W, Li B-s, Rubinow DR (2001) α-Lipoic acid protects rat cortical neurons against cell death induced by amyloid and hydrogen peroxide through the Akt signalling pathway. Neurosci Lett 312:125–128
    • (2001) Neurosci Lett , vol.312 , pp. 125-128
    • Zhang, L.1    Gq, X.2    Barker, J.L.3    Chang, Y.4    Maric, D.5    Ma, W.6    Li, B.-S.7    Rubinow, D.R.8
  • 93
    • 0034087369 scopus 로고    scopus 로고
    • Decreased levels of proteasome activity and proteasome expression in aging spinal cord
    • Keller JN, Huang FF, Markesbery WR (2002) Decreased levels of proteasome activity and proteasome expression in aging spinal cord. Neuroscience 98:149–156
    • (2002) Neuroscience , vol.98 , pp. 149-156
    • Keller, J.N.1    Huang, F.F.2    Markesbery, W.R.3
  • 94
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzeimer’s disease brain: Central role for amyloid β-peptide
    • Butterfield AD, Drake J, Pocernich C, Castegna A (2001) Evidence of oxidative damage in Alzeimer’s disease brain: central role for amyloid β-peptide. Trends Mol Med 7:548–554
    • (2001) Trends Mol Med , vol.7 , pp. 548-554
    • Butterfield, A.D.1    Drake, J.2    Pocernich, C.3    Castegna, A.4
  • 95
    • 0033860372 scopus 로고    scopus 로고
    • Alzheimer’s amyloid β-peptide-associated free radical oxidative stress and neurotoxicity
    • Varadarajan S, Yatin S, Aksenova M, Butterfield DA (2000) Alzheimer’s amyloid β-peptide-associated free radical oxidative stress and neurotoxicity. J Struct Biol 130:184–208
    • (2000) J Struct Biol , vol.130 , pp. 184-208
    • Varadarajan, S.1    Yatin, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 96
    • 0034881033 scopus 로고    scopus 로고
    • Oxidative stress and protein aggregation during biological aging
    • Squier TC (2001) Oxidative stress and protein aggregation during biological aging. Exp Gerontol 36:1539–1550
    • (2001) Exp Gerontol , vol.36 , pp. 1539-1550
    • Squier, T.C.1
  • 97
    • 22144492630 scopus 로고    scopus 로고
    • Disruption of calcium homeostasis in the pathogenesis of Alzheimer’s disease and other conformational diseases
    • Kawahara M (2004) Disruption of calcium homeostasis in the pathogenesis of Alzheimer’s disease and other conformational diseases. Curr Alz Res 1:87–95
    • (2004) Curr Alz Res , vol.1 , pp. 87-95
    • Kawahara, M.1
  • 100
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intracellular environment
    • Ellis RJ (2001) Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr Opin Struct Biol 11:114–119
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 114-119
    • Ellis, R.J.1
  • 101
    • 0033572725 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on protein folding and aggregation
    • van den Berg B, Ellis J, Dobson CM (1999) Effects of macromolecular crowding on protein folding and aggregation. EMBO J 18:6927–6933
    • (1999) EMBO J , vol.18 , pp. 6927-6933
    • van den Berg, B.1    Ellis, J.2    Dobson, C.M.3
  • 102
    • 0036891466 scopus 로고    scopus 로고
    • Phosphatidylserine is a marker of tumour vasculature and a potential target for cancer imaging and therapy
    • Ran S, Thorpe PE (2002) Phosphatidylserine is a marker of tumour vasculature and a potential target for cancer imaging and therapy. Int J Radiat Oncol Biol Phys 54: 1479–1484
    • (2002) Int J Radiat Oncol Biol Phys , vol.54 , pp. 1479-1484
    • Ran, S.1    Thorpe, P.E.2
  • 103
    • 58149216444 scopus 로고    scopus 로고
    • Protein folding, misfolding and aggregation on surfaces
    • Stefani M (2008) Protein folding, misfolding and aggregation on surfaces. Int J Mol Sci 9:2515–2542
    • (2008) Int J Mol Sci , vol.9 , pp. 2515-2542
    • Stefani, M.1
  • 104
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid β induce neurotoxicity by distinct mechanisms in human cortical neurons
    • Deshpande A, Mina E, Glabe C, Busciglio J (2006) Different conformations of amyloid β induce neurotoxicity by distinct mechanisms in human cortical neurons. J Neurosci 26: 6011–6018
    • (2006) J Neurosci , vol.26 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 105
    • 67649856863 scopus 로고    scopus 로고
    • Distinct conformations of in vitro and vivo amyloids of huntingtin-exon 1 show different cytotoxicity
    • Nekooki-Machida Y, Kurosawa M, Nukina N, Ito K, Tanaka M (2009) Distinct conformations of in vitro and vivo amyloids of huntingtin-exon 1 show different cytotoxicity. Proc Natl Acad Sci USA 106:9679–9684
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9679-9684
    • Nekooki-Machida, Y.1    Kurosawa, M.2    Nukina, N.3    Ito, K.4    Tanaka, M.5


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