Therapeutic strategies against protein misfolding in neurodegenerative diseases

Bibliography

• Makin OS, Serpell LC. Examining the structure of the mature amyloid fibril. Biochem Soc Trans 2002;30:521-5
   PubMed Web of Science ®Google Scholar
• Soto C. Unfolding the role of Protein Misfolding in Neurodegenerative Diseases. Nat Rev Neurosci 2003;4:49-60
   PubMed Web of Science ®Google Scholar
• Glenner GG, Wong CW. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 1984;120:885-90
   PubMed Web of Science ®Google Scholar
• Grundke-Iqbal I, Iqbal K, Quinlan M, et al. Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J Biol Chem 1986;261:6084-9
   PubMed Web of Science ®Google Scholar
• Spillantini MG, Schmidt ML, Lee VM, et al. Alpha-synuclein in Lewy bodies. Nature 1997;388:839-40
   PubMed Web of Science ®Google Scholar
• DiFiglia M, Sapp E, Chase KO, et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 1997;277:1990-3
   PubMed Web of Science ®Google Scholar
• Bruijn LI, Houseweart MK, Kato S. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 1998;281:1851-4
   PubMed Web of Science ®Google Scholar
• Bolton DC, McKinley MP, Prusiner SB. Identification of a protein that purifies with the scrapie prion. Science 1982;218:1309-11
   PubMed Web of Science ®Google Scholar
• Hardy J, Gwinn-Hardy K. Genetic classification of primary neurodegenerative disease. Science 1998;282:1075-9
   PubMed Web of Science ®Google Scholar
• Goate A, Chartier-Harlin MC, Mullan M, et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 1991;349:704-6
   PubMed Web of Science ®Google Scholar
• The Huntington's Disease Collaborative Research Group (HDCRG) A novel gene containing a trinucleotide repeat that is unstable on Huntington's disease chromosomes. Cell 1993;72:971-83
   PubMed Web of Science ®Google Scholar
• Hsiao K, Baker HF, Crow TJ, et al. Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome. Nature 1989;338:342-5
   PubMed Web of Science ®Google Scholar
• Rosen DR, Siddique T, Patterson D, et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 1993;362:59-62
   PubMed Web of Science ®Google Scholar
• Hsiao KK, Scott M, Foster D, et al. Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science 1990;250:1587-90
   PubMed Web of Science ®Google Scholar
• Games D, Adams D, Alessandrini R, et al. Alzheimer-type neuropathology in transgenic mice overexpressing V717F beta-amyloid precursor protein. Nature 1995;373:523-7
   PubMed Web of Science ®Google Scholar
• Hsiao K, Chapman P, Nilsen S, et al. Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Science 1996;274:99-102
   PubMed Web of Science ®Google Scholar
• Masliah E, Rockenstein E, Veinbergs I, et al. Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders. Science 2000;287:1265-9
   PubMed Web of Science ®Google Scholar
• Gurney ME, Pu H, Chiu AY. Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science 1994;264:1772-5
   PubMed Web of Science ®Google Scholar
• Mangiarini L, Sathasivam K, Seller M, et al. Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice. Cell 1996;87:493-506
   PubMed Web of Science ®Google Scholar
• Davies SW, Turmaine M, Cozens BA, et al. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 1997;90:537-48
   PubMed Web of Science ®Google Scholar
• DeArmond SJ, Yang SL, Cayetano-Canlas J, et al. The neuropathological phenotype in transgenic mice expressing different prion protein constructs. Philos Trans R Soc Lond B Biol Sci 1994;343:415-23
   PubMed Web of Science ®Google Scholar
• Moechars D, Dewachter I, Lorent K, et al. Early phenotypic changes in transgenic mice that overexpress different mutants of amyloid precursor protein in brain. J Biol Chem 1999;274:6483-92
   PubMed Web of Science ®Google Scholar
• Klement IA, Skinner PJ, Kaytor MD, et al. Ataxin-1 nuclear localization and aggregation: role in polyglutamine- induced disease in SCA1 transgenic mice. Cell 1998;95:41-53
   PubMed Web of Science ®Google Scholar
• Demuro A, Mina E, Kayed R, et al. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 2005;280:17294-300
   PubMed Web of Science ®Google Scholar
• Osborne BM, Butler JJ, Mackay B. Proteinaceous lymphadenopathy with hypergammaglobulinemia. Am J Surg Pathol 1979;3:137-45
   PubMed Web of Science ®Google Scholar
• Wolman M, Bubis JJ. The cause of the green polarization color of amyloid stained with congo red. Histochem 1965;4:351-6
   Google Scholar
• Harper JD, Lansbury PT Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 1997;66:385-407
   PubMed Web of Science ®Google Scholar
• Gajdusek DC. Nucleation of amyloidogenesis in infectious and noninfectious amyloidoses of brain. Ann NY Acad Sci 1994;724:173-90
   PubMed Web of Science ®Google Scholar
• Jarrett JT, Lansbury PT Jr. Seeding “one-dimensional crystallization” of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993;73:1055-8
   PubMed Web of Science ®Google Scholar
• Krebs MR, Morozova-Roche LA, Daniel K. Observation of sequence specificity in the seeding of protein amyloid fibrils. Protein Sci 2004;13:1933-8
   PubMed Web of Science ®Google Scholar
• O'Nuallain B, Williams AD, Westermark P, et al. Seeding specificity in amyloid growth induced by heterologous fibrils. J Biol Chem 2004;279:17490-9
   PubMed Web of Science ®Google Scholar
• Glabe CG. Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. Neurobiol Aging 2006;27:570-5
   PubMed Web of Science ®Google Scholar
• Walsh DM, Selkoe DJ. Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept Lett 2004;11:213-28
   PubMed Web of Science ®Google Scholar
• Kelly JW. Alternative conformations of amyloidogenic proteins govern their behavior. Curr Opin Struct Biol 1996;6:11-17
   PubMed Web of Science ®Google Scholar
• Soto C. Alzheimer's and prion disease as disorders of protein conformation: implications for the design of novel therapeutic approaches. J Mol Med 1999;77:412-8
   PubMed Web of Science ®Google Scholar
• Carrell RW, Gooptu B. Conformational changes and disease–serpins, prions and Alzheimer's. Curr Opin Struct Biol 1998;8:799-809
   PubMed Web of Science ®Google Scholar
• Serpell LC, Sunde M, Fraser PE, et al. Examination of the structure of the transthyretin amyloid fibril by image reconstruction from electron micrographs. J Mol Biol 1995;254:113-8
   PubMed Web of Science ®Google Scholar
• Chromy BA, Nowak RJ, Lambert MP, et al. Self-assembly of Abeta(1-42) into globular neurotoxins. Biochemistry 2003;42:12749-60
   PubMed Web of Science ®Google Scholar
• Simoneau S, Rezaei H, Sales N, et al. In vitro and in vivo neurotoxicity of prion protein oligomers. PLoS Pathog 2007;3:e125
   PubMed Web of Science ®Google Scholar
• Bucciantini M, Calloni G, Chiti F, et al. Prefibrillar amyloid protein aggregates share common features of cytotoxicity. J Biol Chem 2004;279:31374-82
   PubMed Web of Science ®Google Scholar
• Wang HW, Pasternak JF, Kuo H, et al. Soluble oligomers of beta amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus. Brain Res 2002;924:133-40
   PubMed Web of Science ®Google Scholar
• Cleary JP, Walsh DM, Hofmeister JJ, et al. Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat Neurosci 2004;8:79-84
   PubMed Web of Science ®Google Scholar
• Shankar GM, Li S, Mehta TH, et al. Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 2008;14:837-42
   PubMed Web of Science ®Google Scholar
• Walsh DM, Hartley DM, Kusumoto Y, et al. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem 1999;274:25945-52
   PubMed Web of Science ®Google Scholar
• Harper JD, Wong SS, Lieber CM, et al. Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease. Biochemistry 1999;38:8972-80
   PubMed Web of Science ®Google Scholar
• Srinivasan R, Marchant RE, Zagorski MG. ABri peptide associated with familial British dementia forms annular and ring-like protofibrillar structures. Amyloid 2004;11:10-13
   PubMed Web of Science ®Google Scholar
• Lashuel HA, Hartley D, Petre BM, et al. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 2002;418:291
   PubMed Web of Science ®Google Scholar
• Modler AJ, Gast K, Lutsch G, Damaschun G. Assembly of amyloid protofibrils via critical oligomers – a novel pathway of amyloid formation. J Mol Biol 2003;325:135-48
   PubMed Web of Science ®Google Scholar
• Hartley DM, Walsh DM, Ye CP, et al. Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci 1999;19:8876-84
   PubMed Web of Science ®Google Scholar
• Teplow DB. Structural and kinetic features of amyloid beta-protein fibrillogenesis. Amyloid 1998;5:121-42
   PubMed Web of Science ®Google Scholar
• Levine H III. Soluble multimeric Alzheimer beta(1-40) pre-amyloid complexes in dilute solution. Neurobiol Aging 1995;16:755-64
   PubMed Web of Science ®Google Scholar
• Cardone M. Prospects for gene therapy in inherited neurodegenerative diseases. Curr Opin Neurol 2007;20:151-8
   PubMed Web of Science ®Google Scholar
• Boudreau RL, Davidson BL. RNAi therapy for neurodegenerative diseases. Curr Top Dev Biol 2006;75:73-92
   PubMed Web of Science ®Google Scholar
• Koutsilieri E, Rethwilm A, Scheller C. The therapeutic potential of siRNA in gene therapy of neurodegenerative disorders. J Neural Transm Suppl 2007;72 43-9
   PubMedGoogle Scholar
• Kan I, Melamed E, Offen D. Autotransplantation of bone marrow-derived stem cells as a therapy for neurodegenerative diseases. Handb Exp Pharmacol 2007;180 219-42
   PubMedGoogle Scholar
• Sonntag KC, Sanchez-Pernaute R. Tailoring human embryonic stem cells for neurodegenerative disease therapy. Curr Opin Investig Drugs 2006;7:614-8
   PubMed Web of Science ®Google Scholar
• Cohen FE, Kelly JW. Therapeutic approaches to protein-misfolding diseases. Nature 2003;426:905-9
   PubMed Web of Science ®Google Scholar
• Salomon AR, Marcinowski KJ, Friedland RP, Zagorski MG. Nicotine inhibits amyloid formation by the beta-peptide. Biochemistry 1996;35:13568-78
   PubMed Web of Science ®Google Scholar
• Ono K, Hasegawa K, Yamada M, Naiki H. Nicotine breaks down preformed Alzheimer's beta-amyloid fibrils in vitro. Biological Psychiatry 2002;52:880-6
   PubMed Web of Science ®Google Scholar
• Tatzelt J, Prusiner SB, Welch WJ. Chemical chaperones interfere with the formation of scrapie prion protein. EMBO J 1996;15:6363-73
   PubMed Web of Science ®Google Scholar
• Bennion BJ, DeMarco ML, Daggett V. Preventing misfolding of the prion protein by trimethylamine N-oxide. Biochemistry 2004;43:12955-63
   PubMed Web of Science ®Google Scholar
• Adamski-Werner SL, Palaninathan SK, Sacchettini JC, Kelly JW. Diflunisal Analogues Stabilize the Native State of Transthyretin. Potent Inhibition of Amyloidogenesis. J Med Chem 2004;47:355-74
   PubMed Web of Science ®Google Scholar
• Hammarstrom P, Wiseman RL, Powers ET, Kelly JW. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 2003;99:713-6
   Google Scholar
• Hammarstrom P, Schneider F, Kelly JW. Trans-suppression of misfolding in an amyloid disease. Science 2001;293:2459-62
   PubMed Web of Science ®Google Scholar
• Miroy GJ, Lai Z, Lashuel HA, et al. Inhibiting transthyretin amyloid fibril formation via protein stabilization. Proc Natl Acad Sci USA 1996;93:15051-6
   PubMed Web of Science ®Google Scholar
• Villegas V, Zurdo J, Filimonov VV, et al. Protein engineering as a strategy to avoid formation of amyloid fibrils. Protein Sci 2000;9:1700-8
   PubMed Web of Science ®Google Scholar
• Yamamoto A, Lucas JJ, Hen R. Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease. Cell 2000;101:57-66
   PubMed Web of Science ®Google Scholar
• Mallucci GR, Ratte S, Asante EA, et al. Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. EMBO J 2002;21:202-10
   PubMed Web of Science ®Google Scholar
• Mallucci G, Dickinson A, Linehan J, et al. Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis. Science 2003;302:871-4
   PubMed Web of Science ®Google Scholar
• Mallucci GR, White MD, Farmer M, et al. Targeting cellular prion protein reverses early cognitive deficits and neurophysiological dysfunction in prion-infected mice. Neuron 2007;53:325-35
   PubMed Web of Science ®Google Scholar
• Schenk D, Barbour R, Dunn W, et al. Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 1999;400:173-7
   PubMed Web of Science ®Google Scholar
• Solomon B, Koppel R, Hanan E, Katzav T. Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer beta-amyloid peptide. Proc Natl Acad Sci USA 1996;93:452-5
   PubMed Web of Science ®Google Scholar
• Solomon B, Koppel R, Frankel D, Hanan-Aharon E. Disaggregation of Alzheimer beta-amyloid by site-directed mAb. Proc Natl Acad Sci USA 1997;94:4109-12
   PubMed Web of Science ®Google Scholar
• Morgan D, Diamond DM, Gottschall PE, et al. A beta peptide vaccination prevents memory loss in an animal model of Alzheimer's disease. Nature 2000;408:982-5
   PubMed Web of Science ®Google Scholar
• Janus C, Pearson J, McLaurin J, et al. A beta peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature 2000;408:979-82
   PubMed Web of Science ®Google Scholar
• McGavern DB. Immunotherapeutic relief from persistent infections and amyloid disorders. Neurology 2006;66:S59-64
   PubMed Web of Science ®Google Scholar
• McGeer EG, McGeer PL, McGeer EG, McGeer PL. Abeta immunotherapy and other means to remove amyloid. Curr Drug Targets CNS Neurol Disord 2005;4:569-73
   PubMedGoogle Scholar
• Gandy S, Heppner FL. Alzheimer's amyloid immunotherapy: quo vadis? Lancet Neurol 2005;4:452-3
   PubMed Web of Science ®Google Scholar
• Sigurdsson EM, Brown DR, Daniels M, et al. Immunization delays the onset of prion disease in mice. Am J Pathol 2002;161:13-17
   PubMed Web of Science ®Google Scholar
• Goni F, Sigurdsson EM. New directions towards safer and effective vaccines for Alzheimer's disease. Curr Opin Mol Ther 2005;7:17-23
   PubMed Web of Science ®Google Scholar
• Boche D, Nicoll JAR, Weller RO. Immunotherapy for Alzheimer's disease and other dementias. Curr Opin Neurol 2005;18:720-5
   PubMed Web of Science ®Google Scholar
• Magri G, Clerici M, Dall'Ara P, et al. Decrease in pathology and progression of scrapie after immunisation with synthetic prion protein peptides in hamsters. Vaccine 2005;23:2862-8
   PubMed Web of Science ®Google Scholar
• Miller TW, Shirley TL, Wolfgang WJ, et al. DNA vaccination against mutant huntingtin ameliorates the HDR6/2 diabetic phenotype. Mol Ther 2003;7:572-9
   PubMed Web of Science ®Google Scholar
• Schenk D. Amyloid-beta immunotherapy for Alzheimer's disease: the end of the beginning. Nat Rev Neurosci 2002;3:824-8
   PubMed Web of Science ®Google Scholar
• Solomon B. Immunological approaches as therapy for Alzheimer's disease. Expert Opin Biol Ther 2002;2:907-17
   PubMed Web of Science ®Google Scholar
• Sigurdsson EM, Wisniewski T, Frangione B. A safer vaccine for Alzheimer's disease? Neurobiol Aging 2002;23:1001-8
   PubMed Web of Science ®Google Scholar
• Sigurdsson EM. Immunotherapy for conformational diseases. Curr Pharm Des 2006;12:2569-85
   PubMed Web of Science ®Google Scholar
• Solomon B. Anti-aggregating antibodies, a new approach towards treatment of conformational diseases. Curr Med Chem 2002;9:1737-49
   PubMed Web of Science ®Google Scholar
• White AR, Hawke SH. Immunotherapy as a therapeutic treatment for neurodegenerative disorders. J Neurochem 2003;87:801-8
   PubMed Web of Science ®Google Scholar
• Pepys MB, Herbert J, Hutchinson WL, et al. Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. Nature 2002;417:254-9
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Lemieux LJ, Fraser PE, et al. Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease. Nat Med 1995;1:143-8
   PubMed Web of Science ®Google Scholar
• Cherny RA, Atwood CS, Xilinas ME, et al. Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 2001;30:665-76
   PubMed Web of Science ®Google Scholar
• Lee JY, Friedman JE, Angel I, et al. The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human beta-amyloid precursor protein transgenic mice. Neurobiology Aging 2004;25:1315-21
   PubMed Web of Science ®Google Scholar
• Maynard CJ, Bush AI, Masters CL, et al. Metals and amyloid-beta in Alzheimer's disease. Int J Exp Pathol 2005;86:147-59
   PubMed Web of Science ®Google Scholar
• Bossy-Wetzel E, Schwarzenbacher R, Lipton SA. Molecular pathways to neurodegeneration. Nat Med 2004;10(Suppl):S2-S9
   PubMed Web of Science ®Google Scholar
• Mattson MP, Sherman M. Perturbed signal transduction in neurodegenerative disorders involving aberrant protein aggregation. Neuromolecular Med 2003;4:109-32
   PubMed Web of Science ®Google Scholar
• Mattson MP, Duan W, Chan SL, et al. Neuroprotective and neurorestorative signal transduction mechanisms in brain aging: modification by genes, diet and behavior. Neurobiol Aging 2002;23:695-705
   PubMed Web of Science ®Google Scholar
• Mattson MP. Excitotoxic and excitoprotective mechanisms: abundant targets for the prevention and treatment of neurodegenerative disorders. Neuromolecular Med 2003;3:65-94
   PubMed Web of Science ®Google Scholar
• Yuan J, Yankner BA. Apoptosis in the nervous system. Nature 2000;407:802-9
   PubMed Web of Science ®Google Scholar
• Estrada LD, Soto C. Inhibition of protein misfolding and aggregation by small rationally-designed peptides. Curr Pharm Des 2006;12:2557-67
   PubMed Web of Science ®Google Scholar
• De Lorenzi E, Giorgetti S, Grossi S, et al. Pharmaceutical strategies against amyloidosis: old and new drugs in targeting a “protein misfolding disease”. Curr Med Chem 2004;11:1065-84
   PubMed Web of Science ®Google Scholar
• Sterling J, Bojanic D, Eglen RM, et al. Current trends in high-throughput screening. Assay Drug Dev Technol 2008;6:491-504
   PubMed Web of Science ®Google Scholar
• LeVine H III, Scholten JD. Screening for pharmacologic inhibitors of amyloid fibril formation. Methods Enzymol 1999;309:467-76
   PubMed Web of Science ®Google Scholar
• Soto C. Plaque busters: strategies to inhibit amyloid formation in Alzheimer's disease. Mol Med Today 1999;5:343-50
   PubMedGoogle Scholar
• Estrada LD, Yowtak J, Soto C. Protein misfolding disorders and rational design of antimisfolding agents. Methods Mol Biol 2006;340:277-93
   PubMedGoogle Scholar
• LeVine H. The challenge of inhibiting Abeta polymerization. Curr Med Chem 2002;9:1121-33
   PubMed Web of Science ®Google Scholar
• Mason JM, Kokkoni N, Stott K, Doi AJ. Design strategies for anti-amyloid agents. Curr Opin Struct Biol 2003;13:526-32
   PubMed Web of Science ®Google Scholar
• Porat Y, Abramowitz A, Gazit E. Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism. Chem Biol Drug Des 2006;67:27-37
   PubMed Web of Science ®Google Scholar
• Golabek A, Marques MA, Lalowski M, Wisniewski T. Amyloid beta binding proteins in vitro and in normal human cerebrospinal fluid. Neurosci Lett 1995;191:79-82
   PubMed Web of Science ®Google Scholar
• Soto C, Ghiso J, Frangione B. Alzheimer's amyloid-β aggregation is modulated by the interaction of multiple factors. Alzheimer's Res 1997;3:215-22
   Google Scholar
• Evans KC, Berger EP, Cho CG, et al. Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer disease. Proc Natl Acad Sci USA 1995;92:763-7
   PubMed Web of Science ®Google Scholar
• Matsubara E, Soto C, Governale S, et al. Apolipoprotein J and Alzheimer's amyloid beta solubility. Biochem J 1996;316:671-9
   PubMed Web of Science ®Google Scholar
• Schwarzman AL, Gregori L, Vitek MP, et al. Transthyretin sequesters amyloid beta protein and prevents amyloid formation. Proc Natl Acad Sci USA 1994;91:8368-72
   PubMed Web of Science ®Google Scholar
• Janciauskiene S, Garcia DF, Carlemalm E, et al. Inhibition of Alzheimer beta-peptide fibril formation by serum amyloid P component. J Biol Chem 1995;270:26041-4
   PubMed Web of Science ®Google Scholar
• Janciauskiene S, Rubin H, Lukacs CM, Wright HT. Alzheimer's peptide Abeta1-42 binds to two beta-sheets of alpha1-antichymotrypsin and transforms it from inhibitor to substrate. J Biol Chem 1998;273:28360-4
   PubMed Web of Science ®Google Scholar
• Castillo GM, Lukito W, Peskind E, et al. Laminin inhibition of beta-amyloid protein (Abeta) fibrillogenesis and identification of an Abeta binding site localized to the globular domain repeats on the laminin a chain. J Neurosci Res 2000;62:451-62
   PubMed Web of Science ®Google Scholar
• Bronfman FC, Garrido J, Alvarez A, et al. Laminin inhibits amyloid-beta-peptide fibrillation. Neurosci Lett 1996;218:201-3
   PubMed Web of Science ®Google Scholar
• Castano EM, Prelli F, Wisniewski T, et al. Fibrillogenesis in Alzheimer's disease of amyloid beta peptides and apolipoprotein E. Biochem J 1995;306:599-604
   PubMed Web of Science ®Google Scholar
• Ma J, Yee A, Brewer HB Jr, et al. Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments. Nature 1994;372:92-4
   PubMed Web of Science ®Google Scholar
• Hamazaki H. Amyloid P component promotes aggregation of Alzheimer's beta-amyloid peptide. Biochem Biophys Res Commun 1995;211:349-53
   PubMed Web of Science ®Google Scholar
• Geerts H. NC-531 (Neurochem). Curr Opin Investig Drugs 2004;5:95-100
   PubMedGoogle Scholar
• Aisen PS, Gauthier S, Vellas B, et al. Alzhemed: a potential treatment for Alzheimer's disease. Curr Alzheimer Res 2007;4:473-8
   PubMed Web of Science ®Google Scholar
• Bush AI. Copper, zinc, and the metallobiology of Alzheimer disease. Alzheimer Dis Assoc Disord 2003;17:147-50
   PubMed Web of Science ®Google Scholar
• Bush AI. Metals and neuroscience. Curr Opin Chem Biol 2000;4:184-91
   PubMed Web of Science ®Google Scholar
• Bush AI. Metal complexing agents as therapies for Alzheimer's disease. Neurobiol Aging 2002;23:1031-8
   PubMed Web of Science ®Google Scholar
• Barral JM, Broadley SA, Schaffar G, Hartl FU. Roles of molecular chaperones in protein misfolding diseases. Semin Cell Dev Biol 2004;15:17-29
   PubMed Web of Science ®Google Scholar
• Muchowski PJ. Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones? Neuron 2002;35:9-12
   PubMed Web of Science ®Google Scholar
• Morimoto RI. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev 2008;22:1427-38
   PubMed Web of Science ®Google Scholar
• Balch WE, Morimoto RI, Dillin A, Kelly JW. Adapting proteostasis for disease intervention. Science 2008;319:916-9
   PubMed Web of Science ®Google Scholar
• Hetz CA, Soto C. Stressing Out the ER: a role of the unfolded protein response in prion-related disorders. Curr Mol Med 2006;6:37-43
   PubMed Web of Science ®Google Scholar
• Chaudhuri TK, Paul S. Protein-misfolding diseases and chaperone-based therapeutic approaches. FEBS J 2006;273:1331-49
   PubMed Web of Science ®Google Scholar
• Findeis MA. Peptide inhibitors of beta amyloid aggregation. Curr Top Med Chem 2002;2:417-23
   PubMedGoogle Scholar
• Esteras-Chopo A, Pastor MT, Serrano L, Lopez de la PM. New strategy for the generation of specific D-peptide amyloid inhibitors. J Mol Biol 2008;377:1372-81
   PubMed Web of Science ®Google Scholar
• Gilead S, Gazit E. Inhibition of amyloid fibril formation by peptide analogues modified with alpha-aminoisobutyric acid. Angew Chem Int Ed Engl 2004;43:4041-4
   PubMed Web of Science ®Google Scholar
• Findeis MA, Musso GM, Arico-Muendel CC, et al. Modified-peptide inhibitors of amyloid beta-peptide polymerization. Biochemistry 1999;38:6791-800
   PubMed Web of Science ®Google Scholar
• Gordon DJ, Sciarretta KL, Meredith SC. Inhibition of beta-amyloid40; fibrillogenesis and disassembly of beta-amyloid40; fibrils by short beta-amyloid congeners containing N-methyl amino acids at alternate residues. Biochemistry 2001;40:8237-45
   PubMed Web of Science ®Google Scholar
• Hughes E, Burke RM, Doig AJ. Inhibition of toxicity in the beta-amyloid peptide fragment beta-(25-35) using N-methylated derivatives: a general strategy to prevent amyloid formation. J Biol Chem 2000;275:25109-15
   PubMed Web of Science ®Google Scholar
• Kapurniotu A, Schmauder A, Tenidis K. Structure-based design and study of non-amyloidogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicity. J Mol Biol 2002;315:339-50
   PubMed Web of Science ®Google Scholar
• Soto C, Sigurdsson EM, Morelli L, et al. Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nat Med 1998;4:822-6
   PubMed Web of Science ®Google Scholar
• Soto C, Kindy MS, Baumann M, Frangione B. Inhibition of Alzheimer's amyloidosis by peptides that prevent beta-sheet conformation. Biochem Biophys Res Commun 1996;226:672-80
   PubMed Web of Science ®Google Scholar
• Ghanta J, Shen CL, Kiessling LL, Murphy RM. A strategy for designing inhibitors of beta-amyloid toxicity. J Biol Chem 1996;271:29525-8
   PubMed Web of Science ®Google Scholar
• Tjernberg LO, Naslund J, Lindqvist F, et al. Arrest of beta-amyloid fibril formation by a pentapeptide ligand. J Biol Chem 1996;271:8545-8
   PubMed Web of Science ®Google Scholar
• Pallitto MM, Ghanta J, Heinzelman P, et al. Recognition sequence design for peptidyl modulators of beta-amyloid aggregation and toxicity. Biochemistry 1999;38:3570-8
   PubMed Web of Science ®Google Scholar
• Findeis MA, Lee JJ, Kelley M, et al. Characterization of cholyl-leu-val-phe-phe-ala-OH as an inhibitor of amyloid beta-peptide polymerization. Amyloid 2001;8:231-41
   PubMed Web of Science ®Google Scholar
• Wood SJ, Wetzel R, Martin JD, Hurle MR. Prolines and amyloidogenicity in fragments of the Alzheimer's peptide beta/A4. Biochemistry 1995;34:724-30
   PubMed Web of Science ®Google Scholar
• Sigurdsson EM, Permanne B, Soto C, et al. In vivo reversal of amyloid-beta lesions in rat brain. J Neuropathol Exp Neurol 2000;59:11-17
   PubMed Web of Science ®Google Scholar
• Permanne B, Adessi C, Fraga S, et al. Are beta-sheet breaker peptides dissolving the therapeutic problem of Alzheimer's disease? J Neural Transm Suppl 2002;293-301
   PubMed Web of Science ®Google Scholar
• Chacon MA, Barria MI, Soto C, Inestrosa NC. b-sheet breaker peptide prevents Abeta-induced spatial memory impairments with partial reduction of amyloid deposits. Mol Psychiatry 2004;9:953-61
   PubMed Web of Science ®Google Scholar
• Adessi C, Soto C. Converting a peptide into a drug: strategies to improve stability and bioavailability. Curr Med Chem 2002;9:963-78
   PubMed Web of Science ®Google Scholar