The role of β-amyloid peptide in neurodegenerative diseases

Ageing Research Reviews

Volumn 10, Issue 4, 2011, Pages 440-452

  Maltsev, A V ^a,b   Bystryak, S ^c   Galzitskaya, O V ^d  

^a N N BLOKHIN NATIONAL MEDICAL RESEARCH CENTER OF ONCOLOGY   (Russian Federation)

^b INSTITUTE OF THEORETICAL AND EXPERIMENTAL BIOPHYSICS   (Russian Federation)

^c Allied Innovative Systems   (United States)

^d INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

Author keywords

Amyloid peptide; Alzheimer's disease; Amyloid fibril; Neuron loss; Prediction of amyloidogenic regions; Structure

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; TAU PROTEIN;

ALZHEIMER DISEASE; AMYLOIDOSIS; CELL LOSS; CELL MEMBRANE; CELL METABOLISM; DEGENERATIVE DISEASE; DRUG TARGETING; HUMAN; NERVE CELL; OXIDATIVE STRESS; PATHOGENESIS; PLAQUE FORMING CELL; PROTEIN FUNCTION; PROTEIN METABOLISM; REVIEW;

AMYLOID BETA-PEPTIDES; AMYLOIDOSIS; ANIMALS; HUMANS; NEURODEGENERATIVE DISEASES; PEPTIDE FRAGMENTS; PLAQUE, AMYLOID;

EID: 80052315458     PISSN: 15681637     EISSN: 18729649     Source Type: Journal    
DOI: 10.1016/j.arr.2011.03.002     Document Type: Review

References (149)

1. Alzheimer's Association, 2007, http://www.alz.org/national/documents/Report_2007FactsAndFigures.pdf.
2. Arai H., Lee V.M., Messinger M.L., Greenberg B.D., Lowery D.E., Trijanowski J.Q. Expression patterns of beta-amyloid precursor protein (beta-APP) in neural and nonneural human tissues from Alzheimer's disease and control subjects. Ann. Neurol. 1991, 30:686-693.
3. Balbach J.J., Ishii Y., Antzutkin O.N., Leapman R.D., Rizzo N.W., Dyda F., Reed J., Tycko R. Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR. Biochemistry 2000, 39:13748-13759.
4. Balbach J.J., Petkova A.T., Oyler N.A., Antzutkin O.N., Gordon D.J., Meredith S.C., Tycko R. Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance. Biophys. J. 2002, 83:1205-1216.
5. Ban T., Goto Y. Direct observation of amyloid growth monitored by total internal reflection fluorescence microscopy. Methods Enzymol. 2006, 413:91-102.
6. Bayer T.A., Wirths O., Majtenyi K., Hartmann T., Multhaup G., Beyreuther K., Czech C. Key factors in Alzheimer's disease: beta-amyloid precursor protein processing, metabolism and intraneuronal transport. Brain Pathol. 2001, 11:1-11.
7. Bayramov V.M., Kaminsky Y.G., Fedyukin V.S., Brindar N.G., Maltsev A.V. The formation and role of beta-amyloid peptides in neurons upon amyloidosis. Bioorg. Chem. 2006, 32:243-248.
8. Benzinger T.L., Gregory D.M., Burkoth T.S., Miller-Auer H., Lynn D.G., Botto R.E., Meredith S.C. Two-dimensional structure of beta-amyloid(10-35) fibrils. Biochemistry 2000, 39:3491-3499.
9. Bird T.D. Genetic factors in Alzheimer's disease. N. Engl. J. Med. 2005, 352:884-894.
10. Borchelt D.R., Thinakaran G., Eckman C.B., Lee M.K., Davenport F., Ratovitsky T., Prada C.M., Kim G., Seekins S., Yager D., Slunt H.H., Wang R., Seeger M., Levey A.I., Gandy S.E., Copeland N.G., Jenkins N.A., Price D.L., Younkin S.G., Sisodia S.S. Familial Alzheimer's disease-linked presenilin 1 variants elevate Abeta1-42/1-40 ratio in vitro and in vivo. Neuron 1996, 17:1005-1013.
11. Brouwers N., Sleegers K., Van Broeckhoven C. Molecular genetics of Alzheimer's disease: an update. Ann. Med. 2008, 40:562-583.
12. Brown M.S., Ye J., Rawson R.B., Goldstein J.L. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 2000, 100:391-398.
13. Bucciantini M., Calloni G., Chiti F., Formigli L., Nosi D., Dobson C.M., Stefani M. Prefibrillar amyloid protein aggregates share common features of cytotoxicity. J. Biol. Chem. 2004, 279:31374-31382.
14. Buchete N.V., Tycko R., Hummer G. Molecular dynamics simulations of Alzheimer's beta-amyloid protofilaments. J. Mol. Biol. 2005, 353:804-821.
15. Carson J.A., Turner A.J. Beta-amyloid catabolism: roles for neprilysin (NEP) and other metallopeptidases?. J. Neurochem. 2002, 81:1-8.
16. Caspersen C., Wang N., Yao J., Sosunov A., Chen X., Lustbader J.W., Xu H.W., Stern D., McKhann G., Yan S.D. Mitochondrial Abeta: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease. FASEB J. 2005, 19:2040-2041.
17. Castelletto V., Hamley I.W., Hule R.A., Pochan D. Helical-ribbon formation by a beta-amino acid modified amyloid beta-peptide fragment. Angew. Chem. Int. Ed. Engl. 2009, 48:2317-2320.
18. Chamberlain A.K., MacPhee C.E., Zurdo J., Morozova-Roche L.A., Hill H.A., Dobson C.M., Davis J.J. Ultrastructural organization of amyloid fibrils by atomic force microscopy. Biophys. J. 2000, 79:3282-3293.
19. Chen Y.R., Huang H.B., Chyan C.L., Shiao M.S., Lin T.H., Chen Y.C. The effect of Abeta conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy. J. Biochem. 2006, 139:733-740.
20. Chiti F., Stefani M., Taddei N., Ramponi G., Dobson C.M. Rationalization of the effects of mutations on tide and protein aggregation rates. Nature 2003, 424:805-808.
21. Chiti F., Taddei N., Baroni F., Capanni C., Stefani M., Ramponi G., Dobson C.M. Kinetic partitioning of protein folding and aggregation. Nature Struct. Biol. 2002, 9:137-143.
22. Chiti F., Taddei N., Bucciantini M., White P., Ramponi G., Dobson C.M. Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 2000, 19:1441-1449.
23. Chiti F., Webster P., Taddei N., Clark A., Stefani M., Ramponi G., Dobson C.M. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:3590-3594.
24. Christopeit T., Hortschansky P., Schroeckh V., Gührs K., Zandomeneghi G., Fändrich M. Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's beta-amyloid peptide. Protein Sci. 2005, 14:2125-2131.
25. Chun W., Johnson G.V. The role of tau phosphorylation and cleavage in neuronal cell death. Front. Biosci. 2007, 12:733-756.
26. Collins S., Boyd A., Lee J.S., Lewis V., Fletcher A., McLean C.A., Law M., Kaldor J., Smith M.J., Masters C.L. Neurology 2002, 59:1365-1371.
27. Cribbs D.H., Pike C.I., Weinstein S.L., Velazquez P., Cotman C.W. All-d-enantiomers of beta-amyloid exhibit similar biological properties to all-l-beta-amyloids. J. Biol. Chem. 1997, 272:7431-7436.
28. Cummings J.L., Kaufer D. Neuropsychiatric aspects of Alzheimer's disease: the cholinergic hypothesis revisited. Neurology 1996, 47:876-883.
29. De Strooper B., Annaert W. Proteolytic processing and cell biological functions of the amyloid precursor protein. J. Cell Sci. 2002, 113:1857-1870.
30. Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 1999, 24:329-332.
31. Dobson C.M. International Bunsen Discussion Meeting on Structure of Amyloid Fibrils and Mechanism of Amyloid Formation 2009, 12.
32. Dobson C.M., Karplus M. The fundamentals of protein folding: bringing together theory and experiment. Curr. Opin. Struct. Biol. 1999, 9:92-101.
33. Esteras-Chopo A., Serrano L., Lopez de la Paz M. The amyloid stretch hypothesis: recruiting proteins toward the dark side. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:16672-16677.
34. Falkevall A., Alikhani N., Bhushan S., Pavlov P.F., Busch K., Johnson K.A., Eneqvist T., Tjernberg L., Ankarcrona M., Glaser E. Degradation of the amyloid beta-protein by the novel mitochondrial peptidasome, PreP. J. Biol. Chem. 2006, 281:29096-29104.
35. Fändrich M., Fletcher M.A., Dobson C.M. Amyloid fibrils from muscle myoglobin. Nature 2001, 410:165-166.
36. Fändrich M., Forge V., Buder K., Kittler M., Dobson C.M., Diekmann S. Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:15463-15468.
37. Fardilha M., Vieira S.I., Barros A., Sousa M., Da Cruz e Silva O.A., Da Cruz e Silva E.F. Differential distribution of Alzheimer's amyloid precursor protein family variants in human sperm. Ann. N. Y. Acad. Sci. 2007, 1096:196-206.
38. Fernandez-Escamilla A.M., Rousseau F., Schymkowitz J., Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 2004, 22:1302-1306.
39. Ferri C.P., Prince M., Brayne C., Brodaty H., Fratiglioni L., Ganguli M., Hall K., Hasegawa K., Hendrie H., Huang Y., Jorm A., Mathers C., Menezes P.R., Rimmer E., Scazufca M. Alzheimer's disease international global prevalence of dementia: a Delphi consensus study. Lancet 2005, 366:2112-2117.
40. Fodero L.R., Mok S.S., Losic D., Martin L.L., Aguilar M.I., Barrow C.J., Livett B.G., Small D.H. Alpha7-nicotinic acetylcholine receptors mediate an Abeta(1-42)-induced increase in the level of acetylcholinesterase in primary cortical neurones. J. Neurochem. 2004, 88:1186-1193.
41. Frare E., Mossuto M.F., Polverino de Laureto P., Dumoulin M., Dobson C.M., Fontana A. Identification of the core structure of lysozyme amyloid fibrils by proteolysis. J. Mol. Biol. 2006, 361:551-561.
42. Galzitskaya O.V. Search for folding initiation sites from amino acid sequence. J. Bioinform. Comput. Biol. 2008, 6:681-691.
43. Galzitskaya O.V., Garbuzynskiy S.O., Lobanov M.Yu A search of amyloidogenic regions in protein chain. Mol. Biol. (Russia) 2006, 40:910-918.
44. Galzitskaya O.V., Garbuzynskiy S.O., Lobanov M.Yu Is it possible to predict amyloidogenic regions from sequence alone?. J. Bioinform. Comput. Biol. 2006, 4:373-388.
45. Galzitskaya O.V., Garbuzynskiy S.O., Lobanov M.Yu Prediction of amyloidogenic and disordered regions in protein chain. PLoS Comput. Biol. 2006, 2:e177.
46. Galzitskaya O.V., Surin A.K., Nakamura H. Optimal region of average side-chain entropy for fast protein folding. Protein Sci. 2000, 9:580-586.
47. Garbuzynskiy S.O., Lobanov M.Yu., Galzitskaya O.V. FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence. Bioinformatics 2010, 26:326-332.
48. Gelfanova V., Higgs R.E., Dean R.A., Holtzman D.M., Farlow M.R., Siemers E.R., Boodhoo A., Qian Y.W., He X., Jin Z., Fisher D.L., Cox K.L., Hale J.E. Quantitative analysis of amyloid-beta peptides in cerebrospinal fluid using immunoprecipitation and MALDI-Tof mass spectrometry. Breef. Funct. Genom. Proteom. 2007, 6:149-158.
49. Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerhove J. Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat. Biotechnol. 2003, 21:566-569.
50. Ghiso J., Shayo M., Calero M., Ng D., Tomidokoro Y., Gandy S., Rostagno A., Frangione B. Systemic catabolism of Alzheimer's Abeta40 and Abeta42. J. Biol. Chem. 2004, 279:45897-45908.
51. Goedert M., Spillantini M.G., Crowther R.A. Tau proteins and neurofibrillary degeneration. Brain Pathol. 1991, 1:279-286.
52. Gulyaeva, N.V., 2005. Thesis of scientific conference. Neurochemistry: fundamental and applied aspects. RAS, Moscow, p. 163.
53. Hamodrakas S.J., Liappa Ch., Iconomidou V.A. Consensus prediction of amyloidogenic determinants in amyloid fibril-forming proteins. Int. J. Biol. Macromol. 2007, 41:295-300.
54. Hardy J., Allsop D. Amyloid deposition as the central event in the etiology of Alzheimer's disease. Trends Pharmacol. Sci. 1991, 12:383-388.
55. Haspel N., Zanuy D., Ma B., Wolfson H., Nussinov R. A comparative study of amyloid fibril formation by residues 15-19 of the human calcitonin hormone: a single beta-sheet model with a small hydrophobic core. J. Mol. Biol. 2005, 345:1213-1227.
56. Holmes C., Boche D., Wilkinson D., Yadegarfar G., Hopkins V., Bayer A., Jones R.W., Bullock R., Love S., Neal J.W., Zotova E., Nicoll J.A. Long-term effects of Abeta42 immunizations in Alzheimer's disease: follow-up of a randomized, placebo-controlled phase I trial. Lancet 2008, 372:216-223.
57. Hoyer S. Brain glucose and energy metabolism abnormalities in sporadic Alzheimer disease Causes and consequences: an update. Exp. Gerontol. 2000, 35:1363-1372.
58. Iqbal K., Alonso, Adel C., Chen S., Chohan M.O., El-Akkad E., Gong C.X., Khatoon S., Li B., Liu F., Rahman A., Tanimukai H., Grundke-Iqbal I. Tau pathology in Alzheimer disease and other tauopathies. Biochem. Biophys. Acta 2005, 1739(2-3):198-210.
59. Ivanova M.I., Sawaya M.R., Gingery M., Attinger A., Eisenberg D. An amyloid-forming segment of beta2-microglobulin suggests a molecular model for the fibril. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:10584-10589.
60. Jaroniec C.P., MacPhee C.E., Astrof N.S., Dobson C.M., Griffin R.G. Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:16748-16753.
61. Jones S., Manning J., Kad N.M., Radford S.E. Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro. J. Mol. Biol. 2003, 325:249-257.
62. Kajava A.V., Baxa U., Wickner R.B., Steven A.C. A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structure. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:7885-7890.
63. Kaneko I., Yamada N., Sakuraba Y., Kamenosono M., Tutumi S. Suppression of mitochondrial succinate dehydrogenase, a primary target of beta-amyloid, and its derivative racemized at Ser residue. J. Neurochem. 1995, 65:2585-2593.
64. Kang J., Lemaire H.G., Unterbeck A., Salbaum J.M., Masters C.L., Grzeschik K.H., Multhaup G., Beyreuther K., Muller-Hill B. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 1987, 325:733-736.
65. Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., Glabe C.G. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003, 300:486-489.
66. Kern A., Roempp B., Prager K., Walter J., Behl C. Down-regulation of endogenous amyloid precursor protein processing due to cellular aging. J. Biol. Chem. 2006, 281:2405-2413.
67. Kheterpal I., Chen M., Cook K.D., Wetzel R. Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange-mass spectrometry with on-line proteolytic fragmentation. J. Mol. Biol. 2006, 361:785-795.
68. Kirschner D.A., Inouye H., Duffy L.K., Sinclair A., Lind M., Selkoe D.J. Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro. Proc. Natl. Acad. Sci. U. S. A. 1987, 84:6953-6957.
69. Konig G., Monning U., Czech C., Prior R., Banati R., Schreiter-Gasser U., Bauer J., Masters C.L., Beyreuther K. Identification and differential expression of a novel alternative splice isoform of the beta A4 amyloid precursor protein (APP) mRNA in leukocytes and brain microglial cells. J. Biol. Chem. 1992, 267:10804-10809.
70. Koo E.H., Kopan R. Potential role of presenilin-regulated signaling pathways in sporadic neurodegeneration. Nat. Med. 2004, 10:S26-S33.
71. Koudinov A.R., Berezov T.T. Alzheimer's amyloid-beta (A beta) is an essential synaptic protein, not neurotoxic junk. Acta Neurobiol. Exp. (Wars) 2004, 64:71-79.
72. Kozhukh G.V., Hagihara Y., Kawakami T., Hasegawa K., Naiki H., Goto Y. Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I. J. Biol. Chem. 2002, 277:1310-1315.
73. Kubo T., Kumagae Y., Miller C.A., Kaneko I. Beta-amyloid racemized at the Ser26 residue in the brains of patients with Alzheimer disease: implications in the pathogenesis of Alzheimer disease. J. Neuropatol. Exp. Neurol. Res. 2003, 62:248-259.
74. Kubo T., Nishimura S., Kumagae Y., Kaneko I. In vivo conversion of racemized beta-amyloid ([d-Ser 26]A beta 1-40) to truncated and toxic fragments ([d-Ser 26]A beta 25-35/40) and fragment presence in the brains of Alzheimer's patients. J. Neurosci. Res. 2002, 70:474-483.
75. Lanz T.A., Karmilowicz M.J., Wood K.M., Pozdnyakow N., Du P., Piotrowski M.A., Brown T.M., Nolan C.E., Richter K.E., Finley J.E., Fei Q., Ebbinghaus C.F., Chen Y.L., Spraclin D.K., Tate B., Geoghegan K.F., Lau L.F., Auperin D.D., Schachter J.B. Concentration-dependent modulation of amyloid-beta in vivo and in vitro using the gamma-secretase inhibitor, LY-450139. J. Pharmacol. Exp. Ther. 2006, 319:924-933.
76. Ledford H. Key Alzheimer's finding questioned. Nature 2010, 466:1031.
77. Ling G.N. Life at the Cell and Below Cell Level. The Hidden History of a Fundamental Revolution in Biology 2001, Pacific Press, New York.
78. Liu T., Qian W.J., Gritsenko M.A., Camp D.G., Monroe M.E., Move R.J., Smith R.D. Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J. Proteome Res. 2005, 4:2070-2080.
79. Lott I.T., Head E. Alzheimer's disease and Down syndrome: factors in pathogenesis. Neurobiol. Aging 2005, 26:383-389.
80. Louw C., Godon A., Johnston N., Mollatt C., Bradley G., Whiteley C.G. Arginine deiminases: therapeutic tools in the etiology and pathogenesis of Alzheimer's disease. J. Enzyme Inhib. Med. Chem. 2007, 22:121-126.
81. Low L.F., Anstey K.J. Dementia literacy: recognition and beliefs on dementia of the Australian public. J. Alzheimer's Dement. 2009, 5:43-49.
82. Lu X., Wintrode P.L., Surewicz W.K. Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:1510-1515.
83. Lührs T., Ritter C., Adrian M., Riek-Loher D., Bohrmann B., Döbeli H., Schubert D., Riek R. 3D structure of Alzheimer's amyloid-beta(1-42) fibrils. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:17342-17347.
84. Luo Y., Bolon B., Kahn S., Bennett B.D., Babu-Khan S., Denis P., Fan W., Kha H., Zhang J., Gong Y., Martin L., Louis J.C., Yan Q., Richards W.G., Citron M., Vassar R. Mice deficient in BACE1, the Alzheimer's beta-secretase, have normal phenotype and abolished beta-amyloid generation. Nat. Neurosci. 2001, 4:231-232.
85. Ma Q.F., Hu J., Wu W.H., Liu H.D., Du J.T., Fu Y., Wu Y.W., Lei P., Zhao Y.F., Li Y.M. Characterization of copper binding to the peptide amyloid-beta(1-16) associated with Alzheimer's disease. Biopolymers 2006, 83:20-31.
86. Maddalena A.S., Papassotiropoulos A., Gonzalez-Agosti C., Signorell A., Hegi T., Pasch T., Nitsch R.M., Hohk C. Cerebrospinal fluid profile of amyloid beta peptides in patients with Alzheimer's disease determined by protein biochip technology. Neurodegener. Dis. 2004, 1:231-235.
87. Maltsev A.V., Kaminsky Y.G., Ilyasov F.E., Rozanova N.A., Fedyukin V.S., Bayramov V.M. Conformational and intermolecular interactions of proteins in amyloidosis. Biofisika 2005, 50:470-474.
88. Maltsev A.V., Kaminsky Y.G., Rozanova N.A., Bayramov V.M. Neurochimiya 2005, 22:97-101.
89. Maltsev A{cyrillic}.V. International Symposium: Biological Mechanism of Ageing 2008, 68-69.
90. Maltsev A{cyrillic}.V., K{cyrillic}a{cyrillic}minsky Y.G., Bobkova N.V., Budantsev A{cyrillic}.Y., Gavrilova S.I. Anthol. Gerontol. Geriatr. 2004, 3:96-101.
91. Maltsev A{cyrillic}.V., K{cyrillic}a{cyrillic}minsky Y.G., Rozanova N.A., Bayramov V.M., Korneeva O{cyrillic}.S., Pasjkova S.V., Gavrilova S.I. Anthol. Gerontol. Geriatr. 2004, 4:84-88.
92. Maltsev, A.V., Mironova, G.D., Bayramov,V.M., 2008. Official bulletin of federal office of intelligent property on patents and trade marks "Inventions, useful models", No. 16. Ru.2006141527.A{cyrillic}.
93. Martin B., Lopez de Maturana R., Brenneman R., Walent T., Mattson M.P., Maudsley S. Class II G protein-coupled receptors and their ligands in neuronal function and protection. Neuromol. Med. 2005, 7:3-36.
94. Maslow K. How many people with dementia are hospitalized. Improving Hospital Care for Persons with Dementia 2006, 3-21. Springer, New York. N.M. Silvesrtein, K. Maslow (Eds.).
95. Massi F., Straub J.E. Energy landscape theory for Alzheimer's amyloid β-peptide fibril elongation. Proteins 2001, 42:217-229.
96. Mattson M.P. Pathways towards and away from Alzheimer's disease. Nature 2004, 430:631-639.
97. Massi F., Straub J.E. Probing the origins of increased activity of the E22Q "Dutch" mutant Alzheimer's beta-amyloid peptide. Biophys. J. 2001, 81:697-709.
98. Minicozzi V., Stellato F., Comai M., Serra M.D., Potrich C., Meyer-Klaucke W., Morante S. Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides. J. Biol. Chem. 2008, 283:10784-10792.
99. Mita S., Sadlock J., Schon E.A. A cDNA specifying the human amyloid beta precursor protein (ABPP) encodes a 95-kDa polypeptide. Nucl. Acids Res. 1988, 16:9351.
100. Moreno M.J., Romero J. Sporadic Creutzfeldt-Jakob disease: phenotypic variability. Neurologia 2002, 17:366-377.
101. Mudher A., Lovestone S. Alzheimer's disease-do tauists and Baptists finally shake hands?. Trends Neurosci. 2002, 25:22-26.
102. Munoz V., Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. Nat. Struct. Biol. 1994, 1:399-409.
103. Myers A.J., Goate A.M. The genetics of late-onset Alzheimer's disease. Curr. Opin. Neurol. 2001, 14:433-440.
104. Nalivaeva N.N., Fisk L.R., Belyaev N.D., Turner A.J. Amyloid-degrading enzymes as therapeutic targets in Alzheimer's disease. Curr. Alzheimer Res. 2008, 5:212-224.
105. Nguyen P.H., Li M.S., Stock G., Straub J.E., Thirumalai D. Monomer adds to preformed structured oligomers of Abeta-peptides by a two-stage dock-lock mechanism. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:111-116.
106. Ovchinnikova O.Yu., Finder V.H., Vodopivec I., Nitsch R.M., Glockshuber R. International Bunsen Discussion Meeting on Structure of Amyloid Fibrils and Mechanism of Amyloid Formation 2009, 128.
107. Pawar A.P., Dubay K.F., Zurdo J., Chiti F., Vendruscolo M., Dobson C.M. Prediction of "aggregation-pr and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 2005, 350:379-392.
108. Pearson H.A., Peers C. Physiological roles for amyloid beta peptides. J. Physiol. 2006, 575:5-10.
109. Petkova A.T., Buntkowsky G., Dyda F., Leapman R.D., Yau W.M., Tycko R. Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide. J. Mol. Biol. 2004, 335:247-260.
110. Petkova A.T., Yau W.M., Tycko R. Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. Biochemistry 2006, 45:498-512.
111. Picotti P., de Franceschi G., Frare E., Spolaore B., Zambonin M., Chiti F., de Laureto P.P., Fontana A. Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesis. J. Mol. Biol. 2007, 367:1237-1245.
112. Polvikoski T., Sulkava R., Haltia M., Kainulainen K., Vuorio A., Verkkoniemi A., Niinistö L., Halonen P., Kontula K. Apolipoprotein E, dementia, and cortical deposition of beta-amyloid protein. N. Engl. J. Med. 1995, 333:1242-1247.
113. Poulsen S.A., Watson A.A., Fairlie D.P., Craik D.J. Solution structures in aqueous SDS micelles of two amyloid beta peptides of A beta(1-28) mutated at the alpha-secretase cleavage site (K16E, K16F). J. Struct. Biol. 2000, 130:142-152.
114. Prusiner S.B. Molecular biology of prion causing infectious and genetic encephalopathies of humans as well as scrapie of sheep and BSE of cattle. Dev. Biol. Stand. 1991, 75:55-74.
115. Prusiner S.B. Molecular biology and genetics of prion diseases. Trans. R. Soc. Lond. B: Biol. Sci. 1994, 343:447-463.
116. Prusiner S.B. Prion diseases and the BSE crisis. Science 1997, 278:245-251.
117. Robakis, N.K. Mechanisms of AD neurodegeneration may be independent of Abeta and its derivatives. Neurobiol. Aging, 2010, PMID: 20594619 [Epub ahead of print].
118. Rochet J.C., Lansbury P.T. Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct. Biol. 2000, 10:60-68.
119. Roher A.E., Lowenson J.D., Clarke S., Woods A.S., Cotter R.J., Gowing E., Ball M.J. beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. Proc. Natl. Acad. Sci. U. S. A. 1993, 90:10836-10840.
120. Schmitz C., Rutten B.P., Pielen A., Schäfer S., Wirths O., Tremp G., Czech C., Blanchard V., Multhaup G., Rezaie P., Korr H., Steinbusch H.W., Pradier L., Bayer T.A. Hippocampal neuron loss exceeds amyloid plaque load in a transgenic mouse model of Alzheimer's disease. Am. J. Pathol. 2004, 164:1495-1502.
121. Selkoe D.J. Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 1999, 399(Suppl. 6738):A23-A31.
122. Selkoe D.J., Schenk D. Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics. Annu. Rev. Pharmacol. Toxicol. 2003, 43:545-584.
123. Selkoe D.J. Biochemistry and molecular biology of amyloid beta-protein and the mechanism of Alzheimer's disease. Handb. Clin. Neurol. 2008, 89:245-260.
124. Shapira R., Austin G.E., Mirra S.S. Neuritic plaque amyloid in Alzheimer's disease is highly racemized. J. Neurochem. 1988, 50:69-74.
125. Shen Z.X. Brain cholinesterases: II. The molecular and cellular basis of Alzheimer's disease. Med. Hypotheses 2004, 63:308-321.
126. Shioi J., Georgakopoulos A., Mehta P., Kouchi Z., Litterst C.M., Baki L., Robakis N.K. FAD mutants unable to increase neurotoxic Abeta 42 suggest that mutation effects on neurodegeneration may be independent of effects on Abeta. J. Neurochem. 2007, 101:674-681.
127. Singh N., Talalayeva Y., Tsiper M., Romanov V., Dranovsky A., Colflesh D., Rudamen G., Vitek M.P., Shen J., Yang X., Goldgaber D., Schwarzman A.L The role of Alzheimer's disease-related presenilin 1 in intercellular adhesion. Exp. Cell Res. 2001, 263:1-13.
128. Smith D.H., Chen X.H., Iwata A., Graham D.I. Amyloid beta accumulation in axons after traumatic brain injury in humans. J. Neurosurg. 2003, 98:1072-1077.
129. Solomon B. Intravenous immunoglobulin and Alzheimer's disease immunotherapy. Curr. Opin. Mol. Ther. 2007, 1:79-85.
130. Sprecher C.A., Grant F.J., Grimm G., O'Hara P.J., Norris R., Foster D.S. Molecular cloning of the cDNA for a human amyloid precursor protein homolog: evidence for a multigene family. Biochemistry 1993, 32:4481-4486.
131. Sticht H., Bayer P., Willbold D., Dames S., Hilbich C., Beyreuther K., Frank R.W., Rösch P. Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease. Eur. J. Biochem. 1995, 233:293-298.
132. St George-Hyslop P.H. Genetic factors in the genesis of Alzheimer's disease. Ann NY Acad. Sci. 2000, 924:1-7.
133. Suh Y.H., Checler F. Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer's disease. Pharmacol. Rev. 2002, 54:469-525.
134. Suzuki S., Galzitskaya O.V., Mitomo D., Higo J. General dynamic properties of Abeta12-36 amyloid peptide involved in Alzheimer's disease from unfolding simulation. J. Biochem. 2004, 136:583-594.
135. Talmard C., Leuma, Yona R., Faller P. Mechanism of zinc(II)-promoted amyloid formation: zinc(II) binding facilitates the transition from the partially alpha-helical conformer to aggregates of amyloid beta protein(1-28). J. Biol. Inorg. Chem. 2009, 14:449-455.
136. Tanaka C., McGeer P.L., Ihara Y. Neuroscientific Basis of Dementia 2001, Birkhäuser Verlag, Basel/Boston/Berlin, p. 250.
137. Tartaglia G.G., Pawar A.P., Campioni S., Dobson C.M., Chiti F., Vendruscolo M. Prediction of aggregation-prone regions in structured proteins. J. Mol. Biol. 2008, 380:425-436.
138. Tarus B., Straub J.E., Thirumalai D. Probing the initial stage of aggregation of the Abeta(10-35)-protein: assessing the propensity for peptide dimerization. J. Mol. Biol. 2005, 345:1141-1156.
139. Tenidis K., Waldner M., Bernhagen J., Fischle W., Bergmann M., Weber M., Merkle M.L., Voelter W., Brunner H., Kapurniotu A. Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties. J. Mol. Biol. 2000, 295:1055-1071.
140. Thirumalai D., Klimov D.K., Dima R.I. Emerging ideas on the molecular basis of protein and peptide aggregation. Curr. Opin. Struct. Biol. 2003, 13:146-159.
141. Uversky V.N., Gillespie J.R., Fink A.L. Why are "natively unfolded" proteins unstructured under physiologic conditions?. Proteins 2000, 41:415-427.
142. Van Nostrand W.E., Cunningham D.D. Purification of protease nexin II from human fibroblasts. J. Biol. Chem. 1987, 262:8508-8514.
143. Vassar R., Bennett B.D., Babu-Khan S., Kahn S., Mendiaz E.A., Denis P., Teplow D.B., Ross S., Amarante P., Loeloff R., Luo Y., Fisher S., Fuller J., Edenson S., Lile J., Jarosinski M.A., Biere A.L., Curran E., Burgess T., Louis J.C., Collins F., Treanor J., Rogers G., Citron M. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 1999, 286:735-741.
144. Vigo-Pelfrey C., Lee D., Keim P., Lieberburg I., Schenk D.B. Characterization of beta-amyloid peptide from human cerebrospinal fluid. J. Neurochem. 1993, 61:1965-1968.
145. Von Bergen M., Friedhoff P., Biernat J., Heberle J., Mandelkow E.M., Mandelkow E. Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:5129-5134.
146. Waring S.C., Rosenberg R.N. Genome-wide association studies in Alzheimer disease. Arch. Neurol. 2008, 65:329-334.
147. Wenk G.L. Neuropathologic changes in Alzheimer's disease. J. Clin. Psychiatry 2003, 64(Suppl. 9):7-10.
148. Wurth C., Guimard N.K., Hecht M.H. Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis. J. Mol. Biol. 2002, 319:1279-1290.
149. Zhang C., Wu B., Beglopoulos V., Wines-Samuelson M., Zhang D., Dragatsis I., Südhof T.C., Shen J. Presenilins are essential for regulating neurotransmitter release. Nature 2009, 460:632-636.