Biochemistry of Amyloid -Protein and Amyloid Deposits in Alzheimer Disease

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431

Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice

Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210

Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685

Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506

Neuropathological alterations in Alzheimer disease

Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345

Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein

Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516

Aβ Oligomers – a decade of discovery

Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938

Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91209-9 · Cited by 1,693

Natural Oligomers of the Alzheimer Amyloid-β Protein Induce Reversible Synapse Loss by Modulating an NMDA-Type Glutamate Receptor-Dependent Signaling Pathway

Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592

Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers

Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560

Synaptic Activity Regulates Interstitial Fluid Amyloid-β Levels In Vivo

Cirrito, J. R., Yamada, K. A., Finn, M. B., Sloviter, R. S., Bales, K. R., May, P. C., Schoepp, D. D., Paul, S. M., Mennerick, S., & Holtzman, D. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.10.028 · Cited by 1,265

Amyloid β-Protein Fibrillogenesis

Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., & Teplow, D. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22364 · Cited by 1,145

Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils

Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111

Trafficking and Proteolytic Processing of APP

Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075

Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease

Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053 · cited 1×

Neurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction

Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000

Rapid appearance and local toxicity of amyloid-β plaques in a mouse model of Alzheimer’s disease

Meyer-Luehmann, M., Spires-Jones, T. L., Prada, C., Garcia-Alloza, M., de Calignon, A., Rozkalne, A., Koenigsknecht-Talboo, J., Holtzman, D. M., Bacskai, B. J., & Hyman, B. T. (2008) · Nature · doi:10.1038/nature06616 · Cited by 987

Soluble Oligomers of Amyloid β Protein Facilitate Hippocampal Long-Term Depression by Disrupting Neuronal Glutamate Uptake

Li, S., Hong, S., Shepardson, N. E., Walsh, D. M., Shankar, G. M., & Selkoe, D. (2009) · Neuron · doi:10.1016/j.neuron.2009.05.012 · Cited by 972

Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease

Bernstein, S. L., Dupuis, N. F., Lazo, N. D., Wyttenbach, T., Condron, M. M., Bitan, G., Teplow, D. B., Shea, J.-E., Ruotolo, B. T., Robinson, C. V., et al. (2009) · Nature Chemistry · doi:10.1038/nchem.247 · Cited by 918

Immunochemical identification of the serine protease inhibitor α1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease

Abraham, C. R., Selkoe, D. J., & Potter, H. (1988) · Cell · doi:10.1016/0092-8674(88)90462-x · Cited by 900

Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration

Jin, M., Shepardson, N., Yang, T., Chen, G., Walsh, D., & Selkoe, D. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017033108 · Cited by 876

Brain Imaging in Alzheimer Disease

Johnson, K. A., Fox, N. C., Sperling, R. A., & Klunk, W. E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006213 · Cited by 875

Oligomeric amyloid β associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques

Koffie, R. M., Meyer-Luehmann, M., Hashimoto, T., Adams, K. W., Mielke, M. L., Garcia-Alloza, M., Micheva, K. D., Smith, S. J., Kim, M. L., Lee, V. M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811698106 · Cited by 850

Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration

Mandelkow, E.-M., & Mandelkow, E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006247 · Cited by 847

Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease.

Roher, A. E., Lowenson, J. D., Clarke, S., Wolkow, C., Wang, R., Cotter, R. J., Reardon, I. M., Zürcher-Neely, H. A., Heinrikson, R. L., & Ball, M. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53661-9 · Cited by 799

Apolipoprotein E and Apolipoprotein E Receptors: Normal Biology and Roles in Alzheimer Disease

Holtzman, D. M., Herz, J., & Bu, G. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006312 · Cited by 782

Structure–neurotoxicity relationships of amyloid β-protein oligomers

Ono, K., Condron, M. M., & Teplow, D. B. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905127106 · Cited by 770

Cell Biology of the Amyloid beta-Protein Precursor and the Mechanism of Alzheimer's Disease

Selkoe, D. J. (1994) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.10.110194.002105 · Cited by 747

Observation of metastable Aβ amyloid protofibrils by atomic force microscopy

Harper, J. D., Wong, S. S., Lieber, C. M., & Lansbury, P. T. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90255-6 · Cited by 697

Iron-Export Ferroxidase Activity of β-Amyloid Precursor Protein Is Inhibited by Zinc in Alzheimer's Disease

Duce, J. A., Tsatsanis, A., Cater, M. A., James, S. A., Robb, E., Wikhe, K., Leong, S. L., Perez, K., Johanssen, T., Greenough, M. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.014 · Cited by 676

Endocytosis Is Required for Synaptic Activity-Dependent Release of Amyloid-β In Vivo

Cirrito, J. R., Kang, J.-E., Lee, J., Stewart, F. R., Verges, D. K., Silverio, L. M., Bu, G., Mennerick, S., & Holtzman, D. M. (2008) · Neuron · doi:10.1016/j.neuron.2008.02.003 · Cited by 635

Amyloid oligomers: formation and toxicity of Aβ oligomers

Sakono, M., & Zako, T. (2010) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07568.x · Cited by 605

Dominant and differential deposition of distinct β-amyloid peptide species, AβN3(pE), in senile plaques

Saido, T. C., Iwatsubo, T., Mann, D. M. A., Shimada, H., Ihara, Y., & Kawashima, S. (1995) · Neuron · doi:10.1016/0896-6273(95)90301-1 · Cited by 587

Peripherally Applied Aβ-Containing Inoculates Induce Cerebral β-Amyloidosis

Eisele, Y. S., Obermüller, U., Heilbronner, G., Baumann, F., Kaeser, S. A., Wolburg, H., Walker, L. C., Staufenbiel, M., Heikenwalder, M., & Jucker, M. (2010) · Science · doi:10.1126/science.1194516 · Cited by 568

γ-Secretase: Successive Tripeptide and Tetrapeptide Release from the Transmembrane Domain of β-Carboxyl Terminal Fragment

Takami, M., Nagashima, Y., Sano, Y., Ishihara, S., Morishima-Kawashima, M., Funamoto, S., & Ihara, Y. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.2362-09.2009 · Cited by 498

Mass spectrometry of purified amyloid beta protein in Alzheimer's disease.

Mori, H., Takio, K., Ogawara, M., & Selkoe, D. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41896-0 · Cited by 483

Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro.

Kirschner, D. A., Inouye, H., Duffy, L. K., Sinclair, A., Lind, M., & Selkoe, D. J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.19.6953 · Cited by 482

Isolation of Low‐Molecular‐Weight Proteins from Amyloid Plaque Fibers in Alzheimer's Disease

Selkoe, D. J., Abraham, C. R., Podlisny, M. B., & Duffy, L. K. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb08501.x · Cited by 450

Animal Models of Alzheimer Disease

LaFerla, F. M., & Green, K. N. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006320 · Cited by 419

Amyloid beta peptides in human plasma and tissues and their significance for Alzheimer's disease

Roher, A. E., Esh, C. L., Kokjohn, T. A., Castaño, E. M., Van Vickle, G. D., Kalback, W. M., Patton, R. L., Luehrs, D. C., Daugs, I. D., Kuo, Y., et al. (2009) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2008.10.004 · Cited by 414

A Structural Motif of Acetylcholinesterase That Promotes Amyloid β-Peptide Fibril Formation

De Ferrari, G. V., Canales, M. A., Shin, I., Weiner, L. M., Silman, I., & Inestrosa, N. C. (2001) · Biochemistry · doi:10.1021/bi0101392 · Cited by 413

Phenolic Compounds Prevent Alzheimer’s Pathology through Different Effects on the Amyloid-β Aggregation Pathway

Hamaguchi, T., Ono, K., Murase, A., & Yamada, M. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.090417 · Cited by 398

A Mouse Model of Amyloid β Oligomers: Their Contribution to Synaptic Alteration, Abnormal Tau Phosphorylation, Glial Activation, and Neuronal Loss In Vivo

Tomiyama, T., Matsuyama, S., Iso, H., Umeda, T., Takuma, H., Ohnishi, K., Ishibashi, K., Teraoka, R., Sakama, N., Yamashita, T., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5825-09.2010 · Cited by 396

Longer Forms of Amyloid β Protein: Implications for the Mechanism of Intramembrane Cleavage by γ-Secretase

Qi-Takahara, Y., Morishima-Kawashima, M., Tanimura, Y., Dolios, G., Hirotani, N., Horikoshi, Y., Kametani, F., Maeda, M., Saido, T. C., Wang, R., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1575-04.2005 · Cited by 391

Proteolytic Degradation of Amyloid -Protein

Saido, T., & Leissring, M. A. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006379 · Cited by 368

Structural Characterization of a Soluble Amyloid β-Peptide Oligomer

Yu, L., Edalji, R., Harlan, J. E., Holzman, T. F., Lopez, A. P., Labkovsky, B., Hillen, H., Barghorn, S., Ebert, U., Richardson, P. L., et al. (2009) · Biochemistry · doi:10.1021/bi802046n · Cited by 354

A Novel ε-Cleavage within the Transmembrane Domain of the Alzheimer Amyloid Precursor Protein Demonstrates Homology with Notch Processing

Weidemann, A., Eggert, S., Reinhard, F. B. M., Vogel, M., Paliga, K., Baier, G., Masters, C. L., Beyreuther, K., & Evin, G. (2002) · Biochemistry · doi:10.1021/bi015794o · Cited by 351

Annular Protofibrils Are a Structurally and Functionally Distinct Type of Amyloid Oligomer

Kayed, R., Pensalfini, A., Margol, L., Sokolov, Y., Sarsoza, F., Head, E., Hall, J., & Glabe, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808591200 · Cited by 348

Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction

Tomic, J. L., Pensalfini, A., Head, E., & Glabe, C. G. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.05.024 · Cited by 336

Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure

Paravastu, A. K., Qahwash, I., Leapman, R. D., Meredith, S. C., & Tycko, R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812033106 · Cited by 322

Zinc ions promote Alzheimer Aβ aggregation via population shift of polymorphic states

Miller, Y., Ma, B., & Nussinov, R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913114107 · Cited by 301

Resveratrol Selectively Remodels Soluble Oligomers and Fibrils of Amyloid Aβ into Off-pathway Conformers

Ladiwala, A. R. A., Lin, J. C., Bale, S. S., Marcelino-Cruz, A. M., Bhattacharya, M., Dordick, J. S., & Tessier, P. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.133108 · Cited by 297

Resveratrol inhibits beta-amyloid oligomeric cytotoxicity but does not prevent oligomer formation

Feng, Y., Wang, X.-P., Yang, S.-G., Wang, Y.-J., Zhang, X., Du, X.-T., Sun, X.-X., Zhao, M., Huang, L., & Liu, R.-T. (2009) · NeuroToxicology · doi:10.1016/j.neuro.2009.08.013 · Cited by 295

Copper and Zinc Binding to Amyloid‐β: Coordination, Dynamics, Aggregation, Reactivity and Metal‐Ion Transfer

Faller, P. (2009) · ChemBioChem · doi:10.1002/cbic.200900321 · Cited by 285

A facile method for expression and purification of the Alzheimer’s disease‐associated amyloid β‐peptide

Walsh, D. M., Thulin, E., Minogue, A. M., Gustavsson, N., Pang, E., Teplow, D. B., & Linse, S. (2009) · The FEBS Journal · doi:10.1111/j.1742-4658.2008.06862.x · Cited by 284

Induction of cerebral β-amyloidosis: Intracerebral versus systemic Aβ inoculation

Eisele, Y. S., Bolmont, T., Heikenwalder, M., Langer, F., Jacobson, L. H., Yan, Z.-X., Roth, K., Aguzzi, A., Staufenbiel, M., Walker, L. C., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903200106 · Cited by 279

Increasing Cu bioavailability inhibits Aβ oligomers and tau phosphorylation

Crouch, P. J., Hung, L. W., Adlard, P. A., Cortes, M., Lal, V., Filiz, G., Perez, K. A., Nurjono, M., Caragounis, A., Du, T., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809057106 · Cited by 278

Human APOE Isoform-Dependent Effects on Brain β-Amyloid Levels in PDAPP Transgenic Mice

Bales, K. R., Liu, F., Wu, S., Lin, S., Koger, D., DeLong, C., Hansen, J. C., Sullivan, P. M., & Paul, S. M. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.0887-09.2009 · Cited by 274

High‐molecular‐weight β‐amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients

Fukumoto, H., Tokuda, T., Kasai, T., Ishigami, N., Hidaka, H., Kondo, M., Allsop, D., & Nakagawa, M. (2010) · The FASEB Journal · doi:10.1096/fj.09-150359 · Cited by 264

Comparison of Alzheimer Aβ(1–40) and Aβ(1–42) amyloid fibrils reveals similar protofilament structures

Schmidt, M., Sachse, C., Richter, W., Xu, C., Fändrich, M., & Grigorieff, N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905007106 · Cited by 261

Amyloid β-Protein Dimers Rapidly Form Stable Synaptotoxic Protofibrils

O'Nuallain, B., Freir, D. B., Nicoll, A. J., Risse, E., Ferguson, N., Herron, C. E., Collinge, J., & Walsh, D. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.3537-10.2010 · Cited by 259

Pleomorphic Copper Coordination by Alzheimer’s Disease Amyloid-β Peptide

Drew, S. C., Noble, C. J., Masters, C. L., Hanson, G. R., & Barnham, K. J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja808073b · Cited by 241

Elucidation of Amyloid β-Protein Oligomerization Mechanisms: Discrete Molecular Dynamics Study

Urbanc, B., Betnel, M., Cruz, L., Bitan, G., & Teplow, D. B. (2010) · Journal of the American Chemical Society · doi:10.1021/ja9096303 · Cited by 237

The presence of sodium dodecyl sulphate-stable Aβ dimers is strongly associated with Alzheimer-type dementia

Mc Donald, J. M., Savva, G. M., Brayne, C., Welzel, A. T., Forster, G., Shankar, G. M., Selkoe, D. J., Ince, P. G., & Walsh, D. M. (2010) · Brain · doi:10.1093/brain/awq065 · Cited by 234

A Role for Synaptic Zinc in Activity-Dependent Aβ Oligomer Formation and Accumulation at Excitatory Synapses

Deshpande, A., Kawai, H., Metherate, R., Glabe, C. G., & Busciglio, J. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.5980-08.2009 · Cited by 232

Pyroglutamate Formation Influences Solubility and Amyloidogenicity of Amyloid Peptides

Schlenzig, D., Manhart, S., Cinar, Y., Kleinschmidt, M., Hause, G., Willbold, D., Funke, S. A., Schilling, S., & Demuth, H.-U. (2009) · Biochemistry · doi:10.1021/bi900818a · Cited by 228

In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to alzheimer's disease β-protein

Castaño, E. M., Ghiso, J., Prelli, F., Gorevic, P. D., Migheli, A., & Frangione, B. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80241-8 · Cited by 225

A Specific Enzyme-Linked Immunosorbent Assay for Measuring β-Amyloid Protein Oligomers in Human Plasma and Brain Tissue of Patients With Alzheimer Disease

Xia, W., Yang, T., Shankar, G., Smith, I. M., Shen, Y., Walsh, D. M., & Selkoe, D. J. (2009) · Archives of Neurology · doi:10.1001/archneurol.2008.565 · Cited by 216

Design, Selection, and Characterization of Thioflavin-Based Intercalation Compounds with Metal Chelating Properties for Application in Alzheimer’s Disease

Rodríguez-Rodríguez, C., Sánchez de Groot, N., Rimola, A., Álvarez-Larena, Á., Lloveras, V., Vidal-Gancedo, J., Ventura, S., Vendrell, J., Sodupe, M., & González-Duarte, P. (2009) · Journal of the American Chemical Society · doi:10.1021/ja806062g · Cited by 210

Fluid Biomarkers in Alzheimer Disease

Blennow, K., Zetterberg, H., & Fagan, A. M. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006221 · Cited by 208

Copper(II) Binding to Amyloid-β Fibrils of Alzheimer’s Disease Reveals a Picomolar Affinity: Stoichiometry and Coordination Geometry Are Independent of Aβ Oligomeric Form

Sarell, C. J., Syme, C. D., Rigby, S. E. J., & Viles, J. H. (2009) · Biochemistry · doi:10.1021/bi900254n · Cited by 208

The challenges of determining metal–protein affinities

Xiao, Z., & Wedd, A. G. (2010) · Natural Product Reports · doi:10.1039/b906690j · Cited by 207

Progressive accumulation of amyloid‐ β oligomers in Alzheimer’s disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins

Pham, E., Crews, L., Ubhi, K., Hansen, L., Adame, A., Cartier, A., Salmon, D., Galasko, D., Michael, S., Savas, J. N., et al. (2010) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07719.x · Cited by 206

The precursor of Alzheimer??s disease amyloid A4 protein resembles a cell-surface receptor

Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J., Masters, C., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & M??ller-Hill, B. (1987) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-198701030-00032 · Cited by 195

Pulse EPR Spectroscopy Reveals the Coordination Sphere of Copper(II) Ions in the 1–16 Amyloid‐β Peptide: A Key Role of the First Two N‐Terminus Residues

Dorlet, P., Gambarelli, S., Faller, P., & Hureau, C. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200904567 · Cited by 195

Concentration Dependent Cu2+Induced Aggregation and Dityrosine Formation of the Alzheimer's Disease Amyloid-β Peptide

Smith, D. P., Ciccotosto, G. D., Tew, D. J., Fodero-Tavoletti, M. T., Johanssen, T., Masters, C. L., Barnham, K. J., & Cappai, R. (2007) · Biochemistry · doi:10.1021/bi0620961 · Cited by 194

In vivo oxidative stress in brain of Alzheimer disease transgenic mice: Requirement for methionine 35 in amyloid β-peptide of APP

Butterfield, D. A., Galvan, V., Lange, M. B., Tang, H., Sowell, R. A., Spilman, P., Fombonne, J., Gorostiza, O., Zhang, J., Sultana, R., et al. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.035 · Cited by 188

A Novel Nicotinic Acetylcholine Receptor Subtype in Basal Forebrain Cholinergic Neurons with High Sensitivity to Amyloid Peptides

Liu, Q., Huang, Y., Xue, F., Simard, A., DeChon, J., Li, G., Zhang, J., Lucero, L., Wang, M., Sierks, M., et al. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3952-08.2009 · Cited by 182

Zn(II)‐ and Cu(II)‐induced non‐fibrillar aggregates of amyloid‐β (1–42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators

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Size-dependent neurotoxicity of β-amyloid oligomers

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Crystal Structure of the Amyloid-β p3 Fragment Provides a Model for Oligomer Formation in Alzheimer's Disease

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Cholesterol Modulates the Interaction of β-Amyloid Peptide with Lipid Bilayers

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Small moleculeβ‐amyloid inhibitors that stabilize protofibrillar structuresin vitroimprove cognition and pathology in a mouse model of Alzheimer’s disease

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Molecular Dynamics Simulations to Investigate the Aggregation Behaviors of the Aß(17–42) Oligomers

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A domain level interaction network of amyloid precursor protein and Aβ of Alzheimer's disease

Perreau, V. M., Orchard, S. E., Adlard, P. A., Bellingham, S. A., Cappai, R., Ciccotosto, G. D., Cowie, T., Crouch, P. J., Duce, J. A., Evin, G. M., et al. (2010) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/pmic.200900773 · Cited by 51

Mechanism of zinc(II)-promoted amyloid formation: zinc(II) binding facilitates the transition from the partially α-helical conformer to aggregates of amyloid β protein(1–28)

Talmard, C., Yona, R. L., & Faller, P. (2008) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-008-0461-9 · Cited by 51

Surface-induced phase separation of a sphingomyelin/cholesterol/ganglioside GM1-planar bilayer on mica surfaces and microdomain molecular conformation that accelerates Aβ oligomerization

Mao, Y., Shang, Z., Imai, Y., Hoshino, T., Tero, R., Tanaka, M., Yamamoto, N., Yanagisawa, K., & Urisu, T. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.03.003 · Cited by 51

Comparative Molecular Dynamics Study of Aβ Adsorption on the Self-Assembled Monolayers

Wang, Q., Zhao, C., Zhao, J. W., Wang, J., Yang, J.-C., Yu, X., & Zheng, J. (2009) · Langmuir · doi:10.1021/la903070y · Cited by 50

Amyloid-β42 Oligomer Structures from Fibrils: A Systematic Molecular Dynamics Study

Horn, A. H. C., & Sticht, H. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp100023q · Cited by 50

Oligomerization Partially Explains the Lowering of Aβ42 in Alzheimer’s Disease Cerebrospinal Fluid

Englund, H., Gunnarsson, M. D., Brundin, R., Hedlund, M., Kilander, L., Lannfelt, L., & Pettersson, F. E. (2009) · Neurodegenerative Diseases · doi:10.1159/000225376 · Cited by 49

Real-time observation of model membrane dynamics induced by Alzheimer's amyloid beta

Morita, M., Vestergaard, M. C. M., Hamada, T., & Takagi, M. (2009) · Biophysical Chemistry · doi:10.1016/j.bpc.2009.12.004 · Cited by 48

Stereospecific interactions are necessary for Alzheimer disease amyloid-β toxicity.

Ciccotosto, G., Tew, D., Drew, S., Smith, D. G., Johanssen, T., Lal, V., Lau, T., Perez, K., Curtain, C., Wade, J., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.02.018 · Cited by 48

Ganglioside‐mediated aggregation of amyloid β‐proteins (Aβ): comparison between Aβ‐(1–42) and Aβ‐(1–40)

Ogawa, M., Tsukuda, M., YAMAGUCHI, T. J., Ikeda, K., Okada, T., Yano, Y., Hoshino, M., & Matsuzaki, K. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06997.x · Cited by 47

On the Stability of the Soluble Amyloid Aggregates

Sahoo, B., Nag, S., Sengupta, P., & Maiti, S. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.05.055 · Cited by 47

Biophysical analyses of synthetic amyloid-β(1–42) aggregates before and after covalent cross-linking. Implications for deducing the structure of endogenous amyloid-β oligomers

Moore, B. D., Rangachari, V., Tay, W. M., Milkovic, N. M., & Rosenberry, T. L. (2009) · Biochemistry · doi:10.1021/bi901571t · Cited by 43

Quenched hydrogen/deuterium exchange NMR characterization of amyloid‐β peptide aggregates formed in the presence of Cu2+ or Zn2+

Olofsson, A., Lindhagen‐Persson, M., Vestling, M., Sauer-Eriksson, A. E., & Öhman, A. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07113.x · Cited by 42

The interaction of amyloid Aβ(1–40) with lipid bilayers and ganglioside as studied by 31P solid-state NMR

Nakazawa, Y., Suzuki, Y., Williamson, M. P., Saitô, H., & Asakura, T. (2008) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2008.12.001 · Cited by 42

Probing the Effect of Amino-Terminal Truncation for Aβ1−40 Peptides

Takeda, T., & Klimov, D. K. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp9016773 · Cited by 42

Interaction of β-amyloid(1-40) peptide with pairs of metal ions: An electrospray ion trap mass spectrometric model study

Drochioiu, G., Manea, M., Drăguşanu, M., Murariu, M., Drăgan, E. S., Petre, B. A., Mező, G., & Przybylski, M. (2009) · Biophysical Chemistry · doi:10.1016/j.bpc.2009.05.008 · Cited by 42

The effect of solvents on the conformations of Amyloid β-peptide (1–42) studied by molecular dynamics simulation

Cao, Y., Li, J., Li, Y., & Zhu, X. (2008) · Journal of Molecular Structure THEOCHEM · doi:10.1016/j.theochem.2008.10.003 · Cited by 40

Electrochemical and Conformational Consequences of Copper (CuI and CuII) Binding to β‐Amyloid(1–40)

Brzyska, M., Trześniewska, K., Wieckowska, A., Szczepankiewicz, A. A., & Elbaum, D. (2009) · ChemBioChem · doi:10.1002/cbic.200800732 · Cited by 37

Analysis of Single Alzheimer Solid Plaque Cores by Laser Capture Microscopy and Nanoelectrospray/Tandem Mass Spectrometry

Söderberg, L., Bogdanović, N., Axelsson, B., Winblad, B. G., Näslund, J., & Tjernberg, L. O. (2006) · Biochemistry · doi:10.1021/bi060331+ · Cited by 37

Influence of Residue 22 on the Folding, Aggregation Profile, and Toxicity of the Alzheimer's Amyloid β Peptide

Perálvarez‐Marín, A., Mateos, L., Zhang, C., Singh, S., Cedazo-Mı́nguez, Á., Visa, N., Morozova‐Roche, L. A., Gräslund, A., & Barth, A. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.04.017 · Cited by 34

Molecular Modeling of Two Distinct Triangular Oligomers in Amyloid β-protein

Zheng, J., Yu, X., Wang, J., Yang, J.-C., & Wang, Q. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp907608s · Cited by 32

Expression, purification, and characterization of recombinant human β-amyloid42 peptide in Escherichia coli

Zhang, L., Yu, H., Song, C., Lin, X., Chen, B., Tan, C., Cao, G.-X., & Wang, Z. (2008) · Protein Expression and Purification · doi:10.1016/j.pep.2008.10.007 · Cited by 29

A chemical screening approach reveals that indole fluorescence is quenched by pre-fibrillar but not fibrillar amyloid-β

Reinke, A. A., Seh, H. Y., & Gestwicki, J. E. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.07.082 · Cited by 26

Membrane charge dependent states of the β-amyloid fragment Aβ (16–35) with differently charged micelle aggregates

Grimaldi, M., Scrima, M., Esposito, C., Vitiello, G., Ramunno, A., Limongelli, V., D’Errico, G., Novellino, E., & D’Ursi, A. M. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.12.012 · Cited by 26

Deprotonation of the Asp1Ala2 Peptide Bond Induces Modification of the Dynamic Copper(II) Environment in the Amyloid‐β Peptide near Physiological pH

Hureau, C., Coppel, Y., Dorlet, P., Solari, P. L., Sayen, S., Guillon, E., Sabater, L., & Faller, P. (2009) · Angewandte Chemie · doi:10.1002/ange.200904512 · Cited by 26

Methionine does not reduce Cu(II)–β-amyloid!—Rectification of the roles of methionine-35 and reducing agents in metal-centered oxidation chemistry of Cu(II)–β-amyloid

da Silva, G. F. Z., Lykourinou, V., Angerhofer, A., & Ming, L. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.11.004 · Cited by 23

Comparative Study of Inhibition at Multiple Stages of Amyloid-β Self-Assembly Provides Mechanistic Insight

Davis, T. J., Soto-Ortega, D. D., Kotarek, J. A., Gonzalez‐Velasquez, F. J., Sivakumar, K., Wu, L., Wang, Q., & Moss, M. A. (2009) · Molecular Pharmacology · doi:10.1124/mol.109.055301 · Cited by 23

Amyloid-beta peptide Aβp3-42 affects early aggregation of full-length Aβ1-42

Sanders, H. M., Lust, R. M., & Teller, J. K. (2009) · Peptides · doi:10.1016/j.peptides.2009.01.027 · Cited by 21

Effect of transition metals in synaptic damage induced by amyloid beta peptide

Uranga, R. M., Giusto, N. M., & Salvador, G. A. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.07.044 · Cited by 20

A high performance method for thermodynamic study on the binding of copper ion and glycine with Alzheimer’s amyloid β peptide

Behbehani, G. R., & Mirzaie, M. (2009) · Journal of Thermal Analysis and Calorimetry · doi:10.1007/s10973-008-9311-9 · Cited by 20

Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance

Olofsson, A., Sauer-Eriksson, A. E., & Öhman, A. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.10.034 · Cited by 19

Two Distinct Conformations of Aβ Aggregates on the Surface of Living PC12 Cells

Bateman, D. A., & Chakrabartty, A. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.01.056 · Cited by 19

Amphotericin B interactions with soluble oligomers of amyloid Abeta1-42 peptide.

Smith, N. W., Annunziata, O., & Dzyuba, S. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.02.016 · Cited by 19

Alzheimer Disease: An Update on Pathobiology and Treatment Strategies

Long, J. M., & Holtzman, D. M. (2019) · Cell · doi:10.1016/j.cell.2019.09.001 · Cited by 3,204

The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease

Spires-Jones, T. L., & Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.004 · Cited by 1,201

Microglia constitute a barrier that prevents neurotoxic protofibrillar Aβ42 hotspots around plaques

Condello, C., Yuan, P., Schain, A., & Grutzendler, J. (2015) · Nature Communications · doi:10.1038/ncomms7176 · Cited by 718

Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies

Nasica-Labouze, J., Nguyen, P. H., Sterpone, F., Berthoumieu, O., Buchete, N.-V., Coté, S., De Simone, A., Doig, A. J., Faller, P., Garcia, A., et al. (2015) · Chemical Reviews · doi:10.1021/cr500638n · Cited by 584

The preclinical phase of the pathological process underlying sporadic Alzheimer’s disease

Braak, H., & Del Tredici, K. (2015) · Brain · doi:10.1093/brain/awv236 · Cited by 540