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

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works

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 · see citing works

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 · see citing works

Thioflavine T interaction with synthetic Alzheimer's disease β ‐amyloid peptides: Detection of amyloid aggregation in solution

LeVine, H. (1993) · Protein Science · doi:10.1002/pro.5560020312 · Cited by 2,268 · see citing works

3D structure of Alzheimer's amyloid-β(1–42) fibrils

Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D. A., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 2,001 · see citing works

The Scattering of Light and the Radial Distribution Function of High Polymer Solutions

Zimm, B. H. (1948) · The Journal of Chemical Physics · doi:10.1063/1.1746738 · Cited by 1,555 · see citing works

Molecular-weight Determination by Light Scattering.

Debye, P. J. W. (1947) · The Journal of Physical Chemistry · doi:10.1021/j150451a002 · Cited by 1,238 · see citing works

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 1,139 · see citing works

Plaque-independent disruption of neural circuits in Alzheimer’s disease mouse models

Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123 · see citing works

Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum?

Klein, W. (2001) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01749-5 · Cited by 989 · see citing works

Protofibrillar Intermediates of Amyloid β-Protein Induce Acute Electrophysiological Changes and Progressive Neurotoxicity in Cortical Neurons

Hartley, D. M., Walsh, D. M., Ye, C., Diehl, T. S., Vasquez, S., Vassilev, P., Teplow, D. B., & Selkoe, D. J. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-20-08876.1999 · Cited by 965 · see citing works

The Relationship between Aβ and Memory in the Tg2576 Mouse Model of Alzheimer's Disease

Westerman, M. A., Cooper-Blacketer, D., Mariash, A., Kotilinek, L., Kawarabayashi, T., Younkin, L. H., Carlson, G. A., Younkin, S. G., & Ashe, K. H. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-05-01858.2002 · Cited by 714 · see citing works

Binding of Dodecyl Sulfate to Proteins at High Binding Ratios. Possible Implications for the State of Proteins in Biological Membranes

Reynolds, J. A., & Tanford, C. (1970) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.66.3.1002 · Cited by 700 · see citing works

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 691 · see citing works

Characterization of Copper Interactions with Alzheimer Amyloid β Peptides: Identification of an Attomolar‐Affinity Copper Binding Site on Amyloid β1‐42

Atwood, C. S., Scarpa, R. C., Huang, X., Moir, R. D., Jones, W. D., Fairlie, D. P., Tanzi, R. E., & Bush, A. I. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0751219.x · Cited by 641 · see citing works

Effects of secreted oligomers of amyloid β‐protein on hippocampal synaptic plasticity: a potent role for trimers

Townsend, M., Shankar, G. M., Mehta, T., Walsh, D. M., & Selkoe, D. J. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2005.103754 · Cited by 619 · see citing works

Globular amyloid β‐peptide ₁₋₄₂ oligomer − a homogenous and stable neuropathological protein in Alzheimer's disease

Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03407.x · Cited by 559 · see citing works

Amyloid-β oligomers: their production, toxicity and therapeutic inhibition

Walsh, D. M., Klyubin, I. V., Fadeeva, J. V., Rowan, M. J., & Selkoe, D. J. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300552 · Cited by 507 · see citing works

Propagating structure of Alzheimer’s β-amyloid (10–35) is parallel β-sheet with residues in exact register

Benzinger, T. L. S., Gregory, D. M., Burkoth, T. S., Miller-Auer, H., Lynn, D. G., Botto, R. E., & Meredith, S. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13407 · Cited by 390 · see citing works

Interactions of Amyloid β-Protein with Various Gangliosides in Raft-Like Membranes: Importance of GM1 Ganglioside-Bound Form as an Endogenous Seed for Alzheimer Amyloid

Kakio, A., Nishimoto, S., Yanagisawa, K., Kozutsumi, Y., & Matsuzaki, K. (2002) · Biochemistry · doi:10.1021/bi0255874 · Cited by 387 · see citing works

Progress towards a molecular-level structural understanding of amyloid fibrils

Tycko, R. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2003.12.002 · Cited by 374 · see citing works

Copper Mediates Dityrosine Cross-Linking of Alzheimer's Amyloid-β

Atwood, C., Perry, G. L., Zeng, H., Kato, Y., Jones, W. D., Ling, K.-Q., Huang, X., Moir, R. D., Wang, D., Sayre, L. M., et al. (2003) · Biochemistry · doi:10.1021/bi0358824 · Cited by 371 · see citing works

Dimeric Amyloid β Protein Rapidly Accumulates in Lipid Rafts followed by Apolipoprotein E and Phosphorylated Tau Accumulation in the Tg2576 Mouse Model of Alzheimer's Disease

Kawarabayashi, T., Shoji, M., Younkin, L. H., Lin, W.-L., Dickson, D. W., Murakami, T., Matsubara, E., Abe, K., Ashe, K. H., & Younkin, S. G. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.5543-03.2004 · Cited by 365 · see citing works

Structural Characterization of a Soluble Amyloid β-Peptide Oligomer

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

Acceleration of Amyloid Fibril Formation by Specific Binding of Aβ-(1–40) Peptide to Ganglioside-containing Membrane Vesicles

Choo, L.-P., Garzon-Rodriguez, W., Glabe, C. G., & Surewicz, W. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.37.22987 · Cited by 310 · see citing works

Diverse compounds mimic Alzheimer disease–causing mutations by augmenting Aβ42 production

Kukar, T. L., Murphy, M. P., Eriksen, J. L., Sagi, S. A., Weggen, S., Smith, T. E., Ladd, T. B., Khan, M. A., Kache, R., Beard, J. D., et al. (2005) · Nature Medicine · doi:10.1038/nm1235 · Cited by 284 · see citing works

Studies on the in Vitro Assembly of Aβ 1–40: Implications for the Search for Aβ Fibril Formation Inhibitors

Goldsbury, C. S., Wirtz, S., Müller, S. A., Sunderji, S., Wicki, P., Aebi, U., & Frey, P. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4259 · Cited by 274 · see citing works

An improved method of preparing the amyloid β-protein for fibrillogenesis and neurotoxicity experiments

Fezoui, Y., Hartley, D. M., Harper, J. D., Khurana, R., Walsh, D. M., Condron, M. M., Selkoe, D. J., Lansbury, P. T., Fink, A. L., & Teplow, D. B. (2000) · Amyloid · doi:10.3109/13506120009146831 · Cited by 260 · see citing works

Structural Features of the Aβ Amyloid Fibril Elucidated by Limited Proteolysis

Kheterpal, I., Williams, A. D., Murphy, C. L., Bledsoe, B., & Wetzel, R. B. (2001) · Biochemistry · doi:10.1021/bi010805z · Cited by 199 · see citing works

The Oxidative Stress Metabolite 4-Hydroxynonenal Promotes Alzheimer Protofibril Formation

Siegel, S. J., Bieschke, J., Powers, E. T., & Kelly, J. W. (2007) · Biochemistry · doi:10.1021/bi061853s · Cited by 186 · see citing works

Solution State Characterization of Amyloid β-Derived Diffusible Ligands

Hepler, R. W., Grimm, K. M., Nahas, D. D., Breese, R., Chen-Dodson, E., Acton, P. J., Keller, P. M., Yeager, M. D., Wang, H., Shughrue, P. J., et al. (2006) · Biochemistry · doi:10.1021/bi061850f · Cited by 181 · see citing works

Growth of β-Amyloid(1−40) Protofibrils by Monomer Elongation and Lateral Association. Characterization of Distinct Products by Light Scattering and Atomic Force Microscopy

Nichols, M. R., Moss, M. A., Reed, D. K., Lin, W.-L., Mukhopadhyay, R., Hoh, J. H., & Rosenberry, T. L. (2002) · Biochemistry · doi:10.1021/bi015985r · Cited by 179 · see citing works

The interaction between Alzheimer amyloid β(1–40) peptide and ganglioside GM1‐containing membranes

Choo, L.-P., & Surewicz, W. K. (1997) · FEBS Letters · doi:10.1016/s0014-5793(96)01504-9 · Cited by 178 · see citing works

Mechanism of Cross-Species Prion Transmission

Tanaka, M., Chien, P., Yonekura, K., & Weissman, J. S. (2005) · Cell · doi:10.1016/j.cell.2005.03.008 · Cited by 177 · see citing works

Mass spectrometric proteome analyses of synovial fluids and plasmas from patients suffering from rheumatoid arthritis and comparison to reactive arthritis or osteoarthritis.

Sinz, A., Bantscheff, M., Mikkat, S., Ringel, B., Drynda, S., Kekow, J., Thiesen, H., & Glocker, M. O. (2002) · Electrophoresis · doi:10.1002/1522-2683(200210)23:19 · Cited by 176 · see citing works

Amyloid-β(1−42) Rapidly Forms Protofibrils and Oligomers by Distinct Pathways in Low Concentrations of Sodium Dodecylsulfate

Rangachari, V., Moore, B. D., Reed, D. K., Sonoda, L. K., Bridges, A. W., Conboy, E. E., Hartigan, D., & Rosenberry, T. L. (2007) · Biochemistry · doi:10.1021/bi701213s · Cited by 154 · see citing works

APP Transgenic Mice Tg2576 Accumulate Aβ Peptides That Are Distinct from the Chemically Modified and Insoluble Peptides Deposited in Alzheimer's Disease Senile Plaques

Kalback, W. M., Watson, M. D., Kokjohn, T. A., Kuo, Y., Weiss, N., Luehrs, D. C., Lopez, J. C., Brune, D. C., Sisodia, S. S., Staufenbiel, M., et al. (2001) · Biochemistry · doi:10.1021/bi015685+ · Cited by 146 · see citing works

Irreversible dimerization/tetramerization and post-translational modifications inhibit proteolytic degradation of Aβ peptides of Alzheimer's disease

Kuo, Y.-M., Webster, S., Emmerling, M. R., De Lima, N., & Roher, A. E. (1998) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(98)00014-3 · Cited by 122 · see citing works

Amyloid-β Protofibrils Differ from Amyloid-β Aggregates Induced in Dilute Hexafluoroisopropanol in Stability and Morphology

Nichols, M. R., Moss, M. A., Reed, D. K., Cratic-McDaniel, S., Hoh, J. H., & Rosenberry, T. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410553200 · Cited by 113 · see citing works

Transglutaminase facilitates the formation of polymers of the β-amyloid peptide

Dudek, S. M., & Johnson, G. V. W. (1994) · Brain Research · doi:10.1016/0006-8993(94)90688-2 · Cited by 106 · see citing works

Transglutaminase Induces Protofibril-like Amyloid β-Protein Assemblies That Are Protease-resistant and Inhibit Long-term Potentiation

Hartley, D. M., Zhao, C., Speier, A. C., Woodard, G. A., Li, S., Li, Z., & Walz, T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802215200 · Cited by 95 · see citing works

Soluble multimeric Alzheimer β(1–40) pre-amyloid complexes in dilute solution

LeVine, H. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00052-g · Cited by 94 · see citing works

Transglutaminases and Transglutaminase‐Catalyzed Cross‐Links Colocalize with the Pathological Lesions in Alzheimer's Disease Brain

Wilhelmus, M. M. M., Grunberg, S. C. S., Bol, J. G. J. M., van Dam, A., Hoozemans, J. J. M., Rozemüller, A. J. M., & Drukarch, B. (2008) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00197.x · Cited by 90 · see citing works

Secondary Structure and Interfacial Aggregation of Amyloid-β(1−40) on Sodium Dodecyl Sulfate Micelles

Rangachari, V., Reed, D. K., Moore, B. D., & Rosenberry, T. L. (2006) · Biochemistry · doi:10.1021/bi060323t · Cited by 84 · see citing works

Assembly of hereditary amyloid β‐protein variants in the presence of favorable gangliosides

Yamamoto, N., Hirabayashi, Y., Amari, M., Yamaguchi, H., Romanov, G. A., Nostrand, W. E. V., & Yanagisawa, K. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.013 · Cited by 69 · see citing works

Prostaglandin H2 (PGH2) accelerates formation of amyloid β1−42 oligomers

Boutaud, O. G., Ou, J. J., Chaurand, P., et al. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01064.x · Cited by 57 · see citing works

Dissecting the Mechanisms of Tissue Transglutaminase-induced Cross-linking of α-Synuclein

Schmid, A. W., Chiappe, D., Pignat, V., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809067200 · Cited by 49 · see citing works

Covalent Blocking of Fibril Formation and Aggregation of Intracellular Amyloidgenic Proteins by Transglutaminase-Catalyzed Intramolecular Cross-Linking

Konno, T., Morii, T., Hirata, A., et al. (2005) · Biochemistry · doi:10.1021/bi047722d · Cited by 46 · see citing works

PGH2‐derived levuglandin adducts increase the neurotoxicity of amyloid β1–42

Boutaud, O. G., Montine, T. J., Chang, L., Klein, W. L., & Oates, J. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03586.x · Cited by 44 · see citing works

Rapid Assembly of Amyloid-β Peptide at a Liquid/Liquid Interface Produces Unstable β-Sheet Fibers

Nichols, M. R., Moss, M. A., Reed, D. K., Hoh, J. H., & Rosenberry, T. L. (2004) · Biochemistry · doi:10.1021/bi048846t · Cited by 39 · see citing works

Reductive Glutaraldehydation of Amine Groups for Identification of Protein N-termini

Russo, A., Chandramouli, N., Zhang, L., et al. (2008) · Journal of Proteome Research · doi:10.1021/pr800224v · Cited by 23 · see citing works

A triaxial probe for on-line proteolysis coupled with hydrogen/deuterium exchange-electrospray mass spectrometry

Chen, M., Cook, K. D., Kheterpal, I., et al. (2006) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2006.09.011 · Cited by 14 · see citing works

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 · see citing works

APOE4-specific Changes in Aβ Accumulation in a New Transgenic Mouse Model of Alzheimer Disease

Youmans, K. L., Tai, L. M., Nwabuisi-Heath, E., Jungbauer, L., Kanekiyo, T., Gan, M., Kim, J., Eimer, W. A., Estus, S., Rebeck, G. W., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407957 · Cited by 259 · see citing works

Levels of Soluble Apolipoprotein E/Amyloid-β (Aβ) Complex Are Reduced and Oligomeric Aβ Increased with APOE4 and Alzheimer Disease in a Transgenic Mouse Model and Human Samples*

Tai, L. M., Bilousova, T., Jungbauer, L., Roeske, S. K., Youmans, K. L., Yu, C., Poon, W. W., Cornwell, L. B., Miller, C. A., Vinters, H. V., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442103 · Cited by 165 · see citing works

Does deamidation of islet amyloid polypeptide accelerate amyloid fibril formation?

Lam, Y. P. Y., Wootton, C. A., Hands-Portman, I., Wei, J., Chiu, C. K. C., Romero‐Canelón, I., Lermyte, F., Barrow, M. P., & O’Connor, P. B. (2018) · Chemical Communications · doi:10.1039/c8cc06675b · Cited by 12 · see citing works

Amyloid of human islets of Langerhans

Westermark, P. (1977) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/bf00432160 · Cited by 36 · see citing works

Protein amyloid aggregate: Structure and function

Xu, Q., Ma, Y., Sun, Y., Li, D., Zhang, X., & Liu, C. (2023) · Aggregate · doi:10.1002/agt2.333 · Cited by 56 · see citing works

[Systemic amyloidoses--new treatment methods make early and exact diagnosis more and more important].

Westermark, P. (2007) · PubMed · Cited by 4 · see citing works

Senile Cardiac Amyloidosis: Evidence of Two Different Amyloid Substances in the Ageing Heart

Westermark, P., Johansson, B. P., & Natvig, J. B. (1979) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1979.tb01356.x · Cited by 112 · see citing works