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Apolipoprotein E and Amyloidogenesis

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Aβ oligomer toxicity inhibitor protects memory in models of synaptic toxicity

Scopes, D., O‘Hare, E., Jeggo, R., Whyment, A. D., Spanswick, D. C., Kim, E.-M., Gannon, J., Amijee, H., & Treherne, J. M. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.01973.x · Cited by 17

Probing differences among Aβ oligomers with two triangular trimers derived from Aβ

Kreutzer, A. G., Guaglianone, G., Yoo, S., Parrocha, C. M. T., Ruttenberg, S. M., Malonis, R. J., Tong, K., Lin, Y.-F., Nguyen, J. T., Howitz, W. J., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2219216120 · Cited by 18

Copper(II) Can Kinetically Trap Arctic and Italian Amyloid-β40 as Toxic Oligomers, Mimicking Cu(II) Binding to Wild-Type Amyloid-β42: Implications for Familial Alzheimer’s Disease

Tian, Y., Shang, Q., Liang, R., & Viles, J. H. (2024) · JACS Au · doi:10.1021/jacsau.3c00687 · Cited by 18

AA protein in experimental murine AA amyloid fibrils: A high resolution ultrastructural and immunohistochemical study comparing aldehyde-fixed and cryofixed tissues

Inoué, S., Kuroiwa, M., & Kisilevsky, R. (2002) · Amyloid · doi:10.3109/13506120208995244 · Cited by 17

Arctic mutant Aβ40 aggregates on α7 nicotinic acetylcholine receptors and inhibits their functions

Ju, Y., Asahi, T., & Sawamura, N. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12837 · Cited by 17

Protective effects of components of the Chinese herb grassleaf sweetflag rhizome on PC12 cells incubated with amyloid-beta42

Liang, Z.-H., Cheng, X., Ruan, Z., Wang, H., Li, S., Liu, J., Li, G., & Tian, S. (2015) · Neural Regeneration Research · doi:10.4103/1673-5374.162762 · Cited by 17

Validation and Characterization of a Novel Peptide That Binds Monomeric and Aggregated β-Amyloid and Inhibits the Formation of Neurotoxic Oligomers

Barr, R. K., Verdile, G., Wijaya, L. K., Morici, M., Taddei, K., Gupta, V. B., Pedrini, S., Jin, L., Nicolazzo, J. A., Knock, E., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.679993 · Cited by 16

Internalization and resistance to degradation of Alzheimer's Aβ1–42 at nanomolar concentrations in THP-1 human monocytic cell line

Morelli, L., Giambartolomei, G. H., Prat, M. I., & Castaño, E. M. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00023-3 · Cited by 16

“Non‐VSEPR” Structures and Bonding in d0Systems

Kaupp, M. (2001) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20011001)40:19 · Cited by 171

Inhibitory effects of short-term administration of dl-α-lipoic acid on oxidative vulnerability induced by Aβ amyloid fibrils (25–35) in mice

Jesudason, E. P., Masilamoni, J. G., Ashok, B. S., Baben, B., Arul, V., Jesudoss, K. S., Walter, C. E. J., Dhandayuthapani, S., Vignesh, S., & Rajadas, J. (2008) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-008-9705-9 · Cited by 17

Secretases as targets for drug design in Alzheimer’s disease

Hendriksen, J. V. R. B., Nottet, H. S. L. M., & Smits, H. A. (2002) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.2002.00937.x · Cited by 17

Sleep duration and efficiency are associated with plasma amyloid-β in non-demented older people

Liu, Y., Chen, L., Huang, S., Lv, Z., Hu, L., Luo, J., Shang, P., Wang, Y., & Xie, H. (2021) · Neurological Sciences · doi:10.1007/s10072-021-05271-6 · Cited by 18

Influence of TiO2 and ZnO Nanoparticles on α-Synuclein and β-Amyloid Aggregation and Formation of Protein Fibrils

Slekiene, N., Snitka, V. J., Bružaitė, I., & Ramanavičius, A. (2022) · Materials · doi:10.3390/ma15217664 · Cited by 16

Elevation of BACE in an Aβ rat model of Alzheimer's disease: exacerbation by chronic stress and prevention by nicotine

Alkadhi, K. A., Alzoubi, K. H., Srivareerat, M., & Tran, T. T. (2011) · The International Journal of Neuropsychopharmacology · doi:10.1017/s1461145711000162 · Cited by 16

The APP and PS1/2 Mutations Linked to Early Onset Familial Alzheimer’s Disease Increase the Extracellular Concentration of Aβ1–42(43)

Younkin, S. G. (1998) · Springer eBooks · doi:10.1007/978-3-642-72103-8_4 · Cited by 16

Lipid-Induced Conformational Transition of Amyloid β Peptide Fragments

Nagarajan, S., Kirubagaran, R., Thangarajah, H., Malar, E. J. P., & Rajadas, J. (2010) · Journal of Molecular Neuroscience · doi:10.1007/s12031-010-9380-7 · Cited by 16

The βA4 Amyloid Protein Precursor in Human Circulationa

Bush, A. I., Beyreuther, K. T., & Masters, C. L. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb23048.x · Cited by 16

Binding of Amyloid Beta-Protein to Intracellular Brain Proteins in Rat and Human

Ray, I., Chauhan, A., Wı́sniewski, H. M., Węgiel, J., Kim, K. S., & Chauhan, V. P. S. (1998) · Neurochemical Research · doi:10.1023/a:1020744216699 · Cited by 16

Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease

Hilbich, C., Kisters–Woike, B., Reed, J., Masters, C. L., & Beyreuther, K. T. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90881-6 · Cited by 580

Human and rodent sequence analogs of Alzheimer's amyloid beta A4 share similar properties and can be solubilized in buffers of pH 7.4.

Hilbich, C., Kisters-Woike, B., Reed, J., Masters, C. L., & Beyreuther, K. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16256.x · Cited by 82

Amyloid βA4 of Alzheimer’s Disease: Structural Requirements for Folding and Aggregation

Hilbich, C., Kisters–Woike, B., Masters, C. L., & Beyreuther, K. T. (1994) · Springer eBooks · doi:10.1007/978-3-662-01135-5_3 · Cited by 2

Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease

Barrow, C. J., Yasuda, A., Kenny, P. T. M., & Zagorski, M. G. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90106-t · Cited by 644

Structural Determinants of the Alzheimer's Amyloid β‐Peptide

Soto, C. A., Brañes, M. C., Alvarez, J., & Inestrosa, N. C. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63041191.x · Cited by 153