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Icariin Ameliorates Amyloid Pathologies by Maintaining Homeostasis of Autophagic Systems in Aβ1–42-Injected Rats

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Pyk2 overexpression in postsynaptic neurons blocks amyloid β1–42-induced synaptotoxicity in microfluidic co-cultures

Kilinc, D., Vreulx, A.-C., Mendes, T., Flaig, A., Coelho, D. M., Verschoore, M., Demiautte, F., Amouyel, P., Bank, N.-C. B., Eysert, F., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa139 · Cited by 34

Mini-review: Amyloid degradation toxicity hypothesis of Alzheimer’s disease

Zaretsky, D. V., & Zaretskaia, M. V. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.135959 · Cited by 27

Finite-time stability and optimal control of a stochastic reaction-diffusion model for Alzheimer’s disease with impulse and time-varying delay

Hu, J., Zhang, Q., Meyer‐Baese, A., & Ye, M. (2021) · Applied Mathematical Modelling · doi:10.1016/j.apm.2021.10.004 · Cited by 26

Investigation of A β phosphorylated at serine 8 (p A β) in A lzheimer's disease, dementia with L ewy bodies and vascular dementia

Ashby, E. L., Miners, J. S., Kumar, S., Walter, J., Love, S., & Kehoe, P. G. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12212 · Cited by 26

Role of Small Oligomers on the Amyloidogenic Aggregation Free-Energy Landscape

He, X., Giurleo, J. T., & Talaga, D. S. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.10.019 · Cited by 26

Biological Tuning of Synthetic Tactics in Solid-Phase Synthesis: Application to Aβ(1−42)

Kim, Y. S., Moss, J. A., & Janda, K. D. (2004) · The Journal of Organic Chemistry · doi:10.1021/jo048922y · Cited by 27

Molecular determinants for amyloid fibril formation: lessons from lung surfactant protein C

Johansson, J. (2003) · Swiss Medical Weekly · doi:10.4414/smw.2003.09987 · Cited by 26

Neuroprotective effects of diarylpropionitrile against β-amyloid peptide-induced neurotoxicity in rat cultured cortical neurons

Suwanna, N., Thangnipon, W., & Soi‐ampornkul, R. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.06.029 · Cited by 26

Role of Species-Specific Primary Structure Differences in Aβ42 Assembly and Neurotoxicity

Roychaudhuri, R., Zheng, X., Lomakin, A., Maiti, P., Condron, M. M., Benedek, G. B., Bitan, G., Bowers, M. T., & Teplow, D. B. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00180 · Cited by 26

ABCA1 Deficiency Affects Basal Cognitive Deficits and Dendritic Density in Mice

Fitz, N. F., Carter, A. Y., Tapias, V., Castranio, E. L., Kodali, R. B., Lefterov, I. M., & Koldamova, R. P. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161056 · Cited by 27

Gastrodin as a multi-target protective compound reverses learning memory deficits and AD-like pathology in APP/PS1 transgenic mice

Yue-Qin, Z., Gu, J.-H., Chen, L., Zhang, T., & Zhou, X. (2020) · Journal of Functional Foods · doi:10.1016/j.jff.2020.104324 · Cited by 26

Synchrotron X-ray Fluorescence and FTIR Signatures for Amyloid Fibrillary and Nonfibrillary Plaques

Álvarez-Marimon, E., Castillo-Michel, H. A., Reyes-Herrera, J., Curto, J. S., Aso, E., Carmona, M., Ferrer, I., Cladera, J., & Benseny‐Cases, N. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00048 · Cited by 26

Amyloid Beta Peptides Differentially Affect Hippocampal Theta Rhythms In Vitro

Gutiérrez-Lerma, A. I., Ordaz, B., & Peña‐Ortega, F. (2013) · International Journal of Peptides · doi:10.1155/2013/328140 · Cited by 26

Synthesis and Purification of Highly Hydrophobic Peptides Derived from the C-Terminus of Amyloid β-Protein

Condron, M. M., Monien, B. H., & Bitan, G. (2008) · The Open Biotechnology Journal · doi:10.2174/1874070700802010087 · Cited by 27

Effects of Tissue Transglutaminase on β -Amyloid1-42-Induced Apoptosis

Wakshlag, J. J., Antonyak, M. A., Boehm, J. E., Boehm, K., & Cerione, R. A. (2006) · The Protein Journal · doi:10.1007/s10930-006-0009-1 · Cited by 26

In vivo labelling of hippocampal β‐amyloid in triple‐transgenic mice with a fluorescent acetylcholinesterase inhibitor released from nanoparticles

Härtig, W., Kacza, J., Paulke, B., Grosche, J., Bauer, U. U. I., Hoffmann, A., Elsinghorst, P. W., & Gütschow, M. (2009) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.07038.x · Cited by 26

Distinctive roles of different β‐amyloid 42 aggregates in modulation of synaptic functions

Chiang, H., Iijima, K., Hakker, I., & Zhong, Y. (2009) · The FASEB Journal · doi:10.1096/fj.08-121152 · Cited by 25

Monitoring Insulin Aggregation via Capillary Electrophoresis

Pryor, E. N., Kotarek, J. A., Moss, M. A., & Hestekin, C. N. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12129369 · Cited by 28

Triptolide derivatives as potential multifunctional anti-Alzheimer agents: Synthesis and structure–activity relationship studies

Ning, C., Mo, L., Chen, X., Tu, W., Wu, J., Hou, S., & Xu, J. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.01.019 · Cited by 26

Amyloid Beta Secreted during Consolidation Prevents Memory Malleability

Finnie, P. S. B., & Nader, K. (2020) · Current Biology · doi:10.1016/j.cub.2020.02.083 · Cited by 30

Pentapeptides derived from Aβ1–42 protect neurons from the modulatory effect of Aβ fibrils—an in vitro and in vivo electrophysiological study

Szegedi, V., Fülöp, L., Farkas, T., Rózsa, É., Robotka, H., Kis, Z., Penke, Z., Horváth, S., Molnár, Z., Datki, Z., et al. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.12.008 · Cited by 26

Human Amylin Actions on Rat Cholinergic Basal Forebrain Neurons: Antagonism of Beta-Amyloid Effects

Jhamandas, J. H., Harris, K. H., Cho, C., Fu, W., & MacTavish, D. (2003) · Journal of Neurophysiology · doi:10.1152/jn.01138.2002 · Cited by 26

The Alzheimer’s β amyloid (Aβ1–39) monomer in an implicit solvent

Anand, P., Nandel, F. S., & Hansmann, U. H. E. (2008) · The Journal of Chemical Physics · doi:10.1063/1.2907718 · Cited by 26

PACAP–Sirtuin3 alleviates cognitive impairment through autophagy in Alzheimer’s disease

Wang, Q., Wang, Y., Li, S., & Shi, J. (2023) · Alzheimer s Research & Therapy · doi:10.1186/s13195-023-01334-2 · Cited by 25

Drug Development in Alzheimer’s Disease: The Contribution of PET and SPECT

Declercq, L., Vandenberghe, R. R., Laere, K. V., Verbruggen, A., & Bormans, G. M. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00088 · Cited by 27

In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis

Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015

P1‐167: Effects of beta‐amyloid oligomers on neuronal viability and microglial activation

Ferrera, D., Canale, C., Benfenati, F., & Gasparini, L. (2009) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2009.04.173

Effect of different Aβ1-42 assemblies on neuronal cell viability

Morkūnienė, R., Čižas, P., Budvytytė, R., Valinčius, G., & Borutaitė, V. (2010) · Lithuanian University of Health Sciences

P4–014: Divergent cytotoxic mechanisms of soluble and fibrillar forms of AAY in human cortical neurons

Deshpande, A. M., Mina, E. W., Glabe, C. G., & Busciglio, J. A. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.05.1752

Fractionation and characterization of oligomeric, protofibrillar and fibrillar forms of β-amyloid peptide

Ward, R. V., JENNINGS, K. H., Jepras, R., Neville, W. A., OWEN, D. E., HAWKINS, J., Christie, G., Davis, J. B., George, A. R., Karran, E. H., et al. (2000) · Biochemical Journal · doi:10.1042/bj3480137 · Cited by 153