A specific amyloid-β protein assembly in the brain impairs memory

By Sylvain E. Lesné, M. T. Koh, L. Kotilinek, R. Kayed, C. Glabe, A. Yang, M. Gallagher, K. Ashe. Nature, 2006

2,628 citations recorded by the source corpus.

Subfields: Pharmacology, Physiology, Psychiatry and Mental health

View Paper: https://www.semanticscholar.org/paper/59ac83c0996f36ac23f94ddad3d96782c9f157a8

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Citations in the corpus

The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy (2016, background): “Soluble Aβ oligomers have been reported in AD to be organized into different structures ranging from dimers (Walsh et al., 2000), trimers (Walsh et al., 2000; Chen and Glabe, 2006), tetramers (Walsh et al., 2000; Chen and Glabe, 2006), pentamers and decamers (Ahmed et al., 2010), Aβ-derived diffusib”
Alzheimer's disease. (2011, background): “, a metastable docamer designated Ab 56) from the brains of certain APP transgenic mice (Lesne et al. 2006).”
Modeling Alzheimer's disease with iPSCs reveals stress phenotypes associated with intracellular Aβ and differential drug responsiveness. (2013, background): “…Aβ oligomers extracted from AD-model mice or made from synthetic peptide cause neurotoxicity and cognitive impairments in vitro and in vivo (Walsh et al., 2002; Gong et al., 2003; Lesné et al., 2006), and this was also true in humans (Kuo et al., 2006; Shankar et al., 2008; Noguchi et al., 2009).”
Aβ Oligomers Cause Localized Ca2+ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines (2010, background): “We also note that in our preparations we did not consistently observe a band at 56 kDa, a species that has been reported to be toxic for transgenic mice (Lesné et al., 2006) but can be visualized in certain conditions (Walsh et al., 2005; Ashe, 2006; Bernstein et al., 2009).”
Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils (2010, neutral): “Considerably less is known about the molecular structure of A β oligomers, which have been shown to cause neuronal dysfunction 21 – 23 , disrupt long-term potentiation 24 , and impair memory in mouse models of AD 25 .”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “The fibrils are, however, far from innocuous material, as they can deplete key components of the protein homeostasis network (81, 196), (as we discuss farther below in the section titled Protein Metastability and the Proteostasis Network), serve as a reservoir of protein oligomers that can be releas”
Oligomeric amyloid β associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques (2009, background): “Recent evidence strongly indicates that soluble forms of A , including small A oligomers, induce synaptic changes and dendritic spine loss in cultured neurons and organotypic slices (4, 5, 17–20), and an oligomeric form of A correlates with memory loss in the Tg2576 mouse model (21, 22).”
Memantine: a NMDA receptor antagonist that improves memory by restoration of homeostasis in the glutamatergic system--too little activation is bad, too much is even worse. (2007, background): “Amyloid beta (Aß) is the principal constituent of senile plaques in AD and is believed to impair neuronal function and cognition, even before the appearance of overt toxicity (Lesne et al., 2006).”
Aβ Oligomers – a decade of discovery (2007, background): “…performance in a hippocampaldependent contextual fear conditioning assay, decreased spine density in the dentate gyrus, and impairment of long-term potentiation (LTP) at ages long before the first apparent detection of Ab dodecamer (Dineley et al. 2002; Jacobsen et al. 2006; Lesne et al. 2006).”