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Times Cited: 373
Times Cited: 373
Times Cited
Times Co-cited
Similarity
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Soluble oligomers of amyloid Beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake.
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Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory.
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Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway.
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Soluble Aβ oligomers inhibit long-term potentiation through a mechanism involving excessive activation of extrasynaptic NR2B-containing NMDA receptors.
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AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss.
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Mapping synaptic glutamate transporter dysfunction in vivo to regions surrounding Aβ plaques by iGluSnFR two-photon imaging.
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Amyloid-β1-42 slows clearance of synaptically released glutamate by mislocalizing astrocytic GLT-1.
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Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models.
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Stuart A Lipton. Nat Rev Drug Discov 2006
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Mechanisms of hyperexcitability in Alzheimer's disease hiPSC-derived neurons and cerebral organoids vs isogenic controls.
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Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo.
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Synaptic and extrasynaptic NMDA receptors are gated by different endogenous coagonists.
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Complement and microglia mediate early synapse loss in Alzheimer mouse models.
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Aberrant excitatory neuronal activity and compensatory remodeling of inhibitory hippocampal circuits in mouse models of Alzheimer's disease.
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15
Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.