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Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
TLDR
It is reported that natural oligomers of human Aβ are formed soon after generation of the peptide within specific intracellular vesicles and are subsequently secreted from the cell, indicating that synaptotoxic Aβ oligomers can be targeted therapeutically. Expand
Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
TLDR
It is concluded that soluble Aβ oligomers extracted from Alzheimer's disease brains potently impair synapse structure and function and that dimers are the smallest synaptotoxic species. Expand
Natural Oligomers of the Alzheimer Amyloid-β Protein Induce Reversible Synapse Loss by Modulating an NMDA-Type Glutamate Receptor-Dependent Signaling Pathway
TLDR
It is concluded that soluble, low-n oligomers of human Aβ trigger synapse loss that can be reversed by therapeutic agents and provides a quantitative cellular model for elucidating the molecular basis of Aβ-induced neuronal dysfunction. Expand
Aβ Oligomers – a decade of discovery
TLDR
Accumulating evidence suggests that soluble forms of Aβ are indeed the proximate effectors of synapse loss and neuronal injury in Alzheimer’s disease. Expand
Soluble Oligomers of Amyloid β Protein Facilitate Hippocampal Long-Term Depression by Disrupting Neuronal Glutamate Uptake
TLDR
It is concluded that soluble Abeta oligomers perturb synaptic plasticity by altering glutamate recycling at the synapse and promoting synapse depression. Expand
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
TLDR
The biochemical isolation of discrete amyloid-β moieties with pathophysiological properties sets the stage for a new approach to studying the molecular mechanisms of cognitive impairment in Alzheimer disease and related neurodegenerative disorders. Expand
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
TLDR
The phenotype of the exogenously induced amyloidosis depended on both the host and the source of the agent, suggesting the existence of polymorphic Aβ strains with varying biological activities reminiscent of prion strains. Expand
Insulin-degrading Enzyme Regulates Extracellular Levels of Amyloid β-Protein by Degradation*
TLDR
It is concluded that a principal protease capable of down-regulating the levels of secreted Aβ extracellularly is IDE, and activity was unexpectedly found be associated with a time-dependent oligomerization of synthetic Aβ at physiological levels in the conditioned media of cultured cells. Expand
Deciphering the Molecular Basis of Memory Failure in Alzheimer's Disease
TLDR
Experiments in rodents suggest that soluble oligomers of the amyloid beta protein (Abeta) may discretely interfere with synaptic mechanisms mediating aspects of learning and memory, including long-term potentiation. Expand
Effects of secreted oligomers of amyloid β‐protein on hippocampal synaptic plasticity: a potent role for trimers
TLDR
The hypothesis that diffusible oligomers of Aβ initiate a synaptic dysfunction that may be an early event in AD is supported and specific assemblies, particularly timers of naturally secreted Aβ oligomers are potent and selective inhibitors of certain forms of hippocampal LTP. Expand
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