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Alzheimer's Disease Brain-Derived Amyloid-β-Mediated Inhibition of LTP In Vivo Is Prevented by Immunotargeting Cellular Prion Protein.
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- Journal of Neuroscience, 2011, v. 31, n. 20, p. 7259, doi. 10.1523/JNEUROSCI.6500-10.2011
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- Article
Amyloid β Protein Dimer-Containing Human CSF Disrupts Synaptic Plasticity: Prevention by Systemic Passive Immunization.
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- Journal of Neuroscience, 2008, v. 28, n. 16, p. 4231, doi. 10.1523/JNEUROSCI.5161-07.2008
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- Article
A monoclonal antibody against synthetic Aβ dimer assemblies neutralizes brain-derived synaptic plasticity-disrupting Aβ.
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- Journal of Neurochemistry, 2011, v. 119, n. 1, p. 189, doi. 10.1111/j.1471-4159.2011.07389.x
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- Article
Naturally secreted oligomers of amyloid Β protein potently inhibit hippocampal long-term potentiation in vivo.
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- Nature, 2002, v. 416, n. 6880, p. 535, doi. 10.1038/416535a
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- Article
Longitudinal testing of hippocampal plasticity reveals the onset and maintenance of endogenous human Aß-induced synaptic dysfunction in individual freely behaving pre-plaque transgenic rats: rapid reversal by anti-Aß agents.
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- Acta Neuropathologica Communications, 2014, v. 2, n. 1, p. 1, doi. 10.1186/s40478-014-0175-x
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- Article
Exosomes neutralize synaptic-plasticity-disrupting activity of Abeta assemblies in vivo.
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- Molecular Brain, 2013, v. 6, n. 1, p. 1, doi. 10.1186/1756-6606-6-47
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- Article
Alzheimer's disease Aβ assemblies mediating rapid disruption of synaptic plasticity and memory.
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- Molecular Brain, 2012, v. 5, n. 1, p. 25, doi. 10.1186/1756-6606-5-25
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- Article
Persistent inhibition of hippocampal long-term potentiation in vivo by learned helplessness stress.
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- Hippocampus, 2010, v. 20, n. 6, p. 758, doi. 10.1002/hipo.20677
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- Article
Cellular Prion Protein Mediates the Disruption of Hippocampal Synaptic Plasticity by Soluble Tau In Vivo.
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- Journal of Neuroscience, 2018, v. 38, n. 50, p. 10595, doi. 10.1523/JNEUROSCI.1700-18.2018
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- Article
Peripheral Administration of a Humanized Anti-PrP Antibody Blocks Alzheimer's Disease Aβ Synaptotoxicity.
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- Journal of Neuroscience, 2014, v. 34, n. 18, p. 6140, doi. 10.1523/JNEUROSCI.3526-13.2014
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- Article
IMPAIRED REVERSAL OF HIPPOCAMPAL LONG-TERM POTENTIATION IN APP-OVEREXPRESSING RATS IN VIVO.
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- Alzheimer's & Dementia: The Journal of the Alzheimer's Association, 2017, v. 13, p. P283, doi. 10.1016/j.jalz.2017.06.178
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- Article
Alzheimer's disease human brain beta-amyloid-containing extracts inhibit hippocampal long-term potentiation in rats in vivo: Relationship between soluble and insoluble preparations
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- 2012
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- Abstract
Do tau-synaptic long-term depression interactions in the hippocampus play a pivotal role in the progression of Alzheimer's disease?
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- Neural Regeneration Research, 2023, v. 18, n. 6, p. 1213, doi. 10.4103/1673-5374.360166
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- Article
Alzheimer’s Disease Amyloid β-Protein and Synaptic Function.
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- NeuroMolecular Medicine, 2010, v. 12, n. 1, p. 13, doi. 10.1007/s12017-009-8091-0
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- Article
Tau and Amyloid β Protein in Patient-Derived Aqueous Brain Extracts Act Concomitantly to Disrupt Long-Term Potentiation in Vivo.
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- Journal of Neuroscience, 2023, v. 43, n. 32, p. 5870, doi. 10.1523/JNEUROSCI.0082-23.2023
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- Article
Gamma‐patterned sensory stimulation reverses synaptic plasticity deficits in rat models of early Alzheimer's disease.
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- European Journal of Neuroscience, 2023, v. 58, n. 6, p. 3402, doi. 10.1111/ejn.16129
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- Article
Pre-plaque Aß-Mediated Impairment of Synaptic Depotentiation in a Transgenic Rat Model of Alzheimer's Disease Amyloidosis.
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- Frontiers in Neuroscience, 2019, p. 1, doi. 10.3389/fnins.2019.00861
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- Article
Hippocampal hyperactivity in a rat model of Alzheimer's disease.
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- Journal of Neurochemistry, 2021, v. 157, n. 6, p. 2128, doi. 10.1111/jnc.15323
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- Article
Soluble Arctic amyloid β protein inhibits hippocampal long-term potentiation in vivo.
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- European Journal of Neuroscience, 2004, v. 19, n. 10, p. 2839, doi. 10.1111/j.1460-9568.2004.03389.x
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- Article
Amyloidßprotein immunotherapy neutralizes Aßoligomers that disrupt synaptic plasticity in vivo.
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- Nature Medicine, 2005, v. 11, n. 5, p. 556, doi. 10.1038/nm1234
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- Article