Emilie Trillaud-Doppia

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Amyloid-β and tau protein are the two most prominent factors in the pathology of Alzheimer disease. Recent studies indicate that phosphorylated tau might affect synaptic function. We now show that endogenous tau is found at postsynaptic sites where it interacts with the PSD95-NMDA receptor complex. NMDA receptor activation leads to a selective(More)
Locomotion requires the proper sequencing of neural activity to start, maintain, and stop it. Recently, brainstem neurons were shown to specifically stop locomotion in mammals. However, the cellular properties of these neurons and their activity during locomotion are still unknown. Here, we took advantage of the lamprey model to characterize the activity of(More)
Alzheimer disease (AD) is initially characterized as a disease of the synapse that affects synaptic transmission and synaptic plasticity. While amyloid-beta and tau have been traditionally implicated in causing AD, recent studies suggest that other factors, such as the intracellular domain of the amyloid-precursor protein (APP-ICD), can also play a role in(More)
Background: Tau phosphorylation affects synaptic transmission, but the underlying mechanism remains elusive. Results: NMDA-receptor activation leads to phosphorylation of endogenous tau, thereby regulating the interaction of tau with Fyn and postsynaptic scaffolding protein PSD95. Conclusions: Phosphorylation of tau controls the interaction of tau with the(More)
BACKGROUND Human studies and mouse models of Alzheimer's disease suggest that the amyloid precursor protein (APP) can cause changes in synaptic plasticity and is contributing to the memory deficits seen in Alzheimer's disease. While most of these studies attribute these changes to the APP cleavage product Aβ, in recent years it became apparent that the APP(More)
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