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    1. Neuroscience

    Long-term potentiation is independent of the C-tail of the GluA1 AMPA receptor subunit

    Javier Díaz-Alonso et al.
    Despite being the key element of the classic model for excitatory synaptic plasticity, the cytoplasmic AMPA receptor C-tail is not required for hippocampal LTP.
    1. Neuroscience

    Recurrent processes support a cascade of hierarchical decisions

    Laura Gwilliams, Jean-Remi King
    The dynamics of neural responses during visual perception are best explained by a joint feedforward and recurrent architecture, which both maintains and broadcasts input features over time.
    1. Neuroscience

    Post-tetanic potentiation lowers the energy barrier for synaptic vesicle fusion independently of Synaptotagmin-1

    Vincent Huson et al.
    Modulation of the energy barrier for membrane fusion is a common mechanism by which sensors in the synapse produce supralinear calcium dependence of vesicle release and short-term synaptic potentiation.
    1. Cell Biology

    WDR90 is a centriolar microtubule wall protein important for centriole architecture integrity

    Emmanuelle Steib et al.
    Centriole integrity is ensured by the connection between the inner scaffold and microtubule triplets through POC16/WDR90 proteins.
    1. Neuroscience

    Ultra-high-field imaging reveals increased whole brain connectivity underpins cognitive strategies that attenuate pain

    Enrico Schulz et al.
    A single-trial whole-brain analysis of three cognitive strategies to attenuate pain shows that a more effective pain attenuation is associated with increased functional connectivity across the entire brain.
    1. Neuroscience
    2. Structural Biology and Molecular Biophysics

    Ca2+-dependent release of synaptotagmin-1 from the SNARE complex on phosphatidylinositol 4,5-bisphosphate-containing membranes

    Rashmi Voleti et al.
    Ca2+-free synaptotagmin-1 binds to neuronal SNARE complexes anchored on nanodiscs, and Ca2+ releases this interaction to induce tight, specific binding to PIP2-containing membranes.