Thomas A. Blanpied

The paper investigates the nano-organization of PTPσ in cultured rat hippocampal neurons, finding it is enriched at excitatory synapses but does not colocalize with Munc13-1 or predict NMDAR abundance.

This study identifies Btbd11 as a regulator of glutamatergic synapse organization in GABAergic inhibitory interneurons, showing its role in phase separation and synaptic nanoarchitecture.

The paper identifies CGRP receptors on OPCs and demonstrates close spatial contacts between CGRP and OPCs, suggesting direct signaling.

The paper uses multi-omics analysis of lysosomes to identify age-related sphingolipid catabolism changes linked to lysosomal dysfunction in the aging brain.

The paper maps the spatial relationships between NMDA receptor subunits and synaptic proteins, revealing a nanotopography that promotes NMDAR activation and synaptic transmission tuning.

This paper uses a modified CRISPR method to replace the entire coding sequence of LRRTM2 in rat neurons, revealing its synaptic distribution and interactions with AMPARs.

This paper develops a high-throughput optical method to analyze glutamatergic synapse function in cultured rat neurons, revealing functional heterogeneity across synaptic boutons.

This study uses super-resolution microscopy to show that SAP102 forms distinct nanoclusters at synapses, differing from PSD-95 in size, density, and co-localization patterns.

The paper compares nanoscale organization of excitatory synapses onto excitatory and inhibitory neurons, finding conserved and cell-specific structural differences.

This study shows that loss of NMDARs leads to changes in pre- and postsynaptic nanocluster organization, affecting synaptic function differently than pharmacological antagonism.

The paper identifies distinct molecular machineries for Ca2+ channel clustering and synaptic vesicle priming at active zones, showing that Liprin- and PTPσ specifically support priming site assembly.

This study shows that LRRTM2 controls AMPAR subsynaptic positioning, which dynamically regulates synaptic strength by affecting receptor clustering near presynaptic release sites.

The paper examines NMDA receptor activation by spontaneous neurotransmission in cultured rat hippocampal neurons, finding that GluN2B-NMDARs are primarily involved and activation varies independently of synapse size but correlates with distance from the soma.

The paper describes analytical methods for quantitatively analyzing the 3D distribution and trans-synaptic alignment of proteins using single-molecule localization microscopy data.