Thomas A. Blanpied

ORCID: 0000-0003-4957-557X
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About
Contact & Profiles
Research Areas
  • Neuroscience and Neuropharmacology Research
  • Lipid Membrane Structure and Behavior
  • Cellular transport and secretion
  • Photoreceptor and optogenetics research
  • Advanced Fluorescence Microscopy Techniques
  • Cell Image Analysis Techniques
  • Advanced Electron Microscopy Techniques and Applications
  • Receptor Mechanisms and Signaling
  • Ion channel regulation and function
  • Force Microscopy Techniques and Applications
  • Retinal Development and Disorders
  • Alzheimer's disease research and treatments
  • Protein Structure and Dynamics
  • Protein Kinase Regulation and GTPase Signaling
  • Neuroscience and Neural Engineering
  • Cellular Mechanics and Interactions
  • Diffusion and Search Dynamics
  • Neurogenesis and neuroplasticity mechanisms
  • Genetics and Neurodevelopmental Disorders
  • Neural dynamics and brain function
  • RNA Interference and Gene Delivery
  • Photochromic and Fluorescence Chemistry
  • Bacteriophages and microbial interactions
  • Computational Drug Discovery Methods
  • Neuroinflammation and Neurodegeneration Mechanisms

University of Maryland, Baltimore
2016-2025

Institute of Molecular Medicine
2014

Czech Academy of Sciences, Institute of Physiology
2014

University of Mary
2012

Duke University
1999-2008

Duke University Hospital
1999-2008

Duke Medical Center
1999-2008

University of Pittsburgh
1992-2005

University of Southern California
1992

Formation of mature excitatory synapses requires the assembly and delivery NMDA receptors to neuronal plasma membrane. A key step in trafficking is exit newly assembled from endoplasmic reticulum (ER). Here we report identification an RXR-type ER retention/retrieval motif C-terminal tail receptor subunit NR1 that regulates surface expression heterologous cells neurons. In addition, show PKC phosphorylation alternatively spliced consensus type I PDZ-binding domain suppress retention. These...

10.1523/jneurosci.21-09-03063.2001 article EN cc-by-nc-sa Journal of Neuroscience 2001-05-01

Blanpied, Thomas A., Faye Boeckman, Elias Aizenman, and Jon W. Johnson. Trapping channel block of NMDA-activated responses by amantadine memantine. J. Neurophysiol. 77: 309–323, 1997. We investigated the mechanisms which antiparkinsonian neuroprotective agents memantine inhibit to N-methyl-d-aspartic acid (NMDA). Whole cell recordings were performed using cultured rat cortical neurons or Chinese hamster ovary (CHO) cells expressing NMDA receptors. Both blocked channels binding a site at they...

10.1152/jn.1997.77.1.309 article EN Journal of Neurophysiology 1997-01-01

The channel of NMDA receptors is blocked by a wide variety drugs. receptor blockers include drugs abuse that induce psychotic behavior, such as phencyclidine, and with therapeutic utility, amantadine memantine. We describe here the molecular mechanism inhibition. In contrast to most other described channel-blocking molecules, causes gate close more quickly. Our results confirm binding inhibits current flow through channels but show its main inhibitory action at pharmaceutically relevant...

10.1523/jneurosci.4262-04.2005 article EN cc-by-nc-sa Journal of Neuroscience 2005-03-30

The nanoscale distribution of AMPA receptors is under rapid control by adhesion proteins and helps regulate their activation.

10.1126/sciadv.abf3126 article EN cc-by-nc Science Advances 2021-08-20

A key feature of excitatory synapses is the existence subsynaptic protein nanoclusters (NCs) whose precise alignment across cleft in a transsynaptic nanocolumn influences strength synaptic transmission. However, whether properties vary between functioning different cellular contexts unknown. We used combination confocal and DNA-PAINT super-resolution microscopy to directly compare organization shared scaffold proteins at two important synapses—those forming onto principal neurons (Ex→Ex...

10.1073/pnas.2315379121 article EN Proceedings of the National Academy of Sciences 2024-04-16

Synapsin III is the most recently identified member of synapsin family, a group synaptic vesicle proteins that play essential roles in neurotransmitter release and neurite outgrowth. Here, through generation analysis knock-out mice, we demonstrate regulates manner distinct from I or II. In mice lacking III, size recycling pool vesicles was increased, depression reduced. The number fuse per action potential similar between wild-type there no change quantal content EPSCs; however, IPSCs were...

10.1523/jneurosci.22-11-04372.2002 article EN Journal of Neuroscience 2002-06-01

The size, shape, and molecular arrangement of the postsynaptic density (PSD) determine function excitatory synapses in brain. Here, we directly measured internal dynamics scaffold proteins within single living PSDs, focusing on principal protein PSD-95. We found that individual PSDs undergo rapid, continuous changes morphology driven by actin cytoskeleton regulated synaptic activity. This structural plasticity is accompanied rapid fluctuations over submicron distances. Using targeted...

10.1073/pnas.0711669105 article EN Proceedings of the National Academy of Sciences 2008-08-23
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