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Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms
Stargazer, an ataxic and epileptic mutant mouse, lacks functional AMPA receptors on cerebellar granule cells, and expression of a mutant stargazin lacking the PDZ-binding domain in hippocampal pyramidal cells disrupts synaptic AMPA receptor receptors, indicating that st argazin-like mechanisms for targeting AM PA receptors may be widespread in the central nervous system. Expand
Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme.
  • D. Bredt, S. Snyder
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences…
  • 1990
It is shown that nitric oxide synthetase activity requires calmodulin, and the native enzyme appears to be a monomer. Expand
PSD-95 involvement in maturation of excitatory synapses.
It is found that overexpression of PSD-95 in hippocampal neurons can drive maturation of glutamatergic synapses and this results demonstrate that PSd-95 can orchestrate synaptic development and are suggestive of roles for PSD -95 in synapse stabilization and plasticity. Expand
Functional studies and distribution define a family of transmembrane AMPA receptor regulatory proteins
A general role for TARPs is indicated in controlling synaptic AMPA receptors throughout the central nervous system. Expand
Direct interactions between PSD-95 and stargazin control synaptic AMPA receptor number
It is shown that AMPARs are localized to synapses through direct binding of the first two PDZ domains of synaptic PSD-95 (postsynaptic density protein of 95 kDa) to the AMPAR-associated protein, stargazin, and the central role of direct interactions between them in determining the number of synaptic AM PARs is demonstrated. Expand
Interaction of Nitric Oxide Synthase with the Postsynaptic Density Protein PSD-95 and α1-Syntrophin Mediated by PDZ Domains
It is shown that the N-terminus of nNOS, which contains a PDZ protein motif, interacts with similar motifs in postsynaptic density-95 protein (PSD-95) and a related novel protein, PSD-93. Expand
Nitric oxide synthase and neuronal NADPH diaphorase are identical in brain and peripheral tissues.
The identity of neuronal NO synthase and NADPH diaphorase suggests a role for NO in modulating neurotoxicity, and is in line with previous work on neuronal messenger molecules. Expand
AMPA Receptor Trafficking at Excitatory Synapses
This work has shown that neuronal activity controls synaptic AMPA receptor trafficking, and this dynamic process plays a key role in the synaptic plasticity that is thought to underlie aspects of learning and memory. Expand
Nitric oxide in skeletal muscle
It is shown that rat skeletal muscle expresses neuronal-type NO synthase and that activity varies among several respiratory and limb muscles, and that two physiological functions of NO in skeletal muscle are supported. Expand
Localization of nitric oxide synthase indicating a neural role for nitric oxide
It is demonstrated that NO synthase in the brain to be exclusively associated with discrete neuronal populations, and prominent neural localizations provided the first conclusive evidence for a strong association of NO with neurons. Expand