Activity-dependent shedding of the NMDA receptor glycine binding site by matrix metalloproteinase 3: a PUTATIVE mechanism of postsynaptic plasticity.

Activity-dependent shedding of the NMDA receptor glycine binding site by matrix metalloproteinase 3: a PUTATIVE mechanism of postsynaptic plasticity.

Functional and structural alterations of clustered postsynaptic ligand gated ion channels in neuronal cells are thought to contribute to synaptic plasticity and memory formation in the human brain. Here, we describe a novel molecular mechanism for structural alterations of NR1 subunits of the NMDA r...

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Bibliographic Details
Main Authors: Thorsten Pauly, Miriam Ratliff, Eweline Pietrowski, Rainer Neugebauer, Andrea Schlicksupp, Joachim Kirsch, Jochen Kuhse
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2008-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC2443283?pdf=render

Internet

http://europepmc.org/articles/PMC2443283?pdf=render

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