Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-10-17
pubmed:abstractText
N-Methyl-D-aspartate (NMDA) glutamate receptor properties are subject to a fine tuning by several regulatory mechanisms including phosphorylation of the receptor subunits. Here we show that two of these subunits, NR2B and NR2A, are phosphorylated on tyrosine residues in vivo, in rat striatum, where NR2B is by far the most prominent tyrosine phosphorylated protein. Two weeks after unilateral lesioning of nigrostriatal dopaminergic neurones with 6-hydroxydopamine, tyrosine phosphorylation of NR2B was increased by approximately 20% in the ipsilateral striatum. The total amount of NR2B protein was unaltered. Thus, increased tyrosine phosphorylation of NR2B may account for some of the consequences of dopamine deprivation on corticostriatal transmission and may play a role in some forms of synaptic plasticity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0959-4965
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
125-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Tyrosine phosphorylation of NMDA receptor in rat striatum: effects of 6-OH-dopamine lesions.
pubmed:affiliation
Laboratoire de Neuropharmacologie, INSERM U114, Collège de France, Paris.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't