| pubmed-article:8663994 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8663994 | lifeskim:mentions | umls-concept:C0072899 | lld:lifeskim |
| pubmed-article:8663994 | lifeskim:mentions | umls-concept:C1415287 | lld:lifeskim |
| pubmed-article:8663994 | lifeskim:mentions | umls-concept:C1519063 | lld:lifeskim |
| pubmed-article:8663994 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:8663994 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8663994 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:8663994 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:8663994 | pubmed:dateCreated | 1996-8-2 | lld:pubmed |
| pubmed-article:8663994 | pubmed:abstractText | We have characterized the phosphorylation of the glutamate receptor subunit GluR1, using biochemical and electrophysiological techniques. GluR1 is phosphorylated on multiple sites that are all located on the C-terminus of the protein. Cyclic AMP-dependent protein kinase specifically phosphorylates SER-845 of GluR1 in transfected HEK cells and in neurons in culture. Phosphorylation of this residue results in a 40% potentiation of the peak current through GluR1 homomeric channels. In addition, protein kinase C specifically phosphorylates Ser-831 of GluR1 in HEK-293 cells and in cultured neurons. These results are consistent with the recently proposed transmembrane topology models of glutamate receptors, in which the C-terminus is intracellular. In addition, the modulation of GluR1 by PKA phosphorylation of Ser-845 suggests that phosphorylation of this residue may underlie the PKA-induced potentiation of AMPA receptors in neurons. | lld:pubmed |
| pubmed-article:8663994 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8663994 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8663994 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8663994 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8663994 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8663994 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8663994 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8663994 | pubmed:issn | 0896-6273 | lld:pubmed |
| pubmed-article:8663994 | pubmed:author | pubmed-author:BernhardtJJ | lld:pubmed |
| pubmed-article:8663994 | pubmed:author | pubmed-author:O'BrienR JRJ | lld:pubmed |
| pubmed-article:8663994 | pubmed:author | pubmed-author:HuganirR LRL | lld:pubmed |
| pubmed-article:8663994 | pubmed:author | pubmed-author:MammenA LAL | lld:pubmed |
| pubmed-article:8663994 | pubmed:author | pubmed-author:RocheK WKW | lld:pubmed |
| pubmed-article:8663994 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8663994 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:8663994 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8663994 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8663994 | pubmed:pagination | 1179-88 | lld:pubmed |
| pubmed-article:8663994 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8663994 | pubmed:meshHeading | pubmed-meshheading:8663994-... | lld:pubmed |
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| pubmed-article:8663994 | pubmed:meshHeading | pubmed-meshheading:8663994-... | lld:pubmed |
| pubmed-article:8663994 | pubmed:meshHeading | pubmed-meshheading:8663994-... | lld:pubmed |
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| pubmed-article:8663994 | pubmed:meshHeading | pubmed-meshheading:8663994-... | lld:pubmed |
| pubmed-article:8663994 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8663994 | pubmed:articleTitle | Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit. | lld:pubmed |
| pubmed-article:8663994 | pubmed:affiliation | Department of Neuroscience, Howard Hughes Medical Institute, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. | lld:pubmed |
| pubmed-article:8663994 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8663994 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8663994 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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