Linked Life Data

3033168

Source:http://linkedlifedata.com/resource/pubmed/id/3033168

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1987-6-25
pubmed:abstractText
NGF treatment of PC12 cells caused a rapid increase in the state of phosphorylation of synapsin I. This phosphorylation of synapsin I is accompanied by a decrease in its electrophoretic mobility on SDS-PAGE. Phosphopeptide fingerprint analysis of the synapsin I revealed that this phosphorylation occurred on a particular phosphopeptide, designated peptide N. Phosphoserine was the only phosphoamino acid detected in peptide N. Partially purified PC12 synapsin I was a substrate for several protein kinases known to be capable of phosphorylating brain synapsin I, but none of these kinases phosphorylated synapsin I on peptide N. The results suggest that the NGF-stimulated phosphorylation of synapsin I may be mediated by a novel protein kinase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0270-6474
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1300-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Synapsin I in PC12 cells. II. Evidence for regulation by NGF of phosphorylation at a novel site.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't