| pubmed-article:10026255 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10026255 | lifeskim:mentions | umls-concept:C0290068 | lld:lifeskim |
| pubmed-article:10026255 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:10026255 | lifeskim:mentions | umls-concept:C0086982 | lld:lifeskim |
| pubmed-article:10026255 | lifeskim:mentions | umls-concept:C0872252 | lld:lifeskim |
| pubmed-article:10026255 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:10026255 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:10026255 | pubmed:dateCreated | 1999-3-4 | lld:pubmed |
| pubmed-article:10026255 | pubmed:abstractText | We report efficient methods for using functional proteomics to study signal transduction pathways in mouse fibroblasts following stimulation with PDGF. After stimulation, complete cellular proteins were separated using two-dimensional electrophoresis and phosphorylated proteins were detected with anti-phosphotyrosine and anti-phosphoserine antibodies. About 260 and 300 phosphorylated proteins were detected with the anti-phosphotyrosine and anti-phosphoserine antibodies, respectively, at least 100 of which showed prominent changes in phosphorylation as a function of time after stimulation. Proteins showing major time-dependent changes in phosphorylation were subjected to in-gel digestion with trypsin and identified by mass spectroscopy using MALDI-TOF mass fingerprinting and ESI peptide sequencing. We have observed phosphorylated proteins known to be part of the PDGF signal transduction pathway such as ERK 1, serine/threonine protein kinase akt and protein tyrosine phosphatase syp, proteins such as proto-oncogene tyrosine kinase fgr previously known to participate in other signal transduction pathways, and some proteins such as plexin-like protein with no previously known function in signal transduction. Information about the phosphorylation site was obtained for proto-oncogene tyrosine kinase fgr and for cardiac alpha-actin. The methods used here have proven to be suitable for the identification of time-dependent changes in large numbers of proteins involved in signal transduction pathways. | lld:pubmed |
| pubmed-article:10026255 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10026255 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10026255 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10026255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10026255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10026255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10026255 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10026255 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10026255 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:10026255 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:10026255 | pubmed:author | pubmed-author:GörlachMM | lld:pubmed |
| pubmed-article:10026255 | pubmed:author | pubmed-author:BoehmerF DFD | lld:pubmed |
| pubmed-article:10026255 | pubmed:author | pubmed-author:Godovac-Zimme... | lld:pubmed |
| pubmed-article:10026255 | pubmed:author | pubmed-author:PoznanovicSS | lld:pubmed |
| pubmed-article:10026255 | pubmed:author | pubmed-author:SoskicVV | lld:pubmed |
| pubmed-article:10026255 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10026255 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:10026255 | pubmed:volume | 38 | lld:pubmed |
| pubmed-article:10026255 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10026255 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10026255 | pubmed:pagination | 1757-64 | lld:pubmed |
| pubmed-article:10026255 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:10026255 | pubmed:meshHeading | pubmed-meshheading:10026255... | lld:pubmed |
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| pubmed-article:10026255 | pubmed:meshHeading | pubmed-meshheading:10026255... | lld:pubmed |
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| pubmed-article:10026255 | pubmed:meshHeading | pubmed-meshheading:10026255... | lld:pubmed |
| pubmed-article:10026255 | pubmed:meshHeading | pubmed-meshheading:10026255... | lld:pubmed |
| pubmed-article:10026255 | pubmed:meshHeading | pubmed-meshheading:10026255... | lld:pubmed |
| pubmed-article:10026255 | pubmed:meshHeading | pubmed-meshheading:10026255... | lld:pubmed |
| pubmed-article:10026255 | pubmed:meshHeading | pubmed-meshheading:10026255... | lld:pubmed |
| pubmed-article:10026255 | pubmed:meshHeading | pubmed-meshheading:10026255... | lld:pubmed |
| pubmed-article:10026255 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10026255 | pubmed:articleTitle | Functional proteomics analysis of signal transduction pathways of the platelet-derived growth factor beta receptor. | lld:pubmed |
| pubmed-article:10026255 | pubmed:affiliation | Institute for Molecular Biotechnology, Jena, Germany. | lld:pubmed |
| pubmed-article:10026255 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10026255 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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