Linked Life Data

20222723

Source:http://linkedlifedata.com/resource/pubmed/id/20222723

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2010-5-7
pubmed:abstractText
We have used stable isotope labeling by amino acids in cell culture (SILAC), in combination with high-resolution mass spectrometry, to identify common and discrete components of the respective receptor tyrosine kinase-dependent phosphotyrosine-associated networks induced by acute stimulation of A549 lung adenocarcinoma cells with EGF or HGF. In total, we obtained quantitative information for 274 proteins, which respond to either or both stimuli by >1.5 fold changes in enrichment, following immuno-precipitation with antiphosphotyrosine antibodies. The data reveal a high degree of overlap between the respective signaling networks but also clear points of departure. A small number of HGF specific effectors were identified including myosin-X, galectin-1, ELMO2 and EphrinB1, while a larger set of EGF specific effectors (39 proteins) includes both novel (e.g., MAP4K3) and established components of receptor tyrosine kinase receptor signaling pathways. Using available protein-interaction data the identified proteins have been assembled into a highly connected network that can be visualized using the Cytoscape tool.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1535-3907
pubmed:author
pubmed:issnType
Electronic
pubmed:day
7
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2734-42
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Quantitative analysis of HGF and EGF-dependent phosphotyrosine signaling networks.
pubmed:affiliation
Physiological Laboratory, School of Biomedical Sciences, University of Liverpool, Crown Street, Liverpool, L69 3BX, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't