Linked Life Data

1397284

Source:http://linkedlifedata.com/resource/pubmed/id/1397284

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-11-20
pubmed:abstractText
The Dsrc28C gene is a unique member of the extensive tyrosine kinase family. Two proteins, p66Dsrc28C and p55Dsrc28C, are encoded by the gene. Each contains a highly conserved tyrosine kinase domain and each lacks the usual amino-terminal myristylation signal. The protein-tyrosine kinase activity of the two proteins was investigated through a recombinant baculovirus expression system. p66Dsrc28C expressed from a recombinant baculovirus phosphorylated a large number of Sf9 cell proteins on tyrosine. A group of proteins of approximately 100 kDa were the preferred substrates. No evidence of p66Dsrc28C autophosphorylation was found. In contrast to p66Dsrc28C, p55Dsrc28C did not exhibit protein-tyrosine kinase activity when expressed from a recombinant baculovirus. A deletion derivative of p66Dsrc28C lacking the SH3 and SH2 domains also failed to phosphorylate Sf9 cell proteins. These results suggest that the protein-tyrosine kinase activity of Dsrc28C proteins is tightly regulated.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
311
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Protein-tyrosine kinase activity of alternate protein products of the Drosophila Dsrc28C locus.
pubmed:affiliation
Cell Biology Group, Worcester Foundation for Experimental Biology, Shrewsbury, MA 01545.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.