Boerner, R J <br/><br/>
Correlation of the phosphorylation states of pp60c-src with tyrosine kinase activity: the intramolecular pY530-SH2 complex retains significant activity if Y419 is phosphorylated.  [electronic resource] 

 -  Biochemistry  Jul 1996 
 - 9519-25 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi960248u  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Triphosphate--metabolism<br/>Amino Acid Sequence<br/>Chromatography, Affinity<br/>Chromatography, Gel<br/>Electrophoresis, Polyacrylamide Gel<br/>Kinetics<br/>Mass Spectrometry<br/>Molecular Sequence Data<br/>Phosphopeptides--chemistry<br/>Phosphorylation<br/>Protein-Tyrosine Kinases--metabolism<br/>Proto-Oncogene Proteins pp60(c-src)--metabolism<br/>Recombinant Proteins--metabolism<br/>Spectrophotometry<br/>Trypsin--metabolism<br/>Tyrosine--metabolism<br/>src Homology Domains