Seger, R <br/><br/>
Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation.  [electronic resource] 

 -  Proceedings of the National Academy of Sciences of the United States of America  Jul 1991 
 - 6142-6 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0027-8424 
<br/><br/><label>Standard No.: </label>10.1073/pnas.88.14.6142  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Animals<br/>Calcium-Calmodulin-Dependent Protein Kinases<br/>Cattle<br/>Enzyme Activation<br/>Insulin--pharmacology<br/>Kinetics<br/>Mitogen-Activated Protein Kinase 1<br/>Mitogen-Activated Protein Kinase 3<br/>Mitogen-Activated Protein Kinases<br/>Molecular Sequence Data<br/>Phosphoproteins--isolation & purification<br/>Phosphorylation<br/>Phosphoserine--analysis<br/>Phosphotyrosine<br/>Protein Kinases--genetics<br/>Recombinant Proteins--metabolism<br/>Sequence Homology, Nucleic Acid<br/>Tyrosine--analogs & derivatives