Robinson, C J <br/><br/>
Inactivation of JNK activity by mitogen-activated protein kinase phosphatase-2 in EAhy926 endothelial cells is dependent upon agonist-specific JNK translocation to the nucleus.  [electronic resource] 

 -  Cellular signalling  Jan 2001 
 - 29-41 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>0898-6568 
<br/><br/><label>Standard No.: </label>10.1016/s0898-6568(00)00121-2  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Antibodies, Anti-Idiotypic--immunology<br/>Cell Nucleus--enzymology<br/>Dual-Specificity Phosphatases<br/>Endothelium--cytology<br/>Humans<br/>Hydrogen Peroxide--agonists<br/>JNK Mitogen-Activated Protein Kinases<br/>Mitogen-Activated Protein Kinase Phosphatases<br/>Mitogen-Activated Protein Kinases--chemistry<br/>Phosphorylation<br/>Protein Phosphatase 2<br/>Protein Transport--physiology<br/>Protein Tyrosine Phosphatases--metabolism<br/>Substrate Specificity<br/>Tumor Necrosis Factor-alpha--agonists<br/>p38 Mitogen-Activated Protein Kinases