Two‐dimensional electrophoretic analysis of mixed lineage kinase 2 N‐terminal domain binding proteins

@article{Rasmussen1998TwodimensionalEA,
  title={Two‐dimensional electrophoretic analysis of mixed lineage kinase 2 N‐terminal domain binding proteins},
  author={Richele K. Rasmussen and Hong Ji and James Eddes and Robert L. Moritz and Gavin E. Reid and Richard J. Simpson and Donna S. Dorow},
  journal={ELECTROPHORESIS},
  year={1998},
  volume={19}
}
The mixed lineage kinase 2 (MLK2) protein contains several structurally distinct domains including an src homology (SH) 3 domain, a kinase catalytic domain, two leucine zippers, a basic motif and a cdc42/rac interactive binding motif. These domains have been recognized mainly for their involvement in protein‐protein interactions in signal transduction networks. The SH3 domain in particular has been implicated in control of signaling events. To identify proteins that interact with MLK2, the N… 
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