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  1. Cyclophilin A promotes cell migration via the Abl-Crk signaling pathway
  2. Iterative tyrosine phosphorylation controls non-canonical domain utilization in Crk
  3. Domain organization differences explain Bcr-Abl's preference for CrkL over CrkII
  4. Phosphorylation of Crk on tyrosine 251 in the RT loop of the SH3C domain promotes Abl kinase transactivation
  5. Structural basis for regulation of the Crk signaling protein by a proline switch
  6. Proline cis-trans Isomerization Controls Autoinhibition of a Signaling Protein