Population
Recombinant protein kinase DYRK1A expressed in Escherichia coli or mammalian cells (COS-7 cells)
Comparison
Mutagenesis vs Wild-type DYRK1A
Design
Preclinical
Authors
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Tyr-321 autophosphorylation is required for DYRK1A activity in vitro; leaves open its validation as a selective target in disease models.
The enzymic activity of DYRK1A is dependent on the autophosphorylation of the conserved Tyr-321 residue in its activation loop.
Himpel et al. (2001) studied this question.
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