Marveling at the Incredible ULK4
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Updated: Dec 2, 2025

Fluorescence-based Monitoring of PAD4 Activity via a Pro-fluorescence Substrate Analog
Published on: November 5, 2014
1Department of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool L69 7ZB, UK.
Abstract:
Unc-51-like kinase 4 (ULK4) is a pseudokinase conserved in most eukaryotes, yet ULK4 signaling mechanisms remain enigmatic. In this issue of Structure, Preuss and colleagues report a structure of the ATP-bound ULK4 pseudokinase domain, supported by proteomic analysis of the ULK4 interactome and in-depth evolutionary analysis of the intriguingULK4 pseudokinase domain.
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