Role for Slimb in the degradation of Drosophila Period protein phosphorylated by Doubletime

@article{Ko2002RoleFS,
  title={Role for Slimb in the degradation of Drosophila Period protein phosphorylated by Doubletime},
  author={H. Ko and J. Jiang and I. Edery},
  journal={Nature},
  year={2002},
  volume={420},
  pages={673-678}
}
Protein phosphorylation has a key role in modulating the stabilities of circadian clock proteins in a manner specific to the time of day. A conserved feature of animal clocks is that Period (Per) proteins undergo daily rhythms in phosphorylation and levels, events that are crucial for normal clock progression. Casein kinase Iε (CKIε) has a prominent role in regulating the phosphorylation and abundance of Per proteins in animals. This was first shown in Drosophila with the characterization of… Expand
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References

SHOWING 1-10 OF 32 REFERENCES
CASEIN KINASE I: ANOTHER COG IN THE CIRCADIAN CLOCKWORKS
  • 83
Temporal phosphorylation of the Drosophila period protein.
  • 437
  • PDF
...
1
2
3
4
...