Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A.
By Xianjun Fang, S. Yu, Yiling Lu, R. Bast, J. Woodgett, G. Mills. Proceedings of the National Academy of Sciences of the United States of America, 2000
846 citations recorded by the source corpus.
Subfields: Genetics, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/12cf34f5b9b76c8782e3a7c35e5c443146814e45
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Citations in the corpus
- The Ras-ERK and PI3K-mTOR Pathways: Cross-talk and Compensation (2011, background): “PKA, which is activated by cAMP, can also phosphorylate these sites [62].”
- Glucagon-like peptide 1 (GLP-1) (2019, background): “PKA has been demonstrated to inhibit GSK-3beta [134,135], indicating that the CREindependent PKA stimulation of the Gcg promoter might be mediated via negative regulation of the Wnt pathway [132,133].”
- GSK-3: tricks of the trade for a multi-tasking kinase (2003, background): “Although GSK-3 phosphorylation of the mammalian homologues of Ci has yet to be reported, all contain multiple GSK-3 consensus sites next to PKA sites (Ruis i Altaba, 1999; Jia et al., 2002).”
- Genetic interaction of PGE2 and Wnt signaling regulates developmental specification of stem cells and regeneration (2009, neutral): “, 2005), and destruction complex assembly can be blocked by phosphorylation of GSK3b at S9 (Fang et al., 2000).”