Crystal Structure of Glycogen Synthase Kinase 3β: Structural Basis for Phosphate-Primed Substrate Specificity and Autoinhibition
By R. Dajani, Elizabeth Fraser, S. Roe, Neville Young, V. Good, T. Dale, L. Pearl. 2001
668 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/739903858bd0cfdfd25875912d91d941c57cfd2c
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cell Biology
- A. Keith Dunker
- Vladimir N Uversky
- Christopher J. Oldfield
- J. Blenis
- J. Woodgett
- Matthias Mann
- L. Larue
- F. van Roy
In Molecular Biology
- Vladimir N Uversky
- A. Keith Dunker
- Christopher J. Oldfield
- Lukasz Kurgan
- J. Blenis
- Zsuzsanna Dosztányi
- Matthias Mann
- L. Larue
Citations in the corpus
- The Ras-ERK and PI3K-mTOR Pathways: Cross-talk and Compensation (2011, background): “AGC kinases phosphorylate GSK3 α/β on Ser21/Ser9, which creates pseudo-substrate sites that induce intra-molecular inhibition (Figure 3, [8, 41, 59]).”
- The protein kinase Akt induces epithelial mesenchymal transition and promotes enhanced motility and invasiveness of squamous cell carcinoma lines. (2003, background): “The apparent discrepancy can be resolved by recent crystallographic and biochemical studies elucidating the mechanisms of GSK3 regulation (52, 53): Wnt and insulin/AKT signaling pathways affect two distinct pools of GSK3 that in turn target different substrates, thereby giving selective responses an”
- Axin-mediated CKI phosphorylation of beta-catenin at Ser 45: a molecular switch for the Wnt pathway. (2002, background): “This indicates, that contrary to prevailing models (Ali et al. 2001; Cohen and Frame 2001; Dajani et al. 2001; Frame et al. 2001; Harwood, 2001), association with axin does not substitute for the +4p priming of GSK3.”
- Phosphorylation: Implications in Cancer (2017, background): “Protein phosphorylation may occur at multiple sites [11] or at a single site of a protein which is a priming location for subsequent phosphorylation events [12].”