The Structure of Phosphorylated GSK-3β Complexed with a Peptide, FRATtide, that Inhibits β-Catenin Phosphorylation
By B. Bax, P. Carter, C. Lewis, A. R. Guy, A. Bridges, R. Tanner, G. Pettman, C. Mannix, A. Culbert, Murray J. B. Brown and 2 more. 2001
189 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/6671b188eaa901701189769fe14480ea2a4c99d5
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In Cell Biology
- A. Keith Dunker
- Vladimir N Uversky
- Christopher J. Oldfield
- J. Woodgett
- J. Diehl
- Matthias Mann
- B. Doble
- Peter Tompa
In Molecular Biology
- Vladimir N Uversky
- A. Keith Dunker
- Christopher J. Oldfield
- Lukasz Kurgan
- Zsuzsanna Dosztányi
- Matthias Mann
- Jens S. Andersen
- B. Doble
Citations in the corpus
- Axin-mediated CKI phosphorylation of beta-catenin at Ser 45: a molecular switch for the Wnt pathway. (2002, background): “According to a prevailing model, it involves FRAT (GBP), a GSK-3 -binding protein that displaces axin from GSK-3 , resulting in failure to phosphorylate -catenin (Li et al. 1999; Farr et al. 2000; Bax et al. 2001; Fraser et al. 2001).”
- Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling (2005, background): “However, it is induced to accommodate one of the two completely distinct and wellordered structures that are specific to the individual ligand bound (Bax et al., 2001; Dajani et al., 2003): while some residues in this versatile binding site in GSK3 are involved in interactions with both axin and…”
- Phosphorylation-Dependent Ubiquitination of Cyclin D1 by the SCFFBX4-αB Crystallin Complex (2006, background): “1, a region deleted in human cancer (Bax et al., 2001; Dohner et al., 1999).”
- Glycogen and its metabolism: some new developments and old themes. (2012, background): “Several studies, however, argue against GSK3β being a substrate for laforin [36,37,191,250,265].”
- GSK-3: tricks of the trade for a multi-tasking kinase (2003, background): “Comparison of mutations that affect binding of GSK-3 to axin and GBP, as well as analysis of the crystal structure of a GSK-3-FRAT-tide complex, indicates that the binding sites on GSK-3 for GBP/FRAT and axin overlap (Bax et al., 2001; Ferkey and Kimelman, 2002; Fraser et al., 2002).”