The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation (Q27636657)

2

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C Lewis

3

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A R Guy

4

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A Bridges

5

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R Tanner

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G Pettman

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C Mannix

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A A Culbert

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M J Brown

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D G Smith

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A D Reith

Glycogen Synthase Kinase-3 from Rabbit Skeletal Muscle

12

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language of work or name

English

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publication date

December 2001

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published in

Structure

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volume

9

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page(s)

1143-52

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issue

12

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Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta-catenin and promotes GSK-3beta-dependent phosphorylation of beta-catenin

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Activation of a novel proto-oncogene, Frat1, contributes to progression of mouse T-cell lymphomas

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A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of axin and beta-catenin

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GSK-3 inhibition by adenoviral FRAT1 overexpression is neuroprotective and induces Tau dephosphorylation and beta-catenin stabilisation without elevation of glycogen synthase activity

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Identifiers

DOI

0 references

Fatcat ID

release_m35mjj6bjnf2fnusz2zdgssjeq

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/m35mjj6bjnf2fnusz2zdgssjeq

24 November 2022