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| pubmed-article:11738041 | lifeskim:mentions | umls-concept:C0105770 | lld:lifeskim |
| pubmed-article:11738041 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:11738041 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:11738041 | lifeskim:mentions | umls-concept:C0244988 | lld:lifeskim |
| pubmed-article:11738041 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:11738041 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11738041 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:11738041 | pubmed:dateCreated | 2001-12-13 | lld:pubmed |
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| pubmed-article:11738041 | pubmed:abstractText | Glycogen synthase kinase-3 (GSK-3) sequentially phosphorylates four serine residues on glycogen synthase (GS), in the sequence SxxxSxxxSxxx-SxxxS(p), by recognizing and phosphorylating the first serine in the sequence motif SxxxS(P) (where S(p) represents a phosphoserine). FRATtide (a peptide derived from a GSK-3 binding protein) binds to GSK-3 and blocks GSK-3 from interacting with Axin. This inhibits the Axin-dependent phosphorylation of beta-catenin by GSK-3. | lld:pubmed |
| pubmed-article:11738041 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11738041 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11738041 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11738041 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:11738041 | pubmed:author | pubmed-author:LewisCC | lld:pubmed |
| pubmed-article:11738041 | pubmed:author | pubmed-author:SmithD GDG | lld:pubmed |
| pubmed-article:11738041 | pubmed:author | pubmed-author:BrownM JMJ | lld:pubmed |
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| pubmed-article:11738041 | pubmed:author | pubmed-author:BridgesAA | lld:pubmed |
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| pubmed-article:11738041 | pubmed:author | pubmed-author:GuoA XAX | lld:pubmed |
| pubmed-article:11738041 | pubmed:author | pubmed-author:PettmanGG | lld:pubmed |
| pubmed-article:11738041 | pubmed:author | pubmed-author:MannixCC | lld:pubmed |
| pubmed-article:11738041 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11738041 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:11738041 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11738041 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11738041 | pubmed:pagination | 1143-52 | lld:pubmed |
| pubmed-article:11738041 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:11738041 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11738041 | pubmed:articleTitle | The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation. | lld:pubmed |
| pubmed-article:11738041 | pubmed:affiliation | Department of Structural Biology, GlaxoSmithKline Pharmaceuticals, Harlow, Essex CM19 5AD, United Kingdom. benjamin_d_bax@gsk.com | lld:pubmed |
| pubmed-article:11738041 | pubmed:publicationType | Journal Article | lld:pubmed |
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