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BACKGROUND 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(More)
The trityl group was recently introduced for the protection of the side chain carboxamide function of asparagine and glutamine. The 4-methyltrityl (Mtt) group, a structural modification of trityl, is presented here and allows more rapid cleavage from the protected peptides. Procedures for the introduction of the group and comparative cleavage reactions are(More)
In embryonic stem cells (ESCs), gene regulatory networks (GRNs) coordinate gene expression to maintain ESC identity; however, the complete repertoire of factors regulating the ESC state is not fully understood. Our previous temporal microarray analysis of ESC commitment identified the E3 ubiquitin ligase protein Makorin-1 (MKRN1) as a potential novel(More)
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