Synthetic phosphorylation of p38α recapitulates protein kinase activity.

Through a "tag-and-modify" protein chemical modification strategy, we site-selectively phosphorylated the activation loop of protein kinase p38α. Phosphorylation at natural (180) and unnatural (172) sites created two pure phospho-forms. p38α bearing only a single phosphocysteine (pCys) as...

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Bibliographic Details
Main Authors: Chooi, K, Galan, SR, Raj, R, Mccullagh, J, Mohammed, S, Jones, L, Davis, B
Format: Journal article
Language:English
Published: 2014