ArticleCell reports methods2026
Detecting protein higher-order structural changes using kinase as a phospho-labeler.
Article in Cell reports methods, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
We developed an approach to detect protein structural changes on a proteome-wide scale by phosphate labeling through in vitro kinase reactions. This structural proteomics approach combines residue-specific labeling based on kinase substrate recognition with quantitative phosphoproteomics using phosphopeptide enrichment, enabling site-resolved profiling of structural alterations. Using myoglobin with and without heat denaturation and HEK293T cell extracts with and without protease treatment, we demonstrated that phosphorylation efficiency reflects differences in substrate protein structure. Moreover, by comparing phosphorylation efficiencies before and after RNA digestion, we successfully identified proteome-wide structural changes in non-denatured cell extracts. This approach enables a residue-specific readout of structural dynamics within the intracellular proteome.
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