Journal
NATURE CHEMICAL BIOLOGY
Volume 13, Issue 8, Pages 842-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.2406
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Funding
- NIH [R01GM118384]
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Access to phosphoproteins with stoichiometric and site-specific phosphorylation status is key to understanding the role of protein phosphorylation. Here we report an efficient method to generate pure, active phosphotyrosine-containing proteins by genetically encoding a stable phosphotyrosine analog that is convertible to native phosphotyrosine. We demonstrate its general compatibility with proteins of various sizes, phosphotyrosine sites and functions, and reveal a possible role of tyrosine phosphorylation in negative regulation of ubiquitination.
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