Ontology highlight
ABSTRACT:
SUBMITTER: Hoppmann C
PROVIDER: S-EPMC5577362 | biostudies-literature | 2017 Aug
REPOSITORIES: biostudies-literature
Hoppmann Christian C Wong Allison A Yang Bing B Li Shuwei S Hunter Tony T Shokat Kevan M KM Wang Lei L
Nature chemical biology 20170612 8
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 phos ...[more]