Tyrosine phosphorylation is a common protein post-translational modification that plays a
critical role in signal transduction and the regulation of many cellular processes. Using a …

Protein phosphorylation is one of the most important post‐translational modifications in
nature. However, the site‐specific incorporation of O‐phosphotyrosine into proteins in vivo …

p-Carboxymethyl-l-phenylalanine (p CMF), a phosphotyrosine (pTyr) mimetic that is resistant
to protein tyrosine phosphatase hydrolysis, was cotranslationally incorporated into proteins …

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 …

Phosphorylation events modify bacterial and archaeal proteomes, imparting cells with rapid
and reversible responses to specific environmental stimuli or niches. Phosphorylated …

Tyrosine phosphorylation is a key device in numerous cellular functions in eukaryotes, but in
bacteria this protein modification was largely ignored until the mid-1990s. The first …

Serine phosphorylation is a key post-translational modification that regulates diverse
biological processes. Powerful analytical methods have identified thousands of …

Protein phosphorylation on tyrosine has been demonstrated to occur in a wide array of
bacterial species and appears to be ubiquitous among prokaryotes. This covalent …

Adding nonstandard amino acids to the genetic code of E. coli expands the chemical and
biological functional space for proteins. This is accomplished with engineered, orthogonal …

The phosphorylation of threonine residues in proteins regulates diverse processes in
eukaryotic cells, and thousands of threonine phosphorylations have been identified. An …