Protein serine/threonine/tyrosine (S/T/Y) phosphorylation is an essential and frequent post-
translational modification in eukaryotes, but historically has been considered less prevalent …

Several mass spectrometry-based assays have emerged for the quantitative profiling of
cellular tyrosine phosphorylation. Ideally, these methods should reveal the exact sites of …

Gaining insight into phosphoproteomes is of the utmost importance for understanding
regulation processes such as signal transduction and cellular differentiation. While the …

Protein tyrosine phosphatases (PTPs) play important, highly dynamic roles in signaling.
Currently about 90 different PTP genes have been described. The enzymes are highly …

Protein phosphorylation on serine, threonine and tyrosine is established as an important
regulatory modification in bacteria. A growing number of studies employing mass …

We present a new strategy for systematic identification of phosphotyrosine (pTyr) by affinity
purification mass spectrometry (AP-MS) using a Src homology 2 (SH2)-domain-derived pTyr …

Revised Manuscript Received January 25, 1993 abstract: Prior methods for the chemical
synthesis of phosphotyrosine-containing peptides involved the incorporation of fully …

Protein phosphorylation on serine, threonine, and tyrosine (Ser/Thr/Tyr) is well established
as a key regulatory posttranslational modification in eukaryotes, but little is known about its …

Tyrosine kinases and SH2 (phosphotyrosine recognition) domains have binding specificities
that depend on the amino acid sequence surrounding the target (phospho) tyrosine residue …

Protein phosphorylation on serine, threonine and tyrosine is recognized as a major tool of
signal transduction in bacteria. However, progress in the field has been hampered by the …