Reversible phosphorylation of tyrosine residues in proteins is involved in regulating
numerous cellular events, such as cell growth, cell differentiation, cell-cycle regulation …

The role of Asp128 in the catalytic mechanism of the low M r protein-tyrosine phosphatase
(PTPase) from the fission yeast Schizosaccharomyces pombe has been investigated by a …

It is a great honour to give the Eighteenth Hopkins Memorial Lecture, and to join the
distinguished list of past recipients of this medal. In particular, it gives me much pleasure to …

Catalysis by protein-tyrosine phosphatase 1B (PTP1B) occurs through a two-step
mechanism involving a phosphocysteine intermediate. We have solved crystal structures for …

Protein tyrosine phosphatases (PTPs) are a large family of enzymes that catalyze the
hydrolytic removal of the phosphoryl group from phosphotyrosyl (pY) proteins. To date, the in …

Phosphorylation of proteins on tyrosine (Tyr) residues evolved in metazoan organisms as a
mechanism of coordinating tissue growth. Multicellular eukaryotes typically have more than …

Protein tyrosine phosphatases (PTPs) are involved in the regulation of many aspects of
cellular activity including proliferation, differentiation, metabolism, migration, and survival …

Reversible protein phosphorylation is a major mechanism in the regulation of fundamental
signalling events in all living organisms. Bacteria have been shown to possess a versatile …

Dynamic tyrosine phosphorylation is fundamental to a myriad of cellular processes.
However, the inherently low abundance of tyrosine phosphorylation in the proteome and the …

We have successfully designed and synthesized two fluorescently-labeled, activity-based
probes, Probe1 and Probe2, which were shown to label protein tyrosine phosphatases …