tyrosine phosphatase

His research is mainly focused on studying the function and regulation of protein tyrosine phosphatases.

Links to all 107 members of the protein tyrosine phosphatase family can be found in the template at the bottom of this article.

This gene encodes a protein tyrosine phosphatase which is expressed primarily in lymphoid tissues.

Dual-specificity phosphatases are considered a sub-class of protein tyrosine phosphatases.

In kidney cells, the bradykinin receptor B2 has been shown to interact directly with a protein tyrosine phosphatase.

It has the capability to inhibit protein tyrosine phosphatase 1B, a key metabolite involved in insulin signaling.

PTPmu tyrosine phosphatase activity is activated by shear stress.

Receptor tyrosine phosphatase is a type of Enzyme-linked receptor.

CD45 - The transmembrane tail of which functions as a Tyrosine phosphatase)

Most tyrosine kinases have an associated protein tyrosine phosphatase, which removes the phosphate group.

A large number of protein tyrosine phosphatases have been identified, which fall into the broad categories of cytoplasmic and receptor-like molecules.

The VO ion binds reversibly to the active sites of most protein tyrosine phosphatases.

Unlike most of the protein tyrosine phosphatases, this protein preferentially dephosphorylates phosphoinositide substrates.

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family.

Members of the protein tyrosine phosphatase superfamily cooperate with protein kinases to regulate cell proliferation and differentiation.

PTPLAD2 is a protein tyrosine phosphatase.

PTPN11: protein tyrosine phosphatase, non-receptor type 11 (Noonan syndrome 1)

In addition, signaling can be terminated by dephosphorylation of the tyrosine residues by tyrosine phosphatases.

Protein tyrosine phosphatases remove phosphates from cytokine receptors and activated STATs.

It has been shown that new protein tyrosine phosphatase (PTP) activity for EPPase.

Protein tyrosine phosphatases are protein enzymes that remove phosphate moieties from tyrosine residues on other proteins.

Protein tyrosine phosphatase 1B (PTP1B)

It contains a tensin-like domain as well as a catalytic domain similar to that of the dual specificity protein tyrosine phosphatases.

Schally and colleagues have proposed that the growth inhibitory effect of somatostatin and its long acting analogues may by via a tyrosine phosphatase receptor.

The enzyme that deactivates or phosphorylates the insulin-stimulated tyrosine is called tyrosine phosphatases (PTPases).