protein tyrosine

Protein tyrosine kinase plays a role in this task, too.

Also very common among protein tyrosine kinases are two peptide sequences.

Protein tyrosine kinases, have a major role in the activation of lymphocytes.

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

Additional instances of factor-influenced protein tyrosine kinase activity, similar to this one, exist.

As a consequence, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions.

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

Protein tyrosine phosphorylation of capillary endothelial cells plays an important role in their proliferation.

The second target gene, protein tyrosine phosphatase-1B (Ptp1b) is involved in the induction of apoptosis.

The balance between protein tyrosine kinase and phosphatase activity is an integral part of this regulatory mechanism.

It is a member of protein tyrosine phosphatise (PTP) family.

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.

Emodin, a protein tyrosine kinase inhibitor from Polygonum cuspidatum.

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

Much research has already noted the significant effect that inhibitors of the radically functioning protein tyrosine kinase enzymes have on related ailments.

In the absence of cytokine, JAKs lack protein tyrosine kinase activity.

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.