The Eph receptors are the largest of the RTK families. Like other RTKs, they transduce
signals from the cell exterior to the interior through ligand-induced activation of their kinase …

Protein tyrosine phosphorylation is a key regulatory process in virtually all aspects of cellular
functions. Dysregulation of protein tyrosine phosphorylation is a major cause of human …

Cancer cells produce high amounts of reactive oxygen species (ROS) and evade apoptosis.
Hydroperoxides support proliferation, invasion, migration and angiogenesis, but at higher …

Protein tyrosine phosphatases (PTPs) are a diverse family of enzymes encoded by 107
genes in the human genome. Together with protein tyrosine kinases (PTKs), PTPs regulate …

Structural analysis of protein tyrosine phosphatases (PTPs) has expanded considerably in
the last several years, producing more than 200 structures in this class of enzymes (from 35 …

Since the mid-1980s, Eph receptors have evolved from being regarded as orphan receptors
with unknown functions and ligands to becoming one of the most complex" global …

The relevance of potentially reversible post-translational modifications required for
controlling cellular processes in cancer is one of the most thriving arenas of cellular and …

Obesity-associated insulin resistance plays a central role in type 2 diabetes. As such,
tyrosine phosphatases that dephosphorylate the insulin receptor (IR) are potential …

The impact of Eph and ephrin signaling on cell behavior is complex and highly context
dependent. Forward signaling initiated by Eph receptor activation and reverse signaling …

Signaling by receptor tyrosine kinases (RTKs) is mediated by their intrinsic kinase activity.
Typically, kinase-activating mutations result in ligand-independent signaling and gain-of …