Eph receptors, the largest subfamily of receptor tyrosine kinases, are linked with proliferative
disease, such as cancer, as a result of their deregulated expression or mutation. Unlike …

The assembly of complexes following the detection of extracellular signals is often controlled
by signaling proteins comprising multiple peptide binding modules. The SRC homology …

Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays
a crucial role in cell proliferation and differentiation. Its receptor EGFR has been extensively …

Protein–protein interactions (PPIs) between modular binding domains and their target
peptide motifs are thought to largely depend on the intrinsic binding specificities of the …

EPH receptors (EPHRs) constitute the largest family among receptor tyrosine kinases in
humans. They are mainly involved in short-range cell-cell communication events that …

Reversible phosphorylation is a fundamental mechanism for controlling protein function.
Despite the critical roles phosphorylated proteins play in physiology and disease, our ability …

The non-catalytic region of tyrosine kinase (Nck) family of adaptors, consisting of Nck1 and
Nck2, contributes to selectivity and specificity in the flow of cellular information by recruiting …

Abstract Phosphoglycerate mutase 1 (PGAM1) is a key node enzyme that diverts the
metabolic reactions from glycolysis into its shunts to support macromolecule biosynthesis for …

The Nck family of modular adaptor proteins, including Nck1 and Nck2, link phosphotyrosine
signaling to changes in cytoskeletal dynamics and gene expression that critically modulate …

The Eph receptor tyrosine kinases and their ephrin ligands regulate many physiological and
pathological processes. EphA4 plays important roles in nervous system development and …