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The peptide appears to upregulate cell motility and migration by interacting with the cellular cytoskeleton, specifically inhibiting the polymerization of globular actin (G-actin) into filamentous actin (F-actin)

The concept that binding proteins existed for peptide hormones like the IGFs, similar to those for steroid and thyroid hormones, were suggested by studies from Zapf and Froesch (12) and by Hintz (13), demonstrating that NSILA was present in high molecular weight complexes in serum

Recruitment of phosphorylated NPM1 to sites of DNA damage through RNF8-dependent ubiquitin conjugates

IB, inhibitor of kappa B alpha