Serine-threonine kinases are enzymes that catalyze the transfer of phosphate groups from ATP to serine or threonine residues on target proteins, thereby regulating numerous cellular processes including signal transduction, cell growth, and immune responses. Research published in International Physiology Journal has …
Serine-threonine kinases are enzymes that catalyze the transfer of phosphate groups from ATP to serine or threonine residues on target proteins, thereby regulating numerous cellular processes including signal transduction, cell growth, and immune responses. Research published in International Physiology Journal has examined these kinases across diverse biological contexts, from parasitology to cancer biology. One investigation employed shotgun label-free proteomic methods to characterize the oyster parasite Perkinsus marinus, identifying serine-threonine kinases among the molecular components of this pathogen. Another study explored somatic mutations in interferon-gamma signaling molecules in human uterine leiomyosarcoma, examining how alterations in kinase-related pathways may contribute to tumor development. Additional work has investigated the regulatory role of FIP-2, also known as optineurin, in controlling chemokine expression and kinase activity, highlighting the interconnected nature of these signaling networks. These studies collectively demonstrate the importance of serine-threonine kinases in understanding host-pathogen interactions, cancer pathogenesis, and inflammatory signaling, underscoring their relevance as both fundamental regulators of cellular physiology and potential targets for therapeutic intervention across multiple disease contexts.
3 peer-reviewed articles, ranked by relevance. Each links to its DOI.
The 3 articles above have been cited 12 times in the scholarly literature. Citation data via OpenAlex and Crossref, updated Jun 2026.
A sample of recent works citing this journal's research on Serine-threonine Kinases, linking to each citing work.