Cell
ArticleThe crystal structure and biological function of leukemia inhibitory factor: Implications for receptor binding
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Cited by (202)
The emerging role of leukemia inhibitory factor in cancer and therapy
2021, Pharmacology and TherapeuticsLeukemia inhibitory factor: Recent advances and implications in biotechnology
2020, Cytokine and Growth Factor ReviewsCitation Excerpt :This phosphorylation process results in the activation of several signaling pathways (Fig. 1), namely: (i) phosphorylation of signal transducers, STAT, that homodimerize and translocate to the nucleus, binding to DNA; (ii) activation of phosphoinositide-3-Kinase (PI3K) pathway; and (iii) mitogen-activated protein kinase kinase / extracellular signal-regulated kinase (MEK/ERK) pathway. Regarding its structure and phylogeny, LIF is characterized by a four α-helix bundle topology stabilized by three disulfide bridges, highly conserved between mouse and humans [19,20]. This conserved topology is important for the known cross-reactivity of human and murine LIFs – human LIF is active in both human and murine LIFRs, although murine LIF is only capable of eliciting the receptor of the same species [21,22].
The AB loop of oncostatin M (OSM) determines species-specific signaling in humans and mice
2018, Journal of Biological Chemistry