@article {893,
	title = {Biomass-derived Lignin Nanoparticles for the Sustained Delivery of Vascular Endothelial Growth Factor-C},
	journal = {Molecular Pharmaceutics},
	year = {Submitted},
	chapter = {submitted/preprint},
	doi = {10.1101/2025.04.23.649697},
	url = {https://doi.org/10.1101/2025.04.23.649697}
}
@article {861,
	title = {Bioactive VEGF-C from E. coli},
	journal = {Scientific Reports},
	volume = {12},
	year = {2022},
	month = {Jan-12-2022},
	doi = {10.1038/s41598-022-22960-0},
	url = {https://www.nature.com/articles/s41598-022-22960-0},
	author = {Rauniyar, Khushbu and Akhondzadeh, Soheila and G{\k a}ciarz, Anna and K{\"u}nnapuu, Jaana and Jeltsch, Michael}
}
@article {426,
	title = {The basis for the distinct biological activities of vascular endothelial growth factor receptor-1 ligands},
	journal = {Sci Signal},
	volume = {6},
	year = {2013},
	month = {2013},
	pages = {ra52},
	abstract = {<p>Vascular endothelial growth factors (VEGFs) regulate blood and lymphatic vessel development through VEGF receptors (VEGFRs). The VEGFR immunoglobulin homology domain 2 (D2) is critical for ligand binding, and D3 provides additional interaction sites. VEGF-B and placenta growth factor (PlGF) bind to VEGFR-1 with high affinity, but only PlGF is angiogenic in most tissues. We show that VEGF-B, unlike other VEGFs, did not require D3 interactions for high-affinity binding. VEGF-B with a PlGF-derived L1 loop (B-L1(P)) stimulated VEGFR-1 activity, whereas PlGF with a VEGF-B-derived L1 loop (P-L1(B)) did not. Unlike P-L1(B) and VEGF-B, B-L1(P) and PlGF were also angiogenic in mouse skeletal muscle. Furthermore, B-L1(P) also bound to VEGFR-2 and activated downstream signaling. These results establish a role for L1-mediated D3 interactions in VEGFR activation in endothelial cells and indicate that VEGF-B is a high-affinity VEGFR-1 ligand that, unlike PlGF, cannot efficiently induce signaling downstream of VEGFR-1.</p>},
	issn = {1937-9145},
	doi = {10.1126/scisignal.2003905}
}
