@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},
	author = {Mavali-Zadeh, Ahmad and Gatto, Emanuela and Lettieri, Raffaella and Bokharaie, Bokharaie and Caravella, Alice and D{\textquoteright}Ottavi, Cadia and di Bartolomeo, Elisabetta and Domenici, Fabio and Sima, Setareh and Correia, Alexandra and Rauniyar, Khushbu and Klose, Anna and Gounani, Zahra and Laaksonen, Timo and K{\"u}nnapuu, Jaana and Jeltsch, Michael}
}
@article {897,
	title = {Gliflozins, sucrose and flavonoids are allosteric activators of lecithin-cholesterol acyltransferase},
	journal = {Scientific Reports},
	volume = {14},
	year = {2024},
	month = {2024/10/30/},
	pages = {26085},
	abstract = {Abstract            Lecithin-cholesterol acyltransferase (LCAT) serves as a pivotal enzyme in preserving cholesterol homeostasis via reverse cholesterol transport, a process closely associated with the onset of atherosclerosis. Impaired LCAT function can lead to severe LCAT deficiency disorders for which no pharmacological treatment exists. LCAT-based therapies, such as small molecule positive allosteric modulators (PAMs), against LCAT deficiencies and atherosclerosis hold promise, although their efficacy against atherosclerosis remains challenging. Herein we utilized a quantitative in silico metric to predict the activity of novel PAMs and tested their potencies with in vitro enzymatic assays. As predicted, sodium-glucose cotransporter 2 (SGLT2) inhibitors (gliflozins), sucrose and flavonoids activate LCAT. This has intriguing implications for the mechanism of action of gliflozins, which are commonly used in the treatment of type 2 diabetes, and for the endogenous activation of LCAT. Our results underscore the potential of molecular dynamics simulations in rational drug design.},
	isbn = {2045-2322},
	doi = {10.1038/s41598-024-77104-3},
	url = {https://www.nature.com/articles/s41598-024-77104-3},
	author = {Niemel{\"a}, Akseli and Giorgi, Laura and Nouri, Sirine and Yurtta{\c s}, Bet{\"u}l and Rauniyar, Khushbu and Jeltsch, Michael and Koivuniemi, Artturi}
}
@article {860,
	title = {Expansion and collapse of VEGF diversity in major clades of the animal kingdom},
	journal = {Angiogenesis},
	volume = {26},
	year = {2023},
	month = {Jan-08-2023},
	pages = {437 - 461},
	issn = {0969-6970},
	doi = {10.1007/s10456-023-09874-9},
	url = {https://link.springer.com/10.1007/s10456-023-09874-9},
	author = {Rauniyar, Khushbu and Bokharaie, Honey and Jeltsch, Michael}
}
@mastersthesis {863,
	title = {VEGF-C: The evolutionary origin, activation, and potential as a drug target},
	year = {2023},
	month = {2023/06/09/},
	school = {University of Helsinki},
	address = {Helsinki. Finland},
	url = {http://hdl.handle.net/10138/357923},
	author = {Rauniyar, Khushbu}
}
@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 {693,
	title = {KLK3/PSA and cathepsin D activate VEGF-C and VEGF-D},
	journal = {eLife},
	volume = {8},
	year = {2019},
	month = {2019/05/17/},
	pages = {e44478},
	abstract = {Vascular endothelial growth factor-C (VEGF-C) acts primarily on endothelial cells, but also on non-vascular targets, e.g. in the CNS and immune system. Here we describe a novel, unique VEGF-C form in the human reproductive system produced via cleavage by kallikrein-related peptidase 3 (KLK3), aka prostate-specific antigen (PSA). KLK3 activated VEGF-C specifically and efficiently through cleavage at a novel N-terminal site. We detected VEGF-C in seminal plasma, and sperm liquefaction occurred concurrently with VEGF-C activation, which was enhanced by collagen and calcium binding EGF domains 1 (CCBE1). After plasmin and ADAMTS3, KLK3 is the third protease shown to activate VEGF-C. Since differently activated VEGF-Cs are characterized by successively shorter N-terminal helices, we created an even shorter hypothetical form, which showed preferential binding to VEGFR-3. Using mass spectrometric analysis of the isolated VEGF-C-cleaving activity from human saliva, we identified cathepsin D as a protease that can activate VEGF-C as well as VEGF-D.},
	keywords = {cancer biology, Cathepsin D, kallikrein-related peptidases, KLK3/PSA, Lymphangiogenesis, mouse, VEGF-C, VEGF-D},
	isbn = {2050-084X},
	url = {https://elifesciences.org/articles/44478},
	author = {Jha, Sawan K and Rauniyar, Khushbu and Chronowska, Ewa and Mattonet, Kenny and Maina, Eunice W and Koistinen, Hannu and Stenman, Ulf-H{\r a}kan and Alitalo, Kari and Jeltsch, Michael}
}
@article {589,
	title = {Efficient activation of the lymphangiogenic growth factor VEGF-C requires the C-terminal domain of VEGF-C and the N-terminal domain of CCBE1},
	journal = {Scientific Reports},
	volume = {7},
	year = {2017},
	month = {2017/07/07/},
	pages = {4916},
	doi = {10.1038/s41598-017-04982-1},
	url = {https://www.nature.com/articles/s41598-017-04982-1},
	author = {Jha, SK and Rauniyar, Khushbu and K{\"a}rp{\"a}nen, Terhi and Lepp{\"a}nen, Veli-Matti and Brouillard, Pascal and Vikkula, Miikka and Alitalo, Kari and Jeltsch, Michael}
}
