@article {19,
	title = {Current biology of VEGF-B and VEGF-C},
	journal = {Curr Opin Biotechnol},
	volume = {10},
	year = {1999},
	month = {1999/Dec/},
	pages = {528 - 35},
	abstract = {Endothelial growth factors and their receptors may provide important therapeutic tools for the treatment of pathological conditions characterised by defective or aberrant angiogenesis. Vascular endothelial growth factor (VEGF) is pivotal for vasculogenesis and for angiogenesis in normal and pathological conditions. VEGF-B and VEGF-C provide this gene family with additional functions, for example, VEGF-C also regulates lymphangiogenesis.},
	url = {http://view.ncbi.nlm.nih.gov/pubmed/10600689},
	author = {Olofsson, B and Jeltsch, M and Eriksson, U and Alitalo, K}
}
@article {17,
	title = {Vascular endothelial growth factor B (VEGF-B) binds to VEGF receptor-1 and regulates plasminogen activator activity in endothelial cells},
	journal = {Proc Natl Acad Sci U S A},
	volume = {95},
	year = {1998},
	month = {1998/Sep/},
	pages = {11709 - 14},
	abstract = {The vascular endothelial growth factor (VEGF) family has recently expanded by the identification and cloning of three additional members, namely VEGF-B, VEGF-C, and VEGF-D. In this study we demonstrate that VEGF-B binds selectively to VEGF receptor-1/Flt-1. This binding can be blocked by excess VEGF, indicating that the interaction sites on the receptor are at least partially overlapping. Mutating the putative VEGF receptor-1/Flt-1 binding determinants Asp63, Asp64, and Glu67 to alanine residues in VEGF-B reduced the affinity to VEGF receptor-1 but did not abolish binding. Mutational analysis of conserved cysteines contributing to VEGF-B dimer formation suggest a structural conservation with VEGF and platelet-derived growth factor. Proteolytic processing of the 60-kDa VEGF-B186 dimer results in a 34-kDa dimer containing the receptor-binding epitopes. The binding of VEGF-B to its receptor on endothelial cells leads to increased expression and activity of urokinase type plasminogen activator and plasminogen activator inhibitor 1, suggesting a role for VEGF-B in the regulation of extracellular matrix degradation, cell adhesion, and migration.},
	url = {http://view.ncbi.nlm.nih.gov/pubmed/9751730},
	author = {Olofsson, B and Korpelainen, E and Pepper, M S and Mandriota, S J and Aase, K and Kumar, V and Gunji, Y and Jeltsch, M M and Shibuya, M and Alitalo, K and Eriksson, U}
}
@article {12,
	title = {Vascular endothelial growth factors VEGF-B and VEGF-C},
	journal = {J Cell Physiol},
	volume = {173},
	year = {1997},
	month = {1997/Nov/},
	pages = {211 - 5},
	url = {http://view.ncbi.nlm.nih.gov/pubmed/9365524},
	author = {Joukov, V and Kaipainen, A and Jeltsch, M and Pajusola, K and Olofsson, B and Kumar, V and Eriksson, U and Alitalo, K}
}
