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Veli-Matti Leppänen

Researcher at University of Helsinki

Publications -  43
Citations -  3295

Veli-Matti Leppänen is an academic researcher from University of Helsinki. The author has contributed to research in topics: Receptor tyrosine kinase & Vascular endothelial growth factor C. The author has an hindex of 24, co-authored 40 publications receiving 2756 citations. Previous affiliations of Veli-Matti Leppänen include Helsinki University Central Hospital.

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Novel neurotrophic factor CDNF protects and rescues midbrain dopamine neurons in vivo

TL;DR: In vivo and in vivo, CDNF prevented the 6-hydroxydopamine (6-OHDA)-induced degeneration of dopaminergic neurons in a rat experimental model of Parkinson’s disease and suggest that CDNF might be beneficial for the treatment of Parkinson's disease.
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Vascular endothelial growth factor signaling in development and disease

TL;DR: This Development at a Glance article provides an overview of the VEGF signaling pathway and highlights the functions of V EGF/VEGFR signaling in blood and lymphatic vessel development and pathology.
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Endothelial destabilization by angiopoietin-2 via integrin β1 activation

TL;DR: These results establish Ang2-mediated β1-integrin activation as a promoter of endothelial destablization, explaining the controversial vascular functions of Ang1 and Ang2.
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CCBE1 Enhances Lymphangiogenesis via A Disintegrin and Metalloprotease With Thrombospondin Motifs-3–Mediated Vascular Endothelial Growth Factor-C Activation

TL;DR: The results suggest that CCBE1 is a potential therapeutic tool for the modulation of lymphangiogenesis and angiogenesis in a variety of diseases that involve the lymphatic system, such as lymphedema or lymphatic metastasis.
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Structural determinants of growth factor binding and specificity by VEGF receptor 2

TL;DR: The crystal structure of VEGF-C bound to the VEGFR-2 high-affinity-binding site is presented, which reveals a symmetrical 2∶2 complex, in which left-handed twisted receptor domains wrap around the 2-fold axis of VPDG, providing significant insights into the structural features that determine the high affinity and specificity of V EGF/VEGFR interactions.