K
Kari Alitalo
Researcher at University of Helsinki
Publications - 844
Citations - 122462
Kari Alitalo is an academic researcher from University of Helsinki. The author has contributed to research in topics: Angiogenesis & Vascular endothelial growth factor C. The author has an hindex of 174, co-authored 817 publications receiving 114231 citations. Previous affiliations of Kari Alitalo include Mount Sinai Hospital, Toronto & Cornell University.
Papers
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Journal Article
Altered Expression Patterns of VEGF Receptors in Human Diabetic Retina and in Experimental VEGF-Induced Retinopathy in Monkey
A. N. Witmer,H. G. T. Blaauwgeers,Herbert A. Weich,Kari Alitalo,Gijs F.J.M. Vrensen,Reinier O. Schlingemann +5 more
TL;DR: In this paper, the VEGF receptor expression in the retina was investigated in the diabetic retina and in an experimental monkey model of vascular leakage and angiogenesis in diabetic retinopathy.
Journal ArticleDOI
The Bmx Tyrosine Kinase Induces Activation of the Stat Signaling Pathway, Which Is Specifically Inhibited by Protein Kinase Cδ
TL;DR: Two studies show that Bmx, a Tec family kinase, can function as an activator of the Stat signaling pathway and identify a role for PKCdelta in the regulation of Bmx signaling.
Patent
Vascular endothelial growth factor-B and DNA coding therefor
TL;DR: The VEGF-B polypeptides from the PDGF family of growth factors have the property of promoting mitosis and proliferation of vascular endothelial cells and are useful in stimulating angiogenesis as well as in diagnostic applications.
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Induction of TNF-sensitive cellular phenotype by c-Myc involves p53 and impaired NF-kappaB activation.
Juha Klefström,Elena Arighi,Trevor D. Littlewood,Marja Jäättelä,Eero Saksela,Gerard I. Evan,Kari Alitalo +6 more
TL;DR: The present findings show that the cytotoxic activity of TNF towards oncoprotein‐expressing cells involves p53 and an impaired signaling for survival in such cells.
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Overexpressed Csk tyrosine kinase is localized in focal adhesions, causes reorganization of alpha v beta 5 integrin, and interferes with HeLa cell spreading.
TL;DR: Results show that a fraction of cellular Csk is targeted to focal adhesions via its SH2 and SH3 domains, probably interacting with tyrosyl-phosphorylated focal adhesion proteins, and suggest that CSk is involved in the regulation of integrins controlling cell attachment and shape.