Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Christer Wernstedt"'
Autor:
Taro Matsumoto, Peetra U. Magnusson, Hideo Mugishima, Skjalg Bruheim, Tone Berge, Jiong Wu, Debrabata Mukhopadhyay, Johan Dixelius, Svante Bohman, Christer Wernstedt, Charlotte Wikner, Anne Spurkland, Anna Dimberg, Lena Claesson-Welsh, Ling Wang, Jian Hua Qi
Publikováno v:
The EMBO Journal. 24:2342-2353
Vascular endothelial growth factor receptor-2 (VEGFR-2) activation by VEGF-A is essential in vasculogenesis and angiogenesis. We have generated a pan-phosphorylation site map of VEGFR-2 and identified one major tyrosine phosphorylation site in the ki
Autor:
Marika J. Karkkainen, Johan Dixelius, Kari Alitalo, Christer Wernstedt, Lena Claesson-Welsh, Taija Makinen, Maria Wirzenius
Publikováno v:
Journal of Biological Chemistry. 278:40973-40979
Vascular endothelial growth factors (VEGFs) regulate the development and growth of the blood and lymphatic vascular systems. Of the three VEGF receptors (VEGFR), VEGFR-1 and -2 are expressed on blood vessels; VEGFR-2 is found also on lymphatic vessel
Publikováno v:
Experimental Cell Research. 288:110-118
We have previously demonstrated that ligand-stimulation of c-Kit induces phosphorylation of Tyr568 and Tyr570 in the juxtamembrane region of the receptor, leading to recruitment, phosphorylation and activation of members of the Src family of tyrosine
Publikováno v:
Journal of Biological Chemistry. 273:23410-23418
Receptor tyrosine phosphorylation is crucial for signal transduction by creating high affinity binding sites for Src homology 2 domain-containing molecules. By expressing the intracellular domain of Flt-1/vascular endothelial growth factor receptor-1
Publikováno v:
Journal of Biological Chemistry. 273:10147-10152
Prothymosin alpha (PTA) stimulates in a dose-dependent manner the phosphorylation of a 105-kDa protein (p105) in cell extracts from different cell types. Protein sequencing and immunological analysis indicated that this protein is elongation factor 2
Publikováno v:
Lund University
Hormone-sensitive lipase (HSL) is the rate-limiting enzyme in lipolysis. Stimulation of rat adipocytes with isoproterenol results in phosphorylation of HSL and a 50-fold increase in the rate of lipolysis. In this study, we used site-directed mutagene
Autor:
Serhiy Souchelnytskyi, Ulla Engström, Peter ten Dijke, Kiyoshi Tamaki, Christer Wernstedt, Carl-Henrik Heldin
Publikováno v:
Journal of Biological Chemistry. 272:28107-28115
Members of the Smad family of intracellular signal transducers are essential for transforming growth factor-beta (TGF-beta) to exert its multifunctional effects. After activation of TGF-beta receptors, Smad2 and Smad3 become phosphorylated and form h
Autor:
A.K. Arridsson, Christer Wernstedt, Carl-Henrik Heldin, Anders Eriksson, Ulf Hellman, Lena Claesson-Welsh, Lars Rönnstrand, Seijiro Mori
Publikováno v:
Lund University
Two novel sites of autophosphorylation were localized to the C-terminal tail of the PDGF beta-receptor. To evaluate the importance of these phosphorylation sites, receptor mutants in which Tyr1009, Tyr1021 or both were replaced with phenylalanine res
Autor:
Taras Stasyk, Anna Dubrovska, Serhiy Souchelnytskyi, Marta Lomnytska, Christer Wernstedt, Ulf Hellman, Carl-Henrik Heldin, Ihor Yakymovych
Publikováno v:
Molecular biology of the cell. 16(10)
Transforming growth factor-beta (TGFbeta) signaling involves activation of a number of signaling pathways, several of which are controlled by phosphorylation events. Here, we describe a phosphoproteome profiling of MCF-7 human breast epithelial cells
Publikováno v:
Cellular signalling. 16(4)
Binding of fibroblast growth factor (FGF) to the high affinity receptor-1 (FGFR-1) leads to activation of its endogenous tyrosine kinase activity. A number of substrates for the FGFR-1 kinase have been identified. Among those, FGF receptor-substrate-