The multi-site docking protein Gab1 is constitutively phosphorylated independent from its recruitment to the plasma membrane in Jak2-V617Fpositive cells and mediates proliferation of human erythroleukaemia cells
Bongartz, Hannes; Otto-von-Guericke University Magdeburg, Germany > Institute of Biology, Department of Systems Biology
Hessenkemper, Wiebke; Otto-von-Guericke University Magdeburg, Germany > Institute of Biology, Department of Systems Biology
Müller, Christian; Otto-von-Guericke University Magdeburg, Germany
Fensky, Melissa; Otto-von-Guericke University Magdeburg, Germany > Institute of Biology, Department of Systems Biology
Fritsch, Johannes; Otto-von-Guericke University Magdeburg, Germany > Institute of Biology, Department of Systems Biology
Mandel, Katharina; Martin-Luther-University Halle-Wittenberg > Institute of Molecular Medicine
Behrmann, Iris ; University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
Haan, Claude ; University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
Fischer, Thomas; Otto-von-Guericke University Magdeburg, Germany > Department of Hematology and Oncology, Medical Center
Feller, Stephan M.; Martin-Luther-University Halle-Wittenberg > Institute of Molecular Medicine
Schaper, Fred; Otto-von-Guericke University Magdeburg, Germany > Institute of Biology, Department of Systems Biology
External co-authors :
yes
Language :
English
Title :
The multi-site docking protein Gab1 is constitutively phosphorylated independent from its recruitment to the plasma membrane in Jak2-V617Fpositive cells and mediates proliferation of human erythroleukaemia cells
