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Axel Ullrich
Researcher at Max Planck Society
Publications - 436
Citations - 63142
Axel Ullrich is an academic researcher from Max Planck Society. The author has contributed to research in topics: Receptor tyrosine kinase & Tyrosine kinase. The author has an hindex of 124, co-authored 436 publications receiving 61445 citations. Previous affiliations of Axel Ullrich include Institute of Molecular and Cell Biology & Agency for Science, Technology and Research.
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Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site
Jürgen Braunger,Jürgen Braunger,Lothar Schleithoff,Ansgar Schulz,Heidi Kessler,Reiner Lammers,Reiner Lammers,Axel Ullrich,Claus R. Bartram,Claus R. Bartram,Johannes W.G. Janssen,Johannes W.G. Janssen +11 more
TL;DR: In vivo data indicate that further direct or indirect binding sites for PLCγ, GRB2, c-src and lck on the human Ufo receptor may exist, and indicates that intracellular signaling may be regulated by a new family of receptor tyrosine kinases.
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Cellular Redistribution of Protein Tyrosine Phosphatases LAR and PTPσ by Inducible Proteolytic Processing
TL;DR: The functional significance of processing for the receptor-like PTPases LAR and PTPσ and direct association of plakoglobin and β-catenin with the intracellular domain of LAR in vitro suggested an involvement in the regulation of cell contacts in concert with cell adhesion molecules of the cadherin/ catenin family.
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Tyrosine kinase signalling in breast cancer: Epidermal growth factor receptor - convergence point for signal integration and diversification
TL;DR: This work has identified the epidermal growth factor receptor as the convergence point and distribution focus, and proposed a nonclassical mode of signalling system cross-talk, in distinction to receptor activation induced by cognate ligands, called 'signal transactivation'.
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Anti-oncogenic activity of signalling-defective epidermal growth factor receptor mutants.
TL;DR: It is demonstrated that signalling-defective receptor tyrosine kinase mutants differentially interfere with oncogenic signals generated by either overexpressed EGF-R or the retroviral v-erbBES4 oncogene product.
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Characterization of a Conserved Structural Determinant Controlling Protein Kinase Sensitivity to Selective Inhibitors
Stephanie Blencke,Birgit Zech,Ola Engkvist,Zoltán Greff,Laszlo Orfi,Zoltán Horváth,György Kéri,Axel Ullrich,Henrik Daub +8 more
TL;DR: In this paper, a comprehensive mutational analysis of this structural element and determined the cellular sensitivities of several disease-relevant tyrosine kinases against various inhibitors, such as indolinones and pyrido[2,3-d]pyrimidine inhibitors.