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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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Mutation of threonine 766 in the epidermal growth factor receptor reveals a hotspot for resistance formation against selective tyrosine kinase inhibitors.

TL;DR: The data identify Thr-766 of the EGFR as a structural determinant that bears the potential to become a relevant feature in resistance formation during cancer therapy with EGFR-specific 4-anilinoquinazoline inhibitors.
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Characterization of angiogenesis and microcirculation of high-grade glioma : An intravital multifluorescence microscopic approach in the athymic nude mouse

TL;DR: The microvasculature of mature gliomas revealed a microvascular zonal division with a progressive reduction of the functional vessel length per area within the tumor center, the first data from repeated in vivo analysis of glioma growth, vascularization, and microcirculation.
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Mitochondrial AKAP121 Binds and Targets Protein Tyrosine Phosphatase D1, a Novel Positive Regulator of src Signaling

TL;DR: The findings indicate that PTPD1 is a novel positive regulator of src signaling and a key component of the EGF transduction pathway by binding and/or targeting the phosphatase on mitochondria, AKAP121 modulates the amplitude and persistence of src-dependent EGFtransduction pathway.
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Inhibition of glioma cell growth by a truncated platelet-derived growth factor-beta receptor.

TL;DR: The usefulness of dominant-negative mutants of the PDGF receptor are demonstrated for the evaluation of the role of the receptor in tumorigenesis and the ability of cells expressing the truncated receptor to grow as xenografts in nude mice was impaired.
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Helicobacter pylori-stimulated EGF receptor transactivation requires metalloprotease cleavage of HB-EGF.

TL;DR: These findings support a model in which H. pylori triggers constitutive EGFR signal activation, which enhances IL-8 production, and initiates neoplastic transformation of gastric epithelial cells.