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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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GPCR-induced migration of breast carcinoma cells depends on both EGFR signal transactivation and EGFR-independent pathways

TL;DR: It is concluded that GPCR-induced chemotaxis of breast cancer cells is mediated by EGFR-dependent and -independent signalling pathways, with both parallel pathways having to act in concert to achieve a complete migratory response.
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Truncation of the human EGF receptor leads to differential transforming potentials in primary avian fibroblasts and erythroblasts.

TL;DR: The results indicate that the C‐terminal domain of the EGFR is non‐essential in fibroblast transformation, but seems to be crucial for both self renewal induction and specificity of receptor function in erythroblasts.
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Involvement of the FGFR4 Arg388 allele in head and neck squamous cell carcinoma.

TL;DR: Investigation of the expression pattern of FGFR4 and the clinical significance of the recently identified Gly/Arg polymorphism in head and neck squamous cell carcinomas (HNSCCs) of the oral cavity and the oropharynx indicates that high expression ofFGFR4 in connection with the Arg388 allele is associated with poor clinical outcome and supports the significance of FG FR4 as a diagnostic marker and a target for therapeutic intervention in human HNSCC.
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Kinetic parameters of the protein tyrosine kinase activity of EGF-receptor mutants with individually altered autophosphorylation sites

TL;DR: Kinetic parameters of the kinase of wild‐type and mutant receptors were compared and alterations of individual autophosphorylation sites do not have a major effect on kinase activity.
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Phospholipase C-gamma, a substrate for PDGF receptor kinase, is not phosphorylated on tyrosine during the mitogenic response to CSF-1.

TL;DR: Although the PDGF and CSF‐1 receptors are structurally related and appear to be derived from a single ancestor gene, only PDGF‐induced mitogenesis in fibroblasts correlated with tyrosine phosphorylation of PLC‐gamma.