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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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Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs.

TL;DR: It is proposed that vav encodes a new class of substrates whose tyrosine phosphorylation may provide a mechanism for direct signal transduction linking receptors at the cell surface to transcriptional control.
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Strategies to overcome resistance to targeted protein kinase inhibitors.

TL;DR: Structural and mechanistic insights from imatinib-insensitive Bcr–Abl have been exploited to identify second-generation drugs that override acquired target resistance and create a rationale for the development of either multi-targeted protein kinase inhibitors or cocktails of selective antagonists as antitumour drugs.
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PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif

TL;DR: The existence of a conserved ERK1/2 interaction motif within the cytosolic non‐catalytic domains of PTP‐SL and STEP is demonstrated, which is required for the regulation of ERK 1/2 activity and for phosphorylation of the PTPs by these kinases.
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Identification of Trk Binding Sites for SHC and Phosphatidylinositol 3'-kinase and Formation of a Multimeric Signaling Complex

TL;DR: In vitro association of SHC and the p85 subunit of phosphatidylinositol 3'-kinase with the Trk tyrosine kinase was prevented only by phosphorylated Y-490- and Y-751-containing peptides, respectively.
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Neuronal differentiation signals are controlled by nerve growth factor receptor/Trk binding sites for SHC and PLC gamma.

TL;DR: Mutagenesis of the specific binding sites for src homology 2 domain‐containing substrates within the Trk cytoplasmic domain suggests a non‐essential function of PI3′‐K and reveals a major role for the signal controlled by the SHC binding site at tyrosine 490 and a co‐operative function of the PLC gamma‐mediated pathway for neuronal differentiation of PC12 cells.