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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.
Papers
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Journal ArticleDOI
Transforming potentials of epidermal growth factor and nerve growth factor receptors inversely correlate with their phospholipase C gamma affinity and signal activation.
TL;DR: The significance of PLC gamma affinity for signal definition, the role of this receptor tyrosine kinase substrate as a negative feedback regulator and the importance of this regulatory function for mitogenesis and its disturbance in oncogenic aberrations are established.
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Distinct characteristics of heregulin signals mediated by HER3 or HER4.
TL;DR: In this article, the authors analyzed distinct heregulin (HRG) signals mediated by the HRG receptors HER3 and HER4 and demonstrated that HRG-induced transformation by "kinase-impaired" HER3 is dependent on coexpression of kinase active HER2.
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Bosutinib inhibits migration and invasion via ack1 in kras mutant non-small cell lung cancer
Daniel Shao-Weng Tan,Benjamin Haaland,Jia Min Gan,Su Chin Tham,Indrajit Sinha,Eng Huat Tan,Kiat Hon Lim,Angela Takano,Sai Sakktee Krisna,Minn Minn Myint Thu,Hoe Peng Liew,Axel Ullrich,Wan-Teck Lim,Wan-Teck Lim,Boon Tin Chua +14 more
TL;DR: In conclusion, inhibition of ACK1 with bosutinib attenuates migration and invasion in the context of KRAS mutant NSCLC and may fulfil a therapeutic niche through combinatorial treatment approaches.
Patent
Protein tyrosine phosphatase
TL;DR: A protein tyrosine phosphatase designated PTP-S31 and its subfamily are identified in this article, as well as nucleic acid molecule coding therefor, and methods for screening molecules which can bind to PTPS31 proteins or glycoproteins and inhibit or stimulate their enzymatic activity.
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PTP-PEST phosphatase variations in human cancer.
Sylvia Streit,Jens E. Ruhe,Pjotr Knyazev,Tatjana Knyazeva,Stefano Iacobelli,Stephan Peter,Heinz Hoefler,Axel Ullrich +7 more
TL;DR: Functional characterization of the Ile322 and Ala573 PTP-PEST mutants revealed an enhancement of in vitro phosphatase activity, whereas the Lys709 variant showed reduced catalytic activity, and underscore the need for further characterizing PTP -PEST and its signaling pathways in context of this disease.