A
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
More filters
Journal ArticleDOI
Novel signaling pathway suggested by SH3 domain-mediated p95vav/heterogeneous ribonucleoprotein K interaction.
TL;DR: The role of the protooncogene product p95vav in signal transduction was investigated by characterizing its interactions with proteins that may represent components of a novel signaling pathway.
Journal ArticleDOI
Genetic alterations in the tyrosine kinase transcriptome of human cancer cell lines.
Jens E. Ruhe,Sylvia Streit,Stefan Hart,Chee Hong Wong,Katja Specht,Pjotr Knyazev,Tatjana Knyazeva,Liang Seah Tay,Hooi Linn Loo,Priscilla Foo,Winnie Wong,Sharon Pok,Shu Jing Lim,Huimin Ong,Ming Luo,Han Kiat Ho,Kaitian Peng,Tze Chuen Lee,Martin Bezler,Christian Mann,Silvia Gaertner,Heinz Hoefler,Stefano Iacobelli,Stephan Peter,Alice Tay,Sydney Brenner,Byrappa Venkatesh,Axel Ullrich +27 more
TL;DR: A cDNA-based sequence analysis of the entire tyrosine kinase transcriptome of 254 established tumor cell lines provides extensive system information for the design and interpretation of cell line-based cancer research, and may stimulate further investigations into broader clinical applications of current cancer therapeutics.
Journal ArticleDOI
Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor
TL;DR: A novel crosstalk mechanism is established which allows signal integration and definition in cells with many different RTKs and provides evidence that PKD‐mediated dual phosphorylation of these critical threonine residues leads to suppression of EGF‐induced JNK activation.
Journal ArticleDOI
Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos
Hiroaki Terasawa,Daisuke Kohda,Hideki Hatanaka,Shigeo Tsuchiya,Kenji Ogura,Koji Nagata,Shunsuke Ishii,Valsan Mandiyan,Axel Ullrich,Joseph Schlessinger,Fuyuhiko Inagaki,Fuyuhiko Inagaki +11 more
TL;DR: The high-resolution NMR structure of the complex between the amino-terminal SH3 domain of GRB2 and a ten amino acid peptide derived from the guanine nucleotide releasing factor Sos is determined.
Journal Article
SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin.
TL;DR: Evidence is presented that the product of the vav proto-oncogene, p95vav, interacts specifically with the focal adhesion protein zyxin both in vitro and in yeast two hybrid system.