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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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Receptor protein tyrosine phosphatases are expressed by cycling retinal progenitor cells and involved in neuronal development of mouse retina

TL;DR: The results suggest distinct roles of RPTPs in cell proliferation and establishing phenotypes of different retinal cells during retinogenesis as well as later in the maintenance of mature retina.
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Expression, purification and crystallization of human phosphotyrosine phosphatase 1b

TL;DR: Thinner forms of PTP1B retained the same characteristics as the full-length mammalian enzyme, but are not subject to inhibition of enzymic activity mediated by the C-terminus, and it can be assumed that the catalytic domains are advantageous for crystallization studies in comparison to the natural enzyme.
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Selection for transformation and met protooncogene amplification in NIH 3T3 fibroblasts using tumor necrosis factor alpha.

TL;DR: In this paper, the authors show that selection of NIH 3T3 fibroblasts for resistance to the cytotoxic effects of tumor necrosis factor alpha (TNF-alpha), a major mediator of macrophage-induced tumor cell cytotoxicity, leads to enrichment in the remaining cells for those with transformed morphology and is often associated with amplified copy number and expression of the met protooncogene.
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Metformin Triggers Autophagy to Attenuate Drug-Induced Apoptosis in NSCLC Cells, with Minor Effects on Tumors of Diabetic Patients

TL;DR: In the retrospective study of 8 NSCLC patients, the administration of metformin did not induce statistically significant changes as assessed by immunohistochemical staining of pERK, pAKT and cleaved PARP.
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Effect of tumor-associated mutant E-cadherin variants with defects in exons 8 or 9 on matrix metalloproteinase 3

TL;DR: Application of the synthetic inhibitor of M MP‐3 NNGH and small interfering RNA directed against MMP‐3 reduce mutant E‐cadherin‐enhanced cell motility and point to a functional link between MMP•3 and E‐ cadher in.