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Christiane B. Knobbe-Thomsen

Researcher at University of Düsseldorf

Publications -  18
Citations -  1958

Christiane B. Knobbe-Thomsen is an academic researcher from University of Düsseldorf. The author has contributed to research in topics: Cancer & Unfolded protein response. The author has an hindex of 11, co-authored 17 publications receiving 1441 citations. Previous affiliations of Christiane B. Knobbe-Thomsen include University of Toronto & University Health Network.

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Glutathione and Thioredoxin Antioxidant Pathways Synergize to Drive Cancer Initiation and Progression

TL;DR: It is demonstrated that synthesis of the antioxidant glutathione (GSH), driven by GCLM, is required for cancer initiation and combined inhibition of GSH and thioredoxin antioxidant pathways leads to a synergistic cancer cell death in vitro and vivo, demonstrating the importance of these two antioxidants to tumor progression and as potential targets for therapeutic intervention.
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Advances in the molecular genetics of gliomas - implications for classification and therapy.

TL;DR: It is illustrated how advances in the molecular genetics of gliomas can promote the development and clinical translation of novel pathogenesis-based therapeutic approaches, thereby paving the way towards precision medicine in neuro-oncology.
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Somatic CRISPR/Cas9-mediated tumour suppressor disruption enables versatile brain tumour modelling.

TL;DR: This work has established CRISPR/Cas9-mediated somatic gene disruption, allowing for in vivo targeting of TSGs and demonstrates the utility of this approach by deleting single (Ptch1) or multiple genes in the mouse brain, resulting in the development of medulloblastoma and glioblastomas.
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EGFR Phosphorylates Tumor-Derived EGFRvIII Driving STAT3/5 and Progression in Glioblastoma

TL;DR: This work documents coexpression of EGFR and EGFRvIII in primary human glioblastoma that drives transformation and tumorigenesis in a cell-intrinsic manner and demonstrates enhancement of downstream STAT signaling triggered by EGFR-catalyzed phosphorylation of EGfrvIII, implicating EGFR vIII as a substrate for EGFR.