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Silvio Weber

Researcher at Dresden University of Technology

Publications -  27
Citations -  1533

Silvio Weber is an academic researcher from Dresden University of Technology. The author has contributed to research in topics: ADAM10 & Protein phosphatase 1. The author has an hindex of 14, co-authored 25 publications receiving 1281 citations. Previous affiliations of Silvio Weber include University of Göttingen & University of Kiel.

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The Disintegrin/Metalloproteinase ADAM10 Is Essential for the Establishment of the Brain Cortex

TL;DR: This study reveals that ADAM10 plays a central role in the developing brain by controlling mainly Notch-dependent pathways but likely also by reducing surface shedding of other neuronal membrane proteins including APP.
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Notch-RBP-J signaling regulates the transcription factor IRF8 to promote inflammatory macrophage polarization.

TL;DR: A signaling network in which signaling via Notch–RBP-J and TLRs is integrated at the level of synthesis of IRF8 protein is defined and a mechanism by which heterologous signaling pathways can regulate the TLR-induced inflammatory polarization of macrophages is identified.
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Ectodomain shedding and ADAMs in development

TL;DR: This Review summarizes the fascinating roles of ADAMs in embryonic and adult tissue development in both vertebrates and invertebrates.
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The disintegrin/metalloproteinase Adam10 is essential for epidermal integrity and Notch-mediated signaling

TL;DR: The disintegrin and metalloproteinase Adam10 has been implicated in the regulation of key signaling pathways that determine skin morphogenesis and homeostasis, and selectively disrupted Adam10 during skin morphology and in adult skin this article.
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Tetraspanin15 regulates cellular trafficking and activity of the ectodomain sheddase ADAM10

TL;DR: The data show that TSPAN15 is a central modulator of ADAM10-mediated ectodomain shedding and Therapeutic manipulation of its expression levels may be an additional approach to specifically regulate the activity of the amyloid precursor protein alpha-secretase ADAM 10.