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Julie Weidner

Researcher at University of Gothenburg

Publications -  24
Citations -  503

Julie Weidner is an academic researcher from University of Gothenburg. The author has contributed to research in topics: Medicine & P-bodies. The author has an hindex of 10, co-authored 19 publications receiving 267 citations. Previous affiliations of Julie Weidner include Lund University & University of Basel.

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Journal ArticleDOI

Context-dependent deposition and regulation of mRNAs in P-bodies.

TL;DR: A new method is devised to identify both common and stress-specific mRNA subsets associated with P-bodies and it is shown that the Puf5p-dependent storage of a subset of mRNAs in P- bodies under glucose starvation may be beneficial with respect to chronological lifespan.
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Spotlight on microRNAs in allergy and asthma.

TL;DR: An overview of the current research on miRNAs in allergic diseases, including atopic dermatitis, allergic rhinitis, and asthma is given and how individual miRNas function in the regulation of immune responses in epithelial cells and specialized immune cells in response to different environmental factors and respiratory viruses is discussed.
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Defects in the secretory pathway and high Ca2+ induce multiple P-bodies.

TL;DR: This manuscript demonstrates for the first time that P-body (PB) formation in response to stress is a regulated process, and that at least two different pathways drive PB assembly.
Posted ContentDOI

Spotlight on microRNAs in allergy and asthma

TL;DR: An overview of the current research on miRNAs in allergic diseases, including atopic dermatitis, allergic rhinitis and asthma is given and the importance of research into miRNA function in allergy and asthma to improve knowledge of the molecular mechanisms involved in the pathogenesis of this heterogeneous group of diseases is highlighted.
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The polysome-associated proteins Scp160 and Bfr1 prevent P body formation under normal growth conditions

TL;DR: It is shown that the polysome-associated mRNA-binding protein Scp160 interacts with P body components, such as the decapping protein Dcp2 and the scaffold protein Pat1, presumably, on polysomes, to prevent P body formation under normal growth conditions.