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Jana Staňková

Researcher at Université de Sherbrooke

Publications -  9
Citations -  462

Jana Staňková is an academic researcher from Université de Sherbrooke. The author has contributed to research in topics: Receptor & Internalization. The author has an hindex of 8, co-authored 9 publications receiving 453 citations.

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IL-13 and IL-4 up-regulate cysteinyl leukotriene 1 receptor expression in human monocytes and macrophages.

TL;DR: It is reported that IL-13 up-regulates Cys LT1R mRNA levels, with consequently enhanced CysLT1R protein expression and function in human monocytes and monocyte-derived macrophages, and thus contribute to the pathogenesis of asthma and allergic diseases.
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Structural and functional requirements for agonist-induced internalization of the human platelet-activating factor receptor.

TL;DR: Receptor sequestration and ligand uptake was, at least in part, blocked by concanavalin A and blockers of endocytosis mediated by clathrin-coated pits and the C terminus tail of hPAFR, but not the putative internalization motifs, may be involved in the internalization of h PAFR.
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Selective Modulation of Wild Type Receptor Functions by Mutants of G-Protein-coupled Receptors

TL;DR: It is reported that mutant GPCR can affect the functional properties of the co-expressed wild type (WT) receptor, and these findings could be extended to other GPCRs by showing that co-expression of the WT C-C chemokine receptor 2b with a carboxyl-terminal deletion mutant (K311stop), resulted in a decreased affinity and responsiveness to MCP-1.
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Agonist-induced internalization of the platelet-activating factor receptor is dependent on arrestins but independent of G-protein activation. Role of the C terminus and the (D/N)PXXY motif.

TL;DR: The results indicate that ligand-induced PAFR internalization is dependent on arrestins, that PAFR can associate with both arrestin-2 and -3, and that their translocation involves interaction with the region of residues 318–330 in the PAFR C terminus but is independent of G-protein activation.
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Janus kinase 2 activation by the platelet-activating factor receptor (PAFR): roles of Tyk2 and PAFR C terminus.

TL;DR: The results indicate that PAF activates Jak2 and that Tyk2 and the C-terminal tail of PAFR are of critical importance for PAF-induced Jak2 activation.