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Rene Devos

Researcher at Hoffmann-La Roche

Publications -  37
Citations -  10293

Rene Devos is an academic researcher from Hoffmann-La Roche. The author has contributed to research in topics: Receptor & Interleukin-5 receptor. The author has an hindex of 26, co-authored 37 publications receiving 10098 citations. Previous affiliations of Rene Devos include Ghent University.

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Journal ArticleDOI

Identification and expression cloning of a leptin receptor Ob-R

TL;DR: The ob gene product, leptin, is an important circulating signal for the regulation of body weight and a series of leptin-alkaline phosphatase (AP) fusion proteins as well as [125I]leptin fusion proteins were generated to identify high affinity leptin-binding sites in the mouse choroid plexus.
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Recombinant mouse OB protein: evidence for a peripheral signal linking adiposity and central neural networks.

TL;DR: The behavioral effects after brain administration suggest that OB protein can act directly on neuronal networks that control feeding and energy balance in ob/ob and diet-induced obese mice.
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A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific α chain and a β chain shared with the receptor for GM-CSF

TL;DR: The finding that IL5 and GM-CSF share a receptor subunit provides a molecular basis for the observation that these cytokines can partially interfere with each other's binding and have highly overlapping biological activities on eosinophils.
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ESM-1 Is a Novel Human Endothelial Cell-specific Molecule Expressed in Lung and Regulated by Cytokines

TL;DR: Immunoblotting and immunoprecipitation of HUVEC lysates revealed a specific 20-kDa band corresponding to ESM-1, which was shown to be tissue-restricted to the human lung and may have potent implications in the areas of vascular cell biology and human lung physiology.
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Leptin Receptor (OB-R) Signaling CYTOPLASMIC DOMAIN MUTATIONAL ANALYSIS AND EVIDENCE FOR RECEPTOR HOMO-OLIGOMERIZATION

TL;DR: It is reported that deletion and tyrosine substitution mutagenesis of OB-R identifies two distinct regions of the intracellular domain important for signaling, suggesting that mechanisms exist to permit signaling by the long form ofOB-R even in the pretence of excess naturally occurring short form of OB -R.