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Rainer Prohaska

Researcher at Medical University of Vienna

Publications -  49
Citations -  2959

Rainer Prohaska is an academic researcher from Medical University of Vienna. The author has contributed to research in topics: Stomatin & Integral membrane protein. The author has an hindex of 29, co-authored 49 publications receiving 2796 citations. Previous affiliations of Rainer Prohaska include University of Vienna.

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Journal ArticleDOI

Stomatin, flotillin-1, and flotillin-2 are major integral proteins of erythrocyte lipid rafts.

TL;DR: Stomatin and the flotillins are present as independently organized high-order oligomers, suggesting that these complexes act as separate scaffolding components at the cytoplasmic face of erythrocyte lipid rafts.
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Association of stomatin with lipid bodies.

TL;DR: The data suggest that LBs are not only involved in the storage of lipids but also participate actively in the cellular signaling network and the homeostasis oflipids.
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Erythrocyte Glut1 Triggers Dehydroascorbic Acid Uptake in Mammals Unable to Synthesize Vitamin C

TL;DR: It is reported that glucose transport actually decreases during human erythropoiesis despite a >3-log increase in Glut1 transcripts, and stomatin, an integral erythrocyte membrane protein, is identified as regulating the switch from glucose to DHA transport.
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Flotillin-1/reggie-2 traffics to surface raft domains via a novel golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation.

TL;DR: It is shown that newly synthesized flotillin-1 reaches the plasma membrane via a Sar1-independent and brefeldin A-resistant targeting pathway, involving a Golgi-independent trafficking pathway, the PHB domain, and palmitoylation.
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Erythrocyte detergent-resistant membrane proteins: Their characterization and selective uptake during malarial infection

TL;DR: Ten internalized DRM proteins show varied lipid and peptidic anchors indicating that, contrary to the prevailing model of apicomplexan vacuole formation, DRM association, rather than lipid anchors, provides the preferred criteria for protein recruitment to the malarial vacuoles.