F
Felix T. Wieland
Researcher at Heidelberg University
Publications - 158
Citations - 22192
Felix T. Wieland is an academic researcher from Heidelberg University. The author has contributed to research in topics: COPI & Golgi apparatus. The author has an hindex of 71, co-authored 158 publications receiving 20604 citations. Previous affiliations of Felix T. Wieland include Stanford University.
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Journal ArticleDOI
Golgi Phosphoprotein 3 Triggers Signal-mediated Incorporation of Glycosyltransferases into Coatomer-coated (COPI) Vesicles
Elias S.P. Eckert,Ingeborg Reckmann,Andrea Hellwig,Simone Röhling,Assou El-Battari,Felix T. Wieland,Vincent Popoff +6 more
TL;DR: It is shown, for the first time, that GOLPH3 supports incorporation of both core 2 N-acetylglucosamine-transferase 1 and α-2,6-sialyl transferase 1 into COPI vesicles.
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Localization and topology of ratp28, a member of a novel family of putative steroid-binding proteins.
TL;DR: Cloned ratp28, a membrane protein from rat liver homologous to the previously described hpr6.6, a putative steroid-binding protein in humans has a type II topology as determined by protease digestion experiments on intact and detergent-solubilized membranes.
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Non-clathrin-coat protein alpha is a conserved subunit of coatomer and in Saccharomyces cerevisiae is essential for growth.
Beate Gerich,Lelio Orci,Herbert Tschochner,Friedrich Lottspeich,Mariella Ravazzola,Mylène Amherdt,Felix T. Wieland,Cordula Harter +7 more
TL;DR: To complete the molecular characterization of coatomer, the preformed cytosolic complex that is involved in the formation of biosynthetic transport vesicles, the gene for non-clathrin-coat protein alpha (alpha-COP) from Saccharomyces cerevisiae is cloned and characterized.
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Novel isotypic γ/ζ subunits reveal three coatomer complexes in mammals
TL;DR: The ubiquitous expression of two novel isotypes of coatomer subunits γ- and ζ-COP that are incorporated into coatomer are reported, and it is shown that three isotypes exist of the complex defined by the subunit combinations γ1/ζ1,ζ2, and γ2/ε1 in a liver cytosol.
Journal ArticleDOI
Protein-sphingolipid interactions within cellular membranes.
Per Haberkant,Oliver Schmitt,F-Xabier Contreras,Christoph Thiele,Kentaro Hanada,Hein Sprong,Constanze Reinhard,Felix T. Wieland,Britta Brügger +8 more
TL;DR: A novel photolabile sphingolipid probe that allows the detection of protein-sphingoipid interactions within the membrane bilayer of living cells and describes specific in vivo interactions of lipids with caveolin-1, phosphatidylinositol transfer protein β, and the mature form of nicastrin.