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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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The structure of the regulatory domain of the adenylyl cyclase Rv1264 from Mycobacterium tuberculosis with bound oleic acid

TL;DR: Structures at acidic and basic pH values are determined and structure-based mutagenesis in the holoenzyme is employed to elucidate regulation using an AC activity assay and the new studies demonstrate that the length of the linker segment is decisive for regulation.
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Distinct binding sites for the ATPase and substrate-binding domain of human Hsp70 on the cell surface of antigen presenting cells.

TL;DR: The existence of at least two distinct receptors for Hsp70 are established, which are localized to distinct microdomains of the APC membrane, and the interaction of C70 with its putative receptor seems to be responsible for HSp70-mediated cross presentation.
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Differential transport of Influenza A neuraminidase signal anchor peptides to the plasma membrane

TL;DR: Stunningly, subtle differences in the primary structure of the part of the transmembrane domain that resides in the exoplasmic leaflet of the membrane have a major impact on transport efficiency, providing a potential target for the inhibition of virus release.
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Following the Fate In Vivo of COPI Vesicles Generated In Vitro

TL;DR: Fluorescently labeled COPI vesicles were generated in vitro from isolated rat liver Golgi membranes, labeled with the fluorescent dyes Alexa‐488 or Alexa‐568, and appeared to be active and colocalized with endogenous Gol Gi membranes within 30 min after microinjection into mammalian cells.
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Distinct role of subcomplexes of the COPI coat in the regulation of ArfGAP2 activity.

TL;DR: Findings point to a distinct role of each of the two coatomer subcomplexes in the regulation of ArfGAP2‐dependent GTP hydrolysis on Arf1, where the CM4 subcomplex functions in GAP recruitment, while, similarly to the COPII system, the cage‐like CM3 subcomplex stimulates the catalytic reaction.