U
Ulrich Schubert
Researcher at Heinrich Pette Institute
Publications - 4
Citations - 1362
Ulrich Schubert is an academic researcher from Heinrich Pette Institute. The author has contributed to research in topics: Virus & Ubiquitin. The author has an hindex of 4, co-authored 4 publications receiving 1329 citations.
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Journal ArticleDOI
A novel influenza A virus mitochondrial protein that induces cell death
Weisan Chen,Paul A. Calvo,Daniela Malide,James P. Gibbs,Ulrich Schubert,Igor Bacik,Sameh Basta,Robert E. O'Neill,Jeanne Schickli,Peter Palese,Peter Henklein,Jack R. Bennink,Jonathan W. Yewdell +12 more
TL;DR: It is proposed that PB1-F2 functions to kill host immune cells responding to influenza virus infection, and influenza viruses with targeted mutations that interfere with PB1/F2 expression induce less extensive apoptosis in human monocytic cells than those with intact PB1 -F2.
Journal ArticleDOI
Intracellular localization of proteasomal degradation of a viral antigen
Luis C. Antón,Ulrich Schubert,Igor Bacik,Michael F. Princiotta,Pamela A. Wearsch,James S. Gibbs,Patricia M. Day,Claudio Realini,Martin Rechsteiner,Jack R. Bennink,Jonathan W. Yewdell +10 more
TL;DR: It is demonstrated that PODs and the MTOC serve as sites of proteasomal degradation of misfolded dNP and probably cellular proteins as well, and imply that antigenic peptides are generated at one or both of these sites.
Journal ArticleDOI
Retroviruses Have Differing Requirements for Proteasome Function in the Budding Process
TL;DR: Results from other viruses show that proteasome inhibitors reduce the budding of viruses that utilize either a PPPY- or PTAP-based L domain and that this effect does not depend on the assembly site or the presence of monoubiquitinated Gag in the virion.
Journal ArticleDOI
Membrane interactions and alignment of structures within the HIV-1 Vpu cytoplasmic domain: effect of phosphorylation of serines 52 and 56.
TL;DR: Well‐oriented proton‐decoupled 15N solid‐state NMR spectra with 15N chemical shifts at the most upfield position indicate that the amphipathic helix within [15N‐Leu 45]‐Vpu27–57 strongly interacts with mechanically aligned POPC bilayers and adopts an orientation parallel to the membrane surface.