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Christian U. Stirnimann
Researcher at University of Zurich
Publications - 14
Citations - 1430
Christian U. Stirnimann is an academic researcher from University of Zurich. The author has contributed to research in topics: Periplasmic space & DsbA. The author has an hindex of 12, co-authored 13 publications receiving 1286 citations.
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Journal ArticleDOI
WD40 proteins propel cellular networks
TL;DR: The WD40 domain distributions in protein networks and structures of WD40-containing assemblies are discussed to demonstrate their versatility in mediating critical cellular functions.
Journal ArticleDOI
Complex Interdependence Regulates Heterotypic Transcription Factor Distribution and Coordinates Cardiogenesis
Luis Luna-Zurita,Christian U. Stirnimann,Sebastian Glatt,Bogac Kaynak,Sean Thomas,Florence Baudin,Abul Hassan Samee,Daniel He,Eric M. Small,Maria Mileikovsky,Andras Nagy,Andras Nagy,Alisha K. Holloway,Katherine S. Pollard,Christoph W. Müller,Benoit G. Bruneau +15 more
TL;DR: In this paper, the T-box TF TBX5 and the homeodomain TF NKX2-5 co-crystal structures bound to DNA were found to have a direct interaction between the two factors and induced DNA bending.
Journal ArticleDOI
Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD
Anna Rozhkova,Christian U. Stirnimann,Patrick Frei,Ulla Grauschopf,René A. Brunisholz,Markus G. Grütter,Guido Capitani,Rudi Glockshuber +7 more
TL;DR: D from Escherichia coli catalyzes the transport of electrons from cytoplasmic thioredoxin to the periplasmic disulfide isomerase DsbC, and the crystal structure of this catalytic intermediate was solved at 2.85 Å resolution, which revealed large relative domain movements in DsbD as a consequence of a strong overlap between the surface areas of nDsbD that interact with DSBC and cdsbD.
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Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency.
Benjamin L. Schulz,Christian U. Stirnimann,John P.A. Grimshaw,Maurice S. Brozzo,Fabienne Fritsch,Elisabeth Mohorko,Guido Capitani,Rudi Glockshuber,Markus G. Grütter,Markus Aebi +9 more
TL;DR: Functional and structural investigations of the Ost3/6p components of the yeast enzyme show that eukaryotic oligosaccharyltransferase is a multifunctional enzyme that acts at the crossroads of protein modification and protein folding.
Journal ArticleDOI
Structural basis and kinetics of DsbD-dependent cytochrome c maturation.
Christian U. Stirnimann,Anna Rozhkova,Ulla Grauschopf,Markus G. Grütter,Rudi Glockshuber,Guido Capitani +5 more
TL;DR: The crystal structure of the disulfide-linked complex between nDsbD and the soluble part of CcmG is determined and the N-terminal segment of ndsbD contributes to specific recognition of C cmG constitute the structural basis for the adaptability of nDs bD to different protein substrates.