R
Roland Riek
Researcher at ETH Zurich
Publications - 270
Citations - 27414
Roland Riek is an academic researcher from ETH Zurich. The author has contributed to research in topics: Protein structure & Chemistry. The author has an hindex of 71, co-authored 248 publications receiving 24124 citations. Previous affiliations of Roland Riek include Salk Institute for Biological Studies & École Polytechnique Fédérale de Lausanne.
Papers
More filters
Journal ArticleDOI
Attenuated T2 relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
TL;DR: The TROSY principle should benefit a variety of multidimensional solution NMR experiments, especially with future use of yet somewhat higher polarizing magnetic fields than are presently available, and thus largely eliminate one of the key factors that limit work with larger molecules.
Journal ArticleDOI
3D structure of Alzheimer's amyloid-β(1–42) fibrils
Thorsten Lührs,Christiane Ritter,Marc Adrian,Dominique Riek-Loher,Bernd Bohrmann,Heinz Döbeli,David Schubert,Roland Riek +7 more
TL;DR: The 3D structure of the fibrils comprising Aβ(1–42), which was obtained by using hydrogen-bonding constraints from quenched hydrogen/deuterium-exchange NMR, side-chain packing constraints from pairwise mutagenesis studies, and parallel, in-register β-sheet arrangement from previous solid-state NMR studies, explains the sequence selectivity, the cooperativity, and the apparent unidirectionality of Aβ fibril growth.
Journal ArticleDOI
In vivo demonstration that alpha-synuclein oligomers are toxic.
Beate Winner,Roberto Jappelli,Samir K. Maji,Paula Desplats,Leah Boyer,Stefan Aigner,Claudia Hetzer,Thomas Loher,Marçal Vilar,Silvia Campioni,Christos Tzitzilonis,Alice Soragni,Sebastian Jessberger,Helena Mira,Antonella Consiglio,Emiley Pham,Eliezer Masliah,Fred H. Gage,Roland Riek +18 more
TL;DR: It is shown that α-syn oligomers are toxic in vivo and thatα- syn variants that form oligomers might interact with and potentially disrupt membranes and the toxicity of these mutants by using a rat lentivirus system to investigate loss of dopaminergic neurons in the substantia nigra.
Journal ArticleDOI
NMR structure of the mouse prion protein domain PrP(121–231)
TL;DR: The nuclear magnetic resonance (NMR) structure of the autonomously folding PrP domain contains most of the point-mutation sites that have been linked, in human PrP, to the occurrence of familial prion diseases, and shows that these mutations occur within, or directly adjacent to, regular secondary structures.
Journal ArticleDOI
NMR Solution Structure of the Human Prion Protein
Ralph Zahn,Aizhuo Liu,Thorsten Lührs,Roland Riek,Christine von Schroetter,Francisco López García,Martin Billeter,Luigi Calzolai,Gerhard Wider,Kurt Wüthrich +9 more
TL;DR: The NMR structures of the recombinant human prion protein hPrP(23-230) include a globular domain extending from residues 125-228, for which a detailed structure was obtained, and an N-terminal flexibly disordered "tail," which influences the local conformational state of the polypeptide segments.