Roland Riek

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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.

Konstantin Pervushin, Roland Riek, Gerhard Wider, Kurt Wüthrich
Proceedings of the National Academy of Sciences…
1997

Fast transverse relaxation of 1H, 15N, and 13C by dipole-dipole coupling (DD) and chemical shift anisotropy (CSA) modulated by rotational molecular motions has a dominant impact on the size limit for… (More)

3D structure of Alzheimer's amyloid-beta(1-42) fibrils.

Thorsten Lührs, Christiane Ritter, +5 authors Roland Riek
Proceedings of the National Academy of Sciences…
2005

Alzheimer's disease is the most fatal neurodegenerative disorder wherein the process of amyloid-beta (Abeta) amyloidogenesis appears causative. Here, we present the 3D structure of the fibrils… (More)

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core.

Christian Wasmer, Sascha Lange, Hélène Van Melckebeke, Ansgar B Siemer, Roland Riek, Beat H Meier
Science
2008

Prion and nonprion forms of proteins are believed to differ solely in their three-dimensional structure, which is therefore of paramount importance for the prion function. However, no… (More)

Prion (PrPSc)-specific epitope defined by a monoclonal antibody

Carsten Korth, Beat Stierli, +14 authors Bruno Oesch
Nature
1997

Prions are infectious particles causing transmissible spongiform encephalopathies (TSEs). They consist, at least in part, of an isoform (PrPSc) of the ubiquitous cellular prion protein (PrPC).… (More)

TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain.

E M Frickel, Roland Riek, Ilian Jelesarov, Ari Helenius, K. Wuthrich, Lars Ellgaard
Proceedings of the National Academy of Sciences…
2002

The lectin chaperone calreticulin (CRT) assists the folding and quality control of newly synthesized glycoproteins in the endoplasmic reticulum (ER). It interacts with ERp57, a thiol-disulfide… (More)

NMR solution structure of the human prion protein.

Ralph Zahn, Amanda Liu, +7 authors Kurt Wüthrich
Proceedings of the National Academy of Sciences…
2000

The NMR structures of the recombinant human prion protein, hPrP(23-230), and two C-terminal fragments, hPrP(90-230) and hPrP(121-230), include a globular domain extending from residues 125-228, for… (More)

Identifying the amylome, proteins capable of forming amyloid-like fibrils.

Lukasz Goldschmidt, Poh K Teng, Roland Riek, David S Eisenberg
Proceedings of the National Academy of Sciences…
2010

The amylome is the universe of proteins that are capable of forming amyloid-like fibrils. Here we investigate the factors that enable a protein to belong to the amylome. A major factor is the… (More)

The fold of alpha-synuclein fibrils.

Marçal Vilar, Hui-Ting Chou, +6 authors Roland Riek
Proceedings of the National Academy of Sciences…
2008

The aggregation of proteins into amyloid fibrils is associated with several neurodegenerative diseases. In Parkinson's disease it is believed that the aggregation of alpha-synuclein (alpha-syn) from… (More)

NMR structure of the mouse prion protein domain PrP(121–231)

Roland Riek, Simone Hornemann, Gerhard Wider, Martin Urs Billeter, Rudi Glockshuber, Kurt Wüthrich
Nature
1996

THE 'protein only' hypothesis1 states that a modified form of normal prion protein triggers infectious neurodegenerative diseases, such as bovine spongiform encephalopathy (BSE), or Creutzfeldt–Jakob… (More)

Functional amyloids as natural storage of peptide hormones in pituitary secretory granules.

Samir K Maji, Marilyn H. Perrin, +12 authors Roland Riek
Science
2009

Amyloids are highly organized cross-beta-sheet-rich protein or peptide aggregates that are associated with pathological conditions including Alzheimer's disease and type II diabetes. However,… (More)

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