C. Wasmer

发表

The Mechanism of Toxicity in HET-S/HET-s Prion Incompatibility

R. Riek, B. Meier, J. Greenwald, 2012, PLoS biology.

Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded modules.

B. Meier, B. Habenstein, Yannick Sourigues, 2009, Journal of molecular biology.

Atomic-resolution structure determination of amyloid fibrils by solid-state NMR

C. Wasmer, 2010 .

Infectious and noninfectious amyloids of the HET-s(218-289) prion have different NMR spectra.

R. Riek, B. Meier, R. Sabaté, 2008, Angewandte Chemie.

Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity.

Raimon Sabaté, Christiane Ritter, Alice Soragni, 2010, Journal of molecular biology.

Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.

B. Meier, A. Loquet, A. Lange, 2010, Journal of the American Chemical Society.

Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core

Beat H. Meier, Roland Riek, R. Riek, 2008, Science.

Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion

B. Meier, B. Habenstein, Yannick Sourigues, 2011, Journal of biomolecular NMR.

Protocols for the Sequential Solid‐State NMR Spectroscopic Assignment of a Uniformly Labeled 25 kDa Protein: HET‐s(1‐227)

R. Riek, B. Meier, B. Habenstein, 2010, Chembiochem : a European journal of chemical biology.

Contribution of Specific Residues of the β-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability

R. Riek, B. Meier, Celestine N. Chi, 2014, PLoS pathogens.

Residue‐Specific Structural Studies of Inclusion Bodies

M. Wälti, C. Wasmer, Lei Wang, 2014 .

The molecular organization of the fungal prion HET-s in its amyloid form.

R. Riek, B. Meier, A. Schütz, 2009, Journal of molecular biology.

Sequence-specific resonance assignment of soluble nonglobular proteins by 7D APSY-NMR spectroscopy.

Kurt Wüthrich, Sebastian Hiller, Gerhard Wider, 2007, Journal of the American Chemical Society.

A Combined Solid‐State NMR and MD Characterization of the Stability and Dynamics of the HET‐s(218‐289) Prion in its Amyloid Conformation

B. Meier, W. V. van Gunsteren, A. Lange, 2009, Chembiochem : a European journal of chemical biology.

Probing water accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.

P. Schanda, B. Meier, A. Lange, 2011, Journal of molecular biology.

Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids.

R. Riek, B. Meier, M. Steinmetz, 2009, Angewandte Chemie.

Atomic-resolution structure determination of amyloid fibrils by solid-state NMR

C. Wasmer, 2010 .

Sequence-specific resonance assignment of soluble nonglobular proteins by 7D APSY-NMR spectroscopy.

G. Wider, K. Wüthrich, S. Hiller, 2007, Journal of the American Chemical Society.