The Conformation of the Prion Domain of Sup35 p in Isolation and in the Full-Length Protein

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

(2012) Carolin Seuring et al.   PLOS BIOLOGY

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

(2011) Birgit Habenstein et al.   JOURNAL OF BIOMOLECULAR NMR

A software framework for analysing solid-state MAS NMR data

(2011) Tim J. Stevens et al.   JOURNAL OF BIOMOLECULAR NMR

A mutation within the C-terminal domain of Sup35p that affects [PSI+] prion propagation

(2011) Mehdi Kabani et al.   MOLECULAR MICROBIOLOGY

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

(2010) Anne Schuetz et al.   CHEMBIOCHEM

Atomic-Resolution Three-Dimensional Structure of HET-s(218−289) Amyloid Fibrils by Solid-State NMR Spectroscopy

(2010) Hélène Van Melckebeke et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Sequence-Specific Random Coil Chemical Shifts of Intrinsically Disordered Proteins

(2010) Kamil Tamiola et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Differences in prion strain conformations result from non-native interactions in a nucleus

(2010) Yumiko Ohhashi et al.   Nature Chemical Biology

Two Prion Variants of Sup35p Have In-Register Parallel β-Sheet Structures, Independent of Hydration

(2009) Frank Shewmaker et al.   BIOCHEMISTRY

Characterization of different water pools in solid-state NMR protein samples

(2009) Anja Böckmann et al.   JOURNAL OF BIOMOLECULAR NMR

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

(2008) C. Wasmer et al.   SCIENCE