Search Results - "Wasmer, Christian"

The mechanism of toxicity in HET-S/HET-s prion incompatibility by Seuring, Carolin, Greenwald, Jason, Wasmer, Christian, Wepf, Roger, Saupe, Sven J, Meier, Beat H, Riek, Roland

“…The HET-s protein from the filamentous fungus Podospora anserina is a prion involved in a cell death reaction termed heterokaryon incompatibility. This…”
Get full text

Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability by Daskalov, Asen, Gantner, Matthias, Wälti, Marielle Aulikki, Schmidlin, Thierry, Chi, Celestine N, Wasmer, Christian, Schütz, Anne, Ceschin, Johanna, Clavé, Corinne, Cescau, Sandra, Meier, Beat, Riek, Roland, Saupe, Sven J

“…The [Het-s] prion of the fungus Podospora anserina represents a good model system for studying the structure-function relationship in amyloid proteins because…”
Get full text

Amyloid Fibrils of the HET-s(218-289) Prion Form a β Solenoid with a Triangular Hydrophobic Core by Wasmer, Christian, Lange, Adam, Van Melckebeke, Hélène, Siemer, Ansgar B, Riek, Roland, Meier, Beat H

“…Prion and nonprion forms of proteins are believed to differ solely in their three-dimensional structure, which is therefore of paramount importance for the…”
Get full text

Atomic-Resolution Three-Dimensional Structure of HET-s(218−289) Amyloid Fibrils by Solid-State NMR Spectroscopy by Van Melckebeke, Hélène, Wasmer, Christian, Lange, Adam, AB, Eiso, Loquet, Antoine, Böckmann, Anja, Meier, Beat H.

“…We present a strategy to solve the high-resolution structure of amyloid fibrils by solid-state NMR and use it to determine the atomic-resolution structure of…”
Get full text

Sequence-Specific Resonance Assignment of Soluble Nonglobular Proteins by 7D APSY-NMR Spectroscopy by Hiller, Sebastian, Wasmer, Christian, Wider, Gerhard, Wüthrich, Kurt

“…Based on sequence-specific resonance assignments, NMR is the method of choice for obtaining atomic-resolution experimental data on soluble nonglobular…”
Get full text

Protocols for the Sequential Solid-State NMR Spectroscopic Assignment of a Uniformly Labeled 25 kDa Protein: HET-s(1-227) by Schuetz, Anne, Wasmer, Christian, Habenstein, Birgit, Verel, René, Greenwald, Jason, Riek, Roland, Böckmann, Anja, Meier, Beat H

“…The sequence-specific resonance assignment of a protein forms the basis for studies of molecular structure and dynamics, as well as to functional assay studies…”
Get full text

Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion by Habenstein, Birgit, Wasmer, Christian, Bousset, Luc, Sourigues, Yannick, Schütz, Anne, Loquet, Antoine, Meier, Beat H., Melki, Ronald, Böckmann, Anja

“…We present the de novo resonance assignments for the crystalline 33 kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR…”
Get full text

The Molecular Organization of the Fungal Prion HET-s in Its Amyloid Form by Wasmer, Christian, Schütz, Anne, Loquet, Antoine, Buhtz, Carolin, Greenwald, Jason, Riek, Roland, Böckmann, Anja, Meier, Beat H.

“…The prion hypothesis states that it is solely the three-dimensional structure of the polypeptide chain that distinguishes the prion and nonprion forms of the…”
Get full text

Structural Similarity between the Prion Domain of HET-s and a Homologue Can Explain Amyloid Cross-Seeding in Spite of Limited Sequence Identity by Wasmer, Christian, Zimmer, Agnes, Sabaté, Raimon, Soragni, Alice, Saupe, Sven J., Ritter, Christiane, Meier, Beat H.

“…We describe a distant homologue of the fungal HET-s prion, which is found in the fungus Fusarium graminearum. The domain FgHET-s(218–289), which corresponds to…”
Get full text

Probing Water Accessibility in HET-s(218–289) Amyloid Fibrils by Solid-State NMR by Van Melckebeke, Hélène, Schanda, Paul, Gath, Julia, Wasmer, Christian, Verel, René, Lange, Adam, Meier, Beat H., Böckmann, Anja

“…Despite the importance of protein fibrils in the context of conformational diseases, information on their structure is still sparse. Hydrogen/deuterium…”
Get full text

Solid-State NMR Spectroscopy Reveals that E. coli Inclusion Bodies of HET-s(218-289) are Amyloids by Wasmer, Christian, Benkemoun, Laura, Sabaté, Raimon, Steinmetz, Michel O, Coulary-Salin, Bénédicte, Wang, Lei, Riek, Roland, Saupe, Sven J, Meier, Beat H

“…Protein deposition frequently occurs as inclusion bodies (IBs) during heterologous protein expression in E. coli. The structure of these E. coli IBs of the…”
Get full text

Prion Fibrils of Ure2p Assembled under Physiological Conditions Contain Highly Ordered, Natively Folded Modules by Loquet, Antoine, Bousset, Luc, Gardiennet, Carole, Sourigues, Yannick, Wasmer, Christian, Habenstein, Birgit, Schütz, Anne, Meier, Beat H., Melki, Ronald, Böckmann, Anja

“…The difference between the prion and the non-prion form of a protein is given solely by its three-dimensional structure, according to the prion hypothesis. It…”
Get full text

Infectious and Noninfectious Amyloids of the HET-s(218-289) Prion Have Different NMR Spectra by Wasmer, Christian, Soragni, Alice, Sabaté, Raimon, Lange, Adam, Riek, Roland, Meier, Beat H

“…The molecular basis for prion infectivity is not yet understood. The NMR spectra of noninfectious and infectious amyloids of the prion‐forming domain 218–289…”
Get full text

Combined Solid-State NMR and MD Characterization of the Stability and Dynamics of the HET-s(218-289) Prion in its Amyloid Conformation by Lange, Adam, Gattin, Zrinka, Van Melckebeke, Hélène, Wasmer, Christian, Soragni, Alice, van Gunsteren, Wilfred F, Meier, Beat H

“…Dynamic and rigid: The prion HET-s(218-289) consists, in its amyloid form as shown here, of highly ordered and rigid parts and a very dynamic loop, which could…”
Get full text

Contribution of Specific Residues of the [beta]-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability: e1004158 by Daskalov, Asen, Gantner, Matthias, Wälti, Marielle Aulikki, Schmidlin, Thierry, Chi, Celestine N, Wasmer, Christian, Schütz, Anne, Ceschin, Johanna, Clavé, Corinne, Cescau, Sandra, Meier, Beat, Riek, Roland, Saupe, Sven J

“…The [Het-s] prion of the fungus Podospora anserina represents a good model system for studying the structure-function relationship in amyloid proteins because…”
Get full text

Amyloid Fibrils of the HET-s(218-289) Prion Form a [beta] Solenoid with a Triangular Hydrophobic Core by Wasmer, Christian, Lange, Adam, Hélène Van Melckebeke, Siemer, Ansgar B, Riek, Roland, Meier, Beat H

“…Prion and nonprion forms of proteins are believed to differ solely in their three-dimensional structure, which is therefore of paramount importance for the…”
Get full text

Amyloids and Prions: structure, conformations and conformational transitions as seen by NMR by Meier, Beat H, Verel, Rene, Steinmetz, Michel, Siemer, Ansgar B, Köneke, Stephanie, Lange, Adam, Melckebeke, Helene, Wasmer, Christian, Ernst, Matthias

“…While, at the time of the writing of this , no atomic resolution structure of an amyloid fibril is available, considerable progress has been made towards this…”
Get full text

Infektiöse und nichtinfektiöse Amyloide des HET‐s(218‐289)‐Prions haben unterschiedliche NMR‐Spektren by Wasmer, Christian, Soragni, Alice, Sabaté, Raimon, Lange, Adam, Riek, Roland, Meier, Beat H.

“…Unterschiedliche Molekülstrukturen von bei pH 3 und bei physiologischen pH‐Werten gebildeten Fibrillen könnten nach den hier vorgestellten NMR‐Experimenten…”
Get full text

Festkörper‐NMR‐Spektroskopie zeigt: Die Einschlusskörperchen von HET‐s(218–289) in E. coli sind Amyloide by Wasmer, Christian, Benkemoun, Laura, Sabaté, Raimon, Steinmetz, Michel O., Coulary‐Salin, Bénédicte, Wang, Lei, Riek, Roland, Saupe, Sven J., Meier, Beat H.

“…Während der heterologen Expression von Proteinen in E. coli tritt häufig eine Proteinablagerung in Einschlusskörperchen (IBs) auf. Die Struktur der E.‐coli‐IBs…”
Get full text

Infektiöse und nichtinfektiöse Amyloide des HET-s(218-289)-Prions haben unterschiedliche NMR-Spektren by Wasmer, Christian, Soragni, Alice, Sabaté, Raimon, Lange, Adam, Riek, Roland, Meier, Beat H.

Get full text