Publications
27 |
Schütz, A.K. Solid-state NMR approaches to investigate large enzymes in complex with substrates and inhibitors. |
26 |
Jung, S., Jacobs, K. F. K., Shein, M., Schütz, A. K., Mohr, F., Stadler, H., Stadler, D., Lucko, A. M., Altstetter, S. M., Wilsch, F., Deng, L., Protzer, U. Efficient and reproducible depletion of hepatitis B virus from plasma derived extracellular vesicles. |
25 |
Rydzek, S., Shein, M. , Bielytskyi, P., Schütz, A.K. Observation of a transient reaction intermediate illuminates the mechanochemical cycle of the AAA-ATPase p97. |
24 |
Bousset, L.; Luckgei, N.; Kabani, M.; Gardiennet, C.; Schütz, A.; Melki, R.; Meier, B.; Böckmann, A. Prion Amyloid Polymorphs -the Tag Might Change It All. |
23 |
Seitz, S., Habjanic, J., Schütz, A.K., Bartenschlager, R. The Hepatitis B Virus Envelope Proteins: Molecular Gymnastics Throughout the Viral Life Cycle. |
22 |
Jung, S., Altstetter, S.M., Wilsch, F., Shein, M., Schütz, A.K., Protzer, U. Extracellular vesicles derived from Hepatitis-D Virus infected cells induce a proinflammatory cytokine response in human peripheral blood mononuclear cells and macrophages. |
21 |
Schuetz A.K., Hornemann, S., Wälti, M.A., Greuter, L., Tiberi, C., Cadalbert, R., Ganter, M., Riek, R., Hammarström, P., Nilsson, K.P.R., Böckmann, A., Aguzzi, A.A., Meier, B.H. Binding of polythiophenes to amyloids: structural mapping of the pharmacophore. |
20 | Gowda, C., Zandomeneghi G., Zimmermann, H., Schütz, A.K., Böckmann, A., Ernst, M., Meier, B.H. The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218-289): A solid-state NMR study. |
19 |
Schütz A.K., Rennella, E., Kay, L.E. Exploiting conformational plasticity in the AAA+ protein VCP/p97 to modify function. |
18 |
Schütz, A.K., Kay, L.E. A Dynamic Molecular Basis for Malfunction in Disease Mutants of p97/VCP. |
17 |
Rennella, E., Schuetz A.K., Kay, L.E. Quantitative measurement of exchange dynamics in proteins via 13C relaxation dispersion of 13CHD2-labeled samples. |
16 | Herrmann, U.S., Schütz, A.K., Shirani, H., Huang, D., Saban, D., Nuvolone, M., Li, B., Ballmer, B., Åslund, A.K., Mason, J.J., Rushing, E., Budka, H., Nyström, S., Hammarström, P., Böckmann, A., Caflisch, A., Meier, B.H., Nilsson, K.P., Hornemann, S., Aguzzi, A. Structure-based drug design identifies polythiophenes as antiprion compounds. |
15 |
Schütz, A.K., Vagt, T., Huber, M., Ovchinnikova, O.Y., Cadalbert, R., Wall, J., Güntert, P., Böckmann, A., Glockshuber, R., Meier, B.H. Atomic-resolution three-dimensional structure of amyloid fibrils bearing the Osaka mutation. |
14 |
Huber, M., Ovchinnikova, O.Y., Schütz, A.K., Glockshuber, R., Meier, B.H., Böckmann, A. Solid-state NMR sequential assignment of Osaka-mutant amyloid-β (Aβ1-40 E22Δ) fibrils. |
13 |
Daskalov, A., Gantner, M., Wälti, M.A., Schmidlin. T., Chi, C.N., Wasmer, C., Schütz, A., Ceschin, J., Clavé. C., Cescau, S., Meier, B., Riek, R., Saupe, S.J. Contribution of specific residues of the ?-solenoid fold to HET-s prion function, amyloid structure and stability. |
12 |
Luckgei, N., Schütz, A.K., Habenstein. B., Bousset. L., Sourigues. Y., Melki, R., Meier, B.H., Böckmann, A. Solid-state NMR sequential assignments of the amyloid core of Sup35pNM. |
11 |
Schütz, A.K., Habenstein, B., Luckgei, N., Bousset, L., Sourigues, Y., Nielsen, A.B., Melki, R., Böckmann, A., Meier, B.H. Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p. |
10 |
Luckgei, N., Schütz, A.K., Bousset L., Habenstein, B., Sourigues, Y., Gardiennet, C., Meier, B.H., Melki, R., Böckmann, A. The conformation of the prion domain of Sup35p in isolation and in the full-length protein. |
9 |
Gardiennet, C., Schütz, A.K., Hunkeler, A., Kunert, B., Terradot, L., Böckmann, A, and Meier, B.H. A Sedimented Sample of a 59 kDa Dodecameric Helicase Yields High-Resolution Solid-State NMR Spectra. |
8 |
Habenstein, B., Wasmer, C., Bousset, L., Sourigues, Y., Schütz, A., Loquet, A., Meier, B.H, Melki, R., and Böckmann, A. Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion. |
7 |
Schütz, A.K., Soragni, A., Hornemann, S., Aguzzi, A., Ernst, M., Böckmann, A., and Meier, B.H. The amyloid-Congo red interface at atomic resolution. |
6 |
Schütz, A., Wasmer, C., Habenstein, B., Verel, R., Greenwald, J., Riek, R., Böckmann, A., and Meier, B. H. Protocols for the sequential solid-state NMR assignment of a uniformly labeled 25 kDa protein: HET-s(1-227). |
5 |
Loquet, A., Bousset, L., Gardiennet, C., Sourigues, Y., Wasmer, C., Habenstein, B., Schütz, A., Meier, B. H., Melki, R., and Böckmann, A. Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded modules. |
4 |
Wasmer, C., Schütz, A., Loquet, A., Buhtz, C., Greenwald, J., Riek, R., Böckmann, A., and Meier, B. H. The molecular organization of the fungal prion HET-s in its amyloid form. |
3 |
Schuetz, A., Murakami, T., Takada, N., Junker, J., Hashimoto, M., and Griesinger, C. RDC-enhanced NMR spectroscopy in structure elucidation of sucro-neolambertellin. |
2 |
Schuetz, A., Junker, J., Leonov, A., Lange, O.F., Molinski, T.F., and Griesinger, C. Stereochemistry of sagittamide A from residual dipolar coupling enhanced NMR. Journal of the American Chemical Society 129(49), 15114-5 (2007). |
1 |
Scharge, T., Cézard, C., Zielke, P., Schütz, A., Emmeluth, C., and Suhm, M.A. A peptide co-solvent under scrutiny: self-aggregation of 2,2,2-trifluoroethanol. |
Google Scholar
https://scholar.google.ca/citations?user=YKIyUU0AAAAJ&hl=en
ORCID
http://orcid.org/0000-0001-6398-5757
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