Publications

[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. ACS Chem. Neurosci.9(3), 475–481 (2018).

[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. Journal of Biomolecular NMR 69(4), 207-213 (2017).

[19]        Schütz A.K., Rennella, E., Kay, L.E. Exploiting conformational plasticity in the AAA+ protein VCP/p97 to modify function. Proc Natl Acad Sci U S A, 114(33), E6822-E6829 (2017).

[18]       Schütz, A.K., Kay, L.E. A Dynamic Molecular Basis for Malfunction in Disease Mutants of p97/VCP. eLife, 5 (2016).

[17]       Rennella, E., Schuetz A.K., Kay, L.E. Quantitative measurement of exchange dynamics in proteins via 13C relaxation dispersion of 13CHD2-labeled samples. Journal of Biomolecular NMR 65(2), 59-64 (2016).

[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. Science Translational Medicine 7(299):299ra123 (2015).

[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. Angewandte Chemie 54(1), 331-5 (2015).

[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-beta (A?1-40 E22?) fibrils. Biomolecular NMR Assignments, 9(1),7-14 (2015).

[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. PLoS Biology 13(2) (2015).

[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. Biomolecular NMR Assignments 8(2), 365-70 (2014).

[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. Biomolecular NMR Assignments 8(2), 349-56 (2014).

[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. Angewandte Chemie 52(48),12741-4 (2013).

[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. Angewandte Chemie, 51(31), 7855-8 (2012).

[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. Journal of Biomolecular NMR 51(3), 235-43 (2011).

[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. Angewandte Chemie, 50(26), 5956-60 (2011).

[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). Chembiochem 11(11), 1543-1551 (2010).

[5]        Loquet, A., Bousset, L., Gardiennet, C., Sourigues, Y., Wasmer, C., Habenstein, B., Schütz, A., Meier, B. H., Melki, R., and Böckmann, A. Prion ?brils of Ure2p assembled under physiological conditions contain highly ordered, natively folded modules. Journal of Molecular Biology 394(1), 108-118 (2009).

[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. Journal of Molecular Biology 394(1), 119-127 (2009).

[3]        Schuetz, A., Murakami, T., Takada, N., Junker, J., Hashimoto, M., and Griesinger, C. RDC-enhanced NMR spectroscopy in structure elucidation of sucro-neolambertellin. Angewandte Chemie 47(11), 2032-4 (2008).

[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. Phys Chem Chem Phys 9(32), 4472-90 (2007).

 

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http://www.researcherid.com/rid/E-4073-2017