Schütz lab publications

34	Chen, Wu, Holzinger, Götz, Didier, Schütz, Schneider, Kielkowski. Aryl Radicals Generated from Aryl Pinacol Boronates Modify Peptides and Proteins. Eur. J. Org. Chem. (2024).
33	Szanto, Dietschreit, Shein, Schuetz, Ochsenfeld. A systematic QM/MM study for predicting 31P NMR chemical shifts of adenosine nucleotides in solution and stages of ATP hydrolysis in a protein environment Journal of Chemical Theory and Computation (2024).
32	Shein, Hitzenberger, Cheng, Rout, Leitl, Sato, Zacharias, Sakata, Schütz. Unravelling ATP processing by the AAA+ protein p97 at the atomic level. Nature Chemistry (2024). News & Views. Free access link.
31	Su, Harati Taji, Kosinska, Oz, Xie, Bielytskyi, Shein, Hagen, Esmaeili, Steiger, Protzer, Schütz. Introducing adjuvant-loaded particulate hepatitis B core antigen as an alternative therapeutic hepatitis B vaccine component. Journal of Hepatology reports (2023).
30	Wadenpohl, Shein, Lehmann, Schütz, Jung. Economical large-scale purification of extracellular vesicles from urine. Separation and Purification Technology (2023).
29	Harati Taji, Bielytskyi, Shein, Sani, Seitz, Schütz. Transient RNA interactions leave a covalent imprint on a viral capsid protein. Journal of the American Chemical Society (2022).
28	Albanese, Chen, Hüls, Gärtner, Tagawa, Mejias-Perez, Keppler, Göbel, Zeidler, Shein, Schütz, Hammerschmidt. MicroRNAs are minor constituents of extracellular vesicles that are rarely delivered to target cells. Plos Genetics (2021).
27	Schütz. Solid-state NMR approaches to investigate large enzymes in complex with substrates and inhibitors. Biochem Soc Trans (2021).
26	Jung, Jacobs, Shein, Schütz, Mohr, Stadler, Stadler, Lucko, Altstetter, Wilsch, Deng, Protzer. Efficient and reproducible depletion of hepatitis B virus from plasma derived extracellular vesicles. J. Extracell. Vesicles (2020).
25	Rydzek, Shein, Bielytskyi, Schütz. Observation of a transient reaction intermediate illuminates the mechanochemical cycle of the AAA-ATPase p97. J. Am. Chem. Soc. (2020).
24	Bousset, Luckgei, Kabani, Gardiennet, Schütz, Melki, Meier, Böckmann. Prion Amyloid Polymorphs -the Tag Might Change It All. Front Mol Biosci (2020).
23	Seitz, Habjanic, Schütz, Bartenschlager. The Hepatitis B Virus Envelope Proteins: Molecular Gymnastics Throughout the Viral Life Cycle. Annu. Rev. Virology (2020).
22	Jung, Altstetter, Wilsch, Shein, Schütz, Protzer. Extracellular vesicles derived from Hepatitis-D Virus infected cells induce a proinflammatory cytokine response in human peripheral blood mononuclear cells and macrophages. Matters (2020).
21	Schuetz, Hornemann, Wälti, Greuter, Tiberi, Cadalbert, Ganter, Riek, Hammarström, Nilsson, Böckmann, Aguzzi, Meier. Binding of polythiophenes to amyloids: structural mapping of the pharmacophore. ACS Chem. Neurosci. (2018).
20	Gowda, Zandomeneghi, Zimmermann, Schütz, Böckmann, Ernst, Meier. The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218-289): A solid-state NMR study. Journal of Biomolecular NMR (2017).
19	Schütz, Rennella, Kay. Exploiting conformational plasticity in the AAA+ protein VCP/p97 to modify function. Proc Natl Acad Sci U S A (2017).
18	Schütz, Kay. A Dynamic Molecular Basis for Malfunction in Disease Mutants of p97/VCP. eLife (2016).
17	Rennella, Schuetz, Kay. Quantitative measurement of exchange dynamics in proteins via ¹³C relaxation dispersion of ¹³CHD₂-labeled samples. Journal of Biomolecular NMR (2016).
16	Herrmann, Schütz, Shirani, Huang, Saban, Nuvolone, Li, Ballmer, Åslund, Mason, Rushing, Budka, Nyström, Hammarström, Böckmann, Caflisch, Meier, Nilsson, Hornemann, Aguzzi. Structure-based drug design identifies polythiophenes as antiprion compounds. Science Translational Medicine (2015).
15	Schütz, Vagt, Huber, Ovchinnikova, Cadalbert, Wall, Güntert, Böckmann, Glockshuber, Meier. Atomic-resolution three-dimensional structure of amyloid fibrils bearing the Osaka mutation. Angewandte Chemie (2015).
14	Huber, Ovchinnikova, Schütz, Glockshuber, Meier, Böckmann. Solid-state NMR sequential assignment of Osaka-mutant amyloid-β (Aβ1-40 E22Δ) fibrils. Biomolecular NMR Assignments (2015).
13	Daskalov, Gantner, Wälti, Schmidlin, Chi, Wasmer, Schütz, Ceschin, Clavé, Cescau, Meier, Riek, Saupe. Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability. PLoS Biology (2015).
12	Luckgei, Schütz, Habenstein, Bousset, Sourigues, Melki, Meier, Böckmann. Solid-state NMR sequential assignments of the amyloid core of Sup35pNM. Biomolecular NMR Assignments (2014).
11	Schütz, Habenstein, Luckgei, Bousset, Sourigues, Nielsen, Melki, Böckmann, Meier. Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p. Biomolecular NMR Assignments (2014).
10	Luckgei, Schütz, Bousset, Habenstein, Sourigues, Gardiennet, Meier, Melki, Böckmann. The conformation of the prion domain of Sup35p in isolation and in the full-length protein. Angewandte Chemie (2013).
9	Gardiennet, Schütz, Hunkeler, Kunert, Terradot, Böckmann, Meier. A Sedimented Sample of a 59 kDa Dodecameric Helicase Yields High-Resolution Solid-State NMR Spectra. Angewandte Chemie (2012).
8	Habenstein, Wasmer, Bousset, Sourigues, Schütz, Loquet, Meier, Melki, Böckmann. Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion. Journal of Biomolecular NMR (2011).
7	Schütz, Soragni, Hornemann, Aguzzi, Ernst, Böckmann, Meier. The amyloid-Congo red interface at atomic resolution. Angewandte Chemie (2011).
6	Schütz, Wasmer, Habenstein, Verel, Greenwald, Riek, Böckmann, Meier. Protocols for the sequential solid-state NMR assignment of a uniformly labeled 25 kDa protein: HET-s(1-227). Chembiochem (2010).
5	Loquet, Bousset, Gardiennet, Sourigues, Wasmer, Habenstein, Schütz, Meier, Melki, Böckmann. Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded modules. Journal of Molecular Biology (2009).
4	Wasmer, Schütz, Loquet, Buhtz, Greenwald, Riek, Böckmann, Meier. The molecular organization of the fungal prion HET-s in its amyloid form. Journal of Molecular Biology (2009).
3	Schuetz, Murakami, Takada, Junker, Hashimoto, Griesinger. RDC-enhanced NMR spectroscopy in structure elucidation of sucro-neolambertellin. Angewandte Chemie (2008).
2	Schuetz, Junker, Leonov, Lange, Molinski, Griesinger. Stereochemistry of sagittamide A from residual dipolar coupling enhanced NMR. Journal of the American Chemical Society (2007).
1	Scharge, Cézard, Zielke, Schütz, Emmeluth, Suhm, A peptide co-solvent under scrutiny: self-aggregation of 2,2,2-trifluoroethanol. Phys Chem Chem Phys (2007).

Google Scholar:

https://scholar.google.ca/citations?user=YKIyUU0AAAAJ&hl=en

ORCID

https://orcid.org/0000-0001-6398-5757

ResearcherID

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