Schütz AK - Search Results

1

The conformation of the prion domain of Sup35p in isolation and in the full-length protein.

Luckgei N, Schütz AK, Bousset L, Habenstein B, Sourigues Y, Gardiennet C, Meier BH, Melki R, Böckmann A. Luckgei N, et al. Among authors: schutz ak. Angew Chem Int Ed Engl. 2013 Nov 25;52(48):12741-4. doi: 10.1002/anie.201304699. Epub 2013 Oct 9. Angew Chem Int Ed Engl. 2013. PMID: 24123863 No abstract available.

2

A sedimented sample of a 59 kDa dodecameric helicase yields high-resolution solid-state NMR spectra.

Gardiennet C, Schütz AK, Hunkeler A, Kunert B, Terradot L, Böckmann A, Meier BH. Gardiennet C, et al. Among authors: schutz ak. Angew Chem Int Ed Engl. 2012 Jul 27;51(31):7855-8. doi: 10.1002/anie.201200779. Epub 2012 Jun 27. Angew Chem Int Ed Engl. 2012. PMID: 22740125

3

Solid-state NMR sequential assignments of the amyloid core of Sup35pNM.

Luckgei N, Schütz AK, Habenstein B, Bousset L, Sourigues Y, Melki R, Meier BH, Böckmann A. Luckgei N, et al. Among authors: schutz ak. Biomol NMR Assign. 2014 Oct;8(2):365-70. doi: 10.1007/s12104-013-9518-y. Epub 2013 Aug 10. Biomol NMR Assign. 2014. PMID: 23934139

4

Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded modules.

Loquet A, Bousset L, Gardiennet C, Sourigues Y, Wasmer C, Habenstein B, Schütz A, Meier BH, Melki R, Böckmann A. Loquet A, et al. J Mol Biol. 2009 Nov 20;394(1):108-18. doi: 10.1016/j.jmb.2009.09.016. Epub 2009 Sep 11. J Mol Biol. 2009. PMID: 19748512

5

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

Habenstein B, Wasmer C, Bousset L, Sourigues Y, Schütz A, Loquet A, Meier BH, Melki R, Böckmann A. Habenstein B, et al. J Biomol NMR. 2011 Nov;51(3):235-43. doi: 10.1007/s10858-011-9530-4. Epub 2011 Jul 31. J Biomol NMR. 2011. PMID: 21805376

6

The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218-289): a solid-state NMR study.

Gowda C, Zandomeneghi G, Zimmermann H, Schütz AK, Böckmann A, Ernst M, Meier BH. Gowda C, et al. Among authors: schutz ak. J Biomol NMR. 2017 Dec;69(4):207-213. doi: 10.1007/s10858-017-0148-z. Epub 2017 Nov 1. J Biomol NMR. 2017. PMID: 29094285

7

The amyloid-Congo red interface at atomic resolution.

Schütz AK, Soragni A, Hornemann S, Aguzzi A, Ernst M, Böckmann A, Meier BH. Schütz AK, et al. Angew Chem Int Ed Engl. 2011 Jun 20;50(26):5956-60. doi: 10.1002/anie.201008276. Epub 2011 May 17. Angew Chem Int Ed Engl. 2011. PMID: 21591034 No abstract available.

8

Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.

Schütz AK, Habenstein B, Luckgei N, Bousset L, Sourigues Y, Nielsen AB, Melki R, Böckmann A, Meier BH. Schütz AK, et al. Biomol NMR Assign. 2014 Oct;8(2):349-56. doi: 10.1007/s12104-013-9515-1. Epub 2013 Aug 14. Biomol NMR Assign. 2014. PMID: 23943018

9

Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.

Schütz AK, Vagt T, Huber M, Ovchinnikova OY, Cadalbert R, Wall J, Güntert P, Böckmann A, Glockshuber R, Meier BH. Schütz AK, et al. Angew Chem Int Ed Engl. 2015 Jan 2;54(1):331-5. doi: 10.1002/anie.201408598. Epub 2014 Nov 13. Angew Chem Int Ed Engl. 2015. PMID: 25395337 Free PMC article.

10

Prion Amyloid Polymorphs - The Tag Might Change It All.

Bousset L, Luckgei N, Kabani M, Gardiennet C, Schütz AK, Melki R, Meier BH, Böckmann A. Bousset L, et al. Among authors: schutz ak. Front Mol Biosci. 2020 Aug 6;7:190. doi: 10.3389/fmolb.2020.00190. eCollection 2020. Front Mol Biosci. 2020. PMID: 32850974 Free PMC article.

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