Schütz A - Search Results

1

Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.

Daskalov A, Gantner M, Wälti MA, Schmidlin T, Chi CN, Wasmer C, Schütz A, Ceschin J, Clavé C, Cescau S, Meier B, Riek R, Saupe SJ. Daskalov A, et al. Among authors: schutz a. PLoS Pathog. 2014 Jun 12;10(6):e1004158. doi: 10.1371/journal.ppat.1004158. eCollection 2014 Jun. PLoS Pathog. 2014. PMID: 24945274 Free PMC article.

2

The molecular organization of the fungal prion HET-s in its amyloid form.

Wasmer C, Schütz A, Loquet A, Buhtz C, Greenwald J, Riek R, Böckmann A, Meier BH. Wasmer C, et al. Among authors: schutz a. J Mol Biol. 2009 Nov 20;394(1):119-27. doi: 10.1016/j.jmb.2009.09.015. Epub 2009 Sep 11. J Mol Biol. 2009. PMID: 19748509

3

Binding of Polythiophenes to Amyloids: Structural Mapping of the Pharmacophore.

Schütz AK, Hornemann S, Wälti MA, Greuter L, Tiberi C, Cadalbert R, Gantner M, Riek R, Hammarström P, Nilsson KPR, Böckmann A, Aguzzi A, Meier BH. Schütz AK, et al. ACS Chem Neurosci. 2018 Mar 21;9(3):475-481. doi: 10.1021/acschemneuro.7b00397. Epub 2017 Dec 4. ACS Chem Neurosci. 2018. PMID: 29178774

4

Solid-state NMR sequential assignment of Osaka-mutant amyloid-beta (Aβ1-40 E22Δ) fibrils.

Huber M, Ovchinnikova OY, Schütz AK, Glockshuber R, Meier BH, Böckmann A. Huber M, et al. Among authors: schutz ak. Biomol NMR Assign. 2015 Apr;9(1):7-14. doi: 10.1007/s12104-013-9535-x. Epub 2014 Jan 7. Biomol NMR Assign. 2015. PMID: 24395155

5

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.

6

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. Among authors: schutz a. 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

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

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. Among authors: schutz a. 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

9

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

10

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

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