Wälti MA - 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: walti ma. 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

Towards a true protein movie: a perspective on the potential impact of the ensemble-based structure determination using exact NOEs.

Vögeli B, Orts J, Strotz D, Chi C, Minges M, Wälti MA, Güntert P, Riek R. Vögeli B, et al. Among authors: walti ma. J Magn Reson. 2014 Apr;241:53-9. doi: 10.1016/j.jmr.2013.11.016. J Magn Reson. 2014. PMID: 24656080 Review.

3

Solution NMR studies of recombinant Aβ(1-42): from the presence of a micellar entity to residual β-sheet structure in the soluble species.

Wälti MA, Orts J, Vögeli B, Campioni S, Riek R. Wälti MA, et al. Chembiochem. 2015 Mar 2;16(4):659-69. doi: 10.1002/cbic.201402595. Epub 2015 Feb 11. Chembiochem. 2015. PMID: 25676345

4

NMR-Based Determination of the 3D Structure of the Ligand-Protein Interaction Site without Protein Resonance Assignment.

Orts J, Wälti MA, Marsh M, Vera L, Gossert AD, Güntert P, Riek R. Orts J, et al. Among authors: walti ma. J Am Chem Soc. 2016 Apr 6;138(13):4393-400. doi: 10.1021/jacs.5b12391. Epub 2016 Mar 23. J Am Chem Soc. 2016. PMID: 26943491

5

Solid-state NMR sequential assignment of an Amyloid-β(1-42) fibril polymorph.

Ravotti F, Wälti MA, Güntert P, Riek R, Böckmann A, Meier BH. Ravotti F, et al. Among authors: walti ma. Biomol NMR Assign. 2016 Oct;10(2):269-76. doi: 10.1007/s12104-016-9682-y. Epub 2016 May 10. Biomol NMR Assign. 2016. PMID: 27165577

6

Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.

Wälti MA, Ravotti F, Arai H, Glabe CG, Wall JS, Böckmann A, Güntert P, Meier BH, Riek R. Wälti MA, et al. Proc Natl Acad Sci U S A. 2016 Aug 23;113(34):E4976-84. doi: 10.1073/pnas.1600749113. Epub 2016 Jul 28. Proc Natl Acad Sci U S A. 2016. PMID: 27469165 Free PMC article.

7

Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ(1-42) amyloid polymorph.

Wälti MA, Orts J, Riek R. Wälti MA, et al. PLoS One. 2017 Mar 20;12(3):e0172862. doi: 10.1371/journal.pone.0172862. eCollection 2017. PLoS One. 2017. PMID: 28319116 Free PMC article.

8

Fast NMR-Based Determination of the 3D Structure of the Binding Site of Protein-Ligand Complexes with Weak Affinity Binders.

Wälti MA, Riek R, Orts J. Wälti MA, et al. Angew Chem Int Ed Engl. 2017 May 2;56(19):5208-5211. doi: 10.1002/anie.201612304. Epub 2017 Apr 7. Angew Chem Int Ed Engl. 2017. PMID: 28387455

9

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. Among authors: walti ma. 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

10

The three-dimensional structure of human β-endorphin amyloid fibrils.

Seuring C, Verasdonck J, Gath J, Ghosh D, Nespovitaya N, Wälti MA, Maji SK, Cadalbert R, Güntert P, Meier BH, Riek R. Seuring C, et al. Among authors: walti ma. Nat Struct Mol Biol. 2020 Dec;27(12):1178-1184. doi: 10.1038/s41594-020-00515-z. Epub 2020 Oct 12. Nat Struct Mol Biol. 2020. PMID: 33046908

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