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Troussicot, L., Vallet, A., Molin, M., Burmann, B. M., &; Schanda, P. (2023). Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR. Journal of the American Chemical Society. American Chemical Society.https://doi.org/10.1021/jacs.3c01200 

Gauto, D. F., Lebedenko, O. O., Becker, L. M., Ayala, I., Lichtenecker, R., Skrynnikov, N. R., &; Schanda, P. (2023). Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural Biology: X. Elsevier.https://doi.org/10.1016/j.yjsbx.2022.100079 

Degen, M., Santos, J. C., Pluhackova, K., Cebrero, G., Ramos, S., Jankevicius, G.,https://doi.org/10.1038/s41586-023-05991-z__Hiller, S. (2023). Structural basis of NINJ1-mediated plasma membrane rupture in cell death. Nature. Springer Nature.https://doi.org/10.1038/s41586-023-05991-z 

Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B.,https://doi.org/10.1002/anie.202304138__Schanda, P. (2023). Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by MagicAngleSpinning NMR spectroscopy of aromatic residues. Angewandte Chemie International Edition (Vol. 62). Wiley.https://doi.org/10.1002/anie.202304138 

Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B.,https://doi.org/10.1002/ange.202219314__Schanda, P. (2023). Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – MagicAngleSpinning NMR Spektroskopie von aromatischen Resten. Angewandte Chemie. Wiley.https://doi.org/10.1002/ange.202219314 

Sudec, I., &; Schanda, P. (2023). Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies. In S. Hiller, M. Liu, &; L. He (Eds.), Biophysics of Molecular Chaperones (Vol. 29, pp. 136–161). Royal Society of Chemistry.https://doi.org/10.1039/bk9781839165986-00136 

Napoli, F., Becker, L. M., &; Schanda, P. (2023). Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. Current Opinion in Structural Biology. Elsevier.https://doi.org/10.1016/j.sbi.2023.102660 

Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B.,https://doi.org/10.1002/anie.202219314__Schanda, P. (2023). The rigid core and flexible surface of amyloid fibrils probed by MagicAngle Spinning NMR of aromatic residues. Angewandte Chemie International Edition. Wiley.https://doi.org/10.1002/anie.202219314 

Gauto, D. F., Macek, P., Malinverni, D., Fraga, H., Paloni, M., Sudec, I.,https://doi.org/10.1038/s41467-022-29423-0__Schanda, P. (2022). Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR. Nature Communications. Springer Nature.https://doi.org/10.1038/s41467-022-29423-0 

Sudec, I., Bersch, B., &; Schanda, P. (2021). How do chaperones bind (partly) unfolded client proteins? Frontiers in Molecular Biosciences. Frontiers.https://doi.org/10.3389/fmolb.2021.762005