Napoli, F., Guan, J.-Y., Arnaud, C.-A., Macek, P., Fraga, H., Breyton, C., &; Schanda, P. (2024). Deuteration of proteins boosted by cell lysates: High-resolution amide and Ha magic-angle-spinning (MAS) NMR without the reprotonation bottleneck. Magnetic Resonance. Copernicus Publications.https://doi.org/10.5194/mr-5-33-2024 
LibreCat: https://research-explorer.ista.ac.at/record/15401
DOI: 10.5194/mr-5-33-2024

Schanda, P. (2024). Raw data to “MAS NMR experiments of corynebacterial cell walls: complementary 1H- and CPMAS CryoProbe-enhanced 13C-detected experiments.”https://doi.org/10.15479/AT:ISTA:17042__ISTA.https://doi.org/10.15479/AT:ISTA:17042 
LibreCat: https://research-explorer.ista.ac.at/record/17042
DOI: 10.15479/AT:ISTA:17042

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 
LibreCat: https://research-explorer.ista.ac.at/record/13095
DOI: 10.1021/jacs.3c01200
WoS: 000985907400001
PMID: 37140345

Schanda, P. (2023). Research data of the publication “Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR.”https://doi.org/10.15479/AT:ISTA:12820__Institute of Science and Technology Austria.https://doi.org/10.15479/AT:ISTA:12820 
LibreCat: https://research-explorer.ista.ac.at/record/12820
DOI: 10.15479/AT:ISTA:12820

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 
LibreCat: https://research-explorer.ista.ac.at/record/12114
DOI: 10.1016/j.yjsbx.2022.100079
PMID: 36578472

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 
LibreCat: https://research-explorer.ista.ac.at/record/13096
DOI: 10.1038/s41586-023-05991-z
WoS: 000991386800011

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 
LibreCat: https://research-explorer.ista.ac.at/record/14861
DOI: 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 
LibreCat: https://research-explorer.ista.ac.at/record/14835
DOI: 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 
LibreCat: https://research-explorer.ista.ac.at/record/14847
DOI: 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 
LibreCat: https://research-explorer.ista.ac.at/record/14036
DOI: 10.1016/j.sbi.2023.102660
WoS: 001053616200001
PMID: 37536064

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 
LibreCat: https://research-explorer.ista.ac.at/record/12675
DOI: 10.1002/anie.202219314
WoS: 000956919900001
PMID: 36738230

Becker, L. M., &; Schanda, P. (2023). Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues. Institute of Science and Technology Austria.https://doi.org/10.15479/AT:ISTA:12497 
LibreCat: https://research-explorer.ista.ac.at/record/12497
DOI: 10.15479/AT:ISTA:12497

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 
LibreCat: https://research-explorer.ista.ac.at/record/11179
DOI: 10.1038/s41467-022-29423-0
WoS: 000781498700009

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 
LibreCat: https://research-explorer.ista.ac.at/record/10323
DOI: 10.3389/fmolb.2021.762005
WoS: 000717241700001
PMID: 34760928