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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 
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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 
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Isbel, L., Iskar, M., Durdu, S., Weiss, J., Grand, R. S., Hietter-Pfeiffer, E.,https://doi.org/10.1038/s41594-023-01021-8__Schübeler, D. (2023). Readout of histone methylation by Trim24 locally restricts chromatin opening by . Nature Structural &; Molecular Biology. Springer Nature.https://doi.org/10.1038/s41594-023-01021-8 
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Zens, B. (2023). Ultrastructural characterization of natively preserved extracellular matrix by cryo-electron tomography. Institute of Science and Technology Austria.https://doi.org/10.15479/at:ista:12491 
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Obr, M., Hagen, W. J. H., Dick, R. A., Yu, L., Kotecha, A., &; Schur, F. K. (2022). Exploring high-resolution cryo-ET and subtomogram averaging capabilities of contemporary DEDs. Journal of Structural Biology. Elsevier.https://doi.org/10.1016/j.jsb.2022.107852 
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Kampjut, D., &; Sazanov, L. A. (2022). Structure of respiratory complex I – An emerging blueprint for the mechanism. Current Opinion in Structural Biology. Elsevier.https://doi.org/10.1016/j.sbi.2022.102350 
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Gerle, C., Kishikawa, J., Yamaguchi, T., Nakanishi, A., Çoruh, M. O., Makino, F.,https://doi.org/10.1093/jmicro/dfac037__Kato, T. (2022). Structures of multisubunit membrane complexes with the CRYO ARM 200. Microscopy. Oxford University Press.https://doi.org/10.1093/jmicro/dfac037 
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Prattes, M., Grishkovskaya, I., Hodirnau, V.-V., Hetzmannseder, C., Zisser, G., Sailer, C.,https://doi.org/10.1038/s41594-022-00832-5__Bergler, H. (2022). Visualizing maturation factor extraction from the nascent ribosome by the AAA-ATPase Dr. Nature Structural &; Molecular Biology. Springer Nature.https://doi.org/10.1038/s41594-022-00832-5 
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Gisonno, R. A., Masson, T., Ramella, N. A., Barrera, E. E., Romanowski, V., &; Tricerri, M. A. (2022). Evolutionary and structural constraints influencing apolipoprotein AI amyloid behavior. Proteins: Structure, Function, and Bioinformatics. Wiley.https://doi.org/10.1002/prot.26217 
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Yelland, J. N., Bravo, J. P. K., Black, J. J., Taylor, D. W., &; Johnson, A. W. (2022). A single 2-O-methylation of ribosomal RNA gates assembly of a functional ribosome. Nature Structural &; Molecular Biology. Springer Nature.https://doi.org/10.1038/s41594-022-00891-8 
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Dimchev, G. A., Amiri, B., Fäßler, F., Falcke, M., &; Schur, F. K. (2021). Computational toolbox for ultrastructural quantitative analysis of filament networks in cryo-ET data. Journal of Structural Biology. Elsevier .https://doi.org/10.1016/j.jsb.2021.107808 
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Rampelt, H., Sucec, I., Bersch, B., Horten, P., Perschil, I., Martinou, J.-C.,https://doi.org/10.1186/s12915-019-0733-6__Pfanner, N. (2020). The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments. BMC Biology. Springer Nature.https://doi.org/10.1186/s12915-019-0733-6 
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Rosa, H. V. D., Leonardo, D. A., Brognara, G., Brandão-Neto, J., D’Muniz Pereira, H., Araújo, A. P. U., &; Garratt, R. C. (2020). Molecular recognition at septin interfaces: The switches hold the key. Journal of Molecular Biology. Elsevier.https://doi.org/10.1016/j.jmb.2020.09.001 
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Hafner, A. E., Krausser, J., &; Sari, A. (2019). Minimal coarse-grained models for molecular self-organisation in biology. Current Opinion in Structural Biology. Elsevier.https://doi.org/10.1016/j.sbi.2019.05.018 
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Bougault, C., Ayala, I., Vollmer, W., Simorre, J.-P., &; Schanda, P. (2019). Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100fkHz MAS frequency. Journal of Structural Biology. Elsevier.https://doi.org/10.1016/j.jsb.2018.07.009 
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Kurauskas, V., Hessel, A., Dehez, F., Chipot, C., Bersch, B., &; Schanda, P. (2018). Dynamics and interactions of AA in DPC are not functionally relevant. Nature Structural &; Molecular Biology. Springer Nature.https://doi.org/10.1038/s41594-018-0127-4 
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