12 citations as recorded by crossref.

1. Streamlining NMR Chemical Shift Predictions for Intrinsically Disordered Proteins: Design of Ensembles with Dimensionality Reduction and Clustering M. Bakker et al. https://doi.org/10.1021/acs.jcim.4c00809
2. Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins S. Maiti et al. https://doi.org/10.1016/j.crstbi.2024.100138
3. Selective1HαNMR Methods Reveal Functionally Relevant Prolinecis/transIsomers in Intrinsically Disordered Proteins: Characterization of Minor Forms, Effects of Phosphorylation, and Occurrence in Proteome F. Sebák et al. https://doi.org/10.1002/anie.202108361
4. Introduction to “Geoffrey Bodenhausen Festschrift” D. Abergel & F. Ferrage https://doi.org/10.5194/mr-4-111-2023
5. NMR in the Age of Modern Biomedical Research and Drug Discovery X. Lu et al. https://doi.org/10.1016/j.jmb.2025.169302
6. Time-resolved NMR detection of prolyl-hydroxylation in intrinsically disordered region of HIF-1α W. He et al. https://doi.org/10.1073/pnas.2408104121
7. IDRs in Cross-Membrane Transport: Regulation of Ion Channels and Transporters, Mechanistic Studies Made Possible by NMR and Computational Methods O. Vinogradova https://doi.org/10.3389/frbis.2026.1804302
8. Optimal 13C NMR investigation of intrinsically disordered proteins at 1.2 GHz M. Schiavina et al. https://doi.org/10.1038/s41596-023-00921-9
9. Selective1HαNMR Methods Reveal Functionally Relevant Prolinecis/transIsomers in Intrinsically Disordered Proteins: Characterization of Minor Forms, Effects of Phosphorylation, and Occurrence in Proteome F. Sebák et al. https://doi.org/10.1002/ange.202108361
10. 13C Direct Detected NMR for Challenging Systems I. Felli & R. Pierattelli https://doi.org/10.1021/acs.chemrev.1c00871
11. Intrinsically disordered proteins studied by NMR spectroscopy M. Schiavina et al. https://doi.org/10.1016/j.jmro.2023.100143
12. Direct 15N–13C Heteronuclear Correlation Spectroscopy Enhanced by Spin-Lock-Induced Crossing and Reversible Parahydrogen Exchange D. Markelov et al. https://doi.org/10.1021/acs.jpclett.6c01774