2024-2025
243) Schulz, V*., Steinhilper, R.*, Oltmanns, J.*, Freibert, S.-A., Krapoth, N., Linne, U., Welsch, S., Hoock, M.H., Schünemann, V., Murphy, B.J.#, & Lill, R.# (2024). Mechanism and structural dynamics of sulfur transfer during de novo [2Fe-2S] cluster assembly on ISCU2. Nat. Commun. 15, 3269. * Joint first authors; # joint corresponding authors.
244) Braymer, J.J.*, Stehling, O.*, Stümpfig, M., Rösser, R., Spantgar, F., Blinn, C.M., Mühlenhoff, U., Pierik, A.J., & Lill, R. (2024). Requirements for the biogenesis of [2Fe-2S] proteins in the human and yeast cytosol. Proc. Natl. Acad. Sci. U.S.A. 121, e2400740121. * Joint first authors.
245) Peña-Diaz, P.*, Braymer, J.J.*, Vacek, V., Zelená, M., Lometto, S., Mais, C.N., Hrdý, I., Treitli, S.C., Hochberg, G.K.A., Py, B., Lill, R., & Hampl, V. (2024). Characterization of the SUF FeS cluster synthesis machinery in the amitochondriate eukaryote Monocercomonoides exilis. Curr. Biol. 34, 3855-3865. * Joint first authors. Commentary by Lawton, M. & Gawryluk, R.M.R. (2024) Curr. Biol. 34, R823–R826.
246) Lill, R. (2024). Iron-sulfur protein biogenesis in eukaryotes: How all starts. Online-Seminar in the International Biometals Webinars. doi: 10.52843/cassyni.k12ng4
247) Steinhilper, R., Boß, L., Freibert, S.-A., Schulz, V., Krapoth, N., Kaltwasser, S., Lill, R.,#, & Murphy, B.# (2024). Structural evidence for two-stage binding of mitochondrial ferredoxin 2 to the core iron-sulfur cluster assembly complex. Nat. Commun. 15, 10559. # Joint corresponding authors. doi: 10.1038/s41467-024-54585-4.
248) Lill, R. & Barras, F. (2024). Editorial for Special Issue on "Biogenesis and function Iron‑sulfur proteins". Biochim Biophys Acta Mol Cell Res. 25, 119867. doi: 10.1016/j.bbamcr.2024.119867
249) Boß, L., Stehling, O., Elsässer, H.-P., & Lill, R. (2025). Crucial role and conservation of the three [2Fe-2S] clusters in the human mitochondrial ribosome. J. Biol. Chem. 301, 108087. doi: 10.1016/j.jbc.2024.108087
250) Lill, R. (2025). Mitochondriale und zytosolische Systeme der Eisen-Schwefel-Proteinbiogenese. Biospektrum 31, 18-22.
251) Mühlenhoff, U.#, Trauth, D., Śliwińska, W., Boss, L., & Lill, R.# (2025). The cytochrome oxidase defect in ISC-depleted yeast is caused by impaired iron-sulfur cluster maturation of the mitoribosome assembly factor Rsm22. FEBS Lett. 599, 2301-2317. # Joint corresponding authors. doi: 10.1002/1873-3468.70129
252) Zangari, J.*, Stehling, O.*, Freibert, S.-A., Bhattacharya, K., Rouaud, F., Serre-Beinier, V., Maundrell, K., Montessuita, S., Ferre, S.M., Vartholomaiou, E., Schulz, V., Zuhra, K., González-Ruiz, V., Hanschke, S., Tsukamoto, T., Cerezo, M., Szabo, C., Rudaz, S., Boniecki, M.T., Cygler, M., Lill, R.,# & Martinou, J.-C.# (2025). D-Cysteine impairs tumour growth by inhibiting cysteine desulfurase NFS1. Nat. Metabol. 7, 1646–1662. * Joint first authors, # joint corresponding authors. doi: 10.1038/s42255-025-01339-1
253) Heger, L.M.*, Kertess, L.*, Kaufhold, C., Gubinelli, F., Cardona-Alberich, A., Özata, G., Müller, S.A., Tschirner, S.K., Stehling, O., Schifferer, M., Peron, C., Tiranti, V., Lill, R., Iuso, A., Zecca, L., Strupp, M., Oertel, W., Lichtenthaler, S.F., & Burbulla, L.F. (2025). Patient-derived neurons reveal α-synuclein pathology and previously unrecognized MHC-I elevation in Mitochondrial Membrane Protein–Associated Neurodegeneration. Mov. Disord. xxx, in press. * Joint first authors. doi:10.1002/mds.70029.
254) Mühlenhoff, M., Stehling, O., & Lill, R. (2025). Biogenesis of mitochondrial iron-sulfur proteins. In: “Iron-Sulfur Cluster Biogenesis and Biochemistry”. Leimkühler, S. (ed.), Wiley Publishers.