Biaek, M. J., &; Klajn, R. (2019). Diamond grows up. Chem. Elsevier.https://doi.org/10.1016/j.chempr.2019.08.012 

Cohen, S. I. A., Cukalevski, R., Michaels, T. C. T., Sari, A., Törnquist, M., Vendruscolo, M.,https://doi.org/10.1038/s41557-018-0023-x__Linse, S. (2018). Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-;2 peptide. Nature Chemistry. Springer Nature.https://doi.org/10.1038/s41557-018-0023-x 

Chipot, C., Dehez, F., Schnell, J. R., Zitzmann, N., Pebay-Peyroula, E., Catoire, L. J.,https://doi.org/10.1021/acs.chemrev.7b00570__Schanda, P. (2018). Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. Chemical Reviews. American Chemical Society.https://doi.org/10.1021/acs.chemrev.7b00570 

Aubret, A., &; Palacci, J. A. (2018). Diffusiophoretic design of self-spinning microgears from colloidal microswimmers. Soft Matter. Royal Society of Chemistry .https://doi.org/10.1039/c8sm01760c 

Samanta, D., Galaktionova, D., Gemen, J., Shimon, L. J. W., Diskin-Posner, Y., Avram, L.,https://doi.org/10.1038/s41467-017-02715-6__Klajn, R. (2018). Reversible chromism of spiropyran in the cavity of a flexible coordination cage. Nature Communications. Springer Nature.https://doi.org/10.1038/s41467-017-02715-6 

Chu, Z., Han, Y., Král, P., &; Klajn, R. (2018). “Precipitation on nanoparticles”: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles. Angewandte Chemie International Edition. Wiley.https://doi.org/10.1002/anie.201800673 

Bräuning, B., Bertosin, E., Praetorius, F. M., Ihling, C., Schatt, A., Adler, A.,https://doi.org/10.1038/s41467-018-04139-2__Groll, M. (2018). Structure and mechanism of the two-component ;1-helical pore-forming toxin YaxAB. Nature Communications. Springer Nature.https://doi.org/10.1038/s41467-018-04139-2 

Roy, S., Roy, S., Rao, A., Devatha, G., &; Pillai, P. P. (2018). Precise nanoparticle–reactant interaction outplays ligand poisoning in visible-light photocatalysis. Chemistry of Materials. American Chemical Society.https://doi.org/10.1021/acs.chemmater.8b03108 

Simunovic, M., Sari, A., Henderson, J. M., Lee, K. Y. C., &; Voth, G. A. (2017). Long-range organization of membrane-curving proteins. ACS Central Science. American Chemical Society.https://doi.org/10.1021/acscentsci.7b00392 

Meisl, G., Rajah, L., Cohen, S. A. I., Pfammatter, M., Sari, A., Hellstrand, E.,https://doi.org/10.1039/c7sc01965c__Knowles, T. P. J. (2017). Scaling behaviour and rate-determining steps in filamentous self-assembly. Chemical Science. Royal Society of Chemistry.https://doi.org/10.1039/c7sc01965c 

Vahid, A., Sari, A., &; Idema, T. (2017). Curvature variation controls particle aggregation on fluid vesicles. Soft Matter. Royal Society of Chemistry.https://doi.org/10.1039/c7sm00433h 

Buchwalter, A., &; Hetzer, M. (2017). Nucleolar expansion and elevated protein translation in premature aging. Nature Communications. Springer Nature.https://doi.org/10.1038/s41467-017-00322-z 

Gauto, D. F., Hessel, A., Rovó, P., Kurauskas, V., Linser, R., &; Schanda, P. (2017). Protein conformational dynamics studied by 15N and 1H<1 relaxation dispersion: Application to wild-type and A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. Elsevier.https://doi.org/10.1016/j.ssnmr.2017.04.002 

Sawczyk, M., &; Klajn, R. (2017). Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles. Journal of the American Chemical Society. American Chemical Society.https://doi.org/10.1021/jacs.7b09111 

van Esch, J. H., Klajn, R., &; Otto, S. (2017). Chemical systems out of equilibrium. Chemical Society Reviews. Royal Society of Chemistry.https://doi.org/10.1039/c7cs90088k 

Walt, S. G., Bhargava Ram, N., Atala, M., Shvetsov-Shilovski, N. I., von Conta, A., Baykusheva, D. R.,https://doi.org/10.1038/ncomms15651__Wörner, H. J. (2017). Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering. Nature Communications. Springer Nature.https://doi.org/10.1038/ncomms15651 

Bachmann, S. J., Kotar, J., Parolini, L., Sari, A., Cicuta, P., Di Michele, L., &; Mognetti, B. M. (2016). Melting transition in lipid vesicles functionalised by mobile DNA linkers. Soft Matter. Royal Society of Chemistry.https://doi.org/10.1039/c6sm01515h 

van de Ven, R. A. H., de Groot, J. S., Park, D., van Domselaar, R., de Jong, D., Szuhai, K.,https://doi.org/10.1038/ncomms13874__Derksen, P. W. B. (2016). 0-catenin prevents multinucleation through control of MKL-dependent RhoA activity during cytokinesis. Nature Communications. Springer Nature.https://doi.org/10.1038/ncomms13874 

Kurauskas, V., Crublet, E., Macek, P., Kerfah, R., Gauto, D. F., Boisbouvier, J., &; Schanda, P. (2016). Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective Clabelling: Application to the 50S ribosome subunit. Chemical Communications. Royal Society of Chemistry.https://doi.org/10.1039/c6cc04484k 

Bakail, M. M., &; Ochsenbein, F. (2016). Targeting protein–protein interactions, a wide open field for drug design. Comptes Rendus Chimie. Elsevier.https://doi.org/10.1016/j.crci.2015.12.004