M. J. Biaek and R. Klajn, “Diamond grows up,” Chem, vol. 5, no. 9. Elsevier, pp. 2283–2285, 2019.

S. I. A. Cohen et al., “Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-;2 peptide,” Nature Chemistry, vol. 10, no. 5. Springer Nature, pp. 523–531, 2018.

C. Chipot et al., “Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies,” Chemical Reviews, vol. 118, no. 7. American Chemical Society, pp. 3559–3607, 2018.

A. Aubret and J. A. Palacci, “Diffusiophoretic design of self-spinning microgears from colloidal microswimmers,” Soft Matter, vol. 14, no. 47. Royal Society of Chemistry , pp. 9577–9588, 2018.

D. Samanta et al., “Reversible chromism of spiropyran in the cavity of a flexible coordination cage,” Nature Communications, vol. 9. Springer Nature, 2018.

Z. Chu, Y. Han, P. Král, and R. Klajn, “‘Precipitation on nanoparticles’: Attractive intermolecular interactions stabilize specific ligand ratios on the surfaces of nanoparticles,” Angewandte Chemie International Edition, vol. 57, no. 24. Wiley, pp. 7023–7027, 2018.

B. Bräuning et al., “Structure and mechanism of the two-component ;1-helical pore-forming toxin YaxAB,” Nature Communications, vol. 9. Springer Nature, 2018.

S. Roy, S. Roy, A. Rao, G. Devatha, and P. P. Pillai, “Precise nanoparticle–reactant interaction outplays ligand poisoning in visible-light photocatalysis,” Chemistry of Materials, vol. 30, no. 23. American Chemical Society, pp. 8415–8419, 2018.

M. Simunovic, A. Sari, J. M. Henderson, K. Y. C. Lee, and G. A. Voth, “Long-range organization of membrane-curving proteins,” ACS Central Science, vol. 3, no. 12. American Chemical Society, pp. 1246–1253, 2017.

G. Meisl et al., “Scaling behaviour and rate-determining steps in filamentous self-assembly,” Chemical Science, vol. 8, no. 10. Royal Society of Chemistry, pp. 7087–7097, 2017.

A. Vahid, A. Sari, and T. Idema, “Curvature variation controls particle aggregation on fluid vesicles,” Soft Matter, vol. 13, no. 28. Royal Society of Chemistry, pp. 4924–4930, 2017.

A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” Nature Communications, vol. 8. Springer Nature, 2017.

D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, and P. Schanda, “Protein conformational dynamics studied by 15N and 1H<1 relaxation dispersion: Application to wild-type and A ubiquitin crystals,” Solid State Nuclear Magnetic Resonance, vol. 87, no. 10. Elsevier, pp. 86–95, 2017.

M. Sawczyk and R. Klajn, “Out-of-equilibrium aggregates and coatings during seeded growth of metallic nanoparticles,” Journal of the American Chemical Society, vol. 139, no. 49. American Chemical Society, pp. 17973–17978, 2017.

J. H. van Esch, R. Klajn, and S. Otto, “Chemical systems out of equilibrium,” Chemical Society Reviews, vol. 46, no. 18. Royal Society of Chemistry, pp. 5474–5475, 2017.

S. G. Walt et al., “Dynamics of valence-shell electrons and nuclei probed by strong-field holography and rescattering,” Nature Communications, vol. 8. Springer Nature, 2017.

S. J. Bachmann et al., “Melting transition in lipid vesicles functionalised by mobile DNA linkers,” Soft Matter, vol. 12, no. 37. Royal Society of Chemistry, pp. 7804–7817, 2016.

R. A. H. van de Ven et al., “-catenin prevents multinucleation through control of MKL-dependent RhoA activity during cytokinesis,” Nature Communications, vol. 7. Springer Nature, 2016.

V. Kurauskas et al., “Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective Clabelling: Application to the 50S ribosome subunit,” Chemical Communications, vol. 52, no. 61. Royal Society of Chemistry, pp. 9558–9561, 2016.

M. M. Bakail and F. Ochsenbein, “Targeting protein–protein interactions, a wide open field for drug design,” Comptes Rendus Chimie, vol. 19, no. 1–2. Elsevier, pp. 19–27, 2016.