D. F. Gauto et al., “Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR,” Journal of the American Chemical Society, vol. 141, no. 28. American Chemical Society, pp. 11183–11195, 2019.
LibreCat: https://research-explorer.ista.ac.at/record/8408
DOI: 10.1021/jacs.9b04219
PMID: 31199882

Z. Chu, Y. Han, T. Bian, S. De, P. Král, and R. Klajn, “Supramolecular control of azobenzene switching on nanoparticles,” Journal of the American Chemical Society, vol. 141, no. 5. American Chemical Society, pp. 1949–1960, 2019.
LibreCat: https://research-explorer.ista.ac.at/record/13373
DOI: 10.1021/jacs.8b09638
PMID: 30595017

M. Grzelczak, L. M. Liz-Marzán, and R. Klajn, “Stimuli-responsive self-assembly of nanoparticles,” Chemical Society Reviews, vol. 48, no. 5. Royal Society of Chemistry, pp. 1342–1361, 2019.
LibreCat: https://research-explorer.ista.ac.at/record/13372
DOI: 10.1039/c8cs00787j
PMID: 30688963

Z. Chu and R. Klajn, “Polysilsesquioxane nanowire networks as an ‘Artificial Solvent’ for reversible operation of photochromic molecules,” Nano Letters, vol. 19, no. 10. American Chemical Society, pp. 7106–7111, 2019.
LibreCat: https://research-explorer.ista.ac.at/record/13370
DOI: 10.1021/acs.nanolett.9b02642
PMID: 31539469

M. J. Biaek and R. Klajn, “Diamond grows up,” Chem, vol. 5, no. 9. Elsevier, pp. 2283–2285, 2019.
LibreCat: https://research-explorer.ista.ac.at/record/13371
DOI: 10.1016/j.chempr.2019.08.012

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.
LibreCat: https://research-explorer.ista.ac.at/record/10360
DOI: 10.1038/s41557-018-0023-x
PMID: 29581486

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.
LibreCat: https://research-explorer.ista.ac.at/record/8442
DOI: 10.1021/acs.chemrev.7b00570

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.
LibreCat: https://research-explorer.ista.ac.at/record/9053
DOI: 10.1039/c8sm01760c
PMID: 30456407
arXiv: 1909.11121

D. Samanta et al., “Reversible chromism of spiropyran in the cavity of a flexible coordination cage,” Nature Communications, vol. 9. Springer Nature, 2018.
LibreCat: https://research-explorer.ista.ac.at/record/13374
DOI: 10.1038/s41467-017-02715-6
PMID: 29440687

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.
LibreCat: https://research-explorer.ista.ac.at/record/13377
DOI: 10.1002/anie.201800673
PMID: 29673022

B. Bräuning et al., “Structure and mechanism of the two-component ;1-helical pore-forming toxin YaxAB,” Nature Communications, vol. 9. Springer Nature, 2018.
LibreCat: https://research-explorer.ista.ac.at/record/14284
DOI: 10.1038/s41467-018-04139-2
PMID: 29728606

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.
LibreCat: https://research-explorer.ista.ac.at/record/15107
DOI: 10.1021/acs.chemmater.8b03108

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.
LibreCat: https://research-explorer.ista.ac.at/record/10369
DOI: 10.1021/acscentsci.7b00392
PMID: 29296664

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.
LibreCat: https://research-explorer.ista.ac.at/record/10374
DOI: 10.1039/c7sc01965c
PMID: 29147538

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.
LibreCat: https://research-explorer.ista.ac.at/record/10375
DOI: 10.1039/c7sm00433h
PMID: 28677712
arXiv: 1703.00776

A. Buchwalter and M. Hetzer, “Nucleolar expansion and elevated protein translation in premature aging,” Nature Communications, vol. 8. Springer Nature, 2017.
LibreCat: https://research-explorer.ista.ac.at/record/11065
DOI: 10.1038/s41467-017-00322-z
PMID: 28855503

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.
LibreCat: https://research-explorer.ista.ac.at/record/8447
DOI: 10.1016/j.ssnmr.2017.04.002

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.
LibreCat: https://research-explorer.ista.ac.at/record/13380
DOI: 10.1021/jacs.7b09111
PMID: 29193964

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.
LibreCat: https://research-explorer.ista.ac.at/record/13382
DOI: 10.1039/c7cs90088k
PMID: 28884760

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.
LibreCat: https://research-explorer.ista.ac.at/record/14005
DOI: 10.1038/ncomms15651
PMID: 28643771