S. He, M. Vickers, J. Zhang, and X. Feng, “Natural depletion of histone  in sex cells causes DNA demethylation, heterochromatin decondensation and transposon activation,” eLife, vol. 8. eLife Sciences Publications, Ltd, 2019.
LibreCat: https://research-explorer.ista.ac.at/record/12192
DOI: 10.7554/elife.42530

E. J. Lawrence et al., “Natural variation in TBP-ASSOCIATED FACTOR 4b controls meiotic crossover and germline transcription in Arabidopsis,” Current Biology, vol. 29, no. 16. Elsevier BV, p. 2676–2686.e3, 2019.
LibreCat: https://research-explorer.ista.ac.at/record/12190
DOI: 10.1016/j.cub.2019.06.084
PMID: 31378616

A. Buchwalter, R. Schulte, H. Tsai, J. Capitanio, and M. Hetzer, “Selective clearance of the inner nuclear membrane protein emerin by vesicular transport during ER stress,” eLife, vol. 8. eLife Sciences Publications, 2019.
LibreCat: https://research-explorer.ista.ac.at/record/11060
DOI: 10.7554/elife.49796
PMID: 31599721

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. 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

K. Weinhäupl et al., “The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of Clp from Mycobacterium tuberculosis,” Journal of Biological Chemistry, vol. 293, no. 22. American Society for Biochemistry &; Molecular Biology, pp. 8379–8393, 2018.
LibreCat: https://research-explorer.ista.ac.at/record/8440
DOI: 10.1074/jbc.ra118.002251

C. Laguri et al., “Solid state NMR studies of intact lipopolysaccharide endotoxin,” ACS Chemical Biology, vol. 13, no. 8. American Chemical Society, pp. 2106–2113, 2018.
LibreCat: https://research-explorer.ista.ac.at/record/8439
DOI: 10.1021/acschembio.8b00271

K. Weinhäupl et al., “Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space,” Cell, vol. 175, no. 5. Elsevier, p. 1365–1379.e25, 2018.
LibreCat: https://research-explorer.ista.ac.at/record/8436
DOI: 10.1016/j.cell.2018.10.039

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

M. Yuuta and K. Koshiba-Takeuchi, “Significance of whole-genome duplications on the emergence of evolutionary novelties,” Briefings in Functional Genomics, vol. 17, no. 5. Oxford University Press, pp. 329–338, 2018.
LibreCat: https://research-explorer.ista.ac.at/record/10880
DOI: 10.1093/bfgp/ely007
WoS: 000456054400004
PMID: 29579140

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. C. J. Helle et al., “Mechanical force induces mitochondrial fission,” eLife, vol. 6. eLife Sciences Publications, 2017.
LibreCat: https://research-explorer.ista.ac.at/record/10370
DOI: 10.7554/elife.30292
PMID: 29119945

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

R. Franco, A. Favier, P. Schanda, and B. Brutscher, “Optimized fast mixing device for real-time NMR applications,” Journal of Magnetic Resonance, vol. 281, no. 8. Elsevier, pp. 125–129, 2017.
LibreCat: https://research-explorer.ista.ac.at/record/8448
DOI: 10.1016/j.jmr.2017.05.016

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

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

A. K. Michael, J. L. Fribourgh, R. N. Van Gelder, and C. L. Partch, “Animal cryptochromes: Divergent roles in light perception, circadian timekeeping and beyond,” Photochemistry and Photobiology, vol. 93, no. 1. Wiley, pp. 128–140, 2017.
LibreCat: https://research-explorer.ista.ac.at/record/15158
DOI: 10.1111/php.12677

J. C. Fong et al., “Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms,” eLife, vol. 6. eLife Sciences Publications, 2017.
LibreCat: https://research-explorer.ista.ac.at/record/15154
DOI: 10.7554/elife.26163
PMID: 28762945

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.
LibreCat: https://research-explorer.ista.ac.at/record/11072
DOI: 10.1038/ncomms13874
PMID: 28004812

E. M. Hatch and M. Hetzer, “Linking micronuclei to chromosome fragmentation,” Cell, vol. 161, no. 7. Elsevier, pp. 1502–1504, 2015.
LibreCat: https://research-explorer.ista.ac.at/record/11073
DOI: 10.1016/j.cell.2015.06.005
PMID: 26091034