H. Rampelt et al., “The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments,” BMC Biology, vol. 18. Springer Nature, 2020.
LibreCat: https://research-explorer.ista.ac.at/record/8402
DOI: 10.1186/s12915-019-0733-6
PMID: 31907035

G. M. Arnold et al., “Converting microwave and telecom photons with a silicon photonic nanomechanical interface,” Nature Communications, vol. 11. Springer Nature, 2020.
LibreCat: https://research-explorer.ista.ac.at/record/8529
DOI: 10.1038/s41467-020-18269-z
WoS: 000577280200001

A. Tian et al., “Oncogenic state and cell identity combinatorially dictate the susceptibility of cells within glioma development hierarchy to IGR targeting,” Advanced Science, vol. 7, no. 21. Wiley, 2020.
LibreCat: https://research-explorer.ista.ac.at/record/8592
DOI: 10.1002/advs.202001724
WoS: 000573860700001

C. Prehal et al., “Persistent and reversible solid iodine electrodeposition in nanoporous carbons,” Nature Communications, vol. 11. Springer Nature, 2020.
LibreCat: https://research-explorer.ista.ac.at/record/8568
DOI: 10.1038/s41467-020-18610-6
WoS: 000573756600004

L. Schulte et al., “Cysteine oxidation and disulfide formation in the ribosomal exit tunnel,” Nature Communications, vol. 11. Springer Nature, 2020.
LibreCat: https://research-explorer.ista.ac.at/record/8744
DOI: 10.1038/s41467-020-19372-x
WoS: 000592028600001

F. Fäßler, G. A. Dimchev, V.-V. Hodirnau, W. Wan, and F. K. Schur, “Cryo-electron tomography structure of Ar/3 complex in cells reveals new insights into the branch junction,” Nature Communications, vol. 11. Springer Nature, 2020.
LibreCat: https://research-explorer.ista.ac.at/record/8971
DOI: 10.1038/s41467-020-20286-x
WoS: 000603078000003

J. L. Fribourgh et al., “Dynamics at the serine loop underlie differential affinity of cryptochromes for CLOCK:BMAL1 to control circadian timing,” eLife, vol. 9. eLife Sciences Publications, 2020.
LibreCat: https://research-explorer.ista.ac.at/record/15153
DOI: 10.7554/elife.55275

D. F. Gauto et al., “Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex,” Nature Communications, vol. 10. Springer Nature, 2019.
LibreCat: https://research-explorer.ista.ac.at/record/8405
DOI: 10.1038/s41467-019-10490-9
PMID: 31217444

S. Ramananarivo, E. Ducrot, and J. A. Palacci, “Activity-controlled annealing of colloidal monolayers,” Nature Communications, vol. 10, no. 1. Springer Nature, 2019.
LibreCat: https://research-explorer.ista.ac.at/record/9060
DOI: 10.1038/s41467-019-11362-y
PMID: 31358762
arXiv: 1909.07382

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

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

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

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

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