J. Datler et al., “Multi-modal cryo-EM reveals trimers of protein  to form the palisade layer in poxvirus cores,” Nature Structural &; Molecular Biology. Springer Nature, 2024.

B. Zens et al., “Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural landscape of extracellular matrix,” Journal of Cell Biology, vol. 223, no. 6. Rockefeller University Press, 2024.

F. Fäßler, M. Javoor, and F. K. Schur, “Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM,” Biochemical Society Transactions, vol. 51, no. 1. Portland Press, pp. 87–99, 2023.

F. Fäßler et al., “Arp isoforms regulate Ar/3 complex–dependent protrusion through differential Ena/VASP positioning,” Science Advances, vol. 9, no. 3. American Association for the Advancement of Science, 2023.

F. K. Schur, “Research data of the publication ‘Arp isoforms regulate Ar/3 complex-dependent protrusion through differential Ena/VASP positioning.’” Institute of Science and Technology Austria, 2023.

G. A. Dimchev, B. Amiri, F. Fäßler, M. Falcke, and F. K. Schur, “Computational toolbox for ultrastructural quantitative analysis of filament networks in cryo-ET data.” Institute of Science and Technology Austria, 2023.

J. Koch et al., “The phenuivirus Toscana virus makes an atypical use of vacuolar acidity to enter host cells,” PLoS Pathogens, vol. 19, no. 8. Public Library of Science, 2023.

S. Windhaber et al., “The Orthobunyavirus Germiston enters host cells from late endosomes,” Journal of Virology, vol. 96, no. 5. American Society for Microbiology, 2022.

M. Obr, W. J. H. Hagen, R. A. Dick, L. Yu, A. Kotecha, and F. K. Schur, “Exploring high-resolution cryo-ET and subtomogram averaging capabilities of contemporary DEDs,” Journal of Structural Biology, vol. 214, no. 2. Elsevier, 2022.

W. J. Nicolas, F. Fäßler, P. Dutka, F. K. Schur, G. Jensen, and E. Meyerowitz, “Cryo-electron tomography of the onion cell wall shows bimodally oriented cellulose fibers and reticulated homogalacturonan networks,” Current Biology, vol. 32, no. 11. Elsevier, pp. 75-2389, 2022.

M. Obr et al., “Structure of the mature Rous sarcoma virus lattice reveals a role for I in the formation of the capsid hexamer,” Nature Communications, vol. 12, no. 1. Nature Research, 2021.

M. Obr, F. K. Schur, and R. A. Dick, “A structural perspective of the role of I in immature and mature retroviral assembly,” Viruses, vol. 13, no. 9. MDPI, 2021.

G. A. Dimchev, B. Amiri, F. Fäßler, M. Falcke, and F. K. Schur, “Computational toolbox for ultrastructural quantitative analysis of filament networks in cryo-ET data,” Journal of Structural Biology, vol. 213, no. 4. Elsevier , 2021.

J. Morandell et al., “Cul3 regulates cytoskeleton protein homeostasis and cell migration during a critical window of brain development,” Nature Communications, vol. 12, no. 1. Springer Nature, 2021.

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.

R. A. Dick et al., “Structures of immature EIAV Gag lattices reveal a conserved role for I in lentivirus assembly,” PLOS Pathogens, vol. 16, no. 1. Public Library of Science, 2020.

F. K. Schur, “STL-files for 3D-printed grid holders described in  Fäßler F, Zens B, et al.; 3D printed cell culture grid holders for improved cellular specimen preparation in cryo-electron microscopy.” Institute of Science and Technology Austria, 2020.

F. Fäßler et al., “Cryo-electron tomography workflows for quantitative analysis of actin networks involved in cell migration,” Microscopy and Microanalysis, vol. 26, no. . Oxford University Press, pp. 2518–2519, 2020.

F. Fäßler, B. Zens, R. Hauschild, and F. K. Schur, “D printed cell culture grid holders for improved cellular specimen preparation in cryo-electron microscopy,” Journal of Structural Biology, vol. 212, no. 3. Elsevier, 2020.

F. K. Schur, “Toward high-resolution in situ structural biology with cryo-electron tomography and subtomogram averaging,” Current Opinion in Structural Biology, vol. 58, no. 10. Elsevier, pp. 1–9, 2019.

M. Obr and F. K. Schur, “Structural analysis of pleomorphic and asymmetric viruses using cryo-electron tomography and subtomogram averaging,” in Complementary Strategies to Study Virus Structure and Function, vol. 105, F. A. Rey, Ed. Elsevier, 2019, pp. 117–159.

R. Dick et al., “Inositol phosphates are assembly co-factors for HIV-1,” Nature, vol. 560, no. 7719. Nature Publishing Group, pp. 509–512, 2018.

K. Qu et al., “Structure and architecture of immature and mature murine leukemia virus capsids,” Proceedings of the National Academy of Sciences, vol. 115, no. 50. Proceedings of the National Academy of Sciences, pp. 751–760, 2018.

B. Turoová, F. K. Schur, W. Wan, and J. Briggs, “Efficient 3D-CTF correction for cryo-electron tomography using NovaCTF improves subtomogram averaging resolution to 3.4Å,” Journal of Structural Biology, vol. 199, no. 3. Academic Press, pp. 187–195, 2017.

S. Mattei, F. K. Schur, and J. A. Briggs, “Retrovirus maturation—an extraordinary structural transformation,” Current Opinion in Virology, vol. 18, no. 6. Elsevier, pp. 27–35, 2016.

T. Füzik et al., “Nucleic acid binding by Mason-Pfizer monkey virus CA promotes virus assembly and genome packaging,” Journal of Virology, vol. 90, no. 9. ASM, pp. 4593–4603, 2016.

F. K. Schur et al., “An atomic model of HIV-1 capsid-S reveals structures regulating assembly and maturation,” Science, vol. 353, no. 6298. American Association for the Advancement of Science, pp. 506–508, 2016.

A. F. Leithner et al., “Diversified actin protrusions promote environmental exploration but are dispensable for locomotion of leukocytes,” Nature Cell Biology, vol. 18. Nature Publishing Group, pp. 1253–1259, 2016.

F. K. Schur, R. Dick, W. Hagen, V. Vogt, and J. Briggs, “The structure of immature virus like Rous sarcoma virus gag particles reveals a structural role for the  domain in assembly,” Journal of Virology, vol. 89, no. 20. ASM, pp. 10294–10302, 2015.

F. K. Schur et al., “Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution,” Nature, vol. 517, no. 7535. Nature Publishing Group, pp. 505–508, 2015.

T. Bharata et al., “Cryo electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly,” PNAS, vol. 111, no. 22. National Academy of Sciences, pp. 8233–8238, 2014.

A. Steffen et al., “Rac function is crucial for cell migration but is not required for spreading and focal adhesion formation,” Journal of Cell Science, vol. 126, no. 20. Company of Biologists, pp. 4572–4588, 2013.

S. Koestler et al., “Ar/3 complex is essential for actin network treadmilling as well as for targeting of capping protein and cofilin,” Molecular Biology of the Cell, vol. 24, no. 18. American Society for Biology, pp. 2861–2875, 2013.

F. K. Schur, W. Hagen, A. De Marco, and J. Briggs, “Determination of protein structure at 8.5Å resolution using cryo-electron tomography and sub-tomogram averaging,” Journal of Structural Biology, vol. 184, no. 3. Academic Press, pp. 394–400, 2013.

M. Vinzenz et al., “Actin branching in the initiation and maintenance of lamellipodia,” Journal of Cell Science, vol. 125, no. 11. Company of Biologists, pp. 2775–2785, 2012.