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Dos Santos Caldas, P. R. (2020). Organization and dynamics of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinkers. Institute of Science and Technology Austria.https://doi.org/10.15479/AT:ISTA:8358 
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Dos Santos Caldas, P. R., Radler, P., Sommer, C. M., &; Loose, M. (2020). Computational analysis of filament polymerization dynamics in cytoskeletal networks. In P. Tran (Ed.), Methods in Cell Biology (Vol. 158, pp. 145–161). Elsevier.https://doi.org/10.1016/bs.mcb.2020.01.006 
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Baranova, N. S., Radler, P., Hernández-Rocamora, V. M., Alfonso, C., Lopez Pelegrin, M. D., Rivas, G.,https://doi.org/10.1038/s41564-019-0657-5__Loose, M. (2020). Diffusion and capture permits dynamic coupling between treadmilling FtsZ filaments and cell division proteins. Nature Microbiology. Springer Nature.https://doi.org/10.1038/s41564-019-0657-5 
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Rosa, H. V. D., Leonardo, D. A., Brognara, G., Brandão-Neto, J., D’Muniz Pereira, H., Araújo, A. P. U., &; Garratt, R. C. (2020). Molecular recognition at septin interfaces: The switches hold the key. Journal of Molecular Biology. Elsevier.https://doi.org/10.1016/j.jmb.2020.09.001 
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Davies, H. S., Baranova, N. S., El Amri, N., Coche-Guérente, L., Verdier, C., Bureau, L.,https://doi.org/10.1016/j.matbio.2018.12.002__Débarre, D. (2019). An integrated assay to probe endothelial glycocalyx-blood cell interactions under flow in mechanically and biochemically well-defined environments. Matrix Biology. Elsevier.https://doi.org/10.1016/j.matbio.2018.12.002 
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Davies, H. S., Baranova, N. S., El Amri, N., Coche-Guérente, L., Verdier, C., Bureau, L.,https://doi.org/10.1117/12.2527058__Débarre, D. (2019). Blood cell-vessel wall interactions probed by reflection interference contrast microscopy. In Advances in Microscopic Imaging II (Vol. 11076). Munich, Germany: SPIE.https://doi.org/10.1117/12.2527058 
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Dos Santos Caldas, P. R., Lopez Pelegrin, M. D., Pearce, D. J. G., Budanur, N. B., Brugués, J., &; Loose, M. (2019). Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA. Nature Communications. Springer Nature.https://doi.org/10.1038/s41467-019-13702-4 
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Richter, R., Baranova, N. S., Day, A., &; Kwok, J. (2018). Glycosaminoglycans in extracellular matrix organisation: Are concepts from soft matter physics key to understanding the formation of perineuronal nets? Current Opinion in Structural Biology. Elsevier.https://doi.org/10.1016/j.sbi.2017.12.002 
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Fallesen, T., Roostalu, J., Düllberg, C. F., Pruessner, G., &; Surrey, T. (2017). Ensembles of bidirectional kinesin Cin8 produce additive forces in both directions of movement. Biophysical Journal. Biophysical Society.https://doi.org/10.1016/j.bpj.2017.09.006 
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Loose, M., Zieske, K., &; Schwille, P. (2017). Reconstitution of protein dynamics involved in bacterial cell division. In Prokaryotic Cytoskeletons (Vol. 84, pp. 419–444). Springer.https://doi.org/10.1007/978-3-319-53047-5_15 
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Rickman, J., Düllberg, C. F., Cade, N., Griffin, L., &; Surrey, T. (2017). Steady state EB cap size fluctuations are determined by stochastic microtubule growth and maturation. PNAS. National Academy of Sciences.https://doi.org/10.1073/pnas.1620274114 
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Smole, A., Lainsdek, D., Bezeljak, U., Horvat, S., &; Jerala, R. (2017). A synthetic mammalian therapeutic gene circuit for sensing and suppressing inflammation. Molecular Therapy. Elsevier.https://doi.org/10.1016/j.ymthe.2016.10.005 
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Baranova, N. S., &; Loose, M. (2017). Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA copolymers. In A. Echard (Ed.), Cytokinesis (Vol. 137, pp. 355–370). Academic Press.https://doi.org/10.1016/bs.mcb.2016.03.036 
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Hansen, A. H., Düllberg, C. F., Mieck, C., Loose, M., &; Hippenmeyer, S. (2017). Cell polarity in cerebral cortex development - cellular architecture shaped by biochemical networks. Frontiers in Cellular Neuroscience. Frontiers Research Foundation.https://doi.org/10.3389/fncel.2017.00176 
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Nguyen, P., Field, C., Groen, A., Mitchison, T., &; Loose, M. (2015). Using supported bilayers to study the spatiotemporal organization of membrane-bound proteins. In Building a Cell from its Components Parts (Vol. 128, pp. 223–241). Academic Press.https://doi.org/10.1016/bs.mcb.2015.01.007 
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