[{"language":[{"iso":"eng"}],"month":"02","project":[{"name":"Self-Organization of the Bacterial Cell","grant_number":"679239","_id":"2595697A-B435-11E9-9278-68D0E5697425","call_identifier":"H2020"},{"name":"Reconstitution of Bacterial Cell Division Using Purified Components","_id":"260D98C8-B435-11E9-9278-68D0E5697425"}],"oa_version":"Preprint","publication":"Methods in Cell Biology","related_material":{"record":[{"relation":"part_of_dissertation","id":"8358","status":"public"}]},"status":"public","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","main_file_link":[{"url":"https://doi.org/10.1101/839571","open_access":"1"}],"oa":1,"publication_identifier":{"issn":["0091679X"]},"type":"book_chapter","date_published":"2020-02-27T00:00:00Z","editor":[{"last_name":"Tran","first_name":"Phong ","full_name":"Tran, Phong "}],"publisher":"Elsevier","ec_funded":1,"quality_controlled":"1","page":"145-161","intvolume":"       158","alternative_title":["Methods in Cell Biology"],"title":"Computational analysis of filament polymerization dynamics in cytoskeletal networks","date_created":"2020-03-08T23:00:47Z","department":[{"_id":"MaLo"}],"article_processing_charge":"No","publication_status":"published","author":[{"last_name":"Dos Santos Caldas","first_name":"Paulo R","full_name":"Dos Santos Caldas, Paulo R","orcid":"0000-0001-6730-4461","id":"38FCDB4C-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Radler","first_name":"Philipp","full_name":"Radler, Philipp","orcid":"0000-0001-9198-2182 ","id":"40136C2A-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Christoph M","last_name":"Sommer","orcid":"0000-0003-1216-9105","full_name":"Sommer, Christoph M","id":"4DF26D8C-F248-11E8-B48F-1D18A9856A87"},{"orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","first_name":"Martin","last_name":"Loose","id":"462D4284-F248-11E8-B48F-1D18A9856A87"}],"scopus_import":"1","_id":"7572","volume":158,"abstract":[{"lang":"eng","text":"The polymerization–depolymerization dynamics of cytoskeletal proteins play essential roles in the self-organization of cytoskeletal structures, in eukaryotic as well as prokaryotic cells. While advances in fluorescence microscopy and in vitro reconstitution experiments have helped to study the dynamic properties of these complex systems, methods that allow to collect and analyze large quantitative datasets of the underlying polymer dynamics are still missing. Here, we present a novel image analysis workflow to study polymerization dynamics of active filaments in a nonbiased, highly automated manner. Using treadmilling filaments of the bacterial tubulin FtsZ as an example, we demonstrate that our method is able to specifically detect, track and analyze growth and shrinkage of polymers, even in dense networks of filaments. We believe that this automated method can facilitate the analysis of a large variety of dynamic cytoskeletal systems, using standard time-lapse movies obtained from experiments in vitro as well as in the living cell. Moreover, we provide scripts implementing this method as supplementary material."}],"day":"27","doi":"10.1016/bs.mcb.2020.01.006","external_id":{"isi":["000611826500008"]},"isi":1,"citation":{"chicago":"Dos Santos Caldas, Paulo R, Philipp Radler, Christoph M Sommer, and Martin Loose. “Computational Analysis of Filament Polymerization Dynamics in Cytoskeletal Networks.” In <i>Methods in Cell Biology</i>, edited by Phong  Tran, 158:145–61. Elsevier, 2020. <a href=\"https://doi.org/10.1016/bs.mcb.2020.01.006\">https://doi.org/10.1016/bs.mcb.2020.01.006</a>.","ieee":"P. R. Dos Santos Caldas, P. Radler, C. M. Sommer, and M. Loose, “Computational analysis of filament polymerization dynamics in cytoskeletal networks,” in <i>Methods in Cell Biology</i>, vol. 158, P. Tran, Ed. Elsevier, 2020, pp. 145–161.","apa":"Dos Santos Caldas, P. R., Radler, P., Sommer, C. M., &#38; Loose, M. (2020). Computational analysis of filament polymerization dynamics in cytoskeletal networks. In P. Tran (Ed.), <i>Methods in Cell Biology</i> (Vol. 158, pp. 145–161). Elsevier. <a href=\"https://doi.org/10.1016/bs.mcb.2020.01.006\">https://doi.org/10.1016/bs.mcb.2020.01.006</a>","ama":"Dos Santos Caldas PR, Radler P, Sommer CM, Loose M. Computational analysis of filament polymerization dynamics in cytoskeletal networks. In: Tran P, ed. <i>Methods in Cell Biology</i>. Vol 158. Elsevier; 2020:145-161. doi:<a href=\"https://doi.org/10.1016/bs.mcb.2020.01.006\">10.1016/bs.mcb.2020.01.006</a>","ista":"Dos Santos Caldas PR, Radler P, Sommer CM, Loose M. 2020.Computational analysis of filament polymerization dynamics in cytoskeletal networks. In: Methods in Cell Biology. Methods in Cell Biology, vol. 158, 145–161.","short":"P.R. Dos Santos Caldas, P. Radler, C.M. Sommer, M. Loose, in:, P. Tran (Ed.), Methods in Cell Biology, Elsevier, 2020, pp. 145–161.","mla":"Dos Santos Caldas, Paulo R., et al. “Computational Analysis of Filament Polymerization Dynamics in Cytoskeletal Networks.” <i>Methods in Cell Biology</i>, edited by Phong  Tran, vol. 158, Elsevier, 2020, pp. 145–61, doi:<a href=\"https://doi.org/10.1016/bs.mcb.2020.01.006\">10.1016/bs.mcb.2020.01.006</a>."},"year":"2020","date_updated":"2023-10-04T09:50:24Z"},{"status":"public","related_material":{"record":[{"status":"public","id":"8341","relation":"dissertation_contains"}],"link":[{"relation":"press_release","description":"News on IST Homepage","url":"https://ist.ac.at/en/news/proteins-as-molecular-switches/"}]},"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1101/776567"}],"oa":1,"publication_identifier":{"eissn":["1091-6490"],"issn":["0027-8424"]},"type":"journal_article","date_published":"2020-03-24T00:00:00Z","language":[{"iso":"eng"}],"month":"03","project":[{"_id":"2599F062-B435-11E9-9278-68D0E5697425","grant_number":"RGY0083/2016","name":"Reconstitution of cell polarity and axis determination in a cell-free system"}],"oa_version":"Preprint","acknowledged_ssus":[{"_id":"Bio"},{"_id":"LifeSc"}],"publication":"Proceedings of the National Academy of Sciences","volume":117,"abstract":[{"text":"The eukaryotic endomembrane system is controlled by small GTPases of the Rab family, which are activated at defined times and locations in a switch-like manner. While this switch is well understood for an individual protein, how regulatory networks produce intracellular activity patterns is currently not known. Here, we combine in vitro reconstitution experiments with computational modeling to study a minimal Rab5 activation network. We find that the molecular interactions in this system give rise to a positive feedback and bistable collective switching of Rab5. Furthermore, we find that switching near the critical point is intrinsically stochastic and provide evidence that controlling the inactive population of Rab5 on the membrane can shape the network response. Notably, we demonstrate that collective switching can spread on the membrane surface as a traveling wave of Rab5 activation. Together, our findings reveal how biochemical signaling networks control vesicle trafficking pathways and how their nonequilibrium properties define the spatiotemporal organization of the cell.","lang":"eng"}],"day":"24","doi":"10.1073/pnas.1921027117","external_id":{"isi":["000521821800040"]},"isi":1,"year":"2020","citation":{"apa":"Bezeljak, U., Loya, H., Kaczmarek, B. M., Saunders, T. E., &#38; Loose, M. (2020). Stochastic activation and bistability in a Rab GTPase regulatory network. <i>Proceedings of the National Academy of Sciences</i>. Proceedings of the National Academy of Sciences. <a href=\"https://doi.org/10.1073/pnas.1921027117\">https://doi.org/10.1073/pnas.1921027117</a>","ama":"Bezeljak U, Loya H, Kaczmarek BM, Saunders TE, Loose M. Stochastic activation and bistability in a Rab GTPase regulatory network. <i>Proceedings of the National Academy of Sciences</i>. 2020;117(12):6504-6549. doi:<a href=\"https://doi.org/10.1073/pnas.1921027117\">10.1073/pnas.1921027117</a>","ieee":"U. Bezeljak, H. Loya, B. M. Kaczmarek, T. E. Saunders, and M. Loose, “Stochastic activation and bistability in a Rab GTPase regulatory network,” <i>Proceedings of the National Academy of Sciences</i>, vol. 117, no. 12. Proceedings of the National Academy of Sciences, pp. 6504–6549, 2020.","chicago":"Bezeljak, Urban, Hrushikesh Loya, Beata M Kaczmarek, Timothy E. Saunders, and Martin Loose. “Stochastic Activation and Bistability in a Rab GTPase Regulatory Network.” <i>Proceedings of the National Academy of Sciences</i>. Proceedings of the National Academy of Sciences, 2020. <a href=\"https://doi.org/10.1073/pnas.1921027117\">https://doi.org/10.1073/pnas.1921027117</a>.","mla":"Bezeljak, Urban, et al. “Stochastic Activation and Bistability in a Rab GTPase Regulatory Network.” <i>Proceedings of the National Academy of Sciences</i>, vol. 117, no. 12, Proceedings of the National Academy of Sciences, 2020, pp. 6504–49, doi:<a href=\"https://doi.org/10.1073/pnas.1921027117\">10.1073/pnas.1921027117</a>.","short":"U. Bezeljak, H. Loya, B.M. Kaczmarek, T.E. Saunders, M. Loose, Proceedings of the National Academy of Sciences 117 (2020) 6504–6549.","ista":"Bezeljak U, Loya H, Kaczmarek BM, Saunders TE, Loose M. 2020. Stochastic activation and bistability in a Rab GTPase regulatory network. Proceedings of the National Academy of Sciences. 117(12), 6504–6549."},"date_updated":"2023-09-07T13:17:06Z","article_type":"original","publisher":"Proceedings of the National Academy of Sciences","quality_controlled":"1","page":"6504-6549","intvolume":"       117","title":"Stochastic activation and bistability in a Rab GTPase regulatory network","department":[{"_id":"MaLo"},{"_id":"CaBe"}],"date_created":"2020-03-12T05:32:26Z","article_processing_charge":"No","publication_status":"published","issue":"12","author":[{"id":"2A58201A-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-1365-5631","full_name":"Bezeljak, Urban","first_name":"Urban","last_name":"Bezeljak"},{"first_name":"Hrushikesh","last_name":"Loya","full_name":"Loya, Hrushikesh"},{"full_name":"Kaczmarek, Beata M","first_name":"Beata M","last_name":"Kaczmarek","id":"36FA4AFA-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Saunders, Timothy E.","first_name":"Timothy E.","last_name":"Saunders"},{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","last_name":"Loose","first_name":"Martin","full_name":"Loose, Martin","orcid":"0000-0001-7309-9724"}],"scopus_import":"1","_id":"7580"},{"abstract":[{"text":"Wood, as the most abundant carbon dioxide storing bioresource, is currently driven beyond its traditional use through creative innovations and nanotechnology. For many properties the micro- and nanostructure plays a crucial role and one key challenge is control and detection of chemical and physical processes in the confined microstructure and nanopores of the wooden cell wall. In this study, correlative Raman and atomic force microscopy show high potential for tracking in situ molecular rearrangement of wood polymers during compression. More water molecules (interpreted as wider cellulose microfibril distances) and disentangling of hemicellulose chains are detected in the opened cell wall regions, whereas an increase of lignin is revealed in the compressed areas. These results support a new more “loose” cell wall model based on flexible lignin nanodomains and advance our knowledge of the molecular reorganization during deformation of wood for optimized processing and utilization.","lang":"eng"}],"day":"08","doi":"10.1021/acs.nanolett.0c00205","external_id":{"isi":["000526413400055"],"pmid":["32196350"]},"isi":1,"year":"2020","citation":{"ista":"Felhofer M, Bock P, Singh A, Prats Mateu B, Zirbs R, Gierlinger N. 2020. Wood deformation leads to rearrangement of molecules at the nanoscale. Nano Letters. 20(4), 2647–2653.","mla":"Felhofer, Martin, et al. “Wood Deformation Leads to Rearrangement of Molecules at the Nanoscale.” <i>Nano Letters</i>, vol. 20, no. 4, American Chemical Society, 2020, pp. 2647–53, doi:<a href=\"https://doi.org/10.1021/acs.nanolett.0c00205\">10.1021/acs.nanolett.0c00205</a>.","short":"M. Felhofer, P. Bock, A. Singh, B. Prats Mateu, R. Zirbs, N. Gierlinger, Nano Letters 20 (2020) 2647–2653.","chicago":"Felhofer, Martin, Peter Bock, Adya Singh, Batirtze Prats Mateu, Ronald Zirbs, and Notburga Gierlinger. “Wood Deformation Leads to Rearrangement of Molecules at the Nanoscale.” <i>Nano Letters</i>. American Chemical Society, 2020. <a href=\"https://doi.org/10.1021/acs.nanolett.0c00205\">https://doi.org/10.1021/acs.nanolett.0c00205</a>.","ieee":"M. Felhofer, P. Bock, A. Singh, B. Prats Mateu, R. Zirbs, and N. Gierlinger, “Wood deformation leads to rearrangement of molecules at the nanoscale,” <i>Nano Letters</i>, vol. 20, no. 4. American Chemical Society, pp. 2647–2653, 2020.","ama":"Felhofer M, Bock P, Singh A, Prats Mateu B, Zirbs R, Gierlinger N. Wood deformation leads to rearrangement of molecules at the nanoscale. <i>Nano Letters</i>. 2020;20(4):2647-2653. doi:<a href=\"https://doi.org/10.1021/acs.nanolett.0c00205\">10.1021/acs.nanolett.0c00205</a>","apa":"Felhofer, M., Bock, P., Singh, A., Prats Mateu, B., Zirbs, R., &#38; Gierlinger, N. (2020). Wood deformation leads to rearrangement of molecules at the nanoscale. <i>Nano Letters</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.nanolett.0c00205\">https://doi.org/10.1021/acs.nanolett.0c00205</a>"},"date_updated":"2023-08-21T06:12:09Z","ddc":["530"],"volume":20,"intvolume":"        20","title":"Wood deformation leads to rearrangement of molecules at the nanoscale","date_created":"2020-04-19T22:00:54Z","department":[{"_id":"MaLo"}],"article_processing_charge":"No","publication_status":"published","issue":"4","author":[{"last_name":"Felhofer","first_name":"Martin","full_name":"Felhofer, Martin"},{"last_name":"Bock","first_name":"Peter","full_name":"Bock, Peter"},{"full_name":"Singh, Adya","first_name":"Adya","last_name":"Singh"},{"id":"299FE892-F248-11E8-B48F-1D18A9856A87","first_name":"Batirtze","last_name":"Prats Mateu","full_name":"Prats Mateu, Batirtze"},{"first_name":"Ronald","last_name":"Zirbs","full_name":"Zirbs, Ronald"},{"last_name":"Gierlinger","first_name":"Notburga","full_name":"Gierlinger, Notburga"}],"scopus_import":"1","pmid":1,"_id":"7663","article_type":"original","publisher":"American Chemical Society","file_date_updated":"2020-07-14T12:48:01Z","quality_controlled":"1","page":"2647-2653","oa":1,"publication_identifier":{"eissn":["15306992"]},"type":"journal_article","date_published":"2020-04-08T00:00:00Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"status":"public","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","file":[{"date_updated":"2020-07-14T12:48:01Z","content_type":"application/pdf","file_name":"2020_NanoLetters_Felhofer.pdf","date_created":"2020-04-20T10:43:36Z","file_size":7108014,"checksum":"fe46146a9c4c620592a1932a8599069e","file_id":"7667","creator":"dernst","access_level":"open_access","relation":"main_file"}],"month":"04","oa_version":"Published Version","has_accepted_license":"1","publication":"Nano Letters","language":[{"iso":"eng"}]},{"month":"10","oa_version":"Published Version","publication":"Journal of Molecular Biology","keyword":["Molecular Biology","Structural Biology"],"language":[{"iso":"eng"}],"oa":1,"publication_identifier":{"issn":["0022-2836"]},"type":"journal_article","date_published":"2020-10-02T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.jmb.2020.09.001"}],"intvolume":"       432","title":"Molecular recognition at septin interfaces: The switches hold the key","department":[{"_id":"MaLo"}],"date_created":"2024-02-28T08:50:34Z","article_processing_charge":"No","publication_status":"published","issue":"21","author":[{"full_name":"Rosa, Higor Vinícius Dias","first_name":"Higor Vinícius Dias","last_name":"Rosa"},{"last_name":"Leonardo","first_name":"Diego Antonio","full_name":"Leonardo, Diego Antonio"},{"last_name":"Brognara","first_name":"Gabriel","full_name":"Brognara, Gabriel","id":"D96FFDA0-A884-11E9-9968-DC26E6697425"},{"full_name":"Brandão-Neto, José","first_name":"José","last_name":"Brandão-Neto"},{"full_name":"D'Muniz Pereira, Humberto","last_name":"D'Muniz Pereira","first_name":"Humberto"},{"first_name":"Ana Paula Ulian","last_name":"Araújo","full_name":"Araújo, Ana Paula Ulian"},{"full_name":"Garratt, Richard Charles","first_name":"Richard Charles","last_name":"Garratt"}],"pmid":1,"_id":"15036","article_type":"original","publisher":"Elsevier","quality_controlled":"1","page":"5784-5801","abstract":[{"text":"The assembly of a septin filament requires that homologous monomers must distinguish between one another in establishing appropriate interfaces with their neighbors. To understand this phenomenon at the molecular level, we present the first four crystal structures of heterodimeric septin complexes. We describe in detail the two distinct types of G-interface present within the octameric particles, which must polymerize to form filaments. These are formed between SEPT2 and SEPT6 and between SEPT7 and SEPT3, and their description permits an understanding of the structural basis for the selectivity necessary for correct filament assembly. By replacing SEPT6 by SEPT8 or SEPT11, it is possible to rationalize Kinoshita's postulate, which predicts the exchangeability of septins from within a subgroup. Switches I and II, which in classical small GTPases provide a mechanism for nucleotide-dependent conformational change, have been repurposed in septins to play a fundamental role in molecular recognition. Specifically, it is switch I which holds the key to discriminating between the two different G-interfaces. Moreover, residues which are characteristic for a given subgroup play subtle, but pivotal, roles in guaranteeing that the correct interfaces are formed.","lang":"eng"}],"day":"02","doi":"10.1016/j.jmb.2020.09.001","external_id":{"pmid":["32910969"]},"citation":{"ista":"Rosa HVD, Leonardo DA, Brognara G, Brandão-Neto J, D’Muniz Pereira H, Araújo APU, Garratt RC. 2020. Molecular recognition at septin interfaces: The switches hold the key. Journal of Molecular Biology. 432(21), 5784–5801.","short":"H.V.D. Rosa, D.A. Leonardo, G. Brognara, J. Brandão-Neto, H. D’Muniz Pereira, A.P.U. Araújo, R.C. Garratt, Journal of Molecular Biology 432 (2020) 5784–5801.","mla":"Rosa, Higor Vinícius Dias, et al. “Molecular Recognition at Septin Interfaces: The Switches Hold the Key.” <i>Journal of Molecular Biology</i>, vol. 432, no. 21, Elsevier, 2020, pp. 5784–801, doi:<a href=\"https://doi.org/10.1016/j.jmb.2020.09.001\">10.1016/j.jmb.2020.09.001</a>.","chicago":"Rosa, Higor Vinícius Dias, Diego Antonio Leonardo, Gabriel Brognara, José Brandão-Neto, Humberto D’Muniz Pereira, Ana Paula Ulian Araújo, and Richard Charles Garratt. “Molecular Recognition at Septin Interfaces: The Switches Hold the Key.” <i>Journal of Molecular Biology</i>. Elsevier, 2020. <a href=\"https://doi.org/10.1016/j.jmb.2020.09.001\">https://doi.org/10.1016/j.jmb.2020.09.001</a>.","ieee":"H. V. D. Rosa <i>et al.</i>, “Molecular recognition at septin interfaces: The switches hold the key,” <i>Journal of Molecular Biology</i>, vol. 432, no. 21. Elsevier, pp. 5784–5801, 2020.","apa":"Rosa, H. V. D., Leonardo, D. A., Brognara, G., Brandão-Neto, J., D’Muniz Pereira, H., Araújo, A. P. U., &#38; Garratt, R. C. (2020). Molecular recognition at septin interfaces: The switches hold the key. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2020.09.001\">https://doi.org/10.1016/j.jmb.2020.09.001</a>","ama":"Rosa HVD, Leonardo DA, Brognara G, et al. Molecular recognition at septin interfaces: The switches hold the key. <i>Journal of Molecular Biology</i>. 2020;432(21):5784-5801. doi:<a href=\"https://doi.org/10.1016/j.jmb.2020.09.001\">10.1016/j.jmb.2020.09.001</a>"},"year":"2020","date_updated":"2024-02-28T12:37:54Z","volume":432},{"abstract":[{"lang":"eng","text":"Numerous biophysical questions require the quantification of short-range interactions between (functionalized) surfaces and synthetic or biological objects such as cells. Here, we present an original, custom built setup for reflection interference contrast microscopy that can assess distances between a substrate and a flowing object at high speed with nanometric accuracy. We demonstrate its use to decipher the complex biochemical and mechanical interplay regulating blood cell homing at the vessel wall in the microcirculation using an in vitro approach. We show that in the absence of specific biochemical interactions, flowing cells are repelled from the soft layer lining the vessel wall, contributing to red blood cell repulsion in vivo. In contrast, this so-called glycocalyx stabilizes rolling of cells under flow in the presence of a specific receptor naturally present on activated leucocytes and a number of cancer cell lines."}],"doi":"10.1117/12.2527058","day":"22","isi":1,"external_id":{"isi":["000535353000023"]},"date_updated":"2023-08-29T06:54:38Z","citation":{"apa":"Davies, H. S., Baranova, N. S., El Amri, N., Coche-Guérente, L., Verdier, C., Bureau, L., … Débarre, D. (2019). Blood cell-vessel wall interactions probed by reflection interference contrast microscopy. In <i>Advances in Microscopic Imaging II</i> (Vol. 11076). Munich, Germany: SPIE. <a href=\"https://doi.org/10.1117/12.2527058\">https://doi.org/10.1117/12.2527058</a>","ama":"Davies HS, Baranova NS, El Amri N, et al. Blood cell-vessel wall interactions probed by reflection interference contrast microscopy. In: <i>Advances in Microscopic Imaging II</i>. Vol 11076. SPIE; 2019. doi:<a href=\"https://doi.org/10.1117/12.2527058\">10.1117/12.2527058</a>","chicago":"Davies, Heather S., Natalia S. Baranova, Nouha El Amri, Liliane Coche-Guérente, Claude Verdier, Lionel Bureau, Ralf P. Richter, and Delphine Débarre. “Blood Cell-Vessel Wall Interactions Probed by Reflection Interference Contrast Microscopy.” In <i>Advances in Microscopic Imaging II</i>, Vol. 11076. SPIE, 2019. <a href=\"https://doi.org/10.1117/12.2527058\">https://doi.org/10.1117/12.2527058</a>.","ieee":"H. S. Davies <i>et al.</i>, “Blood cell-vessel wall interactions probed by reflection interference contrast microscopy,” in <i>Advances in Microscopic Imaging II</i>, Munich, Germany, 2019, vol. 11076.","short":"H.S. Davies, N.S. Baranova, N. El Amri, L. Coche-Guérente, C. Verdier, L. Bureau, R.P. Richter, D. Débarre, in:, Advances in Microscopic Imaging II, SPIE, 2019.","mla":"Davies, Heather S., et al. “Blood Cell-Vessel Wall Interactions Probed by Reflection Interference Contrast Microscopy.” <i>Advances in Microscopic Imaging II</i>, vol. 11076, 110760V, SPIE, 2019, doi:<a href=\"https://doi.org/10.1117/12.2527058\">10.1117/12.2527058</a>.","ista":"Davies HS, Baranova NS, El Amri N, Coche-Guérente L, Verdier C, Bureau L, Richter RP, Débarre D. 2019. Blood cell-vessel wall interactions probed by reflection interference contrast microscopy. Advances in Microscopic Imaging II. European Conferences on Biomedical Optics vol. 11076, 110760V."},"year":"2019","volume":11076,"title":"Blood cell-vessel wall interactions probed by reflection interference contrast microscopy","intvolume":"     11076","publication_status":"published","article_processing_charge":"No","date_created":"2019-11-12T15:10:18Z","department":[{"_id":"MaLo"}],"author":[{"first_name":"Heather S.","last_name":"Davies","full_name":"Davies, Heather S."},{"last_name":"Baranova","first_name":"Natalia S.","full_name":"Baranova, Natalia S.","orcid":"0000-0002-3086-9124","id":"38661662-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Nouha","last_name":"El Amri","full_name":"El Amri, Nouha"},{"last_name":"Coche-Guérente","first_name":"Liliane","full_name":"Coche-Guérente, Liliane"},{"last_name":"Verdier","first_name":"Claude","full_name":"Verdier, Claude"},{"first_name":"Lionel","last_name":"Bureau","full_name":"Bureau, Lionel"},{"full_name":"Richter, Ralf P.","last_name":"Richter","first_name":"Ralf P."},{"first_name":"Delphine","last_name":"Débarre","full_name":"Débarre, Delphine"}],"_id":"7010","scopus_import":"1","publisher":"SPIE","quality_controlled":"1","oa":1,"publication_identifier":{"isbn":["9781510628458"],"issn":["1605-7422"]},"date_published":"2019-07-22T00:00:00Z","type":"conference","status":"public","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","main_file_link":[{"url":"https://hal.archives-ouvertes.fr/hal-02368135/file/110760V.pdf","open_access":"1"}],"month":"07","article_number":"110760V","oa_version":"Published Version","publication":"Advances in Microscopic Imaging II","conference":{"end_date":"2019-06-27","location":"Munich, Germany","name":"European Conferences on Biomedical Optics","start_date":"2019-06-26"},"language":[{"iso":"eng"}]},{"title":"Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA","intvolume":"        10","publication_status":"published","department":[{"_id":"MaLo"},{"_id":"BjHo"}],"article_processing_charge":"No","date_created":"2019-12-20T12:22:57Z","author":[{"id":"38FCDB4C-F248-11E8-B48F-1D18A9856A87","first_name":"Paulo R","last_name":"Dos Santos Caldas","orcid":"0000-0001-6730-4461","full_name":"Dos Santos Caldas, Paulo R"},{"full_name":"Lopez Pelegrin, Maria D","last_name":"Lopez Pelegrin","first_name":"Maria D","id":"319AA9CE-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Pearce, Daniel J. G.","last_name":"Pearce","first_name":"Daniel J. G."},{"id":"3EA1010E-F248-11E8-B48F-1D18A9856A87","first_name":"Nazmi B","last_name":"Budanur","orcid":"0000-0003-0423-5010","full_name":"Budanur, Nazmi B"},{"first_name":"Jan","last_name":"Brugués","full_name":"Brugués, Jan"},{"full_name":"Loose, Martin","orcid":"0000-0001-7309-9724","last_name":"Loose","first_name":"Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87"}],"_id":"7197","scopus_import":"1","article_type":"original","publisher":"Springer Nature","file_date_updated":"2020-07-14T12:47:53Z","quality_controlled":"1","ec_funded":1,"abstract":[{"text":"During bacterial cell division, the tubulin-homolog FtsZ forms a ring-like structure at the center of the cell. This Z-ring not only organizes the division machinery, but treadmilling of FtsZ filaments was also found to play a key role in distributing proteins at the division site. What regulates the architecture, dynamics and stability of the Z-ring is currently unknown, but FtsZ-associated proteins are known to play an important role. Here, using an in vitro reconstitution approach, we studied how the well-conserved protein ZapA affects FtsZ treadmilling and filament organization into large-scale patterns. Using high-resolution fluorescence microscopy and quantitative image analysis, we found that ZapA cooperatively increases the spatial order of the filament network, but binds only transiently to FtsZ filaments and has no effect on filament length and treadmilling velocity. Together, our data provides a model for how FtsZ-associated proteins can increase the precision and stability of the bacterial cell division machinery in a switch-like manner.","lang":"eng"}],"doi":"10.1038/s41467-019-13702-4","day":"17","isi":1,"external_id":{"isi":["000503009300001"]},"date_updated":"2023-09-07T13:18:51Z","year":"2019","citation":{"mla":"Dos Santos Caldas, Paulo R., et al. “Cooperative Ordering of Treadmilling Filaments in Cytoskeletal Networks of FtsZ and Its Crosslinker ZapA.” <i>Nature Communications</i>, vol. 10, 5744, Springer Nature, 2019, doi:<a href=\"https://doi.org/10.1038/s41467-019-13702-4\">10.1038/s41467-019-13702-4</a>.","short":"P.R. Dos Santos Caldas, M.D. Lopez Pelegrin, D.J.G. Pearce, N.B. Budanur, J. Brugués, M. Loose, Nature Communications 10 (2019).","ista":"Dos Santos Caldas PR, Lopez Pelegrin MD, Pearce DJG, Budanur NB, Brugués J, Loose M. 2019. Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA. Nature Communications. 10, 5744.","apa":"Dos Santos Caldas, P. R., Lopez Pelegrin, M. D., Pearce, D. J. G., Budanur, N. B., Brugués, J., &#38; Loose, M. (2019). Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-019-13702-4\">https://doi.org/10.1038/s41467-019-13702-4</a>","ama":"Dos Santos Caldas PR, Lopez Pelegrin MD, Pearce DJG, Budanur NB, Brugués J, Loose M. Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA. <i>Nature Communications</i>. 2019;10. doi:<a href=\"https://doi.org/10.1038/s41467-019-13702-4\">10.1038/s41467-019-13702-4</a>","ieee":"P. R. Dos Santos Caldas, M. D. Lopez Pelegrin, D. J. G. Pearce, N. B. Budanur, J. Brugués, and M. Loose, “Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA,” <i>Nature Communications</i>, vol. 10. Springer Nature, 2019.","chicago":"Dos Santos Caldas, Paulo R, Maria D Lopez Pelegrin, Daniel J. G. Pearce, Nazmi B Budanur, Jan Brugués, and Martin Loose. “Cooperative Ordering of Treadmilling Filaments in Cytoskeletal Networks of FtsZ and Its Crosslinker ZapA.” <i>Nature Communications</i>. Springer Nature, 2019. <a href=\"https://doi.org/10.1038/s41467-019-13702-4\">https://doi.org/10.1038/s41467-019-13702-4</a>."},"ddc":["570"],"volume":10,"month":"12","article_number":"5744","oa_version":"Published Version","acknowledged_ssus":[{"_id":"LifeSc"},{"_id":"Bio"}],"project":[{"_id":"2595697A-B435-11E9-9278-68D0E5697425","call_identifier":"H2020","grant_number":"679239","name":"Self-Organization of the Bacterial Cell"},{"_id":"260D98C8-B435-11E9-9278-68D0E5697425","name":"Reconstitution of Bacterial Cell Division Using Purified Components"}],"publication":"Nature Communications","has_accepted_license":"1","language":[{"iso":"eng"}],"oa":1,"publication_identifier":{"issn":["2041-1723"]},"date_published":"2019-12-17T00:00:00Z","type":"journal_article","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"status":"public","related_material":{"record":[{"status":"public","relation":"dissertation_contains","id":"8358"}]},"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","file":[{"date_updated":"2020-07-14T12:47:53Z","content_type":"application/pdf","file_name":"2019_NatureComm_Caldas.pdf","date_created":"2019-12-23T07:34:56Z","file_size":8488733,"checksum":"a1b44b427ba341383197790d0e8789fa","file_id":"7208","creator":"dernst","access_level":"open_access","relation":"main_file"}]},{"status":"public","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","file":[{"creator":"dernst","file_id":"7825","access_level":"open_access","relation":"main_file","content_type":"application/pdf","file_name":"2018_MatrixBiology_Davies.pdf","date_updated":"2020-07-14T12:47:27Z","file_size":4444339,"checksum":"790878cd78bfc54a147ddcc7c8f286a0","date_created":"2020-05-14T09:02:07Z"}],"oa":1,"publication_identifier":{"issn":["0945-053X"]},"type":"journal_article","date_published":"2019-05-01T00:00:00Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","image":"/images/cc_by_nc_nd.png"},"language":[{"iso":"eng"}],"month":"05","oa_version":"Submitted Version","has_accepted_license":"1","publication":"Matrix Biology","ddc":["570"],"volume":"78-79","abstract":[{"lang":"eng","text":"Cell-cell and cell-glycocalyx interactions under flow are important for the behaviour of circulating cells in blood and lymphatic vessels. However, such interactions are not well understood due in part to a lack of tools to study them in defined environments. Here, we develop a versatile in vitro platform for the study of cell-glycocalyx interactions in well-defined physical and chemical settings under flow. Our approach is demonstrated with the interaction between hyaluronan (HA, a key component of the endothelial glycocalyx) and its cell receptor CD44. We generate HA brushes in situ within a microfluidic device, and demonstrate the tuning of their physical (thickness and softness) and chemical (density of CD44 binding sites) properties using characterisation with reflection interference contrast microscopy (RICM) and application of polymer theory. We highlight the interactions of HA brushes with CD44-displaying beads and cells under flow. Observations of CD44+ beads on a HA brush with RICM enabled the 3-dimensional trajectories to be generated, and revealed interactions in the form of stop and go phases with reduced rolling velocity and reduced distance between the bead and the HA brush, compared to uncoated beads. Combined RICM and bright-field microscopy of CD44+ AKR1 T-lymphocytes revealed complementary information about the dynamics of cell rolling and cell morphology, and highlighted the formation of tethers and slings, as they interacted with a HA brush under flow. This platform can readily incorporate more complex models of the glycocalyx, and should permit the study of how mechanical and biochemical factors are orchestrated to enable highly selective blood cell-vessel wall interactions under flow."}],"day":"01","doi":"10.1016/j.matbio.2018.12.002","external_id":{"isi":["000468707600005"]},"isi":1,"year":"2019","citation":{"apa":"Davies, H. S., Baranova, N. S., El Amri, N., Coche-Guérente, L., Verdier, C., Bureau, L., … Débarre, D. (2019). An integrated assay to probe endothelial glycocalyx-blood cell interactions under flow in mechanically and biochemically well-defined environments. <i>Matrix Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.matbio.2018.12.002\">https://doi.org/10.1016/j.matbio.2018.12.002</a>","ama":"Davies HS, Baranova NS, El Amri N, et al. An integrated assay to probe endothelial glycocalyx-blood cell interactions under flow in mechanically and biochemically well-defined environments. <i>Matrix Biology</i>. 2019;78-79:47-59. doi:<a href=\"https://doi.org/10.1016/j.matbio.2018.12.002\">10.1016/j.matbio.2018.12.002</a>","chicago":"Davies, Heather S., Natalia S. Baranova, Nouha El Amri, Liliane Coche-Guérente, Claude Verdier, Lionel Bureau, Ralf P. Richter, and Delphine Débarre. “An Integrated Assay to Probe Endothelial Glycocalyx-Blood Cell Interactions under Flow in Mechanically and Biochemically Well-Defined Environments.” <i>Matrix Biology</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.matbio.2018.12.002\">https://doi.org/10.1016/j.matbio.2018.12.002</a>.","ieee":"H. S. Davies <i>et al.</i>, “An integrated assay to probe endothelial glycocalyx-blood cell interactions under flow in mechanically and biochemically well-defined environments,” <i>Matrix Biology</i>, vol. 78–79. Elsevier, pp. 47–59, 2019.","short":"H.S. Davies, N.S. Baranova, N. El Amri, L. Coche-Guérente, C. Verdier, L. Bureau, R.P. Richter, D. Débarre, Matrix Biology 78–79 (2019) 47–59.","mla":"Davies, Heather S., et al. “An Integrated Assay to Probe Endothelial Glycocalyx-Blood Cell Interactions under Flow in Mechanically and Biochemically Well-Defined Environments.” <i>Matrix Biology</i>, vol. 78–79, Elsevier, 2019, pp. 47–59, doi:<a href=\"https://doi.org/10.1016/j.matbio.2018.12.002\">10.1016/j.matbio.2018.12.002</a>.","ista":"Davies HS, Baranova NS, El Amri N, Coche-Guérente L, Verdier C, Bureau L, Richter RP, Débarre D. 2019. An integrated assay to probe endothelial glycocalyx-blood cell interactions under flow in mechanically and biochemically well-defined environments. Matrix Biology. 78–79, 47–59."},"date_updated":"2023-08-25T10:11:28Z","article_type":"original","publisher":"Elsevier","file_date_updated":"2020-07-14T12:47:27Z","quality_controlled":"1","page":"47-59","title":"An integrated assay to probe endothelial glycocalyx-blood cell interactions under flow in mechanically and biochemically well-defined environments","article_processing_charge":"No","date_created":"2019-04-11T20:55:01Z","department":[{"_id":"MaLo"}],"publication_status":"published","author":[{"full_name":"Davies, Heather S.","last_name":"Davies","first_name":"Heather S."},{"full_name":"Baranova, Natalia S.","orcid":"0000-0002-3086-9124","last_name":"Baranova","first_name":"Natalia S.","id":"38661662-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Nouha","last_name":"El Amri","full_name":"El Amri, Nouha"},{"full_name":"Coche-Guérente, Liliane","first_name":"Liliane","last_name":"Coche-Guérente"},{"last_name":"Verdier","first_name":"Claude","full_name":"Verdier, Claude"},{"last_name":"Bureau","first_name":"Lionel","full_name":"Bureau, Lionel"},{"full_name":"Richter, Ralf P.","first_name":"Ralf P.","last_name":"Richter"},{"full_name":"Débarre, Delphine","last_name":"Débarre","first_name":"Delphine"}],"_id":"6297"},{"acknowledgement":"This work was supported by the European Research Council [Starting Grant 306435 ‘JELLY’; to RPR], the Spanish Ministry of Competitiveness and Innovation [MAT2014-54867-R, to RPR], the EPSRC Centre for Doctoral Training in Tissue Engineering and Regenerative Medicine — Innovation in Medical and Biological Engineering [EP/L014823/1, to JCFK], the Royal Society [RG160410, to JCFK], Wings for Life [WFL-UK-008/15, to JCFK] and the European Union, the Operational Programme Research, Development and Education in the framework of the project ‘Centre of Reconstructive Neuroscience’ [CZ.02.1.01/0.0./0.0/15_003/0000419, to JCFK]. AJD would like to thank Arthritis Research UK [16539, 19489] and the MRC [76445, G0900538] for funding his work on GAG–protein interactions.\r\n","volume":50,"doi":"10.1016/j.sbi.2017.12.002","day":"01","abstract":[{"text":"Conventional wisdom has it that proteins fold and assemble into definite structures, and that this defines their function. Glycosaminoglycans (GAGs) are different. In most cases the structures they form have a low degree of order, even when interacting with proteins. Here, we discuss how physical features common to all GAGs — hydrophilicity, charge, linearity and semi-flexibility — underpin the overall properties of GAG-rich matrices. By integrating soft matter physics concepts (e.g. polymer brushes and phase separation) with our molecular understanding of GAG–protein interactions, we can better comprehend how GAG-rich matrices assemble, what their properties are, and how they function. Taking perineuronal nets (PNNs) — a GAG-rich matrix enveloping neurons — as a relevant example, we propose that microphase separation determines the holey PNN anatomy that is pivotal to PNN functions.","lang":"eng"}],"date_updated":"2023-09-11T14:07:03Z","year":"2018","citation":{"mla":"Richter, Ralf, et al. “Glycosaminoglycans in Extracellular Matrix Organisation: Are Concepts from Soft Matter Physics Key to Understanding the Formation of Perineuronal Nets?” <i>Current Opinion in Structural Biology</i>, vol. 50, Elsevier, 2018, pp. 65–74, doi:<a href=\"https://doi.org/10.1016/j.sbi.2017.12.002\">10.1016/j.sbi.2017.12.002</a>.","short":"R. Richter, N.S. Baranova, A. Day, J. Kwok, Current Opinion in Structural Biology 50 (2018) 65–74.","ista":"Richter R, Baranova NS, 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. 50, 65–74.","ama":"Richter R, Baranova NS, Day A, Kwok J. Glycosaminoglycans in extracellular matrix organisation: Are concepts from soft matter physics key to understanding the formation of perineuronal nets? <i>Current Opinion in Structural Biology</i>. 2018;50:65-74. doi:<a href=\"https://doi.org/10.1016/j.sbi.2017.12.002\">10.1016/j.sbi.2017.12.002</a>","apa":"Richter, R., Baranova, N. S., Day, A., &#38; Kwok, J. (2018). Glycosaminoglycans in extracellular matrix organisation: Are concepts from soft matter physics key to understanding the formation of perineuronal nets? <i>Current Opinion in Structural Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.sbi.2017.12.002\">https://doi.org/10.1016/j.sbi.2017.12.002</a>","ieee":"R. Richter, N. S. Baranova, A. Day, and J. Kwok, “Glycosaminoglycans in extracellular matrix organisation: Are concepts from soft matter physics key to understanding the formation of perineuronal nets?,” <i>Current Opinion in Structural Biology</i>, vol. 50. Elsevier, pp. 65–74, 2018.","chicago":"Richter, Ralf, Natalia S. Baranova, Anthony Day, and Jessica Kwok. “Glycosaminoglycans in Extracellular Matrix Organisation: Are Concepts from Soft Matter Physics Key to Understanding the Formation of Perineuronal Nets?” <i>Current Opinion in Structural Biology</i>. Elsevier, 2018. <a href=\"https://doi.org/10.1016/j.sbi.2017.12.002\">https://doi.org/10.1016/j.sbi.2017.12.002</a>."},"isi":1,"external_id":{"isi":["000443661300011"]},"publisher":"Elsevier","article_type":"original","page":"65 - 74","quality_controlled":"1","publication_status":"published","article_processing_charge":"No","department":[{"_id":"MaLo"}],"date_created":"2018-12-11T11:47:09Z","title":"Glycosaminoglycans in extracellular matrix organisation: Are concepts from soft matter physics key to understanding the formation of perineuronal nets?","intvolume":"        50","_id":"555","scopus_import":"1","author":[{"full_name":"Richter, Ralf","last_name":"Richter","first_name":"Ralf"},{"id":"38661662-F248-11E8-B48F-1D18A9856A87","first_name":"Natalia","last_name":"Baranova","orcid":"0000-0002-3086-9124","full_name":"Baranova, Natalia"},{"first_name":"Anthony","last_name":"Day","full_name":"Day, Anthony"},{"first_name":"Jessica","last_name":"Kwok","full_name":"Kwok, Jessica"}],"main_file_link":[{"url":"http://eprints.whiterose.ac.uk/125524/","open_access":"1"}],"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","status":"public","oa":1,"publist_id":"7259","date_published":"2018-06-01T00:00:00Z","type":"journal_article","language":[{"iso":"eng"}],"oa_version":"Submitted Version","month":"06","publication":"Current Opinion in Structural Biology"},{"has_accepted_license":"1","publication":"Molecular Therapy","oa_version":"Published Version","month":"01","language":[{"iso":"eng"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","image":"/images/cc_by_nc_nd.png"},"type":"journal_article","date_published":"2017-01-01T00:00:00Z","publication_identifier":{"issn":["1525-0016"]},"oa":1,"file":[{"access_level":"open_access","relation":"main_file","file_id":"7561","creator":"dernst","date_created":"2020-03-03T10:55:13Z","checksum":"ea8b1b28606dd1edab7379ba4fa3641f","file_size":3404806,"date_updated":"2020-07-14T12:47:56Z","file_name":"2017_MolecularTherapy_Smole.pdf","content_type":"application/pdf"}],"status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"7360","pmid":1,"issue":"1","author":[{"full_name":"Smole, Anže","last_name":"Smole","first_name":"Anže"},{"full_name":"Lainšček, Duško","first_name":"Duško","last_name":"Lainšček"},{"id":"2A58201A-F248-11E8-B48F-1D18A9856A87","full_name":"Bezeljak, Urban","orcid":"0000-0003-1365-5631","last_name":"Bezeljak","first_name":"Urban"},{"last_name":"Horvat","first_name":"Simon","full_name":"Horvat, Simon"},{"last_name":"Jerala","first_name":"Roman","full_name":"Jerala, Roman"}],"department":[{"_id":"MaLo"}],"article_processing_charge":"No","date_created":"2020-01-25T15:55:39Z","publication_status":"published","intvolume":"        25","title":"A synthetic mammalian therapeutic gene circuit for sensing and suppressing inflammation","quality_controlled":"1","page":"102-119","file_date_updated":"2020-07-14T12:47:56Z","publisher":"Elsevier","article_type":"original","year":"2017","citation":{"ama":"Smole A, Lainšček D, Bezeljak U, Horvat S, Jerala R. A synthetic mammalian therapeutic gene circuit for sensing and suppressing inflammation. <i>Molecular Therapy</i>. 2017;25(1):102-119. doi:<a href=\"https://doi.org/10.1016/j.ymthe.2016.10.005\">10.1016/j.ymthe.2016.10.005</a>","apa":"Smole, A., Lainšček, D., Bezeljak, U., Horvat, S., &#38; Jerala, R. (2017). A synthetic mammalian therapeutic gene circuit for sensing and suppressing inflammation. <i>Molecular Therapy</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.ymthe.2016.10.005\">https://doi.org/10.1016/j.ymthe.2016.10.005</a>","ieee":"A. Smole, D. Lainšček, U. Bezeljak, S. Horvat, and R. Jerala, “A synthetic mammalian therapeutic gene circuit for sensing and suppressing inflammation,” <i>Molecular Therapy</i>, vol. 25, no. 1. Elsevier, pp. 102–119, 2017.","chicago":"Smole, Anže, Duško Lainšček, Urban Bezeljak, Simon Horvat, and Roman Jerala. “A Synthetic Mammalian Therapeutic Gene Circuit for Sensing and Suppressing Inflammation.” <i>Molecular Therapy</i>. Elsevier, 2017. <a href=\"https://doi.org/10.1016/j.ymthe.2016.10.005\">https://doi.org/10.1016/j.ymthe.2016.10.005</a>.","short":"A. Smole, D. Lainšček, U. Bezeljak, S. Horvat, R. Jerala, Molecular Therapy 25 (2017) 102–119.","mla":"Smole, Anže, et al. “A Synthetic Mammalian Therapeutic Gene Circuit for Sensing and Suppressing Inflammation.” <i>Molecular Therapy</i>, vol. 25, no. 1, Elsevier, 2017, pp. 102–19, doi:<a href=\"https://doi.org/10.1016/j.ymthe.2016.10.005\">10.1016/j.ymthe.2016.10.005</a>.","ista":"Smole A, Lainšček D, Bezeljak U, Horvat S, Jerala R. 2017. A synthetic mammalian therapeutic gene circuit for sensing and suppressing inflammation. Molecular Therapy. 25(1), 102–119."},"date_updated":"2021-01-12T08:13:14Z","external_id":{"pmid":["28129106"]},"day":"01","doi":"10.1016/j.ymthe.2016.10.005","abstract":[{"text":"Inflammation, which is a highly regulated host response against danger signals, may be harmful if it is excessive and deregulated. Ideally, anti-inflammatory therapy should autonomously commence as soon as possible after the onset of inflammation, should be controllable by a physician, and should not systemically block beneficial immune response in the long term. We describe a genetically encoded anti-inflammatory mammalian cell device based on a modular engineered genetic circuit comprising a sensor, an amplifier, a “thresholder” to restrict activation of a positive-feedback loop, a combination of advanced clinically used biopharmaceutical proteins, and orthogonal regulatory elements that linked modules into the functional device. This genetic circuit was autonomously activated by inflammatory signals, including endogenous cecal ligation and puncture (CLP)-induced inflammation in mice and serum from a systemic juvenile idiopathic arthritis (sIJA) patient, and could be reset externally by a chemical signal. The microencapsulated anti-inflammatory device significantly reduced the pathology in dextran sodium sulfate (DSS)-induced acute murine colitis, demonstrating a synthetic immunological approach for autonomous anti-inflammatory therapy.","lang":"eng"}],"volume":25,"ddc":["570"]},{"_id":"629","pmid":1,"scopus_import":1,"author":[{"orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","first_name":"Martin","last_name":"Loose","id":"462D4284-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Zieske, Katja","last_name":"Zieske","first_name":"Katja"},{"last_name":"Schwille","first_name":"Petra","full_name":"Schwille, Petra"}],"publication_status":"published","date_created":"2018-12-11T11:47:35Z","department":[{"_id":"MaLo"}],"title":"Reconstitution of protein dynamics involved in bacterial cell division","intvolume":"        84","page":"419 - 444","quality_controlled":"1","series_title":"Sub-Cellular Biochemistry","publisher":"Springer","date_updated":"2021-01-12T08:06:57Z","year":"2017","citation":{"ista":"Loose M, Zieske K, Schwille P. 2017.Reconstitution of protein dynamics involved in bacterial cell division. In: Prokaryotic Cytoskeletons. vol. 84, 419–444.","short":"M. Loose, K. Zieske, P. Schwille, in:, Prokaryotic Cytoskeletons, Springer, 2017, pp. 419–444.","mla":"Loose, Martin, et al. “Reconstitution of Protein Dynamics Involved in Bacterial Cell Division.” <i>Prokaryotic Cytoskeletons</i>, vol. 84, Springer, 2017, pp. 419–44, doi:<a href=\"https://doi.org/10.1007/978-3-319-53047-5_15\">10.1007/978-3-319-53047-5_15</a>.","chicago":"Loose, Martin, Katja Zieske, and Petra Schwille. “Reconstitution of Protein Dynamics Involved in Bacterial Cell Division.” In <i>Prokaryotic Cytoskeletons</i>, 84:419–44. Sub-Cellular Biochemistry. Springer, 2017. <a href=\"https://doi.org/10.1007/978-3-319-53047-5_15\">https://doi.org/10.1007/978-3-319-53047-5_15</a>.","ieee":"M. Loose, K. Zieske, and P. Schwille, “Reconstitution of protein dynamics involved in bacterial cell division,” in <i>Prokaryotic Cytoskeletons</i>, vol. 84, Springer, 2017, pp. 419–444.","ama":"Loose M, Zieske K, Schwille P. Reconstitution of protein dynamics involved in bacterial cell division. In: <i>Prokaryotic Cytoskeletons</i>. Vol 84. Sub-Cellular Biochemistry. Springer; 2017:419-444. doi:<a href=\"https://doi.org/10.1007/978-3-319-53047-5_15\">10.1007/978-3-319-53047-5_15</a>","apa":"Loose, M., Zieske, K., &#38; Schwille, P. (2017). Reconstitution of protein dynamics involved in bacterial cell division. In <i>Prokaryotic Cytoskeletons</i> (Vol. 84, pp. 419–444). Springer. <a href=\"https://doi.org/10.1007/978-3-319-53047-5_15\">https://doi.org/10.1007/978-3-319-53047-5_15</a>"},"external_id":{"pmid":["28500535"]},"doi":"10.1007/978-3-319-53047-5_15","day":"13","abstract":[{"text":"Even simple cells like bacteria have precisely regulated cellular anatomies, which allow them to grow, divide and to respond to internal or external cues with high fidelity. How spatial and temporal intracellular organization in prokaryotic cells is achieved and maintained on the basis of locally interacting proteins still remains largely a mystery. Bulk biochemical assays with purified components and in vivo experiments help us to approach key cellular processes from two opposite ends, in terms of minimal and maximal complexity. However, to understand how cellular phenomena emerge, that are more than the sum of their parts, we have to assemble cellular subsystems step by step from the bottom up. Here, we review recent in vitro reconstitution experiments with proteins of the bacterial cell division machinery and illustrate how they help to shed light on fundamental cellular mechanisms that constitute spatiotemporal order and regulate cell division.","lang":"eng"}],"volume":84,"publication":"Prokaryotic Cytoskeletons","oa_version":"None","month":"05","language":[{"iso":"eng"}],"date_published":"2017-05-13T00:00:00Z","type":"book_chapter","publication_identifier":{"eisbn":["978-3-319-53047-5"]},"publist_id":"7165","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public"},{"publist_id":"7073","oa":1,"publication_identifier":{"issn":["00278424"]},"date_published":"2017-03-28T00:00:00Z","type":"journal_article","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","main_file_link":[{"open_access":"1","url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5380103/"}],"month":"03","oa_version":"Submitted Version","publication":"PNAS","language":[{"iso":"eng"}],"abstract":[{"text":"Growing microtubules are protected from depolymerization by the presence of a GTP or GDP/Pi cap. End-binding proteins of the EB1 family bind to the stabilizing cap, allowing monitoring of its size in real time. The cap size has been shown to correlate with instantaneous microtubule stability. Here we have quantitatively characterized the properties of cap size fluctuations during steadystate growth and have developed a theory predicting their timescale and amplitude from the kinetics of microtubule growth and cap maturation. In contrast to growth speed fluctuations, cap size fluctuations show a characteristic timescale, which is defined by the lifetime of the cap sites. Growth fluctuations affect the amplitude of cap size fluctuations; however, cap size does not affect growth speed, indicating that microtubules are far from instability during most of their time of growth. Our theory provides the basis for a quantitative understanding of microtubule stability fluctuations during steady-state growth.","lang":"eng"}],"doi":"10.1073/pnas.1620274114","day":"28","external_id":{"pmid":["28280102"]},"date_updated":"2021-01-12T08:08:09Z","citation":{"chicago":"Rickman, Jamie, Christian F Düllberg, Nicholas Cade, Lewis Griffin, and Thomas Surrey. “Steady State EB Cap Size Fluctuations Are Determined by Stochastic Microtubule Growth and Maturation.” <i>PNAS</i>. National Academy of Sciences, 2017. <a href=\"https://doi.org/10.1073/pnas.1620274114\">https://doi.org/10.1073/pnas.1620274114</a>.","ieee":"J. Rickman, C. F. Düllberg, N. Cade, L. Griffin, and T. Surrey, “Steady state EB cap size fluctuations are determined by stochastic microtubule growth and maturation,” <i>PNAS</i>, vol. 114, no. 13. National Academy of Sciences, pp. 3427–3432, 2017.","ama":"Rickman J, Düllberg CF, Cade N, Griffin L, Surrey T. Steady state EB cap size fluctuations are determined by stochastic microtubule growth and maturation. <i>PNAS</i>. 2017;114(13):3427-3432. doi:<a href=\"https://doi.org/10.1073/pnas.1620274114\">10.1073/pnas.1620274114</a>","apa":"Rickman, J., Düllberg, C. F., Cade, N., Griffin, L., &#38; Surrey, T. (2017). Steady state EB cap size fluctuations are determined by stochastic microtubule growth and maturation. <i>PNAS</i>. National Academy of Sciences. <a href=\"https://doi.org/10.1073/pnas.1620274114\">https://doi.org/10.1073/pnas.1620274114</a>","ista":"Rickman J, Düllberg CF, Cade N, Griffin L, Surrey T. 2017. Steady state EB cap size fluctuations are determined by stochastic microtubule growth and maturation. PNAS. 114(13), 3427–3432.","mla":"Rickman, Jamie, et al. “Steady State EB Cap Size Fluctuations Are Determined by Stochastic Microtubule Growth and Maturation.” <i>PNAS</i>, vol. 114, no. 13, National Academy of Sciences, 2017, pp. 3427–32, doi:<a href=\"https://doi.org/10.1073/pnas.1620274114\">10.1073/pnas.1620274114</a>.","short":"J. Rickman, C.F. Düllberg, N. Cade, L. Griffin, T. Surrey, PNAS 114 (2017) 3427–3432."},"year":"2017","acknowledgement":"We thank Philippe Cluzel for helpful discussions and Gunnar Pruessner for data analysis advice. This work was supported by the Francis Crick Institute, which receives its core funding from Cancer Research UK Grant FC001163, Medical Research Council Grant FC001163, and Wellcome Trust Grant FC001163. This work was also supported by European Research Council Advanced Grant Project 323042 (to C.D. and T.S.).","volume":114,"title":"Steady state EB cap size fluctuations are determined by stochastic microtubule growth and maturation","intvolume":"       114","publication_status":"published","date_created":"2018-12-11T11:47:46Z","department":[{"_id":"MaLo"}],"author":[{"full_name":"Rickman, Jamie","last_name":"Rickman","first_name":"Jamie"},{"last_name":"Düllberg","first_name":"Christian F","full_name":"Düllberg, Christian F","orcid":"0000-0001-6335-9748","id":"459064DC-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Nicholas","last_name":"Cade","full_name":"Cade, Nicholas"},{"full_name":"Griffin, Lewis","last_name":"Griffin","first_name":"Lewis"},{"full_name":"Surrey, Thomas","first_name":"Thomas","last_name":"Surrey"}],"issue":"13","pmid":1,"_id":"660","scopus_import":1,"publisher":"National Academy of Sciences","page":"3427 - 3432","quality_controlled":"1"},{"_id":"960","scopus_import":"1","author":[{"id":"38853E16-F248-11E8-B48F-1D18A9856A87","first_name":"Andi H","last_name":"Hansen","full_name":"Hansen, Andi H"},{"orcid":"0000-0001-6335-9748","full_name":"Düllberg, Christian F","first_name":"Christian F","last_name":"Düllberg","id":"459064DC-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Mieck, Christine","orcid":"0000-0003-1919-7416","last_name":"Mieck","first_name":"Christine","id":"34CAE85C-F248-11E8-B48F-1D18A9856A87"},{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","first_name":"Martin","last_name":"Loose"},{"full_name":"Hippenmeyer, Simon","orcid":"0000-0003-2279-1061","last_name":"Hippenmeyer","first_name":"Simon","id":"37B36620-F248-11E8-B48F-1D18A9856A87"}],"publication_status":"published","department":[{"_id":"SiHi"},{"_id":"MaLo"}],"date_created":"2018-12-11T11:49:25Z","article_processing_charge":"Yes","pubrep_id":"830","title":"Cell polarity in cerebral cortex development - cellular architecture shaped by biochemical networks","intvolume":"        11","quality_controlled":"1","ec_funded":1,"file_date_updated":"2020-07-14T12:48:16Z","publisher":"Frontiers Research Foundation","date_updated":"2024-03-25T23:30:23Z","year":"2017","citation":{"short":"A.H. Hansen, C.F. Düllberg, C. Mieck, M. Loose, S. Hippenmeyer, Frontiers in Cellular Neuroscience 11 (2017).","mla":"Hansen, Andi H., et al. “Cell Polarity in Cerebral Cortex Development - Cellular Architecture Shaped by Biochemical Networks.” <i>Frontiers in Cellular Neuroscience</i>, vol. 11, 176, Frontiers Research Foundation, 2017, doi:<a href=\"https://doi.org/10.3389/fncel.2017.00176\">10.3389/fncel.2017.00176</a>.","ista":"Hansen AH, Düllberg CF, Mieck C, Loose M, Hippenmeyer S. 2017. Cell polarity in cerebral cortex development - cellular architecture shaped by biochemical networks. Frontiers in Cellular Neuroscience. 11, 176.","apa":"Hansen, A. H., Düllberg, C. F., Mieck, C., Loose, M., &#38; Hippenmeyer, S. (2017). Cell polarity in cerebral cortex development - cellular architecture shaped by biochemical networks. <i>Frontiers in Cellular Neuroscience</i>. Frontiers Research Foundation. <a href=\"https://doi.org/10.3389/fncel.2017.00176\">https://doi.org/10.3389/fncel.2017.00176</a>","ama":"Hansen AH, Düllberg CF, Mieck C, Loose M, Hippenmeyer S. Cell polarity in cerebral cortex development - cellular architecture shaped by biochemical networks. <i>Frontiers in Cellular Neuroscience</i>. 2017;11. doi:<a href=\"https://doi.org/10.3389/fncel.2017.00176\">10.3389/fncel.2017.00176</a>","ieee":"A. H. Hansen, C. F. Düllberg, C. Mieck, M. Loose, and S. Hippenmeyer, “Cell polarity in cerebral cortex development - cellular architecture shaped by biochemical networks,” <i>Frontiers in Cellular Neuroscience</i>, vol. 11. Frontiers Research Foundation, 2017.","chicago":"Hansen, Andi H, Christian F Düllberg, Christine Mieck, Martin Loose, and Simon Hippenmeyer. “Cell Polarity in Cerebral Cortex Development - Cellular Architecture Shaped by Biochemical Networks.” <i>Frontiers in Cellular Neuroscience</i>. Frontiers Research Foundation, 2017. <a href=\"https://doi.org/10.3389/fncel.2017.00176\">https://doi.org/10.3389/fncel.2017.00176</a>."},"isi":1,"external_id":{"isi":["000404486700001"]},"doi":"10.3389/fncel.2017.00176","day":"28","abstract":[{"lang":"eng","text":"The human cerebral cortex is the seat of our cognitive abilities and composed of an extraordinary number of neurons, organized in six distinct layers. The establishment of specific morphological and physiological features in individual neurons needs to be regulated with high precision. Impairments in the sequential developmental programs instructing corticogenesis lead to alterations in the cortical cytoarchitecture which is thought to represent the major underlying cause for several neurological disorders including neurodevelopmental and psychiatric diseases. In this review we discuss the role of cell polarity at sequential stages during cortex development. We first provide an overview of morphological cell polarity features in cortical neural stem cells and newly-born postmitotic neurons. We then synthesize a conceptual molecular and biochemical framework how cell polarity is established at the cellular level through a break in symmetry in nascent cortical projection neurons. Lastly we provide a perspective how the molecular mechanisms applying to single cells could be probed and integrated in an in vivo and tissue-wide context."}],"volume":11,"ddc":["570"],"publication":"Frontiers in Cellular Neuroscience","has_accepted_license":"1","oa_version":"Published Version","project":[{"name":"Molecular Mechanisms of Cerebral Cortex Development","grant_number":"618444","_id":"25D61E48-B435-11E9-9278-68D0E5697425","call_identifier":"FP7"},{"name":"Quantitative Structure-Function Analysis of Cerebral Cortex Assembly at Clonal Level","grant_number":"RGP0053/2014","_id":"25D7962E-B435-11E9-9278-68D0E5697425"},{"_id":"25681D80-B435-11E9-9278-68D0E5697425","call_identifier":"FP7","name":"International IST Postdoc Fellowship Programme","grant_number":"291734"},{"grant_number":"T00817-B21","name":"The biochemical basis of PAR polarization","_id":"25985A36-B435-11E9-9278-68D0E5697425","call_identifier":"FWF"}],"month":"06","article_number":"176","language":[{"iso":"eng"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"date_published":"2017-06-28T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["16625102"]},"oa":1,"publist_id":"6445","file":[{"file_size":2153858,"checksum":"dc1f5a475b918d09a0f9f587400b1626","date_created":"2018-12-12T10:09:40Z","file_name":"IST-2017-830-v1+1_2017_Hansen_CellPolarity.pdf","content_type":"application/pdf","date_updated":"2020-07-14T12:48:16Z","relation":"main_file","access_level":"open_access","creator":"system","file_id":"4764"}],"status":"public","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","related_material":{"record":[{"status":"public","id":"9962","relation":"dissertation_contains"}]}},{"type":"book_chapter","date_published":"2017-12-01T00:00:00Z","publication_identifier":{"issn":["0091679X"]},"publist_id":"6134","status":"public","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","publication":"Cytokinesis","project":[{"grant_number":"ALTF 2015-1163","name":"Synthesis of bacterial cell wall","_id":"2596EAB6-B435-11E9-9278-68D0E5697425"},{"_id":"25681D80-B435-11E9-9278-68D0E5697425","call_identifier":"FP7","grant_number":"291734","name":"International IST Postdoc Fellowship Programme"}],"acknowledged_ssus":[{"_id":"Bio"}],"oa_version":"None","month":"12","language":[{"iso":"eng"}],"citation":{"mla":"Baranova, Natalia S., and Martin Loose. “Single-Molecule Measurements to Study Polymerization Dynamics of FtsZ-FtsA Copolymers.” <i>Cytokinesis</i>, edited by Arnaud  Echard, vol. 137, Academic Press, 2017, pp. 355–70, doi:<a href=\"https://doi.org/10.1016/bs.mcb.2016.03.036\">10.1016/bs.mcb.2016.03.036</a>.","short":"N.S. Baranova, M. Loose, in:, A. Echard (Ed.), Cytokinesis, Academic Press, 2017, pp. 355–370.","ista":"Baranova NS, Loose M. 2017.Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA copolymers. In: Cytokinesis. Methods in Cell Biology, vol. 137, 355–370.","ama":"Baranova NS, Loose M. Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA copolymers. In: Echard A, ed. <i>Cytokinesis</i>. Vol 137. Academic Press; 2017:355-370. doi:<a href=\"https://doi.org/10.1016/bs.mcb.2016.03.036\">10.1016/bs.mcb.2016.03.036</a>","apa":"Baranova, N. S., &#38; Loose, M. (2017). Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA copolymers. In A. Echard (Ed.), <i>Cytokinesis</i> (Vol. 137, pp. 355–370). Academic Press. <a href=\"https://doi.org/10.1016/bs.mcb.2016.03.036\">https://doi.org/10.1016/bs.mcb.2016.03.036</a>","ieee":"N. S. Baranova and M. Loose, “Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA copolymers,” in <i>Cytokinesis</i>, vol. 137, A. Echard, Ed. Academic Press, 2017, pp. 355–370.","chicago":"Baranova, Natalia S., and Martin Loose. “Single-Molecule Measurements to Study Polymerization Dynamics of FtsZ-FtsA Copolymers.” In <i>Cytokinesis</i>, edited by Arnaud  Echard, 137:355–70. Academic Press, 2017. <a href=\"https://doi.org/10.1016/bs.mcb.2016.03.036\">https://doi.org/10.1016/bs.mcb.2016.03.036</a>."},"year":"2017","date_updated":"2023-09-20T11:16:30Z","external_id":{"isi":["000403542900022"]},"isi":1,"day":"01","doi":"10.1016/bs.mcb.2016.03.036","abstract":[{"text":"Bacterial cytokinesis is commonly initiated by the Z-ring, a dynamic cytoskeletal structure that assembles at the site of division. Its primary component is FtsZ, a tubulin-like GTPase, that like its eukaryotic relative forms protein filaments in the presence of GTP. Since the discovery of the Z-ring 25 years ago, various models for the role of FtsZ have been suggested. However, important information about the architecture and dynamics of FtsZ filaments during cytokinesis is still missing. One reason for this lack of knowledge has been the small size of bacteria, which has made it difficult to resolve the orientation and dynamics of individual FtsZ filaments in the Z-ring. While superresolution microscopy experiments have helped to gain more information about the organization of the Z-ring in the dividing cell, they were not yet able to elucidate a mechanism of how FtsZ filaments reorganize during assembly and disassembly of the Z-ring. In this chapter, we explain how to use an in vitro reconstitution approach to investigate the self-organization of FtsZ filaments recruited to a biomimetic lipid bilayer by its membrane anchor FtsA. We show how to perform single-molecule experiments to study the behavior of individual FtsZ monomers during the constant reorganization of the FtsZ-FtsA filament network. We describe how to analyze the dynamics of single molecules and explain why this information can help to shed light onto possible mechanism of Z-ring constriction. We believe that similar experimental approaches will be useful to study the mechanism of membrane-based polymerization of other cytoskeletal systems, not only from prokaryotic but also eukaryotic origin.","lang":"eng"}],"volume":137,"acknowledgement":"Natalia Baranova is supported by an EMBO Long-Term Fellowship (EMBO ALTF 1163-2015) and Martin Loose by an ERC Starting Grant (ERCStG-2015-SelfOrganiCell).","scopus_import":"1","_id":"1213","author":[{"id":"38661662-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-3086-9124","full_name":"Baranova, Natalia","first_name":"Natalia","last_name":"Baranova"},{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","last_name":"Loose","first_name":"Martin","full_name":"Loose, Martin","orcid":"0000-0001-7309-9724"}],"article_processing_charge":"No","department":[{"_id":"MaLo"}],"date_created":"2018-12-11T11:50:45Z","publication_status":"published","intvolume":"       137","alternative_title":["Methods in Cell Biology"],"title":"Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA copolymers","quality_controlled":"1","ec_funded":1,"page":"355 - 370","editor":[{"full_name":"Echard, Arnaud ","first_name":"Arnaud ","last_name":"Echard"}],"publisher":"Academic Press"},{"abstract":[{"lang":"eng","text":"Most kinesin motors move in only one direction along microtubules. Members of the kinesin-5 subfamily were initially described as unidirectional plus-end-directed motors and shown to produce piconewton forces. However, some fungal kinesin-5 motors are bidirectional. The force production of a bidirectional kinesin-5 has not yet been measured. Therefore, it remains unknown whether the mechanism of the unconventional minus-end-directed motility differs fundamentally from that of plus-end-directed stepping. Using force spectroscopy, we have measured here the forces that ensembles of purified budding yeast kinesin-5 Cin8 produce in microtubule gliding assays in both plus- and minus-end direction. Correlation analysis of pause forces demonstrated that individual Cin8 molecules produce additive forces in both directions of movement. In ensembles, Cin8 motors were able to produce single-motor forces up to a magnitude of ∼1.5 pN. Hence, these properties appear to be conserved within the kinesin-5 subfamily. Force production was largely independent of the directionality of movement, indicating similarities between the motility mechanisms for both directions. These results provide constraints for the development of models for the bidirectional motility mechanism of fission yeast kinesin-5 and provide insight into the function of this mitotic motor."}],"day":"07","doi":"10.1016/j.bpj.2017.09.006","year":"2017","citation":{"mla":"Fallesen, Todd, et al. “Ensembles of Bidirectional Kinesin Cin8 Produce Additive Forces in Both Directions of Movement.” <i>Biophysical Journal</i>, vol. 113, no. 9, Biophysical Society, 2017, pp. 2055–67, doi:<a href=\"https://doi.org/10.1016/j.bpj.2017.09.006\">10.1016/j.bpj.2017.09.006</a>.","short":"T. Fallesen, J. Roostalu, C.F. Düllberg, G. Pruessner, T. Surrey, Biophysical Journal 113 (2017) 2055–2067.","ista":"Fallesen T, Roostalu J, Düllberg CF, Pruessner G, Surrey T. 2017. Ensembles of bidirectional kinesin Cin8 produce additive forces in both directions of movement. Biophysical Journal. 113(9), 2055–2067.","ama":"Fallesen T, Roostalu J, Düllberg CF, Pruessner G, Surrey T. Ensembles of bidirectional kinesin Cin8 produce additive forces in both directions of movement. <i>Biophysical Journal</i>. 2017;113(9):2055-2067. doi:<a href=\"https://doi.org/10.1016/j.bpj.2017.09.006\">10.1016/j.bpj.2017.09.006</a>","apa":"Fallesen, T., Roostalu, J., Düllberg, C. F., Pruessner, G., &#38; Surrey, T. (2017). Ensembles of bidirectional kinesin Cin8 produce additive forces in both directions of movement. <i>Biophysical Journal</i>. Biophysical Society. <a href=\"https://doi.org/10.1016/j.bpj.2017.09.006\">https://doi.org/10.1016/j.bpj.2017.09.006</a>","chicago":"Fallesen, Todd, Johanna Roostalu, Christian F Düllberg, Gunnar Pruessner, and Thomas Surrey. “Ensembles of Bidirectional Kinesin Cin8 Produce Additive Forces in Both Directions of Movement.” <i>Biophysical Journal</i>. Biophysical Society, 2017. <a href=\"https://doi.org/10.1016/j.bpj.2017.09.006\">https://doi.org/10.1016/j.bpj.2017.09.006</a>.","ieee":"T. Fallesen, J. Roostalu, C. F. Düllberg, G. Pruessner, and T. Surrey, “Ensembles of bidirectional kinesin Cin8 produce additive forces in both directions of movement,” <i>Biophysical Journal</i>, vol. 113, no. 9. Biophysical Society, pp. 2055–2067, 2017."},"date_updated":"2021-01-12T07:59:28Z","ddc":["570"],"volume":113,"acknowledgement":"The plasmid for full-length kinesin-1 was a gift from G. Holzwarth and J. Macosko with permission from J. Howard. We thank I. Lueke and N. I. Cade for technical assistance. G.P. thanks the Francis Crick Institute, and in particular the Surrey and Salbreux groups, for their hospitality during his sabbatical stay, as well as Imperial College London for making it possible. This work was supported by the Francis Crick Institute, which receives its core funding from Cancer Research UK (FC001163), the United Kingdom Medical Research Council (FC001163), and the Wellcome Trust (FC001163), and by Imperial College London. J.R. was also supported by a Sir Henry Wellcome Postdoctoral Fellowship (100145/Z/12/Z) and T.S. by the European Research Council (Advanced Grant, project 323042). ","intvolume":"       113","pubrep_id":"965","title":"Ensembles of bidirectional kinesin Cin8 produce additive forces in both directions of movement","article_processing_charge":"No","department":[{"_id":"MaLo"}],"date_created":"2018-12-11T11:46:33Z","publication_status":"published","issue":"9","author":[{"last_name":"Fallesen","first_name":"Todd","full_name":"Fallesen, Todd"},{"full_name":"Roostalu, Johanna","first_name":"Johanna","last_name":"Roostalu"},{"full_name":"Düllberg, Christian F","orcid":"0000-0001-6335-9748","last_name":"Düllberg","first_name":"Christian F","id":"459064DC-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Pruessner","first_name":"Gunnar","full_name":"Pruessner, Gunnar"},{"full_name":"Surrey, Thomas","first_name":"Thomas","last_name":"Surrey"}],"_id":"453","article_type":"original","publisher":"Biophysical Society","file_date_updated":"2020-07-14T12:46:31Z","quality_controlled":"1","page":"2055 - 2067","oa":1,"publist_id":"7369","type":"journal_article","date_published":"2017-11-07T00:00:00Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","file":[{"date_updated":"2020-07-14T12:46:31Z","content_type":"application/pdf","file_name":"IST-2018-965-v1+1_2017_Duellberg_Ensembles_of.pdf","date_created":"2018-12-12T10:14:03Z","checksum":"99a2474088e20ac74b1882c4fbbb45b1","file_size":977192,"file_id":"5052","creator":"system","access_level":"open_access","relation":"main_file"}],"month":"11","oa_version":"Published Version","has_accepted_license":"1","publication":"Biophysical Journal","language":[{"iso":"eng"}]},{"language":[{"iso":"eng"}],"publication":"Building a Cell from its Components Parts","month":"04","oa_version":"Submitted Version","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","main_file_link":[{"open_access":"1","url":"http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4578691/"}],"type":"book_chapter","date_published":"2015-04-08T00:00:00Z","oa":1,"publist_id":"5627","quality_controlled":"1","page":"223 - 241","publisher":"Academic Press","author":[{"full_name":"Nguyen, Phuong","last_name":"Nguyen","first_name":"Phuong"},{"first_name":"Christine","last_name":"Field","full_name":"Field, Christine"},{"last_name":"Groen","first_name":"Aaron","full_name":"Groen, Aaron"},{"first_name":"Timothy","last_name":"Mitchison","full_name":"Mitchison, Timothy"},{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","last_name":"Loose","first_name":"Martin","full_name":"Loose, Martin","orcid":"0000-0001-7309-9724"}],"scopus_import":1,"pmid":1,"_id":"1544","intvolume":"       128","title":"Using supported bilayers to study the spatiotemporal organization of membrane-bound proteins","date_created":"2018-12-11T11:52:38Z","department":[{"_id":"MaLo"}],"publication_status":"published","volume":128,"external_id":{"pmid":["25997350"]},"citation":{"ista":"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, 223–241.","mla":"Nguyen, Phuong, et al. “Using Supported Bilayers to Study the Spatiotemporal Organization of Membrane-Bound Proteins.” <i>Building a Cell from Its Components Parts</i>, vol. 128, Academic Press, 2015, pp. 223–41, doi:<a href=\"https://doi.org/10.1016/bs.mcb.2015.01.007\">10.1016/bs.mcb.2015.01.007</a>.","short":"P. Nguyen, C. Field, A. Groen, T. Mitchison, M. Loose, in:, Building a Cell from Its Components Parts, Academic Press, 2015, pp. 223–241.","chicago":"Nguyen, Phuong, Christine Field, Aaron Groen, Timothy Mitchison, and Martin Loose. “Using Supported Bilayers to Study the Spatiotemporal Organization of Membrane-Bound Proteins.” In <i>Building a Cell from Its Components Parts</i>, 128:223–41. Academic Press, 2015. <a href=\"https://doi.org/10.1016/bs.mcb.2015.01.007\">https://doi.org/10.1016/bs.mcb.2015.01.007</a>.","ieee":"P. Nguyen, C. Field, A. Groen, T. Mitchison, and M. Loose, “Using supported bilayers to study the spatiotemporal organization of membrane-bound proteins,” in <i>Building a Cell from its Components Parts</i>, vol. 128, Academic Press, 2015, pp. 223–241.","apa":"Nguyen, P., Field, C., Groen, A., Mitchison, T., &#38; Loose, M. (2015). Using supported bilayers to study the spatiotemporal organization of membrane-bound proteins. In <i>Building a Cell from its Components Parts</i> (Vol. 128, pp. 223–241). Academic Press. <a href=\"https://doi.org/10.1016/bs.mcb.2015.01.007\">https://doi.org/10.1016/bs.mcb.2015.01.007</a>","ama":"Nguyen P, Field C, Groen A, Mitchison T, Loose M. Using supported bilayers to study the spatiotemporal organization of membrane-bound proteins. In: <i>Building a Cell from Its Components Parts</i>. Vol 128. Academic Press; 2015:223-241. doi:<a href=\"https://doi.org/10.1016/bs.mcb.2015.01.007\">10.1016/bs.mcb.2015.01.007</a>"},"year":"2015","date_updated":"2021-01-12T06:51:30Z","abstract":[{"lang":"eng","text":"Cell division in prokaryotes and eukaryotes is commonly initiated by the well-controlled binding of proteins to the cytoplasmic side of the cell membrane. However, a precise characterization of the spatiotemporal dynamics of membrane-bound proteins is often difficult to achieve in vivo. Here, we present protocols for the use of supported lipid bilayers to rebuild the cytokinetic machineries of cells with greatly different dimensions: the bacterium Escherichia coli and eggs of the vertebrate Xenopus laevis. Combined with total internal reflection fluorescence microscopy, these experimental setups allow for precise quantitative analyses of membrane-bound proteins. The protocols described to obtain glass-supported membranes from bacterial and vertebrate lipids can be used as starting points for other reconstitution experiments. We believe that similar biochemical assays will be instrumental to study the biochemistry and biophysics underlying a variety of complex cellular tasks, such as signaling, vesicle trafficking, and cell motility."}],"day":"08","doi":"10.1016/bs.mcb.2015.01.007"}]