[{"oa":1,"title":"Blood cell-vessel wall interactions probed by reflection interference contrast microscopy","date_updated":"2026-06-18T19:16:05Z","scopus_import":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","main_file_link":[{"open_access":"1","url":"https://hal.archives-ouvertes.fr/hal-02368135/file/110760V.pdf"}],"_id":"7010","volume":11076,"publication":"Advances in Microscopic Imaging II","citation":{"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.","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>.","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.","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>.","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>","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>"},"external_id":{"isi":["000535353000023"]},"article_number":"110760V","date_created":"2019-11-12T15:10:18Z","quality_controlled":"1","language":[{"iso":"eng"}],"doi":"10.1117/12.2527058","ddc":["570"],"isi":1,"intvolume":"     11076","publication_identifier":{"issn":["1605-7422"],"isbn":["9781510628458"]},"oa_version":"Published Version","day":"22","fulldoi":"https://doi.org/10.1117/12.2527058","author":[{"full_name":"Davies, Heather S.","last_name":"Davies","first_name":"Heather S."},{"last_name":"Baranova","full_name":"Baranova, Natalia S.","id":"38661662-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-3086-9124","first_name":"Natalia S."},{"first_name":"Nouha","last_name":"El Amri","full_name":"El Amri, Nouha"},{"full_name":"Coche-Guérente, Liliane","last_name":"Coche-Guérente","first_name":"Liliane"},{"full_name":"Verdier, Claude","last_name":"Verdier","first_name":"Claude"},{"first_name":"Lionel","full_name":"Bureau, Lionel","last_name":"Bureau"},{"first_name":"Ralf P.","last_name":"Richter","full_name":"Richter, Ralf P."},{"first_name":"Delphine","last_name":"Débarre","full_name":"Débarre, Delphine"}],"department":[{"_id":"MaLo"}],"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."}],"conference":{"name":"European Conferences on Biomedical Optics","end_date":"2019-06-27","start_date":"2019-06-26","location":"Munich, Germany"},"publisher":"SPIE","year":"2019","article_processing_charge":"No","month":"07","type":"conference","publication_status":"published","status":"public","date_published":"2019-07-22T00:00:00Z"},{"intvolume":"        10","isi":1,"ddc":["570"],"doi":"10.1038/s41467-019-13702-4","language":[{"iso":"eng"}],"quality_controlled":"1","date_created":"2019-12-20T12:22:57Z","article_number":"5744","external_id":{"isi":["000503009300001"]},"citation":{"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.","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).","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>.","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>.","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>","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>"},"file":[{"checksum":"a1b44b427ba341383197790d0e8789fa","creator":"dernst","access_level":"open_access","date_created":"2019-12-23T07:34:56Z","content_type":"application/pdf","relation":"main_file","file_name":"2019_NatureComm_Caldas.pdf","file_size":8488733,"file_id":"7208","date_updated":"2020-07-14T12:47:53Z"}],"publication":"Nature Communications","volume":10,"_id":"7197","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","scopus_import":"1","acknowledged_ssus":[{"_id":"LifeSc"},{"_id":"Bio"}],"date_updated":"2026-04-08T07:26:30Z","oa":1,"title":"Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA","license":"https://creativecommons.org/licenses/by/4.0/","date_published":"2019-12-17T00:00:00Z","status":"public","publication_status":"published","type":"journal_article","file_date_updated":"2020-07-14T12:47:53Z","month":"12","year":"2019","article_processing_charge":"No","publisher":"Springer Nature","project":[{"_id":"2595697A-B435-11E9-9278-68D0E5697425","call_identifier":"H2020","name":"Self-Organization of the Bacterial Cell","grant_number":"679239"},{"name":"Reconstitution of Bacterial Cell Division Using Purified Components","_id":"260D98C8-B435-11E9-9278-68D0E5697425"}],"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"}],"related_material":{"record":[{"id":"8358","relation":"dissertation_contains","status":"public"}]},"author":[{"last_name":"Dos Santos Caldas","full_name":"Dos Santos Caldas, Paulo R","first_name":"Paulo R","orcid":"0000-0001-6730-4461","id":"38FCDB4C-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Maria D","id":"319AA9CE-F248-11E8-B48F-1D18A9856A87","last_name":"Lopez Pelegrin","full_name":"Lopez Pelegrin, Maria D"},{"last_name":"Pearce","full_name":"Pearce, Daniel J. G.","first_name":"Daniel J. G."},{"last_name":"Budanur","full_name":"Budanur, Nazmi B","orcid":"0000-0003-0423-5010","first_name":"Nazmi B","id":"3EA1010E-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Jan","last_name":"Brugués","full_name":"Brugués, Jan"},{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-7309-9724","first_name":"Martin","full_name":"Loose, Martin","last_name":"Loose"}],"department":[{"_id":"MaLo"},{"_id":"BjHo"}],"article_type":"original","corr_author":"1","fulldoi":"https://doi.org/10.1038/s41467-019-13702-4","ec_funded":1,"has_accepted_license":"1","day":"17","oa_version":"Published Version","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png"},"publication_identifier":{"issn":["2041-1723"]}},{"publication_status":"published","date_published":"2018-06-01T00:00:00Z","status":"public","type":"journal_article","month":"06","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"}],"publisher":"Elsevier","year":"2018","article_processing_charge":"No","article_type":"original","author":[{"last_name":"Richter","full_name":"Richter, Ralf","first_name":"Ralf"},{"full_name":"Baranova, Natalia","last_name":"Baranova","id":"38661662-F248-11E8-B48F-1D18A9856A87","first_name":"Natalia","orcid":"0000-0002-3086-9124"},{"full_name":"Day, Anthony","last_name":"Day","first_name":"Anthony"},{"full_name":"Kwok, Jessica","last_name":"Kwok","first_name":"Jessica"}],"department":[{"_id":"MaLo"}],"fulldoi":"https://doi.org/10.1016/j.sbi.2017.12.002","day":"01","publist_id":"7259","oa_version":"Submitted Version","isi":1,"intvolume":"        50","language":[{"iso":"eng"}],"doi":"10.1016/j.sbi.2017.12.002","date_created":"2018-12-11T11:47:09Z","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","quality_controlled":"1","external_id":{"isi":["000443661300011"]},"publication":"Current Opinion in Structural Biology","citation":{"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.","short":"R. Richter, N.S. Baranova, A. Day, J. Kwok, Current Opinion in Structural Biology 50 (2018) 65–74.","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.","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>.","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>.","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>"},"_id":"555","volume":50,"page":"65 - 74","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","main_file_link":[{"url":"http://eprints.whiterose.ac.uk/125524/","open_access":"1"}],"title":"Glycosaminoglycans in extracellular matrix organisation: Are concepts from soft matter physics key to understanding the formation of perineuronal nets?","oa":1,"date_updated":"2023-09-11T14:07:03Z","scopus_import":"1"},{"project":[{"grant_number":"ALTF 2015-1163","name":"Synthesis of bacterial cell wall","_id":"2596EAB6-B435-11E9-9278-68D0E5697425"},{"grant_number":"291734","_id":"25681D80-B435-11E9-9278-68D0E5697425","name":"International IST Postdoc Fellowship Programme","call_identifier":"FP7"}],"abstract":[{"lang":"eng","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."}],"year":"2017","article_processing_charge":"No","publisher":"Academic Press","month":"12","type":"book_chapter","publication_status":"published","status":"public","date_published":"2017-12-01T00:00:00Z","publication_identifier":{"issn":["0091-679X"]},"oa_version":"None","day":"01","publist_id":"6134","ec_funded":1,"fulldoi":"https://doi.org/10.1016/bs.mcb.2016.03.036","alternative_title":["Methods in Cell Biology"],"department":[{"_id":"MaLo"}],"author":[{"orcid":"0000-0002-3086-9124","first_name":"Natalia","id":"38661662-F248-11E8-B48F-1D18A9856A87","last_name":"Baranova","full_name":"Baranova, Natalia"},{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","first_name":"Martin","orcid":"0000-0001-7309-9724","last_name":"Loose","full_name":"Loose, Martin"}],"external_id":{"isi":["000403542900022"]},"date_created":"2018-12-11T11:50:45Z","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).","quality_controlled":"1","editor":[{"last_name":"Echard","full_name":"Echard, Arnaud ","first_name":"Arnaud "}],"language":[{"iso":"eng"}],"doi":"10.1016/bs.mcb.2016.03.036","intvolume":"       137","isi":1,"title":"Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA copolymers","acknowledged_ssus":[{"_id":"Bio"}],"scopus_import":"1","date_updated":"2025-07-10T11:50:24Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"1213","volume":137,"page":"355 - 370","publication":"Cytokinesis","citation":{"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>","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>","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>.","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.","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."}},{"has_accepted_license":"1","day":"07","publist_id":"7369","publication_identifier":{"eissn":["1542-0086"],"issn":["0006-3495"]},"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png"},"oa_version":"Published Version","article_type":"original","author":[{"last_name":"Fallesen","full_name":"Fallesen, Todd","first_name":"Todd"},{"full_name":"Roostalu, Johanna","last_name":"Roostalu","first_name":"Johanna"},{"last_name":"Düllberg","full_name":"Düllberg, Christian F","orcid":"0000-0001-6335-9748","first_name":"Christian F","id":"459064DC-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Pruessner, Gunnar","last_name":"Pruessner","first_name":"Gunnar"},{"full_name":"Surrey, Thomas","last_name":"Surrey","first_name":"Thomas"}],"department":[{"_id":"MaLo"}],"OA_place":"publisher","fulldoi":"https://doi.org/10.1016/j.bpj.2017.09.006","month":"11","abstract":[{"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.","lang":"eng"}],"year":"2017","article_processing_charge":"No","publisher":"Biophysical Society","publication_status":"published","pubrep_id":"965","date_published":"2017-11-07T00:00:00Z","status":"public","file_date_updated":"2020-07-14T12:46:31Z","type":"journal_article","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Ensembles of bidirectional kinesin Cin8 produce additive forces in both directions of movement","oa":1,"OA_type":"hybrid","scopus_import":"1","date_updated":"2025-08-05T14:08:52Z","publication":"Biophysical Journal","file":[{"date_updated":"2020-07-14T12:46:31Z","file_size":977192,"file_id":"5052","content_type":"application/pdf","file_name":"IST-2018-965-v1+1_2017_Duellberg_Ensembles_of.pdf","relation":"main_file","date_created":"2018-12-12T10:14:03Z","access_level":"open_access","creator":"system","checksum":"99a2474088e20ac74b1882c4fbbb45b1"}],"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>.","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.","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.","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>","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>","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>."},"_id":"453","volume":113,"page":"2055 - 2067","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). ","date_created":"2018-12-11T11:46:33Z","quality_controlled":"1","pmid":1,"external_id":{"pmid":["29117528"]},"issue":"9","ddc":["570"],"intvolume":"       113","language":[{"iso":"eng"}],"doi":"10.1016/j.bpj.2017.09.006"},{"publication_identifier":{"eisbn":["978-3-319-53047-5"]},"oa_version":"None","day":"13","publist_id":"7165","fulldoi":"https://doi.org/10.1007/978-3-319-53047-5_15","corr_author":"1","department":[{"_id":"MaLo"}],"author":[{"first_name":"Martin","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin","last_name":"Loose"},{"first_name":"Katja","last_name":"Zieske","full_name":"Zieske, Katja"},{"last_name":"Schwille","full_name":"Schwille, Petra","first_name":"Petra"}],"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"}],"publisher":"Springer","year":"2017","month":"05","type":"book_chapter","publication_status":"published","status":"public","date_published":"2017-05-13T00:00:00Z","title":"Reconstitution of protein dynamics involved in bacterial cell division","date_updated":"2024-10-09T20:58:00Z","scopus_import":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"629","volume":84,"page":"419 - 444","publication":"Prokaryotic Cytoskeletons","series_title":"Sub-Cellular Biochemistry","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.","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.","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>.","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"]},"pmid":1,"date_created":"2018-12-11T11:47:35Z","quality_controlled":"1","language":[{"iso":"eng"}],"doi":"10.1007/978-3-319-53047-5_15","intvolume":"        84"},{"day":"28","publist_id":"7073","publication_identifier":{"issn":["0027-8424"]},"oa_version":"Submitted Version","author":[{"last_name":"Rickman","full_name":"Rickman, Jamie","first_name":"Jamie"},{"last_name":"Düllberg","full_name":"Düllberg, Christian F","orcid":"0000-0001-6335-9748","first_name":"Christian F","id":"459064DC-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Nicholas","full_name":"Cade, Nicholas","last_name":"Cade"},{"first_name":"Lewis","full_name":"Griffin, Lewis","last_name":"Griffin"},{"full_name":"Surrey, Thomas","last_name":"Surrey","first_name":"Thomas"}],"department":[{"_id":"MaLo"}],"fulldoi":"https://doi.org/10.1073/pnas.1620274114","month":"03","abstract":[{"lang":"eng","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."}],"year":"2017","article_processing_charge":"No","publisher":"National Academy of Sciences","publication_status":"published","date_published":"2017-03-28T00:00:00Z","status":"public","type":"journal_article","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","main_file_link":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5380103/","open_access":"1"}],"oa":1,"title":"Steady state EB cap size fluctuations are determined by stochastic microtubule growth and maturation","scopus_import":"1","date_updated":"2025-09-11T07:08:20Z","publication":"PNAS","citation":{"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>","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>.","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>","short":"J. Rickman, C.F. Düllberg, N. Cade, L. Griffin, T. Surrey, PNAS 114 (2017) 3427–3432.","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.","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.","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>."},"volume":114,"_id":"660","page":"3427 - 3432","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.).","date_created":"2018-12-11T11:47:46Z","quality_controlled":"1","pmid":1,"external_id":{"isi":["000397607300065"],"pmid":["28280102"]},"issue":"13","intvolume":"       114","isi":1,"language":[{"iso":"eng"}],"doi":"10.1073/pnas.1620274114"},{"article_processing_charge":"No","year":"2017","publisher":"Elsevier","abstract":[{"lang":"eng","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."}],"month":"01","type":"journal_article","file_date_updated":"2020-07-14T12:47:56Z","status":"public","date_published":"2017-01-01T00:00:00Z","publication_status":"published","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","short":"CC BY-NC-ND (4.0)"},"oa_version":"Published Version","publication_identifier":{"issn":["1525-0016"]},"day":"01","has_accepted_license":"1","fulldoi":"https://doi.org/10.1016/j.ymthe.2016.10.005","department":[{"_id":"MaLo"}],"author":[{"last_name":"Smole","full_name":"Smole, Anže","first_name":"Anže"},{"first_name":"Duško","last_name":"Lainšček","full_name":"Lainšček, Duško"},{"last_name":"Bezeljak","full_name":"Bezeljak, Urban","id":"2A58201A-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-1365-5631","first_name":"Urban"},{"first_name":"Simon","last_name":"Horvat","full_name":"Horvat, Simon"},{"last_name":"Jerala","full_name":"Jerala, Roman","first_name":"Roman"}],"article_type":"original","issue":"1","pmid":1,"external_id":{"pmid":["28129106"],"isi":["000391901600013"]},"quality_controlled":"1","date_created":"2020-01-25T15:55:39Z","doi":"10.1016/j.ymthe.2016.10.005","language":[{"iso":"eng"}],"intvolume":"        25","isi":1,"ddc":["570"],"date_updated":"2025-09-18T10:41:35Z","oa":1,"title":"A synthetic mammalian therapeutic gene circuit for sensing and suppressing inflammation","license":"https://creativecommons.org/licenses/by-nc-nd/4.0/","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","page":"102-119","_id":"7360","volume":25,"file":[{"date_created":"2020-03-03T10:55:13Z","access_level":"open_access","file_id":"7561","file_size":3404806,"relation":"main_file","content_type":"application/pdf","file_name":"2017_MolecularTherapy_Smole.pdf","date_updated":"2020-07-14T12:47:56Z","checksum":"ea8b1b28606dd1edab7379ba4fa3641f","creator":"dernst"}],"citation":{"short":"A. Smole, D. Lainšček, U. Bezeljak, S. Horvat, R. Jerala, Molecular Therapy 25 (2017) 102–119.","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.","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>.","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.","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>","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>.","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>"},"publication":"Molecular Therapy"},{"publisher":"Frontiers Research Foundation","article_processing_charge":"Yes","year":"2017","abstract":[{"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.","lang":"eng"}],"project":[{"_id":"25D61E48-B435-11E9-9278-68D0E5697425","name":"Molecular Mechanisms of Cerebral Cortex Development","call_identifier":"FP7","grant_number":"618444"},{"grant_number":"RGP0053/2014","_id":"25D7962E-B435-11E9-9278-68D0E5697425","name":"Quantitative Structure-Function Analysis of Cerebral Cortex Assembly at Clonal Level"},{"grant_number":"291734","call_identifier":"FP7","name":"International IST Postdoc Fellowship Programme","_id":"25681D80-B435-11E9-9278-68D0E5697425"},{"call_identifier":"FWF","name":"The biochemical basis of PAR polarization","_id":"25985A36-B435-11E9-9278-68D0E5697425","grant_number":"T00817-B21"}],"month":"06","type":"journal_article","file_date_updated":"2020-07-14T12:48:16Z","date_published":"2017-06-28T00:00:00Z","status":"public","pubrep_id":"830","publication_status":"published","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png"},"oa_version":"Published Version","publication_identifier":{"issn":["1662-5102"]},"publist_id":"6445","day":"28","has_accepted_license":"1","fulldoi":"https://doi.org/10.3389/fncel.2017.00176","ec_funded":1,"author":[{"full_name":"Hansen, Andi H","last_name":"Hansen","id":"38853E16-F248-11E8-B48F-1D18A9856A87","first_name":"Andi H"},{"last_name":"Düllberg","full_name":"Düllberg, Christian F","id":"459064DC-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-6335-9748","first_name":"Christian F"},{"full_name":"Mieck, Christine","last_name":"Mieck","id":"34CAE85C-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-1919-7416","first_name":"Christine"},{"orcid":"0000-0001-7309-9724","first_name":"Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","last_name":"Loose","full_name":"Loose, Martin"},{"id":"37B36620-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-2279-1061","first_name":"Simon","full_name":"Hippenmeyer, Simon","last_name":"Hippenmeyer"}],"department":[{"_id":"SiHi"},{"_id":"MaLo"}],"related_material":{"record":[{"status":"public","id":"9962","relation":"dissertation_contains"}]},"article_number":"176","external_id":{"isi":["000404486700001"]},"quality_controlled":"1","date_created":"2018-12-11T11:49:25Z","doi":"10.3389/fncel.2017.00176","language":[{"iso":"eng"}],"isi":1,"intvolume":"        11","ddc":["570"],"date_updated":"2026-10-15T22:31:02Z","scopus_import":"1","title":"Cell polarity in cerebral cortex development - cellular architecture shaped by biochemical networks","oa":1,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","_id":"960","volume":11,"citation":{"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>.","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.","short":"A.H. Hansen, C.F. Düllberg, C. Mieck, M. Loose, S. Hippenmeyer, Frontiers in Cellular Neuroscience 11 (2017).","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>","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>."},"file":[{"creator":"system","checksum":"dc1f5a475b918d09a0f9f587400b1626","date_updated":"2020-07-14T12:48:16Z","file_size":2153858,"file_id":"4764","file_name":"IST-2017-830-v1+1_2017_Hansen_CellPolarity.pdf","relation":"main_file","content_type":"application/pdf","date_created":"2018-12-12T10:09:40Z","access_level":"open_access"}],"publication":"Frontiers in Cellular Neuroscience"},{"author":[{"first_name":"Phuong","last_name":"Nguyen","full_name":"Nguyen, Phuong"},{"last_name":"Field","full_name":"Field, Christine","first_name":"Christine"},{"full_name":"Groen, Aaron","last_name":"Groen","first_name":"Aaron"},{"last_name":"Mitchison","full_name":"Mitchison, Timothy","first_name":"Timothy"},{"full_name":"Loose, Martin","last_name":"Loose","id":"462D4284-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-7309-9724","first_name":"Martin"}],"department":[{"_id":"MaLo"}],"fulldoi":"https://doi.org/10.1016/bs.mcb.2015.01.007","corr_author":"1","publist_id":"5627","day":"08","oa_version":"Submitted Version","status":"public","date_published":"2015-04-08T00:00:00Z","publication_status":"published","type":"book_chapter","month":"04","publisher":"Academic Press","year":"2015","article_processing_charge":"No","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."}],"citation":{"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>","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>.","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>.","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.","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.","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."},"publication":"Building a Cell from its Components Parts","page":"223 - 241","_id":"1544","volume":128,"main_file_link":[{"url":"http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4578691/","open_access":"1"}],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","date_updated":"2025-09-29T11:03:06Z","scopus_import":"1","oa":1,"title":"Using supported bilayers to study the spatiotemporal organization of membrane-bound proteins","isi":1,"intvolume":"       128","doi":"10.1016/bs.mcb.2015.01.007","language":[{"iso":"eng"}],"quality_controlled":"1","date_created":"2018-12-11T11:52:38Z","external_id":{"isi":["000370490800013"],"pmid":["25997350"]},"pmid":1}]