[{"date_updated":"2025-07-10T11:50:24Z","article_processing_charge":"No","_id":"1213","language":[{"iso":"eng"}],"publist_id":"6134","external_id":{"isi":["000403542900022"]},"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>","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>.","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>","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.","short":"N.S. Baranova, M. Loose, in:, A. Echard (Ed.), Cytokinesis, 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>.","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."},"publication_identifier":{"issn":["0091-679X"]},"department":[{"_id":"MaLo"}],"ec_funded":1,"oa_version":"None","volume":137,"date_published":"2017-12-01T00:00:00Z","publication_status":"published","publisher":"Academic Press","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).","alternative_title":["Methods in Cell Biology"],"isi":1,"publication":"Cytokinesis","intvolume":"       137","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","month":"12","title":"Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA copolymers","project":[{"_id":"2596EAB6-B435-11E9-9278-68D0E5697425","grant_number":"ALTF 2015-1163","name":"Synthesis of bacterial cell wall"},{"name":"International IST Postdoc Fellowship Programme","_id":"25681D80-B435-11E9-9278-68D0E5697425","grant_number":"291734","call_identifier":"FP7"}],"author":[{"orcid":"0000-0002-3086-9124","last_name":"Baranova","first_name":"Natalia","full_name":"Baranova, Natalia","id":"38661662-F248-11E8-B48F-1D18A9856A87"},{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin","orcid":"0000-0001-7309-9724","first_name":"Martin","last_name":"Loose"}],"doi":"10.1016/bs.mcb.2016.03.036","year":"2017","day":"01","page":"355 - 370","scopus_import":"1","quality_controlled":"1","status":"public","acknowledged_ssus":[{"_id":"Bio"}],"type":"book_chapter","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."}],"editor":[{"last_name":"Echard","first_name":"Arnaud ","full_name":"Echard, Arnaud "}],"date_created":"2018-12-11T11:50:45Z"},{"pmid":1,"department":[{"_id":"MaLo"}],"citation":{"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.","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>.","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>","short":"M. Loose, K. Zieske, P. Schwille, in:, Prokaryotic Cytoskeletons, Springer, 2017, pp. 419–444.","ista":"Loose M, Zieske K, Schwille P. 2017.Reconstitution of protein dynamics involved in bacterial cell division. In: Prokaryotic Cytoskeletons. vol. 84, 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>","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>."},"publication_identifier":{"eisbn":["978-3-319-53047-5"]},"external_id":{"pmid":["28500535"]},"publist_id":"7165","language":[{"iso":"eng"}],"_id":"629","date_updated":"2024-10-09T20:58:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","intvolume":"        84","publication":"Prokaryotic Cytoskeletons","publisher":"Springer","publication_status":"published","volume":84,"date_published":"2017-05-13T00:00:00Z","oa_version":"None","page":"419 - 444","scopus_import":1,"day":"13","doi":"10.1007/978-3-319-53047-5_15","year":"2017","author":[{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin","first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724"},{"full_name":"Zieske, Katja","last_name":"Zieske","first_name":"Katja"},{"full_name":"Schwille, Petra","first_name":"Petra","last_name":"Schwille"}],"series_title":"Sub-Cellular Biochemistry","title":"Reconstitution of protein dynamics involved in bacterial cell division","month":"05","date_created":"2018-12-11T11:47:35Z","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"}],"type":"book_chapter","corr_author":"1","status":"public","quality_controlled":"1"},{"status":"public","quality_controlled":"1","date_created":"2018-12-11T11:47:46Z","main_file_link":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5380103/","open_access":"1"}],"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"}],"type":"journal_article","oa":1,"title":"Steady state EB cap size fluctuations are determined by stochastic microtubule growth and maturation","month":"03","page":"3427 - 3432","scopus_import":"1","day":"28","doi":"10.1073/pnas.1620274114","year":"2017","author":[{"full_name":"Rickman, Jamie","first_name":"Jamie","last_name":"Rickman"},{"full_name":"Düllberg, Christian F","id":"459064DC-F248-11E8-B48F-1D18A9856A87","first_name":"Christian F","last_name":"Düllberg","orcid":"0000-0001-6335-9748"},{"full_name":"Cade, Nicholas","first_name":"Nicholas","last_name":"Cade"},{"full_name":"Griffin, Lewis","last_name":"Griffin","first_name":"Lewis"},{"full_name":"Surrey, Thomas","last_name":"Surrey","first_name":"Thomas"}],"publisher":"National Academy of Sciences","publication_status":"published","date_published":"2017-03-28T00:00:00Z","volume":114,"oa_version":"Submitted Version","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","intvolume":"       114","publication":"PNAS","isi":1,"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.).","issue":"13","_id":"660","article_processing_charge":"No","date_updated":"2025-09-11T07:08:20Z","department":[{"_id":"MaLo"}],"pmid":1,"publication_identifier":{"issn":["0027-8424"]},"citation":{"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>","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>.","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>","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.","short":"J. Rickman, C.F. Düllberg, N. Cade, L. Griffin, T. Surrey, PNAS 114 (2017) 3427–3432.","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."},"external_id":{"pmid":["28280102"],"isi":["000397607300065"]},"publist_id":"7073","language":[{"iso":"eng"}]},{"status":"public","quality_controlled":"1","type":"journal_article","file":[{"file_id":"7561","file_size":3404806,"checksum":"ea8b1b28606dd1edab7379ba4fa3641f","date_updated":"2020-07-14T12:47:56Z","creator":"dernst","access_level":"open_access","relation":"main_file","date_created":"2020-03-03T10:55:13Z","content_type":"application/pdf","file_name":"2017_MolecularTherapy_Smole.pdf"}],"oa":1,"date_created":"2020-01-25T15:55:39Z","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"}],"title":"A synthetic mammalian therapeutic gene circuit for sensing and suppressing inflammation","month":"01","ddc":["570"],"article_type":"original","day":"01","page":"102-119","author":[{"first_name":"Anže","last_name":"Smole","full_name":"Smole, Anže"},{"last_name":"Lainšček","first_name":"Duško","full_name":"Lainšček, Duško"},{"orcid":"0000-0003-1365-5631","last_name":"Bezeljak","first_name":"Urban","id":"2A58201A-F248-11E8-B48F-1D18A9856A87","full_name":"Bezeljak, Urban"},{"full_name":"Horvat, Simon","first_name":"Simon","last_name":"Horvat"},{"full_name":"Jerala, Roman","last_name":"Jerala","first_name":"Roman"}],"doi":"10.1016/j.ymthe.2016.10.005","year":"2017","date_published":"2017-01-01T00:00:00Z","volume":25,"oa_version":"Published Version","publication_status":"published","publisher":"Elsevier","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"},"isi":1,"intvolume":"        25","file_date_updated":"2020-07-14T12:47:56Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","publication":"Molecular Therapy","_id":"7360","date_updated":"2025-09-18T10:41:35Z","article_processing_charge":"No","issue":"1","language":[{"iso":"eng"}],"has_accepted_license":"1","citation":{"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>","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>.","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>","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.","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>.","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."},"publication_identifier":{"issn":["1525-0016"]},"department":[{"_id":"MaLo"}],"pmid":1,"external_id":{"isi":["000391901600013"],"pmid":["28129106"]}},{"date_published":"2017-11-07T00:00:00Z","volume":113,"oa_version":"Published Version","publication_status":"published","publisher":"Biophysical Society","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"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","file_date_updated":"2020-07-14T12:46:31Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Biophysical Journal","_id":"453","date_updated":"2025-08-05T14:08:52Z","article_processing_charge":"No","issue":"9","publist_id":"7369","OA_type":"hybrid","OA_place":"publisher","language":[{"iso":"eng"}],"has_accepted_license":"1","citation":{"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>","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>.","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.","short":"T. Fallesen, J. Roostalu, C.F. Düllberg, G. Pruessner, T. Surrey, Biophysical Journal 113 (2017) 2055–2067.","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."},"publication_identifier":{"eissn":["1542-0086"],"issn":["0006-3495"]},"pmid":1,"department":[{"_id":"MaLo"}],"external_id":{"pmid":["29117528"]},"status":"public","quality_controlled":"1","type":"journal_article","file":[{"file_id":"5052","checksum":"99a2474088e20ac74b1882c4fbbb45b1","file_size":977192,"access_level":"open_access","creator":"system","date_updated":"2020-07-14T12:46:31Z","relation":"main_file","file_name":"IST-2018-965-v1+1_2017_Duellberg_Ensembles_of.pdf","content_type":"application/pdf","date_created":"2018-12-12T10:14:03Z"}],"oa":1,"date_created":"2018-12-11T11:46:33Z","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"}],"title":"Ensembles of bidirectional kinesin Cin8 produce additive forces in both directions of movement","month":"11","pubrep_id":"965","ddc":["570"],"article_type":"original","day":"07","scopus_import":"1","page":"2055 - 2067","author":[{"full_name":"Fallesen, Todd","first_name":"Todd","last_name":"Fallesen"},{"first_name":"Johanna","last_name":"Roostalu","full_name":"Roostalu, Johanna"},{"full_name":"Düllberg, Christian F","id":"459064DC-F248-11E8-B48F-1D18A9856A87","last_name":"Düllberg","first_name":"Christian F","orcid":"0000-0001-6335-9748"},{"first_name":"Gunnar","last_name":"Pruessner","full_name":"Pruessner, Gunnar"},{"full_name":"Surrey, Thomas","last_name":"Surrey","first_name":"Thomas"}],"doi":"10.1016/j.bpj.2017.09.006","year":"2017"},{"status":"public","quality_controlled":"1","date_created":"2018-12-11T11:49:25Z","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"}],"type":"journal_article","file":[{"file_name":"IST-2017-830-v1+1_2017_Hansen_CellPolarity.pdf","content_type":"application/pdf","date_created":"2018-12-12T10:09:40Z","checksum":"dc1f5a475b918d09a0f9f587400b1626","file_size":2153858,"file_id":"4764","relation":"main_file","access_level":"open_access","creator":"system","date_updated":"2020-07-14T12:48:16Z"}],"oa":1,"pubrep_id":"830","related_material":{"record":[{"id":"9962","status":"public","relation":"dissertation_contains"}]},"ddc":["570"],"title":"Cell polarity in cerebral cortex development - cellular architecture shaped by biochemical networks","month":"06","day":"28","scopus_import":"1","author":[{"full_name":"Hansen, Andi H","id":"38853E16-F248-11E8-B48F-1D18A9856A87","first_name":"Andi H","last_name":"Hansen"},{"full_name":"Düllberg, Christian F","id":"459064DC-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-6335-9748","last_name":"Düllberg","first_name":"Christian F"},{"full_name":"Mieck, Christine","id":"34CAE85C-F248-11E8-B48F-1D18A9856A87","first_name":"Christine","last_name":"Mieck","orcid":"0000-0003-1919-7416"},{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin","last_name":"Loose","first_name":"Martin","orcid":"0000-0001-7309-9724"},{"orcid":"0000-0003-2279-1061","last_name":"Hippenmeyer","first_name":"Simon","full_name":"Hippenmeyer, Simon","id":"37B36620-F248-11E8-B48F-1D18A9856A87"}],"project":[{"call_identifier":"FP7","grant_number":"618444","_id":"25D61E48-B435-11E9-9278-68D0E5697425","name":"Molecular Mechanisms of Cerebral Cortex Development"},{"name":"Quantitative Structure-Function Analysis of Cerebral Cortex Assembly at Clonal Level","grant_number":"RGP0053/2014","_id":"25D7962E-B435-11E9-9278-68D0E5697425"},{"name":"International IST Postdoc Fellowship Programme","_id":"25681D80-B435-11E9-9278-68D0E5697425","grant_number":"291734","call_identifier":"FP7"},{"call_identifier":"FWF","grant_number":"T00817-B21","_id":"25985A36-B435-11E9-9278-68D0E5697425","name":"The biochemical basis of PAR polarization"}],"doi":"10.3389/fncel.2017.00176","year":"2017","article_number":"176","publication_status":"published","publisher":"Frontiers Research Foundation","volume":11,"date_published":"2017-06-28T00:00:00Z","ec_funded":1,"oa_version":"Published Version","file_date_updated":"2020-07-14T12:48:16Z","intvolume":"        11","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Frontiers in Cellular Neuroscience","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png"},"isi":1,"_id":"960","date_updated":"2026-04-29T22:30:43Z","article_processing_charge":"Yes","citation":{"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>","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.","short":"A.H. Hansen, C.F. Düllberg, C. Mieck, M. Loose, S. Hippenmeyer, Frontiers in Cellular Neuroscience 11 (2017).","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>","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>.","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."},"publication_identifier":{"issn":["1662-5102"]},"department":[{"_id":"SiHi"},{"_id":"MaLo"}],"external_id":{"isi":["000404486700001"]},"publist_id":"6445","language":[{"iso":"eng"}],"has_accepted_license":"1"},{"corr_author":"1","quality_controlled":"1","status":"public","main_file_link":[{"url":"http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4578691/","open_access":"1"}],"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."}],"date_created":"2018-12-11T11:52:38Z","oa":1,"type":"book_chapter","month":"04","title":"Using supported bilayers to study the spatiotemporal organization of membrane-bound proteins","doi":"10.1016/bs.mcb.2015.01.007","year":"2015","author":[{"full_name":"Nguyen, Phuong","first_name":"Phuong","last_name":"Nguyen"},{"full_name":"Field, Christine","last_name":"Field","first_name":"Christine"},{"full_name":"Groen, Aaron","last_name":"Groen","first_name":"Aaron"},{"full_name":"Mitchison, Timothy","last_name":"Mitchison","first_name":"Timothy"},{"last_name":"Loose","first_name":"Martin","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin"}],"page":"223 - 241","scopus_import":"1","day":"08","publisher":"Academic Press","publication_status":"published","oa_version":"Submitted Version","volume":128,"date_published":"2015-04-08T00:00:00Z","publication":"Building a Cell from its Components Parts","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","intvolume":"       128","isi":1,"article_processing_charge":"No","date_updated":"2025-09-29T11:03:06Z","_id":"1544","external_id":{"isi":["000370490800013"],"pmid":["25997350"]},"pmid":1,"department":[{"_id":"MaLo"}],"citation":{"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>","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.","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."},"language":[{"iso":"eng"}],"publist_id":"5627"}]