[{"language":[{"iso":"eng"}],"date_published":"2013-10-08T00:00:00Z","doi":"10.1039/c3sm51096d","article_type":"original","quality_controlled":"1","publication":"Soft Matter","citation":{"ieee":"S. S. Schoenholz, C. P. Goodrich, O. Kogan, A. J. Liu, and S. R. Nagel, “Stability of jammed packings II: The transverse length scale,” Soft Matter, vol. 9, no. 46. Royal Society of Chemistry, 2013.","apa":"Schoenholz, S. S., Goodrich, C. P., Kogan, O., Liu, A. J., & Nagel, S. R. (2013). Stability of jammed packings II: The transverse length scale. Soft Matter. Royal Society of Chemistry. https://doi.org/10.1039/c3sm51096d","ista":"Schoenholz SS, Goodrich CP, Kogan O, Liu AJ, Nagel SR. 2013. Stability of jammed packings II: The transverse length scale. Soft Matter. 9(46), 11000.","ama":"Schoenholz SS, Goodrich CP, Kogan O, Liu AJ, Nagel SR. Stability of jammed packings II: The transverse length scale. Soft Matter. 2013;9(46). doi:10.1039/c3sm51096d","chicago":"Schoenholz, Samuel S., Carl Peter Goodrich, Oleg Kogan, Andrea J. Liu, and Sidney R. Nagel. “Stability of Jammed Packings II: The Transverse Length Scale.” Soft Matter. Royal Society of Chemistry, 2013. https://doi.org/10.1039/c3sm51096d.","short":"S.S. Schoenholz, C.P. Goodrich, O. Kogan, A.J. Liu, S.R. Nagel, Soft Matter 9 (2013).","mla":"Schoenholz, Samuel S., et al. “Stability of Jammed Packings II: The Transverse Length Scale.” Soft Matter, vol. 9, no. 46, 11000, Royal Society of Chemistry, 2013, doi:10.1039/c3sm51096d."},"day":"08","month":"10","publication_identifier":{"issn":["1744-683X","1744-6848"]},"article_processing_charge":"No","date_updated":"2021-01-12T08:15:27Z","date_created":"2020-04-30T11:43:58Z","volume":9,"oa_version":"None","author":[{"last_name":"Schoenholz","first_name":"Samuel S.","full_name":"Schoenholz, Samuel S."},{"full_name":"Goodrich, Carl Peter","first_name":"Carl Peter","last_name":"Goodrich","id":"EB352CD2-F68A-11E9-89C5-A432E6697425","orcid":"0000-0002-1307-5074"},{"full_name":"Kogan, Oleg","last_name":"Kogan","first_name":"Oleg"},{"first_name":"Andrea J.","last_name":"Liu","full_name":"Liu, Andrea J."},{"full_name":"Nagel, Sidney R.","first_name":"Sidney R.","last_name":"Nagel"}],"publication_status":"published","title":"Stability of jammed packings II: The transverse length scale","status":"public","publisher":"Royal Society of Chemistry","intvolume":" 9","_id":"7775","year":"2013","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","abstract":[{"lang":"eng","text":"As a function of packing fraction at zero temperature and applied stress, an amorphous packing of spheres exhibits a jamming transition where the system is sensitive to boundary conditions even in the thermodynamic limit. Upon further compression, the system should become insensitive to boundary conditions provided it is sufficiently large. Here we explore the linear response to a large class of boundary perturbations in 2 and 3 dimensions. We consider each finite packing with periodic-boundary conditions as the basis of an infinite square or cubic lattice and study properties of vibrational modes at arbitrary wave vector. We find that the stability of such modes can be understood in terms of a competition between plane waves and the anomalous vibrational modes associated with the jamming transition; infinitesimal boundary perturbations become irrelevant for systems that are larger than a length scale that characterizes the transverse excitations. This previously identified length diverges at the jamming transition."}],"issue":"46","article_number":"11000","type":"journal_article"},{"month":"10","day":"08","article_processing_charge":"No","publication_identifier":{"issn":["1744-683X","1744-6848"]},"doi":"10.1039/c3sm51095f","date_published":"2013-10-08T00:00:00Z","language":[{"iso":"eng"}],"publication":"Soft Matter","citation":{"chicago":"Goodrich, Carl Peter, Wouter G. Ellenbroek, and Andrea J. Liu. “Stability of Jammed Packings I: The Rigidity Length Scale.” Soft Matter. Royal Society of Chemistry, 2013. https://doi.org/10.1039/c3sm51095f.","mla":"Goodrich, Carl Peter, et al. “Stability of Jammed Packings I: The Rigidity Length Scale.” Soft Matter, vol. 9, no. 46, 10993, Royal Society of Chemistry, 2013, doi:10.1039/c3sm51095f.","short":"C.P. Goodrich, W.G. Ellenbroek, A.J. Liu, Soft Matter 9 (2013).","ista":"Goodrich CP, Ellenbroek WG, Liu AJ. 2013. Stability of jammed packings I: The rigidity length scale. Soft Matter. 9(46), 10993.","ieee":"C. P. Goodrich, W. G. Ellenbroek, and A. J. Liu, “Stability of jammed packings I: The rigidity length scale,” Soft Matter, vol. 9, no. 46. Royal Society of Chemistry, 2013.","apa":"Goodrich, C. P., Ellenbroek, W. G., & Liu, A. J. (2013). Stability of jammed packings I: The rigidity length scale. Soft Matter. Royal Society of Chemistry. https://doi.org/10.1039/c3sm51095f","ama":"Goodrich CP, Ellenbroek WG, Liu AJ. Stability of jammed packings I: The rigidity length scale. Soft Matter. 2013;9(46). doi:10.1039/c3sm51095f"},"article_type":"original","quality_controlled":"1","abstract":[{"text":"In 2005, Wyart et al. [Europhys. Lett., 2005, 72, 486] showed that the low frequency vibrational properties of jammed amorphous sphere packings can be understood in terms of a length scale, called l*, that diverges as the system becomes marginally unstable. Despite the tremendous success of this theory, it has been difficult to connect the counting argument that defines l* to other length scales that diverge near the jamming transition. We present an alternate derivation of l* based on the onset of rigidity. This phenomenological approach reveals the physical mechanism underlying the length scale and is relevant to a range of systems for which the original argument breaks down. It also allows us to present the first direct numerical measurement of l*.","lang":"eng"}],"issue":"46","extern":"1","article_number":"10993","type":"journal_article","author":[{"full_name":"Goodrich, Carl Peter","id":"EB352CD2-F68A-11E9-89C5-A432E6697425","orcid":"0000-0002-1307-5074","first_name":"Carl Peter","last_name":"Goodrich"},{"last_name":"Ellenbroek","first_name":"Wouter G.","full_name":"Ellenbroek, Wouter G."},{"full_name":"Liu, Andrea J.","last_name":"Liu","first_name":"Andrea J."}],"date_updated":"2021-01-12T08:15:27Z","date_created":"2020-04-30T11:43:42Z","oa_version":"None","volume":9,"_id":"7774","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2013","publication_status":"published","title":"Stability of jammed packings I: The rigidity length scale","status":"public","publisher":"Royal Society of Chemistry","intvolume":" 9"},{"article_number":"119","file_date_updated":"2020-07-16T11:23:40Z","extern":"1","year":"2013","pmid":1,"publication_status":"published","publisher":"Frontiers Media","author":[{"first_name":"Tim P","last_name":"Vogels","id":"CB6FF8D2-008F-11EA-8E08-2637E6697425","orcid":"0000-0003-3295-6181","full_name":"Vogels, Tim P"},{"first_name":"R. C.","last_name":"Froemke","full_name":"Froemke, R. C."},{"full_name":"Doyon, N.","last_name":"Doyon","first_name":"N."},{"last_name":"Gilson","first_name":"M.","full_name":"Gilson, M."},{"first_name":"J. S.","last_name":"Haas","full_name":"Haas, J. S."},{"full_name":"Liu, R.","last_name":"Liu","first_name":"R."},{"full_name":"Maffei, A.","first_name":"A.","last_name":"Maffei"},{"first_name":"P.","last_name":"Miller","full_name":"Miller, P."},{"full_name":"Wierenga, C. J.","first_name":"C. J.","last_name":"Wierenga"},{"full_name":"Woodin, M. A.","last_name":"Woodin","first_name":"M. A."},{"full_name":"Zenke, F.","last_name":"Zenke","first_name":"F."},{"full_name":"Sprekeler, H.","last_name":"Sprekeler","first_name":"H."}],"date_created":"2020-06-25T13:23:50Z","date_updated":"2021-01-12T08:16:38Z","volume":7,"month":"07","publication_identifier":{"eissn":["1662-5110"]},"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/3.0/legalcode","name":"Creative Commons Attribution 3.0 Unported (CC BY 3.0)","short":"CC BY (3.0)","image":"/images/cc_by.png"},"external_id":{"pmid":["23882186"]},"oa":1,"quality_controlled":"1","doi":"10.3389/fncir.2013.00119","language":[{"iso":"eng"}],"type":"journal_article","abstract":[{"text":"While the plasticity of excitatory synaptic connections in the brain has been widely studied, the plasticity of inhibitory connections is much less understood. Here, we present recent experimental and theoretical findings concerning the rules of spike timing-dependent inhibitory plasticity and their putative network function. This is a summary of a workshop at the COSYNE conference 2012.","lang":"eng"}],"_id":"8030","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Inhibitory synaptic plasticity: Spike timing-dependence and putative network function","ddc":["570"],"status":"public","intvolume":" 7","file":[{"creator":"cziletti","content_type":"application/pdf","file_size":1530469,"file_name":"2013_FrontNeurCirc_Vogels.pdf","access_level":"open_access","date_updated":"2020-07-16T11:23:40Z","date_created":"2020-07-16T11:23:40Z","success":1,"checksum":"9c321cb12977d84048712eefa7f0c497","file_id":"8123","relation":"main_file"}],"oa_version":"Published Version","day":"18","article_processing_charge":"No","has_accepted_license":"1","publication":"Frontiers in Neural Circuits","citation":{"chicago":"Vogels, Tim P, R. C. Froemke, N. Doyon, M. Gilson, J. S. Haas, R. Liu, A. Maffei, et al. “Inhibitory Synaptic Plasticity: Spike Timing-Dependence and Putative Network Function.” Frontiers in Neural Circuits. Frontiers Media, 2013. https://doi.org/10.3389/fncir.2013.00119.","short":"T.P. Vogels, R.C. Froemke, N. Doyon, M. Gilson, J.S. Haas, R. Liu, A. Maffei, P. Miller, C.J. Wierenga, M.A. Woodin, F. Zenke, H. Sprekeler, Frontiers in Neural Circuits 7 (2013).","mla":"Vogels, Tim P., et al. “Inhibitory Synaptic Plasticity: Spike Timing-Dependence and Putative Network Function.” Frontiers in Neural Circuits, vol. 7, 119, Frontiers Media, 2013, doi:10.3389/fncir.2013.00119.","apa":"Vogels, T. P., Froemke, R. C., Doyon, N., Gilson, M., Haas, J. S., Liu, R., … Sprekeler, H. (2013). Inhibitory synaptic plasticity: Spike timing-dependence and putative network function. Frontiers in Neural Circuits. Frontiers Media. https://doi.org/10.3389/fncir.2013.00119","ieee":"T. P. Vogels et al., “Inhibitory synaptic plasticity: Spike timing-dependence and putative network function,” Frontiers in Neural Circuits, vol. 7. Frontiers Media, 2013.","ista":"Vogels TP, Froemke RC, Doyon N, Gilson M, Haas JS, Liu R, Maffei A, Miller P, Wierenga CJ, Woodin MA, Zenke F, Sprekeler H. 2013. Inhibitory synaptic plasticity: Spike timing-dependence and putative network function. Frontiers in Neural Circuits. 7, 119.","ama":"Vogels TP, Froemke RC, Doyon N, et al. Inhibitory synaptic plasticity: Spike timing-dependence and putative network function. Frontiers in Neural Circuits. 2013;7. doi:10.3389/fncir.2013.00119"},"article_type":"original","date_published":"2013-07-18T00:00:00Z"},{"date_published":"2013-01-01T00:00:00Z","doi":"10.1242/jcs.118232","page":"4572 - 4588","quality_controlled":0,"citation":{"chicago":"Steffen, Anika, Markus Ladwein, Georgi A Dimchev, Anke Hein, Lisa Schwenkmezger, Stefan Arens, Kathrin Ladwein, et al. “Rac Function Is Crucial for Cell Migration but Is Not Required for Spreading and Focal Adhesion Formation.” Journal of Cell Science. Company of Biologists, 2013. https://doi.org/10.1242/jcs.118232.","short":"A. Steffen, M. Ladwein, G.A. Dimchev, A. Hein, L. Schwenkmezger, S. Arens, K. Ladwein, J. Holleboom, F.K. Schur, J. Small, J. Schwarz, R. Gerhard, J. Faix, T. Stradal, C. Brakebusch, K. Rottner, Journal of Cell Science 126 (2013) 4572–4588.","mla":"Steffen, Anika, et al. “Rac Function Is Crucial for Cell Migration but Is Not Required for Spreading and Focal Adhesion Formation.” Journal of Cell Science, vol. 126, no. 20, Company of Biologists, 2013, pp. 4572–88, doi:10.1242/jcs.118232.","apa":"Steffen, A., Ladwein, M., Dimchev, G. A., Hein, A., Schwenkmezger, L., Arens, S., … Rottner, K. (2013). Rac function is crucial for cell migration but is not required for spreading and focal adhesion formation. Journal of Cell Science. Company of Biologists. https://doi.org/10.1242/jcs.118232","ieee":"A. Steffen et al., “Rac function is crucial for cell migration but is not required for spreading and focal adhesion formation,” Journal of Cell Science, vol. 126, no. 20. Company of Biologists, pp. 4572–4588, 2013.","ista":"Steffen A, Ladwein M, Dimchev GA, Hein A, Schwenkmezger L, Arens S, Ladwein K, Holleboom J, Schur FK, Small J, Schwarz J, Gerhard R, Faix J, Stradal T, Brakebusch C, Rottner K. 2013. Rac function is crucial for cell migration but is not required for spreading and focal adhesion formation. Journal of Cell Science. 126(20), 4572–4588.","ama":"Steffen A, Ladwein M, Dimchev GA, et al. Rac function is crucial for cell migration but is not required for spreading and focal adhesion formation. Journal of Cell Science. 2013;126(20):4572-4588. doi:10.1242/jcs.118232"},"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png"},"publication":"Journal of Cell Science","month":"01","day":"01","volume":126,"date_created":"2018-12-11T11:48:38Z","date_updated":"2021-01-12T08:16:57Z","author":[{"first_name":"Anika","last_name":"Steffen","full_name":"Steffen, Anika"},{"full_name":"Ladwein, Markus","last_name":"Ladwein","first_name":"Markus"},{"full_name":"Georgi Dimchev","id":"38C393BE-F248-11E8-B48F-1D18A9856A87","last_name":"Dimchev","first_name":"Georgi A"},{"first_name":"Anke","last_name":"Hein","full_name":"Hein, Anke"},{"full_name":"Schwenkmezger, Lisa","first_name":"Lisa","last_name":"Schwenkmezger"},{"last_name":"Arens","first_name":"Stefan","full_name":"Arens, Stefan"},{"first_name":"Kathrin","last_name":"Ladwein","full_name":"Ladwein, Kathrin I"},{"last_name":"Holleboom","first_name":"J.","full_name":"Holleboom, J. Margit"},{"first_name":"Florian","last_name":"Schur","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-4790-8078","full_name":"Florian Schur"},{"last_name":"Small","first_name":"John","full_name":"Small, John V"},{"full_name":"Schwarz, Janett","last_name":"Schwarz","first_name":"Janett"},{"full_name":"Gerhard, Ralf","last_name":"Gerhard","first_name":"Ralf"},{"full_name":"Faix, Jan","first_name":"Jan","last_name":"Faix"},{"last_name":"Stradal","first_name":"Theresia","full_name":"Stradal, Theresia E"},{"last_name":"Brakebusch","first_name":"Cord","full_name":"Brakebusch, Cord H"},{"full_name":"Rottner, Klemens","first_name":"Klemens","last_name":"Rottner"}],"publisher":"Company of Biologists","intvolume":" 126","title":"Rac function is crucial for cell migration but is not required for spreading and focal adhesion formation","status":"public","publication_status":"published","acknowledgement":"This work was supported in part by the Deutsche Forschungsgemeinschaft [grants within programs SFB621 to K.R., and FOR629 and SFB629 to T.E.B.S.]. Deposited in PMC for immediate release.\nWe thank Brigitte Denker and Gerd Landsberg for excellent technical assistance. We are grateful to Robert Geffers (HZI Braunschweig, Germany) for microarray analyses and to Mirko Himmel (UKE Hamburg, Germany) for valuable advice on FRAP analysis.","_id":"811","year":"2013","extern":1,"issue":"20","publist_id":"6840","abstract":[{"lang":"eng","text":"Cell migration is commonly accompanied by protrusion of membrane ruffles and lamellipodia. In two-dimensional migration, protrusion of these thin sheets of cytoplasm is considered relevant to both exploration of new space and initiation of nascent adhesion to the substratum. Lamellipodium formation can be potently stimulated by Rho GTPases of the Rac subfamily, but alsoby RhoG or Cdc42. Here we describe viable fibroblast cell lines geneticallydeficient for Rac1 that lack detectable levels of Rac2 and Rac3. Rac-deficient cells were devoid of apparent lamellipodia, but these structures were restored by expression of either Rac subfamily member, but not by Cdc42 or RhoG. Cells deficient in Rac showed strong reduction in wound closure and random cell migration and a notable loss of sensitivity to a chemotactic gradient. Despite these defects, Rac-deficient cells were able to spread, formed filopodia and established focal adhesions. Spreading in these cells was achieved by the extension of filopodia followed by the advancement of cytoplasmic veils between them. The number and size of focal adhesions as well as their intensity were largely unaffected by genetic removal of Rac1. However, Rac deficiency increased the mobility of different components in focal adhesions, potentially explaining how Rac - although not essential - can contribute to focal adhesion assembly. Together, our data demonstrate that Rac signaling is essential for lamellipodium protrusion and for efficient cell migration, but not for spreading or filopodium formation. Our findings also suggest that Rac GTPases are crucial to the establishment or maintenance of polarity in chemotactic migration."}],"type":"journal_article"},{"month":"09","day":"15","page":"2861 - 2875","quality_controlled":0,"citation":{"ama":"Koestler S, Steffen A, Nemethova M, et al. Arp2/3 complex is essential for actin network treadmilling as well as for targeting of capping protein and cofilin. Molecular Biology of the Cell. 2013;24(18):2861-2875. doi:10.1091/mbc.E12-12-0857","ieee":"S. Koestler et al., “Arp2/3 complex is essential for actin network treadmilling as well as for targeting of capping protein and cofilin,” Molecular Biology of the Cell, vol. 24, no. 18. American Society for Biology, pp. 2861–2875, 2013.","apa":"Koestler, S., Steffen, A., Nemethova, M., Winterhoff, M., Luo, N., Holleboom, J., … Rottner, K. (2013). Arp2/3 complex is essential for actin network treadmilling as well as for targeting of capping protein and cofilin. Molecular Biology of the Cell. American Society for Biology. https://doi.org/10.1091/mbc.E12-12-0857","ista":"Koestler S, Steffen A, Nemethova M, Winterhoff M, Luo N, Holleboom J, Krupp J, Jacob S, Vinzenz M, Schur FK, Schlüter K, Gunning P, Winkler C, Schmeiser C, Faix J, Stradal T, Small J, Rottner K. 2013. Arp2/3 complex is essential for actin network treadmilling as well as for targeting of capping protein and cofilin. Molecular Biology of the Cell. 24(18), 2861–2875.","short":"S. Koestler, A. Steffen, M. Nemethova, M. Winterhoff, N. Luo, J. Holleboom, J. Krupp, S. Jacob, M. Vinzenz, F.K. Schur, K. Schlüter, P. Gunning, C. Winkler, C. Schmeiser, J. Faix, T. Stradal, J. Small, K. Rottner, Molecular Biology of the Cell 24 (2013) 2861–2875.","mla":"Koestler, Stefan, et al. “Arp2/3 Complex Is Essential for Actin Network Treadmilling as Well as for Targeting of Capping Protein and Cofilin.” Molecular Biology of the Cell, vol. 24, no. 18, American Society for Biology, 2013, pp. 2861–75, doi:10.1091/mbc.E12-12-0857.","chicago":"Koestler, Stefan, Anika Steffen, Maria Nemethova, Moritz Winterhoff, Ningning Luo, J. Holleboom, Jessica Krupp, et al. “Arp2/3 Complex Is Essential for Actin Network Treadmilling as Well as for Targeting of Capping Protein and Cofilin.” Molecular Biology of the Cell. American Society for Biology, 2013. https://doi.org/10.1091/mbc.E12-12-0857."},"publication":"Molecular Biology of the Cell","doi":"10.1091/mbc.E12-12-0857","date_published":"2013-09-15T00:00:00Z","type":"journal_article","extern":1,"issue":"18","publist_id":"6841","abstract":[{"lang":"eng","text":"Lamellipodia are sheet-like protrusions formed during migration or phagocytosis and comprise a network of actin filaments. Filament formation in this network is initiated by nucleation/branching through the actin-related protein 2/3 (Arp2/3) complex downstream of its activator, suppressor of cAMP receptor/WASP-family verprolin homologous (Scar/WAVE), but the relative relevance of Arp2/3-mediated branching versus actin filament elongation is unknown. Here we use instantaneous interference with Arp2/3 complex function in live fibroblasts with established lamellipodia. This allows direct examination of both the fate of elongating filaments upon instantaneous suppression of Arp2/3 complex activity and the consequences of this treatment on the dynamics of other lamellipodial regulators. We show that Arp2/3 complex is an essential organizer of treadmilling actin filament arrays but has little effect on the net rate of actin filament turnover at the cell periphery. In addition, Arp2/3 complex serves as key upstream factor for the recruitment of modulators of lamellipodia formation such as capping protein or cofilin. Arp2/3 complex is thus decisive for filament organization and geometry within the network not only by generating branches and novel filament ends, but also by directing capping or severing activities to the lamellipodium. Arp2/3 complex is also crucial to lamellipodia-based migration of keratocytes."}],"intvolume":" 24","publisher":"American Society for Biology","publication_status":"published","status":"public","title":"Arp2/3 complex is essential for actin network treadmilling as well as for targeting of capping protein and cofilin","_id":"812","year":"2013","acknowledgement":"This work was supported in part by Deutsche Forschungsgemeinschaft Grants RO2414/3-1 (to K.R.) and FA330/6-1 (to J.F.), Austrian \nScience Fund Projects FWF 1516-B09 and FWF P21292-B09 (to J.V.S.), the Vienna Science and Technology Fund (WWTF, to \nJ.V.S. and C.S.), and Australian National Health and Medical \nResearch Council Grant APP1004175 (to P.W.G.). We thank J. Adams, \nR. Chisholm, A. Hall, L. Machesky, H. G. Mannherz, D. Schafer, and \nR. Wedlich-Söldner for expression constructs and B. Denker, \nP. Hagendorff, and G. Landsberg for technical assistance.","volume":24,"date_created":"2018-12-11T11:48:38Z","date_updated":"2021-01-12T08:17:00Z","author":[{"full_name":"Koestler, Stefan A","last_name":"Koestler","first_name":"Stefan"},{"full_name":"Steffen, Anika","last_name":"Steffen","first_name":"Anika"},{"full_name":"Maria Nemethova","id":"34E27F1C-F248-11E8-B48F-1D18A9856A87","last_name":"Nemethova","first_name":"Maria"},{"last_name":"Winterhoff","first_name":"Moritz","full_name":"Winterhoff, Moritz"},{"full_name":"Luo, Ningning","first_name":"Ningning","last_name":"Luo"},{"last_name":"Holleboom","first_name":"J.","full_name":"Holleboom, J. Margit"},{"last_name":"Krupp","first_name":"Jessica","full_name":"Krupp, Jessica"},{"last_name":"Jacob","first_name":"Sonja","full_name":"Jacob, Sonja"},{"full_name":"Vinzenz, Marlene","first_name":"Marlene","last_name":"Vinzenz"},{"first_name":"Florian","last_name":"Schur","id":"48AD8942-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-4790-8078","full_name":"Florian Schur"},{"first_name":"Kai","last_name":"Schlüter","full_name":"Schlüter, Kai"},{"last_name":"Gunning","first_name":"Peter","full_name":"Gunning, Peter W"},{"last_name":"Winkler","first_name":"Christoph","full_name":"Winkler, Christoph"},{"last_name":"Schmeiser","first_name":"Christian","full_name":"Schmeiser, Christian"},{"full_name":"Faix, Jan","last_name":"Faix","first_name":"Jan"},{"last_name":"Stradal","first_name":"Theresia","full_name":"Stradal, Theresia E"},{"last_name":"Small","first_name":"John","full_name":"Small, John V"},{"full_name":"Rottner, Klemens","last_name":"Rottner","first_name":"Klemens"}]}]