[{"has_accepted_license":"1","publication_status":"published","acknowledged_ssus":[{"_id":"EM-Fac"},{"_id":"Bio"},{"_id":"LifeSc"}],"ddc":["570"],"date_published":"2023-11-10T00:00:00Z","supervisor":[{"full_name":"Friml, Jiří","id":"4159519E-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-8302-7596","last_name":"Friml","first_name":"Jiří"},{"first_name":"Martin","last_name":"Loose","full_name":"Loose, Martin","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87"}],"status":"public","alternative_title":["ISTA Thesis"],"citation":{"ama":"Gnyliukh N. Mechanism of clathrin-coated vesicle  formation during endocytosis in plants. 2023. doi:<a href=\"https://doi.org/10.15479/at:ista:14510\">10.15479/at:ista:14510</a>","ista":"Gnyliukh N. 2023. Mechanism of clathrin-coated vesicle  formation during endocytosis in plants. Institute of Science and Technology Austria.","mla":"Gnyliukh, Nataliia. <i>Mechanism of Clathrin-Coated Vesicle  Formation during Endocytosis in Plants</i>. Institute of Science and Technology Austria, 2023, doi:<a href=\"https://doi.org/10.15479/at:ista:14510\">10.15479/at:ista:14510</a>.","apa":"Gnyliukh, N. (2023). <i>Mechanism of clathrin-coated vesicle  formation during endocytosis in plants</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/at:ista:14510\">https://doi.org/10.15479/at:ista:14510</a>","ieee":"N. Gnyliukh, “Mechanism of clathrin-coated vesicle  formation during endocytosis in plants,” Institute of Science and Technology Austria, 2023.","chicago":"Gnyliukh, Nataliia. “Mechanism of Clathrin-Coated Vesicle  Formation during Endocytosis in Plants.” Institute of Science and Technology Austria, 2023. <a href=\"https://doi.org/10.15479/at:ista:14510\">https://doi.org/10.15479/at:ista:14510</a>.","short":"N. Gnyliukh, Mechanism of Clathrin-Coated Vesicle  Formation during Endocytosis in Plants, Institute of Science and Technology Austria, 2023."},"related_material":{"record":[{"relation":"part_of_dissertation","status":"public","id":"14591"},{"status":"public","id":"9887","relation":"part_of_dissertation"},{"status":"public","id":"8139","relation":"part_of_dissertation"}]},"oa_version":"Published Version","type":"dissertation","month":"11","date_updated":"2024-03-25T23:30:25Z","page":"180","file_date_updated":"2023-11-23T13:10:55Z","date_created":"2023-11-10T09:10:06Z","year":"2023","_id":"14510","publication_identifier":{"isbn":["978-3-99078-037-4"],"issn":["2663-337X"]},"doi":"10.15479/at:ista:14510","project":[{"grant_number":"665385","name":"International IST Doctoral Program","_id":"2564DBCA-B435-11E9-9278-68D0E5697425","call_identifier":"H2020"}],"language":[{"iso":"eng"}],"keyword":["Clathrin-Mediated Endocytosis","vesicle scission","Dynamin-Related Protein 2","SH3P2","TPLATE complex","Total internal reflection fluorescence microscopy","Arabidopsis thaliana"],"day":"10","file":[{"file_id":"14567","date_updated":"2023-11-20T09:18:51Z","checksum":"3d5e680bfc61f98e308c434f45cc9bd6","date_created":"2023-11-20T09:18:51Z","access_level":"closed","file_name":"Thesis_Gnyliukh_final_08_11_23.docx","file_size":20824903,"content_type":"application/vnd.openxmlformats-officedocument.wordprocessingml.document","relation":"source_file","creator":"ngnyliuk"},{"file_size":24871844,"content_type":"application/pdf","embargo":"2024-11-23","relation":"main_file","embargo_to":"open_access","creator":"ngnyliuk","file_name":"Thesis_Gnyliukh_final_20_11_23.pdf","date_created":"2023-11-20T09:23:11Z","access_level":"closed","file_id":"14568","date_updated":"2023-11-23T13:10:55Z","checksum":"bfc96d47fc4e7e857dd71656097214a4"}],"author":[{"orcid":"0000-0002-2198-0509","id":"390C1120-F248-11E8-B48F-1D18A9856A87","full_name":"Gnyliukh, Nataliia","first_name":"Nataliia","last_name":"Gnyliukh"}],"degree_awarded":"PhD","title":"Mechanism of clathrin-coated vesicle  formation during endocytosis in plants","department":[{"_id":"GradSch"},{"_id":"JiFr"},{"_id":"MaLo"}],"user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","publisher":"Institute of Science and Technology Austria","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"ec_funded":1,"article_processing_charge":"No"},{"department":[{"_id":"GradSch"},{"_id":"MaLo"}],"publisher":"Institute of Science and Technology Austria","user_id":"8b945eb4-e2f2-11eb-945a-df72226e66a9","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"article_processing_charge":"No","ec_funded":1,"file":[{"file_id":"14390","date_updated":"2023-10-04T10:28:35Z","checksum":"87eef11fbc5c7df0826f12a3a629b444","date_created":"2023-10-04T10:11:53Z","access_level":"closed","file_name":"PhD Thesis_Philipp Radler_20231004.docx","file_size":114932847,"content_type":"application/vnd.openxmlformats-officedocument.wordprocessingml.document","relation":"source_file","creator":"pradler"},{"checksum":"3253e099b7126469d941fd9419d68b4f","date_updated":"2023-10-04T10:28:35Z","file_id":"14391","access_level":"closed","date_created":"2023-10-04T10:11:21Z","file_name":"PhD Thesis_Philipp Radler_20231004.pdf","embargo_to":"open_access","creator":"pradler","relation":"main_file","content_type":"application/pdf","embargo":"2024-10-04","file_size":37838778}],"day":"25","author":[{"full_name":"Radler, Philipp","orcid":"0000-0001-9198-2182 ","id":"40136C2A-F248-11E8-B48F-1D18A9856A87","first_name":"Philipp","last_name":"Radler"}],"degree_awarded":"PhD","title":"Spatiotemporal signaling during assembly of the bacterial divisome","project":[{"grant_number":"679239","name":"Self-Organization of the Bacterial Cell","_id":"2595697A-B435-11E9-9278-68D0E5697425","call_identifier":"H2020"},{"name":"Understanding bacterial cell division by in vitro\r\nreconstitution","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d","grant_number":"P34607"},{"grant_number":"ALTF 2015-1163","name":"Synthesis of bacterial cell wall","_id":"2596EAB6-B435-11E9-9278-68D0E5697425"},{"grant_number":"LT000824/2016","_id":"259B655A-B435-11E9-9278-68D0E5697425","name":"Reconstitution of bacterial cell wall sythesis"}],"language":[{"iso":"eng"}],"keyword":["Cell Division","Reconstitution","FtsZ","FtsA","Divisome","E.coli"],"publication_identifier":{"issn":["2663-337X"],"isbn":["978-3-99078-033-6"]},"doi":"10.15479/at:ista:14280","year":"2023","_id":"14280","type":"dissertation","oa_version":"Published Version","month":"09","date_updated":"2024-02-21T12:35:18Z","abstract":[{"lang":"eng","text":"Cell division in Escherichia coli is performed by the divisome, a multi-protein complex composed of more than 30 proteins. The divisome spans from the cytoplasm through the inner membrane to the cell wall and the outer membrane. Divisome assembly is initiated by a cytoskeletal structure, the so-called Z-ring, which localizes at the center of the E. coli cell and determines the position of the future cell septum. The Z-ring is composed of the highly conserved bacterial tubulin homologue FtsZ, which forms treadmilling filaments. These filaments are recruited to the inner membrane by FtsA, a highly conserved bacterial actin homologue. FtsA interacts with other proteins in the periplasm and thus connects the cytoplasmic and periplasmic components of the divisome. \r\nA previous model postulated that FtsA regulates maturation of the divisome by switching from an oligomeric, inactive state to a monomeric and active state. This model was based mostly on in vivo studies, as a biochemical characterization of FtsA has been hampered by difficulties in purifying the protein. Here, we studied FtsA using an in vitro reconstitution approach and aimed to answer two questions: (i) How are dynamics from cytoplasmic, treadmilling FtsZ filaments coupled to proteins acting in the periplasmic space and (ii) How does FtsA regulate the maturation of the divisome?\r\nWe found that the cytoplasmic peptides of the transmembrane proteins FtsN and FtsQ interact directly with FtsA and can follow the spatiotemporal signal of FtsA/Z filaments. When we investigated the underlying mechanism by imaging single molecules of FtsNcyto, we found the peptide to interact transiently with FtsA. An in depth analysis of the single molecule trajectories helped to postulate a model where PG synthases follow the dynamics of FtsZ by a diffusion and capture mechanism. \r\nFollowing up on these findings we were interested in how the self-interaction of FtsA changes when it encounters FtsNcyto and if we can confirm the proposed oligomer-monomer switch. For this, we compared the behavior of the previously identified, hyperactive mutant FtsA R286W with wildtype FtsA. The mutant outperforms WT in mirroring and transmitting the spatiotemporal signal of treadmilling FtsZ filaments. Surprisingly however, we found that this was not due to a difference in the self-interaction strength of the two variants, but a difference in their membrane residence time. Furthermore, in contrast to our expectations, upon binding of FtsNcyto the measured self-interaction of FtsA actually increased. \r\nWe propose that FtsNcyto induces a rearrangement of the oligomeric architecture of FtsA. In further consequence this change leads to more persistent FtsZ filaments which results in a defined signalling zone, allowing formation of the mature divisome. The observed difference between FtsA WT and R286W is due to the vastly different membrane turnover of the proteins. R286W cycles 5-10x faster compared to WT which allows to sample FtsZ filaments at faster frequencies. These findings can explain the observed differences in toxicity for overexpression of FtsA WT and R286W and help to understand how FtsA regulates divisome maturation."}],"page":"156","date_created":"2023-09-06T10:58:25Z","file_date_updated":"2023-10-04T10:28:35Z","status":"public","alternative_title":["ISTA Thesis"],"citation":{"ama":"Radler P. Spatiotemporal signaling during assembly of the bacterial divisome. 2023. doi:<a href=\"https://doi.org/10.15479/at:ista:14280\">10.15479/at:ista:14280</a>","apa":"Radler, P. (2023). <i>Spatiotemporal signaling during assembly of the bacterial divisome</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/at:ista:14280\">https://doi.org/10.15479/at:ista:14280</a>","ista":"Radler P. 2023. Spatiotemporal signaling during assembly of the bacterial divisome. Institute of Science and Technology Austria.","mla":"Radler, Philipp. <i>Spatiotemporal Signaling during Assembly of the Bacterial Divisome</i>. Institute of Science and Technology Austria, 2023, doi:<a href=\"https://doi.org/10.15479/at:ista:14280\">10.15479/at:ista:14280</a>.","chicago":"Radler, Philipp. “Spatiotemporal Signaling during Assembly of the Bacterial Divisome.” Institute of Science and Technology Austria, 2023. <a href=\"https://doi.org/10.15479/at:ista:14280\">https://doi.org/10.15479/at:ista:14280</a>.","ieee":"P. Radler, “Spatiotemporal signaling during assembly of the bacterial divisome,” Institute of Science and Technology Austria, 2023.","short":"P. Radler, Spatiotemporal Signaling during Assembly of the Bacterial Divisome, Institute of Science and Technology Austria, 2023."},"related_material":{"record":[{"relation":"part_of_dissertation","id":"11373","status":"public"},{"id":"7387","status":"public","relation":"part_of_dissertation"},{"status":"public","id":"10934","relation":"research_data"}]},"has_accepted_license":"1","publication_status":"published","acknowledged_ssus":[{"_id":"Bio"},{"_id":"LifeSc"}],"date_published":"2023-09-25T00:00:00Z","ddc":["572"],"supervisor":[{"first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin"}]},{"acknowledgement":"My thanks goes to the Loose lab members, BioImaging, Life Science and Nanofabrication Facilities and the wonderful international community at IST for sharing this experience with me.","year":"2020","_id":"8341","page":"215","oa_version":"Published Version","type":"dissertation","month":"09","abstract":[{"lang":"eng","text":"One of the most striking hallmarks of the eukaryotic cell is the presence of intracellular vesicles and organelles. Each of these membrane-enclosed compartments has a distinct composition of lipids and proteins, which is essential for accurate membrane traffic and homeostasis. Interestingly, their biochemical identities are achieved with the help\r\nof small GTPases of the Rab family, which cycle between GDP- and GTP-bound forms on the selected membrane surface. While this activity switch is well understood for an individual protein, how Rab GTPases collectively transition between states to generate decisive signal propagation in space and time is unclear. In my PhD thesis, I present\r\nin vitro reconstitution experiments with theoretical modeling to systematically study a minimal Rab5 activation network from bottom-up. We find that positive feedback based on known molecular interactions gives rise to bistable GTPase activity switching on system’s scale. Furthermore, we determine that collective transition near the critical\r\npoint is intrinsically stochastic and provide evidence that the inactive Rab5 abundance on the membrane can shape the network response. Finally, we demonstrate that collective switching can spread on the lipid bilayer as a traveling activation wave, representing a possible emergent activity pattern in endosomal maturation. Together, our\r\nfindings reveal new insights into the self-organization properties of signaling networks away from chemical equilibrium. Our work highlights the importance of systematic characterization of biochemical systems in well-defined physiological conditions. This way, we were able to answer long-standing open questions in the field and close the gap between regulatory processes on a molecular scale and emergent responses on system’s level."}],"date_updated":"2023-09-07T13:17:06Z","file_date_updated":"2021-09-16T12:49:12Z","date_created":"2020-09-08T08:53:53Z","alternative_title":["ISTA Thesis"],"status":"public","related_material":{"record":[{"relation":"part_of_dissertation","id":"7580","status":"public"}]},"citation":{"short":"U. Bezeljak, In Vitro Reconstitution of a Rab Activation Switch, Institute of Science and Technology Austria, 2020.","chicago":"Bezeljak, Urban. “In Vitro Reconstitution of a Rab Activation Switch.” Institute of Science and Technology Austria, 2020. <a href=\"https://doi.org/10.15479/AT:ISTA:8341\">https://doi.org/10.15479/AT:ISTA:8341</a>.","ieee":"U. Bezeljak, “In vitro reconstitution of a Rab activation switch,” Institute of Science and Technology Austria, 2020.","apa":"Bezeljak, U. (2020). <i>In vitro reconstitution of a Rab activation switch</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT:ISTA:8341\">https://doi.org/10.15479/AT:ISTA:8341</a>","ista":"Bezeljak U. 2020. In vitro reconstitution of a Rab activation switch. Institute of Science and Technology Austria.","mla":"Bezeljak, Urban. <i>In Vitro Reconstitution of a Rab Activation Switch</i>. Institute of Science and Technology Austria, 2020, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:8341\">10.15479/AT:ISTA:8341</a>.","ama":"Bezeljak U. In vitro reconstitution of a Rab activation switch. 2020. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:8341\">10.15479/AT:ISTA:8341</a>"},"publication_status":"published","oa":1,"has_accepted_license":"1","ddc":["570"],"date_published":"2020-09-08T00:00:00Z","supervisor":[{"first_name":"Martin","last_name":"Loose","orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin"}],"acknowledged_ssus":[{"_id":"Bio"},{"_id":"LifeSc"},{"_id":"NanoFab"}],"publisher":"Institute of Science and Technology Austria","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","department":[{"_id":"MaLo"}],"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode","image":"/images/cc_by_nc_sa.png","name":"Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)","short":"CC BY-NC-SA (4.0)"},"article_processing_charge":"No","author":[{"id":"2A58201A-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0003-1365-5631","full_name":"Bezeljak, Urban","last_name":"Bezeljak","first_name":"Urban"}],"license":"https://creativecommons.org/licenses/by-nc-sa/4.0/","day":"08","file":[{"checksum":"70871b335a595252a66c6bbf0824fb02","date_updated":"2021-09-16T12:49:12Z","file_id":"8342","access_level":"closed","date_created":"2020-09-08T09:00:29Z","file_name":"2020_Urban_Bezeljak_Thesis_TeX.zip","creator":"dernst","relation":"source_file","content_type":"application/x-zip-compressed","file_size":65246782},{"creator":"dernst","content_type":"application/pdf","relation":"main_file","file_size":31259058,"file_name":"2020_Urban_Bezeljak_Thesis.pdf","access_level":"open_access","date_created":"2020-09-08T09:00:27Z","checksum":"59a62275088b00b7241e6ff4136434c7","date_updated":"2021-09-16T12:49:12Z","file_id":"8343"}],"title":"In vitro reconstitution of a Rab activation switch","degree_awarded":"PhD","language":[{"iso":"eng"}],"publication_identifier":{"issn":["2663-337X"]},"doi":"10.15479/AT:ISTA:8341"},{"publication_identifier":{"issn":["2663-337X"],"isbn":["978-3-99078-009-1"]},"doi":"10.15479/AT:ISTA:8358","language":[{"iso":"eng"}],"author":[{"id":"38FCDB4C-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0001-6730-4461","full_name":"Dos Santos Caldas, Paulo R","last_name":"Dos Santos Caldas","first_name":"Paulo R"}],"file":[{"checksum":"882f93fe9c351962120e2669b84bf088","file_id":"8364","date_updated":"2020-09-10T12:11:29Z","access_level":"open_access","date_created":"2020-09-10T12:11:29Z","file_name":"phd_thesis_pcaldas.pdf","success":1,"creator":"pcaldas","file_size":141602462,"content_type":"application/pdf","relation":"main_file"},{"checksum":"70cc9e399c4e41e6e6ac445ae55e8558","date_updated":"2020-09-11T07:48:10Z","file_id":"8365","access_level":"closed","date_created":"2020-09-10T12:18:17Z","file_name":"phd_thesis_latex_pcaldas.zip","creator":"pcaldas","content_type":"application/x-zip-compressed","relation":"source_file","file_size":450437458}],"day":"10","title":"Organization and dynamics of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinkers","degree_awarded":"PhD","publisher":"Institute of Science and Technology Austria","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","department":[{"_id":"MaLo"}],"article_processing_charge":"No","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"publication_status":"published","oa":1,"has_accepted_license":"1","supervisor":[{"orcid":"0000-0001-7309-9724","id":"462D4284-F248-11E8-B48F-1D18A9856A87","full_name":"Loose, Martin","first_name":"Martin","last_name":"Loose"}],"ddc":["572"],"date_published":"2020-09-10T00:00:00Z","acknowledged_ssus":[{"_id":"Bio"}],"alternative_title":["ISTA Thesis"],"status":"public","related_material":{"record":[{"status":"public","id":"7572","relation":"dissertation_contains"},{"id":"7197","status":"public","relation":"part_of_dissertation"}]},"citation":{"ista":"Dos Santos Caldas PR. 2020. Organization and dynamics of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinkers. Institute of Science and Technology Austria.","mla":"Dos Santos Caldas, Paulo R. <i>Organization and Dynamics of Treadmilling Filaments in Cytoskeletal Networks of FtsZ and Its Crosslinkers</i>. Institute of Science and Technology Austria, 2020, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:8358\">10.15479/AT:ISTA:8358</a>.","apa":"Dos Santos Caldas, P. R. (2020). <i>Organization and dynamics of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinkers</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT:ISTA:8358\">https://doi.org/10.15479/AT:ISTA:8358</a>","ama":"Dos Santos Caldas PR. Organization and dynamics of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinkers. 2020. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:8358\">10.15479/AT:ISTA:8358</a>","short":"P.R. Dos Santos Caldas, Organization and Dynamics of Treadmilling Filaments in Cytoskeletal Networks of FtsZ and Its Crosslinkers, Institute of Science and Technology Austria, 2020.","ieee":"P. R. Dos Santos Caldas, “Organization and dynamics of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinkers,” Institute of Science and Technology Austria, 2020.","chicago":"Dos Santos Caldas, Paulo R. “Organization and Dynamics of Treadmilling Filaments in Cytoskeletal Networks of FtsZ and Its Crosslinkers.” Institute of Science and Technology Austria, 2020. <a href=\"https://doi.org/10.15479/AT:ISTA:8358\">https://doi.org/10.15479/AT:ISTA:8358</a>."},"page":"135","date_updated":"2023-09-07T13:18:51Z","abstract":[{"lang":"eng","text":"During bacterial cell division, the tubulin-homolog FtsZ forms a ring-like structure at the center of the cell. This so-called Z-ring acts as a scaffold recruiting several division-related proteins to mid-cell and plays a key role in distributing proteins at the division site, a feature driven by the treadmilling motion of FtsZ filaments around the septum. What regulates the architecture, dynamics and stability of the Z-ring is still poorly understood, but FtsZ-associated proteins (Zaps) are known to play an important role. \r\nAdvances in fluorescence microscopy and in vitro reconstitution experiments have helped to shed light into some of the dynamic properties of these complex systems, but methods that allow to collect and analyze large quantitative data sets of the underlying polymer dynamics are still missing.\r\nHere, using an in vitro reconstitution approach, we studied how different Zaps affect FtsZ filament dynamics and organization into large-scale patterns, giving special emphasis to the role of the well-conserved protein ZapA. For this purpose, we use high-resolution fluorescence microscopy combined with novel image analysis workfows to study pattern organization and polymerization dynamics of active filaments. We quantified the influence of Zaps on FtsZ on three diferent spatial scales: the large-scale organization of the membrane-bound filament network, the underlying\r\npolymerization dynamics and the behavior of single molecules.\r\nWe found that ZapA cooperatively increases the spatial order of the filament network, binds only transiently to FtsZ filaments and has no effect on filament length and treadmilling velocity. Our data provides a model for how FtsZ-associated proteins can increase the precision and stability of the bacterial cell division machinery in a\r\nswitch-like manner, without compromising filament dynamics. Furthermore, we believe that our automated quantitative methods can be used to analyze a large variety of dynamic cytoskeletal systems, using standard time-lapse\r\nmovies of homogeneously labeled proteins obtained from experiments in vitro or even inside the living cell.\r\n"}],"oa_version":"Published Version","month":"09","type":"dissertation","date_created":"2020-09-10T09:26:49Z","file_date_updated":"2020-09-11T07:48:10Z","acknowledgement":"I should also express my gratitude to the bioimaging facility at IST Austria, for their assistance with the TIRF setup over the years, and especially to Christoph Sommer, who gave me a lot of input when I was starting to dive into programming.","year":"2020","_id":"8358"}]