[{"article_processing_charge":"Yes","quality_controlled":"1","abstract":[{"lang":"eng","text":"Formation of new amyloid fibrils and oligomers from monomeric protein on the surfaces of existing fibrils is an important driver of many disorders such as Alzheimer’s and Parkinson’s diseases. The structural basis of this secondary nucleation process, however, is poorly understood. Here, we ask whether secondary nucleation sites are found predominantly at rare growth defects: irregularities in the fibril core structure incorporated during their original assembly. We first demonstrate using the specific inhibitor of secondary nucleation, Brichos, that secondary nucleation sites on Alzheimer’s disease-associated fibrils composed of Aβ40 and Aβ42 peptides are rare compared to the number of protein molecules they contain. We then grow Aβ40 fibrils under conditions designed to eliminate most growth defects while leaving the regular fibril morphology unchanged, and confirm the latter using cryo-electron microscopy. We measure both the ability of these annealed fibrils to promote secondary nucleation and the stoichiometry of their secondary nucleation sites, finding that both are greatly reduced as predicted. Re-analysis of published data for other proteins suggests that fibril growth defects may also drive secondary nucleation generally across most amyloids. These findings could unlock structure-based drug design of therapeutics that aim to halt amyloid disorders by inhibiting secondary nucleation sites."}],"article_type":"original","publication":"Nature Communications","project":[{"call_identifier":"H2020","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","grant_number":"802960","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines"}],"file":[{"date_created":"2026-03-02T09:34:18Z","date_updated":"2026-03-02T09:34:18Z","content_type":"application/pdf","access_level":"open_access","file_name":"2026_NatureComm_Hu.pdf","checksum":"fa2b55b3a0d8978de7d2d061c7ad8779","creator":"dernst","file_size":4821073,"file_id":"21377","success":1,"relation":"main_file"}],"acknowledgement":"This work was supported by the Swedish Research Council (2019-02397 to E.S., 2015-00143 to S.L., and 2022-06641 to S.L. and E.S.), and the GenerationNano project, the European Union’s Horizon 2020 research and innovation programme under the Marie Skłodowska-Curie grant agreement No 945378 (S.L. co-PI). We acknowledge support from the Wellcome Trust (T.P.J.K.), the Cambridge Centre for Misfolding Diseases (T.P.J.K.), the BBSRC (T.P.J.K.), the Frances and Augustus Newman Foundation (T.P.J.K.), the ERC PhysProt (agreement n 337969) (T.S., T.P.J.K., S.L.), ETC StG “NEPA” (A.Š. and S.C.), the Royal Society (S.C., A.S.), the ERASMUS Programme (T.S.), and The Danish Council for Independent Research ∣ Natural Sciences (FNU-11-113326) (M.A.). This work was also funded by the Novo Nordisk Foundation (#NNF19OC0054635 to S.L.), ETH Zürich (T.C.T.M.), and the Swiss National Science Foundation (grant no 219703 to A.J.D. and T.C.T.M.). We acknowledge the use of the nano-Characterisation and nano-Manufacturing Research Equipment (nCHREM) facility for access to microscopy instrumentation. We are grateful to the late Professor Sir Christopher Dobson for invaluable conversations regarding the microfluidic diffusional sizing experiments. We are also grateful to Quentin A. E. Peter and Thomas Müller for their guidance on microfluidic device design. The cuvette-filled icon in Fig. 3d is by Servier [https://smart.servier.com/]. It is licensed under CC-BY 3.0 Unported [https://creativecommons.org/licenses/by/3.0/]. The authors would like to acknowledge Umeå Centre for Electron Microscopy (UCEM) for technical assistance and access to electron microscopy. Support was provided by SciLifeLab national Cryo-EM Unit at Umeå University.","doi":"10.1038/s41467-026-69377-1","article_number":"1933","volume":17,"publication_status":"published","oa_version":"Published Version","scopus_import":"1","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"publisher":"Springer Nature","fulldoi":"https://doi.org/10.1038/s41467-026-69377-1","ec_funded":1,"DOAJ_listed":"1","type":"journal_article","month":"02","external_id":{"pmid":["41708600"]},"author":[{"full_name":"Hu, Jing","first_name":"Jing","last_name":"Hu"},{"last_name":"Scheidt","first_name":"Tom","full_name":"Scheidt, Tom"},{"last_name":"Thacker","first_name":"Dev","full_name":"Thacker, Dev"},{"last_name":"Axell","first_name":"Emil","full_name":"Axell, Emil"},{"first_name":"Elin","last_name":"Stemme","full_name":"Stemme, Elin"},{"full_name":"Łapińska, Urszula","first_name":"Urszula","last_name":"Łapińska"},{"full_name":"Wennmalm, Stefan","last_name":"Wennmalm","first_name":"Stefan"},{"last_name":"Meisl","first_name":"Georg","full_name":"Meisl, Georg"},{"id":"031eff0d-d481-11ee-8508-cd12a7a86e5b","last_name":"Curk","first_name":"Samo","full_name":"Curk, Samo","orcid":"0000-0001-6160-9766"},{"last_name":"Andreasen","first_name":"Maria","full_name":"Andreasen, Maria"},{"full_name":"Vendruscolo, Michele","last_name":"Vendruscolo","first_name":"Michele"},{"last_name":"Arosio","first_name":"Paolo","full_name":"Arosio, Paolo"},{"first_name":"Anđela","last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela"},{"full_name":"Schmit, Jeremy D.","last_name":"Schmit","first_name":"Jeremy D."},{"last_name":"Knowles","first_name":"Tuomas P.J.","full_name":"Knowles, Tuomas P.J."},{"first_name":"Emma","last_name":"Sparr","full_name":"Sparr, Emma"},{"last_name":"Linse","first_name":"Sara","full_name":"Linse, Sara"},{"last_name":"Michaels","first_name":"Thomas C.T.","full_name":"Michaels, Thomas C.T."},{"full_name":"Dear, Alexander J.","first_name":"Alexander J.","last_name":"Dear"}],"oa":1,"has_accepted_license":"1","status":"public","department":[{"_id":"AnSa"}],"citation":{"chicago":"Hu, Jing, Tom Scheidt, Dev Thacker, Emil Axell, Elin Stemme, Urszula Łapińska, Stefan Wennmalm, et al. “Structural Defects in Amyloid-β Fibrils Drive Secondary Nucleation.” <i>Nature Communications</i>. Springer Nature, 2026. <a href=\"https://doi.org/10.1038/s41467-026-69377-1\">https://doi.org/10.1038/s41467-026-69377-1</a>.","ista":"Hu J, Scheidt T, Thacker D, Axell E, Stemme E, Łapińska U, Wennmalm S, Meisl G, Curk S, Andreasen M, Vendruscolo M, Arosio P, Šarić A, Schmit JD, Knowles TPJ, Sparr E, Linse S, Michaels TCT, Dear AJ. 2026. Structural defects in amyloid-β fibrils drive secondary nucleation. Nature Communications. 17, 1933.","ieee":"J. Hu <i>et al.</i>, “Structural defects in amyloid-β fibrils drive secondary nucleation,” <i>Nature Communications</i>, vol. 17. Springer Nature, 2026.","ama":"Hu J, Scheidt T, Thacker D, et al. Structural defects in amyloid-β fibrils drive secondary nucleation. <i>Nature Communications</i>. 2026;17. doi:<a href=\"https://doi.org/10.1038/s41467-026-69377-1\">10.1038/s41467-026-69377-1</a>","apa":"Hu, J., Scheidt, T., Thacker, D., Axell, E., Stemme, E., Łapińska, U., … Dear, A. J. (2026). Structural defects in amyloid-β fibrils drive secondary nucleation. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-026-69377-1\">https://doi.org/10.1038/s41467-026-69377-1</a>","short":"J. Hu, T. Scheidt, D. Thacker, E. Axell, E. Stemme, U. Łapińska, S. Wennmalm, G. Meisl, S. Curk, M. Andreasen, M. Vendruscolo, P. Arosio, A. Šarić, J.D. Schmit, T.P.J. Knowles, E. Sparr, S. Linse, T.C.T. Michaels, A.J. Dear, Nature Communications 17 (2026).","mla":"Hu, Jing, et al. “Structural Defects in Amyloid-β Fibrils Drive Secondary Nucleation.” <i>Nature Communications</i>, vol. 17, 1933, Springer Nature, 2026, doi:<a href=\"https://doi.org/10.1038/s41467-026-69377-1\">10.1038/s41467-026-69377-1</a>."},"date_created":"2026-03-01T23:01:38Z","OA_type":"gold","year":"2026","title":"Structural defects in amyloid-β fibrils drive secondary nucleation","PlanS_conform":"1","day":"20","pmid":1,"language":[{"iso":"eng"}],"_id":"21369","file_date_updated":"2026-03-02T09:34:18Z","publication_identifier":{"eissn":["2041-1723"]},"intvolume":"        17","OA_place":"publisher","ddc":["570"],"date_published":"2026-02-20T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2026-03-02T09:36:48Z"},{"scopus_import":"1","publisher":"AIP Publishing","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"type":"journal_article","ec_funded":1,"fulldoi":"https://doi.org/10.1063/5.0325170","volume":164,"article_number":"144902","oa_version":"Published Version","publication_status":"published","corr_author":"1","file":[{"access_level":"open_access","content_type":"application/pdf","date_created":"2026-05-05T12:35:24Z","date_updated":"2026-05-05T12:35:24Z","relation":"main_file","success":1,"file_id":"21801","file_size":8764791,"file_name":"2026_JourChemPhysics_Frey.pdf","checksum":"2e10c4f4531676e0771ef3730e4b63a9","creator":"dernst"}],"acknowledgement":"F.F. acknowledges the financial support from the NOMIS foundation. M.A. and A.Š. acknowledge the funding from the Volkswagen Foundation (Grant No. Az 96727). A.Š. acknowledges the funding from ERC Starting Grant “NEPA” (Grant No. 802960) and the Vallee Scholarship.","related_material":{"record":[{"id":"21800","status":"public","relation":"research_data"}]},"doi":"10.1063/5.0325170","article_processing_charge":"Yes (in subscription journal)","quality_controlled":"1","abstract":[{"lang":"eng","text":"Cells are defined by lipid membranes that differ in their structure across the tree of life. While the membranes of most bacteria and eukaryotes consist of single-headed bilayer lipids, the membranes of archaea are composed of mixtures of single-headed bilayer lipids and double-headed bolalipids. Archaeal bolalipids can adopt straight or u-shaped conformations, enabling them—together with bilayer lipids—to control whether membranes form bilayer or monolayer structures. Yet, the physical principles governing archaeal membranes remain largely unexplored, especially how membrane structure couples to externally imposed curvature during membrane remodeling. Here, we perform coarse-grained molecular dynamics simulations of toroidal vesicles to systematically probe the effects of all relevant combinations of mean and Gaussian curvatures on shape stability and lipid organization. We find that soft bilayer membranes can sustain all curvatures induced, whereas rigid bolalipid monolayer membranes either transition to different vesicle shapes or rupture. Bilayer-mimicking u-shaped bolalipids and bilayer lipids are spatially accumulated in regions of high mean membrane curvature independent of Gaussian curvature. Our work identifies curvature–composition coupling as a physical signature of archaeal membrane remodeling."}],"article_type":"original","publication":"Journal of Chemical Physics","project":[{"call_identifier":"H2020","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","grant_number":"802960","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines"}],"intvolume":"       164","publication_identifier":{"issn":[" 0021-9606"],"eissn":["1089-7690"]},"file_date_updated":"2026-05-05T12:35:24Z","OA_place":"publisher","ddc":["540"],"date_published":"2026-04-14T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2026-05-05T12:40:41Z","arxiv":1,"title":"Cracking donuts and sorting lipids: Geometry controls archaeal membrane stability and lipid organization","issue":"14","PlanS_conform":"1","day":"14","language":[{"iso":"eng"}],"_id":"21748","status":"public","department":[{"_id":"AnSa"}],"OA_type":"hybrid","year":"2026","date_created":"2026-04-19T22:07:45Z","citation":{"mla":"Frey, Felix F., et al. “Cracking Donuts and Sorting Lipids: Geometry Controls Archaeal Membrane Stability and Lipid Organization.” <i>Journal of Chemical Physics</i>, vol. 164, no. 14, 144902, AIP Publishing, 2026, doi:<a href=\"https://doi.org/10.1063/5.0325170\">10.1063/5.0325170</a>.","apa":"Frey, F. F., Santana de Freitas Amaral, M., &#38; Šarić, A. (2026). Cracking donuts and sorting lipids: Geometry controls archaeal membrane stability and lipid organization. <i>Journal of Chemical Physics</i>. AIP Publishing. <a href=\"https://doi.org/10.1063/5.0325170\">https://doi.org/10.1063/5.0325170</a>","short":"F.F. Frey, M. Santana de Freitas Amaral, A. Šarić, Journal of Chemical Physics 164 (2026).","ama":"Frey FF, Santana de Freitas Amaral M, Šarić A. Cracking donuts and sorting lipids: Geometry controls archaeal membrane stability and lipid organization. <i>Journal of Chemical Physics</i>. 2026;164(14). doi:<a href=\"https://doi.org/10.1063/5.0325170\">10.1063/5.0325170</a>","ieee":"F. F. Frey, M. Santana de Freitas Amaral, and A. Šarić, “Cracking donuts and sorting lipids: Geometry controls archaeal membrane stability and lipid organization,” <i>Journal of Chemical Physics</i>, vol. 164, no. 14. AIP Publishing, 2026.","chicago":"Frey, Felix F, Miguel Santana de Freitas Amaral, and Anđela Šarić. “Cracking Donuts and Sorting Lipids: Geometry Controls Archaeal Membrane Stability and Lipid Organization.” <i>Journal of Chemical Physics</i>. AIP Publishing, 2026. <a href=\"https://doi.org/10.1063/5.0325170\">https://doi.org/10.1063/5.0325170</a>.","ista":"Frey FF, Santana de Freitas Amaral M, Šarić A. 2026. Cracking donuts and sorting lipids: Geometry controls archaeal membrane stability and lipid organization. Journal of Chemical Physics. 164(14), 144902."},"month":"04","external_id":{"arxiv":["2603.15170"]},"author":[{"full_name":"Frey, Felix F","orcid":"0000-0001-8501-6017","last_name":"Frey","id":"a0270b37-8f1a-11ec-95c7-8e710c59a4f3","first_name":"Felix F"},{"full_name":"Santana de Freitas Amaral, Miguel","first_name":"Miguel","id":"4f2d02dd-47a9-11ec-ad10-82820ed3f501","last_name":"Santana de Freitas Amaral"},{"orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","first_name":"Anđela"}],"has_accepted_license":"1","oa":1},{"acknowledgement":"The authors acknowledge Crispin Hetherington and L. Tracy Yu for their technical assistance and insights. This work was funded in part by the National Science Foundation (CHE 2203937), the National Science Foundation Graduate Research Fellowship (Grant No. 1842494), the Welch Foundation (C-2141), the Swedish Research Council (2020-04633), and the NIH (GM122510). This work benefited from using the SasView application, originally developed under NSF award DMR-0520547. SasView contains code developed with funding from the European Union’s Horizon 2020 research and innovation program under the SINE2020 project, Grant Agreement No. 654000. This work was partly done using the Shared Equipment Authority resources at Rice University.","doi":"10.1021/acs.biomac.6c00345","article_processing_charge":"No","quality_controlled":"1","abstract":[{"text":"The collagen triple helix assembles hierarchically into bundled oligomers, solvated networks, and fibers. Synthetic peptide assemblies, driven by supramolecular interactions, can form single triple helices through intrahelical amino acid pairs; however, the principles guiding interhelical associations into higher-order structures remain unclear. Here, we incorporate cation−π and electrostatic charge pairs to probe interhelical interactions and elucidate the mechanisms driving triple helix assembly into fibrils, nanotubes, and nanosheets. Introducing cation−π pairs into a fibrillating collagen mimetic resulted in D-periodic fibrils with pH-sensitive gelation. By alternating the presentation of electrostatic and cation−π pairs, the assembly of another D-periodic fibril featuring inner and outer triple-helical layers was resolved by cryo electron microscopy to a resolution of 8 Å. At physiological pH, antiparallel association of these triple helices leads to the formation of nanotubes. The packing behavior of triple helices correlates with the interhelical interactions, where parallel associations favor fibril formation and antiparallel interactions drive nanotube and nanosheet assembly. These self-assembling triple-helical peptides demonstrate how packing of higher-order structures can be tailored with supramolecular interactions and establish the relationship of different hierarchical collagen-mimetic assemblies as pH-dependent.","lang":"eng"}],"article_type":"original","publication":"Biomacromolecules","scopus_import":"1","main_file_link":[{"url":"https://doi.org/10.1101/2025.02.15.637692","open_access":"1"}],"publisher":"American Chemical Society","type":"journal_article","fulldoi":"https://doi.org/10.1021/acs.biomac.6c00345","volume":27,"page":"2956-2965","oa_version":"Preprint","publication_status":"published","status":"public","department":[{"_id":"AnSa"}],"year":"2026","OA_type":"green","date_created":"2026-04-19T22:07:46Z","citation":{"ieee":"C. C. Cole <i>et al.</i>, “Supramolecular assembly of collagen-mimetic eptide D-periodic fibrils and nanoassemblies,” <i>Biomacromolecules</i>, vol. 27, no. 4. American Chemical Society, pp. 2956–2965, 2026.","ista":"Cole CC, Kreutzberger MAB, Klein K, Cahue KA, Pogostin BH, Farsheed AC, Swain JWR, Bui TH, Dey A, Makhoul JT, Dubackic M, Pal A, Olsson U, Šarić A, Egelman EH, Hartgerink JD. 2026. Supramolecular assembly of collagen-mimetic eptide D-periodic fibrils and nanoassemblies. Biomacromolecules. 27(4), 2956–2965.","chicago":"Cole, Carson C., Mark A.B. Kreutzberger, Kevin Klein, Kiana A. Cahue, Brett H. Pogostin, Adam C. Farsheed, Joseph W.R. Swain, et al. “Supramolecular Assembly of Collagen-Mimetic Eptide D-Periodic Fibrils and Nanoassemblies.” <i>Biomacromolecules</i>. American Chemical Society, 2026. <a href=\"https://doi.org/10.1021/acs.biomac.6c00345\">https://doi.org/10.1021/acs.biomac.6c00345</a>.","mla":"Cole, Carson C., et al. “Supramolecular Assembly of Collagen-Mimetic Eptide D-Periodic Fibrils and Nanoassemblies.” <i>Biomacromolecules</i>, vol. 27, no. 4, American Chemical Society, 2026, pp. 2956–65, doi:<a href=\"https://doi.org/10.1021/acs.biomac.6c00345\">10.1021/acs.biomac.6c00345</a>.","short":"C.C. Cole, M.A.B. Kreutzberger, K. Klein, K.A. Cahue, B.H. Pogostin, A.C. Farsheed, J.W.R. Swain, T.H. Bui, A. Dey, J.T. Makhoul, M. Dubackic, A. Pal, U. Olsson, A. Šarić, E.H. Egelman, J.D. Hartgerink, Biomacromolecules 27 (2026) 2956–2965.","apa":"Cole, C. C., Kreutzberger, M. A. B., Klein, K., Cahue, K. A., Pogostin, B. H., Farsheed, A. C., … Hartgerink, J. D. (2026). Supramolecular assembly of collagen-mimetic eptide D-periodic fibrils and nanoassemblies. <i>Biomacromolecules</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.biomac.6c00345\">https://doi.org/10.1021/acs.biomac.6c00345</a>","ama":"Cole CC, Kreutzberger MAB, Klein K, et al. Supramolecular assembly of collagen-mimetic eptide D-periodic fibrils and nanoassemblies. <i>Biomacromolecules</i>. 2026;27(4):2956-2965. doi:<a href=\"https://doi.org/10.1021/acs.biomac.6c00345\">10.1021/acs.biomac.6c00345</a>"},"month":"04","author":[{"full_name":"Cole, Carson C.","first_name":"Carson C.","last_name":"Cole"},{"last_name":"Kreutzberger","first_name":"Mark A.B.","full_name":"Kreutzberger, Mark A.B."},{"full_name":"Klein, Kevin","first_name":"Kevin","id":"1e7ede04-9e54-11f0-9ec4-8d4d5563c398","last_name":"Klein"},{"last_name":"Cahue","first_name":"Kiana A.","full_name":"Cahue, Kiana A."},{"full_name":"Pogostin, Brett H.","last_name":"Pogostin","first_name":"Brett H."},{"last_name":"Farsheed","first_name":"Adam C.","full_name":"Farsheed, Adam C."},{"full_name":"Swain, Joseph W.R.","last_name":"Swain","first_name":"Joseph W.R."},{"full_name":"Bui, Thi H.","first_name":"Thi H.","last_name":"Bui"},{"last_name":"Dey","first_name":"Arghadip","full_name":"Dey, Arghadip"},{"first_name":"Jonathan T.","last_name":"Makhoul","full_name":"Makhoul, Jonathan T."},{"first_name":"Marija","last_name":"Dubackic","full_name":"Dubackic, Marija"},{"full_name":"Pal, Antara","last_name":"Pal","first_name":"Antara"},{"first_name":"Ulf","last_name":"Olsson","full_name":"Olsson, Ulf"},{"orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","first_name":"Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić"},{"full_name":"Egelman, Edward H.","first_name":"Edward H.","last_name":"Egelman"},{"full_name":"Hartgerink, Jeffrey D.","last_name":"Hartgerink","first_name":"Jeffrey D."}],"oa":1,"intvolume":"        27","publication_identifier":{"eissn":["1526-4602"]},"OA_place":"repository","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2026-05-06T05:43:44Z","date_published":"2026-04-13T00:00:00Z","title":"Supramolecular assembly of collagen-mimetic eptide D-periodic fibrils and nanoassemblies","issue":"4","day":"13","language":[{"iso":"eng"}],"_id":"21749"},{"title":"Cracking donuts and sorting lipids: Geometry controls archaeal membrane stability and lipid organization","corr_author":"1","_id":"21800","day":"25","oa_version":"Published Version","publisher":"Zenodo","OA_place":"repository","main_file_link":[{"url":"https://doi.org/10.5281/ZENODO.18772086","open_access":"1"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2026-05-05T12:40:41Z","date_published":"2026-02-25T00:00:00Z","ddc":["540"],"fulldoi":"https://doi.org/10.5281/ZENODO.18772086","type":"research_data_reference","month":"02","article_processing_charge":"No","oa":1,"author":[{"orcid":"0000-0001-8501-6017","full_name":"Frey, Felix F","last_name":"Frey","id":"a0270b37-8f1a-11ec-95c7-8e710c59a4f3","first_name":"Felix F"},{"full_name":"Santana de Freitas Amaral, Miguel","id":"4f2d02dd-47a9-11ec-ad10-82820ed3f501","last_name":"Santana de Freitas Amaral","first_name":"Miguel"},{"first_name":"Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","full_name":"Šarić, Anđela","orcid":"0000-0002-7854-2139"}],"abstract":[{"lang":"eng","text":"LAMMPS input scripts to simulate toroidal vesicles composed of pure bolalipid membranes and archaeal mixture membranes for the following publication: \"Cracking donuts and sorting lipids: geometry controls archaeal membrane stability and lipid organization\" by Felix Frey, Miguel Amaral, and Andela Saric."}],"status":"public","citation":{"ista":"Frey FF, Santana de Freitas Amaral M, Šarić A. 2026. Cracking donuts and sorting lipids: Geometry controls archaeal membrane stability and lipid organization, Zenodo, <a href=\"https://doi.org/10.5281/ZENODO.18772086\">10.5281/ZENODO.18772086</a>.","chicago":"Frey, Felix F, Miguel Santana de Freitas Amaral, and Anđela Šarić. “Cracking Donuts and Sorting Lipids: Geometry Controls Archaeal Membrane Stability and Lipid Organization.” Zenodo, 2026. <a href=\"https://doi.org/10.5281/ZENODO.18772086\">https://doi.org/10.5281/ZENODO.18772086</a>.","ieee":"F. F. Frey, M. Santana de Freitas Amaral, and A. Šarić, “Cracking donuts and sorting lipids: Geometry controls archaeal membrane stability and lipid organization.” Zenodo, 2026.","ama":"Frey FF, Santana de Freitas Amaral M, Šarić A. Cracking donuts and sorting lipids: Geometry controls archaeal membrane stability and lipid organization. 2026. doi:<a href=\"https://doi.org/10.5281/ZENODO.18772086\">10.5281/ZENODO.18772086</a>","apa":"Frey, F. F., Santana de Freitas Amaral, M., &#38; Šarić, A. (2026). Cracking donuts and sorting lipids: Geometry controls archaeal membrane stability and lipid organization. Zenodo. <a href=\"https://doi.org/10.5281/ZENODO.18772086\">https://doi.org/10.5281/ZENODO.18772086</a>","short":"F.F. Frey, M. Santana de Freitas Amaral, A. Šarić, (2026).","mla":"Frey, Felix F., et al. <i>Cracking Donuts and Sorting Lipids: Geometry Controls Archaeal Membrane Stability and Lipid Organization</i>. Zenodo, 2026, doi:<a href=\"https://doi.org/10.5281/ZENODO.18772086\">10.5281/ZENODO.18772086</a>."},"date_created":"2026-05-05T12:11:52Z","doi":"10.5281/ZENODO.18772086","year":"2026","OA_type":"green","related_material":{"record":[{"relation":"used_in_publication","status":"public","id":"21748"}]},"department":[{"_id":"AnSa"}]},{"scopus_import":"1","publisher":"Cell Press","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"type":"journal_article","ec_funded":1,"fulldoi":"https://doi.org/10.1016/j.cell.2026.07.010","dataavailabilitystatement":"The fly line generated in this study is available from the lead contact without restriction.\r\nData and code availability\r\n•\r\nCollagen IV fluorescent timer image data and associated data analysis code have been deposited in the UCL Research Data Repository at https://doi.org/10.5522/04/32647191 and are publicly available as of the date of publication.\r\n•\r\nAll original code associated with the tissue mechanics model has also been deposited in the UCL Research Data Repository at https://doi.org/10.5522/04/32647191 and is publicly available as of the date of publication.\r\n•\r\nAll original code associated with the collagen IV network model has been deposited on Zenodo at https://doi.org/10.5281/zenodo.20719515 and is publicly available as of the date of publication.\r\n•\r\nAny additional information reported in this paper is available from the lead contact upon request.","volume":189,"page":"5611-5624.e4","oa_version":"Published Version","publication_status":"published","file":[{"content_type":"application/pdf","access_level":"open_access","date_updated":"2026-09-24T12:35:11Z","date_created":"2026-09-24T12:35:11Z","relation":"main_file","file_name":"2026_Cell_Barrientos.pdf","file_size":5642382,"checksum":"01e74f866223ca9ea8680b617d4aa4e3","creator":"dernst","success":1,"file_id":"22990"}],"acknowledgement":"We thank all members of the Mao lab for insightful discussions throughout the project, and we thank Giulia Paci and Nargess Khalilgharibi for critical reading of the manuscript. We thank Jonathan Chubb for molecular biology guidance and WellGenetics for generating the timer protein fly lines.\r\nR.B. was funded by a UCL COMPLEX PhD studentship and a Leverhulme Trust project grant RPG-2020-068 awarded to Y.M. B.M. and A.S. were funded by the European Union Horizon 2020 research and innovation programme (ERC starting grant no. 802960). S.B. was funded by NIH R35 GM143042. G.C. was funded by EPSRC Physics of Life, grants EP/W023806 and EP/W023865. B.J.S.S. and B.M.S. are funded by the Wellcome Trust (grant no. 301803/Z/23/Z to B.M.S.). E.K.P. was funded by the Medical Research Council UK (MRC programme award MC_UU_12018/5). Y.M. was funded by MRC award MR/W027437/1, a Lister Institute Research Prize, and the EMBO Young Investigator Programme.","doi":"10.1016/j.cell.2026.07.010","article_processing_charge":"Yes (in subscription journal)","quality_controlled":"1","article_type":"original","abstract":[{"text":"The regulation of 3D cell shape is a fundamental problem of life. In multicellular tissues, cell shape emerges through the balance of forces inside and outside the cell. In epithelia, the basement membrane (BM) is the first extracellular barrier that cells sense biochemically and mechanically. Despite this, little is known about how BM mechanical properties are regulated and how they impact cell shape. Through mathematical modeling, we show that the stress relaxation time of the BM can regulate cell shape. Using molecular dynamics simulations, we show that the stress relaxation time of a collagen IV network can be inferred from the lifetime of collagen IV molecules. To measure collagen IV lifetime in vivo, we develop a fluorescent timer reporter for collagen IV and show that perlecan modifies collagen IV lifetime. This cross-disciplinary approach establishes a multiscale framework to probe matrix turnover, and its regulation and function in cell shape control.","lang":"eng"}],"publication":"Cell","project":[{"call_identifier":"H2020","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","grant_number":"802960","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e"}],"researchdata_availability":"no","publication_identifier":{"issn":["0092-8674"],"eissn":["1097-4172"]},"supplementarymaterial":"yes","intvolume":"       189","file_date_updated":"2026-09-24T12:35:11Z","das_tickbox":"1","OA_place":"publisher","date_updated":"2026-10-20T09:04:52Z","ddc":["570"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2026-09-03T00:00:00Z","title":"Basement membrane turnover controls cell shape","pmid":1,"issue":"18","day":"03","PlanS_conform":"1","_id":"22955","language":[{"iso":"eng"}],"status":"public","department":[{"_id":"AnSa"}],"year":"2026","OA_type":"hybrid","citation":{"apa":"Barrientos, R., Meadowcroft, B., Sánchez-Sánchez, B. J., Stramer, B. M., Paluch, E. K., Charras, G., … Mao, Y. (2026). Basement membrane turnover controls cell shape. <i>Cell</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.cell.2026.07.010\">https://doi.org/10.1016/j.cell.2026.07.010</a>","short":"R. Barrientos, B. Meadowcroft, B.J. Sánchez-Sánchez, B.M. Stramer, E.K. Paluch, G. Charras, S. Banerjee, A. Šarić, Y. Mao, Cell 189 (2026) 5611–5624.e4.","ama":"Barrientos R, Meadowcroft B, Sánchez-Sánchez BJ, et al. Basement membrane turnover controls cell shape. <i>Cell</i>. 2026;189(18):5611-5624.e4. doi:<a href=\"https://doi.org/10.1016/j.cell.2026.07.010\">10.1016/j.cell.2026.07.010</a>","mla":"Barrientos, Ricardo, et al. “Basement Membrane Turnover Controls Cell Shape.” <i>Cell</i>, vol. 189, no. 18, Cell Press, 2026, p. 5611–5624.e4, doi:<a href=\"https://doi.org/10.1016/j.cell.2026.07.010\">10.1016/j.cell.2026.07.010</a>.","ieee":"R. Barrientos <i>et al.</i>, “Basement membrane turnover controls cell shape,” <i>Cell</i>, vol. 189, no. 18. Cell Press, p. 5611–5624.e4, 2026.","chicago":"Barrientos, Ricardo, Billie Meadowcroft, Besaiz J. Sánchez-Sánchez, Brian M. Stramer, Ewa K. Paluch, Guillaume Charras, Shiladitya Banerjee, Anđela Šarić, and Yanlan Mao. “Basement Membrane Turnover Controls Cell Shape.” <i>Cell</i>. Cell Press, 2026. <a href=\"https://doi.org/10.1016/j.cell.2026.07.010\">https://doi.org/10.1016/j.cell.2026.07.010</a>.","ista":"Barrientos R, Meadowcroft B, Sánchez-Sánchez BJ, Stramer BM, Paluch EK, Charras G, Banerjee S, Šarić A, Mao Y. 2026. Basement membrane turnover controls cell shape. Cell. 189(18), 5611–5624.e4."},"date_created":"2026-09-17T11:06:06Z","month":"09","external_id":{"pmid":["42532043"]},"author":[{"last_name":"Barrientos","first_name":"Ricardo","full_name":"Barrientos, Ricardo"},{"full_name":"Meadowcroft, Billie","orcid":"0000-0003-3441-1337","first_name":"Billie","last_name":"Meadowcroft","id":"a4725fd6-932b-11ed-81e2-c098c7f37ae1"},{"full_name":"Sánchez-Sánchez, Besaiz J.","last_name":"Sánchez-Sánchez","first_name":"Besaiz J."},{"first_name":"Brian M.","last_name":"Stramer","full_name":"Stramer, Brian M."},{"full_name":"Paluch, Ewa K.","last_name":"Paluch","first_name":"Ewa K."},{"full_name":"Charras, Guillaume","last_name":"Charras","first_name":"Guillaume"},{"full_name":"Banerjee, Shiladitya","last_name":"Banerjee","first_name":"Shiladitya"},{"first_name":"Anđela","last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","full_name":"Šarić, Anđela","orcid":"0000-0002-7854-2139"},{"full_name":"Mao, Yanlan","last_name":"Mao","first_name":"Yanlan"}],"has_accepted_license":"1","oa":1},{"status":"public","department":[{"_id":"AnSa"},{"_id":"EdHa"}],"year":"2025","OA_type":"gold","date_created":"2026-02-16T14:50:32Z","citation":{"ieee":"V. Sorichetti, P. Robin, I. Palaia, A. Hernandez-Armendariz, S. Cuylen-Haering, and A. Šarić, “Charge distribution of the coating brush drives interchromosome attraction,” <i>PRX Life</i>, vol. 3, no. 3. American Physical Society, 2025.","chicago":"Sorichetti, Valerio, Paul Robin, Ivan Palaia, Alberto Hernandez-Armendariz, Sara Cuylen-Haering, and Anđela Šarić. “Charge Distribution of the Coating Brush Drives Interchromosome Attraction.” <i>PRX Life</i>. American Physical Society, 2025. <a href=\"https://doi.org/10.1103/41fd-r847\">https://doi.org/10.1103/41fd-r847</a>.","ista":"Sorichetti V, Robin P, Palaia I, Hernandez-Armendariz A, Cuylen-Haering S, Šarić A. 2025. Charge distribution of the coating brush drives interchromosome attraction. PRX Life. 3(3), 033010.","mla":"Sorichetti, Valerio, et al. “Charge Distribution of the Coating Brush Drives Interchromosome Attraction.” <i>PRX Life</i>, vol. 3, no. 3, 033010, American Physical Society, 2025, doi:<a href=\"https://doi.org/10.1103/41fd-r847\">10.1103/41fd-r847</a>.","short":"V. Sorichetti, P. Robin, I. Palaia, A. Hernandez-Armendariz, S. Cuylen-Haering, A. Šarić, PRX Life 3 (2025).","apa":"Sorichetti, V., Robin, P., Palaia, I., Hernandez-Armendariz, A., Cuylen-Haering, S., &#38; Šarić, A. (2025). Charge distribution of the coating brush drives interchromosome attraction. <i>PRX Life</i>. American Physical Society. <a href=\"https://doi.org/10.1103/41fd-r847\">https://doi.org/10.1103/41fd-r847</a>","ama":"Sorichetti V, Robin P, Palaia I, Hernandez-Armendariz A, Cuylen-Haering S, Šarić A. Charge distribution of the coating brush drives interchromosome attraction. <i>PRX Life</i>. 2025;3(3). doi:<a href=\"https://doi.org/10.1103/41fd-r847\">10.1103/41fd-r847</a>"},"month":"08","author":[{"full_name":"Sorichetti, Valerio","orcid":"0000-0002-9645-6576","first_name":"Valerio","last_name":"Sorichetti","id":"ef8a92cb-c7b6-11ec-8bea-e1fd5847bc5b"},{"last_name":"Robin","id":"48c58128-57b0-11ee-9095-dc28fd97fc1d","first_name":"Paul","orcid":"0000-0002-5728-9189","full_name":"Robin, Paul"},{"last_name":"Palaia","id":"9c805cd2-4b75-11ec-a374-db6dd0ed57fa","first_name":"Ivan","orcid":" 0000-0002-8843-9485 ","full_name":"Palaia, Ivan"},{"last_name":"Hernandez-Armendariz","first_name":"Alberto","full_name":"Hernandez-Armendariz, Alberto"},{"full_name":"Cuylen-Haering, Sara","last_name":"Cuylen-Haering","first_name":"Sara"},{"orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","first_name":"Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić"}],"has_accepted_license":"1","oa":1,"intvolume":"         3","publication_identifier":{"eissn":["2835-8279"]},"file_date_updated":"2026-02-17T11:12:30Z","OA_place":"publisher","date_published":"2025-08-11T00:00:00Z","ddc":["570"],"date_updated":"2026-02-17T11:16:26Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Charge distribution of the coating brush drives interchromosome attraction","issue":"3","PlanS_conform":"1","day":"11","language":[{"iso":"eng"}],"_id":"21235","file":[{"success":1,"file_id":"21287","checksum":"1702b9bdbfd902a7c08aa4f1479b390d","file_name":"2025_PRXLife_Sorichetti.pdf","creator":"dernst","file_size":3732843,"relation":"main_file","date_created":"2026-02-17T11:12:30Z","date_updated":"2026-02-17T11:12:30Z","access_level":"open_access","content_type":"application/pdf"}],"acknowledgement":"This work was supported by the European Union’s Horizon 2020 research and innovation programme (A.Š. and V.S., ERC grant Agreement No. 802960 to A.Š., I.P. and P.R.,\r\nMarie Skłodowska-Curie Grant Agreement No. 101034413), the German Research Foundation (S.C-H. and A.H.-A., DFG Project No. 402723784 to S.C-H.), the Vallee Scholarship\r\n(A.Š. and V.S.), the EMBO Young Investigator Programme (A.Š.), and a Ph.D. fellowship from the Boehringer Ingelheim Fonds (A.H.-A.).","doi":"10.1103/41fd-r847","article_processing_charge":"Yes","quality_controlled":"1","article_type":"original","abstract":[{"text":"The condensation of charged polymers is an important driver for the formation of biomolecular condensates. Recent experiments suggest that this mechanism also controls the clustering of eukaryotic chromosomes during the late stages of cell division. In this process, interchromosome attraction is driven by the condensation of cytoplasmic RNA and Ki-67, a charged intrinsically disordered protein that coats the chromosomes as a brush. Attraction between chromosomes has been shown to be specifically promoted by a localized charged patch on Ki-67, although the physical mechanism remains unclear. To elucidate this process, we combine coarse-grained simulations and analytical theory to study the RNA-mediated interaction between charged polymer brushes on the chromosome surfaces. We show that the charged patch on Ki-67 leads to interchromosome attraction via RNA bridging between the two brushes, whereby the RNA preferentially interacts with the charged patches, leading to stable, long-range forces. By contrast, if the brush is uniformly charged, bridging is basically absent due to complete adsorption of RNA onto the brush. Moreover, the RNA dynamics becomes caged in presence of the charged patch while remaining diffusive with uniform charge. Our work sheds light on the physical origin of chromosome clustering, while also suggesting a general mechanism for cells to tune work production by biomolecular condensates via different charge distributions.","lang":"eng"}],"publication":"PRX Life","project":[{"call_identifier":"H2020","grant_number":"802960","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e"},{"call_identifier":"H2020","_id":"fc2ed2f7-9c52-11eb-aca3-c01059dda49c","grant_number":"101034413","name":"IST-BRIDGE: International postdoctoral program"},{"name":"EMBO Young Investigator Program - Andela Saric","_id":"349b6ff1-11ca-11ed-8bc3-f006047c2eeb"}],"publisher":"American Physical Society","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"type":"journal_article","DOAJ_listed":"1","ec_funded":1,"fulldoi":"https://doi.org/10.1103/41fd-r847","volume":3,"article_number":"033010","oa_version":"Published Version","publication_status":"published","corr_author":"1"},{"author":[{"last_name":"Santana de Freitas Amaral","id":"4f2d02dd-47a9-11ec-ad10-82820ed3f501","first_name":"Miguel","full_name":"Santana de Freitas Amaral, Miguel"},{"full_name":"Frey, Felix F","orcid":"0000-0001-8501-6017","last_name":"Frey","id":"a0270b37-8f1a-11ec-95c7-8e710c59a4f3","first_name":"Felix F"},{"last_name":"Jiang","first_name":"Xiuyun","full_name":"Jiang, Xiuyun"},{"full_name":"Baum, Buzz","first_name":"Buzz","last_name":"Baum"},{"last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","first_name":"Anđela","full_name":"Šarić, Anđela","orcid":"0000-0002-7854-2139"}],"has_accepted_license":"1","oa":1,"month":"10","external_id":{"pmid":["41056191 "]},"department":[{"_id":"AnSa"}],"year":"2025","OA_type":"gold","date_created":"2026-02-16T15:43:57Z","citation":{"ieee":"M. Santana de Freitas Amaral, F. F. Frey, X. Jiang, B. Baum, and A. Šarić, “Balancing stability and flexibility when reshaping archaeal membranes,” <i>eLife</i>, vol. 14. eLife Sciences Publications, 2025.","chicago":"Santana de Freitas Amaral, Miguel, Felix F Frey, Xiuyun Jiang, Buzz Baum, and Anđela Šarić. “Balancing Stability and Flexibility When Reshaping Archaeal Membranes.” <i>ELife</i>. eLife Sciences Publications, 2025. <a href=\"https://doi.org/10.7554/elife.105432\">https://doi.org/10.7554/elife.105432</a>.","ista":"Santana de Freitas Amaral M, Frey FF, Jiang X, Baum B, Šarić A. 2025. Balancing stability and flexibility when reshaping archaeal membranes. eLife. 14, 105432.","mla":"Santana de Freitas Amaral, Miguel, et al. “Balancing Stability and Flexibility When Reshaping Archaeal Membranes.” <i>ELife</i>, vol. 14, 105432, eLife Sciences Publications, 2025, doi:<a href=\"https://doi.org/10.7554/elife.105432\">10.7554/elife.105432</a>.","short":"M. Santana de Freitas Amaral, F.F. Frey, X. Jiang, B. Baum, A. Šarić, ELife 14 (2025).","apa":"Santana de Freitas Amaral, M., Frey, F. F., Jiang, X., Baum, B., &#38; Šarić, A. (2025). Balancing stability and flexibility when reshaping archaeal membranes. <i>ELife</i>. eLife Sciences Publications. <a href=\"https://doi.org/10.7554/elife.105432\">https://doi.org/10.7554/elife.105432</a>","ama":"Santana de Freitas Amaral M, Frey FF, Jiang X, Baum B, Šarić A. Balancing stability and flexibility when reshaping archaeal membranes. <i>eLife</i>. 2025;14. doi:<a href=\"https://doi.org/10.7554/elife.105432\">10.7554/elife.105432</a>"},"status":"public","pmid":1,"PlanS_conform":"1","day":"07","language":[{"iso":"eng"}],"_id":"21251","title":"Balancing stability and flexibility when reshaping archaeal membranes","ddc":["570"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2025-10-07T00:00:00Z","date_updated":"2026-02-23T11:49:05Z","intvolume":"        14","publication_identifier":{"eissn":["2050-084X"]},"file_date_updated":"2026-02-17T13:02:02Z","OA_place":"publisher","article_type":"original","abstract":[{"text":"Cellular membranes differ across the tree of life. In most bacteria and eukaryotes, single-headed lipids self-assemble into flexible bilayer membranes. By contrast, thermophilic archaea tend to possess bilayer lipids together with double-headed, monolayer spanning bolalipids, which are thought to enable cells to survive in harsh environments. Here, using a minimal computational model for bolalipid membranes, we explore the trade-offs at play when forming membranes. We find that flexible bolalipids form membranes that resemble bilayer membranes because they are able to assume a U-shaped conformation. Conversely, rigid bolalipids, which resemble the bolalipids with cyclic groups found in thermophilic archaea, take on a straight conformation and form membranes that are stiff and prone to pore formation when they undergo changes in shape. Strikingly, however, the inclusion of small amounts of bilayer lipids in a bolalipid membrane is enough to achieve fluid bolalipid membranes that are both stable and flexible, resolving this trade-off. Our study suggests a mechanism by which archaea can tune the material properties of their membranes as and when required to enable them to survive in harsh environments and to undergo essential membrane remodelling events like cell division.","lang":"eng"}],"project":[{"name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","grant_number":"802960","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","call_identifier":"H2020"}],"publication":"eLife","article_processing_charge":"Yes","quality_controlled":"1","acknowledgement":"MA, BB, and AŠ acknowledge funding by the Volkswagen Foundation Grant Az 96727. FF acknowledges financial support by the NOMIS foundation. AŠ acknowledges funding by ERC Starting Grant 'NEPA' 802960. We thank Claudia Flandoli for her help with illustrations.","related_material":{"record":[{"id":"21304","status":"public","relation":"software"}]},"doi":"10.7554/elife.105432","file":[{"file_id":"21305","success":1,"file_size":10668225,"checksum":"4116cd5143558ded995fb9ff5fcbc7e0","file_name":"2025_elife_Amaral.pdf","creator":"dernst","relation":"main_file","date_updated":"2026-02-17T13:02:02Z","date_created":"2026-02-17T13:02:02Z","access_level":"open_access","content_type":"application/pdf"}],"oa_version":"Published Version","publication_status":"published","corr_author":"1","volume":14,"article_number":"105432","DOAJ_listed":"1","type":"journal_article","fulldoi":"https://doi.org/10.7554/elife.105432","ec_funded":1,"publisher":"eLife Sciences Publications","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"}},{"month":"09","has_accepted_license":"1","oa":1,"author":[{"id":"a4725fd6-932b-11ed-81e2-c098c7f37ae1","last_name":"Meadowcroft","first_name":"Billie","full_name":"Meadowcroft, Billie","orcid":"0000-0003-3441-1337"},{"last_name":"Sorichetti","id":"ef8a92cb-c7b6-11ec-8bea-e1fd5847bc5b","first_name":"Valerio","orcid":"0000-0002-9645-6576","full_name":"Sorichetti, Valerio"},{"last_name":"Ratajczyk","first_name":"Eryk","full_name":"Ratajczyk, Eryk"},{"full_name":"Perez Verdugo, Fernanda L","first_name":"Fernanda L","last_name":"Perez Verdugo","id":"4ecec223-9070-11ef-a0a9-bc76077bea8d"},{"first_name":"Nargess","last_name":"Khalilgharibi","full_name":"Khalilgharibi, Nargess"},{"full_name":"Mao, Yanlan","first_name":"Yanlan","last_name":"Mao"},{"full_name":"Palaia, Ivan","orcid":" 0000-0002-8843-9485 ","first_name":"Ivan","id":"9c805cd2-4b75-11ec-a374-db6dd0ed57fa","last_name":"Palaia"},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","first_name":"Anđela","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela"}],"status":"public","OA_type":"gold","year":"2025","citation":{"mla":"Meadowcroft, Billie, et al. “Nonequilibrium Remodeling of Collagen IV Networks in Silico.” <i>PRX Life</i>, vol. 3, 033019, American Physical Society, 2025, doi:<a href=\"https://doi.org/10.1103/gdd5-rnh7\">10.1103/gdd5-rnh7</a>.","ama":"Meadowcroft B, Sorichetti V, Ratajczyk E, et al. Nonequilibrium remodeling of collagen IV networks in Silico. <i>PRX Life</i>. 2025;3. doi:<a href=\"https://doi.org/10.1103/gdd5-rnh7\">10.1103/gdd5-rnh7</a>","short":"B. Meadowcroft, V. Sorichetti, E. Ratajczyk, F.L. Perez Verdugo, N. Khalilgharibi, Y. Mao, I. Palaia, A. Šarić, PRX Life 3 (2025).","apa":"Meadowcroft, B., Sorichetti, V., Ratajczyk, E., Perez Verdugo, F. L., Khalilgharibi, N., Mao, Y., … Šarić, A. (2025). Nonequilibrium remodeling of collagen IV networks in Silico. <i>PRX Life</i>. American Physical Society. <a href=\"https://doi.org/10.1103/gdd5-rnh7\">https://doi.org/10.1103/gdd5-rnh7</a>","chicago":"Meadowcroft, Billie, Valerio Sorichetti, Eryk Ratajczyk, Fernanda L Perez Verdugo, Nargess Khalilgharibi, Yanlan Mao, Ivan Palaia, and Anđela Šarić. “Nonequilibrium Remodeling of Collagen IV Networks in Silico.” <i>PRX Life</i>. American Physical Society, 2025. <a href=\"https://doi.org/10.1103/gdd5-rnh7\">https://doi.org/10.1103/gdd5-rnh7</a>.","ista":"Meadowcroft B, Sorichetti V, Ratajczyk E, Perez Verdugo FL, Khalilgharibi N, Mao Y, Palaia I, Šarić A. 2025. Nonequilibrium remodeling of collagen IV networks in Silico. PRX Life. 3, 033019.","ieee":"B. Meadowcroft <i>et al.</i>, “Nonequilibrium remodeling of collagen IV networks in Silico,” <i>PRX Life</i>, vol. 3. American Physical Society, 2025."},"date_created":"2026-02-16T15:55:03Z","department":[{"_id":"AnSa"}],"title":"Nonequilibrium remodeling of collagen IV networks in Silico","_id":"21256","language":[{"iso":"eng"}],"day":"05","PlanS_conform":"1","OA_place":"publisher","publication_identifier":{"eissn":["2835-8279"]},"intvolume":"         3","file_date_updated":"2026-02-17T13:36:01Z","ddc":["570"],"date_published":"2025-09-05T00:00:00Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2026-02-17T13:37:38Z","quality_controlled":"1","article_processing_charge":"Yes","project":[{"_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","grant_number":"802960","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","call_identifier":"H2020"},{"_id":"fc2ed2f7-9c52-11eb-aca3-c01059dda49c","name":"IST-BRIDGE: International postdoctoral program","grant_number":"101034413","call_identifier":"H2020"},{"name":"EMBO Young Investigator Program - Andela Saric","_id":"349b6ff1-11ca-11ed-8bc3-f006047c2eeb"}],"publication":"PRX Life","abstract":[{"lang":"eng","text":"Collagen IV is one of the main components of the basement membrane, a layer of material that lines the majority of tissues in multicellular organisms. Collagen IV molecules assemble into networks, providing stiffness and elasticity to tissues and informing cell and organ shape, especially during development. In this work, we develop two coarse-grained models for collagen IV molecules that retain biochemical bond specificity and coarse grain at different length scales. Through molecular-dynamics simulations, we test the assembly and mechanics of the resulting networks and measure their response to strain in terms of stress, microscopic alignment, and bond dynamics. Within the basement membrane, collagen IV networks rearrange by molecule turnover, which affects tissue organization and can be linked with enzyme activity. Here we explore network rearrangements via bond remodeling, the process of breaking and remaking of bonds between network molecules. We then investigate the effects of active (enzymatic) bond remodeling. We find that this nonequilibrium remodeling allows a network to keep its integrity under strain, while relaxing fully over a variety of timescales, a dynamic response that is unavailable to networks undergoing equilibrium remodeling."}],"article_type":"original","file":[{"file_size":2277704,"checksum":"04cae5231d97e533145c493880fadbd9","creator":"dernst","file_name":"2025_PRXLife_Meadowcroft.pdf","file_id":"21308","success":1,"relation":"main_file","date_updated":"2026-02-17T13:36:01Z","date_created":"2026-02-17T13:36:01Z","content_type":"application/pdf","access_level":"open_access"}],"doi":"10.1103/gdd5-rnh7","acknowledgement":"This work received funding from the European Research Council under the European Union's Horizon 2020 research and innovation program through Grant Agreement No. 802960 (B.M., V.S., I.P., and A.Š.), the European Union's Horizon 2020 research and innovation program under the Marie Skłodowska-Curie Grant Agreement No. 101034413 (I.P.), the NOMIS Foundation (F.P.-V.), the National Centre for the Replacement, Refinement and Reduction of Animals in Research Grant No. NC/T002425/1 (N.K.), Leverhulme Trust project Grant No. RPG-2020-068 (N.K.), MRC Fellowship No. MR/W027437/1 (Y.M.), a Lister Institute Research Prize (Y.M.) and EMBO Young Investigator Programme (Y.M. and A.Š.).","volume":3,"article_number":"033019","corr_author":"1","oa_version":"Published Version","publication_status":"published","publisher":"American Physical Society","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"type":"journal_article","DOAJ_listed":"1","fulldoi":"https://doi.org/10.1103/gdd5-rnh7","ec_funded":1},{"status":"public","department":[{"_id":"AnSa"}],"year":"2025","OA_type":"hybrid","citation":{"ista":"Muñoz Basagoiti M, Frey FF, Meadowcroft B, Santana de Freitas Amaral M, Prada A, Šarić A. 2025. A tutorial for mesoscale computer simulations of lipid membranes: Tether pulling, tubulation and fluctuations. Soft Matter. 21(40), 7736–7756.","chicago":"Muñoz Basagoiti, Maitane, Felix F Frey, Billie Meadowcroft, Miguel Santana de Freitas Amaral, Adam Prada, and Anđela Šarić. “A Tutorial for Mesoscale Computer Simulations of Lipid Membranes: Tether Pulling, Tubulation and Fluctuations.” <i>Soft Matter</i>. Royal Society of Chemistry, 2025. <a href=\"https://doi.org/10.1039/d5sm00148j\">https://doi.org/10.1039/d5sm00148j</a>.","ieee":"M. Muñoz Basagoiti, F. F. Frey, B. Meadowcroft, M. Santana de Freitas Amaral, A. Prada, and A. Šarić, “A tutorial for mesoscale computer simulations of lipid membranes: Tether pulling, tubulation and fluctuations,” <i>Soft Matter</i>, vol. 21, no. 40. Royal Society of Chemistry, pp. 7736–7756, 2025.","ama":"Muñoz Basagoiti M, Frey FF, Meadowcroft B, Santana de Freitas Amaral M, Prada A, Šarić A. A tutorial for mesoscale computer simulations of lipid membranes: Tether pulling, tubulation and fluctuations. <i>Soft Matter</i>. 2025;21(40):7736-7756. doi:<a href=\"https://doi.org/10.1039/d5sm00148j\">10.1039/d5sm00148j</a>","apa":"Muñoz Basagoiti, M., Frey, F. F., Meadowcroft, B., Santana de Freitas Amaral, M., Prada, A., &#38; Šarić, A. (2025). A tutorial for mesoscale computer simulations of lipid membranes: Tether pulling, tubulation and fluctuations. <i>Soft Matter</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/d5sm00148j\">https://doi.org/10.1039/d5sm00148j</a>","short":"M. Muñoz Basagoiti, F.F. Frey, B. Meadowcroft, M. Santana de Freitas Amaral, A. Prada, A. Šarić, Soft Matter 21 (2025) 7736–7756.","mla":"Muñoz Basagoiti, Maitane, et al. “A Tutorial for Mesoscale Computer Simulations of Lipid Membranes: Tether Pulling, Tubulation and Fluctuations.” <i>Soft Matter</i>, vol. 21, no. 40, Royal Society of Chemistry, 2025, pp. 7736–56, doi:<a href=\"https://doi.org/10.1039/d5sm00148j\">10.1039/d5sm00148j</a>."},"date_created":"2025-09-10T05:34:36Z","month":"07","external_id":{"isi":["001562846800001"],"arxiv":["2502.09798"]},"author":[{"full_name":"Muñoz Basagoiti, Maitane","orcid":"0000-0003-1483-1457","first_name":"Maitane","id":"1a8a7950-82cd-11ed-bd4f-9624c913a607","last_name":"Muñoz Basagoiti"},{"last_name":"Frey","id":"a0270b37-8f1a-11ec-95c7-8e710c59a4f3","first_name":"Felix F","full_name":"Frey, Felix F","orcid":"0000-0001-8501-6017"},{"orcid":"0000-0003-3441-1337","full_name":"Meadowcroft, Billie","first_name":"Billie","last_name":"Meadowcroft","id":"a4725fd6-932b-11ed-81e2-c098c7f37ae1"},{"full_name":"Santana de Freitas Amaral, Miguel","first_name":"Miguel","id":"4f2d02dd-47a9-11ec-ad10-82820ed3f501","last_name":"Santana de Freitas Amaral"},{"first_name":"Adam","id":"a43ed60a-dd22-11ed-9bf7-b34133792ea9","last_name":"Prada","full_name":"Prada, Adam"},{"first_name":"Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela"}],"oa":1,"has_accepted_license":"1","intvolume":"        21","publication_identifier":{"issn":["1744-683X"],"eissn":["1744-6848"]},"file_date_updated":"2025-12-30T10:16:40Z","OA_place":"publisher","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2025-07-28T00:00:00Z","date_updated":"2025-12-30T10:16:52Z","ddc":["540"],"arxiv":1,"title":"A tutorial for mesoscale computer simulations of lipid membranes: Tether pulling, tubulation and fluctuations","issue":"40","isi":1,"day":"28","language":[{"iso":"eng"}],"_id":"20318","file":[{"relation":"main_file","file_size":4841140,"file_name":"2025_SoftMatter_MunozBasagoiti.pdf","creator":"dernst","checksum":"590bedad19b6f6d40a7ee036a056a6d9","success":1,"file_id":"20912","content_type":"application/pdf","access_level":"open_access","date_created":"2025-12-30T10:16:40Z","date_updated":"2025-12-30T10:16:40Z"}],"acknowledgement":"We thank Oded Farago, Angelo Cacciuto, Jeriann Beiter and Pietro Sillano for helpful discussions and a critical reading of the manuscript. MMB and AP acknowledge funding by the European Unions Horizon 2020 research and innovation programme under Marie Skłodowska-Curie Grant Agreement No. 101034413. FF acknowledges financial support by the NOMIS foundation. BM and AŠ acknowledge funding by ERC Starting Grant “NEPA” 802960. MA and AŠ acknowledge funding by the Volkswagen Foundation Grant Az 96727.","doi":"10.1039/d5sm00148j","article_processing_charge":"Yes (via OA deal)","quality_controlled":"1","abstract":[{"text":"Lipid membranes and membrane deformations are a long-standing area of research in soft matter and biophysics. Computer simulations have complemented analytical and experimental approaches as one of the pillars in the field. However, setting up and using membrane simulations can come with barriers due to the multidisciplinary effort involved and the vast choice of existing simulations models. In this review, we introduce the non-expert reader to coarse-grained membrane simulations at the mesoscale. Firstly, we give a concise overview of the modelling approaches to study fluid membranes, together with guidance to more specialized references. Secondly, we provide a conceptual guide on how to develop mesoscale membrane simulations. Lastly, we construct a hands-on tutorial on how to apply mesoscale membrane simulations, by providing a pedagogical examination of membrane tether pulling, shape and mechanics of membrane tubes, and membrane fluctuations with three different membrane models, and discussing them in terms of their scope and how resource-intensive they are. To ease the reader's venture into the field, we provide a repository with ready-to-run tutorials.","lang":"eng"}],"article_type":"original","project":[{"call_identifier":"H2020","_id":"fc2ed2f7-9c52-11eb-aca3-c01059dda49c","grant_number":"101034413","name":"IST-BRIDGE: International postdoctoral program"},{"_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","grant_number":"802960","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","call_identifier":"H2020"},{"_id":"9B861AAC-BA93-11EA-9121-9846C619BF3A","name":"NOMIS Fellowship Program"},{"_id":"eba0f67c-77a9-11ec-83b8-cc8501b3e222","grant_number":"96752","name":"The evolution of trafficking: from archaea to eukaryotes"}],"publication":"Soft Matter","scopus_import":"1","publisher":"Royal Society of Chemistry","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","short":"CC BY-NC (4.0)","name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","image":"/images/cc_by_nc.png"},"license":"https://creativecommons.org/licenses/by-nc/4.0/","type":"journal_article","ec_funded":1,"fulldoi":"https://doi.org/10.1039/d5sm00148j","volume":21,"page":"7736-7756","oa_version":"Published Version","publication_status":"published","corr_author":"1"},{"fulldoi":"https://doi.org/10.1073/pnas.2513939122","ec_funded":1,"type":"journal_article","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"publisher":"National Academy of Sciences","scopus_import":"1","publication_status":"published","oa_version":"Published Version","page":"e2513939122","volume":122,"doi":"10.1073/pnas.2513939122","acknowledgement":"We thank Matthew Kenneth for his assistance with live cell imaging. We thank Arthur Charles-Orszag and Dyche Mullins for generously gifting the SegA and SegB antibodies, and Sonja-Verena Albers for gifting the CdvA-HA overexpression plasmid. We thank the Light Microscopy and Flow Cytometry facilities at the MRC-LMB, and all the core staff at the MRC-LMB for their support. We thank all members of the Baum lab for helpful discussions. We would like to thank Magdalena Lechowska, Gautam Dey, Laura Downie, and Iva Tolic for critical reading of the manuscript. J.P. was supported by the Medical Research Council—Laboratory of Molecular Biology (MC_UP_1201/27). A.C. was funded by an EMBO Postdoctoral fellowship (ALTF_1041-2021), a Marie Sklodowska-Curie Individual Fellowship (101068523) provided by UKRI and by the Wellcome Trust (222460/Z/21/Z). B.H. was supported by Wellcome Trust (203276/A/16/Z). Y.-W.K. was supported by an EMBO postdoctoral fellowship (ALTF 903-2021) and by the Medical Research Council—Laboratory of Molecular Biology (MC_UP_1201/27); S.F. was supported by the Wellcome Trust (222460/Z/21/Z); B.B. received support from the MRC LMB, the Wellcome Trust (203276/Z/16/Z) and (222460/Z/21/Z), the VW Foundation (94933), and from the Gordon and Betty Moore Foundation’s Symbiosis in Aquatic Systems Initiative (9346). V.S. and A.Š. acknowledge funding from the European Research Council under the European Union’s Horizon 2020 research and innovation programme (grant no.802960 to A.Š.), the Vallee Scholarship, and the EMBO Young Investigator Programme (A.Š.). The collaborative work of A.Š.’s and B.B. teams was also supported by a Moore–Simons Project on the Origin of the Eukaryotic Cell, Simons Foundation 735929LPI.","file":[{"relation":"main_file","checksum":"3555d51f438d2e356039a9b697eac3ee","file_size":2649194,"creator":"dernst","file_name":"2025_PNAS_Parham.pdf","success":1,"file_id":"20543","content_type":"application/pdf","access_level":"open_access","date_created":"2025-10-27T08:12:59Z","date_updated":"2025-10-27T08:12:59Z"}],"publication":"Proceedings of the National Academy of Sciences","project":[{"_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","grant_number":"802960","call_identifier":"H2020"},{"name":"EMBO Young Investigator Program - Andela Saric","_id":"349b6ff1-11ca-11ed-8bc3-f006047c2eeb"}],"article_type":"original","abstract":[{"text":"Cells must coordinate DNA segregation with cytokinesis to ensure that each daughter cell inherits a complete genome. Here, we explore how DNA segregation and division are mechanistically coupled in archaeal relatives of eukaryotes, which lack Cyclin-dependent kinase (CDK)/Cyclins. Using live cell imaging, we first describe the series of sequential changes in DNA organization that accompany cell division in Sulfolobus, which computational modeling shows likely aid genome segregation. Through a perturbation analysis we identify a regulatory checkpoint which ensures that the compaction of the genome into two spatially segregated nucleoids only occurs once cells have assembled a division ring—which also defines the axis of DNA segregation. Finally, we show that DNA compaction and segregation depend, in part, on a ParA homologue, SegA, and its partner SegB, whose absence leads to bridging DNA. Taken together, these data show how regulatory checkpoints like those operating in eukaryotes aid high-fidelity division in an archaeon.","lang":"eng"}],"quality_controlled":"1","article_processing_charge":"Yes (in subscription journal)","date_updated":"2026-02-16T12:32:31Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","ddc":["570"],"date_published":"2025-10-21T00:00:00Z","OA_place":"publisher","file_date_updated":"2025-10-27T08:12:59Z","publication_identifier":{"eissn":["1091-6490"]},"intvolume":"       122","_id":"20530","language":[{"iso":"eng"}],"PlanS_conform":"1","day":"21","issue":"42","isi":1,"pmid":1,"title":"Temporal and spatial coordination of DNA segregation and cell division in an archaeon","citation":{"apa":"Parham, J., Sorichetti, V., Cezanne, A., Foo, S., Kuo, Y. W., Hoogenberg, B., … Baum, B. (2025). Temporal and spatial coordination of DNA segregation and cell division in an archaeon. <i>Proceedings of the National Academy of Sciences</i>. National Academy of Sciences. <a href=\"https://doi.org/10.1073/pnas.2513939122\">https://doi.org/10.1073/pnas.2513939122</a>","short":"J. Parham, V. Sorichetti, A. Cezanne, S. Foo, Y.W. Kuo, B. Hoogenberg, A. Radoux-Mergault, E. Mawdesley, L.D. Gatward, J. Boulanger, U. Schulze, A. Šarić, B. Baum, Proceedings of the National Academy of Sciences 122 (2025) e2513939122.","ama":"Parham J, Sorichetti V, Cezanne A, et al. Temporal and spatial coordination of DNA segregation and cell division in an archaeon. <i>Proceedings of the National Academy of Sciences</i>. 2025;122(42):e2513939122. doi:<a href=\"https://doi.org/10.1073/pnas.2513939122\">10.1073/pnas.2513939122</a>","mla":"Parham, Joe, et al. “Temporal and Spatial Coordination of DNA Segregation and Cell Division in an Archaeon.” <i>Proceedings of the National Academy of Sciences</i>, vol. 122, no. 42, National Academy of Sciences, 2025, p. e2513939122, doi:<a href=\"https://doi.org/10.1073/pnas.2513939122\">10.1073/pnas.2513939122</a>.","ieee":"J. Parham <i>et al.</i>, “Temporal and spatial coordination of DNA segregation and cell division in an archaeon,” <i>Proceedings of the National Academy of Sciences</i>, vol. 122, no. 42. National Academy of Sciences, p. e2513939122, 2025.","ista":"Parham J, Sorichetti V, Cezanne A, Foo S, Kuo YW, Hoogenberg B, Radoux-Mergault A, Mawdesley E, Gatward LD, Boulanger J, Schulze U, Šarić A, Baum B. 2025. Temporal and spatial coordination of DNA segregation and cell division in an archaeon. Proceedings of the National Academy of Sciences. 122(42), e2513939122.","chicago":"Parham, Joe, Valerio Sorichetti, Alice Cezanne, Sherman Foo, Yin Wei Kuo, Baukje Hoogenberg, Arthur Radoux-Mergault, et al. “Temporal and Spatial Coordination of DNA Segregation and Cell Division in an Archaeon.” <i>Proceedings of the National Academy of Sciences</i>. National Academy of Sciences, 2025. <a href=\"https://doi.org/10.1073/pnas.2513939122\">https://doi.org/10.1073/pnas.2513939122</a>."},"date_created":"2025-10-26T23:01:33Z","OA_type":"hybrid","year":"2025","department":[{"_id":"AnSa"}],"status":"public","has_accepted_license":"1","oa":1,"author":[{"full_name":"Parham, Joe","last_name":"Parham","first_name":"Joe"},{"last_name":"Sorichetti","id":"ef8a92cb-c7b6-11ec-8bea-e1fd5847bc5b","first_name":"Valerio","full_name":"Sorichetti, Valerio","orcid":"0000-0002-9645-6576"},{"full_name":"Cezanne, Alice","last_name":"Cezanne","first_name":"Alice"},{"full_name":"Foo, Sherman","first_name":"Sherman","last_name":"Foo"},{"first_name":"Yin Wei","last_name":"Kuo","full_name":"Kuo, Yin Wei"},{"first_name":"Baukje","last_name":"Hoogenberg","full_name":"Hoogenberg, Baukje"},{"full_name":"Radoux-Mergault, Arthur","first_name":"Arthur","last_name":"Radoux-Mergault"},{"first_name":"Eloise","last_name":"Mawdesley","full_name":"Mawdesley, Eloise"},{"last_name":"Gatward","first_name":"Lydia Daniels","full_name":"Gatward, Lydia Daniels"},{"last_name":"Boulanger","first_name":"Jerome","full_name":"Boulanger, Jerome"},{"full_name":"Schulze, Ulrike","first_name":"Ulrike","last_name":"Schulze"},{"orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","first_name":"Anđela"},{"full_name":"Baum, Buzz","last_name":"Baum","first_name":"Buzz"}],"external_id":{"isi":["001620648600001"],"pmid":["41091768"]},"month":"10"},{"language":[{"iso":"eng"}],"_id":"14844","pmid":1,"issue":"3","isi":1,"day":"06","title":"Nonadditivity in interactions between three membrane-wrapped colloidal spheres","date_updated":"2026-09-24T10:26:59Z","date_published":"2024-02-06T00:00:00Z","ddc":["570"],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","das_tickbox":"0","supplementarymaterial":"no","intvolume":"       123","publication_identifier":{"issn":["0006-3495"],"eissn":["1542-0086"]},"file_date_updated":"2024-07-16T12:09:55Z","has_accepted_license":"1","oa":1,"author":[{"full_name":"Azadbakht, Ali","first_name":"Ali","last_name":"Azadbakht"},{"full_name":"Meadowcroft, Billie","orcid":"0000-0003-3441-1337","last_name":"Meadowcroft","id":"a4725fd6-932b-11ed-81e2-c098c7f37ae1","first_name":"Billie"},{"full_name":"Majek, Juraj","first_name":"Juraj","id":"3e6d9473-f38e-11ec-8ae0-c4e05a8aa9e1","last_name":"Majek"},{"orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","first_name":"Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić"},{"last_name":"Kraft","first_name":"Daniela J.","full_name":"Kraft, Daniela J."}],"external_id":{"isi":["001185235900001"],"pmid":["38158654"]},"month":"02","year":"2024","date_created":"2024-01-21T23:00:56Z","citation":{"mla":"Azadbakht, Ali, et al. “Nonadditivity in Interactions between Three Membrane-Wrapped Colloidal Spheres.” <i>Biophysical Journal</i>, vol. 123, no. 3, Elsevier, 2024, pp. 307–16, doi:<a href=\"https://doi.org/10.1016/j.bpj.2023.12.020\">10.1016/j.bpj.2023.12.020</a>.","ama":"Azadbakht A, Meadowcroft B, Majek J, Šarić A, Kraft DJ. Nonadditivity in interactions between three membrane-wrapped colloidal spheres. <i>Biophysical Journal</i>. 2024;123(3):307-316. doi:<a href=\"https://doi.org/10.1016/j.bpj.2023.12.020\">10.1016/j.bpj.2023.12.020</a>","short":"A. Azadbakht, B. Meadowcroft, J. Majek, A. Šarić, D.J. Kraft, Biophysical Journal 123 (2024) 307–316.","apa":"Azadbakht, A., Meadowcroft, B., Majek, J., Šarić, A., &#38; Kraft, D. J. (2024). Nonadditivity in interactions between three membrane-wrapped colloidal spheres. <i>Biophysical Journal</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.bpj.2023.12.020\">https://doi.org/10.1016/j.bpj.2023.12.020</a>","chicago":"Azadbakht, Ali, Billie Meadowcroft, Juraj Majek, Anđela Šarić, and Daniela J. Kraft. “Nonadditivity in Interactions between Three Membrane-Wrapped Colloidal Spheres.” <i>Biophysical Journal</i>. Elsevier, 2024. <a href=\"https://doi.org/10.1016/j.bpj.2023.12.020\">https://doi.org/10.1016/j.bpj.2023.12.020</a>.","ista":"Azadbakht A, Meadowcroft B, Majek J, Šarić A, Kraft DJ. 2024. Nonadditivity in interactions between three membrane-wrapped colloidal spheres. Biophysical Journal. 123(3), 307–316.","ieee":"A. Azadbakht, B. Meadowcroft, J. Majek, A. Šarić, and D. J. Kraft, “Nonadditivity in interactions between three membrane-wrapped colloidal spheres,” <i>Biophysical Journal</i>, vol. 123, no. 3. Elsevier, pp. 307–316, 2024."},"department":[{"_id":"AnSa"}],"status":"public","oa_version":"Published Version","publication_status":"published","volume":123,"page":"307-316","type":"journal_article","fulldoi":"https://doi.org/10.1016/j.bpj.2023.12.020","ec_funded":1,"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"},"scopus_import":"1","researchdata_availability":"no","project":[{"name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","grant_number":"802960","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","call_identifier":"H2020"}],"publication":"Biophysical Journal","article_type":"original","abstract":[{"text":"Many cell functions require a concerted effort from multiple membrane proteins, for example, for signaling, cell division, and endocytosis. One contribution to their successful self-organization stems from the membrane deformations that these proteins induce. While the pairwise interaction potential of two membrane-deforming spheres has recently been measured, membrane-deformation-induced interactions have been predicted to be nonadditive, and hence their collective behavior cannot be deduced from this measurement. We here employ a colloidal model system consisting of adhesive spheres and giant unilamellar vesicles to test these predictions by measuring the interaction potential of the simplest case of three membrane-deforming, spherical particles. We quantify their interactions and arrangements and, for the first time, experimentally confirm and quantify the nonadditive nature of membrane-deformation-induced interactions. We furthermore conclude that there exist two favorable configurations on the membrane: (1) a linear and (2) a triangular arrangement of the three spheres. Using Monte Carlo simulations, we corroborate the experimentally observed energy minima and identify a lowering of the membrane deformation as the cause for the observed configurations. The high symmetry of the preferred arrangements for three particles suggests that arrangements of many membrane-deforming objects might follow simple rules.","lang":"eng"}],"quality_controlled":"1","article_processing_charge":"Yes (in subscription journal)","doi":"10.1016/j.bpj.2023.12.020","acknowledgement":"We gratefully acknowledge useful discussions with Casper van der Wel, help by Yogesh Shelke with PAA coverslip preparation, and support by Rachel Doherty with particle functionalization. A.A. and D.J.K. would like to thank Timon Idema and George Dadunashvili for initial attempts to simulate the experimental system. D.J.K. would like to thank the physics department at Leiden University for funding the PhD position of A.A. B.M. and A.Š. acknowledge funding by the European Union’s Horizon 2020 research and innovation programme (ERC starting grant no. 802960).","file":[{"file_id":"17266","success":1,"checksum":"1c8fe1cf950394875b65b90da86428ff","file_name":"2024_BiophysicalJournal_Azadbakht.pdf","creator":"dernst","file_size":3189926,"relation":"main_file","date_updated":"2024-07-16T12:09:55Z","date_created":"2024-07-16T12:09:55Z","access_level":"open_access","content_type":"application/pdf"}]},{"scopus_import":"1","publisher":"National Academy of Sciences","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","image":"/images/cc_by_nc_nd.png"},"type":"journal_article","fulldoi":"https://doi.org/10.1073/pnas.2220075121","ec_funded":1,"dataavailabilitystatement":"Aggregation data and the source code for the coarse-grained computer model have been deposited in Figshare (https://figshare.com/s/85798bba4ebc68d822ed)","volume":121,"article_number":"e2220075121","oa_version":"Published Version","publication_status":"published","corr_author":"1","file":[{"file_id":"15026","success":1,"file_name":"2024_PNAS_Curk.pdf","file_size":7699487,"checksum":"5aeb65bcc0dd829b1f9ab307c5031d4b","creator":"dernst","relation":"main_file","date_updated":"2024-02-26T08:20:00Z","date_created":"2024-02-26T08:20:00Z","access_level":"open_access","content_type":"application/pdf"}],"related_material":{"record":[{"status":"public","relation":"research_data","id":"15027"}]},"acknowledgement":"We acknowledge support from the Erasmus programme and the University College London Institute for the Physics of Living Systems (S.C., T.C.T.M., A.Š.), the Biotechnology and Biological Sciences Research Council (T.P.J.K.), the Engineering and Physical Sciences Research Council (D.F.), the European Research Council (T.P.J.K., S.L., D.F., and A.Š.), the Frances and Augustus Newman Foundation (T.P.J.K.), the Academy of Medical Sciences and Wellcome Trust (A.Š.), and the Royal Society (S.C. and A.Š.).","doi":"10.1073/pnas.2220075121","article_processing_charge":"Yes (in subscription journal)","quality_controlled":"1","abstract":[{"text":"Self-replication of amyloid fibrils via secondary nucleation is an intriguing physicochemical phenomenon in which existing fibrils catalyze the formation of their own copies. The molecular events behind this fibril surface-mediated process remain largely inaccessible to current structural and imaging techniques. Using statistical mechanics, computer modeling, and chemical kinetics, we show that the catalytic structure of the fibril surface can be inferred from the aggregation behavior in the presence and absence of a fibril-binding inhibitor. We apply our approach to the case of Alzheimer’s A\r\n amyloid fibrils formed in the presence of proSP-C Brichos inhibitors. We find that self-replication of A\r\n fibrils occurs on small catalytic sites on the fibril surface, which are far apart from each other, and each of which can be covered by a single Brichos inhibitor.","lang":"eng"}],"article_type":"original","publication":"Proceedings of the National Academy of Sciences of the United States of America","researchdata_availability":"yes","project":[{"call_identifier":"H2020","grant_number":"802960","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e"}],"publication_identifier":{"eissn":["1091-6490"]},"supplementarymaterial":"no","intvolume":"       121","file_date_updated":"2024-02-26T08:20:00Z","das_tickbox":"1","OA_place":"publisher","ddc":["570"],"date_published":"2024-02-13T00:00:00Z","date_updated":"2026-09-24T10:27:36Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","title":"Self-replication of Aβ42 aggregates occurs on small and isolated fibril sites","isi":1,"pmid":1,"issue":"7","day":"13","_id":"15001","language":[{"iso":"eng"}],"APC_amount":"5936,71 EUR","status":"public","department":[{"_id":"AnSa"}],"year":"2024","OA_type":"hybrid","citation":{"mla":"Curk, Samo, et al. “Self-Replication of Aβ42 Aggregates Occurs on Small and Isolated Fibril Sites.” <i>Proceedings of the National Academy of Sciences of the United States of America</i>, vol. 121, no. 7, e2220075121, National Academy of Sciences, 2024, doi:<a href=\"https://doi.org/10.1073/pnas.2220075121\">10.1073/pnas.2220075121</a>.","ama":"Curk S, Krausser J, Meisl G, et al. Self-replication of Aβ42 aggregates occurs on small and isolated fibril sites. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 2024;121(7). doi:<a href=\"https://doi.org/10.1073/pnas.2220075121\">10.1073/pnas.2220075121</a>","apa":"Curk, S., Krausser, J., Meisl, G., Frenkel, D., Linse, S., Michaels, T. C. T., … Šarić, A. (2024). Self-replication of Aβ42 aggregates occurs on small and isolated fibril sites. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. National Academy of Sciences. <a href=\"https://doi.org/10.1073/pnas.2220075121\">https://doi.org/10.1073/pnas.2220075121</a>","short":"S. Curk, J. Krausser, G. Meisl, D. Frenkel, S. Linse, T.C.T. Michaels, T.P.J. Knowles, A. Šarić, Proceedings of the National Academy of Sciences of the United States of America 121 (2024).","chicago":"Curk, Samo, Johannes Krausser, Georg Meisl, Daan Frenkel, Sara Linse, Thomas C.T. Michaels, Tuomas P.J. Knowles, and Anđela Šarić. “Self-Replication of Aβ42 Aggregates Occurs on Small and Isolated Fibril Sites.” <i>Proceedings of the National Academy of Sciences of the United States of America</i>. National Academy of Sciences, 2024. <a href=\"https://doi.org/10.1073/pnas.2220075121\">https://doi.org/10.1073/pnas.2220075121</a>.","ista":"Curk S, Krausser J, Meisl G, Frenkel D, Linse S, Michaels TCT, Knowles TPJ, Šarić A. 2024. Self-replication of Aβ42 aggregates occurs on small and isolated fibril sites. Proceedings of the National Academy of Sciences of the United States of America. 121(7), e2220075121.","ieee":"S. Curk <i>et al.</i>, “Self-replication of Aβ42 aggregates occurs on small and isolated fibril sites,” <i>Proceedings of the National Academy of Sciences of the United States of America</i>, vol. 121, no. 7. National Academy of Sciences, 2024."},"date_created":"2024-02-18T23:01:00Z","month":"02","external_id":{"isi":["001169063600007"],"pmid":["38335256"]},"author":[{"orcid":"0000-0001-6160-9766","full_name":"Curk, Samo","id":"031eff0d-d481-11ee-8508-cd12a7a86e5b","last_name":"Curk","first_name":"Samo"},{"full_name":"Krausser, Johannes","last_name":"Krausser","first_name":"Johannes"},{"full_name":"Meisl, Georg","first_name":"Georg","last_name":"Meisl"},{"first_name":"Daan","last_name":"Frenkel","full_name":"Frenkel, Daan"},{"full_name":"Linse, Sara","first_name":"Sara","last_name":"Linse"},{"full_name":"Michaels, Thomas C.T.","last_name":"Michaels","first_name":"Thomas C.T."},{"last_name":"Knowles","first_name":"Tuomas P.J.","full_name":"Knowles, Tuomas P.J."},{"id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","first_name":"Anđela","full_name":"Šarić, Anđela","orcid":"0000-0002-7854-2139"}],"oa":1,"has_accepted_license":"1"},{"status":"public","year":"2024","citation":{"ista":"Giubertoni G, Feng L, Klein K, Giannetti G, Rutten L, Choi Y, Van Der Net A, Castro-Linares G, Caporaletti F, Micha D, Hunger J, Deblais A, Bonn D, Sommerdijk N, Šarić A, Ilie IM, Koenderink GH, Woutersen S. 2024. Elucidating the role of water in collagen self-assembly by isotopically modulating collagen hydration. Proceedings of the National Academy of Sciences of the United States of America. 121(11), e2313162121.","chicago":"Giubertoni, Giulia, Liru Feng, Kevin Klein, Guido Giannetti, Luco Rutten, Yeji Choi, Anouk Van Der Net, et al. “Elucidating the Role of Water in Collagen Self-Assembly by Isotopically Modulating Collagen Hydration.” <i>Proceedings of the National Academy of Sciences of the United States of America</i>. National Academy of Sciences, 2024. <a href=\"https://doi.org/10.1073/pnas.2313162121\">https://doi.org/10.1073/pnas.2313162121</a>.","ieee":"G. Giubertoni <i>et al.</i>, “Elucidating the role of water in collagen self-assembly by isotopically modulating collagen hydration,” <i>Proceedings of the National Academy of Sciences of the United States of America</i>, vol. 121, no. 11. National Academy of Sciences, 2024.","mla":"Giubertoni, Giulia, et al. “Elucidating the Role of Water in Collagen Self-Assembly by Isotopically Modulating Collagen Hydration.” <i>Proceedings of the National Academy of Sciences of the United States of America</i>, vol. 121, no. 11, e2313162121, National Academy of Sciences, 2024, doi:<a href=\"https://doi.org/10.1073/pnas.2313162121\">10.1073/pnas.2313162121</a>.","ama":"Giubertoni G, Feng L, Klein K, et al. Elucidating the role of water in collagen self-assembly by isotopically modulating collagen hydration. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 2024;121(11). doi:<a href=\"https://doi.org/10.1073/pnas.2313162121\">10.1073/pnas.2313162121</a>","short":"G. Giubertoni, L. Feng, K. Klein, G. Giannetti, L. Rutten, Y. Choi, A. Van Der Net, G. Castro-Linares, F. Caporaletti, D. Micha, J. Hunger, A. Deblais, D. Bonn, N. Sommerdijk, A. Šarić, I.M. Ilie, G.H. Koenderink, S. Woutersen, Proceedings of the National Academy of Sciences of the United States of America 121 (2024).","apa":"Giubertoni, G., Feng, L., Klein, K., Giannetti, G., Rutten, L., Choi, Y., … Woutersen, S. (2024). Elucidating the role of water in collagen self-assembly by isotopically modulating collagen hydration. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. National Academy of Sciences. <a href=\"https://doi.org/10.1073/pnas.2313162121\">https://doi.org/10.1073/pnas.2313162121</a>"},"date_created":"2024-03-17T23:00:57Z","department":[{"_id":"AnSa"}],"external_id":{"pmid":["38451946"],"isi":["001206387400001"]},"month":"03","oa":1,"has_accepted_license":"1","author":[{"first_name":"Giulia","last_name":"Giubertoni","full_name":"Giubertoni, Giulia"},{"last_name":"Feng","first_name":"Liru","full_name":"Feng, Liru"},{"first_name":"Kevin","last_name":"Klein","full_name":"Klein, Kevin"},{"full_name":"Giannetti, Guido","last_name":"Giannetti","first_name":"Guido"},{"full_name":"Rutten, Luco","last_name":"Rutten","first_name":"Luco"},{"first_name":"Yeji","last_name":"Choi","full_name":"Choi, Yeji"},{"full_name":"Van Der Net, Anouk","first_name":"Anouk","last_name":"Van Der Net"},{"first_name":"Gerard","last_name":"Castro-Linares","full_name":"Castro-Linares, Gerard"},{"full_name":"Caporaletti, Federico","first_name":"Federico","last_name":"Caporaletti"},{"last_name":"Micha","first_name":"Dimitra","full_name":"Micha, Dimitra"},{"first_name":"Johannes","last_name":"Hunger","full_name":"Hunger, Johannes"},{"first_name":"Antoine","last_name":"Deblais","full_name":"Deblais, Antoine"},{"last_name":"Bonn","first_name":"Daniel","full_name":"Bonn, Daniel"},{"first_name":"Nico","last_name":"Sommerdijk","full_name":"Sommerdijk, Nico"},{"orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","first_name":"Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić"},{"last_name":"Ilie","first_name":"Ioana M.","full_name":"Ilie, Ioana M."},{"full_name":"Koenderink, Gijsje H.","last_name":"Koenderink","first_name":"Gijsje H."},{"last_name":"Woutersen","first_name":"Sander","full_name":"Woutersen, Sander"}],"das_tickbox":"1","supplementarymaterial":"no","intvolume":"       121","publication_identifier":{"eissn":["1091-6490"],"issn":["0027-8424"]},"file_date_updated":"2024-03-19T10:22:42Z","ddc":["550"],"date_updated":"2026-09-24T10:42:11Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","date_published":"2024-03-12T00:00:00Z","title":"Elucidating the role of water in collagen self-assembly by isotopically modulating collagen hydration","language":[{"iso":"eng"}],"_id":"15116","pmid":1,"isi":1,"issue":"11","day":"12","file":[{"relation":"main_file","checksum":"a3f7fdc29dd9f0a38952ab4e322b3a05","file_name":"2024_PNAS_Giubertoni.pdf","file_size":12952586,"creator":"dernst","file_id":"15125","success":1,"content_type":"application/pdf","access_level":"open_access","date_created":"2024-03-19T10:22:42Z","date_updated":"2024-03-19T10:22:42Z"}],"doi":"10.1073/pnas.2313162121","acknowledgement":"We thank Dr. Steven Roeters (Aarhus University), Dr. Federica Burla, and Prof. Dr. Mischa Bonn (Institute for Polymer Research, Mainz, Germany) for the useful discussions. We thank Dr. Wim Roeterdink and Michiel Hilberts for technical support. G.H.K. acknowledges financial support by the “BaSyC Building a Synthetic Cell” Gravitation grant (024.003.019) of The Netherlands Ministry of Education, Culture and Science (OCW) and The Netherlands Organization for Scientific Research and from NWO grant OCENW.GROOT.2019.022. This work has received support from the National Research Foundation of Korea (NRF), funded by the Ministry of Science and ICT, under Grant No. 2022K1A3A1A04062969. This publication is part of the project (with Project Number VI.Veni.212.240) of the research programme NWO Talent Programme Veni 2021, which is financed by the Dutch Research Council (NWO). I.M.I. acknowledges support from the Sectorplan Bèta & Techniek of the Dutch Government and the Dementia Research - Synapsis Foundation Switzerland. A.Š. and K.K. acknowledge support from Royal Society and European Research Council Starting Grant. G. Giubertoni kindly thanks to the Care4Bones community and the Collagen Café community for reminding that we do not own the knowledge we create, but it is, rather, a collective resource intended for the advancement of human progress.","related_material":{"record":[{"id":"15126","relation":"research_data","status":"public"}]},"quality_controlled":"1","article_processing_charge":"Yes (in subscription journal)","publication":"Proceedings of the National Academy of Sciences of the United States of America","researchdata_availability":"yes","abstract":[{"lang":"eng","text":"Water is known to play an important role in collagen self-assembly, but it is still largely unclear how water–collagen interactions influence the assembly process and determine the fibril network properties. Here, we use the H2O/D2O isotope effect on the hydrogen-bond strength in water to investigate the role of hydration in collagen self-assembly. We dissolve collagen in H2O and D2O and compare the growth kinetics and the structure of the collagen assemblies formed in these water isotopomers. Surprisingly, collagen assembly occurs ten times faster in D2O than in H2O, and collagen in D2O self-assembles into much thinner fibrils, that form a more inhomogeneous and softer network, with a fourfold reduction in elastic modulus when compared to H2O. Combining spectroscopic measurements with atomistic simulations, we show that collagen in D2O is less hydrated than in H2O. This partial dehydration lowers the enthalpic penalty for water removal and reorganization at the collagen–water interface, increasing the self-assembly rate and the number of nucleation centers, leading to thinner fibrils and a softer network. Coarse-grained simulations show that the acceleration in the initial nucleation rate can be reproduced by the enhancement of electrostatic interactions. These results show that water acts as a mediator between collagen monomers, by modulating their interactions so as to optimize the assembly process and, thus, the final network properties. We believe that isotopically modulating the hydration of proteins can be a valuable method to investigate the role of water in protein structural dynamics and protein self-assembly."}],"article_type":"original","publisher":"National Academy of Sciences","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"scopus_import":"1","dataavailabilitystatement":"Turbidity data; IR and 2D-IR data; TEM images; cryo-TEM images; CRM images; coarse grained simulations; molecular dynamics simulation data have been deposited in UvAauas.figshare 10.21942/uva.24829896","type":"journal_article","fulldoi":"https://doi.org/10.1073/pnas.2313162121","volume":121,"article_number":"e2313162121","oa_version":"Published Version","publication_status":"published"},{"status":"public","department":[{"_id":"AnSa"}],"OA_type":"hybrid","year":"2024","date_created":"2024-11-10T23:01:59Z","citation":{"apa":"Weiner, E., Berryman, E., Frey, F. F., Solís, A. G., Leier, A., Lago, T. M., … Otegui, M. S. (2024). Endosomal membrane budding patterns in plants. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. National Academy of Sciences. <a href=\"https://doi.org/10.1073/pnas.2409407121\">https://doi.org/10.1073/pnas.2409407121</a>","short":"E. Weiner, E. Berryman, F.F. Frey, A.G. Solís, A. Leier, T.M. Lago, A. Šarić, M.S. Otegui, Proceedings of the National Academy of Sciences of the United States of America 121 (2024).","ama":"Weiner E, Berryman E, Frey FF, et al. Endosomal membrane budding patterns in plants. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 2024;121(44). doi:<a href=\"https://doi.org/10.1073/pnas.2409407121\">10.1073/pnas.2409407121</a>","mla":"Weiner, Ethan, et al. “Endosomal Membrane Budding Patterns in Plants.” <i>Proceedings of the National Academy of Sciences of the United States of America</i>, vol. 121, no. 44, e2409407121, National Academy of Sciences, 2024, doi:<a href=\"https://doi.org/10.1073/pnas.2409407121\">10.1073/pnas.2409407121</a>.","ieee":"E. Weiner <i>et al.</i>, “Endosomal membrane budding patterns in plants,” <i>Proceedings of the National Academy of Sciences of the United States of America</i>, vol. 121, no. 44. National Academy of Sciences, 2024.","chicago":"Weiner, Ethan, Elizabeth Berryman, Felix F Frey, Ariadna González Solís, André Leier, Tatiana Marquez Lago, Anđela Šarić, and Marisa S. Otegui. “Endosomal Membrane Budding Patterns in Plants.” <i>Proceedings of the National Academy of Sciences of the United States of America</i>. National Academy of Sciences, 2024. <a href=\"https://doi.org/10.1073/pnas.2409407121\">https://doi.org/10.1073/pnas.2409407121</a>.","ista":"Weiner E, Berryman E, Frey FF, Solís AG, Leier A, Lago TM, Šarić A, Otegui MS. 2024. Endosomal membrane budding patterns in plants. Proceedings of the National Academy of Sciences of the United States of America. 121(44), e2409407121."},"month":"10","external_id":{"isi":["001349500800007"],"pmid":["39441629"]},"author":[{"full_name":"Weiner, Ethan","last_name":"Weiner","first_name":"Ethan"},{"last_name":"Berryman","first_name":"Elizabeth","full_name":"Berryman, Elizabeth"},{"orcid":"0000-0001-8501-6017","full_name":"Frey, Felix F","id":"a0270b37-8f1a-11ec-95c7-8e710c59a4f3","last_name":"Frey","first_name":"Felix F"},{"first_name":"Ariadna González","last_name":"Solís","full_name":"Solís, Ariadna González"},{"first_name":"André","last_name":"Leier","full_name":"Leier, André"},{"full_name":"Lago, Tatiana Marquez","last_name":"Lago","first_name":"Tatiana Marquez"},{"last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","first_name":"Anđela","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela"},{"last_name":"Otegui","first_name":"Marisa S.","full_name":"Otegui, Marisa S."}],"has_accepted_license":"1","oa":1,"supplementarymaterial":"yes","publication_identifier":{"issn":["0027-8424"],"eissn":["1091-6490"]},"intvolume":"       121","file_date_updated":"2024-11-11T09:35:15Z","das_tickbox":"1","OA_place":"publisher","date_updated":"2026-09-24T10:41:24Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","date_published":"2024-10-29T00:00:00Z","ddc":["570"],"title":"Endosomal membrane budding patterns in plants","issue":"44","pmid":1,"isi":1,"day":"29","_id":"18526","language":[{"iso":"eng"}],"file":[{"creator":"dernst","file_name":"2024_PNAS_Weiner.pdf","checksum":"21c82d2ab58ff99b2bd0489797be42e5","file_size":5268074,"file_id":"18538","success":1,"relation":"main_file","date_updated":"2024-11-11T09:35:15Z","date_created":"2024-11-11T09:35:15Z","content_type":"application/pdf","access_level":"open_access"}],"acknowledgement":"We would like to thank Janice Pennington for her support with electron tomography data collection, Dr. Ingrid Jordon-Thaden, director of the Botany Garden and Greenhouse of University of Wisconsin Madison, for her invaluable assistance collecting plant materials, Dr. Marie Trest for providing Chara specimens, and Dr. Nicholas Keuler for his advice on statistical analyses. We thank Charlie Hamilton for exploring the initial computational model. This work was supported by grant NSF MCB 2114603 and NIH 1S10OD026769-01 to M.S.O. F.F acknowledges support as a NOMIS Fellow from the NOMIS Foundation. A.Š. acknowledges ERC Starting Grant “NEPA” 802960.","doi":"10.1073/pnas.2409407121","article_processing_charge":"Yes (in subscription journal)","quality_controlled":"1","article_type":"original","abstract":[{"lang":"eng","text":"Multivesicular endosomes (MVEs) sequester membrane proteins destined for degradation within intralumenal vesicles (ILVs), a process mediated by the membrane-remodeling action of Endosomal Sorting Complex Required for Transport (ESCRT) proteins. In Arabidopsis, endosomal membrane constriction and scission are uncoupled, resulting in the formation of extensive concatenated ILV networks and enhancing cargo sequestration efficiency. Here, we used a combination of electron tomography, computer simulations, and mathematical modeling to address the questions of when concatenated ILV networks evolved in plants and what drives their formation. Through morphometric analyses of tomographic reconstructions of endosomes across yeast, algae, and various land plants, we have found that ILV concatenation is widespread within plant species, but only prevalent in seed plants, especially in flowering plants. Multiple budding sites that require the formation of pores in the limiting membrane were only identified in hornworts and seed plants, suggesting that this mechanism has evolved independently in both plant lineages. To identify the conditions under which these multiple budding sites can arise, we used particle-based molecular dynamics simulations and found that changes in ESCRT filament properties, such as filament curvature and membrane binding energy, can generate the membrane shapes observed in multiple budding sites. To understand the relationship between membrane budding activity and ILV network topology, we performed computational simulations and identified a set of membrane remodeling parameters that can recapitulate our tomographic datasets."}],"project":[{"grant_number":"802960","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","call_identifier":"H2020"}],"publication":"Proceedings of the National Academy of Sciences of the United States of America","researchdata_availability":"yes","scopus_import":"1","publisher":"National Academy of Sciences","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","short":"CC BY-NC-ND (4.0)","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","image":"/images/cc_by_nc_nd.png"},"type":"journal_article","fulldoi":"https://doi.org/10.1073/pnas.2409407121","ec_funded":1,"dataavailabilitystatement":"Electron tomogram files are deposited in EMPIAR under EMPIAR-12299 (54). All other data are included in the manuscript and/or supporting information","volume":121,"article_number":"e2409407121","oa_version":"Published Version","publication_status":"published"},{"publisher":"Cell Press","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"scopus_import":"1","dataavailabilitystatement":"Raw image files of all figures have been deposited at Mendeley Data and are publicly available as of the date of publication (Mendeley data: https://doi.org/10.17632/dwcpnncsyd.1). All other data reported in this paper will be shared by the lead contact upon request","type":"journal_article","ec_funded":1,"fulldoi":"https://doi.org/10.1016/j.molcel.2024.07.022","volume":84,"page":"P3254-3270.E9","oa_version":"Published Version","publication_status":"published","file":[{"content_type":"application/pdf","access_level":"open_access","date_created":"2024-09-16T07:38:38Z","date_updated":"2024-09-16T07:38:38Z","relation":"main_file","checksum":"3f360e0287b8ec79fb2b8b02b5070360","file_name":"2024_MolecularCell_HernandezArmendariz.pdf","file_size":11654644,"creator":"dernst","file_id":"18075","success":1}],"doi":"10.1016/j.molcel.2024.07.022","acknowledgement":"We thank Daniel W. Gerlich for providing cell lines, the EMBL Advanced Light Microscopy Facility (ALMF) for support, Christian H. Haering and Thomas Quail for input on the manuscript, and Martina Dees for cloning several Ki-67 constructs. This work was supported by the German Research Foundation (DFG project number 402723784) and the Human Frontier Science Program (CDA00045/2019). A.H.-A. and A.B. have received PhD fellowships from the Boehringer Ingelheim Fonds, V.S. and A.Š. were supported by the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme (grant no. 802960), and Y.H. was supported by a fellowship from the EMBL interdisciplinary Postdoc (EIPOD) program (Marie Sklodowska-Curie Actions, COFUND grant agreement 664726).","related_material":{"record":[{"relation":"research_data","status":"public","id":"22987"}]},"quality_controlled":"1","article_processing_charge":"Yes (in subscription journal)","researchdata_availability":"yes","publication":"Molecular Cell","project":[{"_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","grant_number":"802960","call_identifier":"H2020"}],"article_type":"original","abstract":[{"lang":"eng","text":"The individualization of chromosomes during early mitosis and their clustering upon exit from cell division are two key transitions that ensure efficient segregation of eukaryotic chromosomes. Both processes are regulated by the surfactant-like protein Ki-67, but how Ki-67 achieves these diametric functions has remained unknown. Here, we report that Ki-67 radically switches from a chromosome repellent to a chromosome attractant during anaphase in human cells. We show that Ki-67 dephosphorylation during mitotic exit and the simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface. Experiments and coarse-grained simulations support a model in which the coalescence of chromosome surfaces, driven by co-condensation of Ki-67 and RNA, promotes clustering of chromosomes. Our study reveals how the switch of Ki-67 from a surfactant to a liquid-like condensed phase can generate mechanical forces during genome segregation that are required for re-establishing nuclear-cytoplasmic compartmentalization after mitosis."}],"das_tickbox":"1","publication_identifier":{"eissn":["1097-4164"],"issn":["1097-2765"]},"supplementarymaterial":"yes","intvolume":"        84","file_date_updated":"2024-09-16T07:38:38Z","date_updated":"2026-09-24T10:43:18Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","ddc":["570"],"date_published":"2024-09-05T00:00:00Z","title":"A liquid-like coat mediates chromosome clustering during mitotic exit","language":[{"iso":"eng"}],"_id":"18072","pmid":1,"issue":"17","isi":1,"day":"05","status":"public","year":"2024","citation":{"ista":"Hernandez-Armendariz A, Sorichetti V, Hayashi Y, Koskova Z, Brunner A, Ellenberg J, Šarić A, Cuylen-Haering S. 2024. A liquid-like coat mediates chromosome clustering during mitotic exit. Molecular Cell. 84(17), P3254–3270.E9.","chicago":"Hernandez-Armendariz, Alberto, Valerio Sorichetti, Yuki Hayashi, Zuzana Koskova, Andreas Brunner, Jan Ellenberg, Anđela Šarić, and Sara Cuylen-Haering. “A Liquid-like Coat Mediates Chromosome Clustering during Mitotic Exit.” <i>Molecular Cell</i>. Cell Press, 2024. <a href=\"https://doi.org/10.1016/j.molcel.2024.07.022\">https://doi.org/10.1016/j.molcel.2024.07.022</a>.","ieee":"A. Hernandez-Armendariz <i>et al.</i>, “A liquid-like coat mediates chromosome clustering during mitotic exit,” <i>Molecular Cell</i>, vol. 84, no. 17. Cell Press, p. P3254–3270.E9, 2024.","mla":"Hernandez-Armendariz, Alberto, et al. “A Liquid-like Coat Mediates Chromosome Clustering during Mitotic Exit.” <i>Molecular Cell</i>, vol. 84, no. 17, Cell Press, 2024, p. P3254–3270.E9, doi:<a href=\"https://doi.org/10.1016/j.molcel.2024.07.022\">10.1016/j.molcel.2024.07.022</a>.","ama":"Hernandez-Armendariz A, Sorichetti V, Hayashi Y, et al. A liquid-like coat mediates chromosome clustering during mitotic exit. <i>Molecular Cell</i>. 2024;84(17):P3254-3270.E9. doi:<a href=\"https://doi.org/10.1016/j.molcel.2024.07.022\">10.1016/j.molcel.2024.07.022</a>","short":"A. Hernandez-Armendariz, V. Sorichetti, Y. Hayashi, Z. Koskova, A. Brunner, J. Ellenberg, A. Šarić, S. Cuylen-Haering, Molecular Cell 84 (2024) P3254–3270.E9.","apa":"Hernandez-Armendariz, A., Sorichetti, V., Hayashi, Y., Koskova, Z., Brunner, A., Ellenberg, J., … Cuylen-Haering, S. (2024). A liquid-like coat mediates chromosome clustering during mitotic exit. <i>Molecular Cell</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.molcel.2024.07.022\">https://doi.org/10.1016/j.molcel.2024.07.022</a>"},"date_created":"2024-09-15T22:01:41Z","department":[{"_id":"AnSa"}],"external_id":{"pmid":["39153474"],"isi":["001309051100001"]},"month":"09","has_accepted_license":"1","oa":1,"author":[{"first_name":"Alberto","last_name":"Hernandez-Armendariz","full_name":"Hernandez-Armendariz, Alberto"},{"orcid":"0000-0002-9645-6576","full_name":"Sorichetti, Valerio","first_name":"Valerio","last_name":"Sorichetti","id":"ef8a92cb-c7b6-11ec-8bea-e1fd5847bc5b"},{"first_name":"Yuki","last_name":"Hayashi","full_name":"Hayashi, Yuki"},{"last_name":"Koskova","first_name":"Zuzana","full_name":"Koskova, Zuzana"},{"last_name":"Brunner","first_name":"Andreas","full_name":"Brunner, Andreas"},{"first_name":"Jan","last_name":"Ellenberg","full_name":"Ellenberg, Jan"},{"orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","first_name":"Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić"},{"full_name":"Cuylen-Haering, Sara","first_name":"Sara","last_name":"Cuylen-Haering"}]},{"article_processing_charge":"Yes (in subscription journal)","quality_controlled":"1","abstract":[{"lang":"eng","text":"Collagen is the most abundant protein in tissue scaffolds in live organisms. Collagen can self-assemble in vitro, which has led to a number of biotechnological and biomedical applications. To understand the dominant factors that participate in the formation of collagen nanostructures, here we study in real time and with nanoscale resolution the disassembly and reassembly of collagens. We implement a high-speed force microscope, which provides in situ high spatiotemporal resolution images of collagen nanostructures under changing pH conditions. The disassembly and reassembly are dominated by the electrostatic interactions among amino-acid residues of different molecules. Acidic conditions favor disassembly by neutralizing negatively charged residues. The process sets a net repulsive force between collagen molecules. A neutral pH favors the presence of negative and positively charged residues along the collagen molecules, which promotes their electrostatic attraction. Molecular dynamics simulations reproduce the experimental behavior and validate the electrostatic-based model of the disassembly and reassembly processes."}],"article_type":"original","project":[{"_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","grant_number":"802960","call_identifier":"H2020"}],"researchdata_availability":"no","publication":"ACS Nano","file":[{"relation":"main_file","file_id":"18808","success":1,"file_size":10036838,"file_name":"2024_ACSNano_GarciaSacristan.pdf","creator":"dernst","checksum":"b7e9ce718e92f568bcb3810e8e28e458","access_level":"open_access","content_type":"application/pdf","date_created":"2025-01-09T12:06:48Z","date_updated":"2025-01-09T12:06:48Z"}],"acknowledgement":"We are grateful to Nancy Forde (Simon Fraser University) for her motivating comments. Financial support from the Ministerio de Ciencia, Innovación y Universidades (PID2019-106801GB-I00 and PID2022-136851NB-I00) is acknowledged. A.Š. and K.K. acknowledge support from the Royal Society University Research Fellowship and ERC the European Union’s Horizon 2020584 Research and Innovation Programme (Grant No. 585 80296).","doi":"10.1021/acsnano.4c03839","volume":18,"page":"18485-18492","oa_version":"Published Version","publication_status":"published","scopus_import":"1","publisher":"American Chemical Society","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"type":"journal_article","ec_funded":1,"fulldoi":"https://doi.org/10.1021/acsnano.4c03839","month":"07","external_id":{"isi":["001263155500001"],"pmid":["38958189"]},"author":[{"full_name":"Garcia-Sacristan, Clara","first_name":"Clara","last_name":"Garcia-Sacristan"},{"full_name":"Gisbert, Victor G.","first_name":"Victor G.","last_name":"Gisbert"},{"last_name":"Klein","id":"1e7ede04-9e54-11f0-9ec4-8d4d5563c398","first_name":"Kevin","full_name":"Klein, Kevin"},{"first_name":"Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela"},{"full_name":"Garcia, Ricardo","last_name":"Garcia","first_name":"Ricardo"}],"oa":1,"has_accepted_license":"1","status":"public","department":[{"_id":"AnSa"}],"OA_type":"hybrid","year":"2024","date_created":"2024-07-14T22:01:12Z","citation":{"apa":"Garcia-Sacristan, C., Gisbert, V. G., Klein, K., Šarić, A., &#38; Garcia, R. (2024). In operando imaging electrostatic-driven disassembly and reassembly of collagen nanostructures. <i>ACS Nano</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acsnano.4c03839\">https://doi.org/10.1021/acsnano.4c03839</a>","short":"C. Garcia-Sacristan, V.G. Gisbert, K. Klein, A. Šarić, R. Garcia, ACS Nano 18 (2024) 18485–18492.","ama":"Garcia-Sacristan C, Gisbert VG, Klein K, Šarić A, Garcia R. In operando imaging electrostatic-driven disassembly and reassembly of collagen nanostructures. <i>ACS Nano</i>. 2024;18(28):18485-18492. doi:<a href=\"https://doi.org/10.1021/acsnano.4c03839\">10.1021/acsnano.4c03839</a>","mla":"Garcia-Sacristan, Clara, et al. “In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures.” <i>ACS Nano</i>, vol. 18, no. 28, American Chemical Society, 2024, pp. 18485–92, doi:<a href=\"https://doi.org/10.1021/acsnano.4c03839\">10.1021/acsnano.4c03839</a>.","ieee":"C. Garcia-Sacristan, V. G. Gisbert, K. Klein, A. Šarić, and R. Garcia, “In operando imaging electrostatic-driven disassembly and reassembly of collagen nanostructures,” <i>ACS Nano</i>, vol. 18, no. 28. American Chemical Society, pp. 18485–18492, 2024.","ista":"Garcia-Sacristan C, Gisbert VG, Klein K, Šarić A, Garcia R. 2024. In operando imaging electrostatic-driven disassembly and reassembly of collagen nanostructures. ACS Nano. 18(28), 18485–18492.","chicago":"Garcia-Sacristan, Clara, Victor G. Gisbert, Kevin Klein, Anđela Šarić, and Ricardo Garcia. “In Operando Imaging Electrostatic-Driven Disassembly and Reassembly of Collagen Nanostructures.” <i>ACS Nano</i>. American Chemical Society, 2024. <a href=\"https://doi.org/10.1021/acsnano.4c03839\">https://doi.org/10.1021/acsnano.4c03839</a>."},"title":"In operando imaging electrostatic-driven disassembly and reassembly of collagen nanostructures","isi":1,"issue":"28","pmid":1,"day":"16","language":[{"iso":"eng"}],"_id":"17239","publication_identifier":{"issn":["1936-0851"],"eissn":["1936-086X"]},"supplementarymaterial":"yes","intvolume":"        18","file_date_updated":"2025-01-09T12:06:48Z","das_tickbox":"0","OA_place":"publisher","ddc":["540"],"date_updated":"2026-09-24T10:43:56Z","date_published":"2024-07-16T00:00:00Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345"},{"doi":"10.1038/s41567-024-02597-8","acknowledgement":"We thank I. Palaia (ISTA) for useful discussions and K. Lim and R. W. Wong (WPI-Nano Life Science Institute, Kanazawa University) for providing access to HS-AFM. We would like to thank B. Prats Mateu (MSD Austria, Vienna) for providing the HS-AFM data. This work was supported by the Royal Society (grant no. UF160266; C.V.-C. and A.Š.), the European Union’s Horizon 2020 Research and Innovation Programme (grant no. 802960; A.Š.), the Austrian Science Fund (FWF) Stand-Alone P34607 (M.L.) and a Wellcome Trust and Royal Society Sir Henry Dale Fellowship (grant no. 206670/Z/17/Z; S.H. and K.D.W.).","related_material":{"record":[{"status":"public","relation":"research_data","id":"22988"}]},"file":[{"relation":"main_file","file_size":8058249,"creator":"dernst","file_name":"2024_NaturePhysics_VanhilleCampos.pdf","checksum":"c4842152e2b90d67f48ea8c9ed7c473b","file_id":"19556","success":1,"content_type":"application/pdf","access_level":"open_access","date_updated":"2025-04-14T06:06:35Z","date_created":"2025-04-14T06:06:35Z"}],"researchdata_availability":"yes","publication":"Nature Physics","project":[{"name":"In vitro reconstitution of bacterial cell division","grant_number":"P34607","_id":"fc38323b-9c52-11eb-aca3-ff8afb4a011d"},{"name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","grant_number":"802960","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","call_identifier":"H2020"}],"article_type":"original","abstract":[{"lang":"eng","text":"Filaments in the cell commonly treadmill. Driven by energy consumption, they grow on one end while shrinking on the other, causing filaments to appear motile even though individual proteins remain static. This process is characteristic of cytoskeletal filaments and leads to collective filament self-organization. Here we show that treadmilling drives filament nematic ordering by dissolving misaligned filaments. Taking the bacterial FtsZ protein involved in cell division as an example, we show that this mechanism aligns FtsZ filaments in vitro and drives the organization of the division ring in living Bacillus subtilis cells. We find that ordering via local dissolution also allows the system to quickly respond to chemical and geometrical biases in the cell, enabling us to quantitatively explain the ring formation dynamics in vivo. Beyond FtsZ and other cytoskeletal filaments, our study identifies a mechanism for self-organization via constant birth and death of energy-consuming filaments."}],"quality_controlled":"1","article_processing_charge":"Yes (in subscription journal)","dataavailabilitystatement":"The simulation data presented in this work are available from the University College London public data repository at https://doi.org/10.5522/04/24754527 (ref. 74). Live-cell imaging of FtsZ rings data presented in this work are from ref. 23. High-speed atomic force microscopy data presented in this work are from ref. 9. Total internal reflection fluorescence microscopy data presented in this work are from refs. 37,75,76","type":"journal_article","ec_funded":1,"fulldoi":"https://doi.org/10.1038/s41567-024-02597-8","publisher":"Springer Nature","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"scopus_import":"1","corr_author":"1","oa_version":"Published Version","publication_status":"published","volume":20,"page":"1670-1678","OA_type":"hybrid","year":"2024","citation":{"mla":"Vanhille-Campos, Christian Eduardo, et al. “Self-Organization of Mortal Filaments and Its Role in Bacterial Division Ring Formation.” <i>Nature Physics</i>, vol. 20, Springer Nature, 2024, pp. 1670–78, doi:<a href=\"https://doi.org/10.1038/s41567-024-02597-8\">10.1038/s41567-024-02597-8</a>.","ama":"Vanhille-Campos CE, Whitley KD, Radler P, Loose M, Holden S, Šarić A. Self-organization of mortal filaments and its role in bacterial division ring formation. <i>Nature Physics</i>. 2024;20:1670-1678. doi:<a href=\"https://doi.org/10.1038/s41567-024-02597-8\">10.1038/s41567-024-02597-8</a>","apa":"Vanhille-Campos, C. E., Whitley, K. D., Radler, P., Loose, M., Holden, S., &#38; Šarić, A. (2024). Self-organization of mortal filaments and its role in bacterial division ring formation. <i>Nature Physics</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41567-024-02597-8\">https://doi.org/10.1038/s41567-024-02597-8</a>","short":"C.E. Vanhille-Campos, K.D. Whitley, P. Radler, M. Loose, S. Holden, A. Šarić, Nature Physics 20 (2024) 1670–1678.","chicago":"Vanhille-Campos, Christian Eduardo, Kevin D. Whitley, Philipp Radler, Martin Loose, Séamus Holden, and Anđela Šarić. “Self-Organization of Mortal Filaments and Its Role in Bacterial Division Ring Formation.” <i>Nature Physics</i>. Springer Nature, 2024. <a href=\"https://doi.org/10.1038/s41567-024-02597-8\">https://doi.org/10.1038/s41567-024-02597-8</a>.","ista":"Vanhille-Campos CE, Whitley KD, Radler P, Loose M, Holden S, Šarić A. 2024. Self-organization of mortal filaments and its role in bacterial division ring formation. Nature Physics. 20, 1670–1678.","ieee":"C. E. Vanhille-Campos, K. D. Whitley, P. Radler, M. Loose, S. Holden, and A. Šarić, “Self-organization of mortal filaments and its role in bacterial division ring formation,” <i>Nature Physics</i>, vol. 20. Springer Nature, pp. 1670–1678, 2024."},"date_created":"2024-08-25T22:01:08Z","department":[{"_id":"AnSa"},{"_id":"MaLo"}],"status":"public","APC_amount":"12348 EUR","has_accepted_license":"1","oa":1,"author":[{"full_name":"Vanhille-Campos, Christian Eduardo","first_name":"Christian Eduardo","id":"3adeca52-9313-11ed-b1ac-c170b2505714","last_name":"Vanhille-Campos"},{"full_name":"Whitley, Kevin D.","last_name":"Whitley","first_name":"Kevin D."},{"first_name":"Philipp","id":"40136C2A-F248-11E8-B48F-1D18A9856A87","last_name":"Radler","orcid":"0000-0001-9198-2182 ","full_name":"Radler, Philipp"},{"full_name":"Loose, Martin","orcid":"0000-0001-7309-9724","first_name":"Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87","last_name":"Loose"},{"full_name":"Holden, Séamus","first_name":"Séamus","last_name":"Holden"},{"orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","first_name":"Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić"}],"external_id":{"pmid":["39416851"],"isi":["001289394500005"]},"month":"10","date_published":"2024-10-01T00:00:00Z","ddc":["570"],"date_updated":"2026-09-24T10:58:39Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","das_tickbox":"1","OA_place":"publisher","popular_science":"1","intvolume":"        20","publication_identifier":{"eissn":["1745-2481"],"issn":["1745-2473"]},"supplementarymaterial":"yes","file_date_updated":"2025-04-14T06:06:35Z","language":[{"iso":"eng"}],"_id":"17460","pmid":1,"isi":1,"day":"01","title":"Self-organization of mortal filaments and its role in bacterial division ring formation"},{"abstract":[{"text":"Across the tree of life, distinct designs of cellular membranes have evolved. In bacteria and eukaryotes single-headed lipids self-assemble into flexible bilayer membranes. By contrast, archaea often possess double-headed, monolayer spanning bolalipids, mixed with bilayer lipids, enabling them to survive in harsh environments. Here, using a minimal computational model for bolalipid membranes, we discover trade-offs when forming membranes. We find that membranes made out of flexible bolalipids resemble bilayer membranes as bolalipids exhibit conformational switch into U-shaped conformations to enable higher curvatures. Conversely, stiffer bolalipids, resembling those in extremophile archaea, take on straight conformations and form liquid membranes that are stiff, and prone to pore formation during membrane reshaping. Strikingly, we show how to achieve fluid bolalipid membranes that are both stable and flexible – by including small amounts of bilayer lipids, as archaea do. Our study explains how different organisms resolve trade-offs when generating membranes of desired material properties.","lang":"eng"}],"publication":"bioRxiv","project":[{"grant_number":"802960","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","call_identifier":"H2020"}],"article_processing_charge":"No","related_material":{"record":[{"id":"18661","relation":"dissertation_contains","status":"public"}]},"acknowledgement":"MA, BB, and AŠ acknowledge funding by the\r\nVolkswagen Foundation Grant Az 96727. FF\r\nacknowledges fnancial support by the NOMIS\r\nfoundation. AŠ acknowledges funding by ERC\r\nStarting Grant “NEPA” 802960. We thank\r\nClaudia Flandoli for help with illustrations.","doi":"10.1101/2024.10.18.619072","oa_version":"Preprint","publication_status":"draft","corr_author":"1","type":"preprint","fulldoi":"https://doi.org/10.1101/2024.10.18.619072","ec_funded":1,"main_file_link":[{"url":"https://doi.org/10.1101/2024.10.18.619072","open_access":"1"}],"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"},"author":[{"id":"4f2d02dd-47a9-11ec-ad10-82820ed3f501","last_name":"Santana de Freitas Amaral","first_name":"Miguel","full_name":"Santana de Freitas Amaral, Miguel"},{"first_name":"Felix F","last_name":"Frey","id":"a0270b37-8f1a-11ec-95c7-8e710c59a4f3","full_name":"Frey, Felix F","orcid":"0000-0001-8501-6017"},{"last_name":"Jiang","first_name":"Xiuyun","full_name":"Jiang, Xiuyun"},{"first_name":"Buzz","last_name":"Baum","full_name":"Baum, Buzz"},{"first_name":"Anđela","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","last_name":"Šarić","full_name":"Šarić, Anđela","orcid":"0000-0002-7854-2139"}],"oa":1,"month":"11","department":[{"_id":"AnSa"}],"year":"2024","citation":{"ieee":"M. Santana de Freitas Amaral, F. F. Frey, X. Jiang, B. Baum, and A. Šarić, “Stability vs flexibility: Reshaping archaeal membranes in silico,” <i>bioRxiv</i>. .","ista":"Santana de Freitas Amaral M, Frey FF, Jiang X, Baum B, Šarić A. Stability vs flexibility: Reshaping archaeal membranes in silico. bioRxiv, <a href=\"https://doi.org/10.1101/2024.10.18.619072\">10.1101/2024.10.18.619072</a>.","chicago":"Santana de Freitas Amaral, Miguel, Felix F Frey, Xiuyun Jiang, Buzz Baum, and Anđela Šarić. “Stability vs Flexibility: Reshaping Archaeal Membranes in Silico.” <i>BioRxiv</i>, n.d. <a href=\"https://doi.org/10.1101/2024.10.18.619072\">https://doi.org/10.1101/2024.10.18.619072</a>.","mla":"Santana de Freitas Amaral, Miguel, et al. “Stability vs Flexibility: Reshaping Archaeal Membranes in Silico.” <i>BioRxiv</i>, doi:<a href=\"https://doi.org/10.1101/2024.10.18.619072\">10.1101/2024.10.18.619072</a>.","short":"M. Santana de Freitas Amaral, F.F. Frey, X. Jiang, B. Baum, A. Šarić, BioRxiv (n.d.).","apa":"Santana de Freitas Amaral, M., Frey, F. F., Jiang, X., Baum, B., &#38; Šarić, A. (n.d.). Stability vs flexibility: Reshaping archaeal membranes in silico. <i>bioRxiv</i>. <a href=\"https://doi.org/10.1101/2024.10.18.619072\">https://doi.org/10.1101/2024.10.18.619072</a>","ama":"Santana de Freitas Amaral M, Frey FF, Jiang X, Baum B, Šarić A. Stability vs flexibility: Reshaping archaeal membranes in silico. <i>bioRxiv</i>. doi:<a href=\"https://doi.org/10.1101/2024.10.18.619072\">10.1101/2024.10.18.619072</a>"},"date_created":"2024-12-18T10:07:45Z","status":"public","day":"27","language":[{"iso":"eng"}],"_id":"18670","title":"Stability vs flexibility: Reshaping archaeal membranes in silico","date_published":"2024-11-27T00:00:00Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","date_updated":"2026-10-25T23:31:16Z","OA_place":"repository"},{"oa_version":"Published Version","publication_status":"published","volume":19,"page":"1695-1704","type":"journal_article","ec_funded":1,"fulldoi":"https://doi.org/10.1039/d2sm01562e","scopus_import":"1","publisher":"Royal Society of Chemistry","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"abstract":[{"lang":"eng","text":"Self-organisation is the spontaneous emergence of spatio-temporal structures and patterns from the interaction of smaller individual units. Examples are found across many scales in very different systems and scientific disciplines, from physics, materials science and robotics to biology, geophysics and astronomy. Recent research has highlighted how self-organisation can be both mediated and controlled by confinement. Confinement is an action over a system that limits its units’ translational and rotational degrees of freedom, thus also influencing the system's phase space probability density; it can function as either a catalyst or inhibitor of self-organisation. Confinement can then become a means to actively steer the emergence or suppression of collective phenomena in space and time. Here, to provide a common framework and perspective for future research, we examine the role of confinement in the self-organisation of soft-matter systems and identify overarching scientific challenges that need to be addressed to harness its full scientific and technological potential in soft matter and related fields. By drawing analogies with other disciplines, this framework will accelerate a common deeper understanding of self-organisation and trigger the development of innovative strategies to steer it using confinement, with impact on, e.g., the design of smarter materials, tissue engineering for biomedicine and in guiding active matter."}],"article_type":"original","publication":"Soft Matter","project":[{"call_identifier":"H2020","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","grant_number":"802960","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines"}],"article_processing_charge":"No","quality_controlled":"1","acknowledgement":"All authors are grateful to the Lorentz Center for providing a venue for stimulating scientific discussions and to sponsor a workshop on the topic of “Self-organisation under confinement” along with the 4TU Federation, the J. M. Burgers Center for Fluid Dynamics and the MESA+ Institute for Nanotechnology at the University of Twente. The authors are also grateful to Paolo Malgaretti, Federico Toschi, Twan Wilting and Jaap den Toonder for valuable feedback. N. A. acknowledges financial support from the Portuguese Foundation for Science and Technology (FCT) under Contracts no. PTDC/FIS-MAC/28146/2017 (LISBOA-01-0145-FEDER-028146), UIDB/00618/2020, and UIDP/00618/2020. L. M. C. J. acknowledges financial support from the Netherlands Organisation for Scientific Research (NWO) through a START-UP, Physics Projectruimte, and Vidi grant. I. C. was supported in part by a grant from by the Army Research Office (ARO W911NF-18-1-0032) and the Cornell Center for Materials Research (DMR-1719875). O. D. acknowledges funding by the Agence Nationale pour la Recherche under Grant No ANR-18-CE33-0006 MSR. M. D. acknowledges financial support from the European Research Council (Grant No. ERC-2019-ADV-H2020 884902 SoftML). W. M. D. acknowledges funding from a BBSRC New Investigator Grant (BB/R018383/1). S. G. was supported by DARPA Young Faculty Award # D19AP00046, and NSF IIS grant # 1955210. H. G. acknowledges financial support from the Netherlands Organisation for Scientific Research (NWO) through Veni Grant No. 680-47-451. R. G. acknowledges support from the Max Planck School Matter to Life and the MaxSynBio Consortium, which are jointly funded by the Federal Ministry of Education and Research (BMBF) of Germany, and the Max Planck Society. L. I. acknowledges funding from the Horizon Europe ERC Consolidator Grant ACTIVE_ ADAPTIVE (Grant No. 101001514). G. H. K. gratefully acknowledges the NWO Talent Programme which is financed by the Dutch Research Council (project number VI.C.182.004). H. L. and N. V. acknowledge funding from the Deutsche Forschungsgemeinschaft (DFG) under grant numbers VO 1824/8-1 and LO 418/22-1. R. M. acknowledges funding from the Deutsche Forschungsgemeinschaft (DFG) under grant number ME 1535/13-1 and ME 1535/16-1. M. P. acknowledges funding from the Ramón y Cajal Program, grant no. RYC-2018-02534, and the Leverhulme Trust, grant no. RPG-2018-345. A. Š. acknowledges financial support from the European Research Council (Grant No. ERC-2018-STG-H2020 802960 NEPA). A. S. acknowledges funding from an ATTRACT Investigator Grant (No. A17/MS/11572821/MBRACE) from the Luxembourg National Research Fund. C. S. acknowledges funding from the French Agence Nationale pour la Recherche (ANR), grant ANR-14-CE090006 and ANR-12-BSV5001401, by the Fondation pour la Recherche Médicale (FRM), grant DEQ20120323737, and from the PIC3I of Institut Curie, France. I. T. acknowledges funding from grant IED2019-00058I/AEI/10.13039/501100011033. M. P. and I. T. also acknowledge funding from grant PID2019-104232B-I00/AEI/10.13039/501100011033 and from the H2020 MSCA ITN PHYMOT (Grant agreement No 95591). I. Z. acknowledges funding from Project PID2020-114839GB-I00 MINECO/AEI/FEDER, UE. A. M. acknowledges funding from the European Research Council, Starting Grant No. 678573 NanoPacks. G. V. acknowledges sponsorship for this work by the US Office of Naval Research Global (Award No. N62909-18-1-2170).","doi":"10.1039/d2sm01562e","file":[{"relation":"main_file","file_id":"12711","success":1,"checksum":"af95aa18b9b01e32fb8f13477c0e2687","creator":"cchlebak","file_name":"2023_SoftMatter_Araujo.pdf","file_size":3581939,"access_level":"open_access","content_type":"application/pdf","date_created":"2023-03-07T09:19:41Z","date_updated":"2023-03-07T09:19:41Z"}],"isi":1,"pmid":1,"day":"06","language":[{"iso":"eng"}],"_id":"12708","arxiv":1,"title":"Steering self-organisation through confinement","ddc":["540"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2025-04-23T08:48:51Z","date_published":"2023-02-06T00:00:00Z","publication_identifier":{"issn":["1744-683X"],"eissn":["1744-6848"]},"intvolume":"        19","file_date_updated":"2023-03-07T09:19:41Z","author":[{"last_name":"Araújo","first_name":"Nuno A.M.","full_name":"Araújo, Nuno A.M."},{"last_name":"Janssen","first_name":"Liesbeth M.C.","full_name":"Janssen, Liesbeth M.C."},{"full_name":"Barois, Thomas","first_name":"Thomas","last_name":"Barois"},{"full_name":"Boffetta, Guido","last_name":"Boffetta","first_name":"Guido"},{"first_name":"Itai","last_name":"Cohen","full_name":"Cohen, Itai"},{"last_name":"Corbetta","first_name":"Alessandro","full_name":"Corbetta, Alessandro"},{"last_name":"Dauchot","first_name":"Olivier","full_name":"Dauchot, Olivier"},{"last_name":"Dijkstra","first_name":"Marjolein","full_name":"Dijkstra, Marjolein"},{"full_name":"Durham, William M.","last_name":"Durham","first_name":"William M."},{"last_name":"Dussutour","first_name":"Audrey","full_name":"Dussutour, Audrey"},{"full_name":"Garnier, Simon","last_name":"Garnier","first_name":"Simon"},{"full_name":"Gelderblom, Hanneke","first_name":"Hanneke","last_name":"Gelderblom"},{"first_name":"Ramin","last_name":"Golestanian","full_name":"Golestanian, Ramin"},{"full_name":"Isa, Lucio","last_name":"Isa","first_name":"Lucio"},{"full_name":"Koenderink, Gijsje H.","first_name":"Gijsje H.","last_name":"Koenderink"},{"first_name":"Hartmut","last_name":"Löwen","full_name":"Löwen, Hartmut"},{"first_name":"Ralf","last_name":"Metzler","full_name":"Metzler, Ralf"},{"first_name":"Marco","last_name":"Polin","full_name":"Polin, Marco"},{"first_name":"C. Patrick","last_name":"Royall","full_name":"Royall, C. Patrick"},{"orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela","last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","first_name":"Anđela"},{"last_name":"Sengupta","first_name":"Anupam","full_name":"Sengupta, Anupam"},{"full_name":"Sykes, Cécile","last_name":"Sykes","first_name":"Cécile"},{"full_name":"Trianni, Vito","last_name":"Trianni","first_name":"Vito"},{"full_name":"Tuval, Idan","first_name":"Idan","last_name":"Tuval"},{"first_name":"Nicolas","last_name":"Vogel","full_name":"Vogel, Nicolas"},{"last_name":"Yeomans","first_name":"Julia M.","full_name":"Yeomans, Julia M."},{"full_name":"Zuriguel, Iker","last_name":"Zuriguel","first_name":"Iker"},{"full_name":"Marin, Alvaro","first_name":"Alvaro","last_name":"Marin"},{"first_name":"Giorgio","last_name":"Volpe","full_name":"Volpe, Giorgio"}],"oa":1,"has_accepted_license":"1","month":"02","external_id":{"arxiv":["2204.10059"],"pmid":["36779972"],"isi":["000940388100001"]},"department":[{"_id":"AnSa"}],"year":"2023","date_created":"2023-03-05T23:01:06Z","citation":{"chicago":"Araújo, Nuno A.M., Liesbeth M.C. Janssen, Thomas Barois, Guido Boffetta, Itai Cohen, Alessandro Corbetta, Olivier Dauchot, et al. “Steering Self-Organisation through Confinement.” <i>Soft Matter</i>. Royal Society of Chemistry, 2023. <a href=\"https://doi.org/10.1039/d2sm01562e\">https://doi.org/10.1039/d2sm01562e</a>.","ista":"Araújo NAM, Janssen LMC, Barois T, Boffetta G, Cohen I, Corbetta A, Dauchot O, Dijkstra M, Durham WM, Dussutour A, Garnier S, Gelderblom H, Golestanian R, Isa L, Koenderink GH, Löwen H, Metzler R, Polin M, Royall CP, Šarić A, Sengupta A, Sykes C, Trianni V, Tuval I, Vogel N, Yeomans JM, Zuriguel I, Marin A, Volpe G. 2023. Steering self-organisation through confinement. Soft Matter. 19, 1695–1704.","ieee":"N. A. M. Araújo <i>et al.</i>, “Steering self-organisation through confinement,” <i>Soft Matter</i>, vol. 19. Royal Society of Chemistry, pp. 1695–1704, 2023.","mla":"Araújo, Nuno A. M., et al. “Steering Self-Organisation through Confinement.” <i>Soft Matter</i>, vol. 19, Royal Society of Chemistry, 2023, pp. 1695–704, doi:<a href=\"https://doi.org/10.1039/d2sm01562e\">10.1039/d2sm01562e</a>.","ama":"Araújo NAM, Janssen LMC, Barois T, et al. Steering self-organisation through confinement. <i>Soft Matter</i>. 2023;19:1695-1704. doi:<a href=\"https://doi.org/10.1039/d2sm01562e\">10.1039/d2sm01562e</a>","short":"N.A.M. Araújo, L.M.C. Janssen, T. Barois, G. Boffetta, I. Cohen, A. Corbetta, O. Dauchot, M. Dijkstra, W.M. Durham, A. Dussutour, S. Garnier, H. Gelderblom, R. Golestanian, L. Isa, G.H. Koenderink, H. Löwen, R. Metzler, M. Polin, C.P. Royall, A. Šarić, A. Sengupta, C. Sykes, V. Trianni, I. Tuval, N. Vogel, J.M. Yeomans, I. Zuriguel, A. Marin, G. Volpe, Soft Matter 19 (2023) 1695–1704.","apa":"Araújo, N. A. M., Janssen, L. M. C., Barois, T., Boffetta, G., Cohen, I., Corbetta, A., … Volpe, G. (2023). Steering self-organisation through confinement. <i>Soft Matter</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/d2sm01562e\">https://doi.org/10.1039/d2sm01562e</a>"},"status":"public"},{"title":"The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division","day":"17","isi":1,"pmid":1,"issue":"11","language":[{"iso":"eng"}],"_id":"12756","file_date_updated":"2023-03-27T06:24:49Z","publication_identifier":{"eissn":["2375-2548"]},"intvolume":"         9","date_updated":"2025-04-23T08:50:02Z","date_published":"2023-03-17T00:00:00Z","ddc":["570"],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","month":"03","external_id":{"isi":["000968083500010"],"pmid":["36921039"]},"author":[{"full_name":"Hurtig, Fredrik","first_name":"Fredrik","last_name":"Hurtig"},{"last_name":"Burgers","first_name":"Thomas C.Q.","full_name":"Burgers, Thomas C.Q."},{"full_name":"Cezanne, Alice","last_name":"Cezanne","first_name":"Alice"},{"first_name":"Xiuyun","last_name":"Jiang","full_name":"Jiang, Xiuyun"},{"first_name":"Frank N.","last_name":"Mol","full_name":"Mol, Frank N."},{"last_name":"Traparić","first_name":"Jovan","full_name":"Traparić, Jovan"},{"last_name":"Pulschen","first_name":"Andre Arashiro","full_name":"Pulschen, Andre Arashiro"},{"full_name":"Nierhaus, Tim","last_name":"Nierhaus","first_name":"Tim"},{"first_name":"Gabriel","last_name":"Tarrason-Risa","full_name":"Tarrason-Risa, Gabriel"},{"full_name":"Harker-Kirschneck, Lena","last_name":"Harker-Kirschneck","first_name":"Lena"},{"full_name":"Löwe, Jan","last_name":"Löwe","first_name":"Jan"},{"last_name":"Šarić","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","first_name":"Anđela","orcid":"0000-0002-7854-2139","full_name":"Šarić, Anđela"},{"full_name":"Vlijm, Rifka","first_name":"Rifka","last_name":"Vlijm"},{"first_name":"Buzz","last_name":"Baum","full_name":"Baum, Buzz"}],"oa":1,"has_accepted_license":"1","status":"public","department":[{"_id":"AnSa"}],"citation":{"mla":"Hurtig, Fredrik, et al. “The Patterned Assembly and Stepwise Vps4-Mediated Disassembly of Composite ESCRT-III Polymers Drives Archaeal Cell Division.” <i>Science Advances</i>, vol. 9, no. 11, eade5224, American Association for the Advancement of Science, 2023, doi:<a href=\"https://doi.org/10.1126/sciadv.ade5224\">10.1126/sciadv.ade5224</a>.","short":"F. Hurtig, T.C.Q. Burgers, A. Cezanne, X. Jiang, F.N. Mol, J. Traparić, A.A. Pulschen, T. Nierhaus, G. Tarrason-Risa, L. Harker-Kirschneck, J. Löwe, A. Šarić, R. Vlijm, B. Baum, Science Advances 9 (2023).","apa":"Hurtig, F., Burgers, T. C. Q., Cezanne, A., Jiang, X., Mol, F. N., Traparić, J., … Baum, B. (2023). The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division. <i>Science Advances</i>. American Association for the Advancement of Science. <a href=\"https://doi.org/10.1126/sciadv.ade5224\">https://doi.org/10.1126/sciadv.ade5224</a>","ama":"Hurtig F, Burgers TCQ, Cezanne A, et al. The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division. <i>Science Advances</i>. 2023;9(11). doi:<a href=\"https://doi.org/10.1126/sciadv.ade5224\">10.1126/sciadv.ade5224</a>","ieee":"F. Hurtig <i>et al.</i>, “The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division,” <i>Science Advances</i>, vol. 9, no. 11. American Association for the Advancement of Science, 2023.","ista":"Hurtig F, Burgers TCQ, Cezanne A, Jiang X, Mol FN, Traparić J, Pulschen AA, Nierhaus T, Tarrason-Risa G, Harker-Kirschneck L, Löwe J, Šarić A, Vlijm R, Baum B. 2023. The patterned assembly and stepwise Vps4-mediated disassembly of composite ESCRT-III polymers drives archaeal cell division. Science Advances. 9(11), eade5224.","chicago":"Hurtig, Fredrik, Thomas C.Q. Burgers, Alice Cezanne, Xiuyun Jiang, Frank N. Mol, Jovan Traparić, Andre Arashiro Pulschen, et al. “The Patterned Assembly and Stepwise Vps4-Mediated Disassembly of Composite ESCRT-III Polymers Drives Archaeal Cell Division.” <i>Science Advances</i>. American Association for the Advancement of Science, 2023. <a href=\"https://doi.org/10.1126/sciadv.ade5224\">https://doi.org/10.1126/sciadv.ade5224</a>."},"date_created":"2023-03-26T22:01:06Z","year":"2023","article_number":"eade5224","volume":9,"publication_status":"published","oa_version":"Published Version","corr_author":"1","scopus_import":"1","tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"publisher":"American Association for the Advancement of Science","fulldoi":"https://doi.org/10.1126/sciadv.ade5224","ec_funded":1,"type":"journal_article","article_processing_charge":"No","quality_controlled":"1","article_type":"original","abstract":[{"text":"ESCRT-III family proteins form composite polymers that deform and cut membrane tubes in the context of a wide range of cell biological processes across the tree of life. In reconstituted systems, sequential changes in the composition of ESCRT-III polymers induced by the AAA–adenosine triphosphatase Vps4 have been shown to remodel membranes. However, it is not known how composite ESCRT-III polymers are organized and remodeled in space and time in a cellular context. Taking advantage of the relative simplicity of the ESCRT-III–dependent division system in Sulfolobus acidocaldarius, one of the closest experimentally tractable prokaryotic relatives of eukaryotes, we use super-resolution microscopy, electron microscopy, and computational modeling to show how CdvB/CdvB1/CdvB2 proteins form a precisely patterned composite ESCRT-III division ring, which undergoes stepwise Vps4-dependent disassembly and contracts to cut cells into two. These observations lead us to suggest sequential changes in a patterned composite polymer as a general mechanism of ESCRT-III–dependent membrane remodeling.","lang":"eng"}],"publication":"Science Advances","project":[{"_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","grant_number":"802960","call_identifier":"H2020"}],"file":[{"file_size":1826471,"file_name":"2023_ScienceAdvances_Hurtig.pdf","creator":"dernst","checksum":"6d7dbe9ed86a116c8a002d62971202c5","file_id":"12768","success":1,"relation":"main_file","date_updated":"2023-03-27T06:24:49Z","date_created":"2023-03-27T06:24:49Z","content_type":"application/pdf","access_level":"open_access"}],"acknowledgement":"We thank Y. Liu and V. Hale for help with electron cryotomography; the Medical Research Council (MRC) LMB Electron Microscopy Facility for access, training, and support; and T. Darling and J. Grimmett at the MRC LMB for help with computing infrastructure. We also thank the Flow Cytometry Facility and the MRC LMB for training and support.\r\n F.H. and G.T.-R. were supported by a grant from the Wellcome Trust (203276/Z/16/Z). A.C. was supported by an EMBO long-term fellowship: ALTF_1041-2021. J.T. was supported by a grant from the VW Foundation (94933). A.A.P. was supported by the Wellcome Trust (203276/Z/16/Z) and the HFSP (LT001027/2019). B.B. received support from the MRC LMB, the Wellcome Trust (203276/Z/16/Z), the VW Foundation (94933), the Life Sciences–Moore-Simons Foundation (735929LPI), and a Gordon and Betty Moore Foundation’s Symbiosis in Aquatic Systems Initiative (9346). A.Š. and X.J. acknowledge funding from the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme (grant no. 802960). L.H.-K. acknowledges support from Biotechnology and Biological Sciences Research Council LIDo Programme. T.N. and J.L. were supported by the MRC (U105184326) and the Wellcome Trust (203276/Z/16/Z).","doi":"10.1126/sciadv.ade5224"}]